|
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 ... |
117-695 |
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: 950.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 117 QPYEWISYKEVAELAECIGSGLIQKGFKPCSEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAEL 196
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 197 SVIFADKpekaklllegvenkltpclkiivimdsygsdlvergkkcGVEIISLKALEDLGRVNRVKPKPPEPEDLAIICF 276
Cdd:cd05927 81 SIVFCDA---------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 277 TSGTTGNPKGAMITHQNIINDCSGFIKATESAFIASTDDVLISFLPLAHMFETVVECVMLCHGAKIGFFQGDIRLLMDDL 356
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 357 KVLQPTIFPVVPRLLNRMFDRIFG--QANTSLKRWLLDFASKRKEAELRSGIVRNNSLWDKLIFHKIQSSLGGKVRLMIT 434
Cdd:cd05927 202 KALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 435 GAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDVEEMNYLA--SKGEGEVCVK 512
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAkdPNPRGEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 513 GANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGE 592
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 593 SLQAFLIAVVVPDVESLPSWAQKRGL-QGSFEELCRNKDINKAILDDLLKLGKEAGLKPFEQVKGIAVHPELFSIDNGLL 671
Cdd:cd05927 442 SLKSFLVAIVVPDPDVLKEWAASKGGgTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLL 521
|
570 580
....*....|....*....|....
gi 1039782744 672 TPTLKAKRPELRNYFRSQIDELYA 695
Cdd:cd05927 522 TPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
87-697 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 712.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 87 YDDVRTMYDGFQRGIQVSNNGPCLGSRKPNQ----PYEWISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWV 162
Cdd:PLN02736 40 HPEIGTLHDNFVYAVETFRDYKYLGTRIRVDgtvgEYKWMTYGEAGTARTAIGSGLVQHGIPK--GACVGLYFINRPEWL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 163 IVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFAdKPEKAKLLLEGVENklTPCLKIIVIMDSYGSDLVERGKKC 242
Cdd:PLN02736 118 IVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCLSE--IPSVRLIVVVGGADEPLPSLPSGT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 243 GVEIISLKALEDLGRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKATESafiaSTDDVLISFLP 322
Cdd:PLN02736 195 GVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKF----YPSDVHISYLP 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 323 LAHMFETVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTS--LKRWLLDFASKRKEA 400
Cdd:PLN02736 271 LAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESggLKERLFNAAYNAKKQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 401 ELRSGivRNNS-LWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTEctAGCCLSL--PGDWT 477
Cdd:PLN02736 351 ALENG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTE--TSCVISGmdEGDNL 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 478 AGHVGAPMPCNYVKLVDVEEMNYLASKG---EGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKII 554
Cdd:PLN02736 427 SGHVGSPNPACEVKLVDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKII 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 555 DRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAVVVPDVESLPSWAQKRGLQ-GSFEELCRNKDINK 633
Cdd:PLN02736 507 DRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRVRA 586
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039782744 634 AILDDLLKLGKEAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYATI 697
Cdd:PLN02736 587 AVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYAEL 650
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
87-695 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 533.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 87 YDDVRTMYDGFQRGIQVSNNGPCLgSRKPNQPYEWISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQ 166
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVAL-REKEDGIWQSLTWAEFAERVRALAAGLLALGVKP--GDRVAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 167 GCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFADKPEKAKLLLEGVENklTPCLKIIVIMDsygsdlvERGKKCGVEI 246
Cdd:COG1022 84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDE--LPSLRHIVVLD-------PRGLRDDPRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 247 ISLKALEDLG-----------RVNRVKPkppepEDLAIICFTSGTTGNPKGAMITHQNIINDCsgfiKATESAFIASTDD 315
Cdd:COG1022 155 LSLDELLALGrevadpaeleaRRAAVKP-----DDLATIIYTSGTTGRPKGVMLTHRNLLSNA----RALLERLPLGPGD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 316 VLISFLPLAHMFETVVECVMLCHGAKIGFfQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTS--LKRWLLDF 393
Cdd:COG1022 226 RTLSFLPLAHVFERTVSYYALAAGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAggLKRKLFRW 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 394 A---SKRKEAELRSGivRNNSLW--------DKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRtALGCQFYEGYGQT 462
Cdd:COG1022 305 AlavGRRYARARLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFR-ALGIPVLEGYGLT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 463 ECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDveemnylaskgEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDI 542
Cdd:COG1022 382 ETSPVITVNRPGDNRIGTVGPPLPGVEVKIAE-----------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDI 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 543 GKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESlQAFLIAVVVPDVESLPSWAQKRGLQ-GS 621
Cdd:COG1022 451 GELDEDGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGLPyTS 529
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039782744 622 FEELCRNKDINKAILDDLLKLgkEAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYA 695
Cdd:COG1022 530 YAELAQDPEVRALIQEEVDRA--NAGLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYA 601
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
117-682 |
5.41e-168 |
|
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: 489.41 E-value: 5.41e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 117 QPYEWISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAEL 196
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEP--GDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 197 SVIFADKPEkaklllegvenkltpclkiivimdsygsdlvergkkcgveiislkaledlgrvnrvkpkppepeDLAIICF 276
Cdd:cd05907 79 KALFVEDPD----------------------------------------------------------------DLATIIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 277 TSGTTGNPKGAMITHQNIINDCSGFIKATEsafiASTDDVLISFLPLAHMFETV-VECVMLCHGAKIGFFQgDIRLLMDD 355
Cdd:cd05907 95 TSGTTGRPKGVMLSHRNILSNALALAERLP----ATEGDRHLSFLPLAHVFERRaGLYVPLLAGARIYFAS-SAETLLDD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 356 LKVLQPTIFPVVPRLLNRMFDRIFGQANTSLKRWLLDFASkrkeaelrsgivrnnslwdklifhkiqsslGGKVRLMITG 435
Cdd:cd05907 170 LSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV------------------------------GGRLRFAASG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 436 AAPVSATVLTFLRtALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDveemnylaskgEGEVCVKGAN 515
Cdd:cd05907 220 GAPLPAELLHFFR-ALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPN 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 516 VFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESlQ 595
Cdd:cd05907 288 VMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDG-R 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 596 AFLIAVVVPDVESLPSWAQKRGL-QGSFEELCRNKDINKAILDDLLKLGkeAGLKPFEQVKGIAVHPELFSIDNGLLTPT 674
Cdd:cd05907 367 PFLVALIVPDPEALEAWAEEHGIaYTDVAELAANPAVRAEIEAAVEAAN--ARLSRYEQIKKFLLLPEPFTIENGELTPT 444
|
....*...
gi 1039782744 675 LKAKRPEL 682
Cdd:cd05907 445 LKLKRPVI 452
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
89-698 |
2.24e-162 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 482.80 E-value: 2.24e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 89 DVRTMYDGFQRGIQVSNNGPCLGSRKPNQ----PYEWISYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIV 164
Cdd:PLN02861 41 DIDSPWQFFSDAVKKYPNNQMLGRRQVTDskvgPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDR--CGIYGSNCPEWIIA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 165 EQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFADKPEKAKLLleGVENKLTPCLKIIVIMDSYGSDLVERGKKCGV 244
Cdd:PLN02861 119 MEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKISSIL--SCLPKCSSNLKTIVSFGDVSSEQKEEAEELGV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 245 EIISLKALEDLGRVNRVKPkPPEPEDLAIICFTSGTTGNPKGAMITHQNIINDC---SGFIKATESAfiASTDDVLISFL 321
Cdd:PLN02861 197 SCFSWEEFSLMGSLDCELP-PKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVlstDHLLKVTDRV--ATEEDSYFSYL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 322 PLAHMFETVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLlnrmFDRIFG------QANTSLKRWLLDFAS 395
Cdd:PLN02861 274 PLAHVYDQVIETYCISKGASIGFWQGDIRYLMEDVQALKPTIFCGVPRV----YDRIYTgimqkiSSGGMLRKKLFDFAY 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 396 KRKEAELRSGIVRNNS--LWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLP 473
Cdd:PLN02861 350 NYKLGNLRKGLKQEEAspRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGCFTSIA 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 474 GDWT-AGHVGAPMPCNYVKLVDVEEMNY--LASKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGT 550
Cdd:PLN02861 430 NVFSmVGTVGVPMTTIEARLESVPEMGYdaLSDVPRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGA 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 551 LKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAVVVPDVESLPSWAQKRGLQGSFEELCRNKD 630
Cdd:PLN02861 509 MKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLK 588
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039782744 631 INKAILDDLLKLGKEAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYATIK 698
Cdd:PLN02861 589 ARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYSEAK 656
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
88-698 |
1.43e-161 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 481.06 E-value: 1.43e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 88 DDVRTMYDGFQRGIQVSNNGPCLGSR-----KPNQpYEWISYKEVAELAECIGSGLIQKGFKpcSEQFIGLFSQNRPEWV 162
Cdd:PLN02614 42 EGMDSCWDVFRMSVEKYPNNPMLGRReivdgKPGK-YVWQTYQEVYDIVIKLGNSLRSVGVK--DEAKCGIYGANSPEWI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 163 IVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFADKpEKAKLLLEGVENKlTPCLKIIVIMDSYGSDLVERGKKC 242
Cdd:PLN02614 119 ISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEE-KKISELFKTCPNS-TEYMKTVVSFGGVSREQKEEAETF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 243 GVEIISLKALEDLGRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKATESAFIA-STDDVLISFL 321
Cdd:PLN02614 197 GLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANAAlTVKDVYLSYL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 322 PLAHMFETVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIfgQANTS----LKRWLLDFASKR 397
Cdd:PLN02614 277 PLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGL--QKKLSdggfLKKFVFDSAFSY 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 398 KEAELRSGI--VRNNSLWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGD 475
Cdd:PLN02614 355 KFGNMKKGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDE 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 476 W-TAGHVGAPMPCNYVKLVDVEEMNY--LASKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLK 552
Cdd:PLN02614 435 LdMLGTVGPPVPNVDIRLESVPEMEYdaLASTPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMK 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 553 IIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAVVVPDVESLPSWAQKRGLQGSFEELCRNKDIN 632
Cdd:PLN02614 514 IIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAK 593
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039782744 633 KAILDDLLKLGKEAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYATIK 698
Cdd:PLN02614 594 EFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYKTTN 659
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
118-679 |
1.64e-160 |
|
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: 472.47 E-value: 1.64e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 118 PYEWISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELS 197
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLVELGLKP--GDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 198 VIFADkpekaklllegvenkltpclkiivimdsygsdlvergkkcgveiislkaledlgrvnrvkpkpPEPEDLAIICFT 277
Cdd:cd17639 80 AIFTD---------------------------------------------------------------GKPDDLACIMYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 278 SGTTGNPKGAMITHQNIINDCSGFIKATeSAFIaSTDDVLISFLPLAHMFETVVECVMLCHGAKIGFfqGDIRLLMD--- 354
Cdd:cd17639 97 SGSTGNPKGVMLTHGNLVAGIAGLGDRV-PELL-GPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDksk 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 355 -----DLKVLQPTIFPVVPRLLNRMFDRIFGQANT--SLKRWLLDFASKRKEAELRSGIvrNNSLWDKLIFHKIQSSLGG 427
Cdd:cd17639 173 rgckgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPmgGLKRTLFWTAYQSKLKALKEGP--GTPLLDELVFKKVRAALGG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 428 KVRLMITGAAPVSATVLTFLRTALgCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDVEEMNYLASKGE- 506
Cdd:cd17639 251 RLRYMLSGGAPLSADTQEFLNIVL-CPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDKPPp 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 507 -GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVA 585
Cdd:cd17639 330 rGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVN 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 586 QVFVHGESLQAFLIAVVVPDVESLPSWAQKRGL-QGSFEELCRNKDINKAILDDLLKLGKEAGLKPFEQVKGIAVHPELF 664
Cdd:cd17639 410 NICVYADPDKSYPVAIVVPNEKHLTKLAEKHGViNSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEW 489
|
570
....*....|....*
gi 1039782744 665 SIDNGLLTPTLKAKR 679
Cdd:cd17639 490 TPENGLVTAAQKLKR 504
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
89-697 |
3.16e-158 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 471.99 E-value: 3.16e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 89 DVRTMYDGFQRGIQVSNNGPCLGSRKPNQ----PYEWISYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIV 164
Cdd:PLN02430 40 DITTAWDIFSKSVEKYPDNKMLGWRRIVDgkvgPYMWKTYKEVYEEVLQIGSALRASGAEPGSR--VGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 165 EQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA-DKpeKAKLLLEGvENKLTPCLKIIVIMDSYGSDLVERGKKCG 243
Cdd:PLN02430 118 MEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVqDK--KIKELLEP-DCKSAKRLKAIVSFTSVTEEESDKASQIG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 244 VEIISLKALEDLGRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIINDCSG---FIKATESAFiaSTDDVLISF 320
Cdd:PLN02430 195 VKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGvdlFMEQFEDKM--THDDVYLSF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 321 LPLAHMFETVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFG--QANTSLKRWLLDFASKRK 398
Cdd:PLN02430 273 LPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYKYK 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 399 EAELRSGIVRNNS--LWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDW 476
Cdd:PLN02430 353 LAWMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEM 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 477 TA-GHVGAPMPCNYVKLVDVEEMNY--LASKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKI 553
Cdd:PLN02430 433 CMlGTVGAPAVYNELRLEEVPEMGYdpLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKI 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 554 IDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAVVVPDVESLPSWAQKRGLQGSFEELCRNKDINK 633
Cdd:PLN02430 512 IDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKE 591
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039782744 634 AILDDLLKLGKEAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYATI 697
Cdd:PLN02430 592 HILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMYRKL 655
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
118-695 |
1.64e-138 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 422.60 E-value: 1.64e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 118 PYEWISYKEVAELAECIGSGLIQKGFKpcSEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELS 197
Cdd:PLN02387 103 EYEWITYGQVFERVCNFASGLVALGHN--KEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVT 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 198 VIFADKPEKAKLLleGVENKLTPCLKIIVIMDSYGSDLVERGKKCGVEIISLKALEDLGRVNRVKPKPPEPEDLAIICFT 277
Cdd:PLN02387 181 TVICDSKQLKKLI--DISSQLETVKRVIYMDDEGVDSDSSLSGSSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYT 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 278 SGTTGNPKGAMITHQNIIndcsgfikATESAFIA-----STDDVLISFLPLAHMFETVVECVMLCHGAKIGFfqGDIRLL 352
Cdd:PLN02387 259 SGSTGLPKGVMMTHGNIV--------ATVAGVMTvvpklGKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 353 MD-----------DLKVLQPTIFPVVPRLLNRMFDRIFGQANTS--LKRWLLDFASKRKEAELR------SGIVRnnSLW 413
Cdd:PLN02387 329 TDtsnkikkgtkgDASALKPTLMTAVPAILDRVRDGVRKKVDAKggLAKKLFDIAYKRRLAAIEgswfgaWGLEK--LLW 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 414 DKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLV 493
Cdd:PLN02387 407 DALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLV 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 494 DVEEMNYLASKG---EGEVCVKGANVFKGYLKDPARTAEA--LDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAQG 566
Cdd:PLN02387 487 SWEEGGYLISDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHG 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 567 EYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAVVVPDVESLPSWAQKRGLQ-GSFEELCRNKDINKAILDDLLKLGKE 645
Cdd:PLN02387 567 EYVSLGKVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKA 646
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1039782744 646 AGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYA 695
Cdd:PLN02387 647 ARLEKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
118-564 |
3.74e-130 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 391.29 E-value: 3.74e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 118 PYEWISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELS 197
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRALGVGK--GDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 198 VIFADKPEKAKLLLEGVENKLTPCLKIIVIMDSygsdlvergkkcGVEIISLKALEDLGRVNRVKPKPPEPEDLAIICFT 277
Cdd:pfam00501 96 VLITDDALKLEELLEALGKLEVVKLVLVLDRDP------------VLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 278 SGTTGNPKGAMITHQNIINDCSGFIKATESAFIASTDDVLISFLPLAHMFETVVEC-VMLCHGAKIGFFQGDIRL----L 352
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLlGPLLAGATVVLPPGFPALdpaaL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 353 MDDLKVLQPTIFPVVPRLLNRMFDrifgqantslkrwlldfaSKRKEAELRSGivrnnslwdklifhkiqsslggkVRLM 432
Cdd:pfam00501 244 LELIERYKVTVLYGVPTLLNMLLE------------------AGAPKRALLSS-----------------------LRLV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 433 ITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDW---TAGHVGAPMPCNYVKLVDVEEMNYLASKGEGEV 509
Cdd:pfam00501 283 LSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGEL 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1039782744 510 CVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLA 564
Cdd:pfam00501 363 CVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
122-695 |
8.41e-100 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 321.54 E-value: 8.41e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 122 ISYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLTKGSN--VAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 202 DKpEKAKLLLEGVENKLTPCLKIIvimdsYGSDLVERGKKCGVEIISLKALEDLGR--VNRVKPKPPEP-EDLAIICFTS 278
Cdd:PTZ00216 200 NG-KNVPNLLRLMKSGGMPNTTII-----YLDSLPASVDTEGCRLVAWTDVVAKGHsaGSHHPLNIPENnDDLALIMYTS 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 279 GTTGNPKGAMITHQNIINDCSGF-------IKATESafiastDDVLISFLPLAHMFETVVECVMLCHGAKIGFfqGDIRL 351
Cdd:PTZ00216 274 GTTGDPKGVMHTHGSLTAGILALedrlndlIGPPEE------DETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRT 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 352 LMD-------DLKVLQPTIFPVVPRLlnrmFDRI----------FGqantSLKRWLLDFASKRKEAELRSGivRNNSLWD 414
Cdd:PTZ00216 346 LTDtfarphgDLTEFRPVFLIGVPRI----FDTIkkaveaklppVG----SLKRRVFDHAYQSRLRALKEG--KDTPYWN 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 415 KLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRTALGCqFYEGYGQTECTagCC--LSLPGDWTAGHVGAPMPCNYVKL 492
Cdd:PTZ00216 416 EKVFSAPRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTETV--CCggIQRTGDLEPNAVGQLLKGVEMKL 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 493 VDVEEMNYlASKGE--GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIA 570
Cdd:PTZ00216 493 LDTEEYKH-TDTPEprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIA 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 571 PEKIENIYLRSEAVAQ----VFVHgeSLQAFLIAVVVPDVESLPSWAQKRGLQGSFEELCRNKDINKAILDDLLKLGKEA 646
Cdd:PTZ00216 572 LEALEALYGQNELVVPngvcVLVH--PARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAA 649
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1039782744 647 GLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYA 695
Cdd:PTZ00216 650 GRKSFEIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELFA 698
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
117-680 |
1.68e-90 |
|
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: 290.03 E-value: 1.68e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 117 QPYEWISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAEL 196
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKA--GEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 197 SVIFadkpekaklllegVENkltpclkiivimdsygsdlvergkkcgveiislkaledlgrvnrvkpkppEPEDLAIICF 276
Cdd:cd17640 79 VALV-------------VEN--------------------------------------------------DSDDLATIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 277 TSGTTGNPKGAMITHQNIINDCSGFikateSAFI-ASTDDVLISFLPLAHMFETVVECVMLCHGAKIGFfqGDIRLLMDD 355
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLLHQIRSL-----SDIVpPQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDD 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 356 LKVLQPTIFPVVPRLlnrmfdrifgqantslkrWlldfaskrkEAeLRSGI---VRNNSLWDKLIFHKIQSslGGKVRLM 432
Cdd:cd17640 169 LKRVKPHYIVSVPRL------------------W---------ES-LYSGIqkqVSKSSPIKQFLFLFFLS--GGIFKFG 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 433 ITGAAPVSATVLTFLRtALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDVEEMNYLASKGEGEVCVK 512
Cdd:cd17640 219 ISGGGALPPHVDTFFE-AIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVR 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 513 GANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGE 592
Cdd:cd17640 298 GPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQ 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 593 SlQAFLIAVVVPDVESLPSWAQKRG--LQGSFEELCRNKDINKAILDDLLK-LGKEAGLKPFEQVKGIAVHPELFsIDNG 669
Cdd:cd17640 378 D-QKRLGALIVPNFEELEKWAKESGvkLANDRSQLLASKKVLKLYKNEIKDeISNRPGFKSFEQIAPFALLEEPF-IENG 455
|
570
....*....|.
gi 1039782744 670 LLTPTLKAKRP 680
Cdd:cd17640 456 EMTQTMKIKRN 466
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
119-679 |
8.60e-81 |
|
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: 265.87 E-value: 8.60e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 119 YEWISYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSV 198
Cdd:cd05932 4 VVEFTWGEVADKARRLAAALRALGLEPGSK--IALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 199 IFADKPEKAKLLLEGVENKLTPCLKII--VIMDSYG-SDLVERGKkcgveiislkALEDlgrvnrvKPkPPEPEDLAIIC 275
Cdd:cd05932 82 LFVGKLDDWKAMAPGVPEGLISISLPPpsAANCQYQwDDLIAQHP----------PLEE-------RP-TRFPEQLATLI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 276 FTSGTTGNPKGAMITHQNIINDCSGFIKAtesaFIASTDDVLISFLPLAHMFETV-VECVMLCHGAKIgFFQGDIRLLMD 354
Cdd:cd05932 144 YTSGTTGQPKGVMLTFGSFAWAAQAGIEH----IGTEENDRMLSYLPLAHVTERVfVEGGSLYGGVLV-AFAESLDTFVE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 355 DLKVLQPTIFPVVPRLLNRMFDRIFGQANTSLKRWLLDFaskrkeaelrsgivrnnSLWDKLIFHKIQSSLG-GKVRLMI 433
Cdd:cd05932 219 DVQRARPTLFFSVPRLWTKFQQGVQDKIPQQKLNLLLKI-----------------PVVNSLVKRKVLKGLGlDQCRLAG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 434 TGAAPVSATVLTFLRTaLGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDveemnylaskgEGEVCVKG 513
Cdd:cd05932 282 CGSAPVPPALLEWYRS-LGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEILVRS 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 514 ANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGES 593
Cdd:cd05932 350 PALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSG 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 594 LQAFLIAVVVPDVESLPSWAQKRG-LQGSFEELCrnKDINKAilddllklgkeagLKPFEQVKGIAVHPELFSIDNGLLT 672
Cdd:cd05932 430 LPAPLALVVLSEEARLRADAFARAeLEASLRAHL--ARVNST-------------LDSHEQLAGIVVVKDPWSIDNGILT 494
|
....*..
gi 1039782744 673 PTLKAKR 679
Cdd:cd05932 495 PTLKIKR 501
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
122-616 |
2.83e-73 |
|
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: 244.33 E-value: 2.83e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 122 ISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:COG0318 25 LTYAELDARARRLAAALRALGVGP--GDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 202 dkpekaklllegvenkltpclkiivimdsygsdlvergkkcgveiislkaledlgrvnrvkpkppepedlAIICFTSGTT 281
Cdd:COG0318 103 ----------------------------------------------------------------------ALILYTSGTT 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 282 GNPKGAMITHQNIINDCSGFIKATEsafiASTDDVLISFLPLAHMFETVVECVM-LCHGAKI----GFfqgDIRLLMDDL 356
Cdd:COG0318 113 GRPKGVMLTHRNLLANAAAIAAALG----LTPGDVVLVALPLFHVFGLTVGLLApLLAGATLvllpRF---DPERVLELI 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 357 KVLQPTIFPVVPRLLNRMFDRifgqantslkrwlldfaSKRKEAELRSgivrnnslwdklifhkiqsslggkVRLMITGA 436
Cdd:COG0318 186 ERERVTVLFGVPTMLARLLRH-----------------PEFARYDLSS------------------------LRLVVSGG 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 437 APVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTA--GHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGA 514
Cdd:COG0318 225 APLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGRPLPGVEVRIVD-EDGRELPPGEVGEIVVRGP 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 515 NVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQVFV----- 589
Cdd:COG0318 304 NVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEVLAAHPGVAEAAVvgvpd 381
|
490 500 510
....*....|....*....|....*....|.
gi 1039782744 590 --HGESLQAFLIAV--VVPDVESLPSWAQKR 616
Cdd:COG0318 382 ekWGERVVAFVVLRpgAELDAEELRAFLRER 412
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
114-694 |
1.74e-70 |
|
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: 240.72 E-value: 1.74e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 114 KPNQPYEWISYKEVAELAECIGSGLIQKGFkpcsEQF--IGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIV 191
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLKLGL----ERFhgVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 192 NKAELSVIFADKPEKAKLLLEgVENKLtPCLKIIVImdsYGSDLVErgKKCGVeiISLKALEDLGRvnrvkpKPPEPEDL 271
Cdd:cd05933 77 ETSEANILVVENQKQLQKILQ-IQDKL-PHLKAIIQ---YKEPLKE--KEPNL--YSWDEFMELGR------SIPDEQLD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 272 AII-------C----FTSGTTGNPKGAMITHQNIINDCSGFIKATEsaFIASTD--DVLISFLPLAHMFETVVEcVMLC- 337
Cdd:cd05933 142 AIIssqkpnqCctliYTSGTTGMPKGVMLSHDNITWTAKAASQHMD--LRPATVgqESVVSYLPLSHIAAQILD-IWLPi 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 338 -HGAKIGFFQGDIR--LLMDDLKVLQPTIFPVVPRLLNRMFDRI--FGQANTSLKRWLLDFAsKRKEAE-------LRSG 405
Cdd:cd05933 219 kVGGQVYFAQPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkaVGAKSGTLKRKIASWA-KGVGLEtnlklmgGESP 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 406 IVRNNSLWDKLIFHKIQSSLG-GKVRLMITGAAPVSATVLTFLrTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAP 484
Cdd:cd05933 298 SPLFYRLAKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 485 MPCNYVKLVDVEemnylaSKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLA 564
Cdd:cd05933 377 LPGCKTKIHNPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITA 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 565 QGEYIAPEKIEN-IYLRSEAVAQVFVHGESLQaFLIAVVVPDVESLPswaqKRGLQG---SFE--ELCRNKDINKAILDD 638
Cdd:cd05933 451 GGENVPPVPIEDaVKKELPIISNAMLIGDKRK-FLSMLLTLKCEVNP----ETGEPLdelTEEaiEFCRKLGSQATRVSE 525
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039782744 639 LLKLGKEAGLKPFEQ---------------VKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELY 694
Cdd:cd05933 526 IAGGKDPKVYEAIEEgikrvnkkaisnaqkIQKWVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
148-672 |
6.79e-66 |
|
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: 228.11 E-value: 6.79e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 148 EQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFADkPEKAKLLLEGVENKLTPclKIIVI 227
Cdd:cd17632 93 GDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVS-AEHLDLAVEAVLEGGTP--PRLVV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 228 MDSYGSDLVER-----------GKKCGVEIISLKALEDLGrVNRVKPKPPEPED--LAIICFTSGTTGNPKGAMITHQNI 294
Cdd:cd17632 170 FDHRPEVDAHRaalesarerlaAVGIPVTTLTLIAVRGRD-LPPAPLFRPEPDDdpLALLIYTSGSTGTPKGAMYTERLV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 295 IN---DCSGFIKATESAFIastddvLISFLPLAHMFETVVECVMLCHGAkIGFFQG--DIRLLMDDLKVLQPTIFPVVPR 369
Cdd:cd17632 249 ATfwlKVSSIQDIRPPASI------TLNFMPMSHIAGRISLYGTLARGG-TAYFAAasDMSTLFDDLALVRPTELFLVPR 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 370 LLNRMFDRIfgQAntSLKRWLLDFA-----SKRKEAELRsgivrnnslwdklifhkiQSSLGGKVRLMITGAAPVSATVL 444
Cdd:cd17632 322 VCDMLFQRY--QA--ELDRRSVAGAdaetlAERVKAELR------------------ERVLGGRLLAAVCGSAPLSAEMK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 445 TFLRTALGCQFYEGYGQTEctAGCCLSLpgdwtaGHVGAPMPCNYvKLVDVEEMNYLASKG---EGEVCVKGANVFKGYL 521
Cdd:cd17632 380 AFMESLLDLDLHDGYGSTE--AGAVILD------GVIVRPPVLDY-KLVDVPELGYFRTDRphpRGELLVKTDTLFPGYY 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 522 KDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAV 601
Cdd:cd17632 451 KRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNSERAYLLAV 530
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039782744 602 VVPdveslpswAQKRGLQGSFEELcrnkdiNKAILDDLLKLGKEAGLKPFEQVKGIAVHPELFSIDNGLLT 672
Cdd:cd17632 531 VVP--------TQDALAGEDTARL------RAALAESLQRIAREAGLQSYEIPRDFLIETEPFTIANGLLS 587
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
122-679 |
1.36e-65 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 226.92 E-value: 1.36e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 122 ISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGR--GDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 202 DKPEKAKLLLEgVENKLtPCLKIIVIMDSYGSDLVERGKkcgveIISLKALEDLGR-VNRVKPKPPE-------PEDLAI 273
Cdd:cd17641 90 EDEEQVDKLLE-IADRI-PSVRYVIYCDPRGMRKYDDPR-----LISFEDVVALGRaLDRRDPGLYErevaagkGEDVAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 274 ICFTSGTTGNPKGAMITHQNIINDCSGFIKATesaFIASTDDVLiSFLPLAHMFETVVECVM-LCHGAKIGFFQgDIRLL 352
Cdd:cd17641 163 LCTTSGTTGKPKLAMLSHGNFLGHCAAYLAAD---PLGPGDEYV-SVLPLPWIGEQMYSVGQaLVCGFIVNFPE-EPETM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 353 MDDLKVLQPTIFPVVPRLLNRM--FDRIFGQANTSLKRWLLDF--------ASKRKEAELRSGIVRNNS-LWDKLIFHKI 421
Cdd:cd17641 238 MEDLREIGPTFVLLPPRVWEGIaaDVRARMMDATPFKRFMFELgmklglraLDRGKRGRPVSLWLRLASwLADALLFRPL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 422 QSSLG-GKVRLMITGAAPVSATVLTFLRtALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDVeemny 500
Cdd:cd17641 318 RDRLGfSRLRSAATGGAALGPDTFRFFH-AIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEV----- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 501 laskgeGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIEN---- 576
Cdd:cd17641 392 ------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENklkf 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 577 -IYLRsEAVaqVFVHGeslQAFLIAVVVPDVESLPSWAQKRGLQ-GSFEELCRNKDINKAILDDLLKLGKEagLKPFEQV 654
Cdd:cd17641 466 sPYIA-EAV--VLGAG---RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKVNAS--LPEAQRI 537
|
570 580
....*....|....*....|....*
gi 1039782744 655 KGIAVHPELFSIDNGLLTPTLKAKR 679
Cdd:cd17641 538 RRFLLLYKELDADDGELTRTRKVRR 562
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
270-616 |
1.47e-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: 219.85 E-value: 1.47e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 270 DLAIICFTSGTTGNPKGAMITHQNIIndcsGFIKATESAFIASTDDVLISFLPLAHMFETVVECVMLCHGAKI----GFF 345
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLL----AAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVvllpKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 346 QGDIRLLMDDLKVlqpTIFPVVPRLLNRMFDRIfgqantslkrwlldfasKRKEAELRSgivrnnslwdklifhkiqssl 425
Cdd:cd04433 77 PEAALELIEREKV---TILLGVPTLLARLLKAP-----------------ESAGYDLSS--------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 426 ggkVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWT--AGHVGAPMPCNYVKLVDVEEmNYLAS 503
Cdd:cd04433 116 ---LRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDPDG-GELPP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 504 KGEGEVCVKGANVFKGYLKDPARTAEAlDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEA 583
Cdd:cd04433 192 GEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPG 269
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1039782744 584 VAQVFVHG---ESLQAFLIAVVVP------DVESLPSWAQKR 616
Cdd:cd04433 270 VAEAAVVGvpdPEWGERVVAVVVLrpgadlDAEELRAHVRER 311
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
122-679 |
6.06e-65 |
|
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: 222.32 E-value: 6.06e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 122 ISYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDR--VALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 202 DkpekaklllegvenkltpclkiivimdsygsdlvergkkcgveiislkaledlgrvnrvkpkppEPEDLAIICFTSGTT 281
Cdd:cd05914 86 S----------------------------------------------------------------DEDDVALINYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 282 GNPKGAMITHQNIINDCSGfIKATEsafIASTDDVLISFLPLAHMFETVVECVM-LCHGAKIGFFQGDIRLLMDDLKVLQ 360
Cdd:cd05914 102 GNSKGVMLTYRNIVSNVDG-VKEVV---LLGKGDKILSILPLHHIYPLTFTLLLpLLNGAHVVFLDKIPSAKIIALAFAQ 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 361 PTIFPVVPRLLNRMFDRIFGQANTSLKRWLLdfaskrkeaeLRSGIVRNNSLWDKLIFHKIQSSLGGKVRLMITGAAPVS 440
Cdd:cd05914 178 VTPTLGVPVPLVIEKIFKMDIIPKLTLKKFK----------FKLAKKINNRKIRKLAFKKVHEAFGGNIKEFVIGGAKIN 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 441 ATVLTFLRTaLGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPmpcnyVKLVDVEEMNYLASKGEGEVCVKGANVFKGY 520
Cdd:cd05914 248 PDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKV-----IDGVEVRIDSPDPATGEGEIIVRGPNVMKGY 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 521 LKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQ--VFV-HGEslqaf 597
Cdd:cd05914 322 YKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLEslVVVqEKK----- 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 598 LIAVVVPDveslPSWAQKRGLQgsfeelcrNKDINKAILDDLL-KLGKEagLKPFEQVKGIAVHPELFSidnglLTPTLK 676
Cdd:cd05914 397 LVALAYID----PDFLDVKALK--------QRNIIDAIKWEVRdKVNQK--VPNYKKISKVKIVKEEFE-----KTPKGK 457
|
...
gi 1039782744 677 AKR 679
Cdd:cd05914 458 IKR 460
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
120-609 |
2.85e-63 |
|
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: 217.82 E-value: 2.85e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 120 EWISYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVI 199
Cdd:cd05936 23 RKLTYRELDALAEAFAAGLQNLGVQPGDR--VALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 200 FADKPEKaklllegvenkltpclkiivimdsygsDLVERGKKcgveiislkaledlgrvnRVKPKPPEPEDLAIICFTSG 279
Cdd:cd05936 101 IVAVSFT---------------------------DLLAAGAP------------------LGERVALTPEDVAVLQYTSG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 280 TTGNPKGAMITHQNI---INDCSGFIKATESAfiastDDVLISFLPLAHMF-ETVVECVMLCHGAKIGFFQG-DIRLLMD 354
Cdd:cd05936 136 TTGVPKGAMLTHRNLvanALQIKAWLEDLLEG-----DDVVLAALPLFHVFgLTVALLLPLALGATIVLIPRfRPIGVLK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 355 DLKVLQPTIFPVVPRLLNRMFDrifgqantslkrwlldfASKRKEAELRSgivrnnslwdklifhkiqsslggkVRLMIT 434
Cdd:cd05936 211 EIRKHRVTIFPGVPTMYIALLN-----------------APEFKKRDFSS------------------------LRLCIS 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 435 GAAPVSATVLTFLRTALGCQFYEGYGQTECT-AGCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKG 513
Cdd:cd05936 250 GGAPLPVEVAERFEELTGVPIVEGYGLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVD-DDGEELPPGEVGELWVRG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 514 ANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFV---- 589
Cdd:cd05936 329 PQVMKGYWNRPEETAEAF-VDGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGGFNVYPREVEEVLYEHPAVAEAAVvgvp 406
|
490 500
....*....|....*....|...
gi 1039782744 590 ---HGESLQAFliaVVVPDVESL 609
Cdd:cd05936 407 dpySGEAVKAF---VVLKEGASL 426
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
122-591 |
2.34e-62 |
|
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: 215.92 E-value: 2.34e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 122 ISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKK--GDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 202 DKPEKAKLLleGVENKLTPCLKIIVIMDSygsdlvergKKCGVEIISLKALEDLGRVNRVKPKPPE-PEDLAIICFTSGT 280
Cdd:cd05911 89 DPDGLEKVK--EAAKELGPKDKIIVLDDK---------PDGVLSIEDLLSPTLGEEDEDLPPPLKDgKDDTAAILYSSGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 281 TGNPKGAMITHQNIINDCSGFIKATESAFiaSTDDVLISFLPLAHMFETVVECVMLCHGAK-IGFFQGDIRLLMDDLKVL 359
Cdd:cd05911 158 TGLPKGVCLSHRNLIANLSQVQTFLYGND--GSNDVILGFLPLYHIYGLFTTLASLLNGATvIIMPKFDSELFLDLIEKY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 360 QPTIFPVVPRLLNRMFdrifgqantslkrwlldfaskrkeaelRSGIVRNNSLwdklifhkiqSSLggkvRLMITGAAPV 439
Cdd:cd05911 236 KITFLYLVPPIAAALA---------------------------KSPLLDKYDL----------SSL----RVILSGGAPL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 440 SATVLTFLRTALG-CQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPcNY-VKLVDVEEMNYLASKGEGEVCVKGANVF 517
Cdd:cd05911 275 SKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLP-NVeAKIVDDDGKDSLGPNEPGEICVRGPQVM 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039782744 518 KGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:cd05911 354 KGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAVLLEHPGVADAAVIG 426
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
122-616 |
1.38e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 208.99 E-value: 1.38e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 122 ISYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGKGDR--VAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 202 dkpekAKLLLeGVENKLT---PCLKIIVIMDSYGSDLVERGKKCGVEIISLKalEDLGRVNRVKPkppepEDLAIICFTS 278
Cdd:PRK07656 109 -----LGLFL-GVDYSATtrlPALEHVVICETEEDDPHTEKMKTFTDFLAAG--DPAERAPEVDP-----DDVADILFTS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 279 GTTGNPKGAMITHQNIIndcSGFIKATESAFIASTDDVLISfLPLAHMF---ETVVECVMlcHGAKIgffqgDIRLLMDD 355
Cdd:PRK07656 176 GTTGRPKGAMLTHRQLL---SNAADWAEYLGLTEGDRYLAA-NPFFHVFgykAGVNAPLM--RGATI-----LPLPVFDP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 356 LKVLQ------PTIFPVVPRLLNRMFDrifgqantslkrwlldfASKRKEAELRSgivrnnslwdklifhkiqsslggkV 429
Cdd:PRK07656 245 DEVFRlieterITVLPGPPTMYNSLLQ-----------------HPDRSAEDLSS------------------------L 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 430 RLMITGAAPVSATVLTFLRTALGCQ-FYEGYGQTECTAGCCLSLPGD---WTAGHVGAPMPCNYVKLVDvEEMNYLASKG 505
Cdd:PRK07656 284 RLAVTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIAGVENKIVN-ELGEEVPVGE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 506 EGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVA 585
Cdd:PRK07656 363 VGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IVGGFNVYPAEVEEVLYEHPAVA 441
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1039782744 586 QVFV-------HGESLQAFLIAVVVPDV--ESLPSWAQKR 616
Cdd:PRK07656 442 EAAVigvpderLGEVGKAYVVLKPGAELteEELIAYCREH 481
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
122-605 |
1.31e-56 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 201.18 E-value: 1.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 122 ISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:PRK06187 32 TTYAELDERVNRLANALRALGVKK--GDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 202 DkPEKAKLLlEGVENKLTPCLKIIVIMDSYGSDLVERGKkcgveiislkALEDLgrVNRVKPKPPEPE----DLAIICFT 277
Cdd:PRK06187 110 D-SEFVPLL-AAILPQLPTVRTVIVEGDGPAAPLAPEVG----------EYEEL--LAAASDTFDFPDidenDAAAMLYT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 278 SGTTGNPKGAMITHQNIIndcsGFIKATESAFIASTDDVLISFLPLAHMFETVVECVMLCHGAKI---GFFqgDIRLLMD 354
Cdd:PRK06187 176 SGTTGHPKGVVLSHRNLF----LHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLALMAGAKQvipRRF--DPENLLD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 355 DLKVLQPTIFPVVPRLLNRMFdrifgQANTSLKRWLldfaskrkeaelrsgivrnnslwdklifhkiqSSLggkvRLMIT 434
Cdd:PRK06187 250 LIETERVTFFFAVPTIWQMLL-----KAPRAYFVDF--------------------------------SSL----RLVIY 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 435 GAAPVSATVLTFLRTALGCQFYEGYGQTECT-AGCCL----SLPGDWT-AGHVGAPMPCNYVKLVDvEEMNYLASKGE-- 506
Cdd:PRK06187 289 GGAALPPALLREFKEKFGIDLVQGYGMTETSpVVSVLppedQLPGQWTkRRSAGRPLPGVEARIVD-DDGDELPPDGGev 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 507 GEVCVKGANVFKGYLKDPARTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQ 586
Cdd:PRK06187 368 GEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIKDVIISG-GENIYPRELEDALYGHPAVAE 445
|
490 500
....*....|....*....|
gi 1039782744 587 VfvhgeslqafliAVV-VPD 605
Cdd:PRK06187 446 V------------AVIgVPD 453
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
122-605 |
5.15e-44 |
|
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: 163.94 E-value: 5.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 122 ISYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFa 201
Cdd:cd17631 21 LTYAELDERVNRLAHALRALGVAKGDR--VAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 202 dkpekaklllegvenkltpclkiivimdsygsdlvergkkcgveiislkaledlgrvnrvkpkppepEDLAIICFTSGTT 281
Cdd:cd17631 98 -------------------------------------------------------------------DDLALLMYTSGTT 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 282 GNPKGAMITHQNIINDCSGFIkateSAFIASTDDVLISFLPLAHMFETVVECVM-LCHGAKI----GFfqgDIRLLMDDL 356
Cdd:cd17631 111 GRPKGAMLTHRNLLWNAVNAL----AALDLGPDDVLLVVAPLFHIGGLGVFTLPtLLRGGTVvilrKF---DPETVLDLI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 357 KVLQPTIFPVVPRLLNRMFDRifgqantslkrwlldfaSKRKEAELrsgivrnnslwdklifhkiqSSLggkvRLMITGA 436
Cdd:cd17631 184 ERHRVTSFFLVPTMIQALLQH-----------------PRFATTDL--------------------SSL----RAVIYGG 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 437 APVSATVLTFLRtALGCQFYEGYGQTECTAGCCLSLPGDW--TAGHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGA 514
Cdd:cd17631 223 APMPERLLRALQ-ARGVKFVQGYGMTETSPGVTFLSPEDHrrKLGSAGRPVFFVEVRIVD-PDGREVPPGEVGEIVVRGP 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 515 NVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEAVAQVFV----- 589
Cdd:cd17631 301 HVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDVLYEHPAVAEVAVigvpd 378
|
490
....*....|....*...
gi 1039782744 590 --HGESlqafLIAVVVPD 605
Cdd:cd17631 379 ekWGEA----VVAVVVPR 392
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
122-589 |
3.18e-42 |
|
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: 160.48 E-value: 3.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 122 ISYKE----VAELAECIGSGLIQKGfkpcseQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELS 197
Cdd:cd05904 33 LTYAElerrVRRLAAGLAKRGGRKG------DVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 198 VIFADkpekAKLLlegveNKLTPCLKIIVIMDSYGSDlvergkkcGVEIISLKALEDLGRVNRVKPKPpepEDLAIICFT 277
Cdd:cd05904 107 LAFTT----AELA-----EKLASLALPVVLLDSAEFD--------SLSFSDLLFEADEAEPPVVVIKQ---DDVAALLYS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 278 SGTTGNPKGAMITHQNIINDCSGFIKATESAFiaSTDDVLISFLPLAHMFE-TVVECVMLCHGAKI----GFfqgDIRLL 352
Cdd:cd05904 167 SGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNS--DSEDVFLCVLPMFHIYGlSSFALGLLRLGATVvvmpRF---DLEEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 353 MDDLKVLQPTIFPVVPRLLNRMfdrifgqantslkrwlldfaskrkeaeLRSGIVRNNSLwdklifhkiqSSLggkvRLM 432
Cdd:cd05904 242 LAAIERYKVTHLPVVPPIVLAL---------------------------VKSPIVDKYDL----------SSL----RQI 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 433 ITGAAPVSATVL-TFLRTALGCQFYEGYGQTECTAG---CCLSLPGDWTAGHVGAPMPCNYVKLVDVEEMNYLASKGEGE 508
Cdd:cd05904 281 MSGAAPLGKELIeAFRAKFPNVDLGQGYGMTESTGVvamCFAPEKDRAKYGSVGRLVPNVEAKIVDPETGESLPPNQTGE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 509 VCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVF 588
Cdd:cd05904 361 LWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEALLLSHPEILDAA 439
|
.
gi 1039782744 589 V 589
Cdd:cd05904 440 V 440
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
270-616 |
4.86e-42 |
|
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: 158.61 E-value: 4.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 270 DLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKA---TEsafiastDDVLISFLPLAHMFETVV----------ECVML 336
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAwrwTE-------DDVLLHVLPLHHVHGLVNallcplfagaSVEFL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 337 chgakiGFF---QGDIRLLMDDLkvlqpTIFPVVPRllnrMFDRIFGQANTSLKrwllDFASKRKEAElrsgivrnnslw 413
Cdd:cd05941 163 ------PKFdpkEVAISRLMPSI-----TVFMGVPT----IYTRLLQYYEAHFT----DPQFARAAAA------------ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 414 dklifhkiqsslgGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTEctAGCCLSLP--GDWTAGHVGAPMPCNYVK 491
Cdd:cd05941 212 -------------ERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQAR 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 492 LVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK-HIFKlAQGEYIA 570
Cdd:cd05941 277 IVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVS 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039782744 571 PEKIENIYLRSEAVAQVFVHGESLQAF---LIAVVVP-------DVESLPSWAQKR 616
Cdd:cd05941 356 ALEIERVLLAHPGVSECAVIGVPDPDWgerVVAVVVLragaaalSLEELKEWAKQR 411
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
234-692 |
3.98e-41 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 160.65 E-value: 3.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 234 DLVERGKKCGVEIISLKALEDlGRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIIN------DCSGFIKATES 307
Cdd:PTZ00342 270 DLKEKAKKLGISIILFDDMTK-NKTTNYKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNtvvplcKHSIFKKYNPK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 308 AFIastddvliSFLPLAHMFETVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQAN--TS 385
Cdd:PTZ00342 349 THL--------SYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINnlPP 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 386 LKRWLLdfaskRKEAELRSGivRNNSLWDKL---IFH---KIQSSLGGKVRLMITGAAPVSATVLTFLRTALGCQFYEGY 459
Cdd:PTZ00342 421 LKRFLV-----KKILSLRKS--NNNGGFSKFlegITHissKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGY 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 460 GQTECTAGCCLSLPGDWTAGHVGAPM-PCNYVKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLH 538
Cdd:PTZ00342 494 GLTETTGPIFVQHADDNNTESIGGPIsPNTKYKVRTWETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFK 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 539 TGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAVVVPDVESLPSWAQKRGL 618
Cdd:PTZ00342 574 TGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGDDSMDGPLAIISVDKYLLFKCLKDDNM 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 619 ---QGSFEELCRNK----DINKAILDD-----LLKLGKEAGLKPFEQVKGIAVHPELFSIDNgLLTPTLKAKRPELRNYF 686
Cdd:PTZ00342 654 lesTGINEKNYLEKltdeTINNNIYVDyvkgkMLEVYKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKRFYVFKDY 732
|
....*.
gi 1039782744 687 RSQIDE 692
Cdd:PTZ00342 733 AFFIDQ 738
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
122-577 |
2.18e-39 |
|
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: 152.10 E-value: 2.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 122 ISYKEVAeLAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:cd05909 8 LTYRKLL-TGAIALARKLAKMTKE--GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 202 DKPEKAKLLLEGVENKLTPClKIIVIMDSYGSdlVERGKKCGVEIISLKALEDLGRVNRVKPKppEPEDLAIICFTSGTT 281
Cdd:cd05909 85 SKQFIEKLKLHHLFDVEYDA-RIVYLEDLRAK--ISKADKCKAFLAGKFPPKWLLRIFGVAPV--QPDDPAVILFTSGSE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 282 GNPKGAMITHQNIINDcsgfIKATESAFIASTDDVLISFLPLAHMFetvvecvmlchgakiGFFQGDIRLLMDDLKVLQ- 360
Cdd:cd05909 160 GLPKGVVLSHKNLLAN----VEQITAIFDPNPEDVVFGALPFFHSF---------------GLTGCLWLPLLSGIKVVFh 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 361 --PTIFPVVPRLLNRMFDRIFGQANTSLKRWLldfasKRKEAELRSGIvrnnslwdklifhkiqsslggkvRLMITGAAP 438
Cdd:cd05909 221 pnPLDYKKIPELIYDKKATILLGTPTFLRGYA-----RAAHPEDFSSL-----------------------RLVVAGAEK 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 439 VSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPG-DWTAGHVGAPMPCNYVKLVDVEEMNYLASKGEGEVCVKGANVF 517
Cdd:cd05909 273 LKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVM 352
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 518 KGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 577
Cdd:cd05909 353 LGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDI 410
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
268-599 |
5.64e-39 |
|
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: 147.42 E-value: 5.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 268 PEDLAIICFTSGTTGNPKGAMITHQNIINDcsGFIKATESAFiaSTDDVLISFLPLAHMFETVVEcVMLC--HGAKIGFf 345
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNN--GYFIGERLGL--TEQDRLCIPVPLFHCFGSVLG-VLACltHGATMVF- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 346 qgdIRLLMDDLKVLQ-------------PTIFPvvpRLLNRMFDRIFgqantslkrwllDFASkrkeaeLRSGIvrnnsl 412
Cdd:cd05917 75 ---PSPSFDPLAVLEaiekekctalhgvPTMFI---AELEHPDFDKF------------DLSS------LRTGI------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 413 wdklifhkiqsslggkvrlmiTGAAPVSATVLTFLRTALGC-QFYEGYGQTECTAGCCLSLPGD---WTAGHVGAPMPCN 488
Cdd:cd05917 125 ---------------------MAGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDsieKRVNTVGRIMPHT 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 489 YVKLVDvEEMNYLASKGE-GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGE 567
Cdd:cd05917 184 EAKIVD-PEGGIVPPVGVpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGE 261
|
330 340 350
....*....|....*....|....*....|....*....
gi 1039782744 568 YIAPEKIENIYLRSEAVAQVFV-------HGESLQAFLI 599
Cdd:cd05917 262 NIYPREIEEFLHTHPKVSDVQVvgvpderYGEEVCAWIR 300
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
124-644 |
6.47e-39 |
|
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: 149.52 E-value: 6.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 124 YKEVAELAECIGSGLIQKGfkpcseQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFADk 203
Cdd:TIGR01923 6 DCEAAHLAKALKAQGIRSG------SRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 204 pekAKLLLEGVEnkltpclkiivimdsygSDLVERGKKCGVEIISLKALEDLgrvnrvkpkppepEDLAIICFTSGTTGN 283
Cdd:TIGR01923 79 ---SLLEEKDFQ-----------------ADSLDRIEAAGRYETSLSASFNM-------------DQIATLMFTSGTTGK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 284 PKGAMITHQNIINDCSGfikATESAFIASTDDVLISfLPLAH------MFETVVEcvmlchGAKIGFFQGDIRLLmDDLK 357
Cdd:TIGR01923 126 PKAVPHTFRNHYASAVG---SKENLGFTEDDNWLLS-LPLYHisglsiLFRWLIE------GATLRIVDKFNQLL-EMIA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 358 VLQPTIFPVVPRLLNRMFDRifGQANTSLKRWLLdfaskrkeaelrsgivrnnslwdklifhkiqsslggkvrlmitGAA 437
Cdd:TIGR01923 195 NERVTHISLVPTQLNRLLDE--GGHNENLRKILL-------------------------------------------GGS 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 438 PVSATVLTFLRTaLGCQFYEGYGQTE-CTAGCCLSLPGDWTAGHVGAPMPCNYVKL-VDVEEmnylaskGEGEVCVKGAN 515
Cdd:TIGR01923 230 AIPAPLIEEAQQ-YGLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIkVDNKE-------GHGEIMVKGAN 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 516 VFKGYLkDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVhgeslq 595
Cdd:TIGR01923 302 LMKGYL-YQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVV------ 373
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1039782744 596 afliaVVVPDVEslpsWAQKRGLQGSFeelcrNKDINKAILDDLL--KLGK 644
Cdd:TIGR01923 374 -----VPKPDAE----WGQVPVAYIVS-----ESDISQAKLIAYLteKLAK 410
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
173-609 |
7.35e-39 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 151.74 E-value: 7.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 173 MVVV---PLY----------DTlGADAITYIVNkaelsviFADKPEKAklllegVENklTPCLKiiVIMDSYGsDLVERG 239
Cdd:PRK08974 99 MIVVnvnPLYtprelehqlnDS-GAKAIVIVSN-------FAHTLEKV------VFK--TPVKH--VILTRMG-DQLSTA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 240 KKCGVEI-----------------ISL-KALEDLGRVNRVKPKPpEPEDLAIICFTSGTTGNPKGAMITHQNIINDCSGf 301
Cdd:PRK08974 160 KGTLVNFvvkyikrlvpkyhlpdaISFrSALHKGRRMQYVKPEL-VPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQ- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 302 IKATESAFIASTDDVLISFLPLAHMFETVVECVMLCH-GAKigffqgdirllmdDLKVLQPTIFP-VVPRLLNRMFDRIF 379
Cdd:PRK08974 238 AKAAYGPLLHPGKELVVTALPLYHIFALTVNCLLFIElGGQ-------------NLLITNPRDIPgFVKELKKYPFTAIT 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 380 GqANTSLKRWLldfaskrkeaelrsgivrNNSLWDKLIFhkiqSSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGY 459
Cdd:PRK08974 305 G-VNTLFNALL------------------NNEEFQELDF----SSL----KLSVGGGMAVQQAVAERWVKLTGQYLLEGY 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 460 GQTECT---AGCCLSLPGdwTAGHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALdKDGW 536
Cdd:PRK08974 358 GLTECSplvSVNPYDLDY--YSGSIGLPVPSTEIKLVD-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGW 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 537 LHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVF-------VHGESLQAFliavVVPDVESL 609
Cdd:PRK08974 434 LATGDIAVMDEEGFLRIVDRKKDMI-LVSGFNVYPNEIEDVVMLHPKVLEVAavgvpseVSGEAVKIF----VVKKDPSL 508
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
120-616 |
7.97e-39 |
|
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: 150.54 E-value: 7.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 120 EWISYKEVAELAECIGSGLIQKGFKPCSEQFIGLFsqNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVI 199
Cdd:cd05926 13 PALTYADLAELVDDLARQLAALGIKKGDRVAIALP--NGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 200 FADKPEkaklLLEGVENKLTPCLKII-VIMDSYGSDLVERGKkcgveiiSLKALEDLGRVNRvKPKPPEPEDLAIICFTS 278
Cdd:cd05926 91 LTPKGE----LGPASRAASKLGLAILeLALDVGVLIRAPSAE-------SLSNLLADKKNAK-SEGVPLPDDLALILHTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 279 GTTGNPKGAMITHQNIindcsgfikATESAFIAST-----DDVLISFLPLAHMFETVVECV-MLCHGAKI----GFfqgD 348
Cdd:cd05926 159 GTTGRPKGVPLTHRNL---------AASATNITNTykltpDDRTLVVMPLFHVHGLVASLLsTLAAGGSVvlppRF---S 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 349 IRLLMDDLKVLQPTIFPVVPRLLnrmfdrifgqantslkRWLLDFASKRKEAELrsgivrnnslwdklifhkiqsslgGK 428
Cdd:cd05926 227 ASTFWPDVRDYNATWYTAVPTIH----------------QILLNRPEPNPESPP------------------------PK 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 429 VRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTE-CTAGCCLSLPGDW-TAGHVGAPmpcNYVKLVDV-EEMNYLASKG 505
Cdd:cd05926 267 LRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEaAHQMTSNPLPPGPrKPGSVGKP---VGVEVRILdEDGEILPPGV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 506 EGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVA 585
Cdd:cd05926 344 VGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVLLSHPAVL 422
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1039782744 586 Q--VF-----VHGESLQafliAVVVP------DVESLPSWAQKR 616
Cdd:cd05926 423 EavAFgvpdeKYGEEVA----AAVVLregasvTEEELRAFCRKH 462
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
122-591 |
7.21e-38 |
|
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: 148.44 E-value: 7.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 122 ISYKEVAELAECIGSGLIQKGFKpcSEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:cd17642 45 YSYAEYLEMSVRLAEALKKYGLK--QNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFC 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 202 DKPEKAKLLleGVENKLtPCLKIIVIMDSYgSDLveRGKKCgveIISLKALEDLGRVNRVKPKPPE---PEDLAIICFTS 278
Cdd:cd17642 123 SKKGLQKVL--NVQKKL-KIIKTIIILDSK-EDY--KGYQC---LYTFITQNLPPGFNEYDFKPPSfdrDEQVALIMNSS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 279 GTTGNPKGAMITHQNIindCSGFIKATESAFIA--STDDVLISFLPLAHMFETVVECVMLCHGAKIGF---FQGDIRL-L 352
Cdd:cd17642 194 GSTGLPKGVQLTHKNI---VARFSHARDPIFGNqiIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLmykFEEELFLrS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 353 MDDLKV----LQPTIFPVVPrllnrmfdrifgqantslKRWLLDfaskrkeaelrsgivrnnsLWDKLIFHKIQSslggk 428
Cdd:cd17642 271 LQDYKVqsalLVPTLFAFFA------------------KSTLVD-------------------KYDLSNLHEIAS----- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 429 vrlmitGAAPVSATVLTFLRTALGCQFY-EGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDVEEMNYLASKGEG 507
Cdd:cd17642 309 ------GGAPLSKEVGEAVAKRFKLPGIrQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 508 EVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQV 587
Cdd:cd17642 383 ELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQHPKIFDA 461
|
....
gi 1039782744 588 FVHG 591
Cdd:cd17642 462 GVAG 465
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
255-609 |
5.70e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 143.37 E-value: 5.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 255 LGRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIINDCSGfIKATESAFIASTDDVLISFLPLAHMFETVVECV 334
Cdd:PRK05677 193 KGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQ-CRALMGSNLNEGCEILIAPLPLYHIYAFTFHCM 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 335 MLchgakigffqgdirLLMDDLKVLQPTifpvvPRLLNRMFdrifgqanTSLKRWLLdfaskrkeaelrSGIVRNNSLWD 414
Cdd:PRK05677 272 AM--------------MLIGNHNILISN-----PRDLPAMV--------KELGKWKF------------SGFVGLNTLFV 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 415 KLI----FHKIQSSlggKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYV 490
Cdd:PRK05677 313 ALCnneaFRKLDFS---ALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLC 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 491 KLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIA 570
Cdd:PRK05677 390 KVID-DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVSGFNVY 467
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1039782744 571 PEKIENIYLRSEAVAQVFV-------HGESLQAFliaVVVPDVESL 609
Cdd:PRK05677 468 PNELEDVLAALPGVLQCAAigvpdekSGEAIKVF---VVVKPGETL 510
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
123-629 |
9.29e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 139.52 E-value: 9.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 123 SYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELS-VIFA 201
Cdd:PRK12583 47 TWRQLADAVDRLARGLLALGVQPGDR--VGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRwVICA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 202 DK--------------PEKAKLLLEGVENKLTPCLKIIVIMDSYGS-------DLVERGkkcgvEIISLKALEDlgrvnr 260
Cdd:PRK12583 125 DAfktsdyhamlqellPGLAEGQPGALACERLPELRGVVSLAPAPPpgflawhELQARG-----ETVSREALAE------ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 261 vKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIINDcsGFIKATESAFIAStdDVLISFLPLAHMFETVVeCVMLC--H 338
Cdd:PRK12583 194 -RQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNN--GYFVAESLGLTEH--DRLCVPVPLYHCFGMVL-ANLGCmtV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 339 GAKIgFFQGDirlLMDDLKVLQ-------------PTIFpvVPRLLNRMFDRifgqantslkrwlLDFASkrkeaeLRSG 405
Cdd:PRK12583 268 GACL-VYPNE---AFDPLATLQaveeerctalygvPTMF--IAELDHPQRGN-------------FDLSS------LRTG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 406 IVrnnslwdklifhkiqsslggkvrlmitGAAPVSATVLTFLRTALGC-QFYEGYGQTECTAGCCLSLPGD---WTAGHV 481
Cdd:PRK12583 323 IM---------------------------AGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSLQTTAADdleRRVETV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 482 GAPMPCNYVKLVDVEEmNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIF 561
Cdd:PRK12583 376 GRTQPHLEVKVVDPDG-ATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMI 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039782744 562 kLAQGEYIAPEKIENIYLRSEAVAQVFVHGeslqafliavvVPDV---ESLPSWAQKR-GLQGSFEEL---CRNK 629
Cdd:PRK12583 455 -IRGGENIYPREIEEFLFTHPAVADVQVFG-----------VPDEkygEEIVAWVRLHpGHAASEEELrefCKAR 517
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
267-611 |
1.42e-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: 136.89 E-value: 1.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 267 EPEDLAIICFTSGTTGNPKGAMITHQNIINdcsgFIKATESAFIASTDDVLISFLPLA---HMFETvveCVMLCHGAKI- 342
Cdd:cd05930 91 DPDDLAYVIYTSGSTGKPKGVMVEHRGLVN----LLLWMQEAYPLTPGDRVLQFTSFSfdvSVWEI---FGALLAGATLv 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 343 ---GFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTSLkrwlldfaskrkeaelrsgivrnnslwdklifh 419
Cdd:cd05930 164 vlpEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAALPSL--------------------------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 420 kiqsslggkvRLMITGAAPVSATVLTFLRTAL-GCQFYEGYGQTECTAGCCL--SLPGDWTAGHV--GAPMPCNYVKLVD 494
Cdd:cd05930 211 ----------RLVLVGGEALPPDLVRRWRELLpGARLVNLYGPTEATVDATYyrVPPDDEEDGRVpiGRPIPNTRVYVLD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 495 vEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEA-----LDKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLAqGEY 568
Cdd:cd05930 281 -ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYR 358
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1039782744 569 IAPEKIENIYLRSEAVAQVFV---HGESLQAFLIAVVVPDVESLPS 611
Cdd:cd05930 359 IELGEIEAALLAHPGVREAAVvarEDGDGEKRLVAYVVPDEGGELD 404
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
247-600 |
1.50e-34 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 138.80 E-value: 1.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 247 ISLKALEDLGRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIIND------CSGFIKATESAFIASTDDVLISF 320
Cdd:PRK12492 185 VPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANmlqvraCLSQLGPDGQPLMKEGQEVMIAP 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 321 LPLAHMFETVVECVMLchgakigFFQGDIRLLMDDlkvlqptifpvvPRLLNRMFDRifgqantsLKRWLLdfaskrkea 400
Cdd:PRK12492 265 LPLYHIYAFTANCMCM-------MVSGNHNVLITN------------PRDIPGFIKE--------LGKWRF--------- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 401 elrSGIVRNNSLWDKLIFHKIQSSLGGKvRLMIT---GAAPVSATVLTFlRTALGCQFYEGYGQTECTAGCCLSLPGDWT 477
Cdd:PRK12492 309 ---SALLGLNTLFVALMDHPGFKDLDFS-ALKLTnsgGTALVKATAERW-EQLTGCTIVEGYGLTETSPVASTNPYGELA 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 478 A-GHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDR 556
Cdd:PRK12492 384 RlGTVGIPVPGTALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDR 462
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1039782744 557 KKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFV-------HGESLQAFLIA 600
Cdd:PRK12492 463 KKDLI-IVSGFNVYPNEIEDVVMAHPKVANCAAigvpderSGEAVKLFVVA 512
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
122-616 |
1.61e-34 |
|
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: 1.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 122 ISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRP--GDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 202 DkpekaklllegvenkltpclkiivimdsygsdlvergkkcgveiislkaledlgrvnrvkpkppepedLAIICFTSGTT 281
Cdd:cd05934 82 D--------------------------------------------------------------------PASILYTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 282 GNPKGAMITHQNIINDCSGFIKAtesaFIASTDDVLISFLPLAHMFETVVEC-VMLCHGAKI--------GFFQGDIRll 352
Cdd:cd05934 94 GPPKGVVITHANLTFAGYYSARR----FGLGEDDVYLTVLPLFHINAQAVSVlAALSVGATLvllprfsaSRFWSDVR-- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 353 mddlkVLQPTIF---PVVPRLLNRMFDRIFGQANtslkrwlldfaskrkeaelrsgivrnnslwdklifhkiqsslggKV 429
Cdd:cd05934 168 -----RYGATVTnylGAMLSYLLAQPPSPDDRAH--------------------------------------------RL 198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 430 RLmITGAAPVSATVLTFLRtALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKGEGEV 509
Cdd:cd05934 199 RA-AYGAPNPPELHEEFEE-RFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVD-DDGQELPAGEPGEL 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 510 CVKGAN---VFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEAVAQ 586
Cdd:cd05934 276 VIRGLRgwgFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVERAILRHPAVRE 353
|
490 500 510
....*....|....*....|....*....|....*....
gi 1039782744 587 VFVHG----ESLQAFLIAVVVP-----DVESLPSWAQKR 616
Cdd:cd05934 354 AAVVAvpdeVGEDEVKAVVVLRpgetlDPEELFAFCEGQ 392
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
115-599 |
4.06e-34 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 137.63 E-value: 4.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 115 PNQPYEWiSYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVV---PLYDTlgaDAITYIV 191
Cdd:PRK08315 38 RDQGLRW-TYREFNEEVDALAKGLLALGIEKGDR--VGIWAPNVPEWVLTQFATAKIGAILVtinPAYRL---SELEYAL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 192 NKAELSVIF-ADK--------------PEKAKLLLEGVENKLTPCLKIIVIMDSYG-------SDLVERGKkcGVEIISL 249
Cdd:PRK08315 112 NQSGCKALIaADGfkdsdyvamlyelaPELATCEPGQLQSARLPELRRVIFLGDEKhpgmlnfDELLALGR--AVDDAEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 250 KALEDlgrvnRVKPkppepeDLAI-ICFTSGTTGNPKGAMITHQNIINDcsGFikatesaFIAST------DDVLISfLP 322
Cdd:PRK08315 190 AARQA-----TLDP------DDPInIQYTSGTTGFPKGATLTHRNILNN--GY-------FIGEAmklteeDRLCIP-VP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 323 LAHMFEtvveCVM-----LCHGAKI-----GFfqgdirllmDDLKVLQ-------------PTIFpvVPRLLNRMFDRif 379
Cdd:PRK08315 249 LYHCFG----MVLgnlacVTHGATMvypgeGF---------DPLATLAaveeerctalygvPTMF--IAELDHPDFAR-- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 380 gqantslkrwlLDFASkrkeaeLRSGIvrnnslwdklifhkiqssLGGK---VRLM-----------ITGAapvsatvlt 445
Cdd:PRK08315 312 -----------FDLSS------LRTGI------------------MAGSpcpIEVMkrvidkmhmseVTIA--------- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 446 flrtalgcqfyegYGQTECTAGCCLSLPGD------WTaghVGAPMPCNYVKLVDVEEMNYLASKGEGEVCVKGANVFKG 519
Cdd:PRK08315 348 -------------YGMTETSPVSTQTRTDDplekrvTT---VGRALPHLEVKIVDPETGETVPRGEQGELCTRGYSVMKG 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 520 YLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAV--AQVF-V----HGE 592
Cdd:PRK08315 412 YWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEFLYTHPKIqdVQVVgVpdekYGE 490
|
....*..
gi 1039782744 593 SLQAFLI 599
Cdd:PRK08315 491 EVCAWII 497
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
255-608 |
4.51e-34 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 137.70 E-value: 4.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 255 LGRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIIND---CSGFIKATESafIASTDDVLISFLPLAHMFETVV 331
Cdd:PRK08751 194 LGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANmqqAHQWLAGTGK--LEEGCEVVITALPLYHIFALTA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 332 ECVMLchgAKIGFFQG------DIRLLMDDLKVLQPTIFPVVPRLLNRMFdrifgqantslkrwlldfaskrkeaelrsg 405
Cdd:PRK08751 272 NGLVF---MKIGGCNHlisnprDMPGFVKELKKTRFTAFTGVNTLFNGLL------------------------------ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 406 ivrNNSLWDKLIFHKIQSSLGGkvrlmitGAApVSATVLTFLRTALGCQFYEGYGQTECTAGCCLS-LPGDWTAGHVGAP 484
Cdd:PRK08751 319 ---NTPGFDQIDFSSLKMTLGG-------GMA-VQRSVAERWKQVTGLTLVEAYGLTETSPAACINpLTLKEYNGSIGLP 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 485 MPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLA 564
Cdd:PRK08751 388 IPSTDACIKD-DAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-LV 465
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1039782744 565 QGEYIAPEKIENIYLRSEAVAQVfvhgeslqaflIAVVVPDVES 608
Cdd:PRK08751 466 SGFNVYPNEIEDVIAMMPGVLEV-----------AAVGVPDEKS 498
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
270-616 |
2.10e-33 |
|
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: 131.08 E-value: 2.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 270 DLAIICFTSGTTGNPKGAMITHQNIIndcSGFIKATESAFIASTDDVLIsFLPLAHMFETVVECVM-LCHGAKI---GFF 345
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTL---RAAAAWADCADLTEDDRYLI-INPFFHTFGYKAGIVAcLLTGATVvpvAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 346 qgDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRifgqantslkrwlldfaSKRKEAELrsgivrnnslwdklifhkiqSSL 425
Cdd:cd17638 77 --DVDAILEAIERERITVLPGPPTLFQSLLDH-----------------PGRKKFDL--------------------SSL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 426 ggkvRLMITGAAPVSATVLTFLRTALGCQ-FYEGYGQTECTAGCcLSLPGD---WTAGHVGAPMPCNYVKLVDveemnyl 501
Cdd:cd17638 118 ----RAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVAT-MCRPGDdaeTVATTCGRACPGFEVRIAD------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 502 askgEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRS 581
Cdd:cd17638 186 ----DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGALAEH 260
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1039782744 582 EAVAQVFV-------HGESLQAFLIAV--VVPDVESLPSWAQKR 616
Cdd:cd17638 261 PGVAQVAVigvpderMGEVGKAFVVARpgVTLTEEDVIAWCRER 304
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
182-612 |
3.80e-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: 134.30 E-value: 3.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 182 LGADAITYIVNKAELSVIFADkPEKAKLLlEGVENKLtPCLKIIVIMDSYGSDLVERGKKcgveiisLKALEDLgrVNRV 261
Cdd:cd12119 84 LFPEQIAYIINHAEDRVVFVD-RDFLPLL-EAIAPRL-PTVEHVVVMTDDAAMPEPAGVG-------VLAYEEL--LAAE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 262 KPKPPEPE----DLAIICFTSGTTGNPKGAMITHQNIINDCSGfIKATESAFIASTDdvliSFLPLAHMFE-----TVVE 332
Cdd:cd12119 152 SPEYDWPDfdenTAAAICYTSGTTGNPKGVVYSHRSLVLHAMA-ALLTDGLGLSESD----VVLPVVPMFHvnawgLPYA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 333 CVMLchGAKI----GFFQGDIRL-LMDDLKVlqpTIFPVVPRLLNRMFDrifgqantSLKRWLLDFASKRkeaelrsgiv 407
Cdd:cd12119 227 AAMV--GAKLvlpgPYLDPASLAeLIEREGV---TFAAGVPTVWQGLLD--------HLEANGRDLSSLR---------- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 408 rnnslwdklifhkiqsslggkvRLMITGAAPVSATVLTFLRtaLGCQFYEGYGQTE-CTAGCCLSLPGDWTAGHV----- 481
Cdd:cd12119 284 ----------------------RVVIGGSAVPRSLIEAFEE--RGVRVIHAWGMTEtSPLGTVARPPSEHSNLSEdeqla 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 482 -----GAPMPCNYVKLVDvEEMNYLASKGE--GEVCVKGANVFKGYLKDPaRTAEALDKDGWLHTGDIGKWLPNGTLKII 554
Cdd:cd12119 340 lrakqGRPVPGVELRIVD-DDGRELPWDGKavGELQVRGPWVTKSYYKND-EESEALTEDGWLRTGDVATIDEDGYLTIT 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039782744 555 DRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQVfvhgeslqafliAVV-VPDveslPSW 612
Cdd:cd12119 418 DRSKDVIKSG-GEWISSVELENAIMAHPAVAEA------------AVIgVPH----PKW 459
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
114-579 |
7.06e-33 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 133.72 E-value: 7.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 114 KPNQPYEWiSYKEVAELAECIGSGLIQKGFKP---CSEQFIGLfsqnrPEWVIVEQGCFSYSMVVVPLYDTLGADAITYI 190
Cdd:PRK06087 43 VDNHGASY-TYSALDHAASRLANWLLAKGIEPgdrVAFQLPGW-----CEFTIIYLACLKVGAVSVPLLPSWREAELVWV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 191 VNKAELSVIFADKPEKA----KLLLEgVENKLtPCLKIIVIMDSYGSDLVErgkkcgveiISL-KALEDLGRVNrvKPKP 265
Cdd:PRK06087 117 LNKCQAKMFFAPTLFKQtrpvDLILP-LQNQL-PQLQQIVGVDKLAPATSS---------LSLsQIIADYEPLT--TAIT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 266 PEPEDLAIICFTSGTTGNPKGAMITHQNIIndcsgfikATESAFIAST----DDVLISFLPLAHmfetvvecvmlchgaK 341
Cdd:PRK06087 184 THGDELAAVLFTSGTEGLPKGVMLTHNNIL--------ASERAYCARLnltwQDVFMMPAPLGH---------------A 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 342 IGFFQGDIR-LLMDDLKVLQPTIFPVVP-RLLNRmfdrifgQANTslkrWLL-------DFASKRKEAELRSgivrnnsl 412
Cdd:PRK06087 241 TGFLHGVTApFLIGARSVLLDIFTPDAClALLEQ-------QRCT----CMLgatpfiyDLLNLLEKQPADL-------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 413 wdklifhkiqSSLggkvRLMITGAAPVSATVLtflRTAL--GCQFYEGYGQTECTAGCCLSL--PGDWTAGHVGAPMPCN 488
Cdd:PRK06087 302 ----------SAL----RFFLCGGTTIPKKVA---RECQqrGIKLLSVYGSTESSPHAVVNLddPLSRFMHTDGYAAAGV 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 489 YVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEY 568
Cdd:PRK06087 365 EIKVVD-EARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGEN 442
|
490
....*....|.
gi 1039782744 569 IAPEKIENIYL 579
Cdd:PRK06087 443 ISSREVEDILL 453
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
223-589 |
8.36e-33 |
|
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: 131.23 E-value: 8.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 223 KIIVIMDSYGSDLVERGKKCGVEIISLKALEDLGRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIINdcsgFI 302
Cdd:TIGR01733 74 RLLLTDSALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVN----LL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 303 KATESAFIASTDDVLISFLPLAH------MFETvvecvmLCHGAK--------IGFFQGDIRLLMDDLKVlqpTIFPVVP 368
Cdd:TIGR01733 150 AWLARRYGLDPDDRVLQFASLSFdasveeIFGA------LLAGATlvvppedeERDDAALLAALIAEHPV---TVLNLTP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 369 RLLNRMFDRIFGQANTslkrwlldfaskrkeaelrsgivrnnslwdklifhkiqsslggkVRLMITGA-APVSATVLTFL 447
Cdd:TIGR01733 221 SLLALLAAALPPALAS--------------------------------------------LRLVILGGeALTPALVDRWR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 448 RTALGCQFYEGYGQTECTAGC-CLSLPGDWTAGHV----GAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLK 522
Cdd:TIGR01733 257 ARGPGARLINLYGPTETTVWStATLVDPDDAPRESpvpiGRPLANTRLYVLD-DDLRPVPVGVVGELYIGGPGVARGYLN 335
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039782744 523 DPARTAE--------ALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFV 589
Cdd:TIGR01733 336 RPELTAErfvpdpfaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
255-645 |
1.89e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 132.82 E-value: 1.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 255 LGRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIINDCsgfikATESAFI---ASTDDVLISFLPLAHMFE-TV 330
Cdd:PRK05605 205 GGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANA-----AQGKAWVpglGDGPERVLAALPMFHAYGlTL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 331 VECVMLCHGAKIGFFQG-DIRLLMDDLKVLQPTIFPVVPRLlnrmFDRIfgqantslkrwlldfaskRKEAELRsGIvrn 409
Cdd:PRK05605 280 CLTLAVSIGGELVLLPApDIDLILDAMKKHPPTWLPGVPPL----YEKI------------------AEAAEER-GV--- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 410 nslwdklifhkiqsSLGGkVRLMITGAA--PVSaTVLTFlRTALGCQFYEGYGQTECTA-GCCLSLPGDWTAGHVGAPMP 486
Cdd:PRK05605 334 --------------DLSG-VRNAFSGAMalPVS-TVELW-EKLTGGLLVEGYGLTETSPiIVGNPMSDDRRPGYVGVPFP 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 487 CNYVKLVDVEEMNYLASKGE-GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQ 565
Cdd:PRK05605 397 DTEVRIVDPEDPDETMPDGEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELI-ITG 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 566 GEYIAPEKIENIYLRSEAVAQVFVHG-------ESLQAfliAVV-----VPDVESLPSWAQKRgLQG--------SFEEL 625
Cdd:PRK05605 475 GFNVYPAEVEEVLREHPGVEDAAVVGlpredgsEEVVA---AVVlepgaALDPEGLRAYCREH-LTRykvprrfyHVDEL 550
|
410 420
....*....|....*....|...
gi 1039782744 626 CRN---KDINKAILDDLLKLGKE 645
Cdd:PRK05605 551 PRDqlgKVRRREVREELLEKLGA 573
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
97-575 |
4.88e-32 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 131.26 E-value: 4.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 97 FQRGIQVSNNgPCLGSRKPNQPYewiSYKEVAELAECIGSGL----IQKGfkpcseQFIGLFSQNRPEWVIVEQGCfSYS 172
Cdd:PLN02246 30 FERLSEFSDR-PCLIDGATGRVY---TYADVELLSRRVAAGLhklgIRQG------DVVMLLLPNCPEFVLAFLGA-SRR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 173 MVVV----PLY------DTLGADAITYIVNKA----ELSVIFADKPEKAKLLLEGVENkltpCLKIIVIMDSYGSDLVEr 238
Cdd:PLN02246 99 GAVTttanPFYtpaeiaKQAKASGAKLIITQScyvdKLKGLAEDDGVTVVTIDDPPEG----CLHFSELTQADENELPE- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 239 gkkcgVEIislkaledlgrvnrvkpkppEPEDLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKATESAFIASTDDVLI 318
Cdd:PLN02246 174 -----VEI--------------------SPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYFHSDDVIL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 319 SFLPLAHMFEtvVECVMLCH---GAKIGFFQG-DIRLLMDDLKVLQPTIFPVVPRLLnrmfdrifgqantslkrwlLDFA 394
Cdd:PLN02246 229 CVLPMFHIYS--LNSVLLCGlrvGAAILIMPKfEIGALLELIQRHKVTIAPFVPPIV-------------------LAIA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 395 skrkeaelRSGIVRNNSLwdklifhkiqSSlggkVRLMITGAAPVSATVLTFLRTAL-GCQFYEGYGQTEctAGCCLSL- 472
Cdd:PLN02246 288 --------KSPVVEKYDL----------SS----IRMVLSGAAPLGKELEDAFRAKLpNAVLGQGYGMTE--AGPVLAMc 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 473 ------PGDWTAGHVGAPMPCNYVKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWL 546
Cdd:PLN02246 344 lafakePFPVKSGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYID 423
|
490 500
....*....|....*....|....*....
gi 1039782744 547 PNGTLKIIDRKKHIFKLaQGEYIAPEKIE 575
Cdd:PLN02246 424 DDDELFIVDRLKELIKY-KGFQVAPAELE 451
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
123-627 |
2.42e-31 |
|
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: 127.50 E-value: 2.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 123 SYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELsvifad 202
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDV--VAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKA------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 203 kpekaklllegvenkltpclKIIVIMDSYGSDLVErgkkcgveiislkaledlgrvnrvkpkpPEPEDLAIICFTSGTTG 282
Cdd:cd05903 75 --------------------KVFVVPERFRQFDPA----------------------------AMPDAVALLLFTSGTTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 283 NPKGAMITHQNIIndcsgfikATESAFIA----STDDVLISFLPLAHMFETVvecvmlcHGAKIGFFQGDIRLLMDdlkV 358
Cdd:cd05903 107 EPKGVMHSHNTLS--------ASIRQYAErlglGPGDVFLVASPMAHQTGFV-------YGFTLPLLLGAPVVLQD---I 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 359 LQPTifpVVPRLLNRmfDRI-FGQANTSLKRWLLDfASKRKEAELRSgivrnnslwdklifhkiqsslggkVRLMITGAA 437
Cdd:cd05903 169 WDPD---KALALMRE--HGVtFMMGATPFLTDLLN-AVEEAGEPLSR------------------------LRTFVCGGA 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 438 PVSATVLTFLRTALGCQFYEGYGQTEC--TAGCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGAN 515
Cdd:cd05903 219 TVPRSLARRAAELLGAKVCSAYGSTECpgAVTSITPAPEDRRLYTDGRPLPGVEIKVVD-DTGATLAPGVEGELLSRGPS 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 516 VFKGYLKDPARTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHG---E 592
Cdd:cd05903 298 VFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAVVAlpdE 375
|
490 500 510
....*....|....*....|....*....|....*
gi 1039782744 593 SLQAFLIAVVVPdveslpswaqKRGLQGSFEELCR 627
Cdd:cd05903 376 RLGERACAVVVT----------KSGALLTFDELVA 400
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
174-659 |
6.86e-31 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 130.04 E-value: 6.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 174 VVVPLYDTLGADAITYIVNKAELSVIFADKPEKAKLLLEGVENKLTPCLKIIvimdsYGSDLVER----GKKCGVEIISL 249
Cdd:PRK08633 691 VPVNLNYTASEAALKSAIEQAQIKTVITSRKFLEKLKNKGFDLELPENVKVI-----YLEDLKAKiskvDKLTALLAARL 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 250 KALEDLGRVNRvkpKPPEPEDLAIICFTSGTTGNPKGAMITHQNIINDcsgfIKATESAFIASTDDVLISFLPLAHMFET 329
Cdd:PRK08633 766 LPARLLKRLYG---PTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSN----IEQISDVFNLRNDDVILSSLPFFHSFGL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 330 VVECVM-LCHGAKIGFFQGDirllMDDLKVLQ-------------PTIFpvvprllnRMFDRifgqaNTSLKRwlLDFAS 395
Cdd:PRK08633 839 TVTLWLpLLEGIKVVYHPDP----TDALGIAKlvakhratillgtPTFL--------RLYLR-----NKKLHP--LMFAS 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 396 krkeaelrsgivrnnslwdklifhkiqsslggkVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLP-- 473
Cdd:PRK08633 900 ---------------------------------LRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNLPdv 946
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 474 ---GDWT-----AGHVGAPMPCNYVKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEAL---DKDGWLHTGDI 542
Cdd:PRK08633 947 laaDFKRqtgskEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDK 1026
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 543 GKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEniylrsEAVAQVFvHGESLQafLIAVVVPDveslpswaQKRG----- 617
Cdd:PRK08633 1027 GHLDEDGFLTITDRYSRFAKIG-GEMVPLGAVE------EELAKAL-GGEEVV--FAVTAVPD--------EKKGeklvv 1088
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039782744 618 ----LQGSFEELCR---NKDINKA-------ILDDLLKLGkeAGLKPFEQVKGIAV 659
Cdd:PRK08633 1089 lhtcGAEDVEELKRaikESGLPNLwkpsryfKVEALPLLG--SGKLDLKGLKELAL 1142
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
118-558 |
6.29e-30 |
|
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: 124.70 E-value: 6.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 118 PYEWISYKEVAELAECIGSGLIQKGFKPcSEQFIGLFSQNRpEWVIVEQGCFSYSMVVVPLydtlgADAITYivnkaels 197
Cdd:cd05906 36 SEEFQSYQDLLEDARRLAAGLRQLGLRP-GDSVILQFDDNE-DFIPAFWACVLAGFVPAPL-----TVPPTY-------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 198 vifaDKPEKAKLLLEGVENKLTPClkIIVIMDSYGSDLVERGKKCGVEIISLKALEDLGRVNRVKPKPP-EPEDLAIICF 276
Cdd:cd05906 101 ----DEPNARLRKLRHIWQLLGSP--VVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADHDLPQsRPDDLALLML 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 277 TSGTTGNPKGAMITHQNIINDCSGfikaTESAFIASTDDVLISFLPLAHmfetVVECVMlCHGAkigffqgDIRLLMDDL 356
Cdd:cd05906 175 TSGSTGFPKAVPLTHRNILARSAG----KIQHNGLTPQDVFLNWVPLDH----VGGLVE-LHLR-------AVYLGCQQV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 357 KVLQPTIFPVVPRLLnRMFDRiFGQANTslkrWLLDFA-SKRKEAELRsgivRNNSLWDklifhkiQSSLggkvRLMITG 435
Cdd:cd05906 239 HVPTEEILADPLRWL-DLIDR-YRVTIT----WAPNFAfALLNDLLEE----IEDGTWD-------LSSL----RYLVNA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 436 AAPVSATVLTFLRTAL---GCQ---FYEGYGQTECTAGC--CLSLP-GDWTAGH----VGAPMPCNYVKLVDVEemNYLA 502
Cdd:cd05906 298 GEAVVAKTIRRLLRLLepyGLPpdaIRPAFGMTETCSGViySRSFPtYDHSQALefvsLGRPIPGVSMRIVDDE--GQLL 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039782744 503 SKGE-GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGkWLPNGTLKIIDRKK 558
Cdd:cd05906 376 PEGEvGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
90-694 |
1.78e-29 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 125.74 E-value: 1.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 90 VRTMYDGFQRGIQVSNNGPCLGSRKPNQPYEWISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCF 169
Cdd:PTZ00297 426 VRSLGEMWERSVTRHSTFRCLGQTSESGESEWLTYGTVDARARELGSGLLALGVRP--GDVIGVDCEASRNIVILEVACA 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 170 SYSMVVVPLYDTlgADAITYIVNKAELSVIFADKPEKAKLLlegvenkltPC----LKIIVIMDS-YGSDLVERGKKCGV 244
Cdd:PTZ00297 504 LYGFTTLPLVGK--GSTMRTLIDEHKIKVVFADRNSVAAIL---------TCrsrkLETVVYTHSfYDEDDHAVARDLNI 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 245 EIISLKALEDLGRVNRVKPKPPEPED----LAIICFTSGTTGNPKGAMITHQNIINDCSGFIKateSAFIAST--DDVLI 318
Cdd:PTZ00297 573 TLIPYEFVEQKGRLCPVPLKEHVTTDtvftYVVDNTTSASGDGLAVVRVTHADVLRDISTLVM---TGVLPSSfkKHLMV 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 319 SFLPLAHMFETVVECVMLCHGAKIGffQGDIRLLMDDLKVLQPTIFPVVPRLlnrmfdriFGQANTSLKR---------- 388
Cdd:PTZ00297 650 HFTPFAMLFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSL--------FSTSRLQLSRanerysavys 719
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 389 WLLDfaskrKEAELRSGIV----RNNSLWDKLIFHKIQSSLGGKVRLMITGAAPVSATV-----LTFLRTALGCQ-FYeg 458
Cdd:PTZ00297 720 WLFE-----RAFQLRSRLInihrRDSSLLRFIFFRATQELLGGCVEKIVLCVSEESTSFsllehISVCYVPCLREvFF-- 792
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 459 ygqTECTAGCCLSlpgdwtaghvGAPMPCNYVKLVDVEEMNYLASKGEGEVCVKGanvfkgylkDPARTAEAldkdgwlh 538
Cdd:PTZ00297 793 ---LPSEGVFCVD----------GTPAPSLQVDLEPFDEPSDGAGIGQLVLAKKG---------EPRRTLPI-------- 842
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 539 tgdIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAfLIAVVVPDVESLP-SWAQKRG 617
Cdd:PTZ00297 843 ---AAQWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEfEWRQSHC 918
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 618 --------LQGSFEELCRNKdiNKAILDDLLKLGKEAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQ 689
Cdd:PTZ00297 919 mgegggpaRQLGWTELVAYA--SSLLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSV 996
|
....*
gi 1039782744 690 IDELY 694
Cdd:PTZ00297 997 IERFY 1001
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
123-604 |
2.13e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 123.12 E-value: 2.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 123 SYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFAD 202
Cdd:PRK08316 38 TYAELDAAVNRVAAALLDLGLKKGDR--VAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 203 kPEKAKLLLEGVEnkLTPCLKIIVIMDSYGSDLVErgkkcgveiiSLKALEDLGRVNRVKPKPPEP--EDLAIICFTSGT 280
Cdd:PRK08316 116 -PALAPTAEAALA--LLPVDTLILSLVLGGREAPG----------GWLDFADWAEAGSVAEPDVELadDDLAQILYTSGT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 281 TGNPKGAMITHQNIINDCSGFIKATEsafiASTDDVLISFLPLAHmfetvvecvmlChgAKIGFFqgdirlLMDDLKVLQ 360
Cdd:PRK08316 183 ESLPKGAMLTHRALIAEYVSCIVAGD----MSADDIPLHALPLYH-----------C--AQLDVF------LGPYLYVGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 361 PTIFPVVPRLlNRMFDRIFGQANTSLkrwlldFASKrkeaelrsgivrnnSLWDKLIFHKI-----QSSLggkvRLMITG 435
Cdd:PRK08316 240 TNVILDAPDP-ELILRTIEAERITSF------FAPP--------------TVWISLLRHPDfdtrdLSSL----RKGYYG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 436 AAPVSATVLTFLRTAL-GCQFYEGYGQTEcTAGCCLSLPGDWTAGHVG-APMPCNYV--KLVDvEEMNYLASKGEGEVCV 511
Cdd:PRK08316 295 ASIMPVEVLKELRERLpGLRFYNCYGQTE-IAPLATVLGPEEHLRRPGsAGRPVLNVetRVVD-DDGNDVAPGEVGEIVH 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 512 KGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQVFV-- 589
Cdd:PRK08316 373 RSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEALYTHPAVAEVAVig 450
|
490
....*....|....*..
gi 1039782744 590 --HGESLQAfLIAVVVP 604
Cdd:PRK08316 451 lpDPKWIEA-VTAVVVP 466
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
256-608 |
2.51e-29 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 123.21 E-value: 2.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 256 GRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKATESAFIASTDD---VLISFLPLAHMFETVVE 332
Cdd:PRK07059 191 GARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAFEKKPRPdqlNFVCALPLYHIFALTVC 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 333 CVMlchGAKIGffqG---------DIRLLMDDLKVLQPTIFPVVPRLLNRMFdrifgqantslkrwlldfaskrkeaelr 403
Cdd:PRK07059 271 GLL---GMRTG---GrnilipnprDIPGFIKELKKYQVHIFPAVNTLYNALL---------------------------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 404 sgivrNNSLWDKLIFHKIQSSLGGkvrlmitGAAPVSATVLTFLRTAlGCQFYEGYGQTEcTAGCCLSLPGDWTA--GHV 481
Cdd:PRK07059 317 -----NNPDFDKLDFSKLIVANGG-------GMAVQRPVAERWLEMT-GCPITEGYGLSE-TSPVATCNPVDATEfsGTI 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 482 GAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIF 561
Cdd:PRK07059 383 GLPLPSTEVSIRD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMI 461
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1039782744 562 kLAQGEYIAPEKIEniylrsEAVAQvfvHGESLQAflIAVVVPDVES 608
Cdd:PRK07059 462 -LVSGFNVYPNEIE------EVVAS---HPGVLEV--AAVGVPDEHS 496
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
270-589 |
5.54e-29 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 122.01 E-value: 5.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 270 DLAIICFTSGTTGNPKGAMITHQNII-NDCSGFIkATESAFIASTddVLISFLPLAHMFETVVEC--VMLCHGAKIGFFQ 346
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTHRNLVaNLCSSLF-SVGPEMIGQV--VTLGLIPFFHIYGITGICcaTLRNKGKVVVMSR 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 347 GDIRLLMDDLKVLQPTIFPVVPRLLNRMFdrifgqantslkrwlldfaskrkeaelrsgivrNNSLWDKLIFHKIqsslg 426
Cdd:PLN02330 262 FELRTFLNALITQEVSFAPIVPPIILNLV---------------------------------KNPIVEEFDLSKL----- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 427 gKVRLMITGAAPVSATVLT-FLRTALGCQFYEGYGQTECTagcCLSLP-GDWTAGH-------VGAPMPCNYVKLVDVEE 497
Cdd:PLN02330 304 -KLQAIMTAAAPLAPELLTaFEAKFPGVQVQEAYGLTEHS---CITLThGDPEKGHgiakknsVGFILPNLEVKFIDPDT 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 498 MNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 577
Cdd:PLN02330 380 GRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAI 458
|
330
....*....|..
gi 1039782744 578 YLRSEAVAQVFV 589
Cdd:PLN02330 459 LLTHPSVEDAAV 470
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
266-604 |
5.63e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 120.86 E-value: 5.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 266 PEPEDLAIICFTSGTTGNPKGAMITHQNIINDcsgfIKATESAFIASTDDVLISFLPLAHMfetvvecvmlcHGAKIGff 345
Cdd:PRK07787 125 PDPDAPALIVYTSGTTGPPKGVVLSRRAIAAD----LDALAEAWQWTADDVLVHGLPLFHV-----------HGLVLG-- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 346 qgdirllmddlkVLQPTifpvvpRLLNRMfdrifgqantslkRWLLDFASKRKEAELRSG-------------IVRNNSL 412
Cdd:PRK07787 188 ------------VLGPL------RIGNRF-------------VHTGRPTPEAYAQALSEGgtlyfgvptvwsrIAADPEA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 413 WDKLifhkiqsslgGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKL 492
Cdd:PRK07787 237 ARAL----------RGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 493 VDvEEMNYLASKGE--GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDR------KKHIFKLA 564
Cdd:PRK07787 307 VD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGGYRIG 385
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1039782744 565 QGEyiapekIENIYLRSEAVAQVFVHGE---SLQAFLIAVVVP 604
Cdd:PRK07787 386 AGE------IETALLGHPGVREAAVVGVpddDLGQRIVAYVVG 422
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
265-616 |
8.45e-29 |
|
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: 119.72 E-value: 8.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 265 PPEPEDLAIICFTSGTTGNPKGAMITHQNIINdcsgFIKATESAFIASTDDVLISFLPLA------HMFETvvecvmLCH 338
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLN----YVSQPPARLDVGPGSRVAQVLSIAfdacigEIFST------LCN 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 339 GAKIgFFQGDIRLLMDDLKVLqpTIFPVVPRLLnrmfdrifgqantslkrwlldfaSKRKEAELRSgivrnnslwdklif 418
Cdd:cd17653 171 GGTL-VLADPSDPFAHVARTV--DALMSTPSIL-----------------------STLSPQDFPN-------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 419 hkiqsslggkVRLMITGAAPVSATVLTflRTALGCQFYEGYGQTECTAGCCLS--LPGDWTagHVGAPMPCNYVKLVDVE 496
Cdd:cd17653 211 ----------LKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTelLPGQPV--TIGKPIPNSTCYILDAD 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 497 EMnyLASKGE-GEVCVKGANVFKGYLKDPARTAEAL----DKDGWLH--TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 569
Cdd:cd17653 277 LQ--PVPEGVvGEICISGVQVARGYLGNPALTASKFvpdpFWPGSRMyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRI 353
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1039782744 570 APEKIENIYLRSEAVAQ---VFVHGESLQAFliavVVP---DVESLPSWAQKR 616
Cdd:cd17653 354 NLEEIEEVVLQSQPEVTqaaAIVVNGRLVAF----VTPetvDVDGLRSELAKH 402
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
108-672 |
1.04e-28 |
|
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: 121.38 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 108 PCLGSRKPNQPYEWISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSY---SMVVVPLYDTLGA 184
Cdd:cd05921 12 TWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGLSA--ERPLLILSGNSIEHALMALAAMYAgvpAAPVSPAYSLMSQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 185 D--AITYIVNKAELSVIFADKPEKAKLLLEGVENKLTPclkIIVImdsygsdlveRGKKCGVEIISLKAL---EDLGRVN 259
Cdd:cd05921 90 DlaKLKHLFELLKPGLVFAQDAAPFARALAAIFPLGTP---LVVS----------RNAVAGRGAISFAELaatPPTAAVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 260 RVKPKPpEPEDLAIICFTSGTTGNPKGAMITHQNIINDCSGfiKATESAFIASTDDVLISFLPLAHMFetvvecvmlchG 339
Cdd:cd05921 157 AAFAAV-GPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAM--LEQTYPFFGEEPPVLVDWLPWNHTF-----------G 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 340 AKIGF-----------------FQGDIRLLMDDLKVLQPTIFPVVPrllnrmfdrifgqantslKRWLLDFASKRKEAEL 402
Cdd:cd05921 223 GNHNFnlvlynggtlyiddgkpMPGGFEETLRNLREISPTVYFNVP------------------AGWEMLVAALEKDEAL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 403 RSGIVRNnslwdklifhkiqsslggkVRLMITGAAPVSATVLTFLrTALGCQ-------FYEGYGQTEcTAGCCLSLPGD 475
Cdd:cd05921 285 RRRFFKR-------------------LKLMFYAGAGLSQDVWDRL-QALAVAtvgeripMMAGLGATE-TAPTATFTHWP 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 476 WT-AGHVGAPMPCNYVKLVdveemnylASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWL----PNGT 550
Cdd:cd05921 344 TErSGLIGLPAPGTELKLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpddPAKG 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 551 LKIIDRKKHIFKLAQGEYIA--PekieniyLRSEAVAQ-------VFVHGESlQAFLIAVVVPDVESLpswaqkRGLQG- 620
Cdd:cd05921 416 LVFDGRVAEDFKLASGTWVSvgP-------LRARAVAAcaplvhdAVVAGED-RAEVGALVFPDLLAC------RRLVGl 481
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1039782744 621 ---SFEELCRNKDINKAILDDLLKLGKEAGLKPfEQVKGIAVHPELFSIDNGLLT 672
Cdd:cd05921 482 qeaSDAEVLRHAKVRAAFRDRLAALNGEATGSS-SRIARALLLDEPPSIDKGEIT 535
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
263-577 |
3.31e-28 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 119.56 E-value: 3.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 263 PKPP-EPEDLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKATESAFIAS-TDDVLISFLPLAHMFETVVECV-MLCHG 339
Cdd:PLN02574 191 PKPViKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEYPgSDNVYLAALPMFHIYGLSLFVVgLLSLG 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 340 AKI----GFFQGDIRLLMDDLKVlqpTIFPVVPRLLNRMFDRIFGQANTSLKrwlldfaskrkeaelrsgivrnnslwdk 415
Cdd:PLN02574 271 STIvvmrRFDASDMVKVIDRFKV---THFPVVPPILMALTKKAKGVCGEVLK---------------------------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 416 lifhkiqsslggKVRLMITGAAPVSA-TVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGH--VGAPMPCNYVKL 492
Cdd:PLN02574 320 ------------SLKQVSCGAAPLSGkFIQDFVQTLPHVDFIQGYGMTESTAVGTRGFNTEKLSKYssVGLLAPNMQAKV 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 493 VDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPE 572
Cdd:PLN02574 388 VDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQIAPA 466
|
....*
gi 1039782744 573 KIENI 577
Cdd:PLN02574 467 DLEAV 471
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
265-599 |
3.61e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 119.75 E-value: 3.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 265 PPEPE-DLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKATESAfiASTDDVLISFLPLAHMF-ETVVECVMLCHGAKI 342
Cdd:PRK06710 201 PCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNC--KEGEEVVLGVLPFFHVYgMTAVMNLSIMQGYKM 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 343 GFF-QGDIRLLMDDLKVLQPTIFPVVPRLLNRMFdrifgqaNTSLkrwlldfaskRKEAELRSgivrnnslwdklifhki 421
Cdd:PRK06710 279 VLIpKFDMKMVFEAIKKHKVTLFPGAPTIYIALL-------NSPL----------LKEYDISS----------------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 422 qsslggkVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLS-LPGDWTAGHVGAPMPCNYVKLVDVEEMNY 500
Cdd:PRK06710 325 -------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNfLWEKRVPGSIGVPWPDTEAMIMSLETGEA 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 501 LASKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLR 580
Cdd:PRK06710 398 LPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREVEEVLYE 475
|
330 340
....*....|....*....|....*.
gi 1039782744 581 SEAVAQVFV-------HGESLQAFLI 599
Cdd:PRK06710 476 HEKVQEVVTigvpdpyRGETVKAFVV 501
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
112-611 |
3.71e-28 |
|
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: 118.58 E-value: 3.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 112 SRKPNQPY-----EWISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADA 186
Cdd:cd17655 8 EKTPDHTAvvfedQTLTYRELNERANQLARTLREKGVGP--DTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 187 ITYIVNKAELSVIFADKPEKAKLLLEGvenkltpclkIIVIMDSygsdlvergkkcgvEIISLKALEDLGRVNRvkpkpp 266
Cdd:cd17655 86 IQYILEDSGADILLTQSHLQPPIAFIG----------LIDLLDE--------------DTIYHEESENLEPVSK------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 267 ePEDLAIICFTSGTTGNPKGAMITHQNIINDCSGFikaTESAFIASTDDVLisflplahMFetvvecvmlchgAKIGFfq 346
Cdd:cd17655 136 -SDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWA---NKVIYQGEHLRVA--------LF------------ASISF-- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 347 gdirllmdDLKVLQptIFPvvPRLL-NRMFdrIFGQANTSLKRWLLDFASKRkeaelRSGIVRNNSLWDKLIFHkIQSSL 425
Cdd:cd17655 190 --------DASVTE--IFA--SLLSgNTLY--IVRKETVLDGQALTQYIRQN-----RITIIDLTPAHLKLLDA-ADDSE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 426 GGKVRLMITGAAPVSATVLTFL--RTALGCQFYEGYGQTECTAGCCLSL--PGDWTAGHV--GAPMPCNYVKLVDvEEMN 499
Cdd:cd17655 250 GLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETTVDASIYQyePETDQQVSVpiGKPLGNTRIYILD-QYGR 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 500 YLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 573
Cdd:cd17655 329 PQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-RGYRIELGE 407
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1039782744 574 IENIYLRSEAVAQ--VFVH-GESLQAFLIAVVVPDvESLPS 611
Cdd:cd17655 408 IEARLLQHPDIKEavVIARkDEQGQNYLCAYIVSE-KELPV 447
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
269-592 |
4.76e-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: 117.06 E-value: 4.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 269 EDLAIICFTSGTTGNPKGAMITHQNIindcsgFIKATESAFI--ASTDDVLISFLPLAH------MFETVVE-CVMLCHG 339
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNH------WWSAIGSALNlgLTEDDNWLCALPLFHisglsiLMRSVIYgMTVYLVD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 340 AkigFFQGDIRLLMDDLKVlqpTIFPVVPRLLNRMFDRIFGQANTSLkrwlldfaskrkeaelrsgivrnnslwdklifh 419
Cdd:cd05912 151 K---FDAEQVLHLINSGKV---TIISVVPTMLQRLLEILGEGYPNNL--------------------------------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 420 kiqsslggkvRLMITGAAPVSATVLTFLRTaLGCQFYEGYGQTE-CTAGCCLSlPGDWTA--GHVGAPMPCNYVKLVDVE 496
Cdd:cd05912 192 ----------RCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTEtCSQIVTLS-PEDALNkiGSAGKPLFPVELKIEDDG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 497 EmnylASKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIEN 576
Cdd:cd05912 260 Q----PPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEE 333
|
330
....*....|....*.
gi 1039782744 577 IYLRSEAVAQVFVHGE 592
Cdd:cd05912 334 VLLSHPAIKEAGVVGI 349
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
122-605 |
4.94e-28 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 119.06 E-value: 4.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 122 ISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:COG0365 40 LTYAELRREVNRFANALRALGVKK--GDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLIT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 202 D----KPEKAKLLLEGVEN--KLTPCLKIIVIMDSYGSDLVERGkkcgveIISLKALEDlGRVNRVKPKPPEPEDLAIIC 275
Cdd:COG0365 118 AdgglRGGKVIDLKEKVDEalEELPSLEHVIVVGRTGADVPMEG------DLDWDELLA-AASAEFEPEPTDADDPLFIL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 276 FTSGTTGNPKGAMITH-----------QNIIN-----------DCsGFIKATESAFIAstddvlisflPLAH-----MFE 328
Cdd:COG0365 191 YTSGTTGKPKGVVHTHggylvhaattaKYVLDlkpgdvfwctaDI-GWATGHSYIVYG----------PLLNgatvvLYE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 329 tvvecvmlchgAKIGFFQGDiRL--LMDDLKVlqpTIFPVVPRLLnRMfdrifgqantsLKRWLLDFASKRkeaelrsgi 406
Cdd:COG0365 260 -----------GRPDFPDPG-RLweLIEKYGV---TVFFTAPTAI-RA-----------LMKAGDEPLKKY--------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 407 vrnnSLwdklifhkiqSSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWT-AGHVGAPM 485
Cdd:COG0365 304 ----DL----------SSL----RLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGLPVkPGSMGKPV 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 486 PCNYVKLVDvEEMNYLASKGEGEVCVKGAN--VFKGYLKDPARTAEAL--DKDGWLHTGDIGKWLPNGTLKIIDRKKHIF 561
Cdd:COG0365 366 PGYDVAVVD-EDGNPVPPGEEGELVIKGPWpgMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVI 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1039782744 562 KLAqGEYIAPEKIENIYLRSEAVAqvfvhgESlqafliAVV-VPD 605
Cdd:COG0365 445 NVS-GHRIGTAEIESALVSHPAVA------EA------AVVgVPD 476
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
120-616 |
5.08e-28 |
|
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: 121.12 E-value: 5.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 120 EWISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCF----SYsmvvVPLYDTLGADAITYIVNKAE 195
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALGVGP--GDLVGVCLERSLEMVVALLAVLkagaAY----VPLDPAYPAERLAYMLEDAG 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 196 LSVIFADkpekaklllegvenkltpclkiivimdsygSDLVERGKKCGVEIISLKALEDLGRVNRVKPKPPEPEDLAIIC 275
Cdd:COG1020 574 ARLVLTQ------------------------------SALAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLAYVI 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 276 FTSGTTGNPKGAMITHQNIINdcsgFIKATESAFIASTDDVLISFLPLAhmFE-TVVECVM-LCHGAKIGFFQGDIRLLM 353
Cdd:COG1020 624 YTSGSTGRPKGVMVEHRALVN----LLAWMQRRYGLGPGDRVLQFASLS--FDaSVWEIFGaLLSGATLVLAPPEARRDP 697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 354 DDLKVL----QPTIFPVVPRLLNRMFDRIFgQANTSLKRWLLdfaskrkeaelrsgivrnnslwdklifhkiqsslGGkv 429
Cdd:COG1020 698 AALAELlarhRVTVLNLTPSLLRALLDAAP-EALPSLRLVLV----------------------------------GG-- 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 430 rlmitGAAPVsATVLTFLRTALGCQFYEGYGQTECTAGCCLSL--PGDWTAGHV--GAPMPCNYVKLVDvEEMNyLASKG 505
Cdd:COG1020 741 -----EALPP-ELVRRWRARLPGARLVNLYGPTETTVDSTYYEvtPPDADGGSVpiGRPIANTRVYVLD-AHLQ-PVPVG 812
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 506 -EGEVCVKGANVFKGYLKDPARTAEA-----LDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 577
Cdd:COG1020 813 vPGELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNLEFLGRADDQVKI-RGFRIELGEIEAA 891
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1039782744 578 YLRSEAVAQ--VFVHGESLQA-FLIAVVVPDVESLPSWAQKR 616
Cdd:COG1020 892 LLQHPGVREavVVAREDAPGDkRLVAYVVPEAGAAAAAALLR 933
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
122-604 |
6.86e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 118.55 E-value: 6.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 122 ISYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPE-WVIVEQGCFSySMVVVPLYDTLGADAITYIVNKAELSVIF 200
Cdd:PRK06188 38 LTYGQLADRISRYIQAFEALGLGTGDA--VALLSLNRPEvLMAIGAAQLA-GLRRTALHPLGSLDDHAYVLEDAGISTLI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 201 ADK---PEKAKLLLEGVenkltPCLKIIVIMDS--YGSDLVERGKKCGveiislkaledlgrvnrvkPKPPEPE----DL 271
Cdd:PRK06188 115 VDPapfVERALALLARV-----PSLKHVLTLGPvpDGVDLLAAAAKFG-------------------PAPLVAAalppDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 272 AIICFTSGTTGNPKGAMITHQNIindcsgfikATESAFIAST----DDvlISFL---PLAHMFETVVECVMLCHGAKI-- 342
Cdd:PRK06188 171 AGLAYTGGTTGKPKGVMGTHRSI---------ATMAQIQLAEwewpAD--PRFLmctPLSHAGGAFFLPTLLRGGTVIvl 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 343 -GFfqgDIRLLMDDLKVLQPTIFPVVPRLLNRmfdrifgqantslkrwLLDFASKRKeAELrsgivrnnslwdklifhki 421
Cdd:PRK06188 240 aKF---DPAEVLRAIEEQRITATFLVPTMIYA----------------LLDHPDLRT-RDL------------------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 422 qSSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHV------GAPMPCNYVKLVDv 495
Cdd:PRK06188 281 -SSL----ETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLRVALLD- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 496 EEMNYLASkGE-GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKI 574
Cdd:PRK06188 355 EDGREVAQ-GEvGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMI-VTGGFNVFPREV 431
|
490 500 510
....*....|....*....|....*....|....*..
gi 1039782744 575 ENIYLRSEAVAQVFV-------HGESLQafliAVVVP 604
Cdd:PRK06188 432 EDVLAEHPAVAQVAVigvpdekWGEAVT----AVVVL 464
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
265-558 |
8.29e-28 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 118.05 E-value: 8.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 265 PPEPEDLAIICFTSGTTGNPKGAMITHQNIIN------DCSGFikatesafiaSTDDVLISFLPLAH---MFetVVECVM 335
Cdd:PRK07514 152 PRGADDLAAILYTSGTTGRSKGAMLSHGNLLSnaltlvDYWRF----------TPDDVLIHALPIFHthgLF--VATNVA 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 336 LCHGAKIGFFQG-DIRLLMDDLKvlQPTIFPVVP----RLL-NRMFDRifgqantslkrwlldfaskrkEAelrsgiVRN 409
Cdd:PRK07514 220 LLAGASMIFLPKfDPDAVLALMP--RATVMMGVPtfytRLLqEPRLTR---------------------EA------AAH 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 410 nslwdklifhkiqsslggkVRLMITGAAPVSATvlTFL----RTalGCQFYEGYGQTEctAGCCLSLP--GDWTAGHVGA 483
Cdd:PRK07514 271 -------------------MRLFISGSAPLLAE--THRefqeRT--GHAILERYGMTE--TNMNTSNPydGERRAGTVGF 325
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039782744 484 PMPCNYVKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK 558
Cdd:PRK07514 326 PLPGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGK 400
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
120-621 |
1.36e-27 |
|
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: 116.62 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 120 EWISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVI 199
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARGVGP--GDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 200 FADkpekaklllegvenkltpclkiivimdsygSDLVERGKKCGVEIisLKALEDLGRVNRVKPKPPEPEDLAIICFTSG 279
Cdd:cd12116 89 LTD------------------------------DALPDRLPAGLPVL--LLALAAAAAAPAAPRTPVSPDDLAYVIYTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 280 TTGNPKGAMITHQNIINdcsgFIKATESAFIASTDDVLISFLPLAhmFE-TVVECVM-LCHGAKIGFFQGDI----RLLM 353
Cdd:cd12116 137 STGRPKGVVVSHRNLVN----FLHSMRERLGLGPGDRLLAVTTYA--FDiSLLELLLpLLAGARVVIAPRETqrdpEALA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 354 DDLKVLQPTIFpvvprllnrmfdrifgQANTSLKRWLLDfASKRKEAELRsgivrnnslwdklifhkiqsslggkvrlMI 433
Cdd:cd12116 211 RLIEAHSITVM----------------QATPATWRMLLD-AGWQGRAGLT----------------------------AL 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 434 TGAAPVSATVLTFLrTALGCQFYEGYGQTECT--AGCCLSLPGDwTAGHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCV 511
Cdd:cd12116 246 CGGEALPPDLAARL-LSRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLD-AALRPVPPGVPGELYI 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 512 KGANVFKGYLKDPARTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAV 584
Cdd:cd12116 323 GGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQVKI-RGHRIELGEIEAALAAHPGV 401
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1039782744 585 AQ--VFVHGESLQAFLIAVVVPDVESLPSWAQ-KRGLQGS 621
Cdd:cd12116 402 AQaaVVVREDGGDRRLVAYVVLKAGAAPDAAAlRAHLRAT 441
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
174-585 |
1.54e-26 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 115.05 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 174 VVVPLYDTLGADAITYIVNKAELSVIFADKPE-------KAKLLLEGVenkltPCLKIIVIMDsyGSDLVERGK------ 240
Cdd:PRK07529 108 IANPINPLLEPEQIAELLRAAGAKVLVTLGPFpgtdiwqKVAEVLAAL-----PELRTVVEVD--LARYLPGPKrlavpl 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 241 ---KCGVEIISLKALEDLGRVNR-VKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIINDC---SGFIKATEsafiast 313
Cdd:PRK07529 181 irrKAHARILDFDAELARQPGDRlFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAwlgALLLGLGP------- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 314 DDVLISFLPLAHMFETVVEC-VMLCHGAKIGFF--QG--DIRLLMDDLKVL---QPTIFPVVPRLLNRMFDRIFGQANTS 385
Cdd:PRK07529 254 GDTVFCGLPLFHVNALLVTGlAPLARGAHVVLAtpQGyrGPGVIANFWKIVeryRINFLSGVPTVYAALLQVPVDGHDIS 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 386 lkrwlldfaskrkeaelrsgivrnnslwdklifhkiqsSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECT 465
Cdd:PRK07529 334 --------------------------------------SL----RYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEAT 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 466 AGCCLSLP-GDWTAGHVGAPMPCNYVKLVDVEEM-NYL--ASKGE-GEVCVKGANVFKGYLkDPARTAEALDKDGWLHTG 540
Cdd:PRK07529 372 CVSSVNPPdGERRIGSVGLRLPYQRVRVVILDDAgRYLrdCAVDEvGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTG 450
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1039782744 541 DIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVA 585
Cdd:PRK07529 451 DLGRIDADGYFWLTGRAKDLI-IRGGHNIDPAAIEEALLRHPAVA 494
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
174-618 |
1.63e-26 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 113.30 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 174 VVVPLYDTLGADAITYIVNKAELSVIFADkpekaklllEGVENKLTPCLkiiviMDSYGSDLVergkkcgveiISLKALE 253
Cdd:cd05922 48 VFVPLNPTLKESVLRYLVADAGGRIVLAD---------AGAADRLRDAL-----PASPDPGTV----------LDADGIR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 254 DLGRvnRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIIndcsgfikaTESAFIAS-----TDDVLISFLPLAHMFE 328
Cdd:cd05922 104 AARA--SAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLL---------ANARSIAEylgitADDRALTVLPLSYDYG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 329 TVVECVMLCHGAKIgFFQGDIRL---LMDDLKVLQPTIFPVVPRLLNrMFDRIfgqantslkrwlldfasKRKEAELRSg 405
Cdd:cd05922 173 LSVLNTHLLRGATL-VLTNDGVLddaFWEDLREHGATGLAGVPSTYA-MLTRL-----------------GFDPAKLPS- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 406 ivrnnslwdklifhkiqsslggkVRLMITGAAPVSATVLTFLRTAL-GCQFYEGYGQTECTAGCCLsLPGDWTA---GHV 481
Cdd:cd05922 233 -----------------------LRYLTQAGGRLPQETIARLRELLpGAQVYVMYGQTEATRRMTY-LPPERILekpGSI 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 482 GAPMPCNYVKLVDVEEMnyLASKGE-GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHI 560
Cdd:cd05922 289 GLAIPGGEFEILDDDGT--PTPPGEpGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRM 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039782744 561 FKLAqGEYIAPEKIENIyLRSEAVAQVFV-------HGESLQAFLIAVVVPDVESLPSWAQKRGL 618
Cdd:cd05922 367 IKLF-GNRISPTEIEAA-ARSIGLIIEAAavglpdpLGEKLALFVTAPDKIDPKDVLRSLAERLP 429
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
120-591 |
1.97e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 113.80 E-value: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 120 EWISYKEVAELAECIGSGLIQK-GFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSV 198
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIYElNVKKGER--IAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 199 IFADKpekaklllegvenkltpclkiivimdSYGSDLVERGKKCGVE-IISLKALEDLGRVNRVKPKPPEPEDLAIICFT 277
Cdd:PRK06839 104 LFVEK--------------------------TFQNMALSMQKVSYVQrVISITSLKEIEDRKIDNFVEKNESASFIICYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 278 SGTTGNPKGAMITHQNIindcsgFIKATESAFIA--STDDVLISFLPLAHMfetvvecvmlchgAKIGFFQgdirllmdd 355
Cdd:PRK06839 158 SGTTGKPKGAVLTQENM------FWNALNNTFAIdlTMHDRSIVLLPLFHI-------------GGIGLFA--------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 356 lkvlQPTIFP----VVPRllnrMFDRIFGQANTSLKRWLLDFASKRKEAELRSGIVRNNSLWDKlifhkiqsslggkVRL 431
Cdd:PRK06839 210 ----FPTLFAggviIVPR----KFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQS-------------VRW 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 432 MITGAAPVSATVLTFLRTAlGCQFYEGYGQTECTAGCCLSLPGDW--TAGHVGAPMPCNYVKLVDvEEMNYLASKGEGEV 509
Cdd:PRK06839 269 FYNGGAPCPEELMREFIDR-GFLFGQGFGMTETSPTVFMLSEEDArrKVGSIGKPVLFCDYELID-ENKNKVEVGEVGEL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 510 CVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFV 589
Cdd:PRK06839 347 LIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQVINKLSDVYEVAV 424
|
..
gi 1039782744 590 HG 591
Cdd:PRK06839 425 VG 426
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
268-609 |
2.50e-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: 113.02 E-value: 2.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 268 PEDLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKATEsafIASTDDVL----ISF-LPLAHMFETvvecvmLCHGAKI 342
Cdd:cd05918 105 PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALG---LTSESRVLqfasYTFdVSILEIFTT------LAAGGCL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 343 GffqgdI---RLLMDDLkvlqptifpvvPRLLNRMfdrifgQANTslkrwlldfaskrkeAELRSGIVRnnslwdkLIFH 419
Cdd:cd05918 176 C-----IpseEDRLNDL-----------AGFINRL------RVTW---------------AFLTPSVAR-------LLDP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 420 KIQSSLggkvRLMITGAAPVSATVLTflRTALGCQFYEGYGQTECTAGCCLSLPG-DWTAGHVGAPMPCN-YVklVDVEE 497
Cdd:cd05918 212 EDVPSL----RTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRPLGATcWV--VDPDN 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 498 MNYLASKGE-GEVCVKGANVFKGYLKDPARTAEALDKD-GWLH------------TGDIGKWLPNGTLKIIDRKKHIFKL 563
Cdd:cd05918 284 HDRLVPIGAvGELLIEGPILARGYLNDPEKTAAAFIEDpAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKI 363
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1039782744 564 aQGEYIAPEKIENIYLRS-----EAVAQVFVH-GESLQAFLIAVVVPDVESL 609
Cdd:cd05918 364 -RGQRVELGEIEHHLRQSlpgakEVVVEVVKPkDGSSSPQLVAFVVLDGSSS 414
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
121-629 |
7.28e-26 |
|
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: 111.62 E-value: 7.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 121 WISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIF 200
Cdd:cd12118 29 RYTWRQTYDRCRRLASALAALGISR--GDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 201 ADKPekakLLLEgvenkltpclkiivimdsygsDLVERGKKcgveiislkaledlgrvnRVKPKPPEPEDLAI-ICFTSG 279
Cdd:cd12118 107 VDRE----FEYE---------------------DLLAEGDP------------------DFEWIPPADEWDPIaLNYTSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 280 TTGNPKGAMITHQniindcsgfikateSAFIASTDDVLIS----------FLPLAHmfetvveCVMLCHGAKIGFFQG-- 347
Cdd:cd12118 144 TTGRPKGVVYHHR--------------GAYLNALANILEWemkqhpvylwTLPMFH-------CNGWCFPWTVAAVGGtn 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 348 ------DIRLLMDDLKVLQPTIFPVVPRLLNRMfdrifgqANTSlkrwlldfaskrkeaelrsgivrnnslwdklifHKI 421
Cdd:cd12118 203 vclrkvDAKAIYDLIEKHKVTHFCGAPTVLNML-------ANAP---------------------------------PSD 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 422 QSSLGGKVRLMITGAAPvSATVLtFLRTALGCQFYEGYGQTEcTAG---CCL------SLPGDWTA--------GHVGAp 484
Cdd:cd12118 243 ARPLPHRVHVMTAGAPP-PAAVL-AKMEELGFDVTHVYGLTE-TYGpatVCAwkpewdELPTEERArlkarqgvRYVGL- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 485 mpcNYVKLVDVEEMNYLASKGE--GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFk 562
Cdd:cd12118 319 ---EEVDVLDPETMKPVPRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII- 393
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039782744 563 LAQGEYIAPEKIENIYLRSEAVAQVFVhgeslqafliaVVVPDveslPSWAQ--------KRGLQGSFEEL---CRNK 629
Cdd:cd12118 394 ISGGENISSVEVEGVLYKHPAVLEAAV-----------VARPD----EKWGEvpcafvelKEGAKVTEEEIiafCREH 456
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
122-616 |
7.55e-26 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 111.03 E-value: 7.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 122 ISYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDR--VGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 202 dkpekaklllegvenkltpclkiivimdsyGSDLvergkkcgveiislkaledlgrvnrvkpkppepEDLAIICFTSGTT 281
Cdd:cd05935 80 ------------------------------GSEL---------------------------------DDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 282 GNPKGAMITHQNIINDCSGfikaTESAFIASTDDVLISFLPLAHM--FETVVECVMLCHGAKIGFFQGDIRLLMDDLKVL 359
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQ----SAVWTGLTPSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMARWDRETALELIEKY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 360 QPTIFPVVPRLLNrmfdrifgqantslkrwlldfaskrkeaelrsgivrnnslwDKLIFHKIQSSLGGKVRLMITGAAPV 439
Cdd:cd05935 173 KVTFWTNIPTMLV-----------------------------------------DLLATPEFKTRDLSSLKVLTGGGAPM 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 440 SATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDVEEMNYLASKGEGEVCVKGANVFKG 519
Cdd:cd05935 212 PPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKG 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 520 YLKDPARTAEALDKDG---WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQVFV------- 589
Cdd:cd05935 292 YWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVisvpder 370
|
490 500 510
....*....|....*....|....*....|...
gi 1039782744 590 HGESLQAFLiaVVVP------DVESLPSWAQKR 616
Cdd:cd05935 371 VGEEVKAFI--VLRPeyrgkvTEEDIIEWAREQ 401
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
91-545 |
8.34e-26 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 112.66 E-value: 8.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 91 RTMYDGFQRGIQVSNNGPCLGSRKPNQPYEWISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFS 170
Cdd:PRK08180 39 RRLTDRLVHWAQEAPDRVFLAERGADGGWRRLTYAEALERVRAIAQALLDRGLSA--ERPLMILSGNSIEHALLALAAMY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 171 YSMVVVPL---YDTLGAD--AITYIVNKAELSVIFADKPEKAKLLLEGVEnklTPCLKIIVImdsygsdlveRGKKCGVE 245
Cdd:PRK08180 117 AGVPYAPVspaYSLVSQDfgKLRHVLELLTPGLVFADDGAAFARALAAVV---PADVEVVAV----------RGAVPGRA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 246 IISLKALEDLGRVNRVKPKPPE--PEDLAIICFTSGTTGNPKGAMITHQNIindCSG--FIKATeSAFIASTDDVLISFL 321
Cdd:PRK08180 184 ATPFAALLATPPTAAVDAAHAAvgPDTIAKFLFTSGSTGLPKAVINTHRML---CANqqMLAQT-FPFLAEEPPVLVDWL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 322 PLAHMFETVVEC-VMLCHGAKI---------GFFQGDIRllmdDLKVLQPTIFPVVPR--------------LLNRMFDR 377
Cdd:PRK08180 260 PWNHTFGGNHNLgIVLYNGGTLyiddgkptpGGFDETLR----NLREISPTVYFNVPKgwemlvpalerdaaLRRRFFSR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 378 ifgqantsLKrwLLDFASkrkeAELRSgivrnnSLWDKLifHKI-QSSLGGKVRLMitgaapvsatvltflrTALGCqfy 456
Cdd:PRK08180 336 --------LK--LLFYAG----AALSQ------DVWDRL--DRVaEATCGERIRMM----------------TGLGM--- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 457 egygqTEcTAGCCLSL--PGDwTAGHVGAPMPCNYVKLVDVEemnylaskGEGEVCVKGANVFKGYLKDPARTAEALDKD 534
Cdd:PRK08180 375 -----TE-TAPSATFTtgPLS-RAGNIGLPAPGCEVKLVPVG--------GKLEVRVKGPNVTPGYWRAPELTAEAFDEE 439
|
490
....*....|.
gi 1039782744 535 GWLHTGDIGKW 545
Cdd:PRK08180 440 GYYRSGDAVRF 450
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
124-616 |
1.75e-25 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 110.44 E-value: 1.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 124 YKEVAELAECIGSGLIQKGfkpcseQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFADK 203
Cdd:PRK03640 34 HEAVVSVAGKLAALGVKKG------DRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 204 PEKAKLllegvenkltpclkiivimdsygsdlvergkkcgVEIISLKaLEDLGRVNRVKPKPPEPEDL---AIICFTSGT 280
Cdd:PRK03640 108 DFEAKL----------------------------------IPGISVK-FAELMNGPKEEAEIQEEFDLdevATIMYTSGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 281 TGNPKGAMITHQNiindcsGFIKATESAF---IASTDDVLISfLPLAHM--FETVVECVMlcHGAKI----GFFQGDI-R 350
Cdd:PRK03640 153 TGKPKGVIQTYGN------HWWSAVGSALnlgLTEDDCWLAA-VPIFHIsgLSILMRSVI--YGMRVvlveKFDAEKInK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 351 LLMDDlKVlqpTIFPVVPRLLNRMFDRIfGQANTslkrwlldfaskrkeaelrsgivrNNSLwdklifhkiqsslggkvR 430
Cdd:PRK03640 224 LLQTG-GV---TIISVVSTMLQRLLERL-GEGTY------------------------PSSF-----------------R 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 431 LMITGAAPVSATVLTflrtalGCQ-----FYEGYGQTEcTAGCCLSLPGDWTA---GHVGAPM-PCNyVKLVDveEMNYL 501
Cdd:PRK03640 258 CMLLGGGPAPKPLLE------QCKekgipVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLfPCE-LKIEK--DGVVV 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 502 ASKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRS 581
Cdd:PRK03640 328 PPFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSH 405
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1039782744 582 EAVAQVFVHGESLQ-------AFLIAVVVPDVESLPSWAQKR 616
Cdd:PRK03640 406 PGVAEAGVVGVPDDkwgqvpvAFVVKSGEVTEEELRHFCEEK 447
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
157-616 |
3.01e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 110.64 E-value: 3.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 157 NRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFADKPEKAklLLEGVENkLTPCLKIIVIMDSYGSDLV 236
Cdd:PRK07786 76 NRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAP--VATAVRD-IVPLLSTVVVAGGSSDDSV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 237 ergkkcgveiislKALEDLGRVNRVKPKPPE-PEDL-AIICFTSGTTGNPKGAMITHQNIINDCSGFIKATEsAFIAstD 314
Cdd:PRK07786 153 -------------LGYEDLLAEAGPAHAPVDiPNDSpALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNG-ADIN--S 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 315 DVLISFLPLAHM--FETVVECVMLchGAKIgffqgdirllmddlkVLQPTifpvvprllnRMFDRifGQantslkrwLLD 392
Cdd:PRK07786 217 DVGFVGVPLFHIagIGSMLPGLLL--GAPT---------------VIYPL----------GAFDP--GQ--------LLD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 393 FAskrkEAELRSGIVRNNSLWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRTAL-GCQFYEGYGQTECTAGCCLS 471
Cdd:PRK07786 260 VL----EAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEMSPVTCML 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 472 LPGDWTA--GHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDkDGWLHTGDIGKWLPNG 549
Cdd:PRK07786 336 LGEDAIRklGSVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHSGDLVRQDEEG 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039782744 550 TLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAF---LIAVVVPD-------VESLPSWAQKR 616
Cdd:PRK07786 414 YVWVVDRKKDMI-ISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWgevPVAVAAVRnddaaltLEDLAEFLTDR 489
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
122-604 |
1.24e-24 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 108.60 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 122 ISYKEVAELAECIGSGLIQKGFKP---CSEQFiglfsQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSV 198
Cdd:PRK13295 56 FTYRELAALVDRVAVGLARLGVGRgdvVSCQL-----PNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 199 IFA-------DKPEkaklLLEGVENKLtPCLKIIVIMDSYGSDLVERgkkcgveIISLKALEDLGRVNRVKPKP-PEPED 270
Cdd:PRK13295 131 LVVpktfrgfDHAA----MARRLRPEL-PALRHVVVVGGDGADSFEA-------LLITPAWEQEPDAPAILARLrPGPDD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 271 LAIICFTSGTTGNPKGAMITHQNIIndcSGFIKATESAFIAStDDVLISFLPLAHMfetvvecvmlchgakIGFFQGDIR 350
Cdd:PRK13295 199 VTQLIYTSGTTGEPKGVMHTANTLM---ANIVPYAERLGLGA-DDVILMASPMAHQ---------------TGFMYGLMM 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 351 LLMDDLK-VLQPTIFPVvprllnRMFDRI------FGQANTSlkrWLLDFASKRKEAELRSgivrnnslwdklifhkiqS 423
Cdd:PRK13295 260 PVMLGATaVLQDIWDPA------RAAELIrtegvtFTMASTP---FLTDLTRAVKESGRPV------------------S 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 424 SLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTA--GCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYL 501
Cdd:PRK13295 313 SL----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAvtLTKLDDPDERASTTDGCPLPGVEVRVVD-ADGAPL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 502 ASKGEGEVCVKGANVFKGYLKDPARTAEalDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRS 581
Cdd:PRK13295 388 PAGQIGRLQVRGCSNFGGYLKRPQLNGT--DADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEALLYRH 464
|
490 500
....*....|....*....|....*.
gi 1039782744 582 EAVAQVFVHG---ESLQAFLIAVVVP 604
Cdd:PRK13295 465 PAIAQVAIVAypdERLGERACAFVVP 490
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
122-611 |
1.87e-24 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 108.05 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 122 ISYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGLLPGDR--VALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 202 DKpekaklllEGVENKLTPCLKIIVIMDSYGSDlveRGKKCGVEIISLKALEDLGRVNRVkPKPPEPEDlAIICFTSGTT 281
Cdd:PRK05852 122 DA--------DGPHDRAEPTTRWWPLTVNVGGD---SGPSGGTLSVHLDAATEPTPATST-PEGLRPDD-AMIMFTGGTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 282 GNPKGAMITHQNIindcSGFIKATESAFIASTDDVLISFLPLAHMFETVVECV-MLCHGAKI-----GFFQGdiRLLMDD 355
Cdd:PRK05852 189 GLPKMVPWTHANI----ASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLaTLASGGAVllparGRFSA--HTFWDD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 356 LKVLQPTIFPVVPRLLNRMFDRifgqANTSlkrwlldfASKRKEAELRsgIVRNNSlwdklifhkiqsslggkvrlmitg 435
Cdd:PRK05852 263 IKAVGATWYTAVPTIHQILLER----AATE--------PSGRKPAALR--FIRSCS------------------------ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 436 aAPVSATVLTFLRTALGCQFYEGYGQTECTAGccLSLPGDWTAGHVGAP-MPCNYVKLVDVEEMNYLASKGE-------G 507
Cdd:PRK05852 305 -APLTAETAQALQTEFAAPVVCAFGMTEATHQ--VTTTQIEGIGQTENPvVSTGLVGRSTGAQIRIVGSDGLplpagavG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 508 EVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQV 587
Cdd:PRK05852 382 EVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLASHPNVMEA 459
|
490 500
....*....|....*....|....*..
gi 1039782744 588 FVHGESLQAF---LIAVVVPDVESLPS 611
Cdd:PRK05852 460 AVFGVPDQLYgeaVAAVIVPRESAPPT 486
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
122-616 |
4.08e-24 |
|
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: 106.52 E-value: 4.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 122 ISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:cd12117 23 LTYAELNERANRLARRLRAAGVGP--GDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 202 DKPEKAKLLLegvenklTPCLKIIVIMDSYGSDLVERGkkcgveiislkaledlgrvnrvkpkPPEPEDLAIICFTSGTT 281
Cdd:cd12117 101 DRSLAGRAGG-------LEVAVVIDEALDAGPAGNPAV-------------------------PVSPDDLAYVMYTSGST 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 282 GNPKGAMITHQNIINDC--SGFIKATEsafiastDDVLISFLPL---AHMFETVVEcvmLCHGAKIgffqgdirllmddl 356
Cdd:cd12117 149 GRPKGVAVTHRGVVRLVknTNYVTLGP-------DDRVLQTSPLafdASTFEIWGA---LLNGARL-------------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 357 kVLQPtifPVVPRLLNRMFDRIFGQANTSLkrWLldfaskrkEAELRSGIVRNNSlwdklifhkiqSSLGGkVRLMITGA 436
Cdd:cd12117 205 -VLAP---KGTLLDPDALGALIAEEGVTVL--WL--------TAALFNQLADEDP-----------ECFAG-LRELLTGG 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 437 APVS-ATVLTFLRTALGCQFYEGYGQTECT--AGCCLSLPGDWTAGHV--GAPMPCNYVKLVDveEMNYLASKGE-GEVC 510
Cdd:cd12117 259 EVVSpPHVRRVLAACPGLRLVNGYGPTENTtfTTSHVVTELDEVAGSIpiGRPIANTRVYVLD--EDGRPVPPGVpGELY 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 511 VKGANVFKGYLKDPARTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAV 584
Cdd:cd12117 337 VGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI-RGFRIELGEIEAALRAHPGV 415
|
490 500 510
....*....|....*....|....*....|....*....
gi 1039782744 585 AQVFV------HGE-SLQAFLIAVVVPDVESLPSWAQKR 616
Cdd:cd12117 416 REAVVvvredaGGDkRLVAYVVAEGALDAAELRAFLRER 454
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
128-591 |
5.95e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 106.04 E-value: 5.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 128 AELAECIG--SGLIQK-GFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFADkp 204
Cdd:PRK09088 26 AELDALVGrlAAVLRRrGCVD--GERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGD-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 205 ekaklllegvenkltpclkiivimdsygsDLVERGKKCGVEIISLKALEDLGRVNRVKPKPPEpeDLAIICFTSGTTGNP 284
Cdd:PRK09088 102 -----------------------------DAVAAGRTDVEDLAAFIASADALEPADTPSIPPE--RVSLILFTSGTSGQP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 285 KGAMITHQNIINDCSGFIKATESafiastdDVLISFLPLAHMFETV--VECV--MLCHGAKIGFFQGdirllmddlkvLQ 360
Cdd:PRK09088 151 KGVMLSERNLQQTAHNFGVLGRV-------DAHSSFLCDAPMFHIIglITSVrpVLAVGGSILVSNG-----------FE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 361 PTifpvvpRLLNRMFDRIFGQANTslkrwlldFASKRKEAELRSGIVRNNSLWDKLIfhkiqsslggkvrLMITGAAP-V 439
Cdd:PRK09088 213 PK------RTLGRLGDPALGITHY--------FCVPQMAQAFRAQPGFDAAALRHLT-------------ALFTGGAPhA 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 440 SATVLTFLrtALGCQFYEGYGQTEctAGCCLSLPGDWT-----AGHVGAPMPCNYVKLVDVEEMNYLAskGE-GEVCVKG 513
Cdd:PRK09088 266 AEDILGWL--DDGIPMVDGFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVVDDQGNDCPA--GVpGELLLRG 339
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039782744 514 ANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:PRK09088 340 PNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIEAVLADHPGIRECAVVG 416
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
123-683 |
1.56e-23 |
|
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: 103.96 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 123 SYKEVAELAECIGSGLIQKGFKPcSEQFIGLFSqNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFAD 202
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRK-GDRVAVLLP-RVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 203 KpekaklllegvenkltpclkiivimdsygsdlvergkkcgveiislkaledlgrvnrvkpkppepEDLAIICFTSGTTG 282
Cdd:cd05972 80 A-----------------------------------------------------------------EDPALIYFTSGTTG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 283 NPKGAMITH-------------QNI--------INDcSGFIKATESAFIAstddvlisflPLAHMFetvveCVMLCHGAK 341
Cdd:cd05972 95 LPKGVLHTHsyplghiptaaywLGLrpddihwnIAD-PGWAKGAWSSFFG----------PWLLGA-----TVFVYEGPR 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 342 IgffqgDIRLLMDDLKVLQPTIFPVVPrllnrmfdrifgqanTSLKRWLldfaskrkeAELRSGIVRnnslwdklifhki 421
Cdd:cd05972 159 F-----DAERILELLERYGVTSFCGPP---------------TAYRMLI---------KQDLSSYKF------------- 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 422 qsslgGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYL 501
Cdd:cd05972 197 -----SHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIID-DDGREL 270
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 502 ASKGEGEVCVKGANV--FKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYL 579
Cdd:cd05972 271 PPGEEGDIAIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVESALL 348
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 580 RSEAVAQVFV-------HGESLQAFLiaVVVPDVESLPSWAQkrglqgsfeelcrnkdinkaildDLLKLGKEAgLKPFE 652
Cdd:cd05972 349 EHPAVAEAAVvgspdpvRGEVVKAFV--VLTSGYEPSEELAE-----------------------ELQGHVKKV-LAPYK 402
|
570 580 590
....*....|....*....|....*....|.
gi 1039782744 653 QVKGIAVHPELfsidngLLTPTLKAKRPELR 683
Cdd:cd05972 403 YPREIEFVEEL------PKTISGKIRRVELR 427
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
267-607 |
1.64e-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: 104.25 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 267 EPEDLAIICFTSGTTGNPKGAMITHQNIINdcsgFIKATESAFIASTDDVLISFLPLAhmFETvveCVM-----LCHGAk 341
Cdd:cd05945 95 DGDDNAYIIFTSGSTGRPKGVQISHDNLVS----FTNWMLSDFPLGPGDVFLNQAPFS--FDL---SVMdlypaLASGA- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 342 igffqgdirllmddlkvlqpTIFPVvPRLLNRMFDRIFgqantslkRWLLdfaskrkeaelRSGI---VRNNSLWDKLIF 418
Cdd:cd05945 165 --------------------TLVPV-PRDATADPKQLF--------RFLA-----------EHGItvwVSTPSFAAMCLL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 419 HK--IQSSLGGkVRLMITGAAPVSATVLTFLRTAL-GCQFYEGYGQTECTAGCCL------------SLPgdwtaghVGA 483
Cdd:cd05945 205 SPtfTPESLPS-LRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEATVAVTYievtpevldgydRLP-------IGY 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 484 PMPCnyVKLVDVEEMNYLASKGE-GEVCVKGANVFKGYLKDPARTAEALDKD---GWLHTGDIGKWLPNGTLKIIDRKKH 559
Cdd:cd05945 277 AKPG--AKLVILDEDGRPVPPGEkGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDF 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1039782744 560 IFKLaQGEYIAPEKIENIYLRSEAVAQVFV----HGESLQAfLIAVVVPDVE 607
Cdd:cd05945 355 QVKL-NGYRIELEEIEAALRQVPGVKEAVVvpkyKGEKVTE-LIAFVVPKPG 404
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
268-592 |
3.46e-23 |
|
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: 101.79 E-value: 3.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 268 PEDLAIICFTSGTTGNPKGAMITHQNIINDcsGFIKATESAFiaSTDDVLISFLPLAHMFETVVECVMLchgakigFFQG 347
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYN--AWMLALNSLF--DPDDVLLCGLPLFHVNGSVVTLLTP-------LASG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 348 DIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTSLKRwlldFASKRKEAELrsgivrnnslwdklifhkiqSSLgg 427
Cdd:cd05944 70 AHVVLAGPAGYRNPGLFDNFWKLVERYRITSLSTVPTVYAA----LLQVPVNADI--------------------SSL-- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 428 kvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLP-GDWTAGHVGAPMPCNYVKLVDVE-EMNYL--AS 503
Cdd:cd05944 124 --RFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKVLDgVGRLLrdCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 504 KGE-GEVCVKGANVFKGYLKDpARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSE 582
Cdd:cd05944 202 PDEvGEICVAGPGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLRHP 279
|
330
....*....|
gi 1039782744 583 AVAQVFVHGE 592
Cdd:cd05944 280 AVAFAGAVGQ 289
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
122-629 |
3.97e-23 |
|
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: 103.60 E-value: 3.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 122 ISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVKR--EERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 202 DkPEKAKLLLEGVEnKLTPCLKIIVIMDSYGSdlvERGKKCGVEIISlkALEDLGrvnrvKPKPPEPEDLAIICFTSGTT 281
Cdd:cd05959 108 S-GELAPVLAAALT-KSEHTLVVLIVSGGAGP---EAGALLLAELVA--AEAEQL-----KPAATHADDPAFWLYSSGST 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 282 GNPKGAMITHQNIINDCSGF----IKATEsafiastDDVLISFLPLAHMFEtvvecvmLCHGAKIGFFQGDIRLLM---- 353
Cdd:cd05959 176 GRPKGVVHLHADIYWTAELYarnvLGIRE-------DDVCFSAAKLFFAYG-------LGNSLTFPLSVGATTVLMperp 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 354 ------DDLKVLQPTIFPVVPRLLNRMFdrifgQANTSLKRwllDFASkrkeaelrsgivrnnslwdklifhkiqsslgg 427
Cdd:cd05959 242 tpaavfKRIRRYRPTVFFGVPTLYAAML-----AAPNLPSR---DLSS-------------------------------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 428 kVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKGEG 507
Cdd:cd05959 282 -LRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRD-EDGGDVADGEPG 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 508 EVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEAVAQV 587
Cdd:cd05959 360 ELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSPFEVESALVQHPAVLEA 437
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1039782744 588 FVHGESLQAFLI---AVVVPDVESLPSWAQKRGLQgsfeELCRNK 629
Cdd:cd05959 438 AVVGVEDEDGLTkpkAFVVLRPGYEDSEALEEELK----EFVKDR 478
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
270-611 |
5.16e-23 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 100.48 E-value: 5.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 270 DLAIICFTSGTTGNPKGAMITHQNIINDCSG---FIKATesafiaSTDDVLISfLPLAHM--FETVVECVMLchGAKIGF 344
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGlhsRLGFG------GGDSWLLS-LPLYHVggLAILVRSLLA--GAELVL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 345 FQGDiRLLMDDLKVLQPTIFPVVPRLLNRMFDRifGQANTSLKRwlldfaskrkeaelrsgivrnnslwdklifhkiqss 424
Cdd:cd17630 72 LERN-QALAEDLAPPGVTHVSLVPTQLQRLLDS--GQGPAALKS------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 425 lggkVRLMITGAAPVSAtVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDveemnylask 504
Cdd:cd17630 113 ----LRAVLLGGAPIPP-ELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVE---------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 505 gEGEVCVKGANVFKGYLKdpARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAV 584
Cdd:cd17630 178 -DGEIWVGGASLAMGYLR--GQLVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAV 253
|
330 340 350
....*....|....*....|....*....|
gi 1039782744 585 AQVFVHG---ESLQAFLIAVVVPDVESLPS 611
Cdd:cd17630 254 RDAFVVGvpdEELGQRPVAVIVGRGPADPA 283
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
122-609 |
1.02e-22 |
|
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: 102.20 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 122 ISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAEL-SVIF 200
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRP--GQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMtAAVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 201 ADkpekAKLLLEGvenkltpclkiivIMDSygsdlvergkkcGVEIISLKALEDLGRVNR----VKPKPPEPEDLAIICF 276
Cdd:cd05923 107 AV----DAQVMDA-------------IFQS------------GVRVLALSDLVGLGEPESagplIEDPPREPEQPAFVFY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 277 TSGTTGNPKGAMITHQNIinDCSGFIKATESAFIASTDDVLISFLPLAHMfetvvecvmlchgakIGFFQgdirLLMDDL 356
Cdd:cd05923 158 TSGTTGLPKGAVIPQRAA--ESRVLFMSTQAGLRHGRHNVVLGLMPLYHV---------------IGFFA----VLVAAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 357 kVLQPTIFPVvprllnRMFDRIFgqantslkrwlldfASKRKEAELRSGIVRNNSLWDKLIFHKIQSSLGGK-VRLMITG 435
Cdd:cd05923 217 -ALDGTYVVV------EEFDPAD--------------ALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSsLRHVTFA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 436 AAPVSATVLTFLRTALGCQFYEGYGQTEctAGCCLSLPgDWTAGHVGAPMPCNYVKLVDV-EEMNYLASKG-EGEVCVK- 512
Cdd:cd05923 276 GATMPDAVLERVNQHLPGEKVNIYGTTE--AMNSLYMR-DARTGTEMRPGFFSEVRIVRIgGSPDEALANGeEGELIVAa 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 513 -GANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:cd05923 353 aADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIG 430
|
490 500
....*....|....*....|.
gi 1039782744 592 ---ESLQAFLIAVVVPDVESL 609
Cdd:cd05923 431 vadERWGQSVTACVVPREGTL 451
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
265-617 |
1.13e-22 |
|
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: 102.04 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 265 PPEPEDLAIICFTSGTTGNPKGAMITHQNIINdcsgFIKATESAFIASTDDVLISFLPLAhmFETVVECVM--LCHGAKI 342
Cdd:cd17651 132 ALDADDLAYVIYTSGSTGRPKGVVMPHRSLAN----LVAWQARASSLGPGARTLQFAGLG--FDVSVQEIFstLCAGATL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 343 GFFQGDIRllMDDLKVLqptifpvvpRLLNRM-FDRIFgqANTSLKRWLLdfaskrkeAELRSGIVRNNSLwdklifhki 421
Cdd:cd17651 206 VLPPEEVR--TDPPALA---------AWLDEQrISRVF--LPTVALRALA--------EHGRPLGVRLAAL--------- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 422 qsslggkvRLMITGAAPVSATVLT--FLRTALGCQFYEGYGQTECTAGCCLSLPGD---WTA-GHVGAPMPCNYVKLVDv 495
Cdd:cd17651 256 --------RYLLTGGEQLVLTEDLreFCAGLPGLRLHNHYGPTETHVVTALSLPGDpaaWPApPPIGRPIDNTRVYVLD- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 496 EEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 569
Cdd:cd17651 327 AALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGFRI 405
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1039782744 570 APEKIENIYLRSEAVAQ--VFVHGE-SLQAFLIAVVVPDVESLPSWAQKRG 617
Cdd:cd17651 406 ELGEIEAALARHPGVREavVLAREDrPGEKRLVAYVVGDPEAPVDAAELRA 456
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
267-616 |
1.19e-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: 101.74 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 267 EPEDLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKATesaFIASTDDVLIsFLPLAhmFETVVE--CVMLCHGAKIgf 344
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEY---GITSSDRVLQ-FASIA--FDVAAEeiYVTLLSGATL-- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 345 fqgdirllmddlkVLQPtifpvvprllNRMFdrifgqantslkRWLLDFASKRKEAELRsgiVRN--NSLWDKLIFHKIQ 422
Cdd:cd17644 176 -------------VLRP----------EEMR------------SSLEDFVQYIQQWQLT---VLSlpPAYWHLLVLELLL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 423 SSLGG--KVRLMITGAAPVSATVLTFLRTALG--CQFYEGYGQTECTAGCCLSLPGDWTAGH-----VGAPMPC------ 487
Cdd:cd17644 218 STIDLpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIANtqvyil 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 488 -NYVKLVDVEEMnylaskgeGEVCVKGANVFKGYLKDPARTAEALDKDGWLH--------TGDIGKWLPNGTLKIIDRKK 558
Cdd:cd17644 298 dENLQPVPVGVP--------GELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRID 369
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039782744 559 HIFKLaQGEYIAPEKIENIYLRSEAVAQVFV---HGESLQAFLIAVVVPDVESLPSWAQKR 616
Cdd:cd17644 370 NQVKI-RGFRIELGEIEAVLSQHNDVKTAVVivrEDQPGNKRLVAYIVPHYEESPSTVELR 429
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
122-605 |
5.76e-22 |
|
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: 100.22 E-value: 5.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 122 ISYKEVAELAECIGSGLIQKGFKPcseqfiG---LFsQ--NRPEWVIVEQGCFSysMVVVPLYdTLGAD---AITYIVNK 193
Cdd:COG1021 51 LSYAELDRRADRLAAGLLALGLRP------GdrvVV-QlpNVAEFVIVFFALFR--AGAIPVF-ALPAHrraEISHFAEQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 194 AELS-VIFADKPEK------AKLLLEGVenkltPCLKIIVIMDSYGSDLvergkkcgveiislkALEDLGRVNRVKPKP- 265
Cdd:COG1021 121 SEAVaYIIPDRHRGfdyralARELQAEV-----PSLRHVLVVGDAGEFT---------------SLDALLAAPADLSEPr 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 266 PEPEDLAIICFTSGTTGNPKgaMI--THqniiND--CSgfikATESAFIA--STDDVLISFLPLAHMFETVVECVM--LC 337
Cdd:COG1021 181 PDPDDVAFFQLSGGTTGLPK--LIprTH----DDylYS----VRASAEICglDADTVYLAALPAAHNFPLSSPGVLgvLY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 338 HGAKIgffqgdirllmddlkVLQP-----TIFP-----------VVPRLLNRMfdrifgqantslkrwlLDFASKRKeAE 401
Cdd:COG1021 251 AGGTV---------------VLAPdpspdTAFPlierervtvtaLVPPLALLW----------------LDAAERSR-YD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 402 LrsgivrnnslwdklifhkiqSSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTEctaG--CCLSL--PGDWT 477
Cdd:COG1021 299 L--------------------SSL----RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---GlvNYTRLddPEEVI 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 478 AGHVGAPM-PCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDR 556
Cdd:COG1021 352 LTTQGRPIsPDDEVRIVD-EDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGR 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1039782744 557 KK-HIFKlaQGEYIAPEKIENIYLRSEAVAQVfvhgeslqafliAVV-VPD 605
Cdd:COG1021 431 AKdQINR--GGEKIAAEEVENLLLAHPAVHDA------------AVVaMPD 467
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
267-619 |
6.31e-22 |
|
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: 99.04 E-value: 6.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 267 EPEDLAIICFTSGTTGNPKGAM--------------ITHQNIINDCSGFIKATESAFIASTDDVLisfLPLAHMFETVVE 332
Cdd:cd05971 86 GSDDPALIIYTSGTTGPPKGALhahrvllghlpgvqFPFNLFPRDGDLYWTPADWAWIGGLLDVL---LPSLYFGVPVLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 333 CVMLchgakiGFFQGDIRLLMDDLKV----LQPTIFpvvprllnrmfdRIFGQANTSLKRWLLdfaskrkeaelrsgivr 408
Cdd:cd05971 163 HRMT------KFDPKAALDLMSRYGVttafLPPTAL------------KMMRQQGEQLKHAQV----------------- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 409 nnslwdklifhkiqsslggKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTA--GCCLSLpGDWTAGHVGAPMP 486
Cdd:cd05971 208 -------------------KLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLviGNCSAL-FPIKPGSMGKPIP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 487 CNYVKLVDvEEMNYLASKGEGEVCVK--GANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLA 564
Cdd:cd05971 268 GHRVAIVD-DNGTPLPPGEVGEIAVElpDPVAFLGYWNNPSATEKKM-AGDWLLTGDLGRKDSDGYFWYVGRDDDVITSS 345
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039782744 565 qGEYIAPEKIENIYLRSEAVAQVFV-------HGESLQAFLiaVVVPDVEslPSWAQKRGLQ 619
Cdd:cd05971 346 -GYRIGPAEIEECLLKHPAVLMAAVvgipdpiRGEIVKAFV--VLNPGET--PSDALAREIQ 402
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
270-607 |
7.35e-22 |
|
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: 97.34 E-value: 7.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 270 DLAIICFTSGTTGNPKGAMITHQNIIndCSGFikATESAFIASTDDVLISFLPLAHMFETVVECVMLCHGAK---IGFFQ 346
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLI--AANL--QLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGAnvvMEKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 347 GDIRL-LMDDLKVlqpTIFPVVPRLLNRMFDRIfgqantslkrwlldfasKRKEAELRSgiVRNnslwdklifhkiqssl 425
Cdd:cd17637 77 PAEALeLIEEEKV---TLMGSFPPILSNLLDAA-----------------EKSGVDLSS--LRH---------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 426 ggkvrlmITGA-APvsATVLTFLRTAlGCQFYEGYGQTECTAGCCLSlPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASK 504
Cdd:cd17637 119 -------VLGLdAP--ETIQRFEETT-GATFWSLYGQTETSGLVTLS-PYRERPGSAGRPGPLVRVRIVD-DNDRPVPAG 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 505 GEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRK--KHIFKlAQGEYIAPEKIENIYLRSE 582
Cdd:cd17637 187 ETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKVILEHP 264
|
330 340
....*....|....*....|....*
gi 1039782744 583 AVAQVFVHGeslqafliavvVPDVE 607
Cdd:cd17637 265 AIAEVCVIG-----------VPDPK 278
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
113-607 |
1.26e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 99.26 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 113 RKPNQPYEW-----ISYKEVAELAECIGSGLIQK-GFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADA 186
Cdd:PRK08314 22 RYPDKTAIVfygraISYRELLEEAERLAGYLQQEcGVRKGDR--VLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 187 ITYIVNKAELSVIFAdkpekAKLLLEGVE--NKLTPCLKIIV-----IMDSYGSDLVERGkkCGVEIiSLKALEDLGRV- 258
Cdd:PRK08314 100 LAHYVTDSGARVAIV-----GSELAPKVApaVGNLRLRHVIVaqysdYLPAEPEIAVPAW--LRAEP-PLQALAPGGVVa 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 259 ------NRVKPKPPE--PEDLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKATESAFiastDDVLISFLPLAHMfeTV 330
Cdd:PRK08314 172 wkealaAGLAPPPHTagPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTP----ESVVLAVLPLFHV--TG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 331 VECVMlcHGAkigFFQGDIRLLMddlkvlqptifP-----VVPRLLNRMfdRIFGQANTSlkRWLLDF-ASKR-KEAELR 403
Cdd:PRK08314 246 MVHSM--NAP---IYAGATVVLM-----------PrwdreAAARLIERY--RVTHWTNIP--TMVVDFlASPGlAERDLS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 404 SgivrnnsLWdklifhkiqsSLGGkvrlmitGAAPVSATVLTFLRTALGCQFYEGYGQTECTAG-----------CCLSL 472
Cdd:PRK08314 306 S-------LR----------YIGG-------GGAAMPEAVAERLKELTGLDYVEGYGLTETMAQthsnppdrpklQCLGI 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 473 PgdwTAGhVGApmpcnyvKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEA---LDKDGWLHTGDIGKWLPNG 549
Cdd:PRK08314 362 P---TFG-VDA-------RVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEG 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039782744 550 TLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEAVAQVFV-------HGESLQafliAVVVPDVE 607
Cdd:PRK08314 431 YFFITDRLKRMIN-ASGFKVWPAEVENLLYKHPAIQEACViatpdprRGETVK----AVVVLRPE 490
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
265-599 |
1.73e-21 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 98.60 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 265 PPEPEDLAIICFTSGTTGNPKGAMITHQNIIndCSGFIKATESAFIAstDDVLISFLPLAHM-FETVVECVMLCHGAKIG 343
Cdd:PRK08008 169 PLSTDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYYSAWQCALRD--DDVYLTVMPAFHIdCQCTAAMAAFSAGATFV 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 344 F--------FQGDIRLLmddlkvlQPTIFPVVPRLLNRMfdrifgqantslkrwLLDFASKRKeaelrsgivRNNSLWDK 415
Cdd:PRK08008 245 LlekysaraFWGQVCKY-------RATITECIPMMIRTL---------------MVQPPSAND---------RQHCLREV 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 416 LIFhkiqsslggkvrLMITgaapvSATVLTFLrTALGCQFYEGYGQTECTAGCCLSLPGD---WTAghVGAPMPCNYVKL 492
Cdd:PRK08008 294 MFY------------LNLS-----DQEKDAFE-ERFGVRLLTSYGMTETIVGIIGDRPGDkrrWPS--IGRPGFCYEAEI 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 493 VDvEEMNYLASKGEGEVCVKGA---NVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYI 569
Cdd:PRK08008 354 RD-DHNRPLPAGEIGEICIKGVpgkTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENV 431
|
330 340 350
....*....|....*....|....*....|....*..
gi 1039782744 570 APEKIENIYLRSEAVAQVFVHG-------ESLQAFLI 599
Cdd:PRK08008 432 SCVELENIIATHPKIQDIVVVGikdsirdEAIKAFVV 468
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
269-631 |
1.08e-20 |
|
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: 93.86 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 269 EDLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKATESAfiaSTDDVLISFLPLAHMFETVVECVMLCHGAKIGFFQGD 348
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNW---VVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 349 IRL--LMDDLKVLQPTIFPVVPRLLNRMfdrifgqantslkrwLLDFASKRKEAElrsgivrnnslwdklifhkiqsslg 426
Cdd:cd17635 78 TTYksLFKILTTNAVTTTCLVPTLLSKL---------------VSELKSANATVP------------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 427 gKVRLMITGAA-PVSATVLTFLRTALgCQFYEGYGQTECTAGCCLSLPGDWT-AGHVGAPMPCNYVKLVDVEEMNyLASK 504
Cdd:cd17635 118 -SLRLIGYGGSrAIAADVRFIEATGL-TNTAQVYGLSETGTALCLPTDDDSIeINAVGRPYPGVDVYLAATDGIA-GPSA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 505 GEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAV 584
Cdd:cd17635 195 SFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERIAEGVSGV 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1039782744 585 AQVFVH-------GESLQAFLIAVVVPDvESLPSwAQKRGLQGSFEELCRNKDI 631
Cdd:cd17635 273 QECACYeisdeefGELVGLAVVASAELD-ENAIR-ALKHTIRRELEPYARPSTI 324
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
120-605 |
2.36e-20 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 95.38 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 120 EWISYKEVAELAECIGSGLIQKGfkPCSEQFIGLFSQNrPEWVIVEQGCFSYSMVVVPLYD---TLGADAITYIVNKAEL 196
Cdd:cd05931 23 ETLTYAELDRRARAIAARLQAVG--KPGDRVLLLAPPG-LDFVAAFLGCLYAGAIAVPLPPptpGRHAERLAAILADAGP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 197 SVIFADKPEKAKLLLEGVENKLTPCLKIIVImdsygsDLVErgkkcgveiislkaledLGRVNRVKPKPPEPEDLAIICF 276
Cdd:cd05931 100 RVVLTTAAALAAVRAFAASRPAAGTPRLLVV------DLLP-----------------DTSAADWPPPSPDPDDIAYLQY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 277 TSGTTGNPKGAMITHQNIINDCsgfiKATESAFIASTDDVLISFLPLAH-M------FETVV---ECVMLchgAKIGFFQ 346
Cdd:cd05931 157 TSGSTGTPKGVVVTHRNLLANV----RQIRRAYGLDPGDVVVSWLPLYHdMgligglLTPLYsggPSVLM---SPAAFLR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 347 GDIRLLmddlkvlqptifpvvpRLLNRMFDRI-----FGqantslkrwlLDFASKRKEAELRSGIvrnnslwDkLifhki 421
Cdd:cd05931 230 RPLRWL----------------RLISRYRATIsaapnFA----------YDLCVRRVRDEDLEGL-------D-L----- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 422 qsslgGKVRLMITGAAPVSATVLT-FLRTALGCQF-----YEGYGQTECT----------AGCCLSLPGDWTAGHV---- 481
Cdd:cd05931 271 -----SSWRVALNGAEPVRPATLRrFAEAFAPFGFrpeafRPSYGLAEATlfvsggppgtGPVVLRVDRDALAGRAvava 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 482 ------------GAPMPCNYVKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAE------ALDKDGWLHTGDIG 543
Cdd:cd05931 346 addpaarelvscGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaATDEGGWLRTGDLG 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039782744 544 kWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENiylrseAVAQvfVHGESLQAFLIAVVVPD 605
Cdd:cd05931 426 -FLHDGELYITGRLKDLIIVR-GRNHYPQDIEA------TAEE--AHPALRPGCVAAFSVPD 477
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
55-606 |
3.34e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 96.38 E-value: 3.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 55 CDLSMQSVEiagttdgiRRSAVLEDDKLLVYYYDDvRTMYDGFQRGIQVSNNGPCLGSRKpnqpyEWISYKEVAELAECI 134
Cdd:PRK12467 485 GELPLLDAE--------ERARELVRWNAPATEYAP-DCVHQLIEAQARQHPERPALVFGE-----QVLSYAELNRQANRL 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 135 GSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFADkPEKAKLLlegv 214
Cdd:PRK12467 551 AHVLIAAGVGP--DVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQ-SHLLAQL---- 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 215 enkltpclkiivimdsygsDLVErgkkcGVEIISLKALEDL--GRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQ 292
Cdd:PRK12467 624 -------------------PVPA-----GLRSLCLDEPADLlcGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHG 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 293 NIINdcsgFIKATESAFIASTDDVLISFLPLAHMFETVVECVMLCHGAKIgffqgdirLLMDDLKVLQPTIFpvvprlln 372
Cdd:PRK12467 680 ALAN----YVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATL--------HLLPPDCARDAEAF-------- 739
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 373 rmFDRIFGQANTSLKrwlldfaskrkeaelrsgIVrnNSLWDKLIFHKIQSSLGGKVRLMITGAA-PVSATVLTFlRTAL 451
Cdd:PRK12467 740 --AALMADQGVTVLK------------------IV--PSHLQALLQASRVALPRPQRALVCGGEAlQVDLLARVR-ALGP 796
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 452 GCQFYEGYGQTECTAGC----CLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPART 527
Cdd:PRK12467 797 GARLINHYGPTETTVGVstyeLSDEERDFGNVPIGQPLANLGLYILD-HYLNPVPVGVVGELYIGGAGLARGYHRRPALT 875
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 528 AEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFV--HGESLQAFL 598
Cdd:PRK12467 876 AERFVPDpfgadgGRLYrTGDLARYRADGVIEYLGRMDHQVKI-RGFRIELGEIEARLLAQPGVREAVVlaQPGDAGLQL 954
|
....*...
gi 1039782744 599 IAVVVPDV 606
Cdd:PRK12467 955 VAYLVPAA 962
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
268-683 |
4.10e-20 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 94.48 E-value: 4.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 268 PEDLAIICFTSGTTGNPKGAMITHQNIIndcsgfikaTES-AFIA----STDDVLISFLPLAHM--FETVVECVML--CH 338
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSALI---------VQSlAKIAivgyGEDDVYLHTAPLCHIggLSSALAMLMVgaCH 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 339 GAKIGFfqgDIRLLMDDLKVLQPTIFPVVPRLL------NRMfdRIFGQANTSLKRwLLDFAskrkeaelrsGIVRNNSL 412
Cdd:PLN02860 242 VLLPKF---DAKAALQAIKQHNVTSMITVPAMMadlislTRK--SMTWKVFPSVRK-ILNGG----------GSLSSRLL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 413 WD-KLIF--HKIQSSLGgkvrlmITGAApvsaTVLTFLRtaLGCQFYEGYGQTECTAGCCLSLPGDWTAGH-VGAPMPcn 488
Cdd:PLN02860 306 PDaKKLFpnAKLFSAYG------MTEAC----SSLTFMT--LHDPTLESPKQTLQTVNQTKSSSVHQPQGVcVGKPAP-- 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 489 YVKLvdveEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEY 568
Cdd:PLN02860 372 HVEL----KIGLDESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIK-TGGEN 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 569 IAPEKIENIYLRSEAVAQVFVHGeSLQAFLIAVVVPDVESLPSW--------AQKRGLQGSFEEL---CRNKdinkaild 637
Cdd:PLN02860 447 VYPEEVEAVLSQHPGVASVVVVG-VPDSRLTEMVVACVRLRDGWiwsdnekeNAKKNLTLSSETLrhhCREK-------- 517
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1039782744 638 dllklgkeaGLKPFEQVKGIAVHPELFSidnglLTPTLKAKRPELR 683
Cdd:PLN02860 518 ---------NLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEVR 549
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
267-616 |
4.13e-20 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 93.69 E-value: 4.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 267 EPEDLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKATESAF-------IAStddvlISFLPLAHMFetvveCVMLCHG 339
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSfpvrllqMAS-----FSFDVFAGDF-----ARSLLNG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 340 akigffqGDIRLLMDDLKVLQPTIFpvvpRLLNRMFDRIFgQANTSLKRWLLDFASKRKE--AELRSGIVRNNSLWDKLi 417
Cdd:cd17650 161 -------GTLVICPDEVKLDPAALY----DLILKSRITLM-ESTPALIRPVMAYVYRNGLdlSAMRLLIVGSDGCKAQD- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 418 FHKIQSSLGGKVRLmITGAAPVSATVLTflrtalgcQFYEGYGQTECTAGcclSLPgdwtaghVGAPMPCNYVKLVDvEE 497
Cdd:cd17650 228 FKTLAARFGQGMRI-INSYGVTEATIDS--------TYYEEGRDPLGDSA---NVP-------IGRPLPNTAMYVLD-ER 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 498 MNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAP 571
Cdd:cd17650 288 LQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI-RGFRIEL 366
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1039782744 572 EKIENIYLRSEAVAQVFV---HGESLQAFLIAVVVPDveSLPSWAQKR 616
Cdd:cd17650 367 GEIESQLARHPAIDEAVVavrEDKGGEARLCAYVVAA--ATLNTAELR 412
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
174-591 |
4.23e-20 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 94.46 E-value: 4.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 174 VVVPLYDTLGADAITYIVNKAELSVIFADkPEKAKLLLEGVENklTPCLKIIVIMDSYGSDLVERGKKCGVEIISLKALE 253
Cdd:PRK05620 90 VFNPLNKQLMNDQIVHIINHAEDEVIVAD-PRLAEQLGEILKE--CPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 254 DlGRvNRVKPKPPEPEDLAI-ICFTSGTTGNPKGAMITHQNIINDCSGfIKATESafIASTDDVliSFL---PLAHmfet 329
Cdd:PRK05620 167 D-GR-STVYDWPELDETTAAaICYSTGTTGAPKGVVYSHRSLYLQSLS-LRTTDS--LAVTHGE--SFLccvPIYH---- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 330 vvecvMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRmfdrifgQANTSlkrwlldfaskrkeaelrsgivrn 409
Cdd:PRK05620 236 -----VLSWGVPLAAFMSGTPLVFPGPDLSAPTLAKIIATAMPR-------VAHGV------------------------ 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 410 NSLWDKLIFHKIQS-----SLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGA- 483
Cdd:PRK05620 280 PTLWIQLMVHYLKNppermSL----QEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEARWa 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 484 --------PMPCNYvKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPART----------------AEALDKDGWLHT 539
Cdd:PRK05620 356 yrvsqgrfPASLEY-RIVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPTEEgggaastfrgedvedaNDRFTADGWLRT 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1039782744 540 GDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:PRK05620 435 GDVGSVTRDGFLTIHDRARDVIR-SGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
120-609 |
4.84e-20 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 94.44 E-value: 4.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 120 EWISYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVI 199
Cdd:PRK06155 45 TRWTYAEAARAAAAAAHALAAAGVKRGDR--VALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 200 FADkpekAKLL--LEGVENKLTPcLKIIVIMDSYGSDLVERGkkcgVEIISLKALEDlgrvnRVKPKPPEPEDLAIICFT 277
Cdd:PRK06155 123 VVE----AALLaaLEAADPGDLP-LPAVWLLDAPASVSVPAG----WSTAPLPPLDA-----PAPAAAVQPGDTAAILYT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 278 SGTTGNPKGAMITHQNIindcsgFIKATESAFI--ASTDDVLISFLPLAH-----MFETVvecvmLCHGAKI-------- 342
Cdd:PRK06155 189 SGTTGPSKGVCCPHAQF------YWWGRNSAEDleIGADDVLYTTLPLFHtnalnAFFQA-----LLAGATYvleprfsa 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 343 -GFFqgdirllmDDLKVLQPTIF----PVVPRLLnrmfdrifgqantslkrwlldfaSKRKEAELRSgivrnnslwdkli 417
Cdd:PRK06155 258 sGFW--------PAVRRHGATVTyllgAMVSILL-----------------------SQPARESDRA------------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 418 fHKIQSSLGGKVrlmitgaapvSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDwTAGHVGAPMPCNYVKLVDvEE 497
Cdd:PRK06155 294 -HRVRVALGPGV----------PAALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSMGRLAPGFEARVVD-EH 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 498 MNYLASKGEGEVCVKGANVF---KGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKI 574
Cdd:PRK06155 361 DQELPDGEPGELLLRADEPFafaTGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIKDAIR-RRGENISSFEV 438
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1039782744 575 ENIYLRSEAVAQVFVH------GESlqAFLIAVVVPDVESL 609
Cdd:PRK06155 439 EQVLLSHPAVAAAAVFpvpselGED--EVMAAVVLRDGTAL 477
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
267-616 |
4.85e-20 |
|
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: 93.53 E-value: 4.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 267 EPEDLAIICFTSGTTGNPKGAMITHQNIIndcsGFIKATESAFIASTDDVLISFLPLAHMFeTVVEcvM---LCHGAKIG 343
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVL----ALFAATQRWFGFNEDDVWTLFHSYAFDF-SVWE--IwgaLLHGGRLV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 344 FFQGDIRLLMDDLkvlqptifpvvPRLLNRMFDRIFGQANTSLKRWLldfaskrkEAELRsgivrnnslwdkliFHKIQS 423
Cdd:cd17643 164 VVPYEVARSPEDF-----------ARLLRDEGVTVLNQTPSAFYQLV--------EAADR--------------DGRDPL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 424 SLggkvRLMITGAAPVSATVLT--FLRTALGC-QFYEGYGQTECTAGCCL------SLPGDwTAGHVGAPMPCNYVKLVD 494
Cdd:cd17643 211 AL----RYVIFGGEALEAAMLRpwAGRFGLDRpQLVNMYGITETTVHVTFrpldaaDLPAA-AASPIGRPLPGLRVYVLD 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 495 vEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAE-------ALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGE 567
Cdd:cd17643 286 -ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI-RGF 363
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1039782744 568 YIAPEKIENIYLRSEAVAQVFV---HGESLQAFLIAVVVPDVESLPSWAQKR 616
Cdd:cd17643 364 RIELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVADDGAAADIAELR 415
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
136-577 |
4.91e-20 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 95.42 E-value: 4.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 136 SGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFADKP--EKAKL--LL 211
Cdd:PRK06814 672 GRKLKKNTPP--GENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLTSRAfiEKARLgpLI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 212 EGVENKLtpclKIIVIMDsygsdlVERGKKCGVEIISLKAledlGRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITH 291
Cdd:PRK06814 750 EALEFGI----RIIYLED------VRAQIGLADKIKGLLA----GRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSH 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 292 QNIINDCsgfikATESAFI-ASTDDVLISFLPLAHMFETVVECVM-LCHGAKIGFFQgdirllmddlkvlQPTIFPVVPR 369
Cdd:PRK06814 816 RNLLANR-----AQVAARIdFSPEDKVFNALPVFHSFGLTGGLVLpLLSGVKVFLYP-------------SPLHYRIIPE 877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 370 LLnrmFDR----IFGqANTSLKRWL-----LDFASkrkeaelrsgivrnnslwdklifhkiqsslggkVRLMITGAAPVS 440
Cdd:PRK06814 878 LI---YDTnatiLFG-TDTFLNGYAryahpYDFRS---------------------------------LRYVFAGAEKVK 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 441 ATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDVEEMNylasKGeGEVCVKGANVFKGY 520
Cdd:PRK06814 921 EETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGID----EG-GRLFVRGPNVMLGY 995
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039782744 521 LK-DPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 577
Cdd:PRK06814 996 LRaENPGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAVEEL 1051
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
122-616 |
6.83e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 93.95 E-value: 6.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 122 ISYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:PRK06178 59 ITYAELDELSDRFAALLRQRGVGAGDR--VAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 202 -DKpekaklLLEGVENKLTPCLKIIVIMDSYGS-----------DLVERGKKCGVEIISLKALEDLGRVNRVKPkPPEPE 269
Cdd:PRK06178 137 lDQ------LAPVVEQVRAETSLRHVIVTSLADvlpaeptlplpDSLRAPRLAAAGAIDLLPALRACTAPVPLP-PPALD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 270 DLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKAtesAFIASTDDVLISFLPlahMFETVVEcvmlchgakigffqgdi 349
Cdd:PRK06178 210 ALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAV---AVVGGEDSVFLSFLP---EFWIAGE----------------- 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 350 rllmdDLKVLQPTIF--PVVprLLNRmfdrifgqantslkrwlldfaskrkeaelrsgivrnnslWDKLIF------HKI 421
Cdd:PRK06178 267 -----NFGLLFPLFSgaTLV--LLAR---------------------------------------WDAVAFmaaverYRV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 422 QSSLG---GKVRLMITGAapVSATVLTFLRTAL--------------------GCQFYEG-YGQTEcTAGCclslpGDWT 477
Cdd:PRK06178 301 TRTVMlvdNAVELMDHPR--FAEYDLSSLRQVRvvsfvkklnpdyrqrwraltGSVLAEAaWGMTE-THTC-----DTFT 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 478 AG-------------HVGAPMPCNYVKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGK 544
Cdd:PRK06178 373 AGfqdddfdllsqpvFVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGK 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 545 WLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFV-------HGESLQAFLiaVVVP----DVESLPSWA 613
Cdd:PRK06178 452 IDEQGFLHYLGRRKEMLKV-NGMSVFPSEVEALLGQHPAVLGSAVvgrpdpdKGQVPVAFV--QLKPgadlTAAALQAWC 528
|
...
gi 1039782744 614 QKR 616
Cdd:PRK06178 529 REN 531
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
122-605 |
3.75e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 93.10 E-value: 3.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 122 ISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGVGP--EVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLT 2106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 202 DKPEKAKLLLEGvenkltpclkiivimdsygsdlvergkkcGVEIISLKALEDLGRVNRVKPKPP-EPEDLAIICFTSGT 280
Cdd:PRK12316 2107 QRHLLERLPLPA-----------------------------GVARLPLDRDAEWADYPDTAPAVQlAGENLAYVIYTSGS 2157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 281 TGNPKGAMITHQNIINdcsgFIKATESAFIASTDDVLISFLPLAhmFETVVECVM--LCHGAkigffqgdiRLLMDDLKV 358
Cdd:PRK12316 2158 TGLPKGVAVSHGALVA----HCQAAGERYELSPADCELQFMSFS--FDGAHEQWFhpLLNGA---------RVLIRDDEL 2222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 359 LQPtifpvvprllNRMFDRIFGQANTslkrwLLDFASkrkeaelrsgivrnnSLWDKLIFHKIQSSLGGKVRLMITGAAP 438
Cdd:PRK12316 2223 WDP----------EQLYDEMERHGVT-----ILDFPP---------------VYLQQLAEHAERDGRPPAVRVYCFGGEA 2272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 439 VSATVLTFLRTALGCQF-YEGYGQTECTA-----GCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVK 512
Cdd:PRK12316 2273 VPAASLRLAWEALRPVYlFNGYGPTEAVVtpllwKCRPQDPCGAAYVPIGRALGNRRAYILD-ADLNLLAPGMAGELYLG 2351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 513 GANVFKGYLKDPARTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVA 585
Cdd:PRK12316 2352 GEGLARGYLNRPGLTAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKI-RGFRIELGEIEARLQAHPAVR 2430
|
490 500
....*....|....*....|...
gi 1039782744 586 QVFV---HGESLQAfLIAVVVPD 605
Cdd:PRK12316 2431 EAVVvaqDGASGKQ-LVAYVVPD 2452
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
267-614 |
6.74e-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: 90.12 E-value: 6.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 267 EPEDLAIICFTSGTTGNPKGAMITHQNIINDCsgfiKATESAFIASTDDVLISFLPLAhmFETVVECVM--LCHGAkigf 344
Cdd:cd17649 92 HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHC----QATAERYGLTPGDRELQFASFN--FDGAHEQLLppLICGA---- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 345 fqgdiRLLMDDLKVLQPtifpvvPRLLNRMFDR----IFGQANTSLKRWLLDFASKrkeaelrsgivrnnslwdklifhk 420
Cdd:cd17649 162 -----CVVLRPDELWAS------ADELAEMVRElgvtVLDLPPAYLQQLAEEADRT------------------------ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 421 iQSSLGGKVRLMITGAAPVSATVLTFLRTAlGCQFYEGYGQTEC--TAGCCLSLPGDWTAGH---VGAPMPcNYVKLVDV 495
Cdd:cd17649 207 -GDGRPPSLRLYIFGGEALSPELLRRWLKA-PVRLFNAYGPTEAtvTPLVWKCEAGAARAGAsmpIGRPLG-GRSAYILD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 496 EEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEAL--DKDG-----WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEY 568
Cdd:cd17649 284 ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFvpDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-RGFR 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1039782744 569 IAPEKIENIYLRSEAVAQVFVHGES--LQAFLIAVVVP-DVESLPSWAQ 614
Cdd:cd17649 363 IELGEIEAALLEHPGVREAAVVALDgaGGKQLVAYVVLrAAAAQPELRA 411
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
251-575 |
1.92e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 89.28 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 251 ALEDLGRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKATEsafIASTDDVLISFLPLAH-Mfet 329
Cdd:PRK07768 134 TVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAE---FDVETDVMVSWLPLFHdM--- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 330 vvecvmlchgAKIGFFQGDIRLLMDDLKVlQPTIFPVVPRLLNRMFDRIFGQ-------ANTSLKRwLLDFASKRKEAEL 402
Cdd:PRK07768 208 ----------GMVGFLTVPMYFGAELVKV-TPMDFLRDPLLWAELISKYRGTmtaapnfAYALLAR-RLRRQAKPGAFDL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 403 rsgivrnnslwdklifhkiqSSLggkvRLMITGAAPVS-ATVLTFL---------RTALGCqfyeGYGQTECTAGCCLSL 472
Cdd:PRK07768 276 --------------------SSL----RFALNGAEPIDpADVEDLLdagarfglrPEAILP----AYGMAEATLAVSFSP 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 473 PGD--------------------WTAGHV------GAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLkDPAR 526
Cdd:PRK07768 328 CGAglvvdevdadllaalrravpATKGNTrrlatlGPPLPGLEVRVVD-EDGQVLPPRGVGVIELRGESVTPGYL-TMDG 405
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1039782744 527 TAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIE 575
Cdd:PRK07768 406 FIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPTDIE 453
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
267-600 |
3.67e-18 |
|
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: 87.52 E-value: 3.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 267 EPEDLAIICFTSGTTGNPKGAMITHQNIINDCSGFikATESAFIASTDDVLISflplAHMFETVvecvMLCHGAKIGFFQ 346
Cdd:cd05919 89 SADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAM--AREALGLTPGDRVFSS----AKMFFGY----GLGNSLWFPLAV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 347 GDIRLLMDD----------LKVLQPTIFPVVPRLLNRMFDrifgQANTSlkrwlldfaskrkEAELRSgivrnnslwdkl 416
Cdd:cd05919 159 GASAVLNPGwptaervlatLARFRPTVLYGVPTFYANLLD----SCAGS-------------PDALRS------------ 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 417 ifhkiqsslggkVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDvE 496
Cdd:cd05919 210 ------------LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD-E 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 497 EMNYLASKGEGEVCVKGANVFKGYLKDPaRTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEN 576
Cdd:cd05919 277 EGHTIPPGEEGDLLVRGPSAAVGYWNNP-EKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVES 354
|
330 340 350
....*....|....*....|....*....|.
gi 1039782744 577 IYLRSEAVAQVFV------HGES-LQAFLIA 600
Cdd:cd05919 355 LIIQHPAVAEAAVvavpesTGLSrLTAFVVL 385
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
182-627 |
4.54e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 88.08 E-value: 4.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 182 LGADAITYIVNKAELSVIFADkPEKAKLLLEGVEnkLTPCLKIIVI---MDSYGsdlvergkkcGVEIISLKALEDL--- 255
Cdd:PRK08162 102 LDAASIAFMLRHGEAKVLIVD-TEFAEVAREALA--LLPGPKPLVIdvdDPEYP----------GGRFIGALDYEAFlas 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 256 GRVNRVkPKPPEPEDLAI-ICFTSGTTGNPKGAMITHQN-IINDCSGfikatesafIASTD----DVLISFLPLAHmfet 329
Cdd:PRK08162 169 GDPDFA-WTLPADEWDAIaLNYTSGTTGNPKGVVYHHRGaYLNALSN---------ILAWGmpkhPVYLWTLPMFH---- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 330 vveCVMLCH--------GAKIGFFQGDIRLLMDDLKVLQPTIF---PVVPRLLnrmfdrifgqANTslkrwlldfaskrk 398
Cdd:PRK08162 235 ---CNGWCFpwtvaaraGTNVCLRKVDPKLIFDLIREHGVTHYcgaPIVLSAL----------INA-------------- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 399 EAELRSGIvrnnslwdklifhkiqsslGGKVRLMITGAAPVSAtVLTFLRtALGCQFYEGYGQTEC--TAGCCLSLPGdW 476
Cdd:PRK08162 288 PAEWRAGI-------------------DHPVHAMVAGAAPPAA-VIAKME-EIGFDLTHVYGLTETygPATVCAWQPE-W 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 477 TA----------GHVGAPMPC-NYVKLVDVEEMNYLASKGE--GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIG 543
Cdd:PRK08162 346 DAlplderaqlkARQGVRYPLqEGVTVLDPDTMQPVPADGEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 544 KWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVaqvfvhgeslqafLIAVVV--PDveslPSWAQ------- 614
Cdd:PRK08162 425 VLHPDGYIKIKDRSKDII-ISGGENISSIEVEDVLYRHPAV-------------LVAAVVakPD----PKWGEvpcafve 486
|
490
....*....|....*..
gi 1039782744 615 -KRGLQGSFEEL---CR 627
Cdd:PRK08162 487 lKDGASATEEEIiahCR 503
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
116-688 |
7.29e-18 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 87.16 E-value: 7.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 116 NQPYEWISYKEVAELAECIGSGLIQKGFKPCSEQFIGLfsQNRPEWVIVEQGCFSYSMVVVPlydtlgadaityivnkae 195
Cdd:cd05908 10 DKKEKFVSYRHLREEALGYLGALQELGIKPGQEVVFQI--THNNKFLYLFWACLLGGMIAVP------------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 196 lsvIFADKPEKAKLLLEGVENKLT-PCLkiivimdsygsdlvergkkcgveIISLKALEDLgrvnrvkpkppePEDLAII 274
Cdd:cd05908 70 ---VSIGSNEEHKLKLNKVWNTLKnPYL-----------------------ITEEEVLCEL------------ADELAFI 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 275 CFTSGTTGNPKGAMITHQNIINDCSGFIKATESafiaSTDDVLISFLPLAHMFETVVecvmlCHGAKIgfFQGDIRLLMd 354
Cdd:cd05908 112 QFSSGSTGDPKGVMLTHENLVHNMFAILNSTEW----KTKDRILSWMPLTHDMGLIA-----FHLAPL--IAGMNQYLM- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 355 dlkvlqPT-IFPVVPRLlnrmfdrifgqantslkrWLLDfASKRKEAELRSGIVRNNSLWDKLIFHKIQSSLGGKVRLMI 433
Cdd:cd05908 180 ------PTrLFIRRPIL------------------WLKK-ASEHKATIVSSPNFGYKYFLKTLKPEKANDWDLSSIRMIL 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 434 TGAAPVSATVLTFLRTALGC------QFYEGYGQTECTAGCCLSLPGD----------------------------WTAG 479
Cdd:cd05908 235 NGAEPIDYELCHEFLDHMSKyglkrnAILPVYGLAEASVGASLPKAQSpfktitlgrrhvthgepepevdkkdsecLTFV 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 480 HVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGkWLPNGTLKIIDRKKH 559
Cdd:cd05908 315 EVGKPIDETDIRICD-EDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIRNGRLVITGREKD 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 560 IFkLAQGEYIAPEKIENiylrseavaqvfvhgeslqaflIAVVVPDVESlpswaQKRGLQGSFEELCRNKDI-----NKA 634
Cdd:cd05908 393 II-FVNGQNVYPHDIER----------------------IAEELEGVEL-----GRVVACGVNNSNTRNEEIfcfieHRK 444
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1039782744 635 ILDDLLKLGKEAGlKPFEQVKGIAVHpELFSIDNGLLTPTLKAKRPELRNYFRS 688
Cdd:cd05908 445 SEDDFYPLGKKIK-KHLNKRGGWQIN-EVLPIRRIPKTTSGKVKRYELAQRYQS 496
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
169-604 |
1.80e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 86.23 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 169 FSYSM---VVVPLYDTLGADAITYIVNKAELSVIFADKpEKAKLLLEGVE----NKLTPCLKIIVIMDSygsDLVERgkk 241
Cdd:PLN03102 82 FAVPMagaVLNPINTRLDATSIAAILRHAKPKILFVDR-SFEPLAREVLHllssEDSNLNLPVIFIHEI---DFPKR--- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 242 cgveiISLKALEDLGRVNRVKPKPP---------EPEDLAIICFTSGTTGNPKGAMITHQniindcsGFIKATESAFIA- 311
Cdd:PLN03102 155 -----PSSEELDYECLIQRGEPTPSlvarmfriqDEHDPISLNYTSGTTADPKGVVISHR-------GAYLSTLSAIIGw 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 312 --STDDVLISFLPLAHmfetvvecvmlCHGAKIGF---FQGDIRLLMDdlKVLQPTIFPVVprllnrmfdRIFGQANTSL 386
Cdd:PLN03102 223 emGTCPVYLWTLPMFH-----------CNGWTFTWgtaARGGTSVCMR--HVTAPEIYKNI---------EMHNVTHMCC 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 387 KRWLLDFaskrkeaelrsgIVRNNSLwdklifhkIQSSLGGKVRLMITGAAPVSATVLTFLRtaLGCQFYEGYGQTECTA 466
Cdd:PLN03102 281 VPTVFNI------------LLKGNSL--------DLSPRSGPVHVLTGGSPPPAALVKKVQR--LGFQVMHAYGLTEATG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 467 GCCL--------SLPGDWTAgHVGAPMPCNYVKL--VDVEEMNYLAS-----KGEGEVCVKGANVFKGYLKDPARTAEAL 531
Cdd:PLN03102 339 PVLFcewqdewnRLPENQQM-ELKARQGVSILGLadVDVKNKETQESvprdgKTMGEIVIKGSSIMKGYLKNPKATSEAF 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039782744 532 dKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIylrseavaqVFVHGESLQAFLIAVVVP 604
Cdd:PLN03102 418 -KHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVENV---------LYKYPKVLETAVVAMPHP 479
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
267-615 |
2.09e-17 |
|
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: 85.30 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 267 EPEDLAIICFTSGTTGNPKGAMITHQNIINDCS------GFIKATESAFIAStddvlISFLPLA-HMFETvvecvmLCHG 339
Cdd:cd17645 102 NPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEwhrpyfGVTPADKSLVYAS-----FSFDASAwEIFPH------LTAG 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 340 AKIGFFQGDIRLLMDDLkvlqptifpvvprllnrmfDRIFGQANTSLKRWLLDFASKRKEAElrsgivrNNSLwdklifh 419
Cdd:cd17645 171 AALHVVPSERRLDLDAL-------------------NDYFNQEGITISFLPTGAAEQFMQLD-------NQSL------- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 420 kiqsslggkvRLMITGAAPVSATVLTflrtalGCQFYEGYGQTECTAgCCLSLPGDWTAGHVGAPMPCNYVKLVDVEEMN 499
Cdd:cd17645 218 ----------RVLLTGGDKLKKIERK------GYKLVNNYGPTENTV-VATSFEIDKPYANIPIGKPIDNTRVYILDEAL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 500 YLASKG-EGEVCVKGANVFKGYLKDPARTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPE 572
Cdd:cd17645 281 QLQPIGvAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPG 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1039782744 573 KIENIYLRSEAVAQVFV-------HGESLQAFLIAVVVPDVESLPSWAQK 615
Cdd:cd17645 360 EIEPFLMNHPLIELAAVlakedadGRKYLVAYVTAPEEIPHEELREWLKN 409
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
169-591 |
5.14e-17 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 84.85 E-value: 5.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 169 FSYSM--------VVVPLYDTLGADAITYIVNKAELSVIFADKpekAKLLLEGVENKLTPCLKIIVIMDSYGSDlveRGK 240
Cdd:cd05970 85 FWYSLlalhklgaIAIPATHQLTAKDIVYRIESADIKMIVAIA---EDNIPEEIEKAAPECPSKPKLVWVGDPV---PEG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 241 KCGVEIISLKALEDLGRvnRVKPKPPEPEDLAIICFTSGTTGNPKgaMITHQNIindcsgfikatesafiastddvlisf 320
Cdd:cd05970 159 WIDFRKLIKNASPDFER--PTANSYPCGEDILLVYFSSGTTGMPK--MVEHDFT-------------------------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 321 LPLAHMFETvvecvMLCHGAKigffQGDIRLLMDDLKVLQPtifpvvprllnrMFDRIFGQANTSLKRWLLDFASKRKEA 400
Cdd:cd05970 209 YPLGHIVTA-----KYWQNVR----EGGLHLTVADTGWGKA------------VWGKIYGQWIAGAAVFVYDYDKFDPKA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 401 ELRSgIVRNN--------SLWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAgCCLSL 472
Cdd:cd05970 268 LLEK-LSKYGvttfcappTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTL-TIATF 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 473 PG-DWTAGHVGAPMPCNYVKLVDVEEMNYLASKgEGEVCVKGAN-----VFKGYLKDPARTAEALdKDGWLHTGDIGKWL 546
Cdd:cd05970 346 PWmEPKPGSMGKPAPGYEIDLIDREGRSCEAGE-EGEIVIRTSKgkpvgLFGGYYKDAEKTAEVW-HDGYYHTGDAAWMD 423
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1039782744 547 PNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:cd05970 424 EDGYLWFVGRTDDLIK-SSGYRIGPFEVESALIQHPAVLECAVTG 467
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
263-605 |
5.76e-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: 84.24 E-value: 5.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 263 PKPPEPEDLAIICFTSGTTGNPKGAMITHQNIINDcsgfIKATESAFIASTDDVLISFLPLAH------MFETvvecvmL 336
Cdd:cd12114 120 PVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNT----ILDINRRFAVGPDDRVLALSSLSFdlsvydIFGA------L 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 337 CHGAKIGFFQGDIR----LLMDDLKVLQPTIFPVVPRLLNrMfdrifgqantslkrwLLDfaskrkeaELRSGIVRNNSL 412
Cdd:cd12114 190 SAGATLVLPDEARRrdpaHWAELIERHGVTLWNSVPALLE-M---------------LLD--------VLEAAQALLPSL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 413 wdKLIFHK---IQSSLGGKVRLMITGAAPVSatvltflrtaLGcqfyegyGQTEctaGCCLS-------LPGDWTAGHVG 482
Cdd:cd12114 246 --RLVLLSgdwIPLDLPARLRALAPDARLIS----------LG-------GATE---ASIWSiyhpideVPPDWRSIPYG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 483 APMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEAL--DKDG--WLHTGDIGKWLPNGTLKIIDRKK 558
Cdd:cd12114 304 RPLANQRYRVLD-PRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFvtHPDGerLYRTGDLGRYRPDGTLEFLGRRD 382
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1039782744 559 HIFKLaQGEYIAPEKIENIYLRSEAVAQ--VFVHGESLQAFLIAVVVPD 605
Cdd:cd12114 383 GQVKV-RGYRIELGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPD 430
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
108-672 |
7.10e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 84.71 E-value: 7.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 108 PCLGSRKPNQ-PYEWISYKEVAELAECIGSGLIQKGFKPCSEQFIglFSQNRPEWVIVEQGCFSYSMVVVPL---YDTLG 183
Cdd:PRK12582 66 PWLAQREPGHgQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMI--LSGNSIEHALMTLAAMQAGVPAAPVspaYSLMS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 184 AD--AITYIVNKAELSVIFADKPEK-----AKLLLEGVEnkltpCLKIIVIMDSYGS----DLVERGKKCGVEiislKAL 252
Cdd:PRK12582 144 HDhaKLKHLFDLVKPRVVFAQSGAPfaralAALDLLDVT-----VVHVTGPGEGIASiafaDLAATPPTAAVA----AAI 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 253 EDLGrvnrvkpkppePEDLAIICFTSGTTGNPKGAMITHQNIindCSGfIKATESAFIASTDD---VLISFLPLAHMFet 329
Cdd:PRK12582 215 AAIT-----------PDTVAKYLFTSGSTGMPKAVINTQRMM---CAN-IAMQEQLRPREPDPpppVSLDWMPWNHTM-- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 330 vvecvmlchGAKIGFfQGDIR----LLMDDLKVLqPTIFPVVPRLLNRMFDRIFGQANTSLKrwLLDFASKRKEAELRSg 405
Cdd:PRK12582 278 ---------GGNANF-NGLLWgggtLYIDDGKPL-PGMFEETIRNLREISPTVYGNVPAGYA--MLAEAMEKDDALRRS- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 406 ivrnnslwdkliFHKiqsslggKVRLMITGAAPVSATVLTFLR----TALGCQ--FYEGYGQTEcTAGccLSLPGDWTA- 478
Cdd:PRK12582 344 ------------FFK-------NLRLMAYGGATLSDDLYERMQalavRTTGHRipFYTGYGATE-TAP--TTTGTHWDTe 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 479 --GHVGAPMPCNYVKLVDVEEmNYlaskgegEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWL----PNGTLK 552
Cdd:PRK12582 402 rvGLIGLPLPGVELKLAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdpddPEKGLI 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 553 IIDRKKHIFKLAQGEYIAPEKieniyLRSEAVA-------QVFVHGESlQAFLIAVVVPDVESLPSWAQKRGlqGSFEEL 625
Cdd:PRK12582 474 FDGRVAEDFKLSTGTWVSVGT-----LRPDAVAacspvihDAVVAGQD-RAFIGLLAWPNPAACRQLAGDPD--AAPEDV 545
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1039782744 626 CRNKDINKAILDDLLKLGKEAGlKPFEQVKGIAVHPELFSIDNGLLT 672
Cdd:PRK12582 546 VKHPAVLAILREGLSAHNAEAG-GSSSRIARALLMTEPPSIDAGEIT 591
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
265-586 |
1.22e-16 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 83.99 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 265 PPEPEDLAIICFTSGTTGNPKGAMITHQNIINDCSGfIKAtesafIA--STDDVLISFLPLAHMFE-TVVECVMLCHGAK 341
Cdd:PRK08043 361 KQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQ-IKT-----IAdfTPNDRFMSALPLFHSFGlTVGLFTPLLTGAE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 342 IGFFQgdirllmddlkvlQPTIFPVVPRLLnrmFDR----IFGQAnTSLKRWL-----LDFAskrkeaelrsgivrnnsl 412
Cdd:PRK08043 435 VFLYP-------------SPLHYRIVPELV---YDRnctvLFGTS-TFLGNYArfanpYDFA------------------ 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 413 wdklifhkiqsslggKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKL 492
Cdd:PRK08043 480 ---------------RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARL 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 493 VDVEEMnylaSKGeGEVCVKGANVFKGYLK--DP-------ARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKL 563
Cdd:PRK08043 545 LSVPGI----EQG-GRLQLKGPNIMNGYLRveKPgvlevptAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKI 619
|
330 340
....*....|....*....|...
gi 1039782744 564 AqGEYIAPEKIENIYLRSEAVAQ 586
Cdd:PRK08043 620 A-GEMVSLEMVEQLALGVSPDKQ 641
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
122-616 |
1.88e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 82.87 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 122 ISYKEVAELAECIGSGLIQKGFkpCSEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIfA 201
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGV--RRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWL-V 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 202 DKPEKAKL----LLEGVENKLTPCLKIIVIMDSYGSDLVERGKKCGVEIISLKALEDLGrvnrVKPKPPEPEDLAIICFT 277
Cdd:PRK06164 113 VWPGFKGIdfaaILAAVPPDALPPLRAIAVVDDAADATPAPAPGARVQLFALPDPAPPA----AAGERAADPDAGALLFT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 278 -SGTTGNPK------GAMITHQNIINDCSGFikatesafiaSTDDVLISFLPL--AHMFETVVecvmlchgakiGFFQGD 348
Cdd:PRK06164 189 tSGTTSGPKlvlhrqATLLRHARAIARAYGY----------DPGAVLLAALPFcgVFGFSTLL-----------GALAGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 349 IRLLMDDLkvlqptiF--PVVPRLL-----------NRMFDRIFGQANTSLkrwllDFASKRkeaelrsgivrnnslwdk 415
Cdd:PRK06164 248 APLVCEPV-------FdaARTARALrrhrvthtfgnDEMLRRILDTAGERA-----DFPSAR------------------ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 416 lifhkiqsslggkvRLMITGAAPVSATVLTFLRTAlGCQFYEGYGQTECTA-GCCLSLPGDWTAGHV--GAPM-PCNYVK 491
Cdd:PRK06164 298 --------------LFGFASFAPALGELAALARAR-GVPLTGLYGSSEVQAlVALQPATDPVSVRIEggGRPAsPEARVR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 492 LVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAP 571
Cdd:PRK06164 363 ARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNP 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1039782744 572 EKIENIYLRSEAVAQVFVHGESLQ------AFLIAV--VVPDVESLPSWAQKR 616
Cdd:PRK06164 442 AEIEHALEALPGVAAAQVVGATRDgktvpvAFVIPTdgASPDEAGLMAACREA 494
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
267-616 |
2.74e-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: 81.92 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 267 EPEDLAIICFTSGTTGNPKGAMITHQNIINdcsgFIKATESAFIASTDDVLISFLPLAhmFETVV-ECVM-LCHGAkigf 344
Cdd:cd17652 91 TPDNLAYVIYTSGSTGRPKGVVVTHRGLAN----LAAAQIAAFDVGPGSRVLQFASPS--FDASVwELLMaLLAGA---- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 345 fqgdiRLLMDDLKVLQPtifpvvprllnrmfdrifGQAntslkrwLLDFaskrkeaelrsgivrnnsLWDKLIFHKIQS- 423
Cdd:cd17652 161 -----TLVLAPAEELLP------------------GEP-------LADL------------------LREHRITHVTLPp 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 424 ---------SLGGKVRLMITGAAPVSATVLtflRTALGCQFYEGYGQTECTAGCCLSLP-GDWTAGHVGAPMPCNYVKLV 493
Cdd:cd17652 193 aalaalppdDLPDLRTLVVAGEACPAELVD---RWAPGRRMINAYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYVL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 494 DvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQG 566
Cdd:cd17652 270 D-ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKI-RG 347
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1039782744 567 EYIAPEKIENIYLRSEAVAQ--VFVHGESL-QAFLIAVVVPDVESLPSWAQKR 616
Cdd:cd17652 348 FRIELGEVEAALTEHPGVAEavVVVRDDRPgDKRLVAYVVPAPGAAPTAAELR 400
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
270-600 |
3.28e-16 |
|
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: 81.99 E-value: 3.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 270 DLAIICFTSGTTGNPKGAMITHqniiNDCSGFIKATESAFIASTDDVLISFLPLAHMFetVVEC-----VMLChGAKIGF 344
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTH----NDYAYNVRASAEVCGLDQDTVYLAVLPAAHNF--PLACpgvlgTLLA-GGRVVL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 345 FQ----GDIRLLMDDLKVlqpTIFPVVPRLLnrmfdrifgqantslKRWLlDFASKRKEAElrsgivrnnslwdklifhk 420
Cdd:cd05920 213 APdpspDAAFPLIEREGV---TVTALVPALV---------------SLWL-DAAASRRADL------------------- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 421 iqSSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTE----CTAgccLSLPGDWTAGHVGAPM-PCNYVKLVDv 495
Cdd:cd05920 255 --SSL----RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEgllnYTR---LDDPDEVIIHTQGRPMsPDDEIRVVD- 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 496 EEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIE 575
Cdd:cd05920 325 EEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVE 403
|
330 340 350
....*....|....*....|....*....|..
gi 1039782744 576 NIYLRSEAVAQVFV-------HGESLQAFLIA 600
Cdd:cd05920 404 NLLLRHPAVHDAAVvampdelLGERSCAFVVL 435
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
122-605 |
3.82e-16 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 81.59 E-value: 3.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 122 ISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVGP--ESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 202 DkpekaklllegvenkltpclkiivimdsygsdlvergkkcgveiislkaledlgrvnrvkpkppePEDLAIICFTSGTT 281
Cdd:cd12115 103 D-----------------------------------------------------------------PDDLAYVIYTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 282 GNPKGAMITHQNIINdcsgFIKATESAF--------IASTDdvlISF-LPLAHMFETvvecvmLCHGAKIgffqgdirLL 352
Cdd:cd12115 118 GRPKGVAIEHRNAAA----FLQWAAAAFsaeelagvLASTS---ICFdLSVFELFGP------LATGGKV--------VL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 353 MDDlkVLQPTIFPVVPR--LLNRMfdrifgqanTSLKRWLLDfaskrkeaelrsgivrnnslwdklifhkiQSSLGGKVR 430
Cdd:cd12115 177 ADN--VLALPDLPAAAEvtLINTV---------PSAAAELLR-----------------------------HDALPASVR 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 431 LMITGAAPVSATVLTFLRTAL-GCQFYEGYGQTECT--AGCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKGEG 507
Cdd:cd12115 217 VVNLAGEPLPRDLVQRLYARLqVERVVNLYGPSEDTtySTVAPVPPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVPG 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 508 EVCVKGANVFKGYLKDPARTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRS 581
Cdd:cd12115 296 ELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAALRSI 374
|
490 500
....*....|....*....|....*..
gi 1039782744 582 EAVAQ--VFVHGESL-QAFLIAVVVPD 605
Cdd:cd12115 375 PGVREavVVAIGDAAgERRLVAYIVAE 401
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
216-607 |
3.91e-16 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 81.46 E-value: 3.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 216 NKLTPCLKIIVIMDSYGSDLVergkkcgveiiSLKALEDLGRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNII 295
Cdd:PRK09029 93 EELLPSLTLDFALVLEGENTF-----------SALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 296 NDCSGFIKATesAFIAStDDVLISfLPLAHmfetvvecV--------MLCHGAKIGFfqGDIRLLMDDLkvLQPTIFPVV 367
Cdd:PRK09029 162 ASAEGVLSLM--PFTAQ-DSWLLS-LPLFH--------VsgqgivwrWLYAGATLVV--RDKQPLEQAL--AGCTHASLV 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 368 PRLLNRMFDRifGQANTSLKRWLLdfaskrkeaelrsgivrnnslwdklifhkiqsslGGKvrlMItgaapvsATVLTFL 447
Cdd:PRK09029 226 PTQLWRLLDN--RSEPLSLKAVLL----------------------------------GGA---AI-------PVELTEQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 448 RTALGCQFYEGYGQTECTAGCCL----SLPGdwtaghVGAPMPCNYVKLVDveemnylaskgeGEVCVKGANVFKGYLKD 523
Cdd:PRK09029 260 AEQQGIRCWCGYGLTEMASTVCAkradGLAG------VGSPLPGREVKLVD------------GEIWLRGASLALGYWRQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 524 PARTAeALDKDGWLHTGDIGKWLpNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVhgeslqafliaVVV 603
Cdd:PRK09029 322 GQLVP-LVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQVFV-----------VPV 387
|
....
gi 1039782744 604 PDVE 607
Cdd:PRK09029 388 ADAE 391
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
266-617 |
4.88e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 82.90 E-value: 4.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 266 PEPEDLAIICFTSGTTGNPKGAMITHQNIINdcsgFIKATESAFIASTDDVLISFLPLAhmFETVVECVM--LCHGAKIG 343
Cdd:PRK12467 1715 LAPQNLAYVIYTSGSTGRPKGAGNRHGALVN----RLCATQEAYQLSAADVVLQFTSFA--FDVSVWELFwpLINGARLV 1788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 344 FFQGDIRL----LMDDLKVLQPTIFPVVPRLLNRMFDRIFGQAN-TSLKRwlldfaskrkeaelrsgIVrnnslwdklif 418
Cdd:PRK12467 1789 IAPPGAHRdpeqLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHpLSLRR-----------------VV----------- 1840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 419 hkiqssLGGKvrlmitgAAPVSATVLTFLRtaLG-CQFYEGYGQTECTAG-----CCLSLPGDWTAGHVGAPMPCNYVKL 492
Cdd:PRK12467 1841 ------CGGE-------ALEVEALRPWLER--LPdTGLFNLYGPTETAVDvthwtCRRKDLEGRDSVPIGQPIANLSTYI 1905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 493 VDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEAL------DKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQ 565
Cdd:PRK12467 1906 LD-ASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgTVGSRLYrTGDLARYRADGVIEYLGRIDHQVKI-R 1983
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1039782744 566 GEYIAPEKIENIYLRSEAVAQ--VFVHGESLQAFLIAVVVPDVESLPSWAQKRG 617
Cdd:PRK12467 1984 GFRIELGEIEARLREQGGVREavVIAQDGANGKQLVAYVVPTDPGLVDDDEAQV 2037
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
122-605 |
6.95e-16 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 80.78 E-value: 6.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 122 ISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:cd17646 24 LTYRELDERANRLAHLLRARGVGP--EDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 202 DkpekaklllegvenkltpclkiivimdsygSDLVERGKKcGVEIISLKALEDLGRVNRVKPKPPEPEDLAIICFTSGTT 281
Cdd:cd17646 102 T------------------------------ADLAARLPA-GGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGST 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 282 GNPKGAMITHQNIINDCSGFIkatESAFIASTDDVL--------IS----FLPLAHMfETVVECVMLCHGaKIGFFQGdi 349
Cdd:cd17646 151 GRPKGVMVTHAGIVNRLLWMQ---DEYPLGPGDRVLqktplsfdVSvwelFWPLVAG-ARLVVARPGGHR-DPAYLAA-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 350 rlLMDDLKVlqpTIFPVVPRLLnrmfdRIFGQantslkrwlldfaskrkeaELRSGivRNNSLwdklifhkiqsslggkv 429
Cdd:cd17646 224 --LIREHGV---TTCHFVPSML-----RVFLA-------------------EPAAG--SCASL----------------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 430 RLMITGAAPVSATVLTFLRTALGCQFYEGYGQTEC----TAGCClslPGDWTAGHV--GAPMPCNYVKLVDvEEMNYLAS 503
Cdd:cd17646 256 RRVFCSGEALPPELAARFLALPGAELHNLYGPTEAaidvTHWPV---RGPAETPSVpiGRPVPNTRLYVLD-DALRPVPV 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 504 KGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLH------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 577
Cdd:cd17646 332 GVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKI-RGFRVEPGEIEAA 410
|
490 500 510
....*....|....*....|....*....|.
gi 1039782744 578 YLRSEAVAQVFV---HGESLQAFLIAVVVPD 605
Cdd:cd17646 411 LAAHPAVTHAVVvarAAPAGAARLVGYVVPA 441
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
436-614 |
7.08e-16 |
|
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: 79.27 E-value: 7.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 436 AAPVSATVLTFLRTALGCQFYeGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASkGE-GEVCVKGA 514
Cdd:cd17636 121 AAPEWNDMATVDTSPWGRKPG-GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILD-EDGREVPD-GEvGEIVARGP 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 515 NVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQVFVHGesl 594
Cdd:cd17636 198 TVMAGYWNRPEVNARRT-RGGWHHTNDLGRREPDGSLSFVGPKTRMIKSG-AENIYPAEVERCLRQHPAVADAAVIG--- 272
|
170 180
....*....|....*....|
gi 1039782744 595 qafliavvVPDveslPSWAQ 614
Cdd:cd17636 273 --------VPD----PRWAQ 280
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
174-591 |
1.54e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 79.93 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 174 VVVPLYDTLGADAITYIVNKAelsvifadkpeKAKLLLEGVENKLTPCLKI-IVIMDSYGSDLVERGKKCGVEIISLKal 252
Cdd:PRK06145 78 VFLPINYRLAADEVAYILGDA-----------GAKLLLVDEEFDAIVALETpKIVIDAAAQADSRRLAQGGLEIPPQA-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 253 edlgrvnrvkpkPPEPEDLAIICFTSGTTGNPKGAMITHQNIindcsgFIKATES--AFIASTDDVLISFLPLAHmfetV 330
Cdd:PRK06145 145 ------------AVAPTDLVRLMYTSGTTDRPKGVMHSYGNL------HWKSIDHviALGLTASERLLVVGPLYH----V 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 331 VEC-----VMLCHGAKIGFFQG-DIRLLMDDLKVLQPTIFPVVPRLLNRMF-----DRIfgqaNTSLKRWLLDFASKRKE 399
Cdd:PRK06145 203 GAFdlpgiAVLWVGGTLRIHREfDPEAVLAAIERHRLTCAWMAPVMLSRVLtvpdrDRF----DLDSLAWCIGGGEKTPE 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 400 AELRSgivrnnslwdklifhkiqsslggkvrlmitgaapvsatvltFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTA- 478
Cdd:PRK06145 279 SRIRD-----------------------------------------FTRVFTRARYIDAYGLTETCSGDTLMEAGREIEk 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 479 -GHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRK 557
Cdd:PRK06145 318 iGSTGRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRK 395
|
410 420 430
....*....|....*....|....*....|....
gi 1039782744 558 KHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:PRK06145 396 KDMI-ISGGENIASSEVERVIYELPEVAEAAVIG 428
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
155-612 |
2.84e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 79.31 E-value: 2.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 155 SQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIF--ADKPEKAKLLLEGvenklTPCLK-IIVIMDSY 231
Cdd:PRK07470 64 SRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMIchADFPEHAAAVRAA-----SPDLThVVAIGGAR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 232 GSDLVErgkkcgvEIISlkalEDLGRvnRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQN----IINDCSGFIKATes 307
Cdd:PRK07470 139 AGLDYE-------ALVA----RHLGA--RVANAAVDHDDPCWFFFTSGTTGRPKAAVLTHGQmafvITNHLADLMPGT-- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 308 afiaSTDDVLISFLPLAHMfETVVECVMLCHGAKigffqgDIRLLMDDLKVlqPTIFPVVPRL-LNRMFdrifgQANTSL 386
Cdd:PRK07470 204 ----TEQDASLVVAPLSHG-AGIHQLCQVARGAA------TVLLPSERFDP--AEVWALVERHrVTNLF-----TVPTIL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 387 KRWLLDFASKRKEaelrsgivrnnslwdklifhkiQSSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTa 466
Cdd:PRK07470 266 KMLVEHPAVDRYD----------------------HSSL----RYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVT- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 467 GCCLSLP------GDWTAGHVGapmPCNY------VKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALdKD 534
Cdd:PRK07470 319 GNITVLPpalhdaEDGPDARIG---TCGFertgmeVQIQD-DEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RD 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039782744 535 GWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHGeslqafliavvVPDveslPSW 612
Cdd:PRK07470 394 GWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPREIEEKLLTHPAVSEVAVLG-----------VPD----PVW 455
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
267-577 |
3.79e-15 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 78.70 E-value: 3.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 267 EPEDLAIICFTSGTTGNPKGAMITHQNIINDcsgfIKATESAFIASTDDVLISFLPLAHMFetvvecvmlchgakiGFFQ 346
Cdd:PRK06334 181 DPEDVAVILFTSGTEKLPKGVPLTHANLLAN----QRACLKFFSPKEDDVMMSFLPPFHAY---------------GFNS 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 347 GDIRLLMDDLkvlqPTIF---PVVPRLLNRMFDR----IFGQANTSLKRWLLdfASKRKEAELRS-------GIVRNNSL 412
Cdd:PRK06334 242 CTLFPLLSGV----PVVFaynPLYPKKIVEMIDEakvtFLGSTPVFFDYILK--TAKKQESCLPSlrfvvigGDAFKDSL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 413 WDKlifhkiqsslggkvrlmitgaapvsaTVLTFLRTALgcqfYEGYGQTECTAgcCLSLPGDWTAGH---VGAPMPCNY 489
Cdd:PRK06334 316 YQE--------------------------ALKTFPHIQL----RQGYGTTECSP--VITINTVNSPKHescVGMPIRGMD 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 490 VKLVDvEEMNYLASKGE-GEVCVKGANVFKGYL-KDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGE 567
Cdd:PRK06334 364 VLIVS-EETKVPVSSGEtGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AE 441
|
330
....*....|
gi 1039782744 568 YIAPEKIENI 577
Cdd:PRK06334 442 MVSLEALESI 451
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
264-629 |
2.55e-14 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 76.42 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 264 KPPEPEDLAI-ICFTSGTTGNPKGAMITHQniindcSGFIKATESAFIASTDD--VLISFLPLAHmfetvveCVMLCHGA 340
Cdd:PLN02479 189 KPPADEWQSIaLGYTSGTTASPKGVVLHHR------GAYLMALSNALIWGMNEgaVYLWTLPMFH-------CNGWCFTW 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 341 KIGFFQG-DIRLLMDDLKVLQPTI-------FPVVPRLLNRMFDrifgqantslkrwlldfaSKRKEAELrsgivrnnsl 412
Cdd:PLN02479 256 TLAALCGtNICLRQVTAKAIYSAIanygvthFCAAPVVLNTIVN------------------APKSETIL---------- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 413 wdklifhkiqsSLGGKVRLMITGAAPvSATVLtFLRTALGCQFYEGYGQTEcTAG----CCL-----SLPGDwTAGHVGA 483
Cdd:PLN02479 308 -----------PLPRVVHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSE-TYGpstvCAWkpewdSLPPE-EQARLNA 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 484 PMPCNYVKL-----VDVEEMNYLASKGE--GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDR 556
Cdd:PLN02479 373 RQGVRYIGLegldvVDTKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDR 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 557 KKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFV-------HGESLQAFLiaVVVPDVESlpswAQKRGLQGSFEELCRNK 629
Cdd:PLN02479 452 SKDII-ISGGENISSLEVENVVYTHPAVLEASVvarpderWGESPCAFV--TLKPGVDK----SDEAALAEDIMKFCRER 524
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
111-608 |
2.92e-14 |
|
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: 75.97 E-value: 2.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 111 GSRKPNQPYEWI---------SYKEVAELAECIGSGLIQkgfkPCSEQ---FIGLFSQNRPEWVIVEQGCFSYSMVVVPL 178
Cdd:cd05928 22 GKRPPNPALWWVngkgdevkwSFRELGSLSRKAANVLSG----ACGLQrgdRVAVILPRVPEWWLVNVACIRTGLVFIPG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 179 YDTLGADAITYIVNKAELSVIFADkpEKAKLLLEGVENKlTPCLKIIVIMDSYGSDlvergkkcgvEIISLKALedLGRV 258
Cdd:cd05928 98 TIQLTAKDILYRLQASKAKCIVTS--DELAPEVDSVASE-CPSLKTKLLVSEKSRD----------GWLNFKEL--LNEA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 259 ----NRVKPKPPEPedlAIICFTSGTTGNPKGAMITHQNI---INDCSGFIKA-TESAFIASTDDVLISFLPLAHMFETV 330
Cdd:cd05928 163 stehHCVETGSQEP---MAIYFTSGTTGSPKMAEHSHSSLglgLKVNGRYWLDlTASDIMWNTSDTGWIKSAWSSLFEPW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 331 VE--CVMLCHGAKIgffqgDIRLLMDDLKVLQPTIFPVVPRLLnrmfdRIFGQAntslkrwllDFASkrkeaelrsgivr 408
Cdd:cd05928 240 IQgaCVFVHHLPRF-----DPLVILKTLSSYPITTFCGAPTVY-----RMLVQQ---------DLSS------------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 409 nnslwdklifHKIQSslggkVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCN 488
Cdd:cd05928 288 ----------YKFPS-----LQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPY 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 489 YVKLVDvEEMNYLASKGEGEVCV-----KGANVFKGYLKDPARTAEALDKDGWLhTGDIGKWLPNGTLKIIDRKKHIFkL 563
Cdd:cd05928 353 DVQIID-DNGNVLPPGTEGDIGIrvkpiRPFGLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-N 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1039782744 564 AQGEYIAPEKIENIYLRSEAVAQVFV-------HGESLQAFLiaVVVPDVES 608
Cdd:cd05928 430 SSGYRIGPFEVESALIEHPAVVESAVvsspdpiRGEVVKAFV--VLAPQFLS 479
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
267-610 |
7.29e-14 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 74.36 E-value: 7.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 267 EPEDLAIICFTSGTTGNPKGAMITHQNIINDCSGFIkatESAFIASTDDVLISFLPlAHMFETVVE--CVMLCHGAKIGF 344
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLS---ERYFGRDNGDEAVLFFS-NYVFDFFVEqmTLALLNGQKLVV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 345 FQGDIRL-------LMDDLKVlqpTIFPVVPRLLNRM-FDRIfgqanTSLKRWLL---DFASKRkeaelrsgivrnnslw 413
Cdd:cd17648 168 PPDEMRFdpdrfyaYINREKV---TYLSGTPSVLQQYdLARL-----PHLKRVDAageEFTAPV---------------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 414 dkliFHKIQSSLGGkvrLMITGAAPVSATVLTFLRtalgcqFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVklv 493
Cdd:cd17648 224 ----FEKLRSRFAG---LIINAYGPTETTVTNHKR------FFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAV--- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 494 dveemnylaskgeGEVCVKGANVFKGYLKDPARTAE-------------ALDKDGWLH-TGDIGKWLPNGTLKIIDRKKH 559
Cdd:cd17648 288 -------------GELYLGGDGVARGYLNRPELTAErflpnpfqteqerARGRNARLYkTGDLVRWLPSGELEYLGRNDF 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039782744 560 IFKLaQGEYIAPEKIENIYLRSEAVAQVFV--------HGESLQAFLIAVVVPDVESLP 610
Cdd:cd17648 355 QVKI-RGQRIEPGEVEAALASYPGVRECAVvakedasqAQSRIQKYLVGYYLPEPGHVP 412
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
421-589 |
7.37e-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: 74.14 E-value: 7.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 421 IQSSLGG---KVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSlPGD-WTAGHVGAPMPCNYVKLVDVE 496
Cdd:cd05974 191 IQQDLASfdvKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNS-PGQpVKAGSMGRPLPGYRVALLDPD 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 497 EmnylASKGEGEVCV-----KGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAP 571
Cdd:cd05974 270 G----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SSDYRISP 343
|
170
....*....|....*...
gi 1039782744 572 EKIENIYLRSEAVAQVFV 589
Cdd:cd05974 344 FELESVLIEHPAVAEAAV 361
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
268-627 |
1.11e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 75.38 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 268 PEDLAIICFTSGTTGNPKGAMITHQNIINdcsgFIKATESAFIASTDDVLISFLPLAhmFETVVECVM--LCHGAkigff 345
Cdd:PRK12316 4693 PDNLAYVIYTSGSTGRPKGVAVSHGSLVN----HLHATGERYELTPDDRVLQFMSFS--FDGSHEGLYhpLINGA----- 4761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 346 qgdiRLLMDDLKVLQPTifpvvpRLLNRMFDR--IFGQANTSLKRWLLDFASKRKE-AELRSGIVRNNSLwdklifhkiq 422
Cdd:PRK12316 4762 ----SVVIRDDSLWDPE------RLYAEIHEHrvTVLVFPPVYLQQLAEHAERDGEpPSLRVYCFGGEAV---------- 4821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 423 ssLGGKVRLMITGAAPVSatvltflrtalgcqFYEGYGQTECTAG-CCLSLPGDWTAG----HVGAPMPCNYVKLVDVeE 497
Cdd:PRK12316 4822 --AQASYDLAWRALKPVY--------------LFNGYGPTETTVTvLLWKARDGDACGaaymPIGTPLGNRSGYVLDG-Q 4884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 498 MNYLASKGEGEVCVKGANVFKGYLKDPARTAE-----ALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIA 570
Cdd:PRK12316 4885 LNPLPVGVAGELYLGGEGVARGYLERPALTAErfvpdPFGAPGgrLYRTGDLARYRADGVIDYLGRVDHQVKI-RGFRIE 4963
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 571 PEKIENIYLRSEAVAQVFVHGE--SLQAFLIAVVVPDVESL-PSWAQKRGLQGSFEELCR 627
Cdd:PRK12316 4964 LGEIEARLREHPAVREAVVIAQegAVGKQLVGYVVPQDPALaDADEAQAELRDELKAALR 5023
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
151-607 |
2.96e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 72.79 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 151 IGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFADKPEKAklLLEGVEnkltPCLKIIVIMDS 230
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAE--LLDGLD----PGVRVINVDSP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 231 YGSDLvergkkcgveiisLKALEDlgrvNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIINdcSGFIKATEsaFI 310
Cdd:PRK07867 131 AWADE-------------LAAHRD----AEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVAS--AGVMLAQR--FG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 311 ASTDDVLISFLPLAHMFETVVE-CVMLCHGAKI---------GFfqgdirllMDDLKVLQPTIFPVVPRLLNrmfdrifg 380
Cdd:PRK07867 190 LGPDDVCYVSMPLFHSNAVMAGwAVALAAGASIalrrkfsasGF--------LPDVRRYGATYANYVGKPLS-------- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 381 qantslkrWLLDFASKRKEAElrsgivrnNSLwdklifhkiqsslggkvRLMI-TGAAPVSatVLTFLRTaLGCQFYEGY 459
Cdd:PRK07867 254 --------YVLATPERPDDAD--------NPL-----------------RIVYgNEGAPGD--IARFARR-FGCVVVDGF 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 460 GQTEctAGCCLSLPGDWTAGHVGAPMPCnyVKLVDVE--------------EMNYLASKGEgEVCVKGANVFKGYLKDPA 525
Cdd:PRK07867 298 GSTE--GGVAITRTPDTPPGALGPLPPG--VAIVDPDtgtecppaedadgrLLNADEAIGE-LVNTAGPGGFEGYYNDPE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 526 RTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFVHGeslqafliavvVPD 605
Cdd:PRK07867 373 ADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPIERILLRYPDATEVAVYA-----------VPD 439
|
..
gi 1039782744 606 VE 607
Cdd:PRK07867 440 PV 441
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
108-619 |
1.03e-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: 70.58 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 108 PCLGSrkpnqPYEWISYKEVAELAECIGSGLIQKGFKPCSEQfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAI 187
Cdd:cd05958 2 TCLRS-----PEREWTYRDLLALANRIANVLVGELGIVPGNR-VLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 188 TYIVNKAELSVIFADKPEKAKlllegvenkltpclkiivimdsygsdlvergkkcgveiislkaledlgrvnrvkpkppe 267
Cdd:cd05958 76 AYILDKARITVALCAHALTAS----------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 268 pEDLAIICFTSGTTGNPKGAMITHQNIINDCSGF----IKATEsafiastDDVLISFLPLAHMFET-VVECVMLCHGAKI 342
Cdd:cd05958 97 -DDICILAFTSGTTGAPKATMHFHRDPLASADRYavnvLRLRE-------DDRFVGSPPLAFTFGLgGVLLFPFGVGASG 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 343 GFFQGDI-RLLMDDLKVLQPTIFPVVPRLLNRMFdrifgqantslkrwlldfASKRKEAELRSGivrnnslwdklifhki 421
Cdd:cd05958 169 VLLEEATpDLLLSAIARYKPTVLFTAPTAYRAML------------------AHPDAAGPDLSS---------------- 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 422 qsslggkVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYL 501
Cdd:cd05958 215 -------LRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD-DEGNPV 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 502 ASKGEGEVCVKGANVFKgYLKDPARTAEAldKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRS 581
Cdd:cd05958 287 PDGTIGRLAVRGPTGCR-YLADKRQRTYV--QGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQH 362
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1039782744 582 EAVAQVFVHGESLQAFLI---AVVVPDVESLPSWAQKRGLQ 619
Cdd:cd05958 363 PAVAECAVVGHPDESRGVvvkAFVVLRPGVIPGPVLARELQ 403
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
182-591 |
1.92e-12 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 70.17 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 182 LGADAITYIVNKAELSVIFADK---PekaklLLEGVENKLtPCLKIIVImdsygsdLVERGKKCGVEIISLKALEDL--G 256
Cdd:PRK06018 98 LFPEQIAWIINHAEDRVVITDLtfvP-----ILEKIADKL-PSVERYVV-------LTDAAHMPQTTLKNAVAYEEWiaE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 257 RVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQ-NIINdcsGFIKATESAFIASTDDVLISFLPLAH-------MFE 328
Cdd:PRK06018 165 ADGDFAWKTFDENTAAGMCYTSGTTGDPKGVLYSHRsNVLH---ALMANNGDALGTSAADTMLPVVPLFHanswgiaFSA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 329 TVVECVMLCHGAKIGffQGDIRLLMDDLKVlqpTIFPVVPRLlnrmfdrifgqantslkrWLLDFASKRKEAElrsgivr 408
Cdd:PRK06018 242 PSMGTKLVMPGAKLD--GASVYELLDTEKV---TFTAGVPTV------------------WLMLLQYMEKEGL------- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 409 nnslwdKLIFHKiqsslggkvRLMITGAAPVSATVLTFLRtaLGCQFYEGYGQTECTAGCCLS--------LPGDWTAGH 480
Cdd:PRK06018 292 ------KLPHLK---------MVVCGGSAMPRSMIKAFED--MGVEVRHAWGMTEMSPLGTLAalkppfskLPGDARLDV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 481 V---GAPMPCNYVKLVDvEEMNYLASKGE--GEVCVKGANVFKGYLKDparTAEALDKDGWLHTGDIGKWLPNGTLKIID 555
Cdd:PRK06018 355 LqkqGYPPFGVEMKITD-DAGKELPWDGKtfGRLKVRGPAVAAAYYRV---DGEILDDDGFFDTGDVATIDAYGYMRITD 430
|
410 420 430
....*....|....*....|....*....|....*.
gi 1039782744 556 RKKHIFKlAQGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:PRK06018 431 RSKDVIK-SGGEWISSIDLENLAVGHPKVAEAAVIG 465
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
456-604 |
3.29e-12 |
|
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: 69.33 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 456 YEGYGQTECTAGCCLSlPGDWTA--GHVGAPMPCNyVKLVDvEEMNYLASKGEGEVCVKGANVFKgYLKDPARTAEALDK 533
Cdd:cd05929 273 WEYYGGTEGQGLTIIN-GEEWLThpGSVGRAVLGK-VHILD-EDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNE 348
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039782744 534 DGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHG---ESLQAFLIAVVVP 604
Cdd:cd05929 349 GGWSTLGDVGYLDEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIAHPKVLDAAVVGvpdEELGQRVHAVVQP 421
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
250-576 |
7.34e-12 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 68.39 E-value: 7.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 250 KALEDLGRVNRVKPKPP---EPEDLAIICFTSGTTGNPKGAMITHQNiindcsgF---IKATESAFIASTDDVLISFLPL 323
Cdd:PRK09274 152 TTLATLLRDGAAAPFPMadlAPDDMAAILFTSGSTGTPKGVVYTHGM-------FeaqIEALREDYGIEPGEIDLPTFPL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 324 AHMFE------TVVECvmlchgakigffqgdirllMDDLKVLQptifpVVPRllnRMFDRIFGQANTSLkrwlldFASKr 397
Cdd:PRK09274 225 FALFGpalgmtSVIPD-------------------MDPTRPAT-----VDPA---KLFAAIERYGVTNL------FGSP- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 398 keaelrsgivrnnSLWDKLIFHKIQS--SLGGkVRLMITGAAPVSATVLTFLRTAL--GCQFYEGYGQTEC------TAG 467
Cdd:PRK09274 271 -------------ALLERLGRYGEANgiKLPS-LRRVISAGAPVPIAVIERFRAMLppDAEILTPYGATEAlpissiESR 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 468 CCLSLPGDWT---AGH-VGAPMPCNYVKLVDV--------EEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEA--LDK 533
Cdd:PRK09274 337 EILFATRAATdngAGIcVGRPVDGVEVRIIAIsdapipewDDALRLATGEIGEIVVAGPMVTRSYYNRPEATRLAkiPDG 416
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1039782744 534 DG--WLHTGDIGkWL-PNGTLKIIDRKKHIFKLAQGEY--IAPEKIEN 576
Cdd:PRK09274 417 QGdvWHRMGDLG-YLdAQGRLWFCGRKAHRVETAGGTLytIPCERIFN 463
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
267-607 |
1.45e-11 |
|
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: 67.11 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 267 EPEDLAIICFTSGTTGNPKGAMITHQNIINdcsgFIKAT-ESAFIASTDDVL----ISFLPLAH-MFETvvecvmLCHGA 340
Cdd:cd17656 126 NSDDLLYIIYTSGTTGKPKGVQLEHKNMVN----LLHFErEKTNINFSDKVLqfatCSFDVCYQeIFST------LLSGG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 341 KIGFFQGDIRLLMDDLKVL------QPTIFPVVprLLNRMFdrifgqantSLKRWLLDFASKRKEAeLRSG--IVRNNSL 412
Cdd:cd17656 196 TLYIIREETKRDVEQLFDLvkrhniEVVFLPVA--FLKFIF---------SEREFINRFPTCVKHI-ITAGeqLVITNEF 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 413 WDKLIFHkiqsslggkvrlmitgaapvsatvltflrtalGCQFYEGYG--QTECTAGCCLSLPGDWTA-GHVGAPMPCNY 489
Cdd:cd17656 264 KEMLHEH--------------------------------NVHLHNHYGpsETHVVTTYTINPEAEIPElPPIGKPISNTW 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 490 VKLVDVEEMnyLASKGE-GEVCVKGANVFKGYLKDPARTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFK 562
Cdd:cd17656 312 IYILDQEQQ--LQPQGIvGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVK 389
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1039782744 563 LaQGEYIAPEKIENIYLRSEAVAQ--VFVHGESL-QAFLIAVVVPDVE 607
Cdd:cd17656 390 I-RGYRIELGEIEAQLLNHPGVSEavVLDKADDKgEKYLCAYFVMEQE 436
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
270-607 |
2.40e-11 |
|
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: 66.61 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 270 DLAIICFTSGTTGNPKGAMITHQNIINDCSGFikatESAFIASTDDVLISFLPLAHMFE-TVVECVMLCHGAKIGF---F 345
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFF----AGSGGALPSDVLYTCLPLYHSTAlIVGWSACLASGATLVIrkkF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 346 QGdiRLLMDDLKVLQPTIFPVVPRLLnrmfdrifgqantslkRWLLdfASKRKEAELRsgivrnnslwdklifHKIQSSL 425
Cdd:cd05940 158 SA--SNFWDDIRKYQATIFQYIGELC----------------RYLL--NQPPKPTERK---------------HKVRMIF 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 426 GGKVRLMITGaapvsatvlTFL-RTALGcQFYEGYGQTECTAGcCLSLPG-DWTAGHVGA----PMPCNYVKlVDVEEMN 499
Cdd:cd05940 203 GNGLRPDIWE---------EFKeRFGVP-RIAEFYAATEGNSG-FINFFGkPGAIGRNPSllrkVAPLALVK-YDLESGE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 500 YL---------ASKGEGEVCVKGAN---VFKGYLkDPARTAEAL------DKDGWLHTGDIGKWLPNGTLKIIDRKKHIF 561
Cdd:cd05940 271 PIrdaegrcikVPRGEPGLLISRINplePFDGYT-DPAATEKKIlrdvfkKGDAWFNTGDLMRLDGEGFWYFVDRLGDTF 349
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1039782744 562 KLaQGEYIAPEKIENIYLRSEAVAQVFVHGeslqafliaVVVPDVE 607
Cdd:cd05940 350 RW-KGENVSTTEVAAVLGAFPGVEEANVYG---------VQVPGTD 385
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
430-600 |
4.52e-11 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 65.78 E-value: 4.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 430 RLMITGAAPVSATVLTFLRTALGCQFYEGYGQTE----CTAgccLSLPGDWTAGHVGAPM-PCNYVKLVDvEEMNYLASK 504
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAEglvnYTR---LDDSDERIFTTQGRPMsPDDEVWVAD-ADGNPLPQG 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 505 GEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHifklaQ----GEYIAPEKIENIYLR 580
Cdd:PRK10946 379 EVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGEKIAAEEIENLLLR 453
|
170 180
....*....|....*....|....*..
gi 1039782744 581 SEAVAQVF-------VHGESLQAFLIA 600
Cdd:PRK10946 454 HPAVIHAAlvsmedeLMGEKSCAFLVV 480
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
185-585 |
1.00e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 64.73 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 185 DAITYIVNKAELSVIFAD---KPekaklLLEGVENKLTPCLKIIVIMDSygsdlvergKKCGVEIISLKALEDL-GRVNR 260
Cdd:PRK07008 101 EQIAYIVNHAEDRYVLFDltfLP-----LVDALAPQCPNVKGWVAMTDA---------AHLPAGSTPLLCYETLvGAQDG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 261 VKPKPPEPEDLAI-ICFTSGTTGNPKGAMITHQNIIndCSGFIKATESAFIASTDDVLisfLPLAHMFEtvVECVMLCH- 338
Cdd:PRK07008 167 DYDWPRFDENQASsLCYTSGTTGNPKGALYSHRSTV--LHAYGAALPDAMGLSARDAV---LPVVPMFH--VNAWGLPYs 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 339 ----GAKIgFFQG------DIRLLMDDLKVLQPTIFPVV-PRLLNRMfdrifgqantslkrwlldfaskrKEAELRSGIV 407
Cdd:PRK07008 240 apltGAKL-VLPGpdldgkSLYELIEAERVTFSAGVPTVwLGLLNHM-----------------------REAGLRFSTL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 408 RnnslwdklifhkiqsslggkvRLMITGAAPVSATVLTFlRTALGCQFYEGYGQTE-------CT-AGCCLSLPGD---- 475
Cdd:PRK07008 296 R---------------------RTVIGGSACPPAMIRTF-EDEYGVEVIHAWGMTEmsplgtlCKlKWKHSQLPLDeqrk 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 476 --WTAGHV--GAPMpcnyvKLVDVE--EMNYlASKGEGEVCVKGANVFKGYLKdpaRTAEALDkDGWLHTGDIGKWLPNG 549
Cdd:PRK07008 354 llEKQGRViyGVDM-----KIVGDDgrELPW-DGKAFGDLQVRGPWVIDRYFR---GDASPLV-DGWFPTGDVATIDADG 423
|
410 420 430
....*....|....*....|....*....|....*.
gi 1039782744 550 TLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEAVA 585
Cdd:PRK07008 424 FMQITDRSKDVIK-SGGEWISSIDIENVAVAHPAVA 458
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
423-607 |
1.07e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 64.54 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 423 SSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTEcTAGCCLSLPGDWTA--GHVGAPMPCNyVKLVDvEEMNY 500
Cdd:PRK08276 262 SSL----RVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGE-VRILD-EDGNE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 501 LASKGEGEVCVK-GANVFKgYLKDPARTAEALDKDGWLHTGDIGkWL-PNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 578
Cdd:PRK08276 335 LPPGEIGTVYFEmDGYPFE-YHNDPEKTAAARNPHGWVTVGDVG-YLdEDGYLYLTDRKSDMI-ISGGVNIYPQEIENLL 411
|
170 180
....*....|....*....|....*....
gi 1039782744 579 LRSEAVAQVFVHGeslqafliavvVPDVE 607
Cdd:PRK08276 412 VTHPKVADVAVFG-----------VPDEE 429
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
423-604 |
2.52e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 63.56 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 423 SSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTEcTAGCCLSLPGDWTA--GHVGAPMpcnYVKLVDVEEMNY 500
Cdd:PRK13391 275 SSL----EVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATE-GLGFTACDSEEWLAhpGTVGRAM---FGDLHILDDDGA 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 501 LASKGE-GEVCVKGANVFKgYLKDPARTAEALDKDG-WLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 578
Cdd:PRK13391 347 ELPPGEpGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMI-ISGGVNIYPQEAENLL 424
|
170 180
....*....|....*....|....*....
gi 1039782744 579 LRSEAVAQVFVHG---ESLQAFLIAVVVP 604
Cdd:PRK13391 425 ITHPKVADAAVFGvpnEDLGEEVKAVVQP 453
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
266-586 |
3.76e-10 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 62.86 E-value: 3.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 266 PEPEDLAIICFTSGTTGNPKGAMITHQNIindcSGFIKATESAF-IASTDDVLISFLPLAhMFetvvecvmlchGAKIGf 344
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTF----AAQIDALRQLYgIRPGEVDLATFPLFA-LF-----------GPALG- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 345 fqgdirllmddLKVLQPTIFPVVPrllnrmfdrifGQANtslKRWLLDFASKRKEaelrSGIVRNNSLWDKLIFHKIQSS 424
Cdd:cd05910 145 -----------LTSVIPDMDPTRP-----------ARAD---PQKLVGAIRQYGV----SIVFGSPALLERVARYCAQHG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 425 LG-GKVRLMITGAAPVSATVLTFLRTAL--GCQFYEGYGQTECTAGCC------LSLPGDWTAGH----VGAPMPCNYVK 491
Cdd:cd05910 196 ITlPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrelLATTTAATSGGagtcVGRPIPGVRVR 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 492 LVDVEEMNY--------LASKGEGEVCVKGANVFKGYLKDPARTAEALDKDG----WLHTGDIGKWLPNGTLKIIDRKKH 559
Cdd:cd05910 276 IIEIDDEPIaewddtleLPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAH 355
|
330 340
....*....|....*....|....*..
gi 1039782744 560 IFKLAQGEYIApEKIENIYLRSEAVAQ 586
Cdd:cd05910 356 RVITTGGTLYT-EPVERVFNTHPGVRR 381
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
267-575 |
4.06e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 63.65 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 267 EPEDLAIICFTSGTTGNPKGAMITHQNIINDCS----GFikatesAFIASTDDVLISFLPLAHmfetvvecvmlchgaKI 342
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQlirhGF------GIDLNPDDVIVSWLPLYH---------------DM 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 343 GFFQGdirllmddlkVLQPtIFPVVPRLLnrMFDRIFGQANTslkRWLL-------------DFA----SKR-KEAELRS 404
Cdd:PRK05691 223 GLIGG----------LLQP-IFSGVPCVL--MSPAYFLERPL---RWLEaiseyggtisggpDFAyrlcSERvSESALER 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 405 givRNNSLWdklifhkiqsslggkvRLMITGAAPVSATVL-TFLRTALGC-----QFYEGYGQTECT---AGC------- 468
Cdd:PRK05691 287 ---LDLSRW----------------RVAYSGSEPIRQDSLeRFAEKFAACgfdpdSFFASYGLAEATlfvSGGrrgqgip 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 469 CLSLPGDWTAGHVGAP------MPCNY------VKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEA-LDKDG 535
Cdd:PRK05691 348 ALELDAEALARNRAEPgtgsvlMSCGRsqpghaVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfVEHDG 427
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1039782744 536 --WLHTGDIGkWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIE 575
Cdd:PRK05691 428 rtWLRTGDLG-FLRDGELFVTGRLKDML-IVRGHNLYPQDIE 467
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
484-639 |
4.09e-10 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 62.61 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 484 PMPCNYVK-----LVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEAL-DKDGW--LHTGDIGKwLPNGTLKIID 555
Cdd:PRK04813 317 RLPIGYAKpdsplLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGY-LEDGLLFYQG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 556 RKKHIFKLAqGEYIAPEKIENiYLR-----SEAVAQVFVHGESLQAfLIAVVVPDveslpswaqkrglQGSFEelcRNKD 630
Cdd:PRK04813 396 RIDFQIKLN-GYRIELEEIEQ-NLRqssyvESAVVVPYNKDHKVQY-LIAYVVPK-------------EEDFE---REFE 456
|
....*....
gi 1039782744 631 INKAILDDL 639
Cdd:PRK04813 457 LTKAIKKEL 465
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
122-591 |
6.53e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 62.21 E-value: 6.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 122 ISYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGPGDH--VGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 202 DK---PEKAKLLLEgvenklTPCLKIIVIMDSYGSDLVERGkkcGVEIISLKALEDLGRVnrvkPKPPEPEDLAIICfTS 278
Cdd:PRK07798 107 ERefaPRVAEVLPR------LPKLRTLVVVEDGSGNDLLPG---AVDYEDALAAGSPERD----FGERSPDDLYLLY-TG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 279 GTTGNPKGAMITHQNIINDCSGFIKATESAFIASTDDVL--------ISFLPLAHMfetvvecvMlcHGAK-----IGFF 345
Cdd:PRK07798 173 GTTGMPKGVMWRQEDIFRVLLGGRDFATGEPIEDEEELAkraaagpgMRRFPAPPL--------M--HGAGqwaafAALF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 346 QGdirllmddlkvlQPTIFPVVPRL-------------LNRMFdrIFGQAntsLKRWLLDFASKRKEAELrsgivrnnsl 412
Cdd:PRK07798 243 SG------------QTVVLLPDVRFdadevwrtierekVNVIT--IVGDA---MARPLLDALEARGPYDL---------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 413 wdklifhkiqSSLggkvRLMITGAAPVSATVLTFLRTAL-GCQFYEGYGQTEctAGCCLSLPGDWTAGHVGAP--MPCNY 489
Cdd:PRK07798 296 ----------SSL----FAIASGGALFSPSVKEALLELLpNVVLTDSIGSSE--TGFGGSGTVAKGAVHTGGPrfTIGPR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 490 VKLVDvEEMNYLAsKGEGEVCV--KGANVFKGYLKDPARTAEAL-DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLA 564
Cdd:PRK07798 360 TVVLD-EDGNPVE-PGSGEIGWiaRRGHIPLGYYKDPEKTAETFpTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTG 437
|
490 500
....*....|....*....|....*..
gi 1039782744 565 qGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:PRK07798 438 -GEKVFPEEVEEALKAHPDVADALVVG 463
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
215-599 |
7.33e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 62.09 E-value: 7.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 215 ENKLTPCLKIIV-IMDSYGSDLVE-RGKKCGVEIislkalEDL---GRVNRVKPKPPEP-EDLAIICFTSGTTGNPKGAM 288
Cdd:PRK05851 98 DATLTRFAGIGVrTVLSHGSHLERlRAVDSSVTV------HDLataAHTNRSASLTPPDsGGPAVLQGTAGSTGTPRTAI 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 289 ITHQNIINDCSGFIKATEsafIASTDDVLISFLPLAH-MFETVVECVMLChGAKIGffqgdirllmddlkvLQPTifpvv 367
Cdd:PRK05851 172 LSPGAVLSNLRGLNARVG---LDAATDVGCSWLPLYHdMGLAFLLTAALA-GAPLW---------------LAPT----- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 368 prllnrmfdrifGQANTSLKRWLlDFASkrkeaELRSGIVRNNSLWDKLI---FHKIQSSLGGKVRLMITGAAPVSATVL 444
Cdd:PRK05851 228 ------------TAFSASPFRWL-SWLS-----DSRATLTAAPNFAYNLIgkyARRVSDVDLGALRVALNGGEPVDCDGF 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 445 TFLRTALG-CQFYEG-----YGQTECTAGCCLSLPG-----------DWTAGH----VGAPMPCNYVKLVDVEEMNYLAS 503
Cdd:PRK05851 290 ERFATAMApFGFDAGaaapsYGLAESTCAVTVPVPGiglrvdevttdDGSGARrhavLGNPIPGMEVRISPGDGAAGVAG 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 504 KGEGEVCVKGANVFKGYLKDPartaeALDKDGWLHTGDIGkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIY----- 578
Cdd:PRK05851 370 REIGEIEIRGASMMSGYLGQA-----PIDPDDWFPTGDLG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERVAaqvrg 442
|
410 420
....*....|....*....|.
gi 1039782744 579 LRSEAVAQVFVHGESLQAFLI 599
Cdd:PRK05851 443 VREGAVVAVGTGEGSARPGLV 463
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
269-587 |
9.45e-10 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 61.56 E-value: 9.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 269 EDLAIIcFTSGTTGNPKGAMITHQNI--INDcsgFIKATESAFIASTD-DVLISFLPLAHM--FETVVECVMlcHGAKI- 342
Cdd:PRK05857 170 DPLAMI-FTSGTTGEPKAVLLANRTFfaVPD---ILQKEGLNWVTWVVgETTYSPLPATHIggLWWILTCLM--HGGLCv 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 343 --GFFQGDIRLLMDDLKVLQPTIfpvVPRLLNRMFdrifgqantslkrwlldfaskrkeAELRSGIVRNNSLwdklifhk 420
Cdd:PRK05857 244 tgGENTTSLLEILTTNAVATTCL---VPTLLSKLV------------------------SELKSANATVPSL-------- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 421 iqsslggkvRLMITGAAPVSATVLTFL-----RTAlgcQFYeGYGQTECTAGCclsLPGD------WTAGHVGAPMPCNY 489
Cdd:PRK05857 289 ---------RLVGYGGSRAIAADVRFIeatgvRTA---QVY-GLSETGCTALC---LPTDdgsivkIEAGAVGRPYPGVD 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 490 VKLVDVEEMNYLASKGE-----GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLA 564
Cdd:PRK05857 353 VYLAATDGIGPTAPGAGpsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-IC 430
|
330 340
....*....|....*....|...
gi 1039782744 565 QGEYIAPEKIENIylrSEAVAQV 587
Cdd:PRK05857 431 GGVNIAPDEVDRI---AEGVSGV 450
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
268-621 |
1.23e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 62.10 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 268 PEDLAIICFTSGTTGNPKGAMITHQNIINDCsgfiKATESAFIASTDDVLISFLPLAhmFETVVECVM--LCHGAKIGFF 345
Cdd:PRK12467 3236 GENLAYVIYTSGSTGKPKGVGVRHGALANHL----CWIAEAYELDANDRVLLFMSFS--FDGAQERFLwtLICGGCLVVR 3309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 346 QGDIR---LLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTSLKRWLldfaskrkeaelrsgivrnnslwdklifhkiq 422
Cdd:PRK12467 3310 DNDLWdpeELWQAIHAHRISIACFPPAYLQQFAEDAGGADCASLDIYV-------------------------------- 3357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 423 ssLGGKvrlmitgAAPVSATVLTFlRTALGCQFYEGYGQTECTAGCCL-SLPGDWTAGHVGAPM--PCNYVKLVDVE-EM 498
Cdd:PRK12467 3358 --FGGE-------AVPPAAFEQVK-RKLKPRGLTNGYGPTEAVVTVTLwKCGGDAVCEAPYAPIgrPVAGRSIYVLDgQL 3427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 499 NYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAP 571
Cdd:PRK12467 3428 NPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADpfsgsgGRLYrTGDLARYRADGVIEYLGRIDHQVKI-RGFRIEL 3506
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1039782744 572 EKIENIYLRSEAVAQVFVHGESLQA--FLIAVVVPDVESlPSWAQ--KRGLQGS 621
Cdd:PRK12467 3507 GEIEARLLQHPSVREAVVLARDGAGgkQLVAYVVPADPQ-GDWREtlRDHLAAS 3559
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
113-608 |
1.45e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 61.90 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 113 RKPNQPY-----EWISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAI 187
Cdd:PRK12316 3069 RTPDAVAlafgeQRLSYAELNRRANRLAHRLIERGVGP--DVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERL 3146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 188 TYIVNKAelsvifadkpeKAKLLLEGVENKLTPCLKIIVIMdsygsdlVERGKkcgveiislkalEDLGRVNrvKPKPPE 267
Cdd:PRK12316 3147 AYMLEDS-----------GAQLLLSQSHLRLPLAQGVQVLD-------LDRGD------------ENYAEAN--PAIRTM 3194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 268 PEDLAIICFTSGTTGNPKGAMITHQNIindcSGFIKATESAFIASTDDVLISFLPLAHMFETVVECVMLCHGAKIgffqg 347
Cdd:PRK12316 3195 PENLAYVIYTSGSTGKPKGVGIRHSAL----SNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARV----- 3265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 348 dirllmddlkVLQPTIFPVVPRLLNRMFDRifGQANTSLKRWlldfaskrkeaelrsgivrnnSLWDKLIFHKIQSSLGG 427
Cdd:PRK12316 3266 ----------VLAGPEDWRDPALLVELINS--EGVDVLHAYP---------------------SMLQAFLEEEDAHRCTS 3312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 428 KVRLMITGAAPVSATVLtflRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGH--VGAPMPCNYVKLVDVEeMNYLASKG 505
Cdd:PRK12316 3313 LKRIVCGGEALPADLQQ---QVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILDGS-LEPVPVGA 3388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 506 EGEVCVKGANVFKGYLKDPARTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYL 579
Cdd:PRK12316 3389 LGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQVKI-RGFRIELGEIEARLL 3467
|
490 500
....*....|....*....|....*....
gi 1039782744 580 RSEAVAQVFVHGESLQAfLIAVVVPDVES 608
Cdd:PRK12316 3468 EHPWVREAVVLAVDGRQ-LVAYVVPEDEA 3495
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
123-605 |
1.51e-09 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 60.87 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 123 SYKEVAELAECIGSGLIQKGFKP--CseqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVN--KAELSV 198
Cdd:PRK12406 13 SFDELAQRAARAAGGLAALGVRPgdC----VALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEdsGARVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 199 IFADkpekaklLLEGVENKLTPCLKIIV------IMDSYGSDLVERGKKCGveiislkALEDLGRVNRVKP--KPPEPED 270
Cdd:PRK12406 89 AHAD-------LLHGLASALPAGVTVLSvptppeIAAAYRISPALLTPPAG-------AIDWEGWLAQQEPydGPPVPQP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 271 LAIIcFTSGTTGNPKGAmithqniindcsgfikaTESAFIASTDDVLISFLPLAHMFETVVECVM---LCHGAKIGFFQG 347
Cdd:PRK12406 155 QSMI-YTSGTTGHPKGV-----------------RRAAPTPEQAAAAEQMRALIYGLKPGIRALLtgpLYHSAPNAYGLR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 348 DIRLlmDDLKVLQP-----------------TIFpVVPRllnrMFDRifgqantslkrwLLDFASKRKEAelrsgivrnn 410
Cdd:PRK12406 217 AGRL--GGVLVLQPrfdpeellqlierhritHMH-MVPT----MFIR------------LLKLPEEVRAK---------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 411 slWDklifhkiQSSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTE------CTAGCCLSLPGDwtaghVGAP 484
Cdd:PRK12406 268 --YD-------VSSL----RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTEsgavtfATSEDALSHPGT-----VGKA 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 485 MPCNYVKLVDvEEMNYLASKGEGEVCVK--GANVFKgYLKDPARTAEaLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFk 562
Cdd:PRK12406 330 APGAELRFVD-EDGRPLPQGEIGEIYSRiaGNPDFT-YHNKPEKRAE-IDRGGFITSGDVGYLDADGYLFLCDRKRDMV- 405
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1039782744 563 LAQGEYIAPEKIENIYLRSEAVAQVFVHG---ESLQAFLIAVVVPD 605
Cdd:PRK12406 406 ISGGVNIYPAEIEAVLHAVPGVHDCAVFGipdAEFGEALMAVVEPQ 451
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
423-599 |
2.79e-09 |
|
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: 59.84 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 423 SSLGGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCC--LSLPGDWTAGHVGAPMPCNYVKLVDvEEMNY 500
Cdd:cd05973 201 ARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLAnhHALEHPVHAGSAGRAMPGWRVAVLD-DDGDE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 501 LASKGEGEVCVKGANV----FKGYLKDPARTAEAldkdGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEN 576
Cdd:cd05973 280 LGPGEPGRLAIDIANSplmwFRGYQLPDTPAIDG----GYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFDVES 354
|
170 180 190
....*....|....*....|....*....|
gi 1039782744 577 IYLRSEAVAQVFV-------HGESLQAFLI 599
Cdd:cd05973 355 ALIEHPAVAEAAVigvpdpeRTEVVKAFVV 384
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
269-600 |
6.04e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 59.80 E-value: 6.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 269 EDLAIICFTSGTTGNPKGAMITHQNIINDCSgFIKATesaFIASTDDVLISFLPLAhmFE-TVVECVM-LCHGAKIGFF- 345
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNTHAALAERLQ-WMQAT---YALDDSDVLMQKAPIS--FDvSVWECFWpLITGCRLVLAg 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 346 ---QGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTSLKRwlLDFASKRKEAELRsgivrnNSLWDKLifhkiq 422
Cdd:PRK05691 1347 pgeHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRR--LFSGGEALPAELR------NRVLQRL------ 1412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 423 sslggkvrlmitgaaPvsatvltflrtalGCQFYEGYGQTE----CTAGCCLSLPGDWTAghVGAPMPCNYVKLVDvEEM 498
Cdd:PRK05691 1413 ---------------P-------------QVQLHNRYGPTEtainVTHWQCQAEDGERSP--IGRPLGNVLCRVLD-AEL 1461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 499 NYLASKGEGEVCVKGANVFKGYLKDPARTAE-----ALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAP 571
Cdd:PRK05691 1462 NLLPPGVAGELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL-RGFRVEP 1540
|
330 340 350
....*....|....*....|....*....|.
gi 1039782744 572 EKIENIYLRSEAVAQ--VFVHGESLQAFLIA 600
Cdd:PRK05691 1541 EEIQARLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
268-624 |
1.67e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 58.43 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 268 PEDLAIICFTSGTTGNPKGAMITHQNIIN------------DCSGFIKATESAFIAStddVLISFLPLAHmfetvvecvm 335
Cdd:PRK12316 654 PENLAYVIYTSGSTGKPKGAGNRHRALSNrlcwmqqayglgVGDTVLQKTPFSFDVS---VWEFFWPLMS---------- 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 336 lchGAkigffqgdiRLLmddlkvlqptifpVVPRLLNRMFDRIFGQANTSLKRwLLDFASKRKEAELRSGIVrnnslwdk 415
Cdd:PRK12316 721 ---GA---------RLV-------------VAAPGDHRDPAKLVELINREGVD-TLHFVPSMLQAFLQDEDV-------- 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 416 lifhkiqSSLGGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHV--GAPMPCNYVKLV 493
Cdd:PRK12316 767 -------ASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGGDSVpiGRPIANLACYIL 839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 494 DVEeMNYLASKGEGEVCVKGANVFKGYLKDPARTAEAL------DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGE 567
Cdd:PRK12316 840 DAN-LEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFvpspfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKL-RGL 917
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039782744 568 YIAPEKIENIYLRSEAVAQVFVHGESLQAfLIAVVVPDVE--SLPSwAQKRGLQGSFEE 624
Cdd:PRK12316 918 RIELGEIEARLLEHPWVREAAVLAVDGKQ-LVGYVVLESEggDWRE-ALKAHLAASLPE 974
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
274-593 |
2.48e-08 |
|
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: 56.26 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 274 ICFTSGTTGNPKGAMITHQNIIndcsGFIKATESAFIASTDDVLISFLPLAH-MFETVVECVMLCHGAKIGFFQGDIRLL 352
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERSWI----ESFVCNEDLFNISGEDAILAPGPLSHsLFLYGAISALYLGGTFIGQRKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 353 MDDLKVLQPTIFPVVPRLLNrmfdrifgqantSLKRWLldfaskRKEAELRSgIVRNNSLWDKLIFHKIQSslggkvrlm 432
Cdd:cd17633 81 IRKINQYNATVIYLVPTMLQ------------ALARTL------EPESKIKS-IFSSGQKLFESTKKKLKN--------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 433 itgAAPVSatvltflrtalgcQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCnyvklVDVEEMNYlASKGEGEVCVK 512
Cdd:cd17633 133 ---IFPKA-------------NLIEFYGTSELSFITYNFNQESRPPNSVGRPFPN-----VEIEIRNA-DGGEIGKIFVK 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 513 GANVFKGYLKdpartAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHGE 592
Cdd:cd17633 191 SEMVFSGYVR-----GGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIEEAIVVGI 264
|
.
gi 1039782744 593 S 593
Cdd:cd17633 265 P 265
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
482-575 |
2.66e-08 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 56.94 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 482 GAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPArTAEALDKDGWLHTGDIGkWLPNGTLKIIDRKKHIF 561
Cdd:PRK09192 388 GKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLMSGYFRDEE-SQDVLAADGWLDTGDLG-YLLDGYLYITGRAKDLI 464
|
90
....*....|....
gi 1039782744 562 kLAQGEYIAPEKIE 575
Cdd:PRK09192 465 -IINGRNIWPQDIE 477
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
452-609 |
2.77e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 56.96 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 452 GCQFYEGYGQTEctAGCCLSLPGDWTAGHVGAPMPCnyVKLVDVE-----------EMNYLASKGE--GE-VCVKGANVF 517
Cdd:PRK13388 288 GCQVEDGYGSSE--GAVIVVREPGTPPGSIGRGAPG--VAIYNPEtltecavarfdAHGALLNADEaiGElVNTAGAGFF 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 518 KGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFVHG----ES 593
Cdd:PRK13388 364 EGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYAvpdeRV 441
|
170
....*....|....*.
gi 1039782744 594 LQAFLIAVVVPDVESL 609
Cdd:PRK13388 442 GDQVMAALVLRDGATF 457
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
268-600 |
4.92e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 56.72 E-value: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 268 PEDLAIICFTSGTTGNPKGAMITHQNIINDCSG---FIKATESAFIAST-----DDVLISFLPlAHMFETVVECV--MLC 337
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSkvpYLALSEADVIAQTasqsfDISVWQFLA-APLFGARVEIVpnAIA 3946
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 338 HgakigffqgDIRLLMDDLKVLQPTIFPVVPRLLNRMF--DRifgQANTSLkRWLL--------DFASKRKEAELRSGIV 407
Cdd:PRK05691 3947 H---------DPQGLLAHVQAQGITVLESVPSLIQGMLaeDR---QALDGL-RWMLptgeamppELARQWLQRYPQIGLV 4013
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 408 rnNSLwdklifhkiqsslggkvrlmitGAAPVSATVlTFLRTALgcqfyegygqtECTAGCCLSlpgdwtaghVGAPMPC 487
Cdd:PRK05691 4014 --NAY----------------------GPAECSDDV-AFFRVDL-----------ASTRGSYLP---------IGSPTDN 4048
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 488 NYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGW-------LHTGDIGKWLPNGTLKIIDRKKHI 560
Cdd:PRK05691 4049 NRLYLLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRRSDGVLEYVGRIDHQ 4127
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1039782744 561 -----FKLAQGEyIAPEKIENIYLRSEAVA-QVFVHGESLQAFLIA 600
Cdd:PRK05691 4128 vkirgYRIELGE-IEARLHEQAEVREAAVAvQEGVNGKHLVGYLVP 4172
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
263-607 |
6.65e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 55.70 E-value: 6.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 263 PKPPEPEdlAIICFTSGTTGNPKGAMITHQNIIndcsgfikatesAFIAStddvLISFLPLaHMFETVVECVMLCHG--- 339
Cdd:PRK07788 203 PKPPKPG--GIVILTSGTTGTPKGAPRPEPSPL------------APLAG----LLSRVPF-RAGETTLLPAPMFHAtgw 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 340 --AKIGFFQG---------DIRLLMDDLKVLQPTIFPVVPRLLNRMFDrifgqantslkrwLLDFASKRKEAelrsgivr 408
Cdd:PRK07788 264 ahLTLAMALGstvvlrrrfDPEATLEDIAKHKATALVVVPVMLSRILD-------------LGPEVLAKYDT-------- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 409 nnslwdklifhkiqSSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECtAGCCLSLPGDWTA--GHVGAPMP 486
Cdd:PRK07788 323 --------------SSL----KIIFVSGSALSPELATRALEAFGPVLYNLYGSTEV-AFATIATPEDLAEapGTVGRPPK 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 487 CNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYL--KDPARtaealdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLA 564
Cdd:PRK07788 384 GVTVKILD-ENGNEVPRGVVGRIFVGNGFPFEGYTdgRDKQI------IDGLLSSGDVGYFDEDGLLFVDGRDDDMI-VS 455
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1039782744 565 QGEYIAPEKIENIYLRSEAVAQVFVHGeslqafliavvVPDVE 607
Cdd:PRK07788 456 GGENVFPAEVEDLLAGHPDVVEAAVIG-----------VDDEE 487
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
120-607 |
1.70e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 54.24 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 120 EWISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVI 199
Cdd:PRK13390 23 EQVSYRQLDDDSAALARVLYDAGLRT--GDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 200 FADKPekakllLEGVENKLtpclkiivimdsyGSDLVERgKKCGVEIISLKALEdlGRVNRVKPKPPEPEDLAIICFTSG 279
Cdd:PRK13390 101 VASAA------LDGLAAKV-------------GADLPLR-LSFGGEIDGFGSFE--AALAGAGPRLTEQPCGAVMLYSSG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 280 TTGNPKGAM--ITHQNIINDCSGFIKATESAFIASTDDVLISFLPLAHMfETVVECVMLcH---GAKIGFFQGDIRLLMD 354
Cdd:PRK13390 159 TTGFPKGIQpdLPGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHA-APLRWCSMV-HalgGTVVLAKRFDAQATLG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 355 DLKVLQPTIFPVVPRLLNRMFdrifgqantslkrwlldfaskRKEAELRSgivrnnsLWDklifhkiQSSLggkvRLMIT 434
Cdd:PRK13390 237 HVERYRITVTQMVPTMFVRLL---------------------KLDADVRT-------RYD-------VSSL----RAVIH 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 435 GAAPVSATVLTFLRTALGCQFYEGYGQTEcTAGCCLSLPGDWTA--GHVGAPMpCNYVKLVDvEEMNYLASKGEGEVCVK 512
Cdd:PRK13390 278 AAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGRSV-LGDLHICD-DDGNELPAGRIGTVYFE 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 513 GANVFKGYLKDPARTAEALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVH 590
Cdd:PRK13390 355 RDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQETENALTMHPAVHDVAVI 433
|
490
....*....|....*..
gi 1039782744 591 GeslqafliavvVPDVE 607
Cdd:PRK13390 434 G-----------VPDPE 439
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
276-591 |
2.02e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 54.01 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 276 FTSGTTGNPKGAMITHQNIIN--DCsgfikaTESAF-IASTDDVLISflplahmfETVVECVMLcHGAKIGFFQGDIRLL 352
Cdd:PRK07638 150 FTSGSTGKPKAFLRAQQSWLHsfDC------NVHDFhMKREDSVLIA--------GTLVHSLFL-YGAISTLYVGQTVHL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 353 MddlkvlqPTIFPvvprllNRMFDRIFGQANTslkrwLLDFASKRKEAELRSGIVRNNSLwdklifhKIQSSlGGKvrlm 432
Cdd:PRK07638 215 M-------RKFIP------NQVLDKLETENIS-----VMYTVPTMLESLYKENRVIENKM-------KIISS-GAK---- 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 433 iTGAAPVSATVLTFLRTalgcQFYEGYGQTECTAGCCLSlPGDWTAGHVGAPMPCNYVKLVDVEEMNYLASKGE-GEVCV 511
Cdd:PRK07638 265 -WEAEAKEKIKNIFPYA----KLYEFYGASELSFVTALV-DEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEiGTVYV 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 512 KGANVFKGYLKDpARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:PRK07638 339 KSPQFFMGYIIG-GVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIESVLHEHPAVDEIVVIG 416
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
120-291 |
2.72e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 53.75 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 120 EWISYKEVAELAECIGSGLIQKGFKPCSEQFIglFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVI 199
Cdd:PRK04319 72 EKYTYKELKELSNKFANVLKELGVEKGDRVFI--FMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 200 FADKpekaKLLLEGVENKLtPCLKIIVIMDsygsDLVERGKKCgveiISLKAL-----EDLgrvnrvKPKPPEPEDLAII 274
Cdd:PRK04319 150 ITTP----ALLERKPADDL-PSLKHVLLVG----EDVEEGPGT----LDFNALmeqasDEF------DIEWTDREDGAIL 210
|
170 180
....*....|....*....|...
gi 1039782744 275 CFTSGTTGNPKG------AMITH 291
Cdd:PRK04319 211 HYTSGSTGKPKGvlhvhnAMLQH 233
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
246-558 |
3.88e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 53.41 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 246 IISLKALeDLGRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIINDC----SGFIKATESafIASTDDVLISFL 321
Cdd:PRK05850 138 VIEVDLL-DLDSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFeqlmSDYFGDTGG--VPPPDTTVVSWL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 322 PLAH-MFETVVECV-MLChgakigffqGDIRLLMDDLKVLQPtifpvvP----RLLNRmfdriFGQANTSLKRWLLDFAS 395
Cdd:PRK05850 215 PFYHdMGLVLGVCApILG---------GCPAVLTSPVAFLQR------ParwmQLLAS-----NPHAFSAAPNFAFELAV 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 396 KRKEAELRSGIvrnnslwdklifhkiqsSLGGkVRLMITGAAPV-SATVLTFLRTALGCQFYE-----GYGQTECTAGCC 469
Cdd:PRK05850 275 RKTSDDDMAGL-----------------DLGG-VLGIISGSERVhPATLKRFADRFAPFNLREtairpSYGLAEATVYVA 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 470 LSLPGD-----------WTAGHVgapMPC---------NY-------VKLVDVEEMNYLASKGEGEVCVKGANVFKGYLK 522
Cdd:PRK05850 337 TREPGQppesvrfdyekLSAGHA---KRCetgggtplvSYgsprsptVRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQ 413
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1039782744 523 DPART-----AEALDK-----DG-WLHTGDIGkWLPNGTLKIIDRKK 558
Cdd:PRK05850 414 KPEETertfgATLVDPspgtpEGpWLRTGDLG-FISEGELFIVGRIK 459
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
265-326 |
4.14e-07 |
|
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: 53.06 E-value: 4.14e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039782744 265 PPEPEDLAIICFTSGTTGNPKGAMITHQNIINdCSGFIkateSAFIASTDDVLISFLPLAHM 326
Cdd:cd05938 140 HVTIKSPALYIYTSGTTGLPKAARISHLRVLQ-CSGFL----SLCGVTADDVIYITLPLYHS 196
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
266-557 |
5.17e-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: 52.86 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 266 PEPEDLAIICFTSGTTGNPKGAMITHQNIINdcsgFIKATESAFIASTDDVLIsFLPLAHMFETVVECVM-LCHGAKIgf 344
Cdd:cd17654 115 RTDECLAYVIHTSGTTGTPKIVAVPHKCILP----NIQHFRSLFNITSEDILF-LTSPLTFDPSVVEIFLsLSSGATL-- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 345 fqgdirllmddlkVLQPTIFPVVPRLLNRMFDRIFG----QANTSLKRwllDFASKRKEAELRSGIvrnnslwdklifhk 420
Cdd:cd17654 188 -------------LIVPTSVKVLPSKLADILFKRHRitvlQATPTLFR---RFGSQSIKSTVLSAT-------------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 421 iqSSLggKVrLMITGAAPVSATVLTFLR-TALGCQFYEGYGQTECtagCCLSL----PGDWTAGHVGAPMPCNYVKLVDV 495
Cdd:cd17654 238 --SSL--RV-LALGGEPFPSLVILSSWRgKGNRTRIFNIYGITEV---SCWALaykvPEEDSPVQLGSPLLGTVIEVRDQ 309
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039782744 496 EemnylASKGEGEVCVKGANVfKGYLKDPARTAEALdkdgWLHTGDIGKwLPNGTLKIIDRK 557
Cdd:cd17654 310 N-----GSEGTGQVFLGGLNR-VCILDDEVTVPKGT----MRATGDFVT-VKDGELFFLGRK 360
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
122-342 |
1.30e-06 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 51.80 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 122 ISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWV-----IVEQGcfsysmVVVPLYDT-LGADAITYIVNKAE 195
Cdd:PRK08279 63 ISYAELNARANRYAHWAAARGVGK--GDVVALLMENRPEYLaawlgLAKLG------AVVALLNTqQRGAVLAHSLNLVD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 196 LSVIFADkPEKAKLLlEGVENKLTPCLKIIVIMDSYGSDLVergkkcgveiislkALEDLGRVNRVKPKPPEP------- 268
Cdd:PRK08279 135 AKHLIVG-EELVEAF-EEARADLARPPRLWVAGGDTLDDPE--------------GYEDLAAAAAGAPTTNPAsrsgvta 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039782744 269 EDLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKATEsafiASTDDVLISFLPLAH-MFETVVECVMLCHGAKI 342
Cdd:PRK08279 199 KDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLR----LTPDDVLYCCLPLYHnTGGTVAWSSVLAAGATL 269
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
265-296 |
1.46e-06 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 51.97 E-value: 1.46e-06
10 20 30
....*....|....*....|....*....|..
gi 1039782744 265 PPEPEDLAIICFTSGTTGNPKGAMITHQNIIN 296
Cdd:PRK10252 594 LSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVN 625
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
264-616 |
7.88e-06 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 48.50 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 264 KPPEP--EDLAIICFTSGTTGNPKGAMITHQNIINDCSgfikATEsAFIASTDDVLISfLPLAHmfetvvecvmlchgak 341
Cdd:PRK07824 28 RVGEPidDDVALVVATSGTTGTPKGAMLTAAALTASAD----ATH-DRLGGPGQWLLA-LPAHH---------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 342 IGFFQGDIRLLM---DDLKVLQPTIF--PVVPRLLNRM-FDRIFgqanTSLKRWLLDFASKRKEA--ELRSgivrnnslw 413
Cdd:PRK07824 86 IAGLQVLVRSVIagsEPVELDVSAGFdpTALPRAVAELgGGRRY----TSLVPMQLAKALDDPAAtaALAE--------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 414 dkliFHKIqsslggkvrlmITGAAPVSATVLTfLRTALGCQFYEGYGQTEcTAGCCLslpgdwtagHVGAPMPCNYVKLV 493
Cdd:PRK07824 153 ----LDAV-----------LVGGGPAPAPVLD-AAAAAGINVVRTYGMSE-TSGGCV---------YDGVPLDGVRVRVE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 494 DveemnylaskgeGEVCVKGANVFKGY--LKDPARTAEaldkDGWLHTGDIGKwLPNGTLKIIDRKKHIFKLAqGEYIAP 571
Cdd:PRK07824 207 D------------GRIALGGPTLAKGYrnPVDPDPFAE----PGWFRTDDLGA-LDDGVLTVLGRADDAISTG-GLTVLP 268
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1039782744 572 EKIENIYLRSEAVAQVFVHG---ESLQAFLIAVVVPDVESLPSWAQKR 616
Cdd:PRK07824 269 QVVEAALATHPAVADCAVFGlpdDRLGQRVVAAVVGDGGPAPTLEALR 316
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
266-615 |
1.13e-05 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 48.15 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 266 PEPEDLAIICfTSGTTGNPKGAMITHQNIINDCSGFIKATESAFIASTDDVL-------ISFLPLAHmfetvvecvmLCH 338
Cdd:cd05924 1 RSADDLYILY-TGGTTGMPKGVMWRQEDIFRMLMGGADFGTGEFTPSEDAHKaaaaaagTVMFPAPP----------LMH 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 339 GAK-----IGFFQGDiRLLMDDLKVLQPTIFPVVPR-LLNRMFdrIFGQAntsLKRWLLDfaskrkeaELRSGivRNNSL 412
Cdd:cd05924 70 GTGswtafGGLLGGQ-TVVLPDDRFDPEEVWRTIEKhKVTSMT--IVGDA---MARPLID--------ALRDA--GPYDL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 413 wdklifhkiqSSLggkvRLMITGAAPVSATVLT-FLRTALGCQFYEGYGQTECTA-GCCLSLPGDWTAGHVGAPMPcnYV 490
Cdd:cd05924 134 ----------SSL----FAISSGGALLSPEVKQgLLELVPNITLVDAFGSSETGFtGSGHSAGSGPETGPFTRANP--DT 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 491 KLVDvEEMNYL--ASKGEGEVCVKGaNVFKGYLKDPARTAEAL-DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAq 565
Cdd:cd05924 198 VVLD-DDGRVVppGSGGVGWIARRG-HIPLGYYGDEAKTAETFpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTG- 274
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1039782744 566 GEYIAPEKIENIYLRSEAVAQVFVHGeslqafliavvVPDveslPSWAQK 615
Cdd:cd05924 275 GEKVFPEEVEEALKSHPAVYDVLVVG-----------RPD----ERWGQE 309
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
452-602 |
3.52e-05 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 46.95 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 452 GCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVdVEEMNYLASKGEGEVCVKGANVFKGYLKDPArtaEAL 531
Cdd:PRK06060 286 GIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVV-APDGTTAGPGVEGDLWVRGPAIAKGYWNRPD---SPV 361
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039782744 532 DKDGWLHTGDIGKWLPNGTLKIIDRKKHIfKLAQGEYIAPEKIENIYLRSEAVAQVFVHG-------ESLQAFLIAVV 602
Cdd:PRK06060 362 ANEGWLDTRDRVCIDSDGWVTYRCRADDT-EVIGGVNVDPREVERLIIEDEAVAEAAVVAvrestgaSTLQAFLVATS 438
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
268-614 |
7.72e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 46.31 E-value: 7.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 268 PEDLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKAtesaFIASTDDVLISFLPLAhmFETVVE--CVMLCHGAKIGF- 344
Cdd:PRK05691 2332 PQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIER----FGMRADDCELHFYSIN--FDAASErlLVPLLCGARVVLr 2405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 345 FQG-----DIRLLMDDLKVlqpTIFPVVPRllnrmfdriFGqanTSLKRWLldfaskrkeaelrsgIVRNNSLwdklifh 419
Cdd:PRK05691 2406 AQGqwgaeEICQLIREQQV---SILGFTPS---------YG---SQLAQWL---------------AGQGEQL------- 2448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 420 kiqsslggKVRLMITGAAPVSATVLTFLRTALGCQ-FYEGYGQTE-------CTAGccLSLPGDWTAGHVGAPMPCNYVK 491
Cdd:PRK05691 2449 --------PVRMCITGGEALTGEHLQRIRQAFAPQlFFNAYGPTEtvvmplaCLAP--EQLEEGAASVPIGRVVGARVAY 2518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 492 LVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLa 564
Cdd:PRK05691 2519 ILD-ADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdggrlyrTGDLVRLRADGLVEYVGRIDHQVKI- 2596
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1039782744 565 QGEYIAPEKIENIYLRSEAV--AQVFVHGESLQAFLIAVVVPDVESLPSWAQ 614
Cdd:PRK05691 2597 RGFRIELGEIESRLLEHPAVreAVVLALDTPSGKQLAGYLVSAVAGQDDEAQ 2648
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
488-598 |
2.16e-04 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 44.34 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 488 NYVKLVDVEEMNYLASKGEGE----VCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKL 563
Cdd:cd05915 338 IPLVRLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKS 417
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1039782744 564 AqGEYIAPEKIENIYLRSEAVAQVFV-------HGESLQAFL 598
Cdd:cd05915 418 G-GEWISSVDLENALMGHPKVKEAAVvaiphpkWQERPLAVV 458
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
260-591 |
7.42e-04 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 42.95 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 260 RVKPKPPEPEDLAIICFTSGTTGNPKGAMITHqniindcSGF-IKATESafiastddvlisflpLAHMFETVVECVMLCh 338
Cdd:cd17634 223 EHQPEAMNAEDPLFILYTSGTTGKPKGVLHTT-------GGYlVYAATT---------------MKYVFDYGPGDIYWC- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 339 GAKIGFFQGDIRLLMDDLkVLQPTIF-----PV--VPRLLNRMFDR----IFGQANTSLKrwlldfaSKRKEAelrsgiv 407
Cdd:cd17634 280 TADVGWVTGHSYLLYGPL-ACGATTLlyegvPNwpTPARMWQVVDKhgvnILYTAPTAIR-------ALMAAG------- 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 408 rnnslwDKLIFHKIQSSLggkvRLMITGAAPVSATVLTFLRTALG---CQFYEGYGQTECTAGCCLSLPG--DWTAGHVG 482
Cdd:cd17634 345 ------DDAIEGTDRSSL----RILGSVGEPINPEAYEWYWKKIGkekCPVVDTWWQTETGGFMITPLPGaiELKAGSAT 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039782744 483 APMPCNYVKLVDvEEMNYLASKGEGEVCVKGA--NVFKGYLKDPARTAEALDK--DGWLHTGDIGKWLPNGTLKIIDRKK 558
Cdd:cd17634 415 RPVFGVQPAVVD-NEGHPQPGGTEGNLVITDPwpGQTRTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSD 493
|
330 340 350
....*....|....*....|....*....|...
gi 1039782744 559 HIFKLAqGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:cd17634 494 DVINVA-GHRLGTAEIESVLVAHPKVAEAAVVG 525
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
264-325 |
1.85e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 41.64 E-value: 1.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039782744 264 KPPEP--EDLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKATEsafiASTDDVLISFLPLAH 325
Cdd:PRK07769 173 VPPEAneDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALE----GQEGDRGVSWLPFFH 232
|
|
| |
