|
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: 945.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 117 QPYEWISYKEVAELAECIGSGLIQKGFKPCSEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAEL 196
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 197 SVIFADKpekaklllegvenkltpclkiivimdsygsdlvergkkcGVEIISLKALEDLGRVNRVKPKPPEPEDLAIICF 276
Cdd:cd05927 81 SIVFCDA---------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 277 TSGTTGNPKGAMITHQNIINDCSGFIKATESALTLNASDTQISYLPLAHMYEQQLQCVMLCHGAKIGFFQGDIRLLMDDL 356
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 357 KVLQPTIFPVVPRLLNRMFDRIFG--QANTSLKRWLLDFASKRKEAELRSGIVRNNSLWDKLIFHKIQSSLGGKVRLMIT 434
Cdd:cd05927 202 KALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 435 GAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDVEEMNYLA--SKGEGEVCVK 512
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAkdPNPRGEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 513 GANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGE 592
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 593 SLQAFLIAVVVPDVESLPSWAQKRGL-QGSFEELCRNKDINKAILDDLLKLGKEAGLKPFEQVKGIAVHPELFSIDNGLL 671
Cdd:cd05927 442 SLKSFLVAIVVPDPDVLKEWAASKGGgTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLL 521
|
570 580
....*....|....*....|....
gi 1720426399 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: 718.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 87 YDDVRTMYDGFQRGIQVSNNGPCLGSRKPNQ----PYEWISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWV 162
Cdd:PLN02736 40 HPEIGTLHDNFVYAVETFRDYKYLGTRIRVDgtvgEYKWMTYGEAGTARTAIGSGLVQHGIPK--GACVGLYFINRPEWL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 163 IVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFAdKPEKAKLLLEGVENklTPCLKIIVIMDSYGSDLVERGKKC 242
Cdd:PLN02736 118 IVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCLSE--IPSVRLIVVVGGADEPLPSLPSGT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 243 GVEIISLKALEDLGRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKATEsaltLNASDTQISYLP 322
Cdd:PLN02736 195 GVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTK----FYPSDVHISYLP 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 323 LAHMYEQQLQCVMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTS--LKRWLLDFASKRKEA 400
Cdd:PLN02736 271 LAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESggLKERLFNAAYNAKKQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 401 ELRSGivRNNS-LWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTEctAGCCLSL--PGDWT 477
Cdd:PLN02736 351 ALENG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTE--TSCVISGmdEGDNL 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 478 AGHVGAPMPCNYVKLVDVEEMNYLASKG---EGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKII 554
Cdd:PLN02736 427 SGHVGSPNPACEVKLVDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKII 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 555 DRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAVVVPDVESLPSWAQKRGLQ-GSFEELCRNKDINK 633
Cdd:PLN02736 507 DRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRVRA 586
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720426399 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 1720426399 87 YDDVRTMYDGFQRGIQVSNNGPCLgSRKPNQPYEWISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQ 166
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVAL-REKEDGIWQSLTWAEFAERVRALAAGLLALGVKP--GDRVAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 167 GCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFADKPEKAKLLLEGVENklTPCLKIIVIMDsygsdlvERGKKCGVEI 246
Cdd:COG1022 84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDE--LPSLRHIVVLD-------PRGLRDDPRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 247 ISLKALEDLG-----------RVNRVKPkppepEDLAIICFTSGTTGNPKGAMITHQNIINDCsgfiKATESALTLNASD 315
Cdd:COG1022 155 LSLDELLALGrevadpaeleaRRAAVKP-----DDLATIIYTSGTTGRPKGVMLTHRNLLSNA----RALLERLPLGPGD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 316 TQISYLPLAHMYEQQLQCVMLCHGAKIGFfQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTS--LKRWLLDF 393
Cdd:COG1022 226 RTLSFLPLAHVFERTVSYYALAAGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAggLKRKLFRW 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 394 A---SKRKEAELRSGivRNNSLW--------DKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRtALGCQFYEGYGQT 462
Cdd:COG1022 305 AlavGRRYARARLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFR-ALGIPVLEGYGLT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 463 ECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDveemnylaskgEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDI 542
Cdd:COG1022 382 ETSPVITVNRPGDNRIGTVGPPLPGVEVKIAE-----------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDI 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 543 GKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESlQAFLIAVVVPDVESLPSWAQKRGLQ-GS 621
Cdd:COG1022 451 GELDEDGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGLPyTS 529
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720426399 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 |
5.32e-166 |
|
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: 484.41 E-value: 5.32e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 117 QPYEWISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAEL 196
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEP--GDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 197 SVIFADKPEkaklllegvenkltpclkiivimdsygsdlvergkkcgveiislkaledlgrvnrvkpkppepeDLAIICF 276
Cdd:cd05907 79 KALFVEDPD----------------------------------------------------------------DLATIIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 277 TSGTTGNPKGAMITHQNIINDCSGFIKAtesaLTLNASDTQISYLPLAHMYEQQL-QCVMLCHGAKIGFFQgDIRLLMDD 355
Cdd:cd05907 95 TSGTTGRPKGVMLSHRNILSNALALAER----LPATEGDRHLSFLPLAHVFERRAgLYVPLLAGARIYFAS-SAETLLDD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 356 LKVLQPTIFPVVPRLLNRMFDRIFGQANTSLKRWLLDFASkrkeaelrsgivrnnslwdklifhkiqsslGGKVRLMITG 435
Cdd:cd05907 170 LSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV------------------------------GGRLRFAASG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 436 AAPVSATVLTFLRtALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDveemnylaskgEGEVCVKGAN 515
Cdd:cd05907 220 GAPLPAELLHFFR-ALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPN 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 516 VFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESlQ 595
Cdd:cd05907 288 VMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDG-R 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 596 AFLIAVVVPDVESLPSWAQKRGL-QGSFEELCRNKDINKAILDDLLKLGkeAGLKPFEQVKGIAVHPELFSIDNGLLTPT 674
Cdd:cd05907 367 PFLVALIVPDPEALEAWAEEHGIaYTDVAELAANPAVRAEIEAAVEAAN--ARLSRYEQIKKFLLLPEPFTIENGELTPT 444
|
....*...
gi 1720426399 675 LKAKRPEL 682
Cdd:cd05907 445 LKLKRPVI 452
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
89-698 |
4.08e-161 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 479.34 E-value: 4.08e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 89 DVRTMYDGFQRGIQVSNNGPCLGSRKPNQ----PYEWISYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIV 164
Cdd:PLN02861 41 DIDSPWQFFSDAVKKYPNNQMLGRRQVTDskvgPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDR--CGIYGSNCPEWIIA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 165 EQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFADKPEKAKLLleGVENKLTPCLKIIVIMDSYGSDLVERGKKCGV 244
Cdd:PLN02861 119 MEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKISSIL--SCLPKCSSNLKTIVSFGDVSSEQKEEAEELGV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 245 EIISLKALEDLGRVNRVKPkPPEPEDLAIICFTSGTTGNPKGAMITHQNIINDC---SGFIKATESALTlnASDTQISYL 321
Cdd:PLN02861 197 SCFSWEEFSLMGSLDCELP-PKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVlstDHLLKVTDRVAT--EEDSYFSYL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 322 PLAHMYEQQLQCVMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLlnrmFDRIFG------QANTSLKRWLLDFAS 395
Cdd:PLN02861 274 PLAHVYDQVIETYCISKGASIGFWQGDIRYLMEDVQALKPTIFCGVPRV----YDRIYTgimqkiSSGGMLRKKLFDFAY 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 396 KRKEAELRSGIVRNNS--LWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLP 473
Cdd:PLN02861 350 NYKLGNLRKGLKQEEAspRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGCFTSIA 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 474 GDWT-AGHVGAPMPCNYVKLVDVEEMNY--LASKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGT 550
Cdd:PLN02861 430 NVFSmVGTVGVPMTTIEARLESVPEMGYdaLSDVPRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGA 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 551 LKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAVVVPDVESLPSWAQKRGLQGSFEELCRNKD 630
Cdd:PLN02861 509 MKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLK 588
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720426399 631 INKAILDDLLKLGKEAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYATIK 698
Cdd:PLN02861 589 ARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYSEAK 656
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
88-698 |
3.37e-160 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 477.21 E-value: 3.37e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 88 DDVRTMYDGFQRGIQVSNNGPCLGSR-----KPNQpYEWISYKEVAELAECIGSGLIQKGFKpcSEQFIGLFSQNRPEWV 162
Cdd:PLN02614 42 EGMDSCWDVFRMSVEKYPNNPMLGRReivdgKPGK-YVWQTYQEVYDIVIKLGNSLRSVGVK--DEAKCGIYGANSPEWI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 163 IVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFADKpEKAKLLLEGVENKlTPCLKIIVIMDSYGSDLVERGKKC 242
Cdd:PLN02614 119 ISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEE-KKISELFKTCPNS-TEYMKTVVSFGGVSREQKEEAETF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 243 GVEIISLKALEDLGRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKATESA-LTLNASDTQISYL 321
Cdd:PLN02614 197 GLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSAnAALTVKDVYLSYL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 322 PLAHMYEQQLQCVMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIfgQANTS----LKRWLLDFASKR 397
Cdd:PLN02614 277 PLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGL--QKKLSdggfLKKFVFDSAFSY 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 398 KEAELRSGI--VRNNSLWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGD 475
Cdd:PLN02614 355 KFGNMKKGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDE 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 476 W-TAGHVGAPMPCNYVKLVDVEEMNY--LASKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLK 552
Cdd:PLN02614 435 LdMLGTVGPPVPNVDIRLESVPEMEYdaLASTPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMK 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 553 IIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAVVVPDVESLPSWAQKRGLQGSFEELCRNKDIN 632
Cdd:PLN02614 514 IIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAK 593
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720426399 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 |
1.50e-157 |
|
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: 464.77 E-value: 1.50e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 118 PYEWISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELS 197
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLVELGLKP--GDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 198 VIFADkpekaklllegvenkltpclkiivimdsygsdlvergkkcgveiislkaledlgrvnrvkpkpPEPEDLAIICFT 277
Cdd:cd17639 80 AIFTD---------------------------------------------------------------GKPDDLACIMYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 278 SGTTGNPKGAMITHQNIINDCSGFIKATESalTLNASDTQISYLPLAHMYEQQLQCVMLCHGAKIGFfqGDIRLLMD--- 354
Cdd:cd17639 97 SGSTGNPKGVMLTHGNLVAGIAGLGDRVPE--LLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDksk 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 355 -----DLKVLQPTIFPVVPRLLNRMFDRIFGQANT--SLKRWLLDFASKRKEAELRSGIvrNNSLWDKLIFHKIQSSLGG 427
Cdd:cd17639 173 rgckgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPmgGLKRTLFWTAYQSKLKALKEGP--GTPLLDELVFKKVRAALGG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 428 KVRLMITGAAPVSATVLTFLRTALgCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDVEEMNYLASKGE- 506
Cdd:cd17639 251 RLRYMLSGGAPLSADTQEFLNIVL-CPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDKPPp 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 507 -GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVA 585
Cdd:cd17639 330 rGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVN 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 586 QVFVHGESLQAFLIAVVVPDVESLPSWAQKRGL-QGSFEELCRNKDINKAILDDLLKLGKEAGLKPFEQVKGIAVHPELF 664
Cdd:cd17639 410 NICVYADPDKSYPVAIVVPNEKHLTKLAEKHGViNSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEW 489
|
570
....*....|....*
gi 1720426399 665 SIDNGLLTPTLKAKR 679
Cdd:cd17639 490 TPENGLVTAAQKLKR 504
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
89-697 |
7.84e-155 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 463.52 E-value: 7.84e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 89 DVRTMYDGFQRGIQVSNNGPCLGSRKPNQ----PYEWISYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIV 164
Cdd:PLN02430 40 DITTAWDIFSKSVEKYPDNKMLGWRRIVDgkvgPYMWKTYKEVYEEVLQIGSALRASGAEPGSR--VGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 165 EQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA-DKpeKAKLLLEGvENKLTPCLKIIVIMDSYGSDLVERGKKCG 243
Cdd:PLN02430 118 MEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVqDK--KIKELLEP-DCKSAKRLKAIVSFTSVTEEESDKASQIG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 244 VEIISLKALEDLGRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIINDCSG---FIKATESALTLNasDTQISY 320
Cdd:PLN02430 195 VKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGvdlFMEQFEDKMTHD--DVYLSF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 321 LPLAHMYEQQLQCVMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFG--QANTSLKRWLLDFASKRK 398
Cdd:PLN02430 273 LPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYKYK 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 399 EAELRSGIVRNNS--LWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDW 476
Cdd:PLN02430 353 LAWMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEM 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 477 TA-GHVGAPMPCNYVKLVDVEEMNY--LASKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKI 553
Cdd:PLN02430 433 CMlGTVGAPAVYNELRLEEVPEMGYdpLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKI 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 554 IDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAVVVPDVESLPSWAQKRGLQGSFEELCRNKDINK 633
Cdd:PLN02430 512 IDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKE 591
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720426399 634 AILDDLLKLGKEAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYATI 697
Cdd:PLN02430 592 HILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMYRKL 655
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
118-695 |
1.45e-137 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 419.91 E-value: 1.45e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 118 PYEWISYKEVAELAECIGSGLIQKGFKpcSEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELS 197
Cdd:PLN02387 103 EYEWITYGQVFERVCNFASGLVALGHN--KEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVT 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 198 VIFADKPEKAKLLleGVENKLTPCLKIIVIMDSYGSDLVERGKKCGVEIISLKALEDLGRVNRVKPKPPEPEDLAIICFT 277
Cdd:PLN02387 181 TVICDSKQLKKLI--DISSQLETVKRVIYMDDEGVDSDSSLSGSSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYT 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 278 SGTTGNPKGAMITHQNIIndcsgfikATESALT-----LNASDTQISYLPLAHMYEQQLQCVMLCHGAKIGFfqGDIRLL 352
Cdd:PLN02387 259 SGSTGLPKGVMMTHGNIV--------ATVAGVMtvvpkLGKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 353 MD-----------DLKVLQPTIFPVVPRLLNRMFDRIFGQANTS--LKRWLLDFASKRKEAELR------SGIVRnnSLW 413
Cdd:PLN02387 329 TDtsnkikkgtkgDASALKPTLMTAVPAILDRVRDGVRKKVDAKggLAKKLFDIAYKRRLAAIEgswfgaWGLEK--LLW 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 414 DKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLV 493
Cdd:PLN02387 407 DALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLV 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 494 DVEEMNYLASKG---EGEVCVKGANVFKGYLKDPARTAEA--LDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAQG 566
Cdd:PLN02387 487 SWEEGGYLISDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHG 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 567 EYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAVVVPDVESLPSWAQKRGLQ-GSFEELCRNKDINKAILDDLLKLGKE 645
Cdd:PLN02387 567 EYVSLGKVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKA 646
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1720426399 646 AGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYA 695
Cdd:PLN02387 647 ARLEKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
118-564 |
7.56e-129 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 387.82 E-value: 7.56e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 118 PYEWISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELS 197
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRALGVGK--GDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 198 VIFADKPEKAKLLLEGVENKLTPCLKIIVIMDSygsdlvergkkcGVEIISLKALEDLGRVNRVKPKPPEPEDLAIICFT 277
Cdd:pfam00501 96 VLITDDALKLEELLEALGKLEVVKLVLVLDRDP------------VLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 278 SGTTGNPKGAMITHQNIINDCSGFIKATESALTLNASDTQISYLPLAHMYEQQLQC-VMLCHGAKIGFFQGDIRL----L 352
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLlGPLLAGATVVLPPGFPALdpaaL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 353 MDDLKVLQPTIFPVVPRLLNRMFDrifgqantslkrwlldfaSKRKEAELRSGivrnnslwdklifhkiqsslggkVRLM 432
Cdd:pfam00501 244 LELIERYKVTVLYGVPTLLNMLLE------------------AGAPKRALLSS-----------------------LRLV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 433 ITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDW---TAGHVGAPMPCNYVKLVDVEEMNYLASKGEGEV 509
Cdd:pfam00501 283 LSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGEL 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1720426399 510 CVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLA 564
Cdd:pfam00501 363 CVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
122-695 |
6.32e-98 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 316.53 E-value: 6.32e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 122 ISYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLTKGSN--VAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 202 DKpEKAKLLLEGVENKLTPCLKIIvimdsYGSDLVERGKKCGVEIISLKALEDLGR--VNRVKPKPPEP-EDLAIICFTS 278
Cdd:PTZ00216 200 NG-KNVPNLLRLMKSGGMPNTTII-----YLDSLPASVDTEGCRLVAWTDVVAKGHsaGSHHPLNIPENnDDLALIMYTS 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 279 GTTGNPKGAMITHQNIINDCSGF-IKATESALTLNASDTQISYLPLAHMYEQQLQCVMLCHGAKIGFfqGDIRLLMD--- 354
Cdd:PTZ00216 274 GTTGDPKGVMHTHGSLTAGILALeDRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRTLTDtfa 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 355 ----DLKVLQPTIFPVVPRLlnrmFDRI----------FGqantSLKRWLLDFASKRKEAELRSGivRNNSLWDKLIFHK 420
Cdd:PTZ00216 352 rphgDLTEFRPVFLIGVPRI----FDTIkkaveaklppVG----SLKRRVFDHAYQSRLRALKEG--KDTPYWNEKVFSA 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 421 IQSSLGGKVRLMITGAAPVSATVLTFLRTALGCqFYEGYGQTECTagCC--LSLPGDWTAGHVGAPMPCNYVKLVDVEEM 498
Cdd:PTZ00216 422 PRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTETV--CCggIQRTGDLEPNAVGQLLKGVEMKLLDTEEY 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 499 NYlASKGE--GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIEN 576
Cdd:PTZ00216 499 KH-TDTPEprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEA 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 577 IYLRSEAVAQ----VFVHgeSLQAFLIAVVVPDVESLPSWAQKRGLQGSFEELCRNKDINKAILDDLLKLGKEAGLKPFE 652
Cdd:PTZ00216 578 LYGQNELVVPngvcVLVH--PARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFE 655
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1720426399 653 QVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYA 695
Cdd:PTZ00216 656 IVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELFA 698
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
117-680 |
3.10e-89 |
|
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: 286.95 E-value: 3.10e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 117 QPYEWISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAEL 196
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKA--GEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 197 SVIFadkpekaklllegVENkltpclkiivimdsygsdlvergkkcgveiislkaledlgrvnrvkpkppEPEDLAIICF 276
Cdd:cd17640 79 VALV-------------VEN--------------------------------------------------DSDDLATIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 277 TSGTTGNPKGAMITHQNIINDcsgfIKATESALTLNASDTQISYLPLAHMYEQQLQCVMLCHGAKIGFfqGDIRLLMDDL 356
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLLHQ----IRSLSDIVPPQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDDL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 357 KVLQPTIFPVVPRLlnrmfdrifgqantslkrWlldfaskrkEAeLRSGI---VRNNSLWDKLIFHKIQSslGGKVRLMI 433
Cdd:cd17640 170 KRVKPHYIVSVPRL------------------W---------ES-LYSGIqkqVSKSSPIKQFLFLFFLS--GGIFKFGI 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 434 TGAAPVSATVLTFLRtALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDVEEMNYLASKGEGEVCVKG 513
Cdd:cd17640 220 SGGGALPPHVDTFFE-AIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 514 ANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGES 593
Cdd:cd17640 299 PQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQD 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 594 lQAFLIAVVVPDVESLPSWAQKRG--LQGSFEELCRNKDINKAILDDLLK-LGKEAGLKPFEQVKGIAVHPELFsIDNGL 670
Cdd:cd17640 379 -QKRLGALIVPNFEELEKWAKESGvkLANDRSQLLASKKVLKLYKNEIKDeISNRPGFKSFEQIAPFALLEEPF-IENGE 456
|
570
....*....|
gi 1720426399 671 LTPTLKAKRP 680
Cdd:cd17640 457 MTQTMKIKRN 466
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
119-679 |
3.88e-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: 266.64 E-value: 3.88e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 119 YEWISYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSV 198
Cdd:cd05932 4 VVEFTWGEVADKARRLAAALRALGLEPGSK--IALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 199 IFADKPEKAKLLLEGVENKLTPCLKII--VIMDSYG-SDLVERGKkcgveiislkALEDlgrvnrvKPkPPEPEDLAIIC 275
Cdd:cd05932 82 LFVGKLDDWKAMAPGVPEGLISISLPPpsAANCQYQwDDLIAQHP----------PLEE-------RP-TRFPEQLATLI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 276 FTSGTTGNPKGAMITHQNIINDCSGFIKAtesaLTLNASDTQISYLPLAHMYEQqlqcVMLCHGAKIG----FFQGDIRL 351
Cdd:cd05932 144 YTSGTTGQPKGVMLTFGSFAWAAQAGIEH----IGTEENDRMLSYLPLAHVTER----VFVEGGSLYGgvlvAFAESLDT 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 352 LMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTSLKRWLLDFaskrkeaelrsgivrnnSLWDKLIFHKIQSSLG-GKVR 430
Cdd:cd05932 216 FVEDVQRARPTLFFSVPRLWTKFQQGVQDKIPQQKLNLLLKI-----------------PVVNSLVKRKVLKGLGlDQCR 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 431 LMITGAAPVSATVLTFLRTaLGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDveemnylaskgEGEVC 510
Cdd:cd05932 279 LAGCGSAPVPPALLEWYRS-LGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEIL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 511 VKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVH 590
Cdd:cd05932 347 VRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVI 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 591 GESLQAFLIAVVVPDVESLPSWAQKRG-LQGSFEELCrnKDINKAilddllklgkeagLKPFEQVKGIAVHPELFSIDNG 669
Cdd:cd05932 427 GSGLPAPLALVVLSEEARLRADAFARAeLEASLRAHL--ARVNST-------------LDSHEQLAGIVVVKDPWSIDNG 491
|
570
....*....|
gi 1720426399 670 LLTPTLKAKR 679
Cdd:cd05932 492 ILTPTLKIKR 501
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
114-694 |
9.29e-72 |
|
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: 244.19 E-value: 9.29e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 114 KPNQPYEWISYKEVAELAECIGSGLIQKGFkpcsEQF--IGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIV 191
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLKLGL----ERFhgVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 192 NKAELSVIFADKPEKAKLLLEgVENKLtPCLKIIVImdsYGSDLVErgKKCGVeiISLKALEDLGRvnrvkpKPPEPEDL 271
Cdd:cd05933 77 ETSEANILVVENQKQLQKILQ-IQDKL-PHLKAIIQ---YKEPLKE--KEPNL--YSWDEFMELGR------SIPDEQLD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 272 AII-------C----FTSGTTGNPKGAMITHQNIINDcsgfIKATESALTLNASDTQ----ISYLPLAHMYEQQLQcVML 336
Cdd:cd05933 142 AIIssqkpnqCctliYTSGTTGMPKGVMLSHDNITWT----AKAASQHMDLRPATVGqesvVSYLPLSHIAAQILD-IWL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 337 C--HGAKIGFFQGDIR--LLMDDLKVLQPTIFPVVPRLLNRMFDRI--FGQANTSLKRWLLDFAsKRKEAE-------LR 403
Cdd:cd05933 217 PikVGGQVYFAQPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkaVGAKSGTLKRKIASWA-KGVGLEtnlklmgGE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 404 SGIVRNNSLWDKLIFHKIQSSLG-GKVRLMITGAAPVSATVLTFLrTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVG 482
Cdd:cd05933 296 SPSPLFYRLAKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 483 APMPCNYVKLVDVEemnylaSKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFK 562
Cdd:cd05933 375 KALPGCKTKIHNPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELII 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 563 LAQGEYIAPEKIEN-IYLRSEAVAQVFVHGESLQaFLIAVVVPDVESLPswaqKRGLQG---SFE--ELCRNKDINKAIL 636
Cdd:cd05933 449 TAGGENVPPVPIEDaVKKELPIISNAMLIGDKRK-FLSMLLTLKCEVNP----ETGEPLdelTEEaiEFCRKLGSQATRV 523
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720426399 637 DDLLKLGKEAGLKPFEQ---------------VKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELY 694
Cdd:cd05933 524 SEIAGGKDPKVYEAIEEgikrvnkkaisnaqkIQKWVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
122-616 |
1.24e-71 |
|
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: 239.71 E-value: 1.24e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 122 ISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:COG0318 25 LTYAELDARARRLAAALRALGVGP--GDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 202 dkpekaklllegvenkltpclkiivimdsygsdlvergkkcgveiislkaledlgrvnrvkpkppepedlAIICFTSGTT 281
Cdd:COG0318 103 ----------------------------------------------------------------------ALILYTSGTT 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 282 GNPKGAMITHQNIINDCSGFIkateSALTLNASDTQISYLPLAHMYEQQLQCVM-LCHGAKI----GFfqgDIRLLMDDL 356
Cdd:COG0318 113 GRPKGVMLTHRNLLANAAAIA----AALGLTPGDVVLVALPLFHVFGLTVGLLApLLAGATLvllpRF---DPERVLELI 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 357 KVLQPTIFPVVPRLLNRMFDRifgqantslkrwlldfaSKRKEAELRSgivrnnslwdklifhkiqsslggkVRLMITGA 436
Cdd:COG0318 186 ERERVTVLFGVPTMLARLLRH-----------------PEFARYDLSS------------------------LRLVVSGG 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 437 APVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTA--GHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGA 514
Cdd:COG0318 225 APLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGRPLPGVEVRIVD-EDGRELPPGEVGEIVVRGP 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 515 NVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQVFV----- 589
Cdd:COG0318 304 NVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEVLAAHPGVAEAAVvgvpd 381
|
490 500 510
....*....|....*....|....*....|.
gi 1720426399 590 --HGESLQAFLIAV--VVPDVESLPSWAQKR 616
Cdd:COG0318 382 ekWGERVVAFVVLRpgAELDAEELRAFLRER 412
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
148-672 |
1.86e-67 |
|
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: 232.35 E-value: 1.86e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 148 EQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFADkPEKAKLLLEGVENKLTPclKIIVI 227
Cdd:cd17632 93 GDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVS-AEHLDLAVEAVLEGGTP--PRLVV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 228 MDSYGSDLVER-----------GKKCGVEIISLKALEDLGrVNRVKPKPPEPED--LAIICFTSGTTGNPKGAMITHQNI 294
Cdd:cd17632 170 FDHRPEVDAHRaalesarerlaAVGIPVTTLTLIAVRGRD-LPPAPLFRPEPDDdpLALLIYTSGSTGTPKGAMYTERLV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 295 IN---DCSGFIKATE-SALTLNasdtqisYLPLAHMYEQQLQCVMLCHGAkIGFFQG--DIRLLMDDLKVLQPTIFPVVP 368
Cdd:cd17632 249 ATfwlKVSSIQDIRPpASITLN-------FMPMSHIAGRISLYGTLARGG-TAYFAAasDMSTLFDDLALVRPTELFLVP 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 369 RLLNRMFDRIfgQAntSLKRWLLDFA-----SKRKEAELRsgivrnnslwdklifhkiQSSLGGKVRLMITGAAPVSATV 443
Cdd:cd17632 321 RVCDMLFQRY--QA--ELDRRSVAGAdaetlAERVKAELR------------------ERVLGGRLLAAVCGSAPLSAEM 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 444 LTFLRTALGCQFYEGYGQTEctAGCCLSLpgdwtaGHVGAPMPCNYvKLVDVEEMNYLASKG---EGEVCVKGANVFKGY 520
Cdd:cd17632 379 KAFMESLLDLDLHDGYGSTE--AGAVILD------GVIVRPPVLDY-KLVDVPELGYFRTDRphpRGELLVKTDTLFPGY 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 521 LKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIA 600
Cdd:cd17632 450 YKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNSERAYLLA 529
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720426399 601 VVVPdveslpswAQKRGLQGSFEELcrnkdiNKAILDDLLKLGKEAGLKPFEQVKGIAVHPELFSIDNGLLT 672
Cdd:cd17632 530 VVVP--------TQDALAGEDTARL------RAALAESLQRIAREAGLQSYEIPRDFLIETEPFTIANGLLS 587
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
122-679 |
4.33e-66 |
|
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: 228.08 E-value: 4.33e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 122 ISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGR--GDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 202 DKPEKAKLLLEgVENKLtPCLKIIVIMDSYGSDLVERGKkcgveIISLKALEDLGR-VNRVKPKPPE-------PEDLAI 273
Cdd:cd17641 90 EDEEQVDKLLE-IADRI-PSVRYVIYCDPRGMRKYDDPR-----LISFEDVVALGRaLDRRDPGLYErevaagkGEDVAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 274 ICFTSGTTGNPKGAMITHQNIINDCSGFIKATEsaltLNASDTQISYLPLAHMYEQQLQCVM-LCHGAKIGFFQgDIRLL 352
Cdd:cd17641 163 LCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADP----LGPGDEYVSVLPLPWIGEQMYSVGQaLVCGFIVNFPE-EPETM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 353 MDDLKVLQPTIFPVVPRLLNRM--FDRIFGQANTSLKRWLLDF--------ASKRKEAELRSGIVRNNS-LWDKLIFHKI 421
Cdd:cd17641 238 MEDLREIGPTFVLLPPRVWEGIaaDVRARMMDATPFKRFMFELgmklglraLDRGKRGRPVSLWLRLASwLADALLFRPL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 422 QSSLG-GKVRLMITGAAPVSATVLTFLRtALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDVeemny 500
Cdd:cd17641 318 RDRLGfSRLRSAATGGAALGPDTFRFFH-AIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEV----- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 501 laskgeGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIEN---- 576
Cdd:cd17641 392 ------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENklkf 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 577 -IYLRsEAVaqVFVHGeslQAFLIAVVVPDVESLPSWAQKRGLQ-GSFEELCRNKDINKAILDDLLKLGKEagLKPFEQV 654
Cdd:cd17641 466 sPYIA-EAV--VLGAG---RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKVNAS--LPEAQRI 537
|
570 580
....*....|....*....|....*
gi 1720426399 655 KGIAVHPELFSIDNGLLTPTLKAKR 679
Cdd:cd17641 538 RRFLLLYKELDADDGELTRTRKVRR 562
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
122-679 |
3.18e-64 |
|
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: 220.39 E-value: 3.18e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 122 ISYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDR--VALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 202 DkpekaklllegvenkltpclkiivimdsygsdlvergkkcgveiislkaledlgrvnrvkpkppEPEDLAIICFTSGTT 281
Cdd:cd05914 86 S----------------------------------------------------------------DEDDVALINYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 282 GNPKGAMITHQNIINDcsgfIKATESALTLNASDTQISYLPLAHMYEQQLQCVM-LCHGAKIGFFQGDIRLLMDDLKVLQ 360
Cdd:cd05914 102 GNSKGVMLTYRNIVSN----VDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLpLLNGAHVVFLDKIPSAKIIALAFAQ 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 361 PTIFPVVPRLLNRMFDRIFGQANTSLKRWLLdfaskrkeaeLRSGIVRNNSLWDKLIFHKIQSSLGGKVRLMITGAAPVS 440
Cdd:cd05914 178 VTPTLGVPVPLVIEKIFKMDIIPKLTLKKFK----------FKLAKKINNRKIRKLAFKKVHEAFGGNIKEFVIGGAKIN 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 441 ATVLTFLRTaLGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPmpcnyVKLVDVEEMNYLASKGEGEVCVKGANVFKGY 520
Cdd:cd05914 248 PDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKV-----IDGVEVRIDSPDPATGEGEIIVRGPNVMKGY 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 521 LKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVA--QVFV-HGEslqaf 597
Cdd:cd05914 322 YKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLesLVVVqEKK----- 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 598 LIAVVVPDveslPSWAQKRGLQgsfeelcrNKDINKAILDDLL-KLGKEagLKPFEQVKGIAVHPELFSidnglLTPTLK 676
Cdd:cd05914 397 LVALAYID----PDFLDVKALK--------QRNIIDAIKWEVRdKVNQK--VPNYKKISKVKIVKEEFE-----KTPKGK 457
|
...
gi 1720426399 677 AKR 679
Cdd:cd05914 458 IKR 460
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
270-616 |
1.62e-63 |
|
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: 214.46 E-value: 1.62e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 270 DLAIICFTSGTTGNPKGAMITHQNIIndcsGFIKATESALTLNASDTQISYLPLAHMYEQQLQCVMLCHGAKI----GFF 345
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLL----AAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVvllpKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 346 QGDIRLLMDDLKVlqpTIFPVVPRLLNRMFDRIfgqantslkrwlldfasKRKEAELRSgivrnnslwdklifhkiqssl 425
Cdd:cd04433 77 PEAALELIEREKV---TILLGVPTLLARLLKAP-----------------ESAGYDLSS--------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 426 ggkVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWT--AGHVGAPMPCNYVKLVDVEEmNYLAS 503
Cdd:cd04433 116 ---LRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDPDG-GELPP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 504 KGEGEVCVKGANVFKGYLKDPARTAEAlDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEA 583
Cdd:cd04433 192 GEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPG 269
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1720426399 584 VAQVFVHG---ESLQAFLIAVVVP------DVESLPSWAQKR 616
Cdd:cd04433 270 VAEAAVVGvpdPEWGERVVAVVVLrpgadlDAEELRAHVRER 311
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
122-591 |
1.95e-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: 1.95e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 122 ISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKK--GDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 202 DKPEKAKLLleGVENKLTPCLKIIVIMDSygsdlvergKKCGVEIISLKALEDLGRVNRVKPKPPE-PEDLAIICFTSGT 280
Cdd:cd05911 89 DPDGLEKVK--EAAKELGPKDKIIVLDDK---------PDGVLSIEDLLSPTLGEEDEDLPPPLKDgKDDTAAILYSSGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 281 TGNPKGAMITHQNIINDCSgFIKATESaLTLNASDTQISYLPLAHMYEQQLQCVMLCHGAK-IGFFQGDIRLLMDDLKVL 359
Cdd:cd05911 158 TGLPKGVCLSHRNLIANLS-QVQTFLY-GNDGSNDVILGFLPLYHIYGLFTTLASLLNGATvIIMPKFDSELFLDLIEKY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 360 QPTIFPVVPRLLNRMFdrifgqantslkrwlldfaskrkeaelRSGIVRNNSLwdklifhkiqSSLggkvRLMITGAAPV 439
Cdd:cd05911 236 KITFLYLVPPIAAALA---------------------------KSPLLDKYDL----------SSL----RVILSGGAPL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 440 SATVLTFLRTALG-CQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPcNY-VKLVDVEEMNYLASKGEGEVCVKGANVF 517
Cdd:cd05911 275 SKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLP-NVeAKIVDDDGKDSLGPNEPGEICVRGPQVM 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720426399 518 KGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:cd05911 354 KGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAVLLEHPGVADAAVIG 426
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
120-609 |
7.65e-61 |
|
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: 211.27 E-value: 7.65e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 120 EWISYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVI 199
Cdd:cd05936 23 RKLTYRELDALAEAFAAGLQNLGVQPGDR--VALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 200 FADKPEKaklllegvenkltpclkiivimdsygsDLVERGKKcgveiislkaledlgrvnRVKPKPPEPEDLAIICFTSG 279
Cdd:cd05936 101 IVAVSFT---------------------------DLLAAGAP------------------LGERVALTPEDVAVLQYTSG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 280 TTGNPKGAMITHQNIINDCSGFIKATESALTlnASDTQISYLPLAHMYEQQLQCV-MLCHGAKIGFFQG-DIRLLMDDLK 357
Cdd:cd05936 136 TTGVPKGAMLTHRNLVANALQIKAWLEDLLE--GDDVVLAALPLFHVFGLTVALLlPLALGATIVLIPRfRPIGVLKEIR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 358 VLQPTIFPVVPRLLNRMFDrifgqantslkrwlldfASKRKEAELRSgivrnnslwdklifhkiqsslggkVRLMITGAA 437
Cdd:cd05936 214 KHRVTIFPGVPTMYIALLN-----------------APEFKKRDFSS------------------------LRLCISGGA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 438 PVSATVLTFLRTALGCQFYEGYGQTECT-AGCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANV 516
Cdd:cd05936 253 PLPVEVAERFEELTGVPIVEGYGLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVD-DDGEELPPGEVGELWVRGPQV 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 517 FKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFV------- 589
Cdd:cd05936 332 MKGYWNRPEETAEAF-VDGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGGFNVYPREVEEVLYEHPAVAEAAVvgvpdpy 409
|
490 500
....*....|....*....|
gi 1720426399 590 HGESLQAFliaVVVPDVESL 609
Cdd:cd05936 410 SGEAVKAF---VVLKEGASL 426
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
122-616 |
5.83e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 207.45 E-value: 5.83e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 122 ISYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGKGDR--VAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 202 dkpekAKLLLeGVENKLT---PCLKIIVIMDSYGSDLVERGKKCGVEIISLKalEDLGRVNRVKPkppepEDLAIICFTS 278
Cdd:PRK07656 109 -----LGLFL-GVDYSATtrlPALEHVVICETEEDDPHTEKMKTFTDFLAAG--DPAERAPEVDP-----DDVADILFTS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 279 GTTGNPKGAMITHQNIINDcsgfikATESA--LTLNASDTQISYLPLAHMYEQQ---LQCVMlcHGAKIgffqgDIRLLM 353
Cdd:PRK07656 176 GTTGRPKGAMLTHRQLLSN------AADWAeyLGLTEGDRYLAANPFFHVFGYKagvNAPLM--RGATI-----LPLPVF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 354 DDLKVLQ------PTIFPVVPRLLNRMFDrifgqantslkrwlldfASKRKEAELRSgivrnnslwdklifhkiqsslgg 427
Cdd:PRK07656 243 DPDEVFRlieterITVLPGPPTMYNSLLQ-----------------HPDRSAEDLSS----------------------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 428 kVRLMITGAAPVSATVLTFLRTALGCQ-FYEGYGQTECTAGCCLSLPGD---WTAGHVGAPMPCNYVKLVDvEEMNYLAS 503
Cdd:PRK07656 283 -LRLAVTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIAGVENKIVN-ELGEEVPV 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 504 KGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEA 583
Cdd:PRK07656 361 GEVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IVGGFNVYPAEVEEVLYEHPA 439
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1720426399 584 VAQVFV-------HGESLQAFLIAVVVPDV--ESLPSWAQKR 616
Cdd:PRK07656 440 VAEAAVigvpderLGEVGKAYVVLKPGAELteEELIAYCREH 481
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
122-605 |
8.62e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 196.18 E-value: 8.62e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 122 ISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:PRK06187 32 TTYAELDERVNRLANALRALGVKK--GDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 202 DkPEKAKLLlEGVENKLTPCLKIIVIMDSYGSDLVERGKkcgveiislkALEDLgrVNRVKPKPPEPE----DLAIICFT 277
Cdd:PRK06187 110 D-SEFVPLL-AAILPQLPTVRTVIVEGDGPAAPLAPEVG----------EYEEL--LAAASDTFDFPDidenDAAAMLYT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 278 SGTTGNPKGAMITHQNIIndcsGFIKATESALTLNASDTQISYLPLAHMYEQQLQCVMLCHGAKI---GFFqgDIRLLMD 354
Cdd:PRK06187 176 SGTTGHPKGVVLSHRNLF----LHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLALMAGAKQvipRRF--DPENLLD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 355 DLKVLQPTIFPVVPRLLNRMFdrifgQANTSLKRWLldfaskrkeaelrsgivrnnslwdklifhkiqSSLggkvRLMIT 434
Cdd:PRK06187 250 LIETERVTFFFAVPTIWQMLL-----KAPRAYFVDF--------------------------------SSL----RLVIY 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 435 GAAPVSATVLTFLRTALGCQFYEGYGQTECT-AGCCL----SLPGDWT-AGHVGAPMPCNYVKLVDvEEMNYLASKGE-- 506
Cdd:PRK06187 289 GGAALPPALLREFKEKFGIDLVQGYGMTETSpVVSVLppedQLPGQWTkRRSAGRPLPGVEARIVD-DDGDELPPDGGev 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 507 GEVCVKGANVFKGYLKDPARTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQ 586
Cdd:PRK06187 368 GEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIKDVIISG-GENIYPRELEDALYGHPAVAE 445
|
490 500
....*....|....*....|
gi 1720426399 587 VfvhgeslqafliAVV-VPD 605
Cdd:PRK06187 446 V------------AVIgVPD 453
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
234-692 |
3.37e-43 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 166.82 E-value: 3.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 234 DLVERGKKCGVEIISLKALEDlGRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIIN------DCSGFIKATes 307
Cdd:PTZ00342 270 DLKEKAKKLGISIILFDDMTK-NKTTNYKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNtvvplcKHSIFKKYN-- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 308 altlnaSDTQISYLPLAHMYEQQLQCVMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQAN--TS 385
Cdd:PTZ00342 347 ------PKTHLSYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINnlPP 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 386 LKRWLLdfaskRKEAELRSGivRNNSLWDKL---IFH---KIQSSLGGKVRLMITGAAPVSATVLTFLRTALGCQFYEGY 459
Cdd:PTZ00342 421 LKRFLV-----KKILSLRKS--NNNGGFSKFlegITHissKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGY 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 460 GQTECTAGCCLSLPGDWTAGHVGAPM-PCNYVKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLH 538
Cdd:PTZ00342 494 GLTETTGPIFVQHADDNNTESIGGPIsPNTKYKVRTWETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFK 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 539 TGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAVVVPDVESLPSWAQKRGL 618
Cdd:PTZ00342 574 TGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGDDSMDGPLAIISVDKYLLFKCLKDDNM 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 619 ---QGSFEELCRNK----DINKAILDD-----LLKLGKEAGLKPFEQVKGIAVHPELFSIDNgLLTPTLKAKRPELRNYF 686
Cdd:PTZ00342 654 lesTGINEKNYLEKltdeTINNNIYVDyvkgkMLEVYKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKRFYVFKDY 732
|
....*.
gi 1720426399 687 RSQIDE 692
Cdd:PTZ00342 733 AFFIDQ 738
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
122-605 |
2.62e-42 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 159.31 E-value: 2.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 122 ISYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFa 201
Cdd:cd17631 21 LTYAELDERVNRLAHALRALGVAKGDR--VAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 202 dkpekaklllegvenkltpclkiivimdsygsdlvergkkcgveiislkaledlgrvnrvkpkppepEDLAIICFTSGTT 281
Cdd:cd17631 98 -------------------------------------------------------------------DDLALLMYTSGTT 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 282 GNPKGAMITHQNIINDCSGFIkateSALTLNASDTQISYLPLAHMYEQQLQCVM-LCHGAKI----GFfqgDIRLLMDDL 356
Cdd:cd17631 111 GRPKGAMLTHRNLLWNAVNAL----AALDLGPDDVLLVVAPLFHIGGLGVFTLPtLLRGGTVvilrKF---DPETVLDLI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 357 KVLQPTIFPVVPRLLNRMFDRifgqantslkrwlldfaSKRKEAELrsgivrnnslwdklifhkiqSSLggkvRLMITGA 436
Cdd:cd17631 184 ERHRVTSFFLVPTMIQALLQH-----------------PRFATTDL--------------------SSL----RAVIYGG 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 437 APVSATVLTFLRtALGCQFYEGYGQTECTAGCCLSLPGDW--TAGHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGA 514
Cdd:cd17631 223 APMPERLLRALQ-ARGVKFVQGYGMTETSPGVTFLSPEDHrrKLGSAGRPVFFVEVRIVD-PDGREVPPGEVGEIVVRGP 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 515 NVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEAVAQVFV----- 589
Cdd:cd17631 301 HVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDVLYEHPAVAEVAVigvpd 378
|
490
....*....|....*...
gi 1720426399 590 --HGESlqafLIAVVVPD 605
Cdd:cd17631 379 ekWGEA----VVAVVVPR 392
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
120-616 |
2.12e-40 |
|
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: 154.78 E-value: 2.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 120 EWISYKEVAELAECIGSGLIQKGFKPCSEQFIGLFsqNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVI 199
Cdd:cd05926 13 PALTYADLAELVDDLARQLAALGIKKGDRVAIALP--NGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 200 FADKPEkaklLLEGVENKLTPCLKII-VIMDSYGSDLVERGKkcgveiiSLKALEDLGRVNRvKPKPPEPEDLAIICFTS 278
Cdd:cd05926 91 LTPKGE----LGPASRAASKLGLAILeLALDVGVLIRAPSAE-------SLSNLLADKKNAK-SEGVPLPDDLALILHTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 279 GTTGNPKGAMITHQNIINDcsgfIKATESALTLNASDTQISYLPLAHMYeqQLQCVMLC---HGAKI----GFfqgDIRL 351
Cdd:cd05926 159 GTTGRPKGVPLTHRNLAAS----ATNITNTYKLTPDDRTLVVMPLFHVH--GLVASLLStlaAGGSVvlppRF---SAST 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 352 LMDDLKVLQPTIFPVVPRLLnrmfdrifgqantslkRWLLDFASKRKEAELrsgivrnnslwdklifhkiqsslgGKVRL 431
Cdd:cd05926 230 FWPDVRDYNATWYTAVPTIH----------------QILLNRPEPNPESPP------------------------PKLRF 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 432 MITGAAPVSATVLTFLRTALGCQFYEGYGQTE-CTAGCCLSLPGDW-TAGHVGAPmpcNYVKLVDV-EEMNYLASKGEGE 508
Cdd:cd05926 270 IRSCSASLPPAVLEALEATFGAPVLEAYGMTEaAHQMTSNPLPPGPrKPGSVGKP---VGVEVRILdEDGEILPPGVVGE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 509 VCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQ-- 586
Cdd:cd05926 347 ICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVLLSHPAVLEav 425
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1720426399 587 VF-----VHGESLQafliAVVVP------DVESLPSWAQKR 616
Cdd:cd05926 426 AFgvpdeKYGEEVA----AAVVLregasvTEEELRAFCRKH 462
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
124-644 |
1.53e-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: 151.45 E-value: 1.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 124 YKEVAELAECIGSGLIQKGfkpcseQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFADk 203
Cdd:TIGR01923 6 DCEAAHLAKALKAQGIRSG------SRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 204 pekAKLLLEGVEnkltpclkiivimdsygSDLVERGKKCGVEIISLKALEDLgrvnrvkpkppepEDLAIICFTSGTTGN 283
Cdd:TIGR01923 79 ---SLLEEKDFQ-----------------ADSLDRIEAAGRYETSLSASFNM-------------DQIATLMFTSGTTGK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 284 PKGAMITHQNIINDCSGfikateSALTLNA--SDTQISYLPLAHMYEQQLQCVMLCHGAKIGFFQGDIRLLmDDLKVLQP 361
Cdd:TIGR01923 126 PKAVPHTFRNHYASAVG------SKENLGFteDDNWLLSLPLYHISGLSILFRWLIEGATLRIVDKFNQLL-EMIANERV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 362 TIFPVVPRLLNRMFDRifGQANTSLKRWLLdfaskrkeaelrsgivrnnslwdklifhkiqsslggkvrlmitGAAPVSA 441
Cdd:TIGR01923 199 THISLVPTQLNRLLDE--GGHNENLRKILL-------------------------------------------GGSAIPA 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 442 TVLTFLRTaLGCQFYEGYGQTE-CTAGCCLSLPGDWTAGHVGAPMPCNYVKL-VDVEEmnylaskGEGEVCVKGANVFKG 519
Cdd:TIGR01923 234 PLIEEAQQ-YGLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIkVDNKE-------GHGEIMVKGANLMKG 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 520 YLkDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVhgeslqafli 599
Cdd:TIGR01923 306 YL-YQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVV---------- 373
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1720426399 600 aVVVPDVEslpsWAQKRGLQGSFeelcrNKDINKAILDDLL--KLGK 644
Cdd:TIGR01923 374 -VPKPDAE----WGQVPVAYIVS-----ESDISQAKLIAYLteKLAK 410
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
270-616 |
5.80e-39 |
|
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: 149.75 E-value: 5.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 270 DLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKATESAltlnASDTQISYLPLAHMYE--QQLQCVMLCHGAKI--GFF 345
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWT----EDDVLLHVLPLHHVHGlvNALLCPLFAGASVEflPKF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 346 ---QGDIRLLMDDLkvlqpTIFPVVPRllnrMFDRIFGQANTSLKrwllDFASKRKEAElrsgivrnnslwdklifhkiq 422
Cdd:cd05941 166 dpkEVAISRLMPSI-----TVFMGVPT----IYTRLLQYYEAHFT----DPQFARAAAA--------------------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 423 sslgGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTEctAGCCLSLP--GDWTAGHVGAPMPCNYVKLVDVEEMNY 500
Cdd:cd05941 212 ----ERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVDEETGEP 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 501 LASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK-HIFKlAQGEYIAPEKIENIYL 579
Cdd:cd05941 286 LPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEIERVLL 364
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1720426399 580 RSEAVAQVFVHGESLQAF---LIAVVVP-------DVESLPSWAQKR 616
Cdd:cd05941 365 AHPGVSECAVIGVPDPDWgerVVAVVVLragaaalSLEELKEWAKQR 411
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
122-589 |
6.37e-39 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 150.85 E-value: 6.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 122 ISYKE----VAELAECIGSGLIQKGfkpcseQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELS 197
Cdd:cd05904 33 LTYAElerrVRRLAAGLAKRGGRKG------DVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 198 VIFADkpekAKLLlegveNKLTPCLKIIVIMDSYGSDlvergkkcGVEIISLKALEDLGRVNRVKPKPpepEDLAIICFT 277
Cdd:cd05904 107 LAFTT----AELA-----EKLASLALPVVLLDSAEFD--------SLSFSDLLFEADEAEPPVVVIKQ---DDVAALLYS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 278 SGTTGNPKGAMITHQNIINDCSGFIKATESALTLNasDTQISYLPLAHMYEQQLQCV-MLCHGAKI----GFfqgDIRLL 352
Cdd:cd05904 167 SGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSE--DVFLCVLPMFHIYGLSSFALgLLRLGATVvvmpRF---DLEEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 353 MDDLKVLQPTIFPVVPRLLNRMfdrifgqantslkrwlldfaskrkeaeLRSGIVRNNSLwdklifhkiqSSLggkvRLM 432
Cdd:cd05904 242 LAAIERYKVTHLPVVPPIVLAL---------------------------VKSPIVDKYDL----------SSL----RQI 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 433 ITGAAPVSATVL-TFLRTALGCQFYEGYGQTECTAG---CCLSLPGDWTAGHVGAPMPCNYVKLVDVEEMNYLASKGEGE 508
Cdd:cd05904 281 MSGAAPLGKELIeAFRAKFPNVDLGQGYGMTESTGVvamCFAPEKDRAKYGSVGRLVPNVEAKIVDPETGESLPPNQTGE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 509 VCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVF 588
Cdd:cd05904 361 LWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEALLLSHPEILDAA 439
|
.
gi 1720426399 589 V 589
Cdd:cd05904 440 V 440
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
268-599 |
2.61e-36 |
|
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: 139.72 E-value: 2.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 268 PEDLAIICFTSGTTGNPKGAMITHQNIINDcsGFIkaTESALTLNASDTQISYLPLAHMYeqqlQCVM-----LCHGAKI 342
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNN--GYF--IGERLGLTEQDRLCIPVPLFHCF----GSVLgvlacLTHGATM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 343 GFfqgdIRLLMDDLKVLQ-------------PTIFPvvpRLLNRMFDRIFgqantslkrwllDFASkrkeaeLRSGIvrn 409
Cdd:cd05917 73 VF----PSPSFDPLAVLEaiekekctalhgvPTMFI---AELEHPDFDKF------------DLSS------LRTGI--- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 410 nslwdklifhkiqsslggkvrlmiTGAAPVSATVLTFLRTALGC-QFYEGYGQTECTAGCCLSLPGDWT---AGHVGAPM 485
Cdd:cd05917 125 ------------------------MAGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDSIekrVNTVGRIM 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 486 PCNYVKLVDvEEMNYLASKGE-GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLA 564
Cdd:cd05917 181 PHTEAKIVD-PEGGIVPPVGVpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IR 258
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1720426399 565 QGEYIAPEKIENIYLRSEAVAQVFV-------HGESLQAFLI 599
Cdd:cd05917 259 GGENIYPREIEEFLHTHPKVSDVQVvgvpderYGEEVCAWIR 300
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
255-609 |
2.94e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 144.14 E-value: 2.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 255 LGRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIINDCSGfIKATESALTLNASDTQISYLPLAHMYEQQLQCV 334
Cdd:PRK05677 193 KGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQ-CRALMGSNLNEGCEILIAPLPLYHIYAFTFHCM 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 335 MLchgakigffqgdirLLMDDLKVLQPTifpvvPRLLNRMFdrifgqanTSLKRWLLdfaskrkeaelrSGIVRNNSLWD 414
Cdd:PRK05677 272 AM--------------MLIGNHNILISN-----PRDLPAMV--------KELGKWKF------------SGFVGLNTLFV 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 415 KLI----FHKIQSSlggKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYV 490
Cdd:PRK05677 313 ALCnneaFRKLDFS---ALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLC 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 491 KLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIA 570
Cdd:PRK05677 390 KVID-DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVSGFNVY 467
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1720426399 571 PEKIENIYLRSEAVAQVFV-------HGESLQAFliaVVVPDVESL 609
Cdd:PRK05677 468 PNELEDVLAALPGVLQCAAigvpdekSGEAIKVF---VVVKPGETL 510
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
122-577 |
3.11e-36 |
|
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: 142.86 E-value: 3.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 122 ISYKEVAeLAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:cd05909 8 LTYRKLL-TGAIALARKLAKMTKE--GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 202 DKPEKAKLLLEGVENKLTPClKIIVIMDSYGSdlVERGKKCGVEIISLKALEDLGRVNRVKPKppEPEDLAIICFTSGTT 281
Cdd:cd05909 85 SKQFIEKLKLHHLFDVEYDA-RIVYLEDLRAK--ISKADKCKAFLAGKFPPKWLLRIFGVAPV--QPDDPAVILFTSGSE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 282 GNPKGAMITHQNIINDcsgfIKATESALTLNASDTQISYLPLAHMYeqqlqcvmlchgakiGFFQGDIRLLMDDLKVLQ- 360
Cdd:cd05909 160 GLPKGVVLSHKNLLAN----VEQITAIFDPNPEDVVFGALPFFHSF---------------GLTGCLWLPLLSGIKVVFh 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 361 --PTIFPVVPRLLNRMFDRIFGQANTSLKRWLldfasKRKEAELRSGIvrnnslwdklifhkiqsslggkvRLMITGAAP 438
Cdd:cd05909 221 pnPLDYKKIPELIYDKKATILLGTPTFLRGYA-----RAAHPEDFSSL-----------------------RLVVAGAEK 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 439 VSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPG-DWTAGHVGAPMPCNYVKLVDVEEMNYLASKGEGEVCVKGANVF 517
Cdd:cd05909 273 LKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVM 352
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 518 KGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 577
Cdd:cd05909 353 LGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDI 410
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
173-609 |
8.18e-36 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 142.89 E-value: 8.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 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 1720426399 240 KKCGVEI-----------------ISL-KALEDLGRVNRVKPKPpEPEDLAIICFTSGTTGNPKGAMITHQNIINDCSGf 301
Cdd:PRK08974 160 KGTLVNFvvkyikrlvpkyhlpdaISFrSALHKGRRMQYVKPEL-VPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQ- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 302 IKATESALTLNASDTQISYLPLAHMYEQQLQCVMLCH-GAKigffqgdirllmdDLKVLQPTIFP-VVPRLLNRMFDRIF 379
Cdd:PRK08974 238 AKAAYGPLLHPGKELVVTALPLYHIFALTVNCLLFIElGGQ-------------NLLITNPRDIPgFVKELKKYPFTAIT 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 380 GqANTSLKRWLldfaskrkeaelrsgivrNNSLWDKLIFhkiqSSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGY 459
Cdd:PRK08974 305 G-VNTLFNALL------------------NNEEFQELDF----SSL----KLSVGGGMAVQQAVAERWVKLTGQYLLEGY 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 460 GQTECT---AGCCLSLPGdwTAGHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALdKDGW 536
Cdd:PRK08974 358 GLTECSplvSVNPYDLDY--YSGSIGLPVPSTEIKLVD-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGW 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 537 LHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVF-------VHGESLQAFliavVVPDVESL 609
Cdd:PRK08974 434 LATGDIAVMDEEGFLRIVDRKKDMI-LVSGFNVYPNEIEDVVMLHPKVLEVAavgvpseVSGEAVKIF----VVKKDPSL 508
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
122-591 |
5.05e-35 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 139.97 E-value: 5.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 122 ISYKEVAELAECIGSGLIQKGFKpcSEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:cd17642 45 YSYAEYLEMSVRLAEALKKYGLK--QNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFC 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 202 DKPEKAKLLleGVENKLtPCLKIIVIMDSYgSDLveRGKKCgveIISLKALEDLGRVNRVKPKPPE---PEDLAIICFTS 278
Cdd:cd17642 123 SKKGLQKVL--NVQKKL-KIIKTIIILDSK-EDY--KGYQC---LYTFITQNLPPGFNEYDFKPPSfdrDEQVALIMNSS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 279 GTTGNPKGAMITHQNIINDCSGFIKATeSALTLNASDTQISYLPLAHMYEQQLQCVMLCHGAKIGF---FQGDIRL-LMD 354
Cdd:cd17642 194 GSTGLPKGVQLTHKNIVARFSHARDPI-FGNQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLmykFEEELFLrSLQ 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 355 DLKV----LQPTIFPVVPrllnrmfdrifgqantslKRWLLDfaskrkeaelrsgivrnnsLWDKLIFHKIQSslggkvr 430
Cdd:cd17642 273 DYKVqsalLVPTLFAFFA------------------KSTLVD-------------------KYDLSNLHEIAS------- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 431 lmitGAAPVSATVLTFLRTALGCQFY-EGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDVEEMNYLASKGEGEV 509
Cdd:cd17642 309 ----GGAPLSKEVGEAVAKRFKLPGIrQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGEL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 510 CVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFV 589
Cdd:cd17642 385 CVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQHPKIFDAGV 463
|
..
gi 1720426399 590 HG 591
Cdd:cd17642 464 AG 465
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
247-600 |
4.82e-34 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 137.65 E-value: 4.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 247 ISLKALEDLGRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIIND------CSGFIKATESALTLNASDTQISY 320
Cdd:PRK12492 185 VPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANmlqvraCLSQLGPDGQPLMKEGQEVMIAP 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 321 LPLAHMYEQQLQCVMLchgakigFFQGDIRLLMDDlkvlqptifpvvPRLLNRMFDRifgqantsLKRWLLdfaskrkea 400
Cdd:PRK12492 265 LPLYHIYAFTANCMCM-------MVSGNHNVLITN------------PRDIPGFIKE--------LGKWRF--------- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 401 elrSGIVRNNSLWDKLIFHKIQSSLGGKvRLMIT---GAAPVSATVLTFlRTALGCQFYEGYGQTECTAGCCLSLPGDWT 477
Cdd:PRK12492 309 ---SALLGLNTLFVALMDHPGFKDLDFS-ALKLTnsgGTALVKATAERW-EQLTGCTIVEGYGLTETSPVASTNPYGELA 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 478 A-GHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDR 556
Cdd:PRK12492 384 RlGTVGIPVPGTALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDR 462
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1720426399 557 KKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFV-------HGESLQAFLIA 600
Cdd:PRK12492 463 KKDLI-IVSGFNVYPNEIEDVVMAHPKVANCAAigvpderSGEAVKLFVVA 512
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
267-611 |
5.76e-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: 135.35 E-value: 5.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 267 EPEDLAIICFTSGTTGNPKGAMITHQNIINdcsgFIKATESALTLNASDTQISYLPLAH-MYEQQLqCVMLCHGAKI--- 342
Cdd:cd05930 91 DPDDLAYVIYTSGSTGKPKGVMVEHRGLVN----LLLWMQEAYPLTPGDRVLQFTSFSFdVSVWEI-FGALLAGATLvvl 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 343 -GFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTSLkrwlldfaskrkeaelrsgivrnnslwdklifhki 421
Cdd:cd05930 166 pEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAALPSL----------------------------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 422 qsslggkvRLMITGAAPVSATVLTFLRTAL-GCQFYEGYGQTECTAGCCL--SLPGDWTAGHV--GAPMPCNYVKLVDvE 496
Cdd:cd05930 211 --------RLVLVGGEALPPDLVRRWRELLpGARLVNLYGPTEATVDATYyrVPPDDEEDGRVpiGRPIPNTRVYVLD-E 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 497 EMNYLASKGEGEVCVKGANVFKGYLKDPARTAEA-----LDKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIA 570
Cdd:cd05930 282 NLRPVPPGVPGELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIE 360
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1720426399 571 PEKIENIYLRSEAVAQVFV---HGESLQAFLIAVVVPDVESLPS 611
Cdd:cd05930 361 LGEIEAALLAHPGVREAAVvarEDGDGEKRLVAYVVPDEGGELD 404
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
182-612 |
5.90e-34 |
|
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: 136.61 E-value: 5.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 182 LGADAITYIVNKAELSVIFADkPEKAKLLlEGVENKLtPCLKIIVIMDSYGSDLVERGKKcgveiisLKALEDLgrVNRV 261
Cdd:cd12119 84 LFPEQIAYIINHAEDRVVFVD-RDFLPLL-EAIAPRL-PTVEHVVVMTDDAAMPEPAGVG-------VLAYEEL--LAAE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 262 KPKPPEPE----DLAIICFTSGTTGNPKGAMITHQNIINDCsgFIKATESALTLNASDTqisYLPLAHMYEQQ-----LQ 332
Cdd:cd12119 152 SPEYDWPDfdenTAAAICYTSGTTGNPKGVVYSHRSLVLHA--MAALLTDGLGLSESDV---VLPVVPMFHVNawglpYA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 333 CVMLchGAKI----GFFQGDIRL-LMDDLKVlqpTIFPVVPRLLNRMFDrifgqantSLKRWLLDFASKRkeaelrsgiv 407
Cdd:cd12119 227 AAMV--GAKLvlpgPYLDPASLAeLIEREGV---TFAAGVPTVWQGLLD--------HLEANGRDLSSLR---------- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 408 rnnslwdklifhkiqsslggkvRLMITGAAPVSATVLTFLRtaLGCQFYEGYGQTE-CTAGCCLSLPGDWTAGHV----- 481
Cdd:cd12119 284 ----------------------RVVIGGSAVPRSLIEAFEE--RGVRVIHAWGMTEtSPLGTVARPPSEHSNLSEdeqla 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 482 -----GAPMPCNYVKLVDvEEMNYLASKGE--GEVCVKGANVFKGYLKDPaRTAEALDKDGWLHTGDIGKWLPNGTLKII 554
Cdd:cd12119 340 lrakqGRPVPGVELRIVD-DDGRELPWDGKavGELQVRGPWVTKSYYKND-EESEALTEDGWLRTGDVATIDEDGYLTIT 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720426399 555 DRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQVfvhgeslqafliAVV-VPDveslPSW 612
Cdd:cd12119 418 DRSKDVIKSG-GEWISSVELENAIMAHPAVAEA------------AVIgVPH----PKW 459
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
123-629 |
1.45e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 136.06 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 123 SYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELS-VIFA 201
Cdd:PRK12583 47 TWRQLADAVDRLARGLLALGVQPGDR--VGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRwVICA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 202 DK--------------PEKAKLLLEGVENKLTPCLKIIVIMDSYGS-------DLVERGkkcgvEIISLKALEDlgrvnr 260
Cdd:PRK12583 125 DAfktsdyhamlqellPGLAEGQPGALACERLPELRGVVSLAPAPPpgflawhELQARG-----ETVSREALAE------ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 261 vKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIINDcsGFIKAteSALTLNASDTQISYLPLAH---MYEQQLQCVmlC 337
Cdd:PRK12583 194 -RQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNN--GYFVA--ESLGLTEHDRLCVPVPLYHcfgMVLANLGCM--T 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 338 HGAKIgFFQGDirlLMDDLKVLQ-------------PTIFpvVPRLLNRMFDRifgqantslkrwlLDFASkrkeaeLRS 404
Cdd:PRK12583 267 VGACL-VYPNE---AFDPLATLQaveeerctalygvPTMF--IAELDHPQRGN-------------FDLSS------LRT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 405 GIVrnnslwdklifhkiqsslggkvrlmitGAAPVSATVLTFLRTALGC-QFYEGYGQTECTAGCCLSLPGD---WTAGH 480
Cdd:PRK12583 322 GIM---------------------------AGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSLQTTAADdleRRVET 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 481 VGAPMPCNYVKLVDVEEmNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHI 560
Cdd:PRK12583 375 VGRTQPHLEVKVVDPDG-ATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDM 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720426399 561 FkLAQGEYIAPEKIENIYLRSEAVAQVFVHGeslqafliavvVPDV---ESLPSWAQKR-GLQGSFEEL---CRNK 629
Cdd:PRK12583 454 I-IRGGENIYPREIEEFLFTHPAVADVQVFG-----------VPDEkygEEIVAWVRLHpGHAASEEELrefCKAR 517
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
97-575 |
3.88e-33 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 134.34 E-value: 3.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 97 FQRGIQVSNNgPCLGSRKPNQPYewiSYKEVAELAECIGSGL----IQKGfkpcseQFIGLFSQNRPEWVIVEQGCfSYS 172
Cdd:PLN02246 30 FERLSEFSDR-PCLIDGATGRVY---TYADVELLSRRVAAGLhklgIRQG------DVVMLLLPNCPEFVLAFLGA-SRR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 173 MVVV----PLY------DTLGADAITYIVNKA----ELSVIFADKPEKAKLLLEGVENkltpCLKIIVIMDSYGSDLVEr 238
Cdd:PLN02246 99 GAVTttanPFYtpaeiaKQAKASGAKLIITQScyvdKLKGLAEDDGVTVVTIDDPPEG----CLHFSELTQADENELPE- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 239 gkkcgVEIislkaledlgrvnrvkpkppEPEDLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKATESALTLNASDTQI 318
Cdd:PLN02246 174 -----VEI--------------------SPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYFHSDDVIL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 319 SYLPLAHMYeqQLQCVMLCH---GAKIGFFQG-DIRLLMDDLKVLQPTIFPVVPRLLnrmfdrifgqantslkrwlLDFA 394
Cdd:PLN02246 229 CVLPMFHIY--SLNSVLLCGlrvGAAILIMPKfEIGALLELIQRHKVTIAPFVPPIV-------------------LAIA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 395 skrkeaelRSGIVRNNSLwdklifhkiqSSlggkVRLMITGAAPVSATVLTFLRTAL-GCQFYEGYGQTEctAGCCLSL- 472
Cdd:PLN02246 288 --------KSPVVEKYDL----------SS----IRMVLSGAAPLGKELEDAFRAKLpNAVLGQGYGMTE--AGPVLAMc 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 473 ------PGDWTAGHVGAPMPCNYVKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWL 546
Cdd:PLN02246 344 lafakePFPVKSGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYID 423
|
490 500
....*....|....*....|....*....
gi 1720426399 547 PNGTLKIIDRKKHIFKLaQGEYIAPEKIE 575
Cdd:PLN02246 424 DDDELFIVDRLKELIKY-KGFQVAPAELE 451
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
122-616 |
4.33e-33 |
|
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: 132.42 E-value: 4.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 122 ISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRP--GDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 202 DkpekaklllegvenkltpclkiivimdsygsdlvergkkcgveiislkaledlgrvnrvkpkppepedLAIICFTSGTT 281
Cdd:cd05934 82 D--------------------------------------------------------------------PASILYTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 282 GNPKGAMITHQNIINDCSGFIKAtesaLTLNASDTQISYLPLAHMyeqQLQCV----MLCHGAKI--------GFFQGDI 349
Cdd:cd05934 94 GPPKGVVITHANLTFAGYYSARR----FGLGEDDVYLTVLPLFHI---NAQAVsvlaALSVGATLvllprfsaSRFWSDV 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 350 RllmddlkVLQPTIF---PVVPRLLNRMFDRIFGQANtslkrwlldfaskrkeaelrsgivrnnslwdklifhkiqsslg 426
Cdd:cd05934 167 R-------RYGATVTnylGAMLSYLLAQPPSPDDRAH------------------------------------------- 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 427 gKVRLmITGAAPVSATVLTFLRtALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKGE 506
Cdd:cd05934 197 -RLRA-AYGAPNPPELHEEFEE-RFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVD-DDGQELPAGEP 272
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 507 GEVCVKGAN---VFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEA 583
Cdd:cd05934 273 GELVIRGLRgwgFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVERAILRHPA 350
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1720426399 584 VAQVFVHG----ESLQAFLIAVVVP-----DVESLPSWAQKR 616
Cdd:cd05934 351 VREAAVVAvpdeVGEDEVKAVVVLRpgetlDPEELFAFCEGQ 392
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
270-616 |
1.21e-32 |
|
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: 128.77 E-value: 1.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 270 DLAIICFTSGTTGNPKGAMITHQNIIndcsGFIKATESALTLNASDTQISYLPLAHMYEQQLQCVM-LCHGAKI---GFF 345
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTL----RAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVAcLLTGATVvpvAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 346 qgDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRifgqantslkrwlldfaSKRKEAELrsgivrnnslwdklifhkiqSSL 425
Cdd:cd17638 77 --DVDAILEAIERERITVLPGPPTLFQSLLDH-----------------PGRKKFDL--------------------SSL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 426 ggkvRLMITGAAPVSATVLTFLRTALGCQ-FYEGYGQTECTAGCcLSLPGD---WTAGHVGAPMPCNYVKLVDveemnyl 501
Cdd:cd17638 118 ----RAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVAT-MCRPGDdaeTVATTCGRACPGFEVRIAD------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 502 askgEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRS 581
Cdd:cd17638 186 ----DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGALAEH 260
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1720426399 582 EAVAQVFV-------HGESLQAFLIAV--VVPDVESLPSWAQKR 616
Cdd:cd17638 261 PGVAQVAVigvpderMGEVGKAFVVARpgVTLTEEDVIAWCRER 304
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
123-627 |
2.35e-32 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 130.58 E-value: 2.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 123 SYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELsvifad 202
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDV--VAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKA------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 203 kpekaklllegvenkltpclKIIVIMDSYGSDLVErgkkcgveiislkaledlgrvnrvkpkpPEPEDLAIICFTSGTTG 282
Cdd:cd05903 75 --------------------KVFVVPERFRQFDPA----------------------------AMPDAVALLLFTSGTTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 283 NPKGAMITHQNIIndCSgfIKATESALTLNASDTQISYLPLAHmyeqqlQCVMLcHGAKIGFFQGDIRLLMDdlkVLQPT 362
Cdd:cd05903 107 EPKGVMHSHNTLS--AS--IRQYAERLGLGPGDVFLVASPMAH------QTGFV-YGFTLPLLLGAPVVLQD---IWDPD 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 363 ifpVVPRLLNRmfDRI-FGQANTSLKRWLLDfASKRKEAELRSgivrnnslwdklifhkiqsslggkVRLMITGAAPVSA 441
Cdd:cd05903 173 ---KALALMRE--HGVtFMMGATPFLTDLLN-AVEEAGEPLSR------------------------LRTFVCGGATVPR 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 442 TVLTFLRTALGCQFYEGYGQTEC--TAGCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKG 519
Cdd:cd05903 223 SLARRAAELLGAKVCSAYGSTECpgAVTSITPAPEDRRLYTDGRPLPGVEIKVVD-DTGATLAPGVEGELLSRGPSVFLG 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 520 YLKDPARTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHG---ESLQA 596
Cdd:cd05903 302 YLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAVVAlpdERLGE 379
|
490 500 510
....*....|....*....|....*....|.
gi 1720426399 597 FLIAVVVPdveslpswaqKRGLQGSFEELCR 627
Cdd:cd05903 380 RACAVVVT----------KSGALLTFDELVA 400
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
255-608 |
2.51e-32 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 132.31 E-value: 2.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 255 LGRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIIND---CSGFIKATESalTLNASDTQISYLPLAHMYEQQL 331
Cdd:PRK08751 194 LGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANmqqAHQWLAGTGK--LEEGCEVVITALPLYHIFALTA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 332 QCVMLchgAKIGFFQG------DIRLLMDDLKVLQPTIFPVVPRLLNRMFdrifgqantslkrwlldfaskrkeaelrsg 405
Cdd:PRK08751 272 NGLVF---MKIGGCNHlisnprDMPGFVKELKKTRFTAFTGVNTLFNGLL------------------------------ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 406 ivrNNSLWDKLIFHKIQSSLGGkvrlmitGAApVSATVLTFLRTALGCQFYEGYGQTECTAGCCLS-LPGDWTAGHVGAP 484
Cdd:PRK08751 319 ---NTPGFDQIDFSSLKMTLGG-------GMA-VQRSVAERWKQVTGLTLVEAYGLTETSPAACINpLTLKEYNGSIGLP 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 485 MPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLA 564
Cdd:PRK08751 388 IPSTDACIKD-DAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-LV 465
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1720426399 565 QGEYIAPEKIENIYLRSEAVAQVfvhgeslqaflIAVVVPDVES 608
Cdd:PRK08751 466 SGFNVYPNEIEDVIAMMPGVLEV-----------AAVGVPDEKS 498
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
255-645 |
3.31e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 132.05 E-value: 3.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 255 LGRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIINDC-------SGFIKATESALtlnasdtqiSYLPLAHMY 327
Cdd:PRK05605 205 GGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAaqgkawvPGLGDGPERVL---------AALPMFHAY 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 328 EQQLqCV---MLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLlnrmFDRIfgqantslkrwlldfaskRKEAELRs 404
Cdd:PRK05605 276 GLTL-CLtlaVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPL----YEKI------------------AEAAEER- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 405 GIvrnnslwdklifhkiqsSLGGkVRLMITGAA--PVSaTVLTFlRTALGCQFYEGYGQTECTA-GCCLSLPGDWTAGHV 481
Cdd:PRK05605 332 GV-----------------DLSG-VRNAFSGAMalPVS-TVELW-EKLTGGLLVEGYGLTETSPiIVGNPMSDDRRPGYV 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 482 GAPMPCNYVKLVDVEEMNYLASKGE-GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHI 560
Cdd:PRK05605 392 GVPFPDTEVRIVDPEDPDETMPDGEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKEL 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 561 FkLAQGEYIAPEKIENIYLRSEAVAQVFVHG-------ESLQAfliAVV-----VPDVESLPSWAQKRgLQG-------- 620
Cdd:PRK05605 471 I-ITGGFNVYPAEVEEVLREHPGVEDAAVVGlpredgsEEVVA---AVVlepgaALDPEGLRAYCREH-LTRykvprrfy 545
|
410 420
....*....|....*....|....*...
gi 1720426399 621 SFEELCRN---KDINKAILDDLLKLGKE 645
Cdd:PRK05605 546 HVDELPRDqlgKVRRREVREELLEKLGA 573
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
115-599 |
4.12e-32 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 131.47 E-value: 4.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 115 PNQPYEWiSYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVV---PLYDTlgaDAITYIV 191
Cdd:PRK08315 38 RDQGLRW-TYREFNEEVDALAKGLLALGIEKGDR--VGIWAPNVPEWVLTQFATAKIGAILVtinPAYRL---SELEYAL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 192 NKAELSVIF-ADK--------------PEKAKLLLEGVENKLTPCLKIIVIMDSYG-------SDLVERGKkcGVEIISL 249
Cdd:PRK08315 112 NQSGCKALIaADGfkdsdyvamlyelaPELATCEPGQLQSARLPELRRVIFLGDEKhpgmlnfDELLALGR--AVDDAEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 250 KALEDlgrvnRVKPkppepeDLAI-ICFTSGTTGNPKGAMITHQNIINDcsGFIKAteSALTLNASDTQISYLPLAHMYe 328
Cdd:PRK08315 190 AARQA-----TLDP------DDPInIQYTSGTTGFPKGATLTHRNILNN--GYFIG--EAMKLTEEDRLCIPVPLYHCF- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 329 qqlQCVM-----LCHGAKI-----GFfqgdirllmDDLKVLQ-------------PTIFpvVPRLLNRMFDRifgqants 385
Cdd:PRK08315 254 ---GMVLgnlacVTHGATMvypgeGF---------DPLATLAaveeerctalygvPTMF--IAELDHPDFAR-------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 386 lkrwlLDFASkrkeaeLRSGIvrnnslwdklifhkiqssLGGK---VRLM-----------ITGAapvsatvltflrtal 451
Cdd:PRK08315 312 -----FDLSS------LRTGI------------------MAGSpcpIEVMkrvidkmhmseVTIA--------------- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 452 gcqfyegYGQTECTAGCCLSLPGD------WTaghVGAPMPCNYVKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPA 525
Cdd:PRK08315 348 -------YGMTETSPVSTQTRTDDplekrvTT---VGRALPHLEVKIVDPETGETVPRGEQGELCTRGYSVMKGYWNDPE 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 526 RTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAV--AQVF-V----HGESLQAFL 598
Cdd:PRK08315 418 KTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEFLYTHPKIqdVQVVgVpdekYGEEVCAWI 496
|
.
gi 1720426399 599 I 599
Cdd:PRK08315 497 I 497
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
114-579 |
5.41e-32 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 131.02 E-value: 5.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 114 KPNQPYEWiSYKEVAELAECIGSGLIQKGFKP---CSEQFIGLfsqnrPEWVIVEQGCFSYSMVVVPLYDTLGADAITYI 190
Cdd:PRK06087 43 VDNHGASY-TYSALDHAASRLANWLLAKGIEPgdrVAFQLPGW-----CEFTIIYLACLKVGAVSVPLLPSWREAELVWV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 191 VNKAELSVIFADKPEKA----KLLLEgVENKLtPCLKIIVIMDSYGSDLVErgkkcgveiISL-KALEDLGRVNrvKPKP 265
Cdd:PRK06087 117 LNKCQAKMFFAPTLFKQtrpvDLILP-LQNQL-PQLQQIVGVDKLAPATSS---------LSLsQIIADYEPLT--TAIT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 266 PEPEDLAIICFTSGTTGNPKGAMITHQNIIndcsgfikATESA----LTLNASDTQISYLPLAHmyeqqlqcvmlchgaK 341
Cdd:PRK06087 184 THGDELAAVLFTSGTEGLPKGVMLTHNNIL--------ASERAycarLNLTWQDVFMMPAPLGH---------------A 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 342 IGFFQGDIR-LLMDDLKVLQPTIFPVVP-RLLNRmfdrifgQANTslkrWLL-------DFASKRKEAELRSgivrnnsl 412
Cdd:PRK06087 241 TGFLHGVTApFLIGARSVLLDIFTPDAClALLEQ-------QRCT----CMLgatpfiyDLLNLLEKQPADL-------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 413 wdklifhkiqSSLggkvRLMITGAAPVSATVLtflRTAL--GCQFYEGYGQTECTAGCCLSL--PGDWTAGHVGAPMPCN 488
Cdd:PRK06087 302 ----------SAL----RFFLCGGTTIPKKVA---RECQqrGIKLLSVYGSTESSPHAVVNLddPLSRFMHTDGYAAAGV 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 489 YVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEY 568
Cdd:PRK06087 365 EIKVVD-EARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGEN 442
|
490
....*....|.
gi 1720426399 569 IAPEKIENIYL 579
Cdd:PRK06087 443 ISSREVEDILL 453
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
123-604 |
1.09e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 126.97 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 123 SYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFAD 202
Cdd:PRK08316 38 TYAELDAAVNRVAAALLDLGLKKGDR--VAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 203 kPEKAKLLLEGVEnkLTPCLKIIVIMDSYGSDLVErgkkcgveiiSLKALEDLGRVNRVKPKPPEP--EDLAIICFTSGT 280
Cdd:PRK08316 116 -PALAPTAEAALA--LLPVDTLILSLVLGGREAPG----------GWLDFADWAEAGSVAEPDVELadDDLAQILYTSGT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 281 TGNPKGAMITHQNIINDCSGFIkateSALTLNASDTQISYLPLAHmyEQQLQCVMLCHgakigFFQGDIRLLMDdlkvlQ 360
Cdd:PRK08316 183 ESLPKGAMLTHRALIAEYVSCI----VAGDMSADDIPLHALPLYH--CAQLDVFLGPY-----LYVGATNVILD-----A 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 361 PTIfpvvprllNRMFDRIFGQANTSLkrwlldFASKrkeaelrsgivrnnSLWDKLIFHKI-----QSSLggkvRLMITG 435
Cdd:PRK08316 247 PDP--------ELILRTIEAERITSF------FAPP--------------TVWISLLRHPDfdtrdLSSL----RKGYYG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 436 AAPVSATVLTFLRTAL-GCQFYEGYGQTEcTAGCCLSLPGDWTAGHVG-APMPCNYV--KLVDvEEMNYLASKGEGEVCV 511
Cdd:PRK08316 295 ASIMPVEVLKELRERLpGLRFYNCYGQTE-IAPLATVLGPEEHLRRPGsAGRPVLNVetRVVD-DDGNDVAPGEVGEIVH 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 512 KGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQVFV-- 589
Cdd:PRK08316 373 RSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEALYTHPAVAEVAVig 450
|
490
....*....|....*..
gi 1720426399 590 --HGESLQAfLIAVVVP 604
Cdd:PRK08316 451 lpDPKWIEA-VTAVVVP 466
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
265-616 |
1.51e-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: 122.03 E-value: 1.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 265 PPEPEDLAIICFTSGTTGNPKGAMITHQNIINdcsgFIKATESALTLNASDTQISYLPLAHMYEQQLQCVMLCHGAKIgF 344
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLN----YVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTL-V 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 345 FQGDIRLLMDDLKVLqpTIFPVVPRLLnrmfdrifgqantslkrwlldfaSKRKEAELRSgivrnnslwdklifhkiqss 424
Cdd:cd17653 176 LADPSDPFAHVARTV--DALMSTPSIL-----------------------STLSPQDFPN-------------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 425 lggkVRLMITGAAPVSATVLTflRTALGCQFYEGYGQTECTAGCCLS--LPGDWTagHVGAPMPCNYVKLVDVEEMnyLA 502
Cdd:cd17653 211 ----LKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTelLPGQPV--TIGKPIPNSTCYILDADLQ--PV 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 503 SKGE-GEVCVKGANVFKGYLKDPARTAEAL----DKDGWLH--TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIE 575
Cdd:cd17653 281 PEGVvGEICISGVQVARGYLGNPALTASKFvpdpFWPGSRMyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEIE 359
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1720426399 576 NIYLRSEAVAQ---VFVHGESLQAFliavVVP---DVESLPSWAQKR 616
Cdd:cd17653 360 EVVLQSQPEVTqaaAIVVNGRLVAF----VTPetvDVDGLRSELAKH 402
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
223-589 |
1.91e-29 |
|
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: 121.22 E-value: 1.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 223 KIIVIMDSYGSDLVERGKKCGVEIISLKALEDLGRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIINdcsgFI 302
Cdd:TIGR01733 74 RLLLTDSALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVN----LL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 303 KATESALTLNASDTQISYLPLAH---MYEQqlqCVMLCHGAK--------IGFFQGDIRLLMDDLKVlqpTIFPVVPRLL 371
Cdd:TIGR01733 150 AWLARRYGLDPDDRVLQFASLSFdasVEEI---FGALLAGATlvvppedeERDDAALLAALIAEHPV---TVLNLTPSLL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 372 NRMFDRIFGQANTslkrwlldfaskrkeaelrsgivrnnslwdklifhkiqsslggkVRLMITGA-APVSATVLTFLRTA 450
Cdd:TIGR01733 224 ALLAAALPPALAS--------------------------------------------LRLVILGGeALTPALVDRWRARG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 451 LGCQFYEGYGQTECTAGC-CLSLPGDWTAGHV----GAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPA 525
Cdd:TIGR01733 260 PGARLINLYGPTETTVWStATLVDPDDAPRESpvpiGRPLANTRLYVLD-DDLRPVPVGVVGELYIGGPGVARGYLNRPE 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720426399 526 RTAE--------ALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFV 589
Cdd:TIGR01733 339 LTAErfvpdpfaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAALLRHPGVREAVV 409
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
122-605 |
2.12e-29 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 123.30 E-value: 2.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 122 ISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:COG0365 40 LTYAELRREVNRFANALRALGVKK--GDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLIT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 202 D----KPEKAKLLLEGVEN--KLTPCLKIIVIMDSYGSDLVERGkkcgveIISLKALEDlGRVNRVKPKPPEPEDLAIIC 275
Cdd:COG0365 118 AdgglRGGKVIDLKEKVDEalEELPSLEHVIVVGRTGADVPMEG------DLDWDELLA-AASAEFEPEPTDADDPLFIL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 276 FTSGTTGNPKGAMITHQNIINDCSGFIKA----TESALTLNASD----TQISYL---PLAH-----MYEqqlqcvmlchg 339
Cdd:COG0365 191 YTSGTTGKPKGVVHTHGGYLVHAATTAKYvldlKPGDVFWCTADigwaTGHSYIvygPLLNgatvvLYE----------- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 340 AKIGFFQGDiRL--LMDDLKVlqpTIFPVVPRLLnRMfdrifgqantsLKRWLLDFASKRkeaelrsgivrnnSLwdkli 417
Cdd:COG0365 260 GRPDFPDPG-RLweLIEKYGV---TVFFTAPTAI-RA-----------LMKAGDEPLKKY-------------DL----- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 418 fhkiqSSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWT-AGHVGAPMPCNYVKLVDvE 496
Cdd:COG0365 306 -----SSL----RLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGLPVkPGSMGKPVPGYDVAVVD-E 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 497 EMNYLASKGEGEVCVKGAN--VFKGYLKDPARTAEAL--DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPE 572
Cdd:COG0365 376 DGNPVPPGEEGELVIKGPWpgMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVS-GHRIGTA 454
|
490 500 510
....*....|....*....|....*....|....
gi 1720426399 573 KIENIYLRSEAVAqvfvhgESlqafliAVV-VPD 605
Cdd:COG0365 455 EIESALVSHPAVA------EA------AVVgVPD 476
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
269-592 |
2.73e-29 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 120.91 E-value: 2.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 269 EDLAIICFTSGTTGNPKGAMITHQNIindcsgFIKATESALTL--NASDTQISYLPLAHMyeQQLQCVM--LCHGAKI-- 342
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNH------WWSAIGSALNLglTEDDNWLCALPLFHI--SGLSILMrsVIYGMTVyl 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 343 --GFFQGDIRLLMDDLKVlqpTIFPVVPRLLNRMFDRIFGQANTSLkrwlldfaskrkeaelrsgivrnnslwdklifhk 420
Cdd:cd05912 149 vdKFDAEQVLHLINSGKV---TIISVVPTMLQRLLEILGEGYPNNL---------------------------------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 421 iqsslggkvRLMITGAAPVSATVLTFLRTaLGCQFYEGYGQTE-CTAGCCLSlPGDWTA--GHVGAPMPCNYVKLVDVEE 497
Cdd:cd05912 192 ---------RCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTEtCSQIVTLS-PEDALNkiGSAGKPLFPVELKIEDDGQ 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 498 mnylASKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENI 577
Cdd:cd05912 261 ----PPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEV 334
|
330
....*....|....*
gi 1720426399 578 YLRSEAVAQVFVHGE 592
Cdd:cd05912 335 LLSHPAIKEAGVVGI 349
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
118-558 |
6.26e-29 |
|
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: 121.62 E-value: 6.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 118 PYEWISYKEVAELAECIGSGLIQKGFKPcSEQFIGLFSQNRpEWVIVEQGCFSYSMVVVPLydtlgADAITYivnkaels 197
Cdd:cd05906 36 SEEFQSYQDLLEDARRLAAGLRQLGLRP-GDSVILQFDDNE-DFIPAFWACVLAGFVPAPL-----TVPPTY-------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 198 vifaDKPEKAKLLLEGVENKLTPClkIIVIMDSYGSDLVERGKKCGVEIISLKALEDLGRVNRVKPKPP-EPEDLAIICF 276
Cdd:cd05906 101 ----DEPNARLRKLRHIWQLLGSP--VVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADHDLPQsRPDDLALLML 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 277 TSGTTGNPKGAMITHQNIINDCSGFIKATEsaltLNASDTQISYLPLAHMyeqqlqcvmlchgAKIGFFQ-GDIRLLMDD 355
Cdd:cd05906 175 TSGSTGFPKAVPLTHRNILARSAGKIQHNG----LTPQDVFLNWVPLDHV-------------GGLVELHlRAVYLGCQQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 356 LKVLQPTIFPVVPRLLnRMFDRiFGQANTslkrWLLDFA-SKRKEAELRsgivRNNSLWDklifhkiQSSLggkvRLMIT 434
Cdd:cd05906 238 VHVPTEEILADPLRWL-DLIDR-YRVTIT----WAPNFAfALLNDLLEE----IEDGTWD-------LSSL----RYLVN 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 435 GAAPVSATVLTFLRTAL---GCQ---FYEGYGQTECTAGC--CLSLP-GDWTAGH----VGAPMPCNYVKLVDVEemNYL 501
Cdd:cd05906 297 AGEAVVAKTIRRLLRLLepyGLPpdaIRPAFGMTETCSGViySRSFPtYDHSQALefvsLGRPIPGVSMRIVDDE--GQL 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720426399 502 ASKGE-GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGkWLPNGTLKIIDRKK 558
Cdd:cd05906 375 LPEGEvGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
270-589 |
1.52e-28 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 120.47 E-value: 1.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 270 DLAIICFTSGTTGNPKGAMITHQNII-NDCSGFIKATESALtlnASDTQISYLPLAHMYEQQLQC--VMLCHGAKIGFFQ 346
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTHRNLVaNLCSSLFSVGPEMI---GQVVTLGLIPFFHIYGITGICcaTLRNKGKVVVMSR 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 347 GDIRLLMDDLKVLQPTIFPVVPRLLNRMFdrifgqantslkrwlldfaskrkeaelrsgivrNNSLWDKLIFHKIqsslg 426
Cdd:PLN02330 262 FELRTFLNALITQEVSFAPIVPPIILNLV---------------------------------KNPIVEEFDLSKL----- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 427 gKVRLMITGAAPVSATVLT-FLRTALGCQFYEGYGQTECTagcCLSLP-GDWTAGH-------VGAPMPCNYVKLVDVEE 497
Cdd:PLN02330 304 -KLQAIMTAAAPLAPELLTaFEAKFPGVQVQEAYGLTEHS---CITLThGDPEKGHgiakknsVGFILPNLEVKFIDPDT 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 498 MNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 577
Cdd:PLN02330 380 GRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAI 458
|
330
....*....|..
gi 1720426399 578 YLRSEAVAQVFV 589
Cdd:PLN02330 459 LLTHPSVEDAAV 470
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
112-611 |
1.70e-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: 119.74 E-value: 1.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 112 SRKPNQPY-----EWISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADA 186
Cdd:cd17655 8 EKTPDHTAvvfedQTLTYRELNERANQLARTLREKGVGP--DTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 187 ITYIVNKAELSVIFADKPEKAKLLLEGvenkltpclkIIVIMDSygsdlvergkkcgvEIISLKALEDLGRVNRvkpkpp 266
Cdd:cd17655 86 IQYILEDSGADILLTQSHLQPPIAFIG----------LIDLLDE--------------DTIYHEESENLEPVSK------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 267 ePEDLAIICFTSGTTGNPKGAMITHQNIINdcsgFIKATESALTLNASDTQISYLPLAhmyeqqlqcvmlchgakigfFq 346
Cdd:cd17655 136 -SDDLAYVIYTSGSTGKPKGVMIEHRGVVN----LVEWANKVIYQGEHLRVALFASIS--------------------F- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 347 gdirllmdDLKVLQptIFPvvPRLL-NRMFdrIFGQANTSLKRWLLDFASKRkeaelRSGIVRNNSLWDKLIFHkIQSSL 425
Cdd:cd17655 190 --------DASVTE--IFA--SLLSgNTLY--IVRKETVLDGQALTQYIRQN-----RITIIDLTPAHLKLLDA-ADDSE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 426 GGKVRLMITGAAPVSATVLTFL--RTALGCQFYEGYGQTECTAGCCLSL--PGDWTAGHV--GAPMPCNYVKLVDvEEMN 499
Cdd:cd17655 250 GLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETTVDASIYQyePETDQQVSVpiGKPLGNTRIYILD-QYGR 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 500 YLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 573
Cdd:cd17655 329 PQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-RGYRIELGE 407
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1720426399 574 IENIYLRSEAVAQ--VFVH-GESLQAFLIAVVVPDvESLPS 611
Cdd:cd17655 408 IEARLLQHPDIKEavVIARkDEQGQNYLCAYIVSE-KELPV 447
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
90-694 |
3.33e-28 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 121.50 E-value: 3.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 90 VRTMYDGFQRGIQVSNNGPCLGSRKPNQPYEWISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCF 169
Cdd:PTZ00297 426 VRSLGEMWERSVTRHSTFRCLGQTSESGESEWLTYGTVDARARELGSGLLALGVRP--GDVIGVDCEASRNIVILEVACA 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 170 SYSMVVVPLYDTlgADAITYIVNKAELSVIFADKPEKAKLLlegvenkltPC----LKIIVIMDS-YGSDLVERGKKCGV 244
Cdd:PTZ00297 504 LYGFTTLPLVGK--GSTMRTLIDEHKIKVVFADRNSVAAIL---------TCrsrkLETVVYTHSfYDEDDHAVARDLNI 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 245 EIISLKALEDLGRVNRVKPKPPEPED----LAIICFTSGTTGNPKGAMITHQNIINDCSGFIkATESALTLNASDTQISY 320
Cdd:PTZ00297 573 TLIPYEFVEQKGRLCPVPLKEHVTTDtvftYVVDNTTSASGDGLAVVRVTHADVLRDISTLV-MTGVLPSSFKKHLMVHF 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 321 LPLAHMYEQQLQCVMLCHGAKIGffQGDIRLLMDDLKVLQPTIFPVVPRLlnrmfdriFGQANTSLKR----------WL 390
Cdd:PTZ00297 652 TPFAMLFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSL--------FSTSRLQLSRanerysavysWL 721
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 391 LDfaskrKEAELRSGIV----RNNSLWDKLIFHKIQSSLGGKVRLMITGAAPVSATV-----LTFLRTALGCQ-FYegyg 460
Cdd:PTZ00297 722 FE-----RAFQLRSRLInihrRDSSLLRFIFFRATQELLGGCVEKIVLCVSEESTSFsllehISVCYVPCLREvFF---- 792
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 461 qTECTAGCCLSlpgdwtaghvGAPMPCNYVKLVDVEEMNYLASKGEGEVCVKGanvfkgylkDPARTAEAldkdgwlhtg 540
Cdd:PTZ00297 793 -LPSEGVFCVD----------GTPAPSLQVDLEPFDEPSDGAGIGQLVLAKKG---------EPRRTLPI---------- 842
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 541 dIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAfLIAVVVPDVESLP-SWAQKRG-- 617
Cdd:PTZ00297 843 -AAQWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEfEWRQSHCmg 920
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 618 ------LQGSFEELCRNKdiNKAILDDLLKLGKEAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQID 691
Cdd:PTZ00297 921 egggpaRQLGWTELVAYA--SSLLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIE 998
|
...
gi 1720426399 692 ELY 694
Cdd:PTZ00297 999 RFY 1001
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
174-659 |
4.84e-28 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 120.80 E-value: 4.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 174 VVVPLYDTLGADAITYIVNKAELSVIFADKPEKAKLLLEGVENKLTPCLKIIvimdsYGSDLVER-GKKCGVEIISLKAL 252
Cdd:PRK08633 691 VPVNLNYTASEAALKSAIEQAQIKTVITSRKFLEKLKNKGFDLELPENVKVI-----YLEDLKAKiSKVDKLTALLAARL 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 253 EDLGRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIINDcsgfIKATESALTLNASDTQISYLPLAHMYeqqlq 332
Cdd:PRK08633 766 LPARLLKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSN----IEQISDVFNLRNDDVILSSLPFFHSF----- 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 333 cvmlchgakiGFfqgDIRLLMddlkvlqPTI--FPVV----PrllnrmfdrifgqantslkrwlLD-FASKRKEAELRSG 405
Cdd:PRK08633 837 ----------GL---TVTLWL-------PLLegIKVVyhpdP----------------------TDaLGIAKLVAKHRAT 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 406 I-----------VRNNSLwDKLIFhkiqSSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLP- 473
Cdd:PRK08633 875 IllgtptflrlyLRNKKL-HPLMF----ASL----RLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNLPd 945
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 474 ----GDWT-----AGHVGAPMPCNYVKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEAL---DKDGWLHTGD 541
Cdd:PRK08633 946 vlaaDFKRqtgskEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGD 1025
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 542 IGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEniylrsEAVAQVFvHGESLQafLIAVVVPDveslpswaQKRG---- 617
Cdd:PRK08633 1026 KGHLDEDGFLTITDRYSRFAKIG-GEMVPLGAVE------EELAKAL-GGEEVV--FAVTAVPD--------EKKGeklv 1087
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720426399 618 -----LQGSFEELCR---NKDINKA-------ILDDLLKLGkeAGLKPFEQVKGIAV 659
Cdd:PRK08633 1088 vlhtcGAEDVEELKRaikESGLPNLwkpsryfKVEALPLLG--SGKLDLKGLKELAL 1142
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
263-577 |
8.02e-28 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 118.41 E-value: 8.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 263 PKPP-EPEDLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKATESALTLNASDT-QISYLPLAHMYEQQLQCV-MLCHG 339
Cdd:PLN02574 191 PKPViKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEYPGSDNvYLAALPMFHIYGLSLFVVgLLSLG 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 340 AKI----GFFQGDIRLLMDDLKVlqpTIFPVVPRLLNRMFDRIFGQANTSLKrwlldfaskrkeaelrsgivrnnslwdk 415
Cdd:PLN02574 271 STIvvmrRFDASDMVKVIDRFKV---THFPVVPPILMALTKKAKGVCGEVLK---------------------------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 416 lifhkiqsslggKVRLMITGAAPVSA-TVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGH--VGAPMPCNYVKL 492
Cdd:PLN02574 320 ------------SLKQVSCGAAPLSGkFIQDFVQTLPHVDFIQGYGMTESTAVGTRGFNTEKLSKYssVGLLAPNMQAKV 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 493 VDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPE 572
Cdd:PLN02574 388 VDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQIAPA 466
|
....*
gi 1720426399 573 KIENI 577
Cdd:PLN02574 467 DLEAV 471
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
120-621 |
1.20e-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: 117.01 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 120 EWISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVI 199
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARGVGP--GDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 200 FADkpekaklllegvenkltpclkiivimdsygSDLVERGKKCGVEIisLKALEDLGRVNRVKPKPPEPEDLAIICFTSG 279
Cdd:cd12116 89 LTD------------------------------DALPDRLPAGLPVL--LLALAAAAAAPAAPRTPVSPDDLAYVIYTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 280 TTGNPKGAMITHQNIINdcsgFIKATESALTLNASDT---------QIS----YLPLahmyeqqlqcvmlCHGAKIGFFQ 346
Cdd:cd12116 137 STGRPKGVVVSHRNLVN----FLHSMRERLGLGPGDRllavttyafDISllelLLPL-------------LAGARVVIAP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 347 GDI----RLLMDDLKVLQPTIFpvvprllnrmfdrifgQANTSLKRWLLDfASKRKEAELRsgivrnnslwdklifhkiq 422
Cdd:cd12116 200 RETqrdpEALARLIEAHSITVM----------------QATPATWRMLLD-AGWQGRAGLT------------------- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 423 sslggkvrlMITGAAPVSATVLTFLrTALGCQFYEGYGQTECT--AGCCLSLPGDwTAGHVGAPMPCNYVKLVDvEEMNY 500
Cdd:cd12116 244 ---------ALCGGEALPPDLAARL-LSRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLD-AALRP 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 501 LASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 573
Cdd:cd12116 312 VPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQVKI-RGHRIELGE 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1720426399 574 IENIYLRSEAVAQ--VFVHGESLQAFLIAVVVPDVESLPSWAQ-KRGLQGS 621
Cdd:cd12116 391 IEAALAAHPGVAQaaVVVREDGGDRRLVAYVVLKAGAAPDAAAlRAHLRAT 441
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
256-608 |
1.54e-27 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 117.81 E-value: 1.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 256 GRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKATESALTLNASDTQ---ISYLPLAHMYEQQLQ 332
Cdd:PRK07059 191 GARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAFEKKPRPDQlnfVCALPLYHIFALTVC 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 333 CVMlchGAKIGffqG---------DIRLLMDDLKVLQPTIFPVVPRLLNRMFdrifgqantslkrwlldfaskrkeaelr 403
Cdd:PRK07059 271 GLL---GMRTG---GrnilipnprDIPGFIKELKKYQVHIFPAVNTLYNALL---------------------------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 404 sgivrNNSLWDKLIFHKIQSSLGGkvrlmitGAAPVSATVLTFLRTAlGCQFYEGYGQTEcTAGCCLSLPGDWTA--GHV 481
Cdd:PRK07059 317 -----NNPDFDKLDFSKLIVANGG-------GMAVQRPVAERWLEMT-GCPITEGYGLSE-TSPVATCNPVDATEfsGTI 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 482 GAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIF 561
Cdd:PRK07059 383 GLPLPSTEVSIRD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMI 461
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1720426399 562 kLAQGEYIAPEKIEniylrsEAVAQvfvHGESLQAflIAVVVPDVES 608
Cdd:PRK07059 462 -LVSGFNVYPNEIE------EVVAS---HPGVLEV--AAVGVPDEHS 496
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
122-604 |
2.19e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 117.01 E-value: 2.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 122 ISYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPE-WVIVEQGCFSySMVVVPLYDTLGADAITYIVNKAELSVIF 200
Cdd:PRK06188 38 LTYGQLADRISRYIQAFEALGLGTGDA--VALLSLNRPEvLMAIGAAQLA-GLRRTALHPLGSLDDHAYVLEDAGISTLI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 201 ADK---PEKAKLLLEGVenkltPCLKIIVIMDS--YGSDLVERGKKCGveiislkaledlgrvnrvkPKPPEPE----DL 271
Cdd:PRK06188 115 VDPapfVERALALLARV-----PSLKHVLTLGPvpDGVDLLAAAAKFG-------------------PAPLVAAalppDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 272 AIICFTSGTTGNPKGAMITHQNIindcsgfikATESALTLNASD--TQISYL---PLAH----MYEQQLQ---CVMLCHG 339
Cdd:PRK06188 171 AGLAYTGGTTGKPKGVMGTHRSI---------ATMAQIQLAEWEwpADPRFLmctPLSHaggaFFLPTLLrggTVIVLAK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 340 AKIGFFqgdIRLLMDDlkvlQPTIFPVVPRLLNRmfdrifgqantslkrwLLDFASKRKeAELrsgivrnnslwdklifh 419
Cdd:PRK06188 242 FDPAEV---LRAIEEQ----RITATFLVPTMIYA----------------LLDHPDLRT-RDL----------------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 420 kiqSSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHV------GAPMPCNYVKLV 493
Cdd:PRK06188 281 ---SSL----ETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLRVALL 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 494 DvEEMNYLASkGE-GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPE 572
Cdd:PRK06188 354 D-EDGREVAQ-GEvGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMI-VTGGFNVFPR 429
|
490 500 510
....*....|....*....|....*....|....*....
gi 1720426399 573 KIENIYLRSEAVAQVFV-------HGESLQafliAVVVP 604
Cdd:PRK06188 430 EVEDVLAEHPAVAQVAVigvpdekWGEAVT----AVVVL 464
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
124-616 |
2.63e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 116.22 E-value: 2.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 124 YKEVAELAECIGSGLIQKGfkpcseQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFADK 203
Cdd:PRK03640 34 HEAVVSVAGKLAALGVKKG------DRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 204 PEKAKLllegvenkltpclkiivimdsygsdlvergkkcgVEIISLKaLEDLGRVNRVKPKPPEPEDL---AIICFTSGT 280
Cdd:PRK03640 108 DFEAKL----------------------------------IPGISVK-FAELMNGPKEEAEIQEEFDLdevATIMYTSGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 281 TGNPKGAMITHQNiindcsGFIKATESALTL--NASDTQISYLPLAHMyeQQLQCVM--LCHGAKI----GFFQGDI-RL 351
Cdd:PRK03640 153 TGKPKGVIQTYGN------HWWSAVGSALNLglTEDDCWLAAVPIFHI--SGLSILMrsVIYGMRVvlveKFDAEKInKL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 352 LMDDlKVlqpTIFPVVPRLLNRMFDRIfGQANTslkrwlldfaskrkeaelrsgivrNNSLwdklifhkiqsslggkvRL 431
Cdd:PRK03640 225 LQTG-GV---TIISVVSTMLQRLLERL-GEGTY------------------------PSSF-----------------RC 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 432 MITGAAPVSATVLTflrtalGCQ-----FYEGYGQTEcTAGCCLSLPGDWTA---GHVGAPM-PCNyVKLVDveEMNYLA 502
Cdd:PRK03640 259 MLLGGGPAPKPLLE------QCKekgipVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLfPCE-LKIEK--DGVVVP 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 503 SKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSE 582
Cdd:PRK03640 329 PFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHP 406
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1720426399 583 AVAQVFVHGESLQ-------AFLIAVVVPDVESLPSWAQKR 616
Cdd:PRK03640 407 GVAEAGVVGVPDDkwgqvpvAFVVKSGEVTEEELRHFCEEK 447
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
266-604 |
3.70e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 115.47 E-value: 3.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 266 PEPEDLAIICFTSGTTGNPKGAMITHQNIINDcsgfIKATESALTLNASDTQISYLPLAHMyeqqlqcvmlcHGAKIGff 345
Cdd:PRK07787 125 PDPDAPALIVYTSGTTGPPKGVVLSRRAIAAD----LDALAEAWQWTADDVLVHGLPLFHV-----------HGLVLG-- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 346 qgdirllmddlkVLQPTifpvvpRLLNRMfdrifgqantslkRWLLDFASKRKEAELRSG-------------IVRNNSL 412
Cdd:PRK07787 188 ------------VLGPL------RIGNRF-------------VHTGRPTPEAYAQALSEGgtlyfgvptvwsrIAADPEA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 413 WDKLifhkiqsslgGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKL 492
Cdd:PRK07787 237 ARAL----------RGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 493 VDvEEMNYLASKGE--GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDR------KKHIFKLA 564
Cdd:PRK07787 307 VD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGGYRIG 385
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1720426399 565 QGEyiapekIENIYLRSEAVAQVFVHGE---SLQAFLIAVVVP 604
Cdd:PRK07787 386 AGE------IETALLGHPGVREAAVVGVpddDLGQRIVAYVVG 422
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
120-616 |
4.34e-27 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 118.04 E-value: 4.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 120 EWISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCF----SYsmvvVPLYDTLGADAITYIVNKAE 195
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALGVGP--GDLVGVCLERSLEMVVALLAVLkagaAY----VPLDPAYPAERLAYMLEDAG 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 196 LSVIFADkpekaklllegvenkltpclkiivimdsygSDLVERGKKCGVEIISLKALEDLGRVNRVKPKPPEPEDLAIIC 275
Cdd:COG1020 574 ARLVLTQ------------------------------SALAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLAYVI 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 276 FTSGTTGNPKGAMITHQNIINdcsgFIKATESALTLNASD--TQISylPLAH---MYEQqlqCVMLCHGAKIGFFQGDIR 350
Cdd:COG1020 624 YTSGSTGRPKGVMVEHRALVN----LLAWMQRRYGLGPGDrvLQFA--SLSFdasVWEI---FGALLSGATLVLAPPEAR 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 351 LLMDDLKVL----QPTIFPVVPRLLNRMFDRIFgQANTSLKRWLLdfaskrkeaelrsgivrnnslwdklifhkiqsslG 426
Cdd:COG1020 695 RDPAALAELlarhRVTVLNLTPSLLRALLDAAP-EALPSLRLVLV----------------------------------G 739
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 427 GkvrlmitGAAPVsATVLTFLRTALGCQFYEGYGQTECTAGCCLSL--PGDWTAGHV--GAPMPCNYVKLVDvEEMNyLA 502
Cdd:COG1020 740 G-------EALPP-ELVRRWRARLPGARLVNLYGPTETTVDSTYYEvtPPDADGGSVpiGRPIANTRVYVLD-AHLQ-PV 809
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 503 SKG-EGEVCVKGANVFKGYLKDPARTAEA-----LDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKI 574
Cdd:COG1020 810 PVGvPGELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNLEFLGRADDQVKI-RGFRIELGEI 888
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1720426399 575 ENIYLRSEAVAQ--VFVHGESLQA-FLIAVVVPDVESLPSWAQKR 616
Cdd:COG1020 889 EAALLQHPGVREavVVAREDAPGDkRLVAYVVPEAGAAAAAALLR 933
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
120-591 |
6.44e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 114.96 E-value: 6.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 120 EWISYKEVAELAECIGSGLIQK-GFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSV 198
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIYElNVKKGER--IAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 199 IFADKpekaklllegvenkltpclkiivimdSYGSDLVERGKKCGVE-IISLKALEDLGRVNRVKPKPPEPEDLAIICFT 277
Cdd:PRK06839 104 LFVEK--------------------------TFQNMALSMQKVSYVQrVISITSLKEIEDRKIDNFVEKNESASFIICYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 278 SGTTGNPKGAMITHQNIindcsgFIKATES--ALTLNASDTQISYLPLAHMyeqqlqcvmlchgAKIGFFQgdirllmdd 355
Cdd:PRK06839 158 SGTTGKPKGAVLTQENM------FWNALNNtfAIDLTMHDRSIVLLPLFHI-------------GGIGLFA--------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 356 lkvlQPTIFP----VVPRllnrMFDRIFGQANTSLKRWLLDFASKRKEAELRSGIVRNNSLWDKlifhkiqsslggkVRL 431
Cdd:PRK06839 210 ----FPTLFAggviIVPR----KFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQS-------------VRW 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 432 MITGAAPVSATVLTFLRTAlGCQFYEGYGQTECTAGCCLSLPGDW--TAGHVGAPMPCNYVKLVDvEEMNYLASKGEGEV 509
Cdd:PRK06839 269 FYNGGAPCPEELMREFIDR-GFLFGQGFGMTETSPTVFMLSEEDArrKVGSIGKPVLFCDYELID-ENKNKVEVGEVGEL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 510 CVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFV 589
Cdd:PRK06839 347 LIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQVINKLSDVYEVAV 424
|
..
gi 1720426399 590 HG 591
Cdd:PRK06839 425 VG 426
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
265-599 |
6.93e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 115.90 E-value: 6.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 265 PPEPE-DLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKATESALtlNASDTQISYLPLAHMYeqQLQCVM---LCHGA 340
Cdd:PRK06710 201 PCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCK--EGEEVVLGVLPFFHVY--GMTAVMnlsIMQGY 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 341 KIGFF-QGDIRLLMDDLKVLQPTIFPVVPRLLNRMFdrifgqaNTSLkrwlldfaskRKEAELRSgivrnnslwdklifh 419
Cdd:PRK06710 277 KMVLIpKFDMKMVFEAIKKHKVTLFPGAPTIYIALL-------NSPL----------LKEYDISS--------------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 420 kiqsslggkVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLS-LPGDWTAGHVGAPMPCNYVKLVDVEEM 498
Cdd:PRK06710 325 ---------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNfLWEKRVPGSIGVPWPDTEAMIMSLETG 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 499 NYLASKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 578
Cdd:PRK06710 396 EALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREVEEVL 473
|
330 340
....*....|....*....|....*...
gi 1720426399 579 LRSEAVAQVFV-------HGESLQAFLI 599
Cdd:PRK06710 474 YEHEKVQEVVTigvpdpyRGETVKAFVV 501
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
174-618 |
1.17e-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: 113.69 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 174 VVVPLYDTLGADAITYIVNKAELSVIFADkpekaklllEGVENKLTPCLkiiviMDSYGSDLVergkkcgveiISLKALE 253
Cdd:cd05922 48 VFVPLNPTLKESVLRYLVADAGGRIVLAD---------AGAADRLRDAL-----PASPDPGTV----------LDADGIR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 254 DLGRvnRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIINDCSgfikATESALTLNASDTQISYLPLAHMYE-QQLQ 332
Cdd:cd05922 104 AARA--SAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANAR----SIAEYLGITADDRALTVLPLSYDYGlSVLN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 333 CVMLChGAKIgFFQGDIRL---LMDDLKVLQPTIFPVVPRLLNrMFDRIfgqantslkrwlldfasKRKEAELRSgivrn 409
Cdd:cd05922 178 THLLR-GATL-VLTNDGVLddaFWEDLREHGATGLAGVPSTYA-MLTRL-----------------GFDPAKLPS----- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 410 nslwdklifhkiqsslggkVRLMITGAAPVSATVLTFLRTAL-GCQFYEGYGQTECTAGCCLsLPGDWTA---GHVGAPM 485
Cdd:cd05922 233 -------------------LRYLTQAGGRLPQETIARLRELLpGAQVYVMYGQTEATRRMTY-LPPERILekpGSIGLAI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 486 PCNYVKLVDVEEMnyLASKGE-GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLA 564
Cdd:cd05922 293 PGGEFEILDDDGT--PTPPGEpGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720426399 565 qGEYIAPEKIENIyLRSEAVAQVFV-------HGESLQAFLIAVVVPDVESLPSWAQKRGL 618
Cdd:cd05922 371 -GNRISPTEIEAA-ARSIGLIIEAAavglpdpLGEKLALFVTAPDKIDPKDVLRSLAERLP 429
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
108-672 |
1.28e-26 |
|
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: 114.84 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 108 PCLGSRKPNQPYEWISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSY---SMVVVPLYDTLGA 184
Cdd:cd05921 12 TWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGLSA--ERPLLILSGNSIEHALMALAAMYAgvpAAPVSPAYSLMSQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 185 D--AITYIVNKAELSVIFADKPEKAKLLLEGVENKLTPclkIIVImdsygsdlveRGKKCGVEIISLKAL---EDLGRVN 259
Cdd:cd05921 90 DlaKLKHLFELLKPGLVFAQDAAPFARALAAIFPLGTP---LVVS----------RNAVAGRGAISFAELaatPPTAAVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 260 RVKPKPpEPEDLAIICFTSGTTGNPKGAMITHQNI------INDCSGFIKATESALtlnasdtqISYLPLAHMYeqqlqc 333
Cdd:cd05921 157 AAFAAV-GPDTVAKFLFTSGSTGLPKAVINTQRMLcanqamLEQTYPFFGEEPPVL--------VDWLPWNHTF------ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 334 vmlchGAKIGF-----------------FQGDIRLLMDDLKVLQPTIFPVVPrllnrmfdrifgqantslKRWLLDFASK 396
Cdd:cd05921 222 -----GGNHNFnlvlynggtlyiddgkpMPGGFEETLRNLREISPTVYFNVP------------------AGWEMLVAAL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 397 RKEAELRSGIVRNnslwdklifhkiqsslggkVRLMITGAAPVSATVLTFLrTALGCQ-------FYEGYGQTEcTAGCC 469
Cdd:cd05921 279 EKDEALRRRFFKR-------------------LKLMFYAGAGLSQDVWDRL-QALAVAtvgeripMMAGLGATE-TAPTA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 470 LSLPGDWT-AGHVGAPMPCNYVKLVdveemnylASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWL-- 546
Cdd:cd05921 338 TFTHWPTErSGLIGLPAPGTELKLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdp 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 547 --PNGTLKIIDRKKHIFKLAQGEYIA--PekieniyLRSEAVAQ-------VFVHGESlQAFLIAVVVPDVESLpswaqk 615
Cdd:cd05921 410 ddPAKGLVFDGRVAEDFKLASGTWVSvgP-------LRARAVAAcaplvhdAVVAGED-RAEVGALVFPDLLAC------ 475
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720426399 616 RGLQG----SFEELCRNKDINKAILDDLLKLGKEAGLKPfEQVKGIAVHPELFSIDNGLLT 672
Cdd:cd05921 476 RRLVGlqeaSDAEVLRHAKVRAAFRDRLAALNGEATGSS-SRIARALLLDEPPSIDKGEIT 535
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
121-629 |
2.93e-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: 112.78 E-value: 2.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 121 WISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIF 200
Cdd:cd12118 29 RYTWRQTYDRCRRLASALAALGISR--GDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 201 ADKPekakLLLEgvenkltpclkiivimdsygsDLVERGKKcgveiislkaledlgrvnRVKPKPPEPEDLAI-ICFTSG 279
Cdd:cd12118 107 VDRE----FEYE---------------------DLLAEGDP------------------DFEWIPPADEWDPIaLNYTSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 280 TTGNPKGAMITHQniindcSGFIKATESALTlNASDTQISYL---PLAHmyeqqlqCVMLCHGAKIGFFQG--------D 348
Cdd:cd12118 144 TTGRPKGVVYHHR------GAYLNALANILE-WEMKQHPVYLwtlPMFH-------CNGWCFPWTVAAVGGtnvclrkvD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 349 IRLLMDDLKVLQPTIFPVVPRLLNRMfdrifgqANTSlkrwlldfaskrkeaelrsgivrnnslwdklifHKIQSSLGGK 428
Cdd:cd12118 210 AKAIYDLIEKHKVTHFCGAPTVLNML-------ANAP---------------------------------PSDARPLPHR 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 429 VRLMITGAAPvSATVLtFLRTALGCQFYEGYGQTEcTAG---CCL------SLPGDWTA--------GHVGApmpcNYVK 491
Cdd:cd12118 250 VHVMTAGAPP-PAAVL-AKMEELGFDVTHVYGLTE-TYGpatVCAwkpewdELPTEERArlkarqgvRYVGL----EEVD 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 492 LVDVEEMNYLASKGE--GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYI 569
Cdd:cd12118 323 VLDPETMKPVPRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENI 400
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720426399 570 APEKIENIYLRSEAVAQVFVhgeslqafliaVVVPDveslPSWAQ--------KRGLQGSFEEL---CRNK 629
Cdd:cd12118 401 SSVEVEGVLYKHPAVLEAAV-----------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 |
6.64e-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: 6.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 122 ISYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDR--VGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 202 dkpekaklllegvenkltpclkiivimdsyGSDLvergkkcgveiislkaledlgrvnrvkpkppepEDLAIICFTSGTT 281
Cdd:cd05935 80 ------------------------------GSEL---------------------------------DDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 282 GNPKGAMITHQNIINDCSGFIKATesalTLNASDTQISYLPLAHMYEqqlqcvmlchgakigfFQGDIRLlmddlkvlqp 361
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQSAVWT----GLTPSDVILACLPLFHVTG----------------FVGSLNT---------- 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 362 tifPVVprllnrmfdriFGQANTSLKRWLLDFAskRKEAELRSGIVRNNS---LWDKLIFHKIQSSLGGKVRLMITGAAP 438
Cdd:cd05935 147 ---AVY-----------VGGTYVLMARWDRETA--LELIEKYKVTFWTNIptmLVDLLATPEFKTRDLSSLKVLTGGGAP 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 439 VSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDVEEMNYLASKGEGEVCVKGANVFK 518
Cdd:cd05935 211 MPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFK 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 519 GYLKDPARTAEALDKDG---WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQVFV------ 589
Cdd:cd05935 291 GYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVisvpde 369
|
490 500 510
....*....|....*....|....*....|....
gi 1720426399 590 -HGESLQAFLiaVVVP------DVESLPSWAQKR 616
Cdd:cd05935 370 rVGEEVKAFI--VLRPeyrgkvTEEDIIEWAREQ 401
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
122-604 |
1.06e-25 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 112.07 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 122 ISYKEVAELAECIGSGLIQKGFKP---CSEQFiglfsQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSV 198
Cdd:PRK13295 56 FTYRELAALVDRVAVGLARLGVGRgdvVSCQL-----PNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 199 IFA-------DKPEkaklLLEGVENKLtPCLKIIVIMDSYGSDLVERgkkcgveIISLKALEDLGRVNRVKPKP-PEPED 270
Cdd:PRK13295 131 LVVpktfrgfDHAA----MARRLRPEL-PALRHVVVVGGDGADSFEA-------LLITPAWEQEPDAPAILARLrPGPDD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 271 LAIICFTSGTTGNPKGAMITHQNIINDcsgfIKATESALTLNASDTQISYLPLAH----MYEQQLQcVMLchGAKIgffq 346
Cdd:PRK13295 199 VTQLIYTSGTTGEPKGVMHTANTLMAN----IVPYAERLGLGADDVILMASPMAHqtgfMYGLMMP-VML--GATA---- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 347 gdirllmddlkVLQPTIFPVvprllnRMFDRI------FGQANTSlkrWLLDFASKRKEAELRSgivrnnslwdklifhk 420
Cdd:PRK13295 268 -----------VLQDIWDPA------RAAELIrtegvtFTMASTP---FLTDLTRAVKESGRPV---------------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 421 iqSSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTA--GCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEM 498
Cdd:PRK13295 312 --SSL----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAvtLTKLDDPDERASTTDGCPLPGVEVRVVD-ADG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 499 NYLASKGEGEVCVKGANVFKGYLKDPARTAEalDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 578
Cdd:PRK13295 385 APLPAGQIGRLQVRGCSNFGGYLKRPQLNGT--DADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEALL 461
|
490 500
....*....|....*....|....*....
gi 1720426399 579 LRSEAVAQVFVHG---ESLQAFLIAVVVP 604
Cdd:PRK13295 462 YRHPAIAQVAIVAypdERLGERACAFVVP 490
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
268-609 |
2.74e-25 |
|
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: 109.94 E-value: 2.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 268 PEDLAIICFTSGTTGNPKGAMITHQNIindCSGfIKATESALTLNaSDTQI----SYLPLAHMYEQqlqCVMLCHGAKIG 343
Cdd:cd05918 105 PSDAAYVIFTSGSTGKPKGVVIEHRAL---STS-ALAHGRALGLT-SESRVlqfaSYTFDVSILEI---FTTLAAGGCLC 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 344 ffqgdI---RLLMDDLkvlqptifpvvPRLLNRMfdrifgQANTslkrwlldfaskrkeAELRSGIVRnnslwdkLIFHK 420
Cdd:cd05918 177 -----IpseEDRLNDL-----------AGFINRL------RVTW---------------AFLTPSVAR-------LLDPE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 421 IQSSLggkvRLMITGAAPVSATVLTflRTALGCQFYEGYGQTECTAGCCLSLPG-DWTAGHVGAPMPCN-YVklVDVEEM 498
Cdd:cd05918 213 DVPSL----RTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRPLGATcWV--VDPDNH 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 499 NYLASKGE-GEVCVKGANVFKGYLKDPARTAEALDKD-GWLH------------TGDIGKWLPNGTLKIIDRKKHIFKLa 564
Cdd:cd05918 285 DRLVPIGAvGELLIEGPILARGYLNDPEKTAAAFIEDpAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKI- 363
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1720426399 565 QGEYIAPEKIENIYLRS-----EAVAQVFVH-GESLQAFLIAVVVPDVESL 609
Cdd:cd05918 364 RGQRVELGEIEHHLRQSlpgakEVVVEVVKPkDGSSSPQLVAFVVLDGSSS 414
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
270-611 |
6.12e-25 |
|
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: 106.26 E-value: 6.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 270 DLAIICFTSGTTGNPKGAMITHQNIINDCSGfikaTESALTLNASDTQISYLPLAHM--YEQQLQCVMLchGAKIGFFQG 347
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAG----LHSRLGFGGGDSWLLSLPLYHVggLAILVRSLLA--GAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 348 DiRLLMDDLKVLQPTIFPVVPRLLNRMFDRifGQANTSLKRwlldfaskrkeaelrsgivrnnslwdklifhkiqsslgg 427
Cdd:cd17630 75 N-QALAEDLAPPGVTHVSLVPTQLQRLLDS--GQGPAALKS--------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 428 kVRLMITGAAPVSAtVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDveemnylaskgEG 507
Cdd:cd17630 113 -LRAVLLGGAPIPP-ELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVE-----------DG 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 508 EVCVKGANVFKGYLKdpARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQV 587
Cdd:cd17630 180 EIWVGGASLAMGYLR--GQLVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAVRDA 256
|
330 340
....*....|....*....|....*..
gi 1720426399 588 FVHG---ESLQAFLIAVVVPDVESLPS 611
Cdd:cd17630 257 FVVGvpdEELGQRPVAVIVGRGPADPA 283
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
157-616 |
9.48e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 109.10 E-value: 9.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 157 NRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFADKPEKAklLLEGVENkLTPCLKIIVIMDSYGSDLV 236
Cdd:PRK07786 76 NRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAP--VATAVRD-IVPLLSTVVVAGGSSDDSV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 237 ergkkcgveiislKALEDLGRVNRVKPKPPE-PEDL-AIICFTSGTTGNPKGAMITHQNIINDCSGFIKATESAltlNAS 314
Cdd:PRK07786 153 -------------LGYEDLLAEAGPAHAPVDiPNDSpALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGAD---INS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 315 DTQISYLPLAHMYEQQLQCVMLCHGAKIgffqgdirllmddlkVLQPTifpvvprllnRMFDRifGQantslkrwLLDFA 394
Cdd:PRK07786 217 DVGFVGVPLFHIAGIGSMLPGLLLGAPT---------------VIYPL----------GAFDP--GQ--------LLDVL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 395 skrkEAELRSGIVRNNSLWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRTAL-GCQFYEGYGQTECTAGCCLSLP 473
Cdd:PRK07786 262 ----EAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEMSPVTCMLLG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 474 GDWTA--GHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDkDGWLHTGDIGKWLPNGTL 551
Cdd:PRK07786 338 EDAIRklGSVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHSGDLVRQDEEGYV 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720426399 552 KIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAF---LIAVVVPD-------VESLPSWAQKR 616
Cdd:PRK07786 416 WVVDRKKDMI-ISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWgevPVAVAAVRnddaaltLEDLAEFLTDR 489
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
122-611 |
1.37e-24 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 108.44 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 122 ISYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGLLPGDR--VALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 202 DKpekaklllEGVENKLTPCLKIIVIMDSYGSDlveRGKKCGVEIISLKALEDLGRVNRVkPKPPEPEDlAIICFTSGTT 281
Cdd:PRK05852 122 DA--------DGPHDRAEPTTRWWPLTVNVGGD---SGPSGGTLSVHLDAATEPTPATST-PEGLRPDD-AMIMFTGGTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 282 GNPKGAMITHQNIindcSGFIKATESALTLNASDTQISYLPLAHMYeqQLQCVML---CHGAKI-----GFFQGdiRLLM 353
Cdd:PRK05852 189 GLPKMVPWTHANI----ASSVRAIITGYRLSPRDATVAVMPLYHGH--GLIAALLatlASGGAVllparGRFSA--HTFW 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 354 DDLKVLQPTIFPVVPRLLNRMFDRifgqANTSlkrwlldfASKRKEAELRsgIVRNNSlwdklifhkiqsslggkvrlmi 433
Cdd:PRK05852 261 DDIKAVGATWYTAVPTIHQILLER----AATE--------PSGRKPAALR--FIRSCS---------------------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 434 tgaAPVSATVLTFLRTALGCQFYEGYGQTECTAGccLSLPGDWTAGHVGAP-MPCNYVKLVDVEEMNYLASKGE------ 506
Cdd:PRK05852 305 ---APLTAETAQALQTEFAAPVVCAFGMTEATHQ--VTTTQIEGIGQTENPvVSTGLVGRSTGAQIRIVGSDGLplpaga 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 507 -GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVA 585
Cdd:PRK05852 380 vGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLASHPNVM 457
|
490 500
....*....|....*....|....*....
gi 1720426399 586 QVFVHGESLQAF---LIAVVVPDVESLPS 611
Cdd:PRK05852 458 EAAVFGVPDQLYgeaVAAVIVPRESAPPT 486
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
123-683 |
1.45e-24 |
|
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: 107.04 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 123 SYKEVAELAECIGSGLIQKGFKPcSEQFIGLFSqNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFAD 202
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRK-GDRVAVLLP-RVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 203 KpekaklllegvenkltpclkiivimdsygsdlvergkkcgveiislkaledlgrvnrvkpkppepEDLAIICFTSGTTG 282
Cdd:cd05972 80 A-----------------------------------------------------------------EDPALIYFTSGTTG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 283 NPKGAMITHQ---NIINDCSGFIKATESALTLNASDTQISYLPLAHMYEQQLQ--CVMLCHGAKIgffqgDIRLLMDDLK 357
Cdd:cd05972 95 LPKGVLHTHSyplGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLgaTVFVYEGPRF-----DAERILELLE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 358 VLQPTIFPVVPrllnrmfdrifgqanTSLKRWLldfaskrkeAELRSGIVRnnslwdklifhkiqsslgGKVRLMITGAA 437
Cdd:cd05972 170 RYGVTSFCGPP---------------TAYRMLI---------KQDLSSYKF------------------SHLRLVVSAGE 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 438 PVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANV- 516
Cdd:cd05972 208 PLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIID-DDGRELPPGEEGDIAIKLPPPg 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 517 -FKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEAVAQVFV------ 589
Cdd:cd05972 287 lFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVESALLEHPAVAEAAVvgspdp 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 590 -HGESLQAFLiaVVVPDVESLPSWAQkrglqgsfeelcrnkdinkaildDLLKLGKEAgLKPFEQVKGIAVHPELfsidn 668
Cdd:cd05972 365 vRGEVVKAFV--VLTSGYEPSEELAE-----------------------ELQGHVKKV-LAPYKYPREIEFVEEL----- 413
|
570
....*....|....*
gi 1720426399 669 gLLTPTLKAKRPELR 683
Cdd:cd05972 414 -PKTISGKIRRVELR 427
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
174-585 |
4.41e-24 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 107.35 E-value: 4.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 174 VVVPLYDTLGADAITYIVNKAELSVIFADKPE-------KAKLLLEGVenkltPCLKIIVIMDsyGSDLVERGK------ 240
Cdd:PRK07529 108 IANPINPLLEPEQIAELLRAAGAKVLVTLGPFpgtdiwqKVAEVLAAL-----PELRTVVEVD--LARYLPGPKrlavpl 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 241 ---KCGVEIISLKALEDLGRVNR-VKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIINDcsGFIKATESALTLNasDT 316
Cdd:PRK07529 181 irrKAHARILDFDAELARQPGDRlFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVAN--AWLGALLLGLGPG--DT 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 317 QISYLPLAHMYEQQLQC-VMLCHGAKIGFF--QG--DIRLLMDDLKVL---QPTIFPVVPRLLNRMFDRIFGQANTSlkr 388
Cdd:PRK07529 257 VFCGLPLFHVNALLVTGlAPLARGAHVVLAtpQGyrGPGVIANFWKIVeryRINFLSGVPTVYAALLQVPVDGHDIS--- 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 389 wlldfaskrkeaelrsgivrnnslwdklifhkiqsSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGC 468
Cdd:PRK07529 334 -----------------------------------SL----RYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVS 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 469 CLSLP-GDWTAGHVGAPMPCNYVKLVDVEEM-NYL--ASKGE-GEVCVKGANVFKGYLkDPARTAEALDKDGWLHTGDIG 543
Cdd:PRK07529 375 SVNPPdGERRIGSVGLRLPYQRVRVVILDDAgRYLrdCAVDEvGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDLG 453
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1720426399 544 KWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVA 585
Cdd:PRK07529 454 RIDADGYFWLTGRAKDLI-IRGGHNIDPAAIEEALLRHPAVA 494
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
265-558 |
4.92e-24 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 106.50 E-value: 4.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 265 PPEPEDLAIICFTSGTTGNPKGAMITHQNIINDcsgfikatesALTLN------ASDTQISYLPLAHMYEQQLQC-VMLC 337
Cdd:PRK07514 152 PRGADDLAAILYTSGTTGRSKGAMLSHGNLLSN----------ALTLVdywrftPDDVLIHALPIFHTHGLFVATnVALL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 338 HGAKIGFFQG-DIRLLMDDLKvlQPTIFPVVP----RLL-NRMFDRifgqantslkrwlldfaskrkEAelrsgiVRNns 411
Cdd:PRK07514 222 AGASMIFLPKfDPDAVLALMP--RATVMMGVPtfytRLLqEPRLTR---------------------EA------AAH-- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 412 lwdklifhkiqsslggkVRLMITGAAPVSATvlTFL----RTalGCQFYEGYGQTEctAGCCLSLP--GDWTAGHVGAPM 485
Cdd:PRK07514 271 -----------------MRLFISGSAPLLAE--THRefqeRT--GHAILERYGMTE--TNMNTSNPydGERRAGTVGFPL 327
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720426399 486 PCNYVKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK 558
Cdd:PRK07514 328 PGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGK 400
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
122-629 |
8.08e-24 |
|
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: 105.91 E-value: 8.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 122 ISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVKR--EERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 202 DkPEKAKLLLEGVEnKLTPCLKIIVIMDSYGSdlvERGKKCGVEIISlkALEDLGrvnrvKPKPPEPEDLAIICFTSGTT 281
Cdd:cd05959 108 S-GELAPVLAAALT-KSEHTLVVLIVSGGAGP---EAGALLLAELVA--AEAEQL-----KPAATHADDPAFWLYSSGST 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 282 GNPKGAMITHQNIINDCSGFIKATesaLTLNASDTQISYLPLAHMYEqqlqcvmLCHGAKIGFFQGDIRLLM-------- 353
Cdd:cd05959 176 GRPKGVVHLHADIYWTAELYARNV---LGIREDDVCFSAAKLFFAYG-------LGNSLTFPLSVGATTVLMperptpaa 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 354 --DDLKVLQPTIFPVVPRLLNRMFdrifgQANTSLKRwllDFASkrkeaelrsgivrnnslwdklifhkiqsslggkVRL 431
Cdd:cd05959 246 vfKRIRRYRPTVFFGVPTLYAAML-----AAPNLPSR---DLSS---------------------------------LRL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 432 MITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCV 511
Cdd:cd05959 285 CVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRD-EDGGDVADGEPGELYV 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 512 KGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:cd05959 364 RGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSPFEVESALVQHPAVLEAAVVG 441
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1720426399 592 ESLQAFLI---AVVVPDVESLPSWAQKRGLQgsfeELCRNK 629
Cdd:cd05959 442 VEDEDGLTkpkAFVVLRPGYEDSEALEEELK----EFVKDR 478
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
270-607 |
1.81e-23 |
|
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: 101.96 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 270 DLAIICFTSGTTGNPKGAMITHQNIIndCSGFikATESALTLNASDTQISYLPLAHMYEQQLQCVMLCHGAK---IGFFQ 346
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLI--AANL--QLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGAnvvMEKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 347 GDIRL-LMDDLKVlqpTIFPVVPRLLNRMFDRIfgqantslkrwlldfasKRKEAELRSgiVRNnslwdklifhkiqssl 425
Cdd:cd17637 77 PAEALeLIEEEKV---TLMGSFPPILSNLLDAA-----------------EKSGVDLSS--LRH---------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 426 ggkvrlmITGA-APvsATVLTFLRTAlGCQFYEGYGQTECTAGCCLSlPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASK 504
Cdd:cd17637 119 -------VLGLdAP--ETIQRFEETT-GATFWSLYGQTETSGLVTLS-PYRERPGSAGRPGPLVRVRIVD-DNDRPVPAG 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 505 GEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRK--KHIFKlAQGEYIAPEKIENIYLRSE 582
Cdd:cd17637 187 ETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKVILEHP 264
|
330 340
....*....|....*....|....*
gi 1720426399 583 AVAQVFVHGeslqafliavvVPDVE 607
Cdd:cd17637 265 AIAEVCVIG-----------VPDPK 278
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
91-545 |
3.10e-23 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 104.58 E-value: 3.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 91 RTMYDGFQRGIQVSNNGPCLGSRKPNQPYEWISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFS 170
Cdd:PRK08180 39 RRLTDRLVHWAQEAPDRVFLAERGADGGWRRLTYAEALERVRAIAQALLDRGLSA--ERPLMILSGNSIEHALLALAAMY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 171 YSMVVVPL---YDTLGAD--AITYIVNKAELSVIFADKPEKAKLLLEGVEnklTPCLKIIVImdsygsdlveRGKKCGVE 245
Cdd:PRK08180 117 AGVPYAPVspaYSLVSQDfgKLRHVLELLTPGLVFADDGAAFARALAAVV---PADVEVVAV----------RGAVPGRA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 246 IISLKALEDLGRVNRVKPKPPE--PEDLAIICFTSGTTGNPKGAMITHQNI------INDCSGFIKATESALtlnasdtq 317
Cdd:PRK08180 184 ATPFAALLATPPTAAVDAAHAAvgPDTIAKFLFTSGSTGLPKAVINTHRMLcanqqmLAQTFPFLAEEPPVL-------- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 318 ISYLPLAH---------MyeqqlqcvMLCHGAKI---------GFFQGDIRllmdDLKVLQPTIFPVVPR---------- 369
Cdd:PRK08180 256 VDWLPWNHtfggnhnlgI--------VLYNGGTLyiddgkptpGGFDETLR----NLREISPTVYFNVPKgwemlvpale 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 370 ----LLNRMFDRifgqantsLKrwLLDFASkrkeAELRSgivrnnSLWDKLifHKI-QSSLGGKVRLMitgaapvsatvl 444
Cdd:PRK08180 324 rdaaLRRRFFSR--------LK--LLFYAG----AALSQ------DVWDRL--DRVaEATCGERIRMM------------ 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 445 tflrTALGCqfyegygqTEcTAGCCLSL--PGDwTAGHVGAPMPCNYVKLVDVEemnylaskGEGEVCVKGANVFKGYLK 522
Cdd:PRK08180 370 ----TGLGM--------TE-TAPSATFTtgPLS-RAGNIGLPAPGCEVKLVPVG--------GKLEVRVKGPNVTPGYWR 427
|
490 500
....*....|....*....|...
gi 1720426399 523 DPARTAEALDKDGWLHTGDIGKW 545
Cdd:PRK08180 428 APELTAEAFDEEGYYRSGDAVRF 450
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
122-616 |
6.61e-23 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 102.66 E-value: 6.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 122 ISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:cd12117 23 LTYAELNERANRLARRLRAAGVGP--GDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 202 DKPEKAKLLLegvenklTPCLKIIVIMDSYGSDLVERGkkcgveiislkaledlgrvnrvkpkPPEPEDLAIICFTSGTT 281
Cdd:cd12117 101 DRSLAGRAGG-------LEVAVVIDEALDAGPAGNPAV-------------------------PVSPDDLAYVMYTSGST 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 282 GNPKGAMITHQNIINDCSGfikatESALTLNASDTQISYLPL---AHMYEQQlqcVMLCHGAKIgffqgdirllmddlkV 358
Cdd:cd12117 149 GRPKGVAVTHRGVVRLVKN-----TNYVTLGPDDRVLQTSPLafdASTFEIW---GALLNGARL---------------V 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 359 LQPtifPVVPRLLNRMFDRIFGQANTSLkrWLldfaskrkEAELRSGIVRNNSlwdklifhkiqSSLGGkVRLMITGAAP 438
Cdd:cd12117 206 LAP---KGTLLDPDALGALIAEEGVTVL--WL--------TAALFNQLADEDP-----------ECFAG-LRELLTGGEV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 439 VS-ATVLTFLRTALGCQFYEGYGQTECT--AGCCLSLPGDWTAGHV--GAPMPCNYVKLVDveEMNYLASKGE-GEVCVK 512
Cdd:cd12117 261 VSpPHVRRVLAACPGLRLVNGYGPTENTtfTTSHVVTELDEVAGSIpiGRPIANTRVYVLD--EDGRPVPPGVpGELYVG 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 513 GANVFKGYLKDPARTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQ 586
Cdd:cd12117 339 GDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI-RGFRIELGEIEAALRAHPGVRE 417
|
490 500 510
....*....|....*....|....*....|....*..
gi 1720426399 587 VFV------HGE-SLQAFLIAVVVPDVESLPSWAQKR 616
Cdd:cd12117 418 AVVvvredaGGDkRLVAYVVAEGALDAAELRAFLRER 454
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
122-609 |
2.01e-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: 101.43 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 122 ISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAEL-SVIF 200
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRP--GQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMtAAVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 201 ADkpekAKLLLEGvenkltpclkiivIMDSygsdlvergkkcGVEIISLKALEDLGRVNR----VKPKPPEPEDLAIICF 276
Cdd:cd05923 107 AV----DAQVMDA-------------IFQS------------GVRVLALSDLVGLGEPESagplIEDPPREPEQPAFVFY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 277 TSGTTGNPKGAMITHQNIinDCSGFIKATESALTLNASDTQISYLPLAHMyeqqlqcvmlchgakIGFFQgdirLLMDDL 356
Cdd:cd05923 158 TSGTTGLPKGAVIPQRAA--ESRVLFMSTQAGLRHGRHNVVLGLMPLYHV---------------IGFFA----VLVAAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 357 kVLQPTIFPVvprllnRMFDRIFgqantslkrwlldfASKRKEAELRSGIVRNNSLWDKLIFHKIQSSLGGK-VRLMITG 435
Cdd:cd05923 217 -ALDGTYVVV------EEFDPAD--------------ALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSsLRHVTFA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 436 AAPVSATVLTFLRTALGCQFYEGYGQTEctAGCCLSLPgDWTAGHVGAPMPCNYVKLVDV-EEMNYLASKG-EGEVCVK- 512
Cdd:cd05923 276 GATMPDAVLERVNQHLPGEKVNIYGTTE--AMNSLYMR-DARTGTEMRPGFFSEVRIVRIgGSPDEALANGeEGELIVAa 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 513 -GANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:cd05923 353 aADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIG 430
|
490 500
....*....|....*....|.
gi 1720426399 592 ---ESLQAFLIAVVVPDVESL 609
Cdd:cd05923 431 vadERWGQSVTACVVPREGTL 451
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
128-591 |
2.85e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 100.65 E-value: 2.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 128 AELAECIG--SGLIQK-GFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFADkp 204
Cdd:PRK09088 26 AELDALVGrlAAVLRRrGCVD--GERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGD-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 205 ekaklllegvenkltpclkiivimdsygsDLVERGKKCGVEIISLKALEDLGRVNRVKPKPPEpeDLAIICFTSGTTGNP 284
Cdd:PRK09088 102 -----------------------------DAVAAGRTDVEDLAAFIASADALEPADTPSIPPE--RVSLILFTSGTSGQP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 285 KGAMITHQNIINDCSGFIKATESaltlnasDTQISYLPLAHMYeqqlQCVMLCHGAKIGFFQGDIRLLMDDLkvlQPTif 364
Cdd:PRK09088 151 KGVMLSERNLQQTAHNFGVLGRV-------DAHSSFLCDAPMF----HIIGLITSVRPVLAVGGSILVSNGF---EPK-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 365 pvvpRLLNRMFDRIFGQANTslkrwlldFASKRKEAELRSGIVRNNSLWDKLIfhkiqsslggkvrLMITGAAP-VSATV 443
Cdd:PRK09088 215 ----RTLGRLGDPALGITHY--------FCVPQMAQAFRAQPGFDAAALRHLT-------------ALFTGGAPhAAEDI 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 444 LTFLrtALGCQFYEGYGQTEctAGCCLSLPGDWT-----AGHVGAPMPCNYVKLVDVEEMNYLAskGE-GEVCVKGANVF 517
Cdd:PRK09088 270 LGWL--DDGIPMVDGFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVVDDQGNDCPA--GVpGELLLRGPNLS 343
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720426399 518 KGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:PRK09088 344 PGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIEAVLADHPGIRECAVVG 416
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
267-619 |
3.56e-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: 99.81 E-value: 3.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 267 EPEDLAIICFTSGTTGNPKGAMITHQNIIndcsGFIKATESALTLNASDTQISYLPlahmyeqqlqcvmlchgAKIGFFQ 346
Cdd:cd05971 86 GSDDPALIIYTSGTTGPPKGALHAHRVLL----GHLPGVQFPFNLFPRDGDLYWTP-----------------ADWAWIG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 347 GdirlLMDdlkVLQPTIFPVVPRLLNRM--FDRifGQANTSLKRWLLDFASKRKEAeLRsgIVRnnslwdkliFHKIQSS 424
Cdd:cd05971 145 G----LLD---VLLPSLYFGVPVLAHRMtkFDP--KAALDLMSRYGVTTAFLPPTA-LK--MMR---------QQGEQLK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 425 LGG-KVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTA--GCCLSLpGDWTAGHVGAPMPCNYVKLVDvEEMNYL 501
Cdd:cd05971 204 HAQvKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLviGNCSAL-FPIKPGSMGKPIPGHRVAIVD-DNGTPL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 502 ASKGEGEVCVK--GANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYL 579
Cdd:cd05971 282 PPGEVGEIAVElpDPVAFLGYWNNPSATEKKM-AGDWLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAEIEECLL 359
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1720426399 580 RSEAVAQVFV-------HGESLQAFLiaVVVPDVEslPSWAQKRGLQ 619
Cdd:cd05971 360 KHPAVLMAAVvgipdpiRGEIVKAFV--VLNPGET--PSDALAREIQ 402
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
265-617 |
4.32e-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: 100.11 E-value: 4.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 265 PPEPEDLAIICFTSGTTGNPKGAMITHQNIINdcsgFIKATESALTLNASDTQISYLPLAHMYEQQLQCVMLCHGAKIGF 344
Cdd:cd17651 132 ALDADDLAYVIYTSGSTGRPKGVVMPHRSLAN----LVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 345 FQGDIRllMDDLKVLqptifpvvpRLLNRM-FDRIFgqANTSLKRWLLdfaskrkeAELRSGIVRNNSLwdklifhkiqs 423
Cdd:cd17651 208 PPEEVR--TDPPALA---------AWLDEQrISRVF--LPTVALRALA--------EHGRPLGVRLAAL----------- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 424 slggkvRLMITGAAPVSATVLT--FLRTALGCQFYEGYGQTECTAGCCLSLPGD---WTA-GHVGAPMPCNYVKLVDvEE 497
Cdd:cd17651 256 ------RYLLTGGEQLVLTEDLreFCAGLPGLRLHNHYGPTETHVVTALSLPGDpaaWPApPPIGRPIDNTRVYVLD-AA 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 498 MNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAP 571
Cdd:cd17651 329 LRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGFRIEL 407
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1720426399 572 EKIENIYLRSEAVAQ--VFVHGE-SLQAFLIAVVVPDVESLPSWAQKRG 617
Cdd:cd17651 408 GEIEAALARHPGVREavVLAREDrPGEKRLVAYVVGDPEAPVDAAELRA 456
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
267-607 |
1.93e-21 |
|
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: 97.70 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 267 EPEDLAIICFTSGTTGNPKGAMITHQNIINdcsgFIKATESALTLNAsdtqisylplahmyeqqlQCVMLCHgAKIGFfq 346
Cdd:cd05945 95 DGDDNAYIIFTSGSTGRPKGVQISHDNLVS----FTNWMLSDFPLGP------------------GDVFLNQ-APFSF-- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 347 gdirllmdDLKVLqpTIFP---------VVPRLLNRMFDRIFgqantslkRWLLdfaskrkeaelRSGI---VRNNSLWD 414
Cdd:cd05945 150 --------DLSVM--DLYPalasgatlvPVPRDATADPKQLF--------RFLA-----------EHGItvwVSTPSFAA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 415 KLIFHK--IQSSLGGkVRLMITGAAPVSATVLTFLRTAL-GCQFYEGYGQTECTAGCCL------------SLPgdwtag 479
Cdd:cd05945 201 MCLLSPtfTPESLPS-LRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEATVAVTYievtpevldgydRLP------ 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 480 hVGAPMPCnyVKLVDVEEMNYLASKGE-GEVCVKGANVFKGYLKDPARTAEALDKD---GWLHTGDIGKWLPNGTLKIID 555
Cdd:cd05945 274 -IGYAKPG--AKLVILDEDGRPVPPGEkGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRG 350
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720426399 556 RKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFV----HGESLQAfLIAVVVPDVE 607
Cdd:cd05945 351 RLDFQVKL-NGYRIELEEIEAALRQVPGVKEAVVvpkyKGEKVTE-LIAFVVPKPG 404
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
265-599 |
4.49e-21 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 97.45 E-value: 4.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 265 PPEPEDLAIICFTSGTTGNPKGAMITHQNIIndCSGFIKATESALTlnASDTQISYLPLAHMyeqQLQCV----MLCHGA 340
Cdd:PRK08008 169 PLSTDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYYSAWQCALR--DDDVYLTVMPAFHI---DCQCTaamaAFSAGA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 341 KIGF--------FQGDIRLLmddlkvlQPTIFPVVPRLLNRMfdrifgqantslkrwLLDFASKRKeaelrsgivRNNSL 412
Cdd:PRK08008 242 TFVLlekysaraFWGQVCKY-------RATITECIPMMIRTL---------------MVQPPSAND---------RQHCL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 413 WDKLIFhkiqsslggkvrLMITgaapvSATVLTFLrTALGCQFYEGYGQTECTAGCCLSLPGD---WTAghVGAPMPCNY 489
Cdd:PRK08008 291 REVMFY------------LNLS-----DQEKDAFE-ERFGVRLLTSYGMTETIVGIIGDRPGDkrrWPS--IGRPGFCYE 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 490 VKLVDvEEMNYLASKGEGEVCVKGA---NVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqG 566
Cdd:PRK08008 351 AEIRD-DHNRPLPAGEIGEICIKGVpgkTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-G 428
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1720426399 567 EYIAPEKIENIYLRSEAVAQVFVHG-------ESLQAFLI 599
Cdd:PRK08008 429 ENVSCVELENIIATHPKIQDIVVVGikdsirdEAIKAFVV 468
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
113-607 |
4.64e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 97.34 E-value: 4.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 113 RKPNQPYEW-----ISYKEVAELAECIGSGLIQK-GFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADA 186
Cdd:PRK08314 22 RYPDKTAIVfygraISYRELLEEAERLAGYLQQEcGVRKGDR--VLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 187 ITYIVNKAELSVIFAdkpekAKLLLEGVE--NKLTPCLKIIV-----IMDSYGSDLVERGkkCGVEIiSLKALEDLGRV- 258
Cdd:PRK08314 100 LAHYVTDSGARVAIV-----GSELAPKVApaVGNLRLRHVIVaqysdYLPAEPEIAVPAW--LRAEP-PLQALAPGGVVa 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 259 ------NRVKPKPPE--PEDLAIICFTSGTTGNPKGAMITHQNIINDCSGfikateSAL--TLNASDTQISYLPLAHMye 328
Cdd:PRK08314 172 wkealaAGLAPPPHTagPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVG------SVLwsNSTPESVVLAVLPLFHV-- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 329 QQLQCVMlcHGAkigFFQGDIRLLMddlkvlqptifP-----VVPRLLNRMfdRIFGQANTSlkRWLLDF-ASKR-KEAE 401
Cdd:PRK08314 244 TGMVHSM--NAP---IYAGATVVLM-----------PrwdreAAARLIERY--RVTHWTNIP--TMVVDFlASPGlAERD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 402 LRSgivrnnsLWdklifhkiqsSLGGkvrlmitGAAPVSATVLTFLRTALGCQFYEGYGQTECTAG-----------CCL 470
Cdd:PRK08314 304 LSS-------LR----------YIGG-------GGAAMPEAVAERLKELTGLDYVEGYGLTETMAQthsnppdrpklQCL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 471 SLPgdwTAGhVGApmpcnyvKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEA---LDKDGWLHTGDIGKWLP 547
Cdd:PRK08314 360 GIP---TFG-VDA-------RVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDE 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720426399 548 NGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEAVAQVFV-------HGESLQafliAVVVPDVE 607
Cdd:PRK08314 429 EGYFFITDRLKRMIN-ASGFKVWPAEVENLLYKHPAIQEACViatpdprRGETVK----AVVVLRPE 490
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
267-616 |
1.43e-20 |
|
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: 95.19 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 267 EPEDLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKA----TESALTLNAS---DTQIsylplahmyeQQLQcVMLCHG 339
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEygitSSDRVLQFASiafDVAA----------EEIY-VTLLSG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 340 AKIgffqgdirllmddlkVLQPtifpvvprllNRMFdrifgqantslkRWLLDFASKRKEAELRsgiVRN--NSLWDKLI 417
Cdd:cd17644 173 ATL---------------VLRP----------EEMR------------SSLEDFVQYIQQWQLT---VLSlpPAYWHLLV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 418 FHKIQSSLGG--KVRLMITGAAPVSATVLTFLRTALG--CQFYEGYGQTECTAGCCLSLPGDWTAGH-----VGAPMPC- 487
Cdd:cd17644 213 LELLLSTIDLpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIANt 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 488 ------NYVKLVDVEEMnylaskgeGEVCVKGANVFKGYLKDPARTAEALDKDGWLH--------TGDIGKWLPNGTLKI 553
Cdd:cd17644 293 qvyildENLQPVPVGVP--------GELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEY 364
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720426399 554 IDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFV---HGESLQAFLIAVVVPDVESLPSWAQKR 616
Cdd:cd17644 365 LGRIDNQVKI-RGFRIELGEIEAVLSQHNDVKTAVVivrEDQPGNKRLVAYIVPHYEESPSTVELR 429
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
120-609 |
1.63e-20 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 95.60 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 120 EWISYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVI 199
Cdd:PRK06155 45 TRWTYAEAARAAAAAAHALAAAGVKRGDR--VALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 200 FADkpekAKLL--LEGVENKLTPcLKIIVIMDSYGSDLVERGkkcgVEIISLKALEDlgrvnRVKPKPPEPEDLAIICFT 277
Cdd:PRK06155 123 VVE----AALLaaLEAADPGDLP-LPAVWLLDAPASVSVPAG----WSTAPLPPLDA-----PAPAAAVQPGDTAAILYT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 278 SGTTGNPKGAMITHQNIindcsgFIKATESA--LTLNASDTQISYLPLAHMYEQQLQCVMLCHGAKI---------GFFq 346
Cdd:PRK06155 189 SGTTGPSKGVCCPHAQF------YWWGRNSAedLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYvleprfsasGFW- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 347 gdirllmDDLKVLQPTIF----PVVPRLLnrmfdrifgqantslkrwlldfaSKRKEAELRSgivrnnslwdklifHKIQ 422
Cdd:PRK06155 262 -------PAVRRHGATVTyllgAMVSILL-----------------------SQPARESDRA--------------HRVR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 423 SSLGGKvrlmitgaapVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDwTAGHVGAPMPCNYVKLVDvEEMNYLA 502
Cdd:PRK06155 298 VALGPG----------VPAALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSMGRLAPGFEARVVD-EHDQELP 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 503 SKGEGEVCVKGANVF---KGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYL 579
Cdd:PRK06155 366 DGEPGELLLRADEPFafaTGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIKDAIR-RRGENISSFEVEQVLL 443
|
490 500 510
....*....|....*....|....*....|....*.
gi 1720426399 580 RSEAVAQVFVH------GESlqAFLIAVVVPDVESL 609
Cdd:PRK06155 444 SHPAVAAAAVFpvpselGED--EVMAAVVLRDGTAL 477
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
267-616 |
2.38e-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: 94.46 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 267 EPEDLAIICFTSGTTGNPKGAMITHQNIINdcsgfikatesaltlnasdtqiSYLPLAHMYEQQLQCVMLCHGAKIGF-- 344
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVAH----------------------AAHAWRREYELDSFPVRLLQMASFSFdv 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 345 FQGDI-RLLM---------DDLKVLQPTIFpvvpRLLNRMFDRIFgQANTSLKRWLLDFASKRKE--AELRSGIVRNNSL 412
Cdd:cd17650 149 FAGDFaRSLLnggtlvicpDEVKLDPAALY----DLILKSRITLM-ESTPALIRPVMAYVYRNGLdlSAMRLLIVGSDGC 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 413 WDKLiFHKIQSSLGGKVRLmITGAAPVSATVLTflrtalgcQFYEGYGQTECTAGcclSLPgdwtaghVGAPMPCNYVKL 492
Cdd:cd17650 224 KAQD-FKTLAARFGQGMRI-INSYGVTEATIDS--------TYYEEGRDPLGDSA---NVP-------IGRPLPNTAMYV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 493 VDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQG 566
Cdd:cd17650 284 LD-ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI-RG 361
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1720426399 567 EYIAPEKIENIYLRSEAVAQVFV---HGESLQAFLIAVVVPDveSLPSWAQKR 616
Cdd:cd17650 362 FRIELGEIESQLARHPAIDEAVVavrEDKGGEARLCAYVVAA--ATLNTAELR 412
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
122-605 |
4.94e-20 |
|
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: 94.06 E-value: 4.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 122 ISYKEVAELAECIGSGLIQKGFKPcseqfiG---LFsQ--NRPEWVIVEQGCFSysMVVVPLYdTLGAD---AITYIVNK 193
Cdd:COG1021 51 LSYAELDRRADRLAAGLLALGLRP------GdrvVV-QlpNVAEFVIVFFALFR--AGAIPVF-ALPAHrraEISHFAEQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 194 AELS-VIFADKPEK------AKLLLEGVenkltPCLKIIVIMDSYGSDLvergkkcgveiislkALEDLGRVNRVKPKP- 265
Cdd:COG1021 121 SEAVaYIIPDRHRGfdyralARELQAEV-----PSLRHVLVVGDAGEFT---------------SLDALLAAPADLSEPr 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 266 PEPEDLAIICFTSGTTGNPKgaMI--THqniiND--CSgfikATESA--LTLNASDTQISYLPLAHMYeqqlqcVMLCHG 339
Cdd:COG1021 181 PDPDDVAFFQLSGGTTGLPK--LIprTH----DDylYS----VRASAeiCGLDADTVYLAALPAAHNF------PLSSPG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 340 AkIGFFQ--GDIRL-----------LMDDLKVlqpTIFPVVPRLLNRMfdrifgqantslkrwlLDFASKRKeAELrsgi 406
Cdd:COG1021 245 V-LGVLYagGTVVLapdpspdtafpLIERERV---TVTALVPPLALLW----------------LDAAERSR-YDL---- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 407 vrnnslwdklifhkiqSSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTEctaG--CCLSL--PGDWTAGHVG 482
Cdd:COG1021 300 ----------------SSL----RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---GlvNYTRLddPEEVILTTQG 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 483 APM-PCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK-HI 560
Cdd:COG1021 357 RPIsPDDEVRIVD-EDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKdQI 435
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1720426399 561 FKlaQGEYIAPEKIENIYLRSEAVAQVfvhgeslqafliAVV-VPD 605
Cdd:COG1021 436 NR--GGEKIAAEEVENLLLAHPAVHDA------------AVVaMPD 467
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
174-591 |
1.52e-19 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 92.92 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 174 VVVPLYDTLGADAITYIVNKAELSVIFADkPEKAKLLLEGVENklTPCLKIIVIMDSYGSDLVERGKKCGVEIISLKALE 253
Cdd:PRK05620 90 VFNPLNKQLMNDQIVHIINHAEDEVIVAD-PRLAEQLGEILKE--CPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 254 DlGRvNRVKPKPPEPEDLAI-ICFTSGTTGNPKGAMITHQNIINDCSGfIKATESaLTLNASDTQISYLPLAHmyeqqlq 332
Cdd:PRK05620 167 D-GR-STVYDWPELDETTAAaICYSTGTTGAPKGVVYSHRSLYLQSLS-LRTTDS-LAVTHGESFLCCVPIYH------- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 333 cvMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRmfdrifgQANTSlkrwlldfaskrkeaelrsgivrnNSL 412
Cdd:PRK05620 236 --VLSWGVPLAAFMSGTPLVFPGPDLSAPTLAKIIATAMPR-------VAHGV------------------------PTL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 413 WDKLIFHKIQS-----SLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGA---- 483
Cdd:PRK05620 283 WIQLMVHYLKNppermSL----QEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEARWayrv 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 484 -----PMPCNYvKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPART----------------AEALDKDGWLHTGDI 542
Cdd:PRK05620 359 sqgrfPASLEY-RIVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPTEEgggaastfrgedvedaNDRFTADGWLRTGDV 437
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1720426399 543 GKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:PRK05620 438 GSVTRDGFLTIHDRARDVIR-SGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
120-605 |
1.82e-19 |
|
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: 92.30 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 120 EWISYKEVAELAECIGSGLIQKGfkPCSEQFIGLFSQNrPEWVIVEQGCFSYSMVVVPLYD---TLGADAITYIVNKAEL 196
Cdd:cd05931 23 ETLTYAELDRRARAIAARLQAVG--KPGDRVLLLAPPG-LDFVAAFLGCLYAGAIAVPLPPptpGRHAERLAAILADAGP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 197 SVIFADKPEKAKLLLEGVENKLTPCLKIIVImdsygsDLVErgkkcgveiislkaledLGRVNRVKPKPPEPEDLAIICF 276
Cdd:cd05931 100 RVVLTTAAALAAVRAFAASRPAAGTPRLLVV------DLLP-----------------DTSAADWPPPSPDPDDIAYLQY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 277 TSGTTGNPKGAMITHQNIINDCSGFIKATEsaltLNASDTQISYLPLAH-MyeqqlqcvmlchgakiGFFQGdirllmdd 355
Cdd:cd05931 157 TSGSTGTPKGVVVTHRNLLANVRQIRRAYG----LDPGDVVVSWLPLYHdM----------------GLIGG-------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 356 lkVLQPTI--FPVV---PR-LLNRMFdrifgqantslkRWL-----------------LDFASKRKEAELRSGIvrnnsl 412
Cdd:cd05931 209 --LLTPLYsgGPSVlmsPAaFLRRPL------------RWLrlisryratisaapnfaYDLCVRRVRDEDLEGL------ 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 413 wDkLifhkiqsslgGKVRLMITGAAPVSATVLT-FLRTALGCQF-----YEGYGQTECT----------AGCCLSLPGDW 476
Cdd:cd05931 269 -D-L----------SSWRVALNGAEPVRPATLRrFAEAFAPFGFrpeafRPSYGLAEATlfvsggppgtGPVVLRVDRDA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 477 TAGHV----------------GAPMPCNYVKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAE------ALDKD 534
Cdd:cd05931 337 LAGRAvavaaddpaarelvscGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaATDEG 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720426399 535 GWLHTGDIGkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENiylrseAVAQvfVHGESLQAFLIAVVVPD 605
Cdd:cd05931 417 GWLRTGDLG-FLHDGELYITGRLKDLIIVR-GRNHYPQDIEA------TAEE--AHPALRPGCVAAFSVPD 477
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
269-631 |
2.84e-19 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 89.63 E-value: 2.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 269 EDLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKAtesALTLNASDTQISYLPLAHMYEQQLQCVMLCHGAKIGFFQGD 348
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKE---GLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 349 IRL--LMDDLKVLQPTIFPVVPRLLNRMfdrifgqantslkrwLLDFASKRKEAElrsgivrnnslwdklifhkiqsslg 426
Cdd:cd17635 78 TTYksLFKILTTNAVTTTCLVPTLLSKL---------------VSELKSANATVP------------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 427 gKVRLMITGAA-PVSATVLTFLRTALgCQFYEGYGQTECTAGCCLSLPGDWT-AGHVGAPMPCNYVKLVDVEEMNyLASK 504
Cdd:cd17635 118 -SLRLIGYGGSrAIAADVRFIEATGL-TNTAQVYGLSETGTALCLPTDDDSIeINAVGRPYPGVDVYLAATDGIA-GPSA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 505 GEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAV 584
Cdd:cd17635 195 SFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERIAEGVSGV 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1720426399 585 AQVFVH-------GESLQAFLIAVVVPDvESLPSwAQKRGLQGSFEELCRNKDI 631
Cdd:cd17635 273 QECACYeisdeefGELVGLAVVASAELD-ENAIR-ALKHTIRRELEPYARPSTI 324
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
268-592 |
3.58e-19 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 89.85 E-value: 3.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 268 PEDLAIICFTSGTTGNPKGAMITHQNIIndcsgfikATESALTLNA----SDTQISYLPLAHMYEQQLQCVMLchgakig 343
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEV--------YNAWMLALNSlfdpDDVLLCGLPLFHVNGSVVTLLTP------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 344 FFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTSLKRwlldFASKRKEAELrsgivrnnslwdklifhkiqS 423
Cdd:cd05944 66 LASGAHVVLAGPAGYRNPGLFDNFWKLVERYRITSLSTVPTVYAA----LLQVPVNADI--------------------S 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 424 SLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLP-GDWTAGHVGAPMPCNYVKLVDVE-EMNYL 501
Cdd:cd05944 122 SL----RFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKVLDgVGRLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 502 --ASKGE-GEVCVKGANVFKGYLKDpARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 578
Cdd:cd05944 198 rdCAPDEvGEICVAGPGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEAL 275
|
330
....*....|....
gi 1720426399 579 LRSEAVAQVFVHGE 592
Cdd:cd05944 276 LRHPAVAFAGAVGQ 289
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
55-606 |
6.37e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 92.15 E-value: 6.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 55 CDLSMQSVEiagttdgiRRSAVLEDDKLLVYYYDDvRTMYDGFQRGIQVSNNGPCLGSRKpnqpyEWISYKEVAELAECI 134
Cdd:PRK12467 485 GELPLLDAE--------ERARELVRWNAPATEYAP-DCVHQLIEAQARQHPERPALVFGE-----QVLSYAELNRQANRL 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 135 GSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFADkPEKAKLLlegv 214
Cdd:PRK12467 551 AHVLIAAGVGP--DVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQ-SHLLAQL---- 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 215 enkltpclkiivimdsygsDLVErgkkcGVEIISLKALEDL--GRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQ 292
Cdd:PRK12467 624 -------------------PVPA-----GLRSLCLDEPADLlcGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHG 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 293 NIINdcsgFIKATESALTLNASDTQISYLPLAHMYEQQLQCVMLCHGAKIgffqgdirLLMDDLKVLQPTIFpvvprlln 372
Cdd:PRK12467 680 ALAN----YVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATL--------HLLPPDCARDAEAF-------- 739
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 373 rmFDRIFGQANTSLKrwlldfaskrkeaelrsgIVrnNSLWDKLIFHKIQSSLGGKVRLMITGAA-PVSATVLTFlRTAL 451
Cdd:PRK12467 740 --AALMADQGVTVLK------------------IV--PSHLQALLQASRVALPRPQRALVCGGEAlQVDLLARVR-ALGP 796
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 452 GCQFYEGYGQTECTAGC----CLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPART 527
Cdd:PRK12467 797 GARLINHYGPTETTVGVstyeLSDEERDFGNVPIGQPLANLGLYILD-HYLNPVPVGVVGELYIGGAGLARGYHRRPALT 875
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 528 AEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFV--HGESLQAFL 598
Cdd:PRK12467 876 AERFVPDpfgadgGRLYrTGDLARYRADGVIEYLGRMDHQVKI-RGFRIELGEIEARLLAQPGVREAVVlaQPGDAGLQL 954
|
....*...
gi 1720426399 599 IAVVVPDV 606
Cdd:PRK12467 955 VAYLVPAA 962
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
136-577 |
9.85e-19 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 91.18 E-value: 9.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 136 SGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFADKP--EKAKL--LL 211
Cdd:PRK06814 672 GRKLKKNTPP--GENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLTSRAfiEKARLgpLI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 212 EGVENKLtpclKIIVIMDsygsdlVERGKKCGVEIISLKAledlGRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITH 291
Cdd:PRK06814 750 EALEFGI----RIIYLED------VRAQIGLADKIKGLLA----GRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSH 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 292 QNIINDCSgfikATESALTLNASDTQISYLPLAHMYeqqlqcvmlchgakiGFFQGDIRLLMDDLKVL---QPTIFPVVP 368
Cdd:PRK06814 816 RNLLANRA----QVAARIDFSPEDKVFNALPVFHSF---------------GLTGGLVLPLLSGVKVFlypSPLHYRIIP 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 369 RLLnrmFDR----IFGqANTSLKRWL-----LDFASkrkeaelrsgivrnnslwdklifhkiqsslggkVRLMITGAAPV 439
Cdd:PRK06814 877 ELI---YDTnatiLFG-TDTFLNGYAryahpYDFRS---------------------------------LRYVFAGAEKV 919
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 440 SATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDVEEMNylasKGeGEVCVKGANVFKG 519
Cdd:PRK06814 920 KEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGID----EG-GRLFVRGPNVMLG 994
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720426399 520 YLK-DPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 577
Cdd:PRK06814 995 YLRaENPGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAVEEL 1051
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
122-605 |
1.58e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 91.17 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 122 ISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGVGP--EVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLT 2106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 202 DKPEKAKLLLEGvenkltpclkiivimdsygsdlvergkkcGVEIISLKALEDLGRVNRVKPKPP-EPEDLAIICFTSGT 280
Cdd:PRK12316 2107 QRHLLERLPLPA-----------------------------GVARLPLDRDAEWADYPDTAPAVQlAGENLAYVIYTSGS 2157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 281 TGNPKGAMITHQNIINdcsgFIKATESALTLNASDTQISYLPLAH--MYEQQLqcVMLCHGAkigffqgdiRLLMDDLKV 358
Cdd:PRK12316 2158 TGLPKGVAVSHGALVA----HCQAAGERYELSPADCELQFMSFSFdgAHEQWF--HPLLNGA---------RVLIRDDEL 2222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 359 LQPtifpvvprllNRMFDRIFGQANTslkrwLLDFASkrkeaelrsgivrnnSLWDKLIFHKIQSSLGGKVRLMITGAAP 438
Cdd:PRK12316 2223 WDP----------EQLYDEMERHGVT-----ILDFPP---------------VYLQQLAEHAERDGRPPAVRVYCFGGEA 2272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 439 VSATVLTFLRTALGCQF-YEGYGQTECTA-----GCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVK 512
Cdd:PRK12316 2273 VPAASLRLAWEALRPVYlFNGYGPTEAVVtpllwKCRPQDPCGAAYVPIGRALGNRRAYILD-ADLNLLAPGMAGELYLG 2351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 513 GANVFKGYLKDPARTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVA 585
Cdd:PRK12316 2352 GEGLARGYLNRPGLTAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKI-RGFRIELGEIEARLQAHPAVR 2430
|
490 500
....*....|....*....|...
gi 1720426399 586 QVFV---HGESLQAfLIAVVVPD 605
Cdd:PRK12316 2431 EAVVvaqDGASGKQ-LVAYVVPD 2452
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
267-600 |
3.15e-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: 87.90 E-value: 3.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 267 EPEDLAIICFTSGTTGNPKGAMITHQNIINDCSGFikATEsALTLNASDTQISylpLAHMYEQqlqcVMLCHGAKIGFFQ 346
Cdd:cd05919 89 SADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAM--ARE-ALGLTPGDRVFS---SAKMFFG----YGLGNSLWFPLAV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 347 GDIRLLMDD----------LKVLQPTIFPVVPRLLNRMFDrifgQANTSlkrwlldfaskrkEAELRSgivrnnslwdkl 416
Cdd:cd05919 159 GASAVLNPGwptaervlatLARFRPTVLYGVPTFYANLLD----SCAGS-------------PDALRS------------ 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 417 ifhkiqsslggkVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDvE 496
Cdd:cd05919 210 ------------LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD-E 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 497 EMNYLASKGEGEVCVKGANVFKGYLKDPaRTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEN 576
Cdd:cd05919 277 EGHTIPPGEEGDLLVRGPSAAVGYWNNP-EKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVES 354
|
330 340 350
....*....|....*....|....*....|.
gi 1720426399 577 IYLRSEAVAQVFV------HGES-LQAFLIA 600
Cdd:cd05919 355 LIIQHPAVAEAAVvavpesTGLSrLTAFVVL 385
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
182-627 |
3.39e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 88.47 E-value: 3.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 182 LGADAITYIVNKAELSVIFADkPEKAKLLLEGVEnkLTPCLKIIVI---MDSYGsdlvergkkcGVEIISLKALEDL--- 255
Cdd:PRK08162 102 LDAASIAFMLRHGEAKVLIVD-TEFAEVAREALA--LLPGPKPLVIdvdDPEYP----------GGRFIGALDYEAFlas 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 256 GRVNRVkPKPPEPEDLAI-ICFTSGTTGNPKGAMITHQniindcsgfikatesALTLNASDTQISY-----------LPL 323
Cdd:PRK08162 169 GDPDFA-WTLPADEWDAIaLNYTSGTTGNPKGVVYHHR---------------GAYLNALSNILAWgmpkhpvylwtLPM 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 324 AHmyeqqlqCVMLCH--------GAKIGFFQGDIRLLMDDLKVLQPTIF---PVVPRLLnrmfdrifgqANTslkrwlld 392
Cdd:PRK08162 233 FH-------CNGWCFpwtvaaraGTNVCLRKVDPKLIFDLIREHGVTHYcgaPIVLSAL----------INA-------- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 393 faskrkEAELRSGIvrnnslwdklifhkiqsslGGKVRLMITGAAPVSAtVLTFLRtALGCQFYEGYGQTEC--TAGCCL 470
Cdd:PRK08162 288 ------PAEWRAGI-------------------DHPVHAMVAGAAPPAA-VIAKME-EIGFDLTHVYGLTETygPATVCA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 471 SLPGdWTA----------GHVGAPMPC-NYVKLVDVEEMNYLASKGE--GEVCVKGANVFKGYLKDPARTAEALdKDGWL 537
Cdd:PRK08162 341 WQPE-WDAlplderaqlkARQGVRYPLqEGVTVLDPDTMQPVPADGEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 538 HTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVaqvfvhgeslqafLIAVVV--PDveslPSWAQ- 614
Cdd:PRK08162 419 HTGDLAVLHPDGYIKIKDRSKDII-ISGGENISSIEVEDVLYRHPAV-------------LVAAVVakPD----PKWGEv 480
|
490 500
....*....|....*....|...
gi 1720426399 615 -------KRGLQGSFEEL---CR 627
Cdd:PRK08162 481 pcafvelKDGASATEEEIiahCR 503
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
169-591 |
6.33e-18 |
|
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: 87.55 E-value: 6.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 169 FSYSM--------VVVPLYDTLGADAITYIVNKAELSVIFADKpekAKLLLEGVENKLTPCLKIIVIMDSYGSDlveRGK 240
Cdd:cd05970 85 FWYSLlalhklgaIAIPATHQLTAKDIVYRIESADIKMIVAIA---EDNIPEEIEKAAPECPSKPKLVWVGDPV---PEG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 241 KCGVEIISLKALEDLGRvnRVKPKPPEPEDLAIICFTSGTTGNPKgaMITHQNI-----INDCSGFIKATESALTLNASD 315
Cdd:cd05970 159 WIDFRKLIKNASPDFER--PTANSYPCGEDILLVYFSSGTTGMPK--MVEHDFTyplghIVTAKYWQNVREGGLHLTVAD 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 316 TQISYLPLAHMYEQQLQcvmlchGAKI---GFFQGDIRLLMDDLKVLQPTIF---PVVPRLLNRmfdrifgqanTSLKRW 389
Cdd:cd05970 235 TGWGKAVWGKIYGQWIA------GAAVfvyDYDKFDPKALLEKLSKYGVTTFcapPTIYRFLIR----------EDLSRY 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 390 llDFASkrkeaelrsgivrnnslwdklifhkiqsslggkVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAgCC 469
Cdd:cd05970 299 --DLSS---------------------------------LRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTL-TI 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 470 LSLPG-DWTAGHVGAPMPCNYVKLVDVEEMNYLASKgEGEVCVKGAN-----VFKGYLKDPARTAEALdKDGWLHTGDIG 543
Cdd:cd05970 343 ATFPWmEPKPGSMGKPAPGYEIDLIDREGRSCEAGE-EGEIVIRTSKgkpvgLFGGYYKDAEKTAEVW-HDGYYHTGDAA 420
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1720426399 544 KWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:cd05970 421 WMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVESALIQHPAVLECAVTG 467
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
122-616 |
8.45e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 87.40 E-value: 8.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 122 ISYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:PRK06178 59 ITYAELDELSDRFAALLRQRGVGAGDR--VAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 202 -DKpekaklLLEGVENKLTPCLKIIVIMDSYGS-----------DLVERGKKCGVEIISLKALEDLGRVNRVKPkPPEPE 269
Cdd:PRK06178 137 lDQ------LAPVVEQVRAETSLRHVIVTSLADvlpaeptlplpDSLRAPRLAAAGAIDLLPALRACTAPVPLP-PPALD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 270 DLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKAtesALTLNASDTQISYLPLahmyeqqlqcvmlchgakigFFqgdi 349
Cdd:PRK06178 210 ALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAV---AVVGGEDSVFLSFLPE--------------------FW---- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 350 rLLMDDLKVLQPTIF--PVVprLLNRmfdrifgqantslkrwlldfaskrkeaelrsgivrnnslWDKLIF------HKI 421
Cdd:PRK06178 263 -IAGENFGLLFPLFSgaTLV--LLAR---------------------------------------WDAVAFmaaverYRV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 422 QSSLG---GKVRLMITGAapVSATVLTFLRTAL--------------------GCQFYEG-YGQTEcTAGCclslpGDWT 477
Cdd:PRK06178 301 TRTVMlvdNAVELMDHPR--FAEYDLSSLRQVRvvsfvkklnpdyrqrwraltGSVLAEAaWGMTE-THTC-----DTFT 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 478 AG-------------HVGAPMPCNYVKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGK 544
Cdd:PRK06178 373 AGfqdddfdllsqpvFVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGK 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 545 WLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFV-------HGESLQAFLiaVVVP----DVESLPSWA 613
Cdd:PRK06178 452 IDEQGFLHYLGRRKEMLKV-NGMSVFPSEVEALLGQHPAVLGSAVvgrpdpdKGQVPVAFV--QLKPgadlTAAALQAWC 528
|
...
gi 1720426399 614 QKR 616
Cdd:PRK06178 529 REN 531
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
267-616 |
1.20e-17 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 86.21 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 267 EPEDLAIICFTSGTTGNPKGAMITHQNIIndcsGFIKATESALTLNASDTQIsylpLAHMY-------EQQLQcvmLCHG 339
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVL----ALFAATQRWFGFNEDDVWT----LFHSYafdfsvwEIWGA---LLHG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 340 AKIGFFQGDIRLLMDDLkvlqptifpvvPRLLNRMFDRIFGQANTSLKRWLldfaskrkEAELRsgivrnnslwdkliFH 419
Cdd:cd17643 160 GRLVVVPYEVARSPEDF-----------ARLLRDEGVTVLNQTPSAFYQLV--------EAADR--------------DG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 420 KIQSSLggkvRLMITGAAPVSATVLT--FLRTALGC-QFYEGYGQTECTAGCCL------SLPGDwTAGHVGAPMPCNYV 490
Cdd:cd17643 207 RDPLAL----RYVIFGGEALEAAMLRpwAGRFGLDRpQLVNMYGITETTVHVTFrpldaaDLPAA-AASPIGRPLPGLRV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 491 KLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAE-------ALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKL 563
Cdd:cd17643 282 YVLD-ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720426399 564 aQGEYIAPEKIENIYLRSEAVAQVFV---HGESLQAFLIAVVVPDVESLPSWAQKR 616
Cdd:cd17643 361 -RGFRIELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVADDGAAADIAELR 415
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
116-688 |
1.22e-17 |
|
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: 86.39 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 116 NQPYEWISYKEVAELAECIGSGLIQKGFKPCSEQFIGLfsQNRPEWVIVEQGCFSYSMVVVPlydtlgadaityivnkae 195
Cdd:cd05908 10 DKKEKFVSYRHLREEALGYLGALQELGIKPGQEVVFQI--THNNKFLYLFWACLLGGMIAVP------------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 196 lsvIFADKPEKAKLLLEGVENKLT-PCLkiivimdsygsdlvergkkcgveIISLKALEDLgrvnrvkpkppePEDLAII 274
Cdd:cd05908 70 ---VSIGSNEEHKLKLNKVWNTLKnPYL-----------------------ITEEEVLCEL------------ADELAFI 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 275 CFTSGTTGNPKGAMITHQNIINDCSGFIKATEsaltLNASDTQISYLPLAH---MYEQQLQCVMlchgakigffQGDIRL 351
Cdd:cd05908 112 QFSSGSTGDPKGVMLTHENLVHNMFAILNSTE----WKTKDRILSWMPLTHdmgLIAFHLAPLI----------AGMNQY 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 352 LMddlkvlqPT-IFPVVPRLlnrmfdrifgqantslkrWLLDfASKRKEAELRSGIVRNNSLWDKLIFHKIQSSLGGKVR 430
Cdd:cd05908 178 LM-------PTrLFIRRPIL------------------WLKK-ASEHKATIVSSPNFGYKYFLKTLKPEKANDWDLSSIR 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 431 LMITGAAPVSATVLTFLRTALGC------QFYEGYGQTECTAGCCLSLPGD----------------------------W 476
Cdd:cd05908 232 MILNGAEPIDYELCHEFLDHMSKyglkrnAILPVYGLAEASVGASLPKAQSpfktitlgrrhvthgepepevdkkdsecL 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 477 TAGHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGkWLPNGTLKIIDR 556
Cdd:cd05908 312 TFVEVGKPIDETDIRICD-EDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIRNGRLVITGR 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 557 KKHIFkLAQGEYIAPEKIENiylrseavaqvfvhgeslqaflIAVVVPDVESlpswaQKRGLQGSFEELCRNKDI----- 631
Cdd:cd05908 390 EKDII-FVNGQNVYPHDIER----------------------IAEELEGVEL-----GRVVACGVNNSNTRNEEIfcfie 441
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720426399 632 NKAILDDLLKLGKEAGlKPFEQVKGIAVHpELFSIDNGLLTPTLKAKRPELRNYFRS 688
Cdd:cd05908 442 HRKSEDDFYPLGKKIK-KHLNKRGGWQIN-EVLPIRRIPKTTSGKVKRYELAQRYQS 496
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
268-683 |
1.41e-17 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 86.78 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 268 PEDLAIICFTSGTTGNPKGAMITHQNIINDCSGFIkateSALTLNASDTQISYLPLAHM--YEQQLQCVML--CHGAKIG 343
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKI----AIVGYGEDDVYLHTAPLCHIggLSSALAMLMVgaCHVLLPK 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 344 FfqgDIRLLMDDLKVLQPTIFPVVPRLL------NRMfdRIFGQANTSLKRwLLDFAskrkeaelrsGIVRNNSLWD-KL 416
Cdd:PLN02860 247 F---DAKAALQAIKQHNVTSMITVPAMMadlislTRK--SMTWKVFPSVRK-ILNGG----------GSLSSRLLPDaKK 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 417 IF--HKIQSSLGgkvrlmITGAApvsaTVLTFLRtaLGCQFYEGYGQTECTAGCCLSLPGDWTAGH-VGAPMPcnYVKLv 493
Cdd:PLN02860 311 LFpnAKLFSAYG------MTEAC----SSLTFMT--LHDPTLESPKQTLQTVNQTKSSSVHQPQGVcVGKPAP--HVEL- 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 494 dveEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEK 573
Cdd:PLN02860 376 ---KIGLDESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIK-TGGENVYPEE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 574 IENIYLRSEAVAQVFVHGeSLQAFLIAVVVPDVESLPSW--------AQKRGLQGSFEEL---CRNKdinkailddllkl 642
Cdd:PLN02860 452 VEAVLSQHPGVASVVVVG-VPDSRLTEMVVACVRLRDGWiwsdnekeNAKKNLTLSSETLrhhCREK------------- 517
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1720426399 643 gkeaGLKPFEQVKGIAVHPELFSidnglLTPTLKAKRPELR 683
Cdd:PLN02860 518 ----NLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEVR 549
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
267-614 |
1.89e-17 |
|
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: 85.50 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 267 EPEDLAIICFTSGTTGNPKGAMITHQNIINDCsgfiKATESALTLNASDTQISYLPLAhmYEQQLQCVM--LCHGAkigf 344
Cdd:cd17649 92 HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHC----QATAERYGLTPGDRELQFASFN--FDGAHEQLLppLICGA---- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 345 fqgdiRLLMDDLKVLQPtifpvvPRLLNRMFDR----IFGQANTSLKRWLLDFASKrkeaelrsgivrnnslwdklifhk 420
Cdd:cd17649 162 -----CVVLRPDELWAS------ADELAEMVRElgvtVLDLPPAYLQQLAEEADRT------------------------ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 421 iQSSLGGKVRLMITGAAPVSATVLTFLRTAlGCQFYEGYGQTEC--TAGCCLSLPGDWTAGH---VGAPMPcNYVKLVDV 495
Cdd:cd17649 207 -GDGRPPSLRLYIFGGEALSPELLRRWLKA-PVRLFNAYGPTEAtvTPLVWKCEAGAARAGAsmpIGRPLG-GRSAYILD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 496 EEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEAL--DKDG-----WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEY 568
Cdd:cd17649 284 ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFvpDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-RGFR 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1720426399 569 IAPEKIENIYLRSEAVAQVFVHGES--LQAFLIAVVVP-DVESLPSWAQ 614
Cdd:cd17649 363 IELGEIEAALLEHPGVREAAVVALDgaGGKQLVAYVVLrAAAAQPELRA 411
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
267-615 |
3.46e-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: 84.53 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 267 EPEDLAIICFTSGTTGNPKGAMITHQNIINDCSGFikatESALTLNASDTQISYLPL---AHMYEqqlqcvMLCH---GA 340
Cdd:cd17645 102 NPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWH----RPYFGVTPADKSLVYASFsfdASAWE------IFPHltaGA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 341 KIGFFQGDIRLLMDDLkvlqptifpvvprllnrmfDRIFGQANTSLKRWLLDFASKRKEAElrsgivrNNSLwdklifhk 420
Cdd:cd17645 172 ALHVVPSERRLDLDAL-------------------NDYFNQEGITISFLPTGAAEQFMQLD-------NQSL-------- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 421 iqsslggkvRLMITGAAPVSATVLTflrtalGCQFYEGYGQTECTAgCCLSLPGDWTAGHVGAPMPCNYVKLVDVEEMNY 500
Cdd:cd17645 218 ---------RVLLTGGDKLKKIERK------GYKLVNNYGPTENTV-VATSFEIDKPYANIPIGKPIDNTRVYILDEALQ 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 501 LASKG-EGEVCVKGANVFKGYLKDPARTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 573
Cdd:cd17645 282 LQPIGvAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGE 360
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1720426399 574 IENIYLRSEAVAQVFV-------HGESLQAFLIAVVVPDVESLPSWAQK 615
Cdd:cd17645 361 IEPFLMNHPLIELAAVlakedadGRKYLVAYVTAPEEIPHEELREWLKN 409
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
251-575 |
3.92e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 85.05 E-value: 3.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 251 ALEDLGRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKATESALtlnASDTQISYLPLAH-Myeq 329
Cdd:PRK07768 134 TVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDV---ETDVMVSWLPLFHdM--- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 330 qlqcvmlchgAKIGFFQGDIRLLMDDLKVlQPTIFPVVPRLLNRMFDRIFGQ-------ANTSLKRwLLDFASKRKEAEL 402
Cdd:PRK07768 208 ----------GMVGFLTVPMYFGAELVKV-TPMDFLRDPLLWAELISKYRGTmtaapnfAYALLAR-RLRRQAKPGAFDL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 403 rsgivrnnslwdklifhkiqSSLggkvRLMITGAAPVS-ATVLTFL---------RTALGCqfyeGYGQTECTAGCCLSL 472
Cdd:PRK07768 276 --------------------SSL----RFALNGAEPIDpADVEDLLdagarfglrPEAILP----AYGMAEATLAVSFSP 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 473 PGD--------------------WTAGHV------GAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLkDPAR 526
Cdd:PRK07768 328 CGAglvvdevdadllaalrravpATKGNTrrlatlGPPLPGLEVRVVD-EDGQVLPPRGVGVIELRGESVTPGYL-TMDG 405
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1720426399 527 TAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIE 575
Cdd:PRK07768 406 FIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPTDIE 453
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
108-672 |
4.06e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 85.48 E-value: 4.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 108 PCLGSRKPNQ-PYEWISYKEVAELAECIGSGLIQKGFKPCSEQFIglFSQNRPEWVIVEQGCFSYSMVVVPL---YDTLG 183
Cdd:PRK12582 66 PWLAQREPGHgQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMI--LSGNSIEHALMTLAAMQAGVPAAPVspaYSLMS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 184 AD--AITYIVNKAELSVIFADKPEK-----AKLLLEGVEnkltpCLKIIVIMDSYGS----DLVERGKKCGVEiislKAL 252
Cdd:PRK12582 144 HDhaKLKHLFDLVKPRVVFAQSGAPfaralAALDLLDVT-----VVHVTGPGEGIASiafaDLAATPPTAAVA----AAI 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 253 EDLGrvnrvkpkppePEDLAIICFTSGTTGNPKGAMITHQNIindCSgfIKATESALTLNASDTQIS----YLPLAHmye 328
Cdd:PRK12582 215 AAIT-----------PDTVAKYLFTSGSTGMPKAVINTQRMM---CA--NIAMQEQLRPREPDPPPPvsldWMPWNH--- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 329 qqlqcvmlCHGAKIGFfQGDIR----LLMDDLKVLqPTIFPVVPRLLNRMFDRIFGQANTSLKrwLLDFASKRKEAELRS 404
Cdd:PRK12582 276 --------TMGGNANF-NGLLWgggtLYIDDGKPL-PGMFEETIRNLREISPTVYGNVPAGYA--MLAEAMEKDDALRRS 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 405 givrnnslwdkliFHKiqsslggKVRLMITGAAPVSATVLTFLR----TALGCQ--FYEGYGQTEcTAGccLSLPGDWTA 478
Cdd:PRK12582 344 -------------FFK-------NLRLMAYGGATLSDDLYERMQalavRTTGHRipFYTGYGATE-TAP--TTTGTHWDT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 479 ---GHVGAPMPCNYVKLVDVEEmNYlaskgegEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWL----PNGTL 551
Cdd:PRK12582 401 ervGLIGLPLPGVELKLAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdpddPEKGL 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 552 KIIDRKKHIFKLAQGEYIAPEKieniyLRSEAVA-------QVFVHGESlQAFLIAVVVPDVESLPSWAQKRGlqGSFEE 624
Cdd:PRK12582 473 IFDGRVAEDFKLSTGTWVSVGT-----LRPDAVAacspvihDAVVAGQD-RAFIGLLAWPNPAACRQLAGDPD--AAPED 544
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1720426399 625 LCRNKDINKAILDDLLKLGKEAGlKPFEQVKGIAVHPELFSIDNGLLT 672
Cdd:PRK12582 545 VVKHPAVLAILREGLSAHNAEAG-GSSSRIARALLMTEPPSIDAGEIT 591
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
174-591 |
4.76e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 84.55 E-value: 4.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 174 VVVPLYDTLGADAITYIVNKAelsvifadkpeKAKLLLEGVENKLTPCLKI-IVIMDSYGSDLVERGKKCGVEIISLKal 252
Cdd:PRK06145 78 VFLPINYRLAADEVAYILGDA-----------GAKLLLVDEEFDAIVALETpKIVIDAAAQADSRRLAQGGLEIPPQA-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 253 edlgrvnrvkpkPPEPEDLAIICFTSGTTGNPKGAMITHQNIindcsgFIKATES--ALTLNASDTQISYLPLAHMYEQQ 330
Cdd:PRK06145 145 ------------AVAPTDLVRLMYTSGTTDRPKGVMHSYGNL------HWKSIDHviALGLTASERLLVVGPLYHVGAFD 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 331 LQCV-MLCHGAKIGFFQG-DIRLLMDDLKVLQPTIFPVVPRLLNRMF-----DRIfgqaNTSLKRWLLDFASKRKEAELR 403
Cdd:PRK06145 207 LPGIaVLWVGGTLRIHREfDPEAVLAAIERHRLTCAWMAPVMLSRVLtvpdrDRF----DLDSLAWCIGGGEKTPESRIR 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 404 SgivrnnslwdklifhkiqsslggkvrlmitgaapvsatvltFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTA--GHV 481
Cdd:PRK06145 283 D-----------------------------------------FTRVFTRARYIDAYGLTETCSGDTLMEAGREIEkiGST 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 482 GAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIF 561
Cdd:PRK06145 322 GRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMI 399
|
410 420 430
....*....|....*....|....*....|
gi 1720426399 562 kLAQGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:PRK06145 400 -ISGGENIASSEVERVIYELPEVAEAAVIG 428
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
216-607 |
1.06e-16 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 83.38 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 216 NKLTPCLKIIVIMDSYGSDLVergkkcgveiiSLKALEDLGRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNII 295
Cdd:PRK09029 93 EELLPSLTLDFALVLEGENTF-----------SALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 296 NDCSGFIkateSALTLNASDTQISYLPLAHMYEQQLQCVMLCHGAKIGFfqGDIRLLMDDLkvLQPTIFPVVPRLLNRMF 375
Cdd:PRK09029 162 ASAEGVL----SLMPFTAQDSWLLSLPLFHVSGQGIVWRWLYAGATLVV--RDKQPLEQAL--AGCTHASLVPTQLWRLL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 376 DRifGQANTSLKRWLLdfaskrkeaelrsgivrnnslwdklifhkiqsslGGKvrlMItgaapvsATVLTFLRTALGCQF 455
Cdd:PRK09029 234 DN--RSEPLSLKAVLL----------------------------------GGA---AI-------PVELTEQAEQQGIRC 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 456 YEGYGQTECTAGCCL----SLPGdwtaghVGAPMPCNYVKLVDveemnylaskgeGEVCVKGANVFKGYLKDPARTAeAL 531
Cdd:PRK09029 268 WCGYGLTEMASTVCAkradGLAG------VGSPLPGREVKLVD------------GEIWLRGASLALGYWRQGQLVP-LV 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720426399 532 DKDGWLHTGDIGKWLpNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVhgeslqafliaVVVPDVE 607
Cdd:PRK09029 329 NDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQVFV-----------VPVADAE 391
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
111-608 |
2.92e-16 |
|
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: 82.13 E-value: 2.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 111 GSRKPNQPYEWI---------SYKEVAELAECIGSGLIQkgfkPCSEQ---FIGLFSQNRPEWVIVEQGCFSYSMVVVPL 178
Cdd:cd05928 22 GKRPPNPALWWVngkgdevkwSFRELGSLSRKAANVLSG----ACGLQrgdRVAVILPRVPEWWLVNVACIRTGLVFIPG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 179 YDTLGADAITYIVNKAELSVIFADkpEKAKLLLEGVENKlTPCLKIIVIMDSYGSDlvergkkcgvEIISLKALedLGRV 258
Cdd:cd05928 98 TIQLTAKDILYRLQASKAKCIVTS--DELAPEVDSVASE-CPSLKTKLLVSEKSRD----------GWLNFKEL--LNEA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 259 ----NRVKPKPPEPedlAIICFTSGTTGNPKGAMITHQNI---INDCSGFIKA-TESALTLNASDTQISYLPLAHMYEQQ 330
Cdd:cd05928 163 stehHCVETGSQEP---MAIYFTSGTTGSPKMAEHSHSSLglgLKVNGRYWLDlTASDIMWNTSDTGWIKSAWSSLFEPW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 331 LQ--CVMLCHGAKIgffqgDIRLLMDDLKVLQPTIFPVVPRLLnrmfdRIFGQAntslkrwllDFASkrkeaelrsgivr 408
Cdd:cd05928 240 IQgaCVFVHHLPRF-----DPLVILKTLSSYPITTFCGAPTVY-----RMLVQQ---------DLSS------------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 409 nnslwdklifHKIQSslggkVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCN 488
Cdd:cd05928 288 ----------YKFPS-----LQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPY 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 489 YVKLVDvEEMNYLASKGEGEVCV-----KGANVFKGYLKDPARTAEALDKDGWLhTGDIGKWLPNGTLKIIDRKKHIFkL 563
Cdd:cd05928 353 DVQIID-DNGNVLPPGTEGDIGIrvkpiRPFGLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-N 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1720426399 564 AQGEYIAPEKIENIYLRSEAVAQVFV-------HGESLQAFLiaVVVPDVES 608
Cdd:cd05928 430 SSGYRIGPFEVESALIEHPAVVESAVvsspdpiRGEVVKAFV--VLAPQFLS 479
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
169-604 |
3.08e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 82.37 E-value: 3.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 169 FSYSM---VVVPLYDTLGADAITYIVNKAELSVIFADKpEKAKLLLEGVE----NKLTPCLKIIVIMDSygsDLVERgkk 241
Cdd:PLN03102 82 FAVPMagaVLNPINTRLDATSIAAILRHAKPKILFVDR-SFEPLAREVLHllssEDSNLNLPVIFIHEI---DFPKR--- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 242 cgveiISLKALEDLGRVNRVKPKPP---------EPEDLAIICFTSGTTGNPKGAMITHQniindcsGFIKATESALT-- 310
Cdd:PLN03102 155 -----PSSEELDYECLIQRGEPTPSlvarmfriqDEHDPISLNYTSGTTADPKGVVISHR-------GAYLSTLSAIIgw 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 311 -LNASDTQISYLPLAHmyeqqlqcvmlCHGAKIGF---FQGDIRLLMDdlKVLQPTIFPVVprllnrmfdRIFGQANTSL 386
Cdd:PLN03102 223 eMGTCPVYLWTLPMFH-----------CNGWTFTWgtaARGGTSVCMR--HVTAPEIYKNI---------EMHNVTHMCC 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 387 KRWLLDFaskrkeaelrsgIVRNNSLwdklifhkIQSSLGGKVRLMITGAAPVSATVLTFLRtaLGCQFYEGYGQTECTA 466
Cdd:PLN03102 281 VPTVFNI------------LLKGNSL--------DLSPRSGPVHVLTGGSPPPAALVKKVQR--LGFQVMHAYGLTEATG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 467 GCCL--------SLPGDWTAgHVGAPMPCNYVKL--VDVEEMNYLAS-----KGEGEVCVKGANVFKGYLKDPARTAEAL 531
Cdd:PLN03102 339 PVLFcewqdewnRLPENQQM-ELKARQGVSILGLadVDVKNKETQESvprdgKTMGEIVIKGSSIMKGYLKNPKATSEAF 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720426399 532 dKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIylrseavaqVFVHGESLQAFLIAVVVP 604
Cdd:PLN03102 418 -KHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVENV---------LYKYPKVLETAVVAMPHP 479
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
270-600 |
4.76e-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: 81.22 E-value: 4.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 270 DLAIICFTSGTTGNPKGAMITHqniiNDCSGFIKATESALTLNASDTQISYLPLAHMYeqQLQC-----VMLChGAKIGF 344
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTH----NDYAYNVRASAEVCGLDQDTVYLAVLPAAHNF--PLACpgvlgTLLA-GGRVVL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 345 FQ----GDIRLLMDDLKVlqpTIFPVVPRLLnrmfdrifgqantslKRWLlDFASKRKEAElrsgivrnnslwdklifhk 420
Cdd:cd05920 213 APdpspDAAFPLIEREGV---TVTALVPALV---------------SLWL-DAAASRRADL------------------- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 421 iqSSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTE----CTAgccLSLPGDWTAGHVGAPM-PCNYVKLVDv 495
Cdd:cd05920 255 --SSL----RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEgllnYTR---LDDPDEVIIHTQGRPMsPDDEIRVVD- 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 496 EEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIE 575
Cdd:cd05920 325 EEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVE 403
|
330 340 350
....*....|....*....|....*....|..
gi 1720426399 576 NIYLRSEAVAQVFV-------HGESLQAFLIA 600
Cdd:cd05920 404 NLLLRHPAVHDAAVvampdelLGERSCAFVVL 435
|
|
| 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 1720426399 436 AAPVSATVLTFLRTALGCQFYeGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASkGE-GEVCVKGA 514
Cdd:cd17636 121 AAPEWNDMATVDTSPWGRKPG-GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILD-EDGREVPD-GEvGEIVARGP 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 515 NVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQVFVHGesl 594
Cdd:cd17636 198 TVMAGYWNRPEVNARRT-RGGWHHTNDLGRREPDGSLSFVGPKTRMIKSG-AENIYPAEVERCLRQHPAVADAAVIG--- 272
|
170 180
....*....|....*....|
gi 1720426399 595 qafliavvVPDveslPSWAQ 614
Cdd:cd17636 273 --------VPD----PRWAQ 280
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
263-605 |
1.04e-15 |
|
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: 80.39 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 263 PKPPEPEDLAIICFTSGTTGNPKGAMITHQNIINDcsgfIKATESALTLNASDTQISYLPLAHmyeqqlqcvmlchgaki 342
Cdd:cd12114 120 PVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNT----ILDINRRFAVGPDDRVLALSSLSF----------------- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 343 gffqgdirllmdDLKVlqptifpvvprllnrmFDrIFGQantslkrwlldfaskrkeaeLRSG--IV-------RNNSLW 413
Cdd:cd12114 179 ------------DLSV----------------YD-IFGA--------------------LSAGatLVlpdearrRDPAHW 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 414 DKLIfHKIQSSLGGKVRL---MITGAAPVSATVLTFLRTAL-------------------GCQFYEGYGQTEctaGCCLS 471
Cdd:cd12114 210 AELI-ERHGVTLWNSVPAlleMLLDVLEAAQALLPSLRLVLlsgdwipldlparlralapDARLISLGGATE---ASIWS 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 472 -------LPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEAL--DKDG--WLHTG 540
Cdd:cd12114 286 iyhpideVPPDWRSIPYGRPLANQRYRVLD-PRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFvtHPDGerLYRTG 364
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720426399 541 DIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQ--VFVHGESLQAFLIAVVVPD 605
Cdd:cd12114 365 DLGRYRPDGTLEFLGRRDGQVKV-RGYRIELGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPD 430
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
265-586 |
2.08e-15 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 80.14 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 265 PPEPEDLAIICFTSGTTGNPKGAMITHQNIINDcsgfIKATESALTLNASDTQISYLPLAHMYeqqlqcvmlchGAKIGF 344
Cdd:PRK08043 361 KQQPEDAALILFTSGSEGHPKGVVHSHKSLLAN----VEQIKTIADFTPNDRFMSALPLFHSF-----------GLTVGL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 345 FQGdirlLMDDLKVL---QPTIFPVVPRLLnrmFDR----IFGQAnTSLKRWL-----LDFAskrkeaelrsgivrnnsl 412
Cdd:PRK08043 426 FTP----LLTGAEVFlypSPLHYRIVPELV---YDRnctvLFGTS-TFLGNYArfanpYDFA------------------ 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 413 wdklifhkiqsslggKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKL 492
Cdd:PRK08043 480 ---------------RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARL 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 493 VDVEEMnylaSKGeGEVCVKGANVFKGYLK--DP-------ARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKL 563
Cdd:PRK08043 545 LSVPGI----EQG-GRLQLKGPNIMNGYLRveKPgvlevptAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKI 619
|
330 340
....*....|....*....|...
gi 1720426399 564 AqGEYIAPEKIENIYLRSEAVAQ 586
Cdd:PRK08043 620 A-GEMVSLEMVEQLALGVSPDKQ 641
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
155-612 |
2.51e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 79.31 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 155 SQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIF--ADKPEKAKLLLEGvenklTPCLK-IIVIMDSY 231
Cdd:PRK07470 64 SRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMIchADFPEHAAAVRAA-----SPDLThVVAIGGAR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 232 GSDLVErgkkcgvEIISlkalEDLGRvnRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQN----IINDCSGFIKATES 307
Cdd:PRK07470 139 AGLDYE-------ALVA----RHLGA--RVANAAVDHDDPCWFFFTSGTTGRPKAAVLTHGQmafvITNHLADLMPGTTE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 308 AltlnasDTQISYLPLAHMYEQQlQCVMLCHGAKigffqgDIRLLMDDLKVlqPTIFPVVPRL-LNRMFdrifgQANTSL 386
Cdd:PRK07470 206 Q------DASLVVAPLSHGAGIH-QLCQVARGAA------TVLLPSERFDP--AEVWALVERHrVTNLF-----TVPTIL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 387 KRWLLDFASKRKEaelrsgivrnnslwdklifhkiQSSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTa 466
Cdd:PRK07470 266 KMLVEHPAVDRYD----------------------HSSL----RYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVT- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 467 GCCLSLP------GDWTAGHVGapmPCNY------VKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALdKD 534
Cdd:PRK07470 319 GNITVLPpalhdaEDGPDARIG---TCGFertgmeVQIQD-DEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RD 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720426399 535 GWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHGeslqafliavvVPDveslPSW 612
Cdd:PRK07470 394 GWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPREIEEKLLTHPAVSEVAVLG-----------VPD----PVW 455
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
122-605 |
5.72e-15 |
|
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: 78.09 E-value: 5.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 122 ISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:cd17646 24 LTYRELDERANRLAHLLRARGVGP--EDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 202 DkpekaklllegvenkltpclkiivimdsygSDLVERGKKcGVEIISLKALEDLGRVNRVKPKPPEPEDLAIICFTSGTT 281
Cdd:cd17646 102 T------------------------------ADLAARLPA-GGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGST 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 282 GNPKGAMITHQNIINdcsgfikatesaltlnasdtqisylplahmyeqqlqcvmlchgaKIGFFQGDIRLLMDDlKVLQP 361
Cdd:cd17646 151 GRPKGVMVTHAGIVN--------------------------------------------RLLWMQDEYPLGPGD-RVLQK 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 362 T----------IF-PVV---------------PRLLNRMFDRifgQANT------SLKRWLLDFASKRKEAELRsgivrn 409
Cdd:cd17646 186 TplsfdvsvweLFwPLVagarlvvarpgghrdPAYLAALIRE---HGVTtchfvpSMLRVFLAEPAAGSCASLR------ 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 410 nslwdklifhkiqsslggkvRLMITGAApVSATVLTFLRTALGCQFYEGYGQTEC----TAGCClslPGDWTAGHV--GA 483
Cdd:cd17646 257 --------------------RVFCSGEA-LPPELAARFLALPGAELHNLYGPTEAaidvTHWPV---RGPAETPSVpiGR 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 484 PMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLH------TGDIGKWLPNGTLKIIDRK 557
Cdd:cd17646 313 PVPNTRLYVLD-DALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRS 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1720426399 558 KHIFKLaQGEYIAPEKIENIYLRSEAVAQVFV---HGESLQAFLIAVVVPD 605
Cdd:cd17646 392 DDQVKI-RGFRVEPGEIEAALAAHPAVTHAVVvarAAPAGAARLVGYVVPA 441
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
122-616 |
6.25e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 78.25 E-value: 6.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 122 ISYKEVAELAECIGSGLIQKGFkpCSEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIfA 201
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGV--RRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWL-V 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 202 DKPEKAKL----LLEGVENKLTPCLKIIVIMDSYGSDLVERGKKCGVEIISLKALEDLGrvnrVKPKPPEPEDLAIICFT 277
Cdd:PRK06164 113 VWPGFKGIdfaaILAAVPPDALPPLRAIAVVDDAADATPAPAPGARVQLFALPDPAPPA----AAGERAADPDAGALLFT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 278 -SGTTGNPK------GAMITHQNIINDcsgfikatesALTLNASDTQISYLPLahmyeqqlqCVMLCHGAKIGFFQGDIR 350
Cdd:PRK06164 189 tSGTTSGPKlvlhrqATLLRHARAIAR----------AYGYDPGAVLLAALPF---------CGVFGFSTLLGALAGGAP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 351 LLMDDLkvlqptiF--PVVPRLL-----------NRMFDRIFGQANTSLkrwllDFASKRkeaelrsgivrnnslwdkli 417
Cdd:PRK06164 250 LVCEPV-------FdaARTARALrrhrvthtfgnDEMLRRILDTAGERA-----DFPSAR-------------------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 418 fhkiqsslggkvRLMITGAAPVSATVLTFLRTAlGCQFYEGYGQTECTA-GCCLSLPGDWTAGHV--GAPM-PCNYVKLV 493
Cdd:PRK06164 298 ------------LFGFASFAPALGELAALARAR-GVPLTGLYGSSEVQAlVALQPATDPVSVRIEggGRPAsPEARVRAR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 494 DVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEK 573
Cdd:PRK06164 365 DPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNPAE 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1720426399 574 IENIYLRSEAVAQVFVHGESLQ------AFLIAV--VVPDVESLPSWAQKR 616
Cdd:PRK06164 444 IEHALEALPGVAAAQVVGATRDgktvpvAFVIPTdgASPDEAGLMAACREA 494
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
122-605 |
7.13e-15 |
|
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: 77.36 E-value: 7.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 122 ISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVGP--ESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 202 DkpekaklllegvenkltpclkiivimdsygsdlvergkkcgveiislkaledlgrvnrvkpkppePEDLAIICFTSGTT 281
Cdd:cd12115 103 D-----------------------------------------------------------------PDDLAYVIYTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 282 GNPKGAMITHQNIINdcsgFIK-------ATESALTLNAsdTQISY-LPLAHMYeqqlqcVMLCHGAKIgffqgdirLLM 353
Cdd:cd12115 118 GRPKGVAIEHRNAAA----FLQwaaaafsAEELAGVLAS--TSICFdLSVFELF------GPLATGGKV--------VLA 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 354 DDlkVLQPTIFPVVPR--LLNRMfdrifgqanTSLKRWLLDfaskrkeaelrsgivrnnslwdklifhkiQSSLGGKVRL 431
Cdd:cd12115 178 DN--VLALPDLPAAAEvtLINTV---------PSAAAELLR-----------------------------HDALPASVRV 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 432 MITGAAPVSATVLTFLRTAL-GCQFYEGYGQTECT--AGCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKGEGE 508
Cdd:cd12115 218 VNLAGEPLPRDLVQRLYARLqVERVVNLYGPSEDTtySTVAPVPPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVPGE 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 509 VCVKGANVFKGYLKDPARTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSE 582
Cdd:cd12115 297 LYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAALRSIP 375
|
490 500
....*....|....*....|....*.
gi 1720426399 583 AVAQ--VFVHGESL-QAFLIAVVVPD 605
Cdd:cd12115 376 GVREavVVAIGDAAgERRLVAYIVAE 401
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
429-629 |
3.31e-14 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 76.04 E-value: 3.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 429 VRLMITGAAPvSATVLtFLRTALGCQFYEGYGQTEcTAG----CCL-----SLPGDwTAGHVGAPMPCNYVKL-----VD 494
Cdd:PLN02479 313 VHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSE-TYGpstvCAWkpewdSLPPE-EQARLNARQGVRYIGLegldvVD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 495 VEEMNYLASKGE--GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPE 572
Cdd:PLN02479 389 TKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGGENISSL 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720426399 573 KIENIYLRSEAVAQVFV-------HGESLQAFLiaVVVPDVESlpswAQKRGLQGSFEELCRNK 629
Cdd:PLN02479 467 EVENVVYTHPAVLEASVvarpderWGESPCAFV--TLKPGVDK----SDEAALAEDIMKFCRER 524
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
267-616 |
5.44e-14 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 74.60 E-value: 5.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 267 EPEDLAIICFTSGTTGNPKGAMITHQNIINdcsgFIKATESALTLNASDTQISYLPL---AHMYEQqlqCVMLCHGAkig 343
Cdd:cd17652 91 TPDNLAYVIYTSGSTGRPKGVVVTHRGLAN----LAAAQIAAFDVGPGSRVLQFASPsfdASVWEL---LMALLAGA--- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 344 ffqgdiRLLMDDLKVLQPtifpvvprllnrmfdrifGQAntslkrwLLDFaskrkeaelrsgivrnnsLWDKLIFHKIQS 423
Cdd:cd17652 161 ------TLVLAPAEELLP------------------GEP-------LADL------------------LREHRITHVTLP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 424 ----------SLGGKVRLMITGAAPVSATVLtflRTALGCQFYEGYGQTECTAGCCLSLP-GDWTAGHVGAPMPCNYVKL 492
Cdd:cd17652 192 paalaalppdDLPDLRTLVVAGEACPAELVD---RWAPGRRMINAYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 493 VDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQ 565
Cdd:cd17652 269 LD-ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKI-R 346
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1720426399 566 GEYIAPEKIENIYLRSEAVAQ--VFVHGESL-QAFLIAVVVPDVESLPSWAQKR 616
Cdd:cd17652 347 GFRIELGEVEAALTEHPGVAEavVVVRDDRPgDKRLVAYVVPAPGAAPTAAELR 400
|
|
| 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 1720426399 421 IQSSLGG---KVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSlPGD-WTAGHVGAPMPCNYVKLVDVE 496
Cdd:cd05974 191 IQQDLASfdvKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNS-PGQpVKAGSMGRPLPGYRVALLDPD 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 497 EmnylASKGEGEVCV-----KGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAP 571
Cdd:cd05974 270 G----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SSDYRISP 343
|
170
....*....|....*...
gi 1720426399 572 EKIENIYLRSEAVAQVFV 589
Cdd:cd05974 344 FELESVLIEHPAVAEAAV 361
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
267-577 |
1.43e-13 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 73.70 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 267 EPEDLAIICFTSGTTGNPKGAMITHQNIIND---CSGFIKATESaltlnasDTQISYLPLAHMYeqqlqcvmlchgakiG 343
Cdd:PRK06334 181 DPEDVAVILFTSGTEKLPKGVPLTHANLLANqraCLKFFSPKED-------DVMMSFLPPFHAY---------------G 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 344 FFQGDIRLLMDDLkvlqPTIF---PVVPRLLNRMFDR----IFGQANTSLKRWLLdfASKRKEAELRS-------GIVRN 409
Cdd:PRK06334 239 FNSCTLFPLLSGV----PVVFaynPLYPKKIVEMIDEakvtFLGSTPVFFDYILK--TAKKQESCLPSlrfvvigGDAFK 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 410 NSLWDKlifhkiqsslggkvrlmitgaapvsaTVLTFLRTALgcqfYEGYGQTECTAgcCLSLPGDWTAGH---VGAPMP 486
Cdd:PRK06334 313 DSLYQE--------------------------ALKTFPHIQL----RQGYGTTECSP--VITINTVNSPKHescVGMPIR 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 487 CNYVKLVDvEEMNYLASKGE-GEVCVKGANVFKGYL-KDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLA 564
Cdd:PRK06334 361 GMDVLIVS-EETKVPVSSGEtGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG 439
|
330
....*....|...
gi 1720426399 565 qGEYIAPEKIENI 577
Cdd:PRK06334 440 -AEMVSLEALESI 451
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
266-617 |
1.78e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 74.43 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 266 PEPEDLAIICFTSGTTGNPKGAMITHQNIINdcsgFIKATESALTLNASDTQISYLPLAHMYEQQLQCVMLCHGAKIGFF 345
Cdd:PRK12467 1715 LAPQNLAYVIYTSGSTGRPKGAGNRHGALVN----RLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIA 1790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 346 QGDIRL----LMDDLKVLQPTIFPVVPRLLNRMFDRIFGQAN-TSLKRwlldfaskrkeaelrsgIVrnnslwdklifhk 420
Cdd:PRK12467 1791 PPGAHRdpeqLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHpLSLRR-----------------VV------------- 1840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 421 iqssLGGKvrlmitgAAPVSATVLTFLRtaLG-CQFYEGYGQTECTAG-----CCLSLPGDWTAGHVGAPMPCNYVKLVD 494
Cdd:PRK12467 1841 ----CGGE-------ALEVEALRPWLER--LPdTGLFNLYGPTETAVDvthwtCRRKDLEGRDSVPIGQPIANLSTYILD 1907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 495 vEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEAL------DKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGE 567
Cdd:PRK12467 1908 -ASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgTVGSRLYrTGDLARYRADGVIEYLGRIDHQVKI-RGF 1985
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1720426399 568 YIAPEKIENIYLRSEAVAQ--VFVHGESLQAFLIAVVVPDVESLPSWAQKRG 617
Cdd:PRK12467 1986 RIELGEIEARLREQGGVREavVIAQDGANGKQLVAYVVPTDPGLVDDDEAQV 2037
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
182-591 |
2.14e-13 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 73.25 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 182 LGADAITYIVNKAELSVIFADK---PekaklLLEGVENKLtPCLKIIVImdsygsdLVERGKKCGVEIISLKALEDL--G 256
Cdd:PRK06018 98 LFPEQIAWIINHAEDRVVITDLtfvP-----ILEKIADKL-PSVERYVV-------LTDAAHMPQTTLKNAVAYEEWiaE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 257 RVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQ-NIINdcsGFIKATESALTLNASDTQISYLPLAH-------MYE 328
Cdd:PRK06018 165 ADGDFAWKTFDENTAAGMCYTSGTTGDPKGVLYSHRsNVLH---ALMANNGDALGTSAADTMLPVVPLFHanswgiaFSA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 329 QQLQCVMLCHGAKIGffQGDIRLLMDDLKVlqpTIFPVVPRLlnrmfdrifgqantslkrWLLDFASKRKEAElrsgivr 408
Cdd:PRK06018 242 PSMGTKLVMPGAKLD--GASVYELLDTEKV---TFTAGVPTV------------------WLMLLQYMEKEGL------- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 409 nnslwdKLIFHKiqsslggkvRLMITGAAPVSATVLTFLRtaLGCQFYEGYGQTECTAGCCLS--------LPGDWTAGH 480
Cdd:PRK06018 292 ------KLPHLK---------MVVCGGSAMPRSMIKAFED--MGVEVRHAWGMTEMSPLGTLAalkppfskLPGDARLDV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 481 V---GAPMPCNYVKLVDvEEMNYLASKGE--GEVCVKGANVFKGYLKDparTAEALDKDGWLHTGDIGKWLPNGTLKIID 555
Cdd:PRK06018 355 LqkqGYPPFGVEMKITD-DAGKELPWDGKtfGRLKVRGPAVAAAYYRV---DGEILDDDGFFDTGDVATIDAYGYMRITD 430
|
410 420 430
....*....|....*....|....*....|....*.
gi 1720426399 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 1720426399 456 YEGYGQTECTAGCCLSlPGDWTA--GHVGAPMPCNyVKLVDvEEMNYLASKGEGEVCVKGANVFKgYLKDPARTAEALDK 533
Cdd:cd05929 273 WEYYGGTEGQGLTIIN-GEEWLThpGSVGRAVLGK-VHILD-EDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNE 348
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720426399 534 DGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHG---ESLQAFLIAVVVP 604
Cdd:cd05929 349 GGWSTLGDVGYLDEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIAHPKVLDAAVVGvpdEELGQRVHAVVQP 421
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
185-585 |
3.38e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 69.35 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 185 DAITYIVNKAELSVIFAD---KPekaklLLEGVENKLTPCLKIIVIMDSygsdlvergKKCGVEIISLKALEDL-GRVNR 260
Cdd:PRK07008 101 EQIAYIVNHAEDRYVLFDltfLP-----LVDALAPQCPNVKGWVAMTDA---------AHLPAGSTPLLCYETLvGAQDG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 261 VKPKPPEPEDLAI-ICFTSGTTGNPKGAMITHQNIIndCSGFIKATESALTLNASDTQISYLPLAHMYEQQLQCVMLCHG 339
Cdd:PRK07008 167 DYDWPRFDENQASsLCYTSGTTGNPKGALYSHRSTV--LHAYGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPLTG 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 340 AKIgFFQG------DIRLLMDDLKVLQPTIFPVV-PRLLNRMfdrifgqantslkrwlldfaskrKEAELRSGIVRnnsl 412
Cdd:PRK07008 245 AKL-VLPGpdldgkSLYELIEAERVTFSAGVPTVwLGLLNHM-----------------------REAGLRFSTLR---- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 413 wdklifhkiqsslggkvRLMITGAAPVSATVLTFlRTALGCQFYEGYGQTE-------CT-AGCCLSLPGD------WTA 478
Cdd:PRK07008 297 -----------------RTVIGGSACPPAMIRTF-EDEYGVEVIHAWGMTEmsplgtlCKlKWKHSQLPLDeqrkllEKQ 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 479 GHV--GAPMpcnyvKLVDVE--EMNYlASKGEGEVCVKGANVFKGYLKdpaRTAEALDkDGWLHTGDIGKWLPNGTLKII 554
Cdd:PRK07008 359 GRViyGVDM-----KIVGDDgrELPW-DGKAFGDLQVRGPWVIDRYFR---GDASPLV-DGWFPTGDVATIDADGFMQIT 428
|
410 420 430
....*....|....*....|....*....|.
gi 1720426399 555 DRKKHIFKlAQGEYIAPEKIENIYLRSEAVA 585
Cdd:PRK07008 429 DRSKDVIK-SGGEWISSIDIENVAVAHPAVA 458
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
108-619 |
3.53e-12 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 69.04 E-value: 3.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 108 PCLGSrkpnqPYEWISYKEVAELAECIGSGLIQKGFKPCSEQfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAI 187
Cdd:cd05958 2 TCLRS-----PEREWTYRDLLALANRIANVLVGELGIVPGNR-VLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 188 TYIVNKAELSVIFADKPEKAKlllegvenkltpclkiivimdsygsdlvergkkcgveiislkaledlgrvnrvkpkppe 267
Cdd:cd05958 76 AYILDKARITVALCAHALTAS----------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 268 pEDLAIICFTSGTTGNPKGAMITHQNIINDCSGFikaTESALTLNASDTQISYLPLAHMYEQQLQCV-MLCHGAKIGFFQ 346
Cdd:cd05958 97 -DDICILAFTSGTTGAPKATMHFHRDPLASADRY---AVNVLRLREDDRFVGSPPLAFTFGLGGVLLfPFGVGASGVLLE 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 347 GDI-RLLMDDLKVLQPTIFPVVPRLLNRMFdrifgqantslkrwlldfASKRKEAELRSGivrnnslwdklifhkiqssl 425
Cdd:cd05958 173 EATpDLLLSAIARYKPTVLFTAPTAYRAML------------------AHPDAAGPDLSS-------------------- 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 426 ggkVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKG 505
Cdd:cd05958 215 ---LRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD-DEGNPVPDGT 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 506 EGEVCVKGANVFKgYLKDPARTAEAldKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVA 585
Cdd:cd05958 291 IGRLAVRGPTGCR-YLADKRQRTYV--QGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQHPAVA 366
|
490 500 510
....*....|....*....|....*....|....*..
gi 1720426399 586 QVFVHGESLQAFLI---AVVVPDVESLPSWAQKRGLQ 619
Cdd:cd05958 367 ECAVVGHPDESRGVvvkAFVVLRPGVIPGPVLARELQ 403
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
151-607 |
7.25e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 68.55 E-value: 7.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 151 IGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFADKPEKAklLLEGVEnkltPCLKIIVIMDS 230
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAE--LLDGLD----PGVRVINVDSP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 231 YGSDLvergkkcgveiisLKALEDlgrvNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHqniindcsGFIKATESALT 310
Cdd:PRK07867 131 AWADE-------------LAAHRD----AEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTH--------RKVASAGVMLA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 311 ----LNASDTQISYLPLAH----MyeqQLQCVMLCHGAKI---------GFfqgdirllMDDLKVLQPTIFPVVPRLLNr 373
Cdd:PRK07867 186 qrfgLGPDDVCYVSMPLFHsnavM---AGWAVALAAGASIalrrkfsasGF--------LPDVRRYGATYANYVGKPLS- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 374 mfdrifgqantslkrWLLDFASKRKEAElrsgivrnNSLwdklifhkiqsslggkvRLMI-TGAAPVSatVLTFLRTaLG 452
Cdd:PRK07867 254 ---------------YVLATPERPDDAD--------NPL-----------------RIVYgNEGAPGD--IARFARR-FG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 453 CQFYEGYGQTEctAGCCLSLPGDWTAGHVGAPMPCnyVKLVDVE--------------EMNYLASKGEgEVCVKGANVFK 518
Cdd:PRK07867 291 CVVVDGFGSTE--GGVAITRTPDTPPGALGPLPPG--VAIVDPDtgtecppaedadgrLLNADEAIGE-LVNTAGPGGFE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 519 GYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFVHGeslqafl 598
Cdd:PRK07867 366 GYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPIERILLRYPDATEVAVYA------- 436
|
....*....
gi 1720426399 599 iavvVPDVE 607
Cdd:PRK07867 437 ----VPDPV 441
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
250-576 |
7.87e-12 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 68.39 E-value: 7.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 250 KALEDLGRVNRVKPKPP---EPEDLAIICFTSGTTGNPKGAMITHQniindcsgfikatesaltlnasdtqisylplahM 326
Cdd:PRK09274 152 TTLATLLRDGAAAPFPMadlAPDDMAAILFTSGSTGTPKGVVYTHG---------------------------------M 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 327 YEQQLQcvMLCHGAKIGffQGDIrllmdDLkvlqPTiFP-------------VVPRL---------LNRMFDRIFGQANT 384
Cdd:PRK09274 199 FEAQIE--ALREDYGIE--PGEI-----DL----PT-FPlfalfgpalgmtsVIPDMdptrpatvdPAKLFAAIERYGVT 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 385 SLkrwlldFASKrkeaelrsgivrnnSLWDKLIFHKIQS--SLGGkVRLMITGAAPVSATVLTFLRTAL--GCQFYEGYG 460
Cdd:PRK09274 265 NL------FGSP--------------ALLERLGRYGEANgiKLPS-LRRVISAGAPVPIAVIERFRAMLppDAEILTPYG 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 461 QTEC------TAGCCLSLPGDWT---AGH-VGAPMPCNYVKLVDV--------EEMNYLASKGEGEVCVKGANVFKGYLK 522
Cdd:PRK09274 324 ATEAlpissiESREILFATRAATdngAGIcVGRPVDGVEVRIIAIsdapipewDDALRLATGEIGEIVVAGPMVTRSYYN 403
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720426399 523 DPARTAEA--LDKDG--WLHTGDIGkWL-PNGTLKIIDRKKHIFKLAQGEY--IAPEKIEN 576
Cdd:PRK09274 404 RPEATRLAkiPDGQGdvWHRMGDLG-YLdAQGRLWFCGRKAHRVETAGGTLytIPCERIFN 463
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
267-607 |
9.86e-12 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 67.88 E-value: 9.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 267 EPEDLAIICFTSGTTGNPKGAMITHQNIINdcsgfikatesaltlnasdtqisylPLAHMYEQQLqcvmlchgakIGFFQ 346
Cdd:cd17656 126 NSDDLLYIIYTSGTTGKPKGVQLEHKNMVN-------------------------LLHFEREKTN----------INFSD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 347 GdirllmddlkVLQPTIFPvvprlLNRMFDRIFGQANTSLKRWLLDFASKRKEAELRSGIVRNN--------SLWdKLIF 418
Cdd:cd17656 171 K----------VLQFATCS-----FDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNievvflpvAFL-KFIF 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 419 HKIQ--SSLGGKVRLMITGAAP--VSATVLTFLRTAlGCQFYEGYG--QTECTAGCCLSLPGDWTA-GHVGAPMPCNYVK 491
Cdd:cd17656 235 SEREfiNRFPTCVKHIITAGEQlvITNEFKEMLHEH-NVHLHNHYGpsETHVVTTYTINPEAEIPElPPIGKPISNTWIY 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 492 LVDVEEMnyLASKGE-GEVCVKGANVFKGYLKDPARTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLa 564
Cdd:cd17656 314 ILDQEQQ--LQPQGIvGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI- 390
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1720426399 565 QGEYIAPEKIENIYLRSEAVAQ--VFVHGESL-QAFLIAVVVPDVE 607
Cdd:cd17656 391 RGYRIELGEIEAQLLNHPGVSEavVLDKADDKgEKYLCAYFVMEQE 436
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
268-627 |
1.20e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 68.45 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 268 PEDLAIICFTSGTTGNPKGAMITHQNIINdcsgFIKATESALTLNASDTQISYLPLAHMYEQQLQCVMLCHGAkigffqg 347
Cdd:PRK12316 4693 PDNLAYVIYTSGSTGRPKGVAVSHGSLVN----HLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGA------- 4761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 348 diRLLMDDLKVLQPTifpvvpRLLNRMFDR--IFGQANTSLKRWLLDFASKRKE-AELRSGIVRNNSLwdklifhkiqss 424
Cdd:PRK12316 4762 --SVVIRDDSLWDPE------RLYAEIHEHrvTVLVFPPVYLQQLAEHAERDGEpPSLRVYCFGGEAV------------ 4821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 425 LGGKVRLMITGAAPVSatvltflrtalgcqFYEGYGQTECTAG-CCLSLPGDWTAG----HVGAPMPCNYVKLVDVEeMN 499
Cdd:PRK12316 4822 AQASYDLAWRALKPVY--------------LFNGYGPTETTVTvLLWKARDGDACGaaymPIGTPLGNRSGYVLDGQ-LN 4886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 500 YLASKGEGEVCVKGANVFKGYLKDPARTAE-----ALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPE 572
Cdd:PRK12316 4887 PLPVGVAGELYLGGEGVARGYLERPALTAErfvpdPFGAPGgrLYRTGDLARYRADGVIDYLGRVDHQVKI-RGFRIELG 4965
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720426399 573 KIENIYLRSEAVAQVFVHGE--SLQAFLIAVVVPDVESL-PSWAQKRGLQGSFEELCR 627
Cdd:PRK12316 4966 EIEARLREHPAVREAVVIAQegAVGKQLVGYVVPQDPALaDADEAQAELRDELKAALR 5023
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
267-610 |
1.56e-11 |
|
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: 67.04 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 267 EPEDLAIICFTSGTTGNPKGAMITHQNIINDCSGFIK-------ATESALTLNasdtqiSYLpLAHMYEQQLQCVMlcHG 339
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSEryfgrdnGDEAVLFFS------NYV-FDFFVEQMTLALL--NG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 340 AKIGFFQGDIRL-------LMDDLKVlqpTIFPVVPRLLNRM-FDRIfgqanTSLKRWLL---DFASKRkeaelrsgivr 408
Cdd:cd17648 163 QKLVVPPDEMRFdpdrfyaYINREKV---TYLSGTPSVLQQYdLARL-----PHLKRVDAageEFTAPV----------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 409 nnslwdkliFHKIQSSLGGkvrLMITGAAPVSATVLTFLRtalgcqFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCN 488
Cdd:cd17648 224 ---------FEKLRSRFAG---LIINAYGPTETTVTNHKR------FFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVG 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 489 YVklvdveemnylaskgeGEVCVKGANVFKGYLKDPARTAE-------------ALDKDGWLH-TGDIGKWLPNGTLKII 554
Cdd:cd17648 286 AV----------------GELYLGGDGVARGYLNRPELTAErflpnpfqteqerARGRNARLYkTGDLVRWLPSGELEYL 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720426399 555 DRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFV--------HGESLQAFLIAVVVPDVESLP 610
Cdd:cd17648 350 GRNDFQVKI-RGQRIEPGEVEAALASYPGVRECAVvakedasqAQSRIQKYLVGYYLPEPGHVP 412
|
|
| 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 1720426399 430 RLMITGAAPVSATVLTFLRTALGCQFYEGYGQTE----CTAgccLSLPGDWTAGHVGAPM-PCNYVKLVDvEEMNYLASK 504
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAEglvnYTR---LDDSDERIFTTQGRPMsPDDEVWVAD-ADGNPLPQG 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 505 GEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHifklaQ----GEYIAPEKIENIYLR 580
Cdd:PRK10946 379 EVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGEKIAAEEIENLLLR 453
|
170 180
....*....|....*....|....*..
gi 1720426399 581 SEAVAQVF-------VHGESLQAFLIA 600
Cdd:PRK10946 454 HPAVIHAAlvsmedeLMGEKSCAFLVV 480
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
243-639 |
4.60e-11 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 65.69 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 243 GVEIISLKALEDLGRvnrvKPKPPEPE------DLAIICFTSGTTGNPKGAMITHQNIINdcsgFikaTESALTLNASDT 316
Cdd:PRK04813 115 GIPVITLDELKDIFA----TGNPYDFDhavkgdDNYYIIFTSGTTGKPKGVQISHDNLVS----F---TNWMLEDFALPE 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 317 QISYLPLAhMYEQQLQcVM-----LCHGAKIGFFQGDI----RLLMDDLKVLQPTIFPVVPR-----LLNRMFDrifGQA 382
Cdd:PRK04813 184 GPQFLNQA-PYSFDLS-VMdlyptLASGGTLVALPKDMtanfKQLFETLPQLPINVWVSTPSfadmcLLDPSFN---EEH 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 383 NTSLKRWLLDfaskrKEaELRsgivrnnslwdklifHKIQSSLggKVRLmitgaaPvSATVltflrtalgcqfYEGYGQT 462
Cdd:PRK04813 259 LPNLTHFLFC-----GE-ELP---------------HKTAKKL--LERF------P-SATI------------YNTYGPT 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 463 ECTAGCclslpgdwTAGHVGA-------PMPCNYVK-----LVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEA 530
Cdd:PRK04813 297 EATVAV--------TSIEITDemldqykRLPIGYAKpdsplLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEA 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 531 L-DKDGW--LHTGDIGKwLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENiYLR-----SEAVAQVFVHGESLQAfLIAVV 602
Cdd:PRK04813 369 FfTFDGQpaYHTGDAGY-LEDGLLFYQGRIDFQIKLN-GYRIELEEIEQ-NLRqssyvESAVVVPYNKDHKVQY-LIAYV 444
|
410 420 430
....*....|....*....|....*....|....*..
gi 1720426399 603 VPDveslpswaqkrglQGSFEelcRNKDINKAILDDL 639
Cdd:PRK04813 445 VPK-------------EEDFE---REFELTKAIKKEL 465
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
113-604 |
9.27e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 64.71 E-value: 9.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 113 RKPNQPY-------EWISYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGAD 185
Cdd:PRK13391 9 TTPDKPAvimastgEVVTYRELDERSNRLAHLFRSLGLKRGDH--VAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 186 AITYIVNKAELSVIF--ADKPEKAKLLLEGVENkLTPCLKIIVIMDSYGSDLVErgkkcgveiislKALEDLGRVnrvkP 263
Cdd:PRK13391 87 EAAYIVDDSGARALItsAAKLDVARALLKQCPG-VRHRLVLDGDGELEGFVGYA------------EAVAGLPAT----P 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 264 KPPEPEDLAIIcFTSGTTGNPKGamithqniindcsgfIKAtesALTLNASDTQISYL-PLAHMYEQQLQCVMLC----- 337
Cdd:PRK13391 150 IADESLGTDML-YSSGTTGRPKG---------------IKR---PLPEQPPDTPLPLTaFLQRLWGFRSDMVYLSpaply 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 338 HGAKIGFFQGDIRL-----LMDD------LKVLQP---TIFPVVPRLLNRMFdrifgqantslkrwlldfasKRKEAelr 403
Cdd:PRK13391 211 HSAPQRAVMLVIRLggtviVMEHfdaeqyLALIEEygvTHTQLVPTMFSRML--------------------KLPEE--- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 404 sgiVRNNslWDklifhkiQSSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTEcTAGCCLSLPGDWTA--GHV 481
Cdd:PRK13391 268 ---VRDK--YD-------LSSL----EVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATE-GLGFTACDSEEWLAhpGTV 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 482 GAPMpcnYVKLVDVEEMNYLASKGE-GEVCVKGANVFKgYLKDPARTAEALDKDG-WLHTGDIGKWLPNGTLKIIDRKKH 559
Cdd:PRK13391 331 GRAM---FGDLHILDDDGAELPPGEpGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAF 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1720426399 560 IFkLAQGEYIAPEKIENIYLRSEAVAQVFVHG---ESLQAFLIAVVVP 604
Cdd:PRK13391 407 MI-ISGGVNIYPQEAENLLITHPKVADAAVFGvpnEDLGEEVKAVVQP 453
|
|
| 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 1720426399 423 SSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTEcTAGCCLSLPGDWTA--GHVGAPMPCNyVKLVDvEEMNY 500
Cdd:PRK08276 262 SSL----RVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGE-VRILD-EDGNE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 501 LASKGEGEVCVK-GANVFKgYLKDPARTAEALDKDGWLHTGDIGkWL-PNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 578
Cdd:PRK08276 335 LPPGEIGTVYFEmDGYPFE-YHNDPEKTAAARNPHGWVTVGDVG-YLdEDGYLYLTDRKSDMI-ISGGVNIYPQEIENLL 411
|
170 180
....*....|....*....|....*....
gi 1720426399 579 LRSEAVAQVFVHGeslqafliavvVPDVE 607
Cdd:PRK08276 412 VTHPKVADVAVFG-----------VPDEE 429
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
122-591 |
1.91e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 63.75 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 122 ISYKEVAELAECIGSGLIQKGFKPCSEqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFA 201
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGPGDH--VGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 202 DK---PEKAKLLLEgvenklTPCLKIIVIMDSYGSDLVERGkkcGVEIISLKALEDLGRVnrvkPKPPEPEDLAIICfTS 278
Cdd:PRK07798 107 ERefaPRVAEVLPR------LPKLRTLVVVEDGSGNDLLPG---AVDYEDALAAGSPERD----FGERSPDDLYLLY-TG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 279 GTTGNPKGAMITHQNI-------INDCSGFIKATESALTLNASD-TQISYLPLAHMyeqqlqcvMlcHGAK-----IGFF 345
Cdd:PRK07798 173 GTTGMPKGVMWRQEDIfrvllggRDFATGEPIEDEEELAKRAAAgPGMRRFPAPPL--------M--HGAGqwaafAALF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 346 QGdirllmddlkvlQPTIFPVVPRL-------------LNRMFdrIFGQAntsLKRWLLDFASKRKEAELrsgivrnnsl 412
Cdd:PRK07798 243 SG------------QTVVLLPDVRFdadevwrtierekVNVIT--IVGDA---MARPLLDALEARGPYDL---------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 413 wdklifhkiqSSLggkvRLMITGAAPVSATVLTFLRTAL-GCQFYEGYGQTEctAGCCLSLPGDWTAGHVGAP--MPCNY 489
Cdd:PRK07798 296 ----------SSL----FAIASGGALFSPSVKEALLELLpNVVLTDSIGSSE--TGFGGSGTVAKGAVHTGGPrfTIGPR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 490 VKLVDvEEMNYLAsKGEGEVCV--KGANVFKGYLKDPARTAEAL-DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLA 564
Cdd:PRK07798 360 TVVLD-EDGNPVE-PGSGEIGWiaRRGHIPLGYYKDPEKTAETFpTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTG 437
|
490 500
....*....|....*....|....*..
gi 1720426399 565 qGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:PRK07798 438 -GEKVFPEEVEEALKAHPDVADALVVG 463
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
123-605 |
1.99e-10 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 63.56 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 123 SYKEVAELAECIGSGLIQKGFKP--CseqfIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVN--KAELSV 198
Cdd:PRK12406 13 SFDELAQRAARAAGGLAALGVRPgdC----VALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEdsGARVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 199 IFADkpekaklLLEGVENKLTPCLKIIV------IMDSYGSDLVERGKKCGveiislkALEDLGRVNRVKP--KPPEPED 270
Cdd:PRK12406 89 AHAD-------LLHGLASALPAGVTVLSvptppeIAAAYRISPALLTPPAG-------AIDWEGWLAQQEPydGPPVPQP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 271 LAIIcFTSGTTGNPKGamithqniindcsgfIKATESALTLNASDTQIsylpLAHMYEQQLQCVMLC-----HGAKIGFF 345
Cdd:PRK12406 155 QSMI-YTSGTTGHPKG---------------VRRAAPTPEQAAAAEQM----RALIYGLKPGIRALLtgplyHSAPNAYG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 346 QGDIRLlmDDLKVLQP-----------------TIFpVVPRllnrMFDRifgqantslkrwLLDFASKRKEAelrsgivr 408
Cdd:PRK12406 215 LRAGRL--GGVLVLQPrfdpeellqlierhritHMH-MVPT----MFIR------------LLKLPEEVRAK-------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 409 nnslWDklifhkiQSSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTE------CTAGCCLSLPGDwtaghVG 482
Cdd:PRK12406 268 ----YD-------VSSL----RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTEsgavtfATSEDALSHPGT-----VG 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 483 APMPCNYVKLVDvEEMNYLASKGEGEVCVK--GANVFKgYLKDPARTAEaLDKDGWLHTGDIGKWLPNGTLKIIDRKKHI 560
Cdd:PRK12406 328 KAAPGAELRFVD-EDGRPLPQGEIGEIYSRiaGNPDFT-YHNKPEKRAE-IDRGGFITSGDVGYLDADGYLFLCDRKRDM 404
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1720426399 561 FkLAQGEYIAPEKIENIYLRSEAVAQVFVHG---ESLQAFLIAVVVPD 605
Cdd:PRK12406 405 V-ISGGVNIYPAEIEAVLHAVPGVHDCAVFGipdAEFGEALMAVVEPQ 451
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
269-587 |
3.91e-10 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 62.72 E-value: 3.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 269 EDLAIIcFTSGTTGNPKGAMITHQNI--INDcsgfIKATESALTLNASDTQISYLPLAHMYEQQLQCVMLC--HGAKI-- 342
Cdd:PRK05857 170 DPLAMI-FTSGTTGEPKAVLLANRTFfaVPD----ILQKEGLNWVTWVVGETTYSPLPATHIGGLWWILTClmHGGLCvt 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 343 -GFFQGDIRLLMDDLKVLQPTIfpvVPRLLNRMFdrifgqantslkrwlldfaskrkeAELRSGIVRNNSLwdklifhki 421
Cdd:PRK05857 245 gGENTTSLLEILTTNAVATTCL---VPTLLSKLV------------------------SELKSANATVPSL--------- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 422 qsslggkvRLMITGAAPVSATVLTFL-----RTAlgcQFYeGYGQTECTAGCclsLPGD------WTAGHVGAPMPCNYV 490
Cdd:PRK05857 289 --------RLVGYGGSRAIAADVRFIeatgvRTA---QVY-GLSETGCTALC---LPTDdgsivkIEAGAVGRPYPGVDV 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 491 KLVDVEEMNYLASKGE-----GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQ 565
Cdd:PRK05857 354 YLAATDGIGPTAPGAGpsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-ICG 431
|
330 340
....*....|....*....|..
gi 1720426399 566 GEYIAPEKIENIylrSEAVAQV 587
Cdd:PRK05857 432 GVNIAPDEVDRI---AEGVSGV 450
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
215-599 |
5.90e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 62.09 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 215 ENKLTPCLKIIV-IMDSYGSDLVE-RGKKCGVEIislkalEDL---GRVNRVKPKPPEP-EDLAIICFTSGTTGNPKGAM 288
Cdd:PRK05851 98 DATLTRFAGIGVrTVLSHGSHLERlRAVDSSVTV------HDLataAHTNRSASLTPPDsGGPAVLQGTAGSTGTPRTAI 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 289 ITHQNIINDCSGFIKATesaLTLNASDTQISYLPLAH-MYEQQLQCVMLChGAKIGffqgdirllmddlkvLQPTifpvv 367
Cdd:PRK05851 172 LSPGAVLSNLRGLNARV---GLDAATDVGCSWLPLYHdMGLAFLLTAALA-GAPLW---------------LAPT----- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 368 prllnrmfdrifGQANTSLKRWLlDFASkrkeaELRSGIVRNNSLWDKLI---FHKIQSSLGGKVRLMITGAAPVSATVL 444
Cdd:PRK05851 228 ------------TAFSASPFRWL-SWLS-----DSRATLTAAPNFAYNLIgkyARRVSDVDLGALRVALNGGEPVDCDGF 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 445 TFLRTALG-CQFYEG-----YGQTECTAGCCLSLPG-----------DWTAGH----VGAPMPCNYVKLVDVEEMNYLAS 503
Cdd:PRK05851 290 ERFATAMApFGFDAGaaapsYGLAESTCAVTVPVPGiglrvdevttdDGSGARrhavLGNPIPGMEVRISPGDGAAGVAG 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 504 KGEGEVCVKGANVFKGYLKDPartaeALDKDGWLHTGDIGkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIY----- 578
Cdd:PRK05851 370 REIGEIEIRGASMMSGYLGQA-----PIDPDDWFPTGDLG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERVAaqvrg 442
|
410 420
....*....|....*....|.
gi 1720426399 579 LRSEAVAQVFVHGESLQAFLI 599
Cdd:PRK05851 443 VREGAVVAVGTGEGSARPGLV 463
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
268-621 |
6.05e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 62.87 E-value: 6.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 268 PEDLAIICFTSGTTGNPKGAMITHQNIINDCsgfiKATESALTLNASDTQISYLPLAHMYEQQLQCVMLCHGAKIGFFQG 347
Cdd:PRK12467 3236 GENLAYVIYTSGSTGKPKGVGVRHGALANHL----CWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDN 3311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 348 DIR---LLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTSLKRWLldfaskrkeaelrsgivrnnslwdklifhkiqss 424
Cdd:PRK12467 3312 DLWdpeELWQAIHAHRISIACFPPAYLQQFAEDAGGADCASLDIYV---------------------------------- 3357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 425 LGGKvrlmitgAAPVSATVLTFlRTALGCQFYEGYGQTECTAGCCL-SLPGDWTAGHVGAPM--PCNYVKLVDVE-EMNY 500
Cdd:PRK12467 3358 FGGE-------AVPPAAFEQVK-RKLKPRGLTNGYGPTEAVVTVTLwKCGGDAVCEAPYAPIgrPVAGRSIYVLDgQLNP 3429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 501 LASKGEGEVCVKGANVFKGYLKDPARTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 573
Cdd:PRK12467 3430 VPVGVAGELYIGGVGLARGYHQRPSLTAERFVADpfsgsgGRLYrTGDLARYRADGVIEYLGRIDHQVKI-RGFRIELGE 3508
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1720426399 574 IENIYLRSEAVAQVFVHGESLQA--FLIAVVVPDVESlPSWAQ--KRGLQGS 621
Cdd:PRK12467 3509 IEARLLQHPSVREAVVLARDGAGgkQLVAYVVPADPQ-GDWREtlRDHLAAS 3559
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
267-575 |
6.82e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 62.88 E-value: 6.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 267 EPEDLAIICFTSGTTGNPKGAMITHQNIINDCS----GFikatesALTLNASDTQISYLPLAHmyeqqlqcvmlchgaKI 342
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQlirhGF------GIDLNPDDVIVSWLPLYH---------------DM 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 343 GFFQGdirllmddlkVLQPtIFPVVPRLLnrMFDRIFGQANTslkRWLL-------------DFA----SKR-KEAELRS 404
Cdd:PRK05691 223 GLIGG----------LLQP-IFSGVPCVL--MSPAYFLERPL---RWLEaiseyggtisggpDFAyrlcSERvSESALER 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 405 givRNNSLWdklifhkiqsslggkvRLMITGAAPVSATVL-TFLRTALGC-----QFYEGYGQTECT---AGC------- 468
Cdd:PRK05691 287 ---LDLSRW----------------RVAYSGSEPIRQDSLeRFAEKFAACgfdpdSFFASYGLAEATlfvSGGrrgqgip 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 469 CLSLPGDWTAGHVGAP------MPCNY------VKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEA-LDKDG 535
Cdd:PRK05691 348 ALELDAEALARNRAEPgtgsvlMSCGRsqpghaVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfVEHDG 427
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1720426399 536 --WLHTGDIGkWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIE 575
Cdd:PRK05691 428 rtWLRTGDLG-FLRDGELFVTGRLKDML-IVRGHNLYPQDIE 467
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
113-608 |
7.11e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 62.67 E-value: 7.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 113 RKPNQPY-----EWISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAI 187
Cdd:PRK12316 3069 RTPDAVAlafgeQRLSYAELNRRANRLAHRLIERGVGP--DVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERL 3146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 188 TYIVNKAelsvifadkpeKAKLLLEGVENKLTPCLKIIVIMdsygsdlVERGKkcgveiislkalEDLGRVNrvKPKPPE 267
Cdd:PRK12316 3147 AYMLEDS-----------GAQLLLSQSHLRLPLAQGVQVLD-------LDRGD------------ENYAEAN--PAIRTM 3194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 268 PEDLAIICFTSGTTGNPKGAMITHQNIindcSGFIKATESALTLNASDTQISYLPLAHMYEQQLQCVMLCHGAKIgffqg 347
Cdd:PRK12316 3195 PENLAYVIYTSGSTGKPKGVGIRHSAL----SNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARV----- 3265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 348 dirllmddlkVLQPTIFPVVPRLLNRMFDRifGQANTSLKRWlldfaskrkeaelrsgivrnnSLWDKLIFHKIQSSLGG 427
Cdd:PRK12316 3266 ----------VLAGPEDWRDPALLVELINS--EGVDVLHAYP---------------------SMLQAFLEEEDAHRCTS 3312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 428 KVRLMITGAAPVSATVltfLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGH--VGAPMPCNYVKLVDVeEMNYLASKG 505
Cdd:PRK12316 3313 LKRIVCGGEALPADLQ---QQVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILDG-SLEPVPVGA 3388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 506 EGEVCVKGANVFKGYLKDPARTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYL 579
Cdd:PRK12316 3389 LGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQVKI-RGFRIELGEIEARLL 3467
|
490 500
....*....|....*....|....*....
gi 1720426399 580 RSEAVAQVFVHGESLQAfLIAVVVPDVES 608
Cdd:PRK12316 3468 EHPWVREAVVLAVDGRQ-LVAYVVPEDEA 3495
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
268-624 |
1.36e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 61.90 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 268 PEDLAIICFTSGTTGNPKGAMITHQNIINdcsgFIKATESALTLNASDTQISYLPLAHMYEQQLQCVMLCHGAkigffqg 347
Cdd:PRK12316 654 PENLAYVIYTSGSTGKPKGAGNRHRALSN----RLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGA------- 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 348 diRLLmddlkvlqptifpVVPRLLNRMFDRIFGQANTSLKRwLLDFASKRKEAELRSGIVrnnslwdklifhkiqSSLGG 427
Cdd:PRK12316 723 --RLV-------------VAAPGDHRDPAKLVELINREGVD-TLHFVPSMLQAFLQDEDV---------------ASCTS 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 428 KVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHV--GAPMPCNYVKLVDVeEMNYLASKG 505
Cdd:PRK12316 772 LRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGGDSVpiGRPIANLACYILDA-NLEPVPVGV 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 506 EGEVCVKGANVFKGYLKDPARTAEAL------DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYL 579
Cdd:PRK12316 851 LGELYLAGRGLARGYHGRPGLTAERFvpspfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKL-RGLRIELGEIEARLL 929
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1720426399 580 RSEAVAQVFVHGESLQAfLIAVVVPDVE--SLPSwAQKRGLQGSFEE 624
Cdd:PRK12316 930 EHPWVREAAVLAVDGKQ-LVGYVVLESEggDWRE-ALKAHLAASLPE 974
|
|
| 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 1720426399 423 SSLGGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCC--LSLPGDWTAGHVGAPMPCNYVKLVDvEEMNY 500
Cdd:cd05973 201 ARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLAnhHALEHPVHAGSAGRAMPGWRVAVLD-DDGDE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 501 LASKGEGEVCVKGANV----FKGYLKDPARTAEAldkdGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEN 576
Cdd:cd05973 280 LGPGEPGRLAIDIANSplmwFRGYQLPDTPAIDG----GYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFDVES 354
|
170 180 190
....*....|....*....|....*....|
gi 1720426399 577 IYLRSEAVAQVFV-------HGESLQAFLI 599
Cdd:cd05973 355 ALIEHPAVAEAAVigvpdpeRTEVVKAFVV 384
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
270-607 |
6.84e-09 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 58.52 E-value: 6.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 270 DLAIICFTSGTTGNPKGAMITHQNIINDCSGFikatESALTLNASDTQISYLPLAHMYEQQLQ-CVMLCHGAKIGF---F 345
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFF----AGSGGALPSDVLYTCLPLYHSTALIVGwSACLASGATLVIrkkF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 346 QGdiRLLMDDLKVLQPTIFPVVPRLLnrmfdrifgqantslkRWLLdfASKRKEAELRsgivrnnslwdklifHKIQSSL 425
Cdd:cd05940 158 SA--SNFWDDIRKYQATIFQYIGELC----------------RYLL--NQPPKPTERK---------------HKVRMIF 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 426 GGKVRLMITGaapvsatvlTFL-RTALGcQFYEGYGQTECTAGcCLSLPG-DWTAGHVGA----PMPCNYVKlVDVEEMN 499
Cdd:cd05940 203 GNGLRPDIWE---------EFKeRFGVP-RIAEFYAATEGNSG-FINFFGkPGAIGRNPSllrkVAPLALVK-YDLESGE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 500 YL---------ASKGEGEVCVKGAN---VFKGYLkDPARTAEAL------DKDGWLHTGDIGKWLPNGTLKIIDRKKHIF 561
Cdd:cd05940 271 PIrdaegrcikVPRGEPGLLISRINplePFDGYT-DPAATEKKIlrdvfkKGDAWFNTGDLMRLDGEGFWYFVDRLGDTF 349
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1720426399 562 KLaQGEYIAPEKIENIYLRSEAVAQVFVHGeslqafliaVVVPDVE 607
Cdd:cd05940 350 RW-KGENVSTTEVAAVLGAFPGVEEANVYG---------VQVPGTD 385
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
266-586 |
7.19e-09 |
|
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: 58.63 E-value: 7.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 266 PEPEDLAIICFTSGTTGNPKGAMITHQNIindcSGFIKATESALTLNASDTQISYLPLAHMYeqqlqcvmlchGAKIGff 345
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTF----AAQIDALRQLYGIRPGEVDLATFPLFALF-----------GPALG-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 346 qgdirllmddLKVLQPTIFPVVPrllnrmfdrifGQANtslKRWLLDFASKRKEaelrSGIVRNNSLWDKLIFHKIQSSL 425
Cdd:cd05910 145 ----------LTSVIPDMDPTRP-----------ARAD---PQKLVGAIRQYGV----SIVFGSPALLERVARYCAQHGI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 426 G-GKVRLMITGAAPVSATVLTFLRTAL--GCQFYEGYGQTECTAGCC------LSLPGDWTAGH----VGAPMPCNYVKL 492
Cdd:cd05910 197 TlPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrelLATTTAATSGGagtcVGRPIPGVRVRI 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 493 VDVEEMNY--------LASKGEGEVCVKGANVFKGYLKDPARTAEALDKDG----WLHTGDIGKWLPNGTLKIIDRKKHI 560
Cdd:cd05910 277 IEIDDEPIaewddtleLPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHR 356
|
330 340
....*....|....*....|....*.
gi 1720426399 561 FKLAQGEYIApEKIENIYLRSEAVAQ 586
Cdd:cd05910 357 VITTGGTLYT-EPVERVFNTHPGVRR 381
|
|
| 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 1720426399 482 GAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPArTAEALDKDGWLHTGDIGkWLPNGTLKIIDRKKHIF 561
Cdd:PRK09192 388 GKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLMSGYFRDEE-SQDVLAADGWLDTGDLG-YLLDGYLYITGRAKDLI 464
|
90
....*....|....
gi 1720426399 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 1720426399 452 GCQFYEGYGQTEctAGCCLSLPGDWTAGHVGAPMPCnyVKLVDVE-----------EMNYLASKGE--GE-VCVKGANVF 517
Cdd:PRK13388 288 GCQVEDGYGSSE--GAVIVVREPGTPPGSIGRGAPG--VAIYNPEtltecavarfdAHGALLNADEaiGElVNTAGAGFF 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 518 KGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFVHG----ES 593
Cdd:PRK13388 364 EGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYAvpdeRV 441
|
170
....*....|....*.
gi 1720426399 594 LQAFLIAVVVPDVESL 609
Cdd:PRK13388 442 GDQVMAALVLRDGATF 457
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
274-593 |
1.70e-07 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 53.56 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 274 ICFTSGTTGNPKGAMITHQNIIndcsGFIKATESALTLNASDTQISYLPLAH-------MYeqqlqcVMLCHGAKIGFFQ 346
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERSWI----ESFVCNEDLFNISGEDAILAPGPLSHslflygaIS------ALYLGGTFIGQRK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 347 GDIRLLMDDLKVLQPTIFPVVPRLLNrmfdrifgqantSLKRWLldfaskRKEAELRSgIVRNNSLWDKLIFHKIQSslg 426
Cdd:cd17633 75 FNPKSWIRKINQYNATVIYLVPTMLQ------------ALARTL------EPESKIKS-IFSSGQKLFESTKKKLKN--- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 427 gkvrlmitgAAPVSatvltflrtalgcQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCnyvklVDVEEMNYlASKGE 506
Cdd:cd17633 133 ---------IFPKA-------------NLIEFYGTSELSFITYNFNQESRPPNSVGRPFPN-----VEIEIRNA-DGGEI 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 507 GEVCVKGANVFKGYLKdpartAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQ 586
Cdd:cd17633 185 GKIFVKSEMVFSGYVR-----GGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIEE 258
|
....*..
gi 1720426399 587 VFVHGES 593
Cdd:cd17633 259 AIVVGIP 265
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
120-607 |
2.26e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 53.86 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 120 EWISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVI 199
Cdd:PRK13390 23 EQVSYRQLDDDSAALARVLYDAGLRT--GDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 200 FADKPekakllLEGVENKLtpclkiivimdsyGSDLVERgKKCGVEIISLKALEdlGRVNRVKPKPPEPEDLAIICFTSG 279
Cdd:PRK13390 101 VASAA------LDGLAAKV-------------GADLPLR-LSFGGEIDGFGSFE--AALAGAGPRLTEQPCGAVMLYSSG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 280 TTGNPKGAM--ITHQNIINDCSGFIKATESALTLNASDTQISYLPLAHmyEQQLQCVMLCH---GAKIGFFQGDIRLLMD 354
Cdd:PRK13390 159 TTGFPKGIQpdLPGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYH--AAPLRWCSMVHalgGTVVLAKRFDAQATLG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 355 DLKVLQPTIFPVVPRLLNRMFdrifgqantslkrwlldfaskRKEAELRSgivrnnsLWDklifhkiQSSLggkvRLMIT 434
Cdd:PRK13390 237 HVERYRITVTQMVPTMFVRLL---------------------KLDADVRT-------RYD-------VSSL----RAVIH 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 435 GAAPVSATVLTFLRTALGCQFYEGYGQTEcTAGCCLSLPGDWTA--GHVGAPMpCNYVKLVDvEEMNYLASKGEGEVCVK 512
Cdd:PRK13390 278 AAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGRSV-LGDLHICD-DDGNELPAGRIGTVYFE 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 513 GANVFKGYLKDPARTAEALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVH 590
Cdd:PRK13390 355 RDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQETENALTMHPAVHDVAVI 433
|
490
....*....|....*..
gi 1720426399 591 GeslqafliavvVPDVE 607
Cdd:PRK13390 434 G-----------VPDPE 439
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
263-607 |
2.56e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 53.78 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 263 PKPPEPEdlAIICFTSGTTGNPKGAMITHQNIINDCSGFIkateSALTLNASDTQISYLPLAHMYEQQLQCVMLCHGAKI 342
Cdd:PRK07788 203 PKPPKPG--GIVILTSGTTGTPKGAPRPEPSPLAPLAGLL----SRVPFRAGETTLLPAPMFHATGWAHLTLAMALGSTV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 343 GF---FqgDIRLLMDDLKVLQPTIFPVVPRLLNRMFDrifgqantslkrwLLDFASKRKEAelrsgivrnnslwdklifh 419
Cdd:PRK07788 277 VLrrrF--DPEATLEDIAKHKATALVVVPVMLSRILD-------------LGPEVLAKYDT------------------- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 420 kiqSSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECtAGCCLSLPGDWTA--GHVGAPMPCNYVKLVDvEE 497
Cdd:PRK07788 323 ---SSL----KIIFVSGSALSPELATRALEAFGPVLYNLYGSTEV-AFATIATPEDLAEapGTVGRPPKGVTVKILD-EN 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 498 MNYLASKGEGEVCVKGANVFKGYL--KDPARtaealdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIE 575
Cdd:PRK07788 394 GNEVPRGVVGRIFVGNGFPFEGYTdgRDKQI------IDGLLSSGDVGYFDEDGLLFVDGRDDDMI-VSGGENVFPAEVE 466
|
330 340 350
....*....|....*....|....*....|..
gi 1720426399 576 NIYLRSEAVAQVFVHGeslqafliavvVPDVE 607
Cdd:PRK07788 467 DLLAGHPDVVEAAVIG-----------VDDEE 487
|
|
| 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 1720426399 120 EWISYKEVAELAECIGSGLIQKGFKPCSEQFIglFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVI 199
Cdd:PRK04319 72 EKYTYKELKELSNKFANVLKELGVEKGDRVFI--FMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 200 FADKpekaKLLLEGVENKLtPCLKIIVIMDsygsDLVERGKKCgveiISLKAL-----EDLgrvnrvKPKPPEPEDLAII 274
Cdd:PRK04319 150 ITTP----ALLERKPADDL-PSLKHVLLVG----EDVEEGPGT----LDFNALmeqasDEF------DIEWTDREDGAIL 210
|
170 180
....*....|....*....|...
gi 1720426399 275 CFTSGTTGNPKG------AMITH 291
Cdd:PRK04319 211 HYTSGSTGKPKGvlhvhnAMLQH 233
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
268-600 |
3.05e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.40 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 268 PEDLAIICFTSGTTGNPKGAMITHQNIINDcsgfikatesaltlnasdtQISYLPLAHMYEQQL------QCVMLC---- 337
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEQRGMLNN-------------------QLSKVPYLALSEADViaqtasQSFDISvwqf 3928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 338 -----HGAKIGFFQGDI----RLLMDDLKVLQPTIFPVVPRLLNRMF--DRifgQANTSLkRWLL--------DFASKRK 398
Cdd:PRK05691 3929 laaplFGARVEIVPNAIahdpQGLLAHVQAQGITVLESVPSLIQGMLaeDR---QALDGL-RWMLptgeamppELARQWL 4004
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 399 EAELRSGIVrnNSLwdklifhkiqsslggkvrlmitGAAPVSATVlTFLRTALgcqfyegygqtECTAGCCLSlpgdwta 478
Cdd:PRK05691 4005 QRYPQIGLV--NAY----------------------GPAECSDDV-AFFRVDL-----------ASTRGSYLP------- 4041
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 479 ghVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGW-------LHTGDIGKWLPNGTL 551
Cdd:PRK05691 4042 --IGSPTDNNRLYLLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRRSDGVL 4118
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1720426399 552 KIIDRKKHI-----FKLAQGEyIAPEKIENIYLRSEAVA-QVFVHGESLQAFLIA 600
Cdd:PRK05691 4119 EYVGRIDHQvkirgYRIELGE-IEARLHEQAEVREAAVAvQEGVNGKHLVGYLVP 4172
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
429-600 |
3.32e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.02 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 429 VRLMITGAAPVSATVLTFLRTAL-GCQFYEGYGQTE----CTAGCCLSLPGDWTAghVGAPMPCNYVKLVDvEEMNYLAS 503
Cdd:PRK05691 1390 LRRLFSGGEALPAELRNRVLQRLpQVQLHNRYGPTEtainVTHWQCQAEDGERSP--IGRPLGNVLCRVLD-AELNLLPP 1466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 504 KGEGEVCVKGANVFKGYLKDPARTAE-----ALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIEN 576
Cdd:PRK05691 1467 GVAGELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL-RGFRVEPEEIQA 1545
|
170 180
....*....|....*....|....*.
gi 1720426399 577 IYLRSEAVAQ--VFVHGESLQAFLIA 600
Cdd:PRK05691 1546 RLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
246-558 |
6.29e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 52.64 E-value: 6.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 246 IISLKALeDLGRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIINDC----SGFIKATESALTLNAsdTQISYL 321
Cdd:PRK05850 138 VIEVDLL-DLDSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFeqlmSDYFGDTGGVPPPDT--TVVSWL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 322 PLAH-MyeqqlqCVMLchGAKIGFFQGDIRLLMDDLKVLQPtifpvvP----RLLNRmfdriFGQANTSLKRWLLDFASK 396
Cdd:PRK05850 215 PFYHdM------GLVL--GVCAPILGGCPAVLTSPVAFLQR------ParwmQLLAS-----NPHAFSAAPNFAFELAVR 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 397 RKEAELRSGIvrnnslwdklifhkiqsSLGGkVRLMITGAAPV-SATVLTFLRTALGCQFYE-----GYGQTECTAGCCL 470
Cdd:PRK05850 276 KTSDDDMAGL-----------------DLGG-VLGIISGSERVhPATLKRFADRFAPFNLREtairpSYGLAEATVYVAT 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 471 SLPGD-----------WTAGHVgapMPC---------NY-------VKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKD 523
Cdd:PRK05850 338 REPGQppesvrfdyekLSAGHA---KRCetgggtplvSYgsprsptVRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQK 414
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1720426399 524 PART-----AEALDK-----DG-WLHTGDIGkWLPNGTLKIIDRKK 558
Cdd:PRK05850 415 PEETertfgATLVDPspgtpEGpWLRTGDLG-FISEGELFIVGRIK 459
|
|
| 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 1720426399 265 PPEPEDLAIICFTSGTTGNPKGAMITHQNIIN 296
Cdd:PRK10252 594 LSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVN 625
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
266-615 |
4.29e-06 |
|
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: 49.30 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 266 PEPEDLAIICfTSGTTGNPKGAMITHQNIindcsgFIKATESALTLNASDTQISYLPLAHMYEQQLQCVMLC---HGAK- 341
Cdd:cd05924 1 RSADDLYILY-TGGTTGMPKGVMWRQEDI------FRMLMGGADFGTGEFTPSEDAHKAAAAAAGTVMFPAPplmHGTGs 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 342 ----IGFFQGDiRLLMDDLKVLQPTIFPVVPR-LLNRMFdrIFGQAntsLKRWLLDfaskrkeaELRSGivRNNSLwdkl 416
Cdd:cd05924 74 wtafGGLLGGQ-TVVLPDDRFDPEEVWRTIEKhKVTSMT--IVGDA---MARPLID--------ALRDA--GPYDL---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 417 ifhkiqSSLggkvRLMITGAAPVSATVLT-FLRTALGCQFYEGYGQTECTA-GCCLSLPGDWTAGHVGAPMPcnYVKLVD 494
Cdd:cd05924 134 ------SSL----FAISSGGALLSPEVKQgLLELVPNITLVDAFGSSETGFtGSGHSAGSGPETGPFTRANP--DTVVLD 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 495 vEEMNYL--ASKGEGEVCVKGaNVFKGYLKDPARTAEAL-DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYI 569
Cdd:cd05924 202 -DDGRVVppGSGGVGWIARRG-HIPLGYYGDEAKTAETFpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTG-GEKV 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1720426399 570 APEKIENIYLRSEAVAQVFVHGeslqafliavvVPDveslPSWAQK 615
Cdd:cd05924 279 FPEEVEEALKSHPAVYDVLVVG-----------RPD----ERWGQE 309
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
454-591 |
5.18e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 49.39 E-value: 5.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 454 QFYEGYGQTECTAGCCLSlPGDWTAGHVGAPMPCNYVKLVDVEEMNYLASKGE-GEVCVKGANVFKGYLKDpARTAEALD 532
Cdd:PRK07638 281 KLYEFYGASELSFVTALV-DEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEiGTVYVKSPQFFMGYIIG-GVLARELN 358
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720426399 533 KDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:PRK07638 359 ADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIESVLHEHPAVDEIVVIG 416
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
264-616 |
1.03e-05 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 48.12 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 264 KPPEP--EDLAIICFTSGTTGNPKGAMIThqniindcsgfikatESALTLNASDTqisylplaHMY---EQQLQCVMLCH 338
Cdd:PRK07824 28 RVGEPidDDVALVVATSGTTGTPKGAMLT---------------AAALTASADAT--------HDRlggPGQWLLALPAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 339 gaKIGFFQGDIRLLM---DDLKVLQPTIF--PVVPRLLNRM-FDRIFgqanTSLKRWLLDFASKRKEA--ELRSgivrnn 410
Cdd:PRK07824 85 --HIAGLQVLVRSVIagsEPVELDVSAGFdpTALPRAVAELgGGRRY----TSLVPMQLAKALDDPAAtaALAE------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 411 slwdkliFHKIqsslggkvrlmITGAAPVSATVLTfLRTALGCQFYEGYGQTEcTAGCCLslpgdwtagHVGAPMPCNYV 490
Cdd:PRK07824 153 -------LDAV-----------LVGGGPAPAPVLD-AAAAAGINVVRTYGMSE-TSGGCV---------YDGVPLDGVRV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 491 KLVDveemnylaskgeGEVCVKGANVFKGY--LKDPARTAEaldkDGWLHTGDIGKwLPNGTLKIIDRKKHIFKLAqGEY 568
Cdd:PRK07824 204 RVED------------GRIALGGPTLAKGYrnPVDPDPFAE----PGWFRTDDLGA-LDDGVLTVLGRADDAISTG-GLT 265
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1720426399 569 IAPEKIENIYLRSEAVAQVFVHG---ESLQAFLIAVVVPDVESLPSWAQKR 616
Cdd:PRK07824 266 VLPQVVEAALATHPAVADCAVFGlpdDRLGQRVVAAVVGDGGPAPTLEALR 316
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
265-326 |
2.86e-05 |
|
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: 47.29 E-value: 2.86e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720426399 265 PPEPEDLAIICFTSGTTGNPKGAMITHQNIINdCSGFIkateSALTLNASDTQISYLPLAHM 326
Cdd:cd05938 140 HVTIKSPALYIYTSGTTGLPKAARISHLRVLQ-CSGFL----SLCGVTADDVIYITLPLYHS 196
|
|
| 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 1720426399 452 GCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVdVEEMNYLASKGEGEVCVKGANVFKGYLKDPArtaEAL 531
Cdd:PRK06060 286 GIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVV-APDGTTAGPGVEGDLWVRGPAIAKGYWNRPD---SPV 361
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720426399 532 DKDGWLHTGDIGKWLPNGTLKIIDRKKHIfKLAQGEYIAPEKIENIYLRSEAVAQVFVHG-------ESLQAFLIAVV 602
Cdd:PRK06060 362 ANEGWLDTRDRVCIDSDGWVTYRCRADDT-EVIGGVNVDPREVERLIIEDEAVAEAAVVAvrestgaSTLQAFLVATS 438
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
122-325 |
1.02e-04 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 45.64 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 122 ISYKEVAELAECIGSGLIQKGFKPcsEQFIGLFSQNRPEWV-----IVEQGcfsysmVVVPLYDT-LGADAITYIVNKAE 195
Cdd:PRK08279 63 ISYAELNARANRYAHWAAARGVGK--GDVVALLMENRPEYLaawlgLAKLG------AVVALLNTqQRGAVLAHSLNLVD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 196 LSVIFADkPEKAKLLlEGVENKLTPCLKIIVIMDSYGSDLVergkkcgveiislkALEDLGRVNRVKPKPPEP------- 268
Cdd:PRK08279 135 AKHLIVG-EELVEAF-EEARADLARPPRLWVAGGDTLDDPE--------------GYEDLAAAAAGAPTTNPAsrsgvta 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720426399 269 EDLAIICFTSGTTGNPKGAMITHQNIINDCSGFikatesALTLNASDTQISY--LPLAH 325
Cdd:PRK08279 199 KDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGF------GGLLRLTPDDVLYccLPLYH 251
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
268-614 |
1.40e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 45.54 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 268 PEDLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKAtesaLTLNASDTQIsylplaHMYE-------QQLQCVMLChGA 340
Cdd:PRK05691 2332 PQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIER----FGMRADDCEL------HFYSinfdaasERLLVPLLC-GA 2400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 341 KIGF-FQG-----DIRLLMDDLKVlqpTIFPVVPRllnrmfdriFGqanTSLKRWLldfaskrkeaelrsgIVRNNSLwd 414
Cdd:PRK05691 2401 RVVLrAQGqwgaeEICQLIREQQV---SILGFTPS---------YG---SQLAQWL---------------AGQGEQL-- 2448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 415 klifhkiqsslggKVRLMITGAAPVSATVLTFLRTALGCQ-FYEGYGQTE-------CTAGccLSLPGDWTAGHVGAPMP 486
Cdd:PRK05691 2449 -------------PVRMCITGGEALTGEHLQRIRQAFAPQlFFNAYGPTEtvvmplaCLAP--EQLEEGAASVPIGRVVG 2513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 487 CNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKH 559
Cdd:PRK05691 2514 ARVAYILD-ADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdggrlyrTGDLVRLRADGLVEYVGRIDH 2592
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720426399 560 IFKLaQGEYIAPEKIENIYLRSEAV--AQVFVHGESLQAFLIAVVVPDVESLPSWAQ 614
Cdd:PRK05691 2593 QVKI-RGFRIELGEIESRLLEHPAVreAVVLALDTPSGKQLAGYLVSAVAGQDDEAQ 2648
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
488-598 |
2.07e-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: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 488 NYVKLVDVEEMNYLASKGEGE----VCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKL 563
Cdd:cd05915 338 IPLVRLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKS 417
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1720426399 564 AqGEYIAPEKIENIYLRSEAVAQVFV-------HGESLQAFL 598
Cdd:cd05915 418 G-GEWISSVDLENALMGHPKVKEAAVvaiphpkWQERPLAVV 458
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
264-325 |
3.00e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 43.95 E-value: 3.00e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720426399 264 KPPEP--EDLAIICFTSGTTGNPKGAMITHQNIindCSGFIKATEsALTLNASDTQISYLPLAH 325
Cdd:PRK07769 173 VPPEAneDTIAYLQYTSGSTRIPAGVQITHLNL---PTNVLQVID-ALEGQEGDRGVSWLPFFH 232
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
260-591 |
8.58e-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: 42.56 E-value: 8.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 260 RVKPKPPEPEDLAIICFTSGTTGNPKGAMITHqniindcSGF-IKATESaltlnasdtqisylpLAHMYEQQLQCVMLCh 338
Cdd:cd17634 223 EHQPEAMNAEDPLFILYTSGTTGKPKGVLHTT-------GGYlVYAATT---------------MKYVFDYGPGDIYWC- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 339 GAKIGFFQGDIRLLMDDLkVLQPTIF-----PV--VPRLLNRMFDR----IFGQANTSLKrwlldfaSKRKEAelrsgiv 407
Cdd:cd17634 280 TADVGWVTGHSYLLYGPL-ACGATTLlyegvPNwpTPARMWQVVDKhgvnILYTAPTAIR-------ALMAAG------- 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 408 rnnslwDKLIFHKIQSSLggkvRLMITGAAPVSATVLTFLRTALG---CQFYEGYGQTECTAGCCLSLPG--DWTAGHVG 482
Cdd:cd17634 345 ------DDAIEGTDRSSL----RILGSVGEPINPEAYEWYWKKIGkekCPVVDTWWQTETGGFMITPLPGaiELKAGSAT 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426399 483 APMPCNYVKLVDvEEMNYLASKGEGEVCVKGA--NVFKGYLKDPARTAEALDK--DGWLHTGDIGKWLPNGTLKIIDRKK 558
Cdd:cd17634 415 RPVFGVQPAVVD-NEGHPQPGGTEGNLVITDPwpGQTRTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSD 493
|
330 340 350
....*....|....*....|....*....|...
gi 1720426399 559 HIFKLAqGEYIAPEKIENIYLRSEAVAQVFVHG 591
Cdd:cd17634 494 DVINVA-GHRLGTAEIESVLVAHPKVAEAAVVG 525
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
267-325 |
8.47e-03 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 39.34 E-value: 8.47e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720426399 267 EPEDLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKatesALTLNASDTQISYLPLAH 325
Cdd:cd05937 85 DPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSH----DLNLKNGDRTYTCMPLYH 139
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