|
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 ... |
116-660 |
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: 911.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 116 QPYEWLSYKQ----------------------------------WVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAEL 161
Cdd:cd05927 1 GPYEWISYKEvaeradnigsalrslggkpapasfvgiysinrpeWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 162 SLVFVDKpekaklllegvenklipglkiivvmdaygselvergqrcGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICF 241
Cdd:cd05927 81 SIVFCDA---------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 242 TSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDL 321
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 322 KVLQPTVFPVVPRLLNRMFDRIFG--QANTTLKRWLLDFASKRKEAELRSGIIRNNSLWDRLIFHKVQSSLGGRVRLMVT 399
Cdd:cd05927 202 KALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 400 GAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAA--EGEGEVCVK 477
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAKdpNPRGEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 478 GPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGE 557
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 558 SLQAFLIAIVVPDVETLCSWA-QKRGFEGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLL 636
Cdd:cd05927 442 SLKSFLVAIVVPDPDVLKEWAaSKGGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLL 521
|
570 580
....*....|....*....|....
gi 557878740 637 TPTMKAKRPELRNYFRSQIDDLYS 660
Cdd:cd05927 522 TPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
86-662 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 674.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 86 YDDVTTLYEGFQRGIQVSNNGPCLGSR-KPDQ---PYEWLSY--------------------------------KQWVII 129
Cdd:PLN02736 40 HPEIGTLHDNFVYAVETFRDYKYLGTRiRVDGtvgEYKWMTYgeagtartaigsglvqhgipkgacvglyfinrPEWLIV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 130 EQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVdKPEKAKLLLEGVENklIPGLKIIVVMDAYGSELVERGQRCGV 209
Cdd:PLN02736 120 DHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCLSE--IPSVRLIVVVGGADEPLPSLPSGTGV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 210 EVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENtvnpCPDDTLISFLPLA 289
Cdd:PLN02736 197 EIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKF----YPSDVHISYLPLA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 290 HMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFG--QANTTLKRWLLDFASKRKEAEL 367
Cdd:PLN02736 273 HIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNavKESGGLKERLFNAAYNAKKQAL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 368 RSGiiRNNS-LWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHV 446
Cdd:PLN02736 353 ENG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHV 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 447 GAPMPCNLIKLVDVEEMNYMAAEG---EGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK 523
Cdd:PLN02736 431 GSPNPACEVKLVDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKK 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 524 HIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRGFE-GSFEELCRNKDVKKAILE 602
Cdd:PLN02736 511 NIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRVRAAVLA 590
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 603 DMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYSTI 662
Cdd:PLN02736 591 DMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYAEL 650
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
86-660 |
1.19e-170 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 500.40 E-value: 1.19e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 86 YDDVTTLYEGFQRGIQVSNNGPCLgSRKPDQPYEWLSYKQ--------------------------------WVIIEQGC 133
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVAL-REKEDGIWQSLTWAEfaervralaagllalgvkpgdrvailsdnrpeWVIADLAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 134 FAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLLLEGVENklIPGLKIIVVMDaygselvERGQRCGVEVTS 213
Cdd:COG1022 86 LAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDE--LPSLRHIVVLD-------PRGLRDDPRLLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 214 MKAMEDLGRANR------RKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKAtentVNPCPDDTLISFLP 287
Cdd:COG1022 157 LDELLALGREVAdpaeleARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLER----LPLGPGDRTLSFLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 288 LAHMFERVVECVMLCHGAKIGFfQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQAN--TTLKRWLLDFA---SKR 362
Cdd:COG1022 233 LAHVFERTVSYYALAAGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEeaGGLKRKLFRWAlavGRR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 363 KEAELRSGiiRNNSLW--------DRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCC 434
Cdd:COG1022 312 YARARLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPVIT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 435 LTMPGDWTAGHVGAPMPCNLIKLvdveemnymaAEgEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNG 514
Cdd:COG1022 389 VNRPGDNRIGTVGPPLPGVEVKI----------AE-DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 515 TLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESlQAFLIAIVVPDVETLCSWAQKRG-FEGSFEELCRN 593
Cdd:COG1022 458 FLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGlPYTSYAELAQD 536
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557878740 594 KDVKKAILEDMVRLGKdsGLKPFEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYS 660
Cdd:COG1022 537 PEVRALIQEEVDRANA--GLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYA 601
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
85-647 |
7.94e-162 |
|
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: 472.47 E-value: 7.94e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 85 FYDDVTTLYEGFQR-GIQV-------SNNGPclgsrkpdqpyewlsykQWVIIEQGCFAYSMVIVPLYDTLGNEAITYIV 156
Cdd:cd05907 11 FAEEVRALAKGLIAlGVEPgdrvailSRNRP-----------------EWTIADLAILAIGAVPVPIYPTSSAEQIAYIL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 157 NKAELSLVFVDKPEkaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppapeDL 236
Cdd:cd05907 74 NDSEAKALFVEDPD----------------------------------------------------------------DL 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 237 AVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKAtentVNPCPDDTLISFLPLAHMFERV-VECVMLCHGAKIGFFQgDIR 315
Cdd:cd05907 90 ATIIYTSGTTGRPKGVMLSHRNILSNALALAER----LPATEGDRHLSFLPLAHVFERRaGLYVPLLAGARIYFAS-SAE 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 316 LLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQANTTLKRWLLDFASkrkeaelrsgiirnnslwdrlifhkvqsslGGRVR 395
Cdd:cd05907 165 TLLDDLSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV------------------------------GGRLR 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 396 LMVTGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDveemnymaaegEGEVC 475
Cdd:cd05907 215 FAASGGAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEIL 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 476 VKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVH 555
Cdd:cd05907 283 VRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVI 362
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 556 GESlQAFLIAIVVPDVETLCSWAQKRG-FEGSFEELCRNKDVKKAILEDMVRLGKdsGLKPFEQVKGITLHPELFSIDNG 634
Cdd:cd05907 363 GDG-RPFLVALIVPDPEALEAWAEEHGiAYTDVAELAANPAVRAEIEAAVEAANA--RLSRYEQIKKFLLLPEPFTIENG 439
|
570
....*....|...
gi 557878740 635 LLTPTMKAKRPEL 647
Cdd:cd05907 440 ELTPTLKLKRPVI 452
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
125-664 |
1.08e-146 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 441.20 E-value: 1.08e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 125 QWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLLleGVENKLIPGLKIIVVMDAYGSELVERG 204
Cdd:PLN02861 114 EWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKISSIL--SCLPKCSSNLKTIVSFGDVSSEQKEEA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 205 QRCGVEVTSMKAMEDLGRANRRKPkPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCP-DDTLI 283
Cdd:PLN02861 192 EELGVSCFSWEEFSLMGSLDCELP-PKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKVTDRVATeEDSYF 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 284 SFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLlnrmFDRIFG------QANTTLKRWLLD 357
Cdd:PLN02861 271 SYLPLAHVYDQVIETYCISKGASIGFWQGDIRYLMEDVQALKPTIFCGVPRV----YDRIYTgimqkiSSGGMLRKKLFD 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 358 FASKRKEAELRSGIIRNNS--LWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCL 435
Cdd:PLN02861 347 FAYNYKLGNLRKGLKQEEAspRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGCFT 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 436 TMPGDWT-AGHVGAPMPCNLIKLVDVEEMNYMAAEG--EGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLP 512
Cdd:PLN02861 427 SIANVFSmVGTVGVPMTTIEARLESVPEMGYDALSDvpRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQP 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 513 NGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRGFEGSFEELCR 592
Cdd:PLN02861 506 NGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCK 585
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557878740 593 NKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYSTIKV 664
Cdd:PLN02861 586 NLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYSEAKG 657
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
117-644 |
2.02e-146 |
|
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: 435.11 E-value: 2.02e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 117 PYEWLSYKQ--------------------------------WVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLV 164
Cdd:cd17639 2 EYKYMSYAEvwervlnfgrglvelglkpgdkvaifaetraeWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 165 FVDkpekaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkpPAPEDLAVICFTSG 244
Cdd:cd17639 82 FTD---------------------------------------------------------------GKPDDLACIMYTSG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 245 TTGNPKGAMVTHRNIVSDCSAFVKATENTVnpCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFfqGDIRLLMD----- 319
Cdd:cd17639 99 STGNPKGVMLTHGNLVAGIAGLGDRVPELL--GPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDkskrg 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 320 ---DLKVLQPTVFPVVPRLLNRMFDRIFGQANT--TLKRWLLDFASKRKEAELRSGIirNNSLWDRLIFHKVQSSLGGRV 394
Cdd:cd17639 175 ckgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPmgGLKRTLFWTAYQSKLKALKEGP--GTPLLDELVFKKVRAALGGRL 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 395 RLMVTGAAPVSATVLTFLrAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYM--AAEGEG 472
Cdd:cd17639 253 RYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYStdKPPPRG 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 473 EVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQV 552
Cdd:cd17639 332 EILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVNNI 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 553 FVHGESLQAFLIAIVVPDVETLCSWAQKRGF-EGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHPELFSI 631
Cdd:cd17639 412 CVYADPDKSYPVAIVVPNEKHLTKLAEKHGViNSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEWTP 491
|
570
....*....|...
gi 557878740 632 DNGLLTPTMKAKR 644
Cdd:cd17639 492 ENGLVTAAQKLKR 504
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
125-662 |
2.84e-146 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 440.02 E-value: 2.84e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 125 QWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV-DKpeKAKLLLEGvENKLIPGLKIIVVMDAYGSELVER 203
Cdd:PLN02430 113 QWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVqDK--KIKELLEP-DCKSAKRLKAIVSFTSVTEEESDK 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 204 GQRCGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRN---IVSDCSAFVKATENTVNPcpDD 280
Cdd:PLN02430 190 ASQIGVKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAvatFVRGVDLFMEQFEDKMTH--DD 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 281 TLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFG--QANTTLKRWLLDF 358
Cdd:PLN02430 268 VYLSFLPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNA 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 359 ASKRKEAELRSGIIRNNS--LWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLT 436
Cdd:PLN02430 348 LYKYKLAWMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLG 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 437 MPGDWTA-GHVGAPMPCNLIKLVDVEEMNY--MAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPN 513
Cdd:PLN02430 428 FPDEMCMlGTVGAPAVYNELRLEEVPEMGYdpLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPN 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 514 GTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRGFEGSFEELCRN 593
Cdd:PLN02430 507 GVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSL 586
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557878740 594 KDVKKAILEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYSTI 662
Cdd:PLN02430 587 PELKEHILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMYRKL 655
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
87-663 |
7.13e-145 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 436.76 E-value: 7.13e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 87 DDVTTLYEGFQRGIQVSNNGPCLGSR-----KPDQpYEWLSYKQ--------------------------------WVII 129
Cdd:PLN02614 42 EGMDSCWDVFRMSVEKYPNNPMLGRReivdgKPGK-YVWQTYQEvydiviklgnslrsvgvkdeakcgiyganspeWIIS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 130 EQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLLlegvenKLIPG----LKIIVVMDAYGSELVERGQ 205
Cdd:PLN02614 121 MEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKISELF------KTCPNsteyMKTVVSFGGVSREQKEEAE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 206 RCGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENtVNPC--PDDTLI 283
Cdd:PLN02614 195 TFGLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKS-ANAAltVKDVYL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 284 SFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQANTT--LKRWLLDFASK 361
Cdd:PLN02614 274 SYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGgfLKKFVFDSAFS 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 362 RKEAELRSGI--IRNNSLWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPG 439
Cdd:PLN02614 354 YKFGNMKKGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPD 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 440 DW-TAGHVGAPMPCNLIKLVDVEEMNY--MAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTL 516
Cdd:PLN02614 434 ELdMLGTVGPPVPNVDIRLESVPEMEYdaLASTPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSM 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 517 KIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRGFEGSFEELCRNKDV 596
Cdd:PLN02614 513 KIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKA 592
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557878740 597 KKAILEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYSTIK 663
Cdd:PLN02614 593 KEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYKTTN 659
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
62-660 |
8.30e-125 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 385.62 E-value: 8.30e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 62 VEVAGSGG-ARRSALLDsdEPLVYFYDDVTTLYEGFQRGIQVSNNGPCLGSRK---------PDQ---------PYEWLS 122
Cdd:PLN02387 31 VDVGGEPGyAIRNARFP--ELVETPWEGATTLAALFEQSCKKYSDKRLLGTRKlisrefetsSDGrkfeklhlgEYEWIT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 123 YKQ--------------------------------WVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDKPE 170
Cdd:PLN02387 109 YGQvfervcnfasglvalghnkeervaifadtraeWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQ 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 171 KAKLLleGVENKLiPGLKIIVVMDAYGSELVERG-QRCGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNP 249
Cdd:PLN02387 189 LKKLI--DISSQL-ETVKRVIYMDDEGVDSDSSLsGSSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLP 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 250 KGAMVTHRNIVSDCSAFVkatenTVNP--CPDDTLISFLPLAHMFERVVECVMLCHGAKIGFfqGDIRLLMD-------- 319
Cdd:PLN02387 266 KGVMMTHGNIVATVAGVM-----TVVPklGKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDtsnkikkg 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 320 ---DLKVLQPTVFPVVPRLLNRMFDRIFGQANTT--LKRWLLDFASKRKEAELR------SGIIRnnSLWDRLIFHKVQS 388
Cdd:PLN02387 339 tkgDASALKPTLMTAVPAILDRVRDGVRKKVDAKggLAKKLFDIAYKRRLAAIEgswfgaWGLEK--LLWDALVFKKIRA 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 389 SLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAA 468
Cdd:PLN02387 417 VLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLIS 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 469 EG---EGEVCVKGPNVFQGYLKDPAKTAEA--LDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIEN 541
Cdd:PLN02387 497 DKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEA 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 542 IYMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRGFE-GSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVK 620
Cdd:PLN02387 577 ALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPA 656
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 557878740 621 GITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYS 660
Cdd:PLN02387 657 KIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
125-529 |
2.82e-114 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 349.30 E-value: 2.82e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 125 QWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLLLEGVENKLIPGLKIIVVMDAYGSELVerg 204
Cdd:pfam00501 58 EWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEP--- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 205 qrcgvevtsMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCPDDTLIS 284
Cdd:pfam00501 135 ---------LPEEAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 285 FLPLAHMFERVVEC-VMLCHGAKIGFFQGDIRL----LMDDLKVLQPTVFPVVPRLLNRMFDrifgqaNTTLKRWLLdfa 359
Cdd:pfam00501 206 TLPLFHDFGLSLGLlGPLLAGATVVLPPGFPALdpaaLLELIERYKVTVLYGVPTLLNMLLE------AGAPKRALL--- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 360 skrkeaelrsgiirnnslwdrlifhkvqsslgGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPG 439
Cdd:pfam00501 277 --------------------------------SSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 440 DW---TAGHVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTL 516
Cdd:pfam00501 325 DEdlrSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYL 404
|
410
....*....|...
gi 557878740 517 KIIDRKKHIFKLA 529
Cdd:pfam00501 405 EIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
79-659 |
1.89e-99 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 319.61 E-value: 1.89e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 79 DEPLVYFYDDVTTLYEGFQRGIQVsnngpcLGSRKPDQP--YE---WlsykQWVIIEQGCFAYSMVIVPLYDTLGNEAIT 153
Cdd:PTZ00216 117 NETRYITYAELWERIVNFGRGLAE------LGLTKGSNVaiYEetrW----EWLASIYGIWSQSMVAATVYANLGEDALA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 154 YIVNKAELSLVfVDKPEKAKLLLEGVENKLIPGLKIIvvmdaYGSELVERGQRCGVEVTSMKAMEDLGRANRRKPKPPAP 233
Cdd:PTZ00216 187 YALRETECKAI-VCNGKNVPNLLRLMKSGGMPNTTII-----YLDSLPASVDTEGCRLVAWTDVVAKGHSAGSHHPLNIP 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 234 ED---LAVICFTSGTTGNPKGAMVTHRNIVSDCSAFV-KATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGF 309
Cdd:PTZ00216 261 ENnddLALIMYTSGTTGDPKGVMHTHGSLTAGILALEdRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGF 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 310 fqGDIRLLMD-------DLKVLQPTVFPVVPRLlnrmFDRI----------FGqantTLKRWLLDFASKRKEAELRSGii 372
Cdd:PTZ00216 341 --GSPRTLTDtfarphgDLTEFRPVFLIGVPRI----FDTIkkaveaklppVG----SLKRRVFDHAYQSRLRALKEG-- 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 373 RNNSLWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCqFYEGYGQTECTagCC--LTMPGDWTAGHVGAPM 450
Cdd:PTZ00216 409 KDTPYWNEKVFSAPRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTETV--CCggIQRTGDLEPNAVGQLL 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 451 PCNLIKLVDVEEMNYM-AAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLA 529
Cdd:PTZ00216 486 KGVEMKLLDTEEYKHTdTPEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNC 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 530 QGEYIAPEKIENIYMRSEPVAQ----VFVHgeSLQAFLIAIVVPDVETLCSWAQKRGFEGSFEELCRNKDVKKAILEDMV 605
Cdd:PTZ00216 566 LGEYIALEALEALYGQNELVVPngvcVLVH--PARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQ 643
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 557878740 606 RLGKDSGLKPFEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLY 659
Cdd:PTZ00216 644 ETARAAGRKSFEIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
232-645 |
1.80e-87 |
|
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: 281.17 E-value: 1.80e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 232 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKatenTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFfq 311
Cdd:cd17640 86 DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSD----IVPPQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY-- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 312 GDIRLLMDDLKVLQPTVFPVVPRLlnrmfdrifgqanttlkrWlldfaskrkEAeLRSGI---IRNNSLWDRLIFHKVQS 388
Cdd:cd17640 160 TSIRTLKDDLKRVKPHYIVSVPRL------------------W---------ES-LYSGIqkqVSKSSPIKQFLFLFFLS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 389 slGGRVRLMVTGAAPVSATVLTFLRaALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAA 468
Cdd:cd17640 212 --GGIFKFGISGGGALPPHVDTFFE-AIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPP 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 469 EGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEP 548
Cdd:cd17640 289 GEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPF 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 549 VAQVFVHGESlQAFLIAIVVPDVETLCSWAQKRG--FEGSFEELCRNKDVKKAI-LEDMVRLGKDSGLKPFEQVKGITLH 625
Cdd:cd17640 369 IEQIMVVGQD-QKRLGALIVPNFEELEKWAKESGvkLANDRSQLLASKKVLKLYkNEIKDEISNRPGFKSFEQIAPFALL 447
|
410 420
....*....|....*....|
gi 557878740 626 PELFsIDNGLLTPTMKAKRP 645
Cdd:cd17640 448 EEPF-IENGEMTQTMKIKRN 466
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
125-644 |
4.57e-78 |
|
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: 257.78 E-value: 4.57e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 125 QWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLLLEGVenkliPGlKIIVVMDAYGSELverg 204
Cdd:cd05932 43 EWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGKLDDWKAMAPGV-----PE-GLISISLPPPSAA---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 205 qRCGVEVTSMKAMedlGRANRRKPkPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVkateNTVNPCPDDTLIS 284
Cdd:cd05932 113 -NCQYQWDDLIAQ---HPPLEERP-TRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGI----EHIGTEENDRMLS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 285 FLPLAHMFERV-VECVMLCHGAKIgFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFgqanttlkrwlldfaSKRK 363
Cdd:cd05932 184 YLPLAHVTERVfVEGGSLYGGVLV-AFAESLDTFVEDVQRARPTLFFSVPRLWTKFQQGVQ---------------DKIP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 364 EAELRsgIIRNNSLWDRLIFHKVQSSLG-GRVRLMVTGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLTMPGDWT 442
Cdd:cd05932 248 QQKLN--LLLKIPVVNSLVKRKVLKGLGlDQCRLAGCGSAPVPPALLEWYRS-LGLNILEAYGMTENFAYSHLNYPGRDK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 443 AGHVGAPMPCNLIKLVDveemnymaaegEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRK 522
Cdd:cd05932 325 IGTVGNAGPGVEVRISE-----------DGEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 523 KHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRG-FEGSFeelcrnkdvkKAIL 601
Cdd:cd05932 394 KDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSGLPAPLALVVLSEEARLRADAFARAeLEASL----------RAHL 463
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 557878740 602 EDMvrlgkDSGLKPFEQVKGITLHPELFSIDNGLLTPTMKAKR 644
Cdd:cd05932 464 ARV-----NSTLDSHEQLAGIVVVKDPWSIDNGILTPTLKIKR 501
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
95-644 |
3.24e-67 |
|
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: 230.39 E-value: 3.24e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 95 GFQRGIQVSnngpCLGSRKPdqpyEWLsykqWV-IIEQGCFAYSMvivPLYDTLGNEAITYIVNKAELSLVFVDKPEKAK 173
Cdd:cd17641 32 GVGRGDVVA----ILGDNRP----EWV----WAeLAAQAIGALSL---GIYQDSMAEEVAYLLNYTGARVVIAEDEEQVD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 174 LLLEGVENklIPGLKIIVVMDAYGSELVERGQrcgveVTSMKAMEDLGRA-NRRKPK-------PPAPEDLAVICFTSGT 245
Cdd:cd17641 97 KLLEIADR--IPSVRYVIYCDPRGMRKYDDPR-----LISFEDVVALGRAlDRRDPGlyerevaAGKGEDVAVLCTTSGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 246 TGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVECVM-LCHGAKIGFFQgDIRLLMDDLKVL 324
Cdd:cd17641 170 TGKPKLAMLSHGNFLGHCAAYLAADPLG----PGDEYVSVLPLPWIGEQMYSVGQaLVCGFIVNFPE-EPETMMEDLREI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 325 QPTVFPVVPRLLNRM--FDRIFGQANTTLKRWLLDF--------ASKRKEAELRSGIIRNNS-LWDRLIFHKVQSSLG-G 392
Cdd:cd17641 245 GPTFVLLPPRVWEGIaaDVRARMMDATPFKRFMFELgmklglraLDRGKRGRPVSLWLRLASwLADALLFRPLRDRLGfS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 393 RVRLMVTGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVeemnymaaegeG 472
Cdd:cd17641 325 RLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEV-----------G 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 473 EVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQV 552
Cdd:cd17641 393 EILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKFSPYIAEA 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 553 FVHGESlQAFLIAIVVPDVETLCSWAQKRGFE-GSFEELCRNKDVKKAILEDMVRLGKDsgLKPFEQV-KGITLHPELfS 630
Cdd:cd17641 473 VVLGAG-RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKVNAS--LPEAQRIrRFLLLYKEL-D 548
|
570
....*....|....
gi 557878740 631 IDNGLLTPTMKAKR 644
Cdd:cd17641 549 ADDGELTRTRKVRR 562
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
237-581 |
1.11e-66 |
|
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: 225.85 E-value: 1.11e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 237 AVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVECVM-LCHGAKI----GFfq 311
Cdd:COG0318 103 ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLT----PGDVVLVALPLFHVFGLTVGLLApLLAGATLvllpRF-- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 312 gDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRifgqanttlkrwlldfaSKRKEAELRSgiirnnslwdrlifhkvqsslg 391
Cdd:COG0318 177 -DPERVLELIERERVTVLFGVPTMLARLLRH-----------------PEFARYDLSS---------------------- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 392 grVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTA--GHVGAPMPCNLIKLVDvEEMNYMAAE 469
Cdd:COG0318 217 --LRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGRPLPGVEVRIVD-EDGRELPPG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 470 GEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPV 549
Cdd:COG0318 294 EVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEVLAAHPGV 371
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 557878740 550 AQVFV-------HGESLQAFLI--AIVVPDVETLCSWAQKR 581
Cdd:COG0318 372 AEAAVvgvpdekWGERVVAFVVlrPGAELDAEELRAFLRER 412
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
125-659 |
1.50e-66 |
|
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: 229.17 E-value: 1.50e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 125 QWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLLLEgVENKLiPGLKIIVvmdAYGSELVERG 204
Cdd:cd05933 45 EWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVENQKQLQKILQ-IQDKL-PHLKAII---QYKEPLKEKE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 205 QRcgveVTSMKAMEDLGR-----ANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCPD 279
Cdd:cd05933 120 PN----LYSWDEFMELGRsipdeQLDAIISSQKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 280 DTLISFLPLAHMFERVVEcVMLC--HGAKIGFFQGDIR--LLMDDLKVLQPTVFPVVPRLLNRMFDRI--FGQANTTLKR 353
Cdd:cd05933 196 ESVVSYLPLSHIAAQILD-IWLPikVGGQVYFAQPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkaVGAKSGTLKR 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 354 WLLDFAsKRKEAE-------LRSGIIRNNSLWDRLIFHKVQSSLG-GRVRLMVTGAAPVSATVLTFLrAALGCQFYEGYG 425
Cdd:cd05933 275 KIASWA-KGVGLEtnlklmgGESPSPLFYRLAKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYG 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 426 QTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEemnymaAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTG 505
Cdd:cd05933 353 MSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSG 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 506 DIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIEN-IYMRSEPVAQVFVHGESLQaFLIAIVV----PDVET------- 573
Cdd:cd05933 427 DLGKLDEDGFLYITGRIKELIITAGGENVPPVPIEDaVKKELPIISNAMLIGDKRK-FLSMLLTlkceVNPETgepldel 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 574 ---LCSWAQKRGFEGS-FEELCRNKD--VKKAILEDMVRLGKDSGLKPfEQVKGITLHPELFSIDNGLLTPTMKAKRPEL 647
Cdd:cd05933 506 teeAIEFCRKLGSQATrVSEIAGGKDpkVYEAIEEGIKRVNKKAISNA-QKIQKWVILEKDFSVPGGELGPTMKLKRPVV 584
|
570
....*....|..
gi 557878740 648 RNYFRSQIDDLY 659
Cdd:cd05933 585 AKKYKDEIDKLY 596
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
208-637 |
5.45e-66 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 227.72 E-value: 5.45e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 208 GVEVTSMKAMEDLGRANRRKPKPPAPED---LAVICFTSGTTGNPKGAMVTHRNIVSdcsAFVKATENTVNPCPDDTLIS 284
Cdd:cd17632 194 GIPVTTLTLIAVRGRDLPPAPLFRPEPDddpLALLIYTSGSTGTPKGAMYTERLVAT---FWLKVSSIQDIRPPASITLN 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 285 FLPLAHMFERVVECVMLCHGAkIGFFQG--DIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIfgQAntTLKRWLLDFA--- 359
Cdd:cd17632 271 FMPMSHIAGRISLYGTLARGG-TAYFAAasDMSTLFDDLALVRPTELFLVPRVCDMLFQRY--QA--ELDRRSVAGAdae 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 360 --SKRKEAELRsgiirnnslwdrlifhkvQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctAGCCLTm 437
Cdd:cd17632 346 tlAERVKAELR------------------ERVLGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE--AGAVIL- 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 438 pgdwtAGHVGAPmPCNLIKLVDVEEMNYMAAEG---EGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNG 514
Cdd:cd17632 405 -----DGVIVRP-PVLDYKLVDVPELGYFRTDRphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPD 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 515 TLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRgfegsfeelcrnk 594
Cdd:cd17632 479 RLVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDALAGEDTAR------------- 545
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 557878740 595 dVKKAILEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLLT 637
Cdd:cd17632 546 -LRAALAESLQRIAREAGLQSYEIPRDFLIETEPFTIANGLLS 587
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
235-581 |
2.38e-64 |
|
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: 216.00 E-value: 2.38e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 235 DLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKI----GFF 310
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLL----AAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVvllpKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 311 QGDIRLLMDDLKVlqpTVFPVVPRLLNRMFDRIfgqanttlkrwlldfasKRKEAELRSgiirnnslwdrlifhkvqssl 390
Cdd:cd04433 77 PEAALELIEREKV---TILLGVPTLLARLLKAP-----------------ESAGYDLSS--------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 391 ggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWT--AGHVGAPMPCNLIKLVDVEEmNYMAA 468
Cdd:cd04433 116 ---LRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDPDG-GELPP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 469 EGEGEVCVKGPNVFQGYLKDPAKTAEAlDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEP 548
Cdd:cd04433 192 GEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPG 269
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 557878740 549 VAQVFVHG---ESLQAFLIAIVVP------DVETLCSWAQKR 581
Cdd:cd04433 270 VAEAAVVGvpdPEWGERVVAVVVLrpgadlDAEELRAHVRER 311
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
233-644 |
3.69e-62 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 213.84 E-value: 3.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 233 PEDLAVICFTSGTTGNPKGAMVTHRNIVSD---CSAFVKATENtvnpcpdDTLISFLPLAHMFERVVECVM-LCHGAKIG 308
Cdd:cd05914 88 EDDVALINYTSGTTGNSKGVMLTYRNIVSNvdgVKEVVLLGKG-------DKILSILPLHHIYPLTFTLLLpLLNGAHVV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 309 FFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQAN-TTLKRWLLDFASKRKEAELRSgiirnnslwdrLIFHKVQ 387
Cdd:cd05914 161 FLDKIPSAKIIALAFAQVTPTLGVPVPLVIEKIFKMDIIPkLTLKKFKFKLAKKINNRKIRK-----------LAFKKVH 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 388 SSLGGRVRLMVTGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPmpcnlIKLVDVEEMNYMA 467
Cdd:cd05914 230 EAFGGNIKEFVIGGAKINPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKV-----IDGVEVRIDSPDP 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 468 AEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSE 547
Cdd:cd05914 304 ATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMP 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 548 PVA--QVFVHGESLQAflIAIVVPDvetlcswaqkrgFEGSFEELCRNKdvKKAILEDmVRLGKDSGLKPFEQVKGITLH 625
Cdd:cd05914 384 FVLesLVVVQEKKLVA--LAYIDPD------------FLDVKALKQRNI--IDAIKWE-VRDKVNQKVPNYKKISKVKIV 446
|
410
....*....|....*....
gi 557878740 626 PELFSidnglLTPTMKAKR 644
Cdd:cd05914 447 KEEFE-----KTPKGKIKR 460
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
218-569 |
1.05e-57 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 202.02 E-value: 1.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 218 EDLGRANRRKPKPPA--PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAfVKATENTVNPcPDDTLISFLPLAHMFERV 295
Cdd:cd05936 107 TDLLAAGAPLGERVAltPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQ-IKAWLEDLLE-GDDVVLAALPLFHVFGLT 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 296 VECV-MLCHGAKIGFFQG-DIRLLMDDLKVLQPTVFPVVPRLLNRMFDrifgqanttlkrwlldfASKRKEAELRSgiir 373
Cdd:cd05936 185 VALLlPLALGATIVLIPRfRPIGVLKEIRKHRVTIFPGVPTMYIALLN-----------------APEFKKRDFSS---- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 374 nnslwdrlifhkvqsslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECT-AGCCLTMPGDWTAGHVGAPMPC 452
Cdd:cd05936 244 --------------------LRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSpVVAVNPLDGPRKPGSIGIPLPG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 453 NLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGE 532
Cdd:cd05936 304 TEVKIVD-DDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAF-VDGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGGF 380
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 557878740 533 YIAPEKIENIYMRSEPVAQVFV-------HGESLQAFliaiVVP 569
Cdd:cd05936 381 NVYPREVEEVLYEHPAVAEAAVvgvpdpySGEAVKAF----VVL 420
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
134-557 |
1.27e-57 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 203.11 E-value: 1.27e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 134 FAYSM---VIVPLYDTLGNEAITYIVNKAELSLVFVDkPEKAKLLlEGVENKLiPGLKIIVVMDAYGSElvergqRCGVE 210
Cdd:PRK06187 74 FAVPKigaVLHPINIRLKPEEIAYILNDAEDRVVLVD-SEFVPLL-AAILPQL-PTVRTVIVEGDGPAA------PLAPE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 211 VTSMKAMedLGRANRRKPKPPAPE-DLAVICFTSGTTGNPKGAMVTHRNIVSD---CSAFVKATentvnpcPDDTLISFL 286
Cdd:PRK06187 145 VGEYEEL--LAAASDTFDFPDIDEnDAAAMLYTSGTTGHPKGVVLSHRNLFLHslaVCAWLKLS-------RDDVYLVIV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 287 PLAHMFERVVECVMLCHGAKI---GFFqgDIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgQANTTLKRWLldfaskrk 363
Cdd:PRK06187 216 PMFHVHAWGLPYLALMAGAKQvipRRF--DPENLLDLIETERVTFFFAVPTIWQMLL-----KAPRAYFVDF-------- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 364 eaelrsgiirnnslwdrlifhkvqsslgGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECT-AGCCLT----MP 438
Cdd:PRK06187 281 ----------------------------SSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSpVVSVLPpedqLP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 439 GDWT-AGHVGAPMPCNLIKLVDvEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAKTAEALDkDGWLHTGDIGKWLPNGT 515
Cdd:PRK06187 333 GQWTkRRSAGRPLPGVEARIVD-DDGDELPPDGGevGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGY 410
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 557878740 516 LKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPVAQVFVHGE 557
Cdd:PRK06187 411 LYITDRIKDVIISG-GENIYPRELEDALYGHPAVAEVAVIGV 451
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
132-556 |
2.70e-56 |
|
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: 198.59 E-value: 2.70e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 132 GCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLLleGVENKLIPGLKIIVvMDAYGSELVERGQrcGVEV 211
Cdd:cd05911 54 GCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDPDGLEKVK--EAAKELGPKDKIIV-LDDKPDGVLSIED--LLSP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 212 TSMKAMEDlgranRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSaFVKATEnTVNPCPDDTLISFLPLAHM 291
Cdd:cd05911 129 TLGEEDED-----LPPPLKDGKDDTAAILYSSGTTGLPKGVCLSHRNLIANLS-QVQTFL-YGNDGSNDVILGFLPLYHI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 292 FervveCVMLCHGAKIgffQG---------DIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskr 362
Cdd:cd05911 202 Y-----GLFTTLASLL---NGatviimpkfDSELFLDLIEKYKITFLYLVPPIAAALA---------------------- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 363 keaelrsgiirNNSLWDRlifHKVQSslggrVRLMVTGAAPVSATVLTFLRAALG-CQFYEGYGQTECTAGCCLTMPGDW 441
Cdd:cd05911 252 -----------KSPLLDK---YDLSS-----LRVILSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 442 TAGHVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDR 521
Cdd:cd05911 313 KPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDR 392
|
410 420 430
....*....|....*....|....*....|....*
gi 557878740 522 KKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFVHG 556
Cdd:cd05911 393 KKELIKY-KGFQVAPAELEAVLLEHPGVADAAVIG 426
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
125-581 |
1.12e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 192.04 E-value: 1.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 125 QWVIieqGCFAYSM---VIVPLYDTLGNEAITYIVNKAELSLVFVdkpekAKLLLeGVENKL---IPGLKIIVVMDaygs 198
Cdd:PRK07656 67 HWVI---AALGALKagaVVVPLNTRYTADEAAYILARGDAKALFV-----LGLFL-GVDYSAttrLPALEHVVICE---- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 199 elVERGQRCGVEVTSMKAMedLGRANRRKPKPP-APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpc 277
Cdd:PRK07656 134 --TEEDDPHTEKMKTFTDF--LAAGDPAERAPEvDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLT---- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 278 PDDTLISFLPLAHMF---ERVVECVMlcHGAKIgffqgDIRLLMDDLKVLQ------PTVFPVVPrllnrmfdrifgqan 348
Cdd:PRK07656 206 EGDRYLAANPFFHVFgykAGVNAPLM--RGATI-----LPLPVFDPDEVFRlieterITVLPGPP--------------- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 349 tTLKRWLLDFAsKRKEAELRSgiirnnslwdrlifhkvqsslggrVRLMVTGAAPVSATVLTFLRAALGCQ-FYEGYGQT 427
Cdd:PRK07656 264 -TMYNSLLQHP-DRSAEDLSS------------------------LRLAVTGAASMPVALLERFESELGVDiVLTGYGLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 428 ECTAGCCLTMPGD---WTAGHVGAPMPCNLIKLVDveEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLH 503
Cdd:PRK07656 318 EASGVTTFNRLDDdrkTVAGTIGTAIAGVENKIVN--ELGEEVPVGEvGELLVRGPNVMKGYYDDPEATAAAIDADGWLH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 504 TGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFV-------HGESLQAFliaiVVP------D 570
Cdd:PRK07656 396 TGDLGRLDEEGYLYIVDRKKDMF-IVGGFNVYPAEVEEVLYEHPAVAEAAVigvpderLGEVGKAY----VVLkpgaelT 470
|
490
....*....|.
gi 557878740 571 VETLCSWAQKR 581
Cdd:PRK07656 471 EEELIAYCREH 481
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
235-581 |
3.51e-45 |
|
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: 167.08 E-value: 3.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 235 DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVV----------ECVMLchg 304
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWT----EDDVLLHVLPLHHVHGLVNallcplfagaSVEFL--- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 305 akiGFF---QGDIRLLMDDLkvlqpTVFPVVPRllnrMFDRIFGQANTTLKrwllDFASKRKEAElrsgiirnnslwdrl 381
Cdd:cd05941 163 ---PKFdpkEVAISRLMPSI-----TVFMGVPT----IYTRLLQYYEAHFT----DPQFARAAAA--------------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 382 ifhkvqsslgGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctAGCCLTMP--GDWTAGHVGAPMPCNLIKLVD 459
Cdd:cd05941 212 ----------ERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 460 VEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK-HIFKlAQGEYIAPEK 538
Cdd:cd05941 280 EETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALE 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 557878740 539 IENIYMRSEPVAQVFVHGESLQAF---LIAIVVP-------DVETLCSWAQKR 581
Cdd:cd05941 359 IERVLLAHPGVSECAVIGVPDPDWgerVVAVVVLragaaalSLEELKEWAKQR 411
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
198-542 |
9.65e-41 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 155.86 E-value: 9.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 198 SELVERGQRCGVEVTSMKAMEDLGRANRR------KPKPPAPE----DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFV 267
Cdd:cd05904 112 AELAEKLASLALPVVLLDSAEFDSLSFSDllfeadEAEPPVVVikqdDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFV 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 268 KATENtvNPCPDDTLISFLPLAHMFERVVECV-MLCHGAKI----GFfqgDIRLLMDDLKVLQPTVFPVVPRLLNRMfdr 342
Cdd:cd05904 192 AGEGS--NSDSEDVFLCVLPMFHIYGLSSFALgLLRLGATVvvmpRF---DLEELLAAIERYKVTHLPVVPPIVLAL--- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 343 ifgqanttlkrwlldfaskrkeaeLRSGIIRNNSLwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAAL-GCQFY 421
Cdd:cd05904 264 ------------------------VKSPIVDKYDL----------SSL----RQIMSGAAPLGKELIEAFRAKFpNVDLG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 422 EGYGQTECTAGCCLTMPGDWTAGHVG-----APMPCnlIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL 496
Cdd:cd05904 306 QGYGMTESTGVVAMCFAPEKDRAKYGsvgrlVPNVE--AKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATI 383
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 557878740 497 DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 542
Cdd:cd05904 384 DKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEAL 428
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
139-582 |
2.13e-39 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 151.72 E-value: 2.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 139 VIVPLYDTLGNEAITYIVNKAELSLVFVDKP--EKAKLL-------------LEGVENKLIPGLKIIVVMDAYgselver 203
Cdd:cd05909 57 VPVMLNYTAGLRELRACIKLAGIKTVLTSKQfiEKLKLHhlfdveydarivyLEDLRAKISKADKCKAFLAGK------- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 204 gqrcgveVTSMKAMEDLGRANRRkpkppaPEDLAVICFTSGTTGNPKGAMVTHRNIVSDcsafVKATENTVNPCPDDTLI 283
Cdd:cd05909 130 -------FPPKWLLRIFGVAPVQ------PDDPAVILFTSGSEGLPKGVVLSHKNLLAN----VEQITAIFDPNPEDVVF 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 284 SFLPLAHMFervvecvmlchgakiGFFQGDIRLLMDDLKVLQ---PTVFPVVPRLLNRMFDRIFGQANTTLKRWLldfas 360
Cdd:cd05909 193 GALPFFHSF---------------GLTGCLWLPLLSGIKVVFhpnPLDYKKIPELIYDKKATILLGTPTFLRGYA----- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 361 KRKEAELRSGIirnnslwdrlifhkvqsslggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPG- 439
Cdd:cd05909 253 RAAHPEDFSSL-----------------------RLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQs 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 440 DWTAGHVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKII 519
Cdd:cd05909 310 PNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTIT 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557878740 520 DRKKHIFKLAqGEYIAPEKIENIYMRSEP----VAQVFV----HGESLQAFLIAIvVPDVETLCSWAQKRG 582
Cdd:cd05909 389 GRLSRFAKIA-GEMVSLEAIEDILSEILPedneVAVVSVpdgrKGEKIVLLTTTT-DTDPSSLNDILKNAG 457
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
234-570 |
1.08e-38 |
|
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: 148.53 E-value: 1.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 234 EDLAVICFTSGTTGNPKGAMVTHRNIvsdcsafvkaTENTVN------PCPDDTLISFLPLAHMFERVVECVM-LCHGAK 306
Cdd:cd17631 98 DDLALLMYTSGTTGRPKGAMLTHRNL----------LWNAVNalaaldLGPDDVLLVVAPLFHIGGLGVFTLPtLLRGGT 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 307 I----GFfqgDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRifGQANTTlkrwllDFASkrkeaelrsgiirnnslwdrli 382
Cdd:cd17631 168 VvilrKF---DPETVLDLIERHRVTSFFLVPTMIQALLQH--PRFATT------DLSS---------------------- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 383 fhkvqsslggrVRLMVTGAAPVSATVLTFLRAAlGCQFYEGYGQTECTAGCCLTMPGDW--TAGHVGAPMPCNLIKLVDv 460
Cdd:cd17631 215 -----------LRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHrrKLGSAGRPVFFVEVRIVD- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 461 EEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIE 540
Cdd:cd17631 282 PDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVE 359
|
330 340 350
....*....|....*....|....*....|....*..
gi 557878740 541 NIYMRSEPVAQVFV-------HGESlqafLIAIVVPD 570
Cdd:cd17631 360 DVLYEHPAVAEVAVigvpdekWGEA----VVAVVVPR 392
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
233-657 |
1.29e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 152.57 E-value: 1.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 233 PEDLAVICFTSGTTGNPKGAMVTHRNI------VSDCSAFVKatentVNPcpdDTLISFLPLAHMFERVVECVMLCHGAK 306
Cdd:PTZ00342 303 PDFITSIVYTSGTSGKPKGVMLSNKNLyntvvpLCKHSIFKK-----YNP---KTHLSYLPISHIYERVIAYLSFMLGGT 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 307 IGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQAN--TTLKRWLLdfaskRKEAELRSGiiRNNSLWDRL--- 381
Cdd:PTZ00342 375 INIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINnlPPLKRFLV-----KKILSLRKS--NNNGGFSKFleg 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 382 IFH---KVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPM-PCNLIKL 457
Cdd:PTZ00342 448 ITHissKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTGPIFVQHADDNNTESIGGPIsPNTKYKV 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 458 VDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPE 537
Cdd:PTZ00342 528 RTWETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETD 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 538 KIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRGF-------EGSFEELCRNKDVKKAILEDMVR---- 606
Cdd:PTZ00342 608 MLNNLYSQISFINFCVVYGDDSMDGPLAIISVDKYLLFKCLKDDNMlestginEKNYLEKLTDETINNNIYVDYVKgkml 687
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 557878740 607 -LGKDSGLKPFEQVKGITLHPELFSIDNgLLTPTMKAKRPELRNYFRSQIDD 657
Cdd:PTZ00342 688 eVYKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKRFYVFKDYAFFIDQ 738
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
220-574 |
2.44e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 149.91 E-value: 2.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 220 LGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSD---CSAFVKAteNTVNPCpdDTLISFLPLAHMFERVV 296
Cdd:PRK05677 193 KGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANmlqCRALMGS--NLNEGC--EILIAPLPLYHIYAFTF 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 297 ECVMLchgakigffqgdirLLMDDLKVLQPTvfpvvPRLLNRMFdrifgqanTTLKRWLLdfaskrkeaelrSGIIRNNS 376
Cdd:PRK05677 269 HCMAM--------------MLIGNHNILISN-----PRDLPAMV--------KELGKWKF------------SGFVGLNT 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 377 LWDRLI----FHKVQSSlggRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPC 452
Cdd:PRK05677 310 LFVALCnneaFRKLDFS---ALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPS 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 453 NLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGE 532
Cdd:PRK05677 387 TLCKVID-DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVSGF 464
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 557878740 533 YIAPEKIENIYMRSEPVAQVFV-------HGESLQAFliaIVVPDVETL 574
Cdd:PRK05677 465 NVYPNELEDVLAALPGVLQCAAigvpdekSGEAIKVF---VVVKPGETL 510
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
233-565 |
1.61e-37 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 147.51 E-value: 1.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 233 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPcPDDTLISFLPLAHMFERVVECVMLCH-GAKigffq 311
Cdd:PRK08974 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGPLLHP-GKELVVTALPLYHIFALTVNCLLFIElGGQ----- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 312 gdirllmdDLKVLQPTVFP-VVPRLLNRMFDRIFGqANTTLKRWLldfaskrkeaelrsgiirNNSLwdrliFHKVQSSl 390
Cdd:PRK08974 279 --------NLLITNPRDIPgFVKELKKYPFTAITG-VNTLFNALL------------------NNEE-----FQELDFS- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 391 ggRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECT---AGCcltmPGDWT--AGHVGAPMPCNLIKLVDvEEMNY 465
Cdd:PRK08974 326 --SLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVN----PYDLDyySGSIGLPVPSTEIKLVD-DDGNE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 466 MAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMR 545
Cdd:PRK08974 399 VPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMI-LVSGFNVYPNEIEDVVML 476
|
330 340
....*....|....*....|....*..
gi 557878740 546 SEPVAQVF-------VHGESLQAFLIA 565
Cdd:PRK08974 477 HPKVLEVAavgvpseVSGEAVKIFVVK 503
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
233-594 |
1.34e-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: 140.49 E-value: 1.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 233 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDcSAFV----KATENTVNPCPddtlisfLPLAHMFERVVEcVMLC--HGAK 306
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNN-GYFIgerlGLTEQDRLCIP-------VPLFHCFGSVLG-VLACltHGAT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 307 IGFfqgdIRLLMDDLKVLQP------TVFPVVPRllnrMFDRIFGQAnttlKRWLLDFASkrkeaeLRSGIIrnnslwdr 380
Cdd:cd05917 72 MVF----PSPSFDPLAVLEAiekekcTALHGVPT----MFIAELEHP----DFDKFDLSS------LRTGIM-------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 381 lifhkvqsslggrvrlmvtGAAPVSATVLTFLRAALGC-QFYEGYGQTECTAGCCLTMPGDWT---AGHVGAPMPCNLIK 456
Cdd:cd05917 126 -------------------AGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDSIekrVNTVGRIMPHTEAK 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 457 LVDvEEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIA 535
Cdd:cd05917 187 IVD-PEGGIVPPVGVpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGENIY 264
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 557878740 536 PEKIENIYMRSEPVAQVFVHGeslqafliaivVPDV---ETLCSWAQ-KRGFEGSFEEL---CRNK 594
Cdd:cd05917 265 PREIEEFLHTHPKVSDVQVVG-----------VPDErygEEVCAWIRlKEGAELTEEDIkayCKGK 319
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
223-581 |
1.89e-36 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 143.22 E-value: 1.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 223 ANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDcsafVKATENTVNPCPDDTLISFLPLAHMFERVVECV-ML 301
Cdd:cd05926 138 KNAKSEGVPLPDDLALILHTSGTTGRPKGVPLTHRNLAAS----ATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLsTL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 302 CHGAKI----GFfqgDIRLLMDDLKVLQPTVFPVVPrllnrmfdrifgqantTLKRWLLDFASKRKEAELrsgiirnnsl 377
Cdd:cd05926 214 AAGGSVvlppRF---SASTFWPDVRDYNATWYTAVP----------------TIHQILLNRPEPNPESPP---------- 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 378 wdrlifhkvqsslgGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAgcclTM------PGDWTAGHVGAPMP 451
Cdd:cd05926 265 --------------PKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAH----QMtsnplpPGPRKPGSVGKPVG 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 452 cNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqG 531
Cdd:cd05926 327 -VEVRILD-EDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-G 403
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557878740 532 EYIAPEKIENIYMRSEPVAQ--VF-----VHGESLQAFliaiVVP------DVETLCSWAQKR 581
Cdd:cd05926 404 EKISPLEVDGVLLSHPAVLEavAFgvpdeKYGEEVAAA----VVLregasvTEEELRAFCRKH 462
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
235-581 |
4.98e-36 |
|
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: 138.40 E-value: 4.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 235 DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVECVM-LCHGAKI---GFF 310
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLT----EDDRYLIINPFFHTFGYKAGIVAcLLTGATVvpvAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 311 qgDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRifgqanttlkrwlldfaSKRKEAELrsgiirnnslwdrlifhkvqSSL 390
Cdd:cd17638 77 --DVDAILEAIERERITVLPGPPTLFQSLLDH-----------------PGRKKFDL--------------------SSL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 391 ggrvRLMVTGAAPVSATVLTFLRAALGCQ-FYEGYGQTECTagcCLTM--PGD---WTAGHVGAPMPcnliklvDVEemn 464
Cdd:cd17638 118 ----RAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAG---VATMcrPGDdaeTVATTCGRACP-------GFE--- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 465 yMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYM 544
Cdd:cd17638 181 -VRIADDGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGALA 258
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 557878740 545 RSEPVAQVFV-------HGESLQAFLIA--IVVPDVETLCSWAQKR 581
Cdd:cd17638 259 EHPGVAQVAVigvpderMGEVGKAFVVArpGVTLTEEDVIAWCRER 304
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
220-525 |
7.42e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 142.83 E-value: 7.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 220 LGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCS---AFVKATentvnPCPDDTLISFLPLAHMF--ER 294
Cdd:PRK05605 205 GGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqgkAWVPGL-----GDGPERVLAALPMFHAYglTL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 295 VVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLlnrmFDRIfgqanttlkrwlldfaskRKEAELRsGIirn 374
Cdd:PRK05605 280 CLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPL----YEKI------------------AEAAEER-GV--- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 375 nslwdrlifhkvqsSLGGrVRLMVTGAA--PVSaTVLTFlRAALGCQFYEGYGQTECTA-GCCLTMPGDWTAGHVGAPMP 451
Cdd:PRK05605 334 --------------DLSG-VRNAFSGAMalPVS-TVELW-EKLTGGLLVEGYGLTETSPiIVGNPMSDDRRPGYVGVPFP 396
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 557878740 452 CNLIKLVDVEEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHI 525
Cdd:PRK05605 397 DTEVRIVDPEDPDETMPDGEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKEL 470
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
213-565 |
8.04e-35 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 139.57 E-value: 8.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 213 SMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSD------CSAFVKATENTVNPCPDDTLISFL 286
Cdd:PRK12492 186 PFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANmlqvraCLSQLGPDGQPLMKEGQEVMIAPL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 287 PLAHMFERVVECVMLchgakigFFQGDIRLLMDDlkvlqptvfpvvPRLLNRMFDRifgqanttLKRWLLdfaskrkeae 366
Cdd:PRK12492 266 PLYHIYAFTANCMCM-------MVSGNHNVLITN------------PRDIPGFIKE--------LGKWRF---------- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 367 lrSGIIRNNSLWDRLIFHKVQSSLGGRvRLMVT---GAAPVSATVLTFlRAALGCQFYEGYGQTECTAGCCLTMPGDWTA 443
Cdd:PRK12492 309 --SALLGLNTLFVALMDHPGFKDLDFS-ALKLTnsgGTALVKATAERW-EQLTGCTIVEGYGLTETSPVASTNPYGELAR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 444 -GHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRK 522
Cdd:PRK12492 385 lGTVGIPVPGTALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRK 463
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 557878740 523 KHIFkLAQGEYIAPEKIENIYMRSEPVAQVFV-------HGESLQAFLIA 565
Cdd:PRK12492 464 KDLI-IVSGFNVYPNEIEDVVMAHPKVANCAAigvpderSGEAVKLFVVA 512
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
147-556 |
1.10e-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: 138.53 E-value: 1.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 147 LGNEAITYIVNKAELSLVFVDkPEKAKLLlEGVENKLiPGLKIIVVMDAYGSELVERGQRCGvevtsmkAMEDL-GRANR 225
Cdd:cd12119 84 LFPEQIAYIINHAEDRVVFVD-RDFLPLL-EAIAPRL-PTVEHVVVMTDDAAMPEPAGVGVL-------AYEELlAAESP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 226 RKPKPPAPE-DLAVICFTSGTTGNPKGAMVTHRNIVSdcSAFVKATENTVNPCPDDTlisFLPLAHMFErvVE------- 297
Cdd:cd12119 154 EYDWPDFDEnTAAAICYTSGTTGNPKGVVYSHRSLVL--HAMAALLTDGLGLSESDV---VLPVVPMFH--VNawglpya 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 298 CVMLchGAKI----GFFQGDIRL-LMDDLKVlqpTVFPVVPRLLNRMFDRifgqanttLKRWLLDFASKRkeaelrsgii 372
Cdd:cd12119 227 AAMV--GAKLvlpgPYLDPASLAeLIEREGV---TFAAGVPTVWQGLLDH--------LEANGRDLSSLR---------- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 373 rnnslwdrlifhkvqsslggrvRLMVTGAAPVSATVLTFlrAALGCQFYEGYGQTE-CTAGCCLTMPGDWTAGHV----- 446
Cdd:cd12119 284 ----------------------RVVIGGSAVPRSLIEAF--EERGVRVIHAWGMTEtSPLGTVARPPSEHSNLSEdeqla 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 447 -----GAPMPCNLIKLVDvEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAkTAEALDKDGWLHTGDIGKWLPNGTLKII 519
Cdd:cd12119 340 lrakqGRPVPGVELRIVD-DDGRELPWDGKavGELQVRGPWVTKSYYKNDE-ESEALTEDGWLRTGDVATIDEDGYLTIT 417
|
410 420 430
....*....|....*....|....*....|....*..
gi 557878740 520 DRKKHIFKLAqGEYIAPEKIENIYMRSEPVAQVFVHG 556
Cdd:cd12119 418 DRSKDVIKSG-GEWISSVELENAIMAHPAVAEAAVIG 453
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
140-542 |
1.37e-34 |
|
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: 138.43 E-value: 1.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 140 IVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLLleGVENKLiPGLKIIVVMDaygSELVERGQRCgveVTSMKAMED 219
Cdd:cd17642 96 VAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVL--NVQKKL-KIIKTIIILD---SKEDYKGYQC---LYTFITQNL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 220 LGRANRRKPKPPA---PEDLAVICFTSGTTGNPKGAMVTHRNIvsdCSAFVKATENTV--NPCPDDTLISFLPLAHMFER 294
Cdd:cd17642 167 PPGFNEYDFKPPSfdrDEQVALIMNSSGSTGLPKGVQLTHKNI---VARFSHARDPIFgnQIIPDTAILTVIPFHHGFGM 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 295 VVECVMLCHGAKIGF---FQGDIRL-LMDDLKV----LQPTVFPVVPRllnrmfdrifgqanttlkrwlldfaskrkeae 366
Cdd:cd17642 244 FTTLGYLICGFRVVLmykFEEELFLrSLQDYKVqsalLVPTLFAFFAK-------------------------------- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 367 lrSGIIRNNSLwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFY-EGYGQTECTAGCCLTMPGDWTAGH 445
Cdd:cd17642 292 --STLVDKYDL----------SNL----HEIASGGAPLSKEVGEAVAKRFKLPGIrQGYGLTETTSAILITPEGDDKPGA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 446 VGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHI 525
Cdd:cd17642 356 VGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSL 435
|
410
....*....|....*..
gi 557878740 526 FKLaQGEYIAPEKIENI 542
Cdd:cd17642 436 IKY-KGYQVPPAELESI 451
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
220-649 |
4.21e-34 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 137.32 E-value: 4.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 220 LGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSD---CSAFVKATENTVNPCpdDTLISFLPLAHMFERVV 296
Cdd:PRK08751 194 LGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANmqqAHQWLAGTGKLEEGC--EVVITALPLYHIFALTA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 297 ECVMLchgAKIGFFQG------DIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeaelrsg 370
Cdd:PRK08751 272 NGLVF---MKIGGCNHlisnprDMPGFVKELKKTRFTAFTGVNTLFNGLL------------------------------ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 371 iirNNSLWDRLIFHKVQSSLGGrvrlmvtGAApVSATVLTFLRAALGCQFYEGYGQTECTAGCCLT-MPGDWTAGHVGAP 449
Cdd:PRK08751 319 ---NTPGFDQIDFSSLKMTLGG-------GMA-VQRSVAERWKQVTGLTLVEAYGLTETSPAACINpLTLKEYNGSIGLP 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 450 MPCNLIKLVDveEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkL 528
Cdd:PRK08751 388 IPSTDACIKD--DAGTVLAIGEiGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-L 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 529 AQGEYIAPEKIENIYMRSEPVAQVfvhgeslqaflIAIVVPDvetlcswaQKRGfegsfeELCRNKDVKK--AILEDMVR 606
Cdd:PRK08751 465 VSGFNVYPNEIEDVIAMMPGVLEV-----------AAVGVPD--------EKSG------EIVKVVIVKKdpALTAEDVK 519
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 557878740 607 LGKDSGLKPFEQVKGITLHPELFSIDNGlltptmKAKRPELRN 649
Cdd:PRK08751 520 AHARANLTGYKQPRIIEFRKELPKTNVG------KILRRELRD 556
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
234-581 |
4.90e-34 |
|
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: 135.27 E-value: 4.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 234 EDLAVICFTSGTTGNPKGAMVTHRNIvsdcSAFVKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGD 313
Cdd:TIGR01923 111 DQIATLMFTSGTTGKPKAVPHTFRNH----YASAVGSKENLGFTEDDNWLLSLPLYHISGLSILFRWLIEGATLRIVDKF 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 314 IRLLmDDLKVLQPTVFPVVPRLLNRMFDRifGQANTTLKRWLLdfaskrkeaelrsgiirnnslwdrlifhkvqsslggr 393
Cdd:TIGR01923 187 NQLL-EMIANERVTHISLVPTQLNRLLDE--GGHNENLRKILL------------------------------------- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 394 vrlmvtGAAPVSATVLTFLRAaLGCQFYEGYGQTE-CTAGCCLTMPGDWTAGHVGAPMPCNLIKL-VDveemnymAAEGE 471
Cdd:TIGR01923 227 ------GGSAIPAPLIEEAQQ-YGLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIkVD-------NKEGH 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 472 GEVCVKGPNVFQGYLkDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQ 551
Cdd:TIGR01923 293 GEIMVKGANLMKGYL-YQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQE 370
|
330 340 350
....*....|....*....|....*....|....*..
gi 557878740 552 VFV-------HGESLQAFLIAIVVPDVETLCSWAQKR 581
Cdd:TIGR01923 371 AVVvpkpdaeWGQVPVAYIVSESDISQAKLIAYLTEK 407
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
221-603 |
1.49e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 134.35 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 221 GRANRRKPKPPaPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMfervvecvm 300
Cdd:PRK07787 116 ARSWHRYPEPD-PDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWT----ADDVLVHGLPLFHV--------- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 301 lcHGAKIGffqgdirllmddlkVLQPTvfpvvprllnrmfdRIFGQANTTLKrwlldFASKRKEAELRSGiirnNSL--- 377
Cdd:PRK07787 182 --HGLVLG--------------VLGPL--------------RIGNRFVHTGR-----PTPEAYAQALSEG----GTLyfg 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 378 ----WDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCN 453
Cdd:PRK07787 223 vptvWSRIAADPEAARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 454 LIKLVDvEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDR------KKHI 525
Cdd:PRK07787 303 ETRLVD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGG 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 526 FKLAQGEyiapekIENIYMRSEPVAQVFVHGE---SLQAFLIAIVVPD-----------VETLCSwAQKRGFEGSF-EEL 590
Cdd:PRK07787 382 YRIGAGE------IETALLGHPGVREAAVVGVpddDLGQRIVAYVVGAddvaadelidfVAQQLS-VHKRPREVRFvDAL 454
|
410
....*....|....*.
gi 557878740 591 CRN---KDVKKAILED 603
Cdd:PRK07787 455 PRNamgKVLKKQLLSE 470
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
232-540 |
7.91e-33 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 133.18 E-value: 7.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 232 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCPDDTLISFLPLAHMFErvVECVMLCH---GAKIG 308
Cdd:PLN02246 177 SPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYFHSDDVILCVLPMFHIYS--LNSVLLCGlrvGAAIL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 309 FFQG-DIRLLMDDLKVLQPTVFPVVPRLLnrmfdrifgqanttlkrwlLDFAskrkeaelRSGIIRNNSLwdrlifhkvq 387
Cdd:PLN02246 255 IMPKfEIGALLELIQRHKVTIAPFVPPIV-------------------LAIA--------KSPVVEKYDL---------- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 388 SSlggrVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTEctAGCCLTM-------PGDWTAGHVGAPMPCNLIKLVD 459
Cdd:PLN02246 298 SS----IRMVLSGAAPLGKELEDAFRAKLpNAVLGQGYGMTE--AGPVLAMclafakePFPVKSGSCGTVVRNAELKIVD 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 460 VEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKI 539
Cdd:PLN02246 372 PETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAEL 450
|
.
gi 557878740 540 E 540
Cdd:PLN02246 451 E 451
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
232-573 |
1.10e-32 |
|
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: 131.11 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 232 APEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATENTVNPCPDDTLISFLPLAH-MFerVVE-CVMLCHGAKI-- 307
Cdd:cd05930 91 DPDDLAYVIYTSGSTGKPKGVMVEHRGLVN----LLLWMQEAYPLTPGDRVLQFTSFSFdVS--VWEiFGALLAGATLvv 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 308 --GFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQANTTLKRwlldfaskrkeaelrsgiirnnslwdrlifhk 385
Cdd:cd05930 165 lpEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAALPSLRL-------------------------------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 386 vqsslggrvrLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLT--MPGDWTAGHV--GAPMPCNLIKLVDvE 461
Cdd:cd05930 213 ----------VLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYrvPPDDEEDGRVpiGRPIPNTRVYVLD-E 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 462 EMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEA-----LDKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIA 535
Cdd:cd05930 282 NLRPVPPGVPGELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIE 360
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 557878740 536 PEKIENIYMRSEPVAQVFV---HGESLQAFLIAIVVPDVET 573
Cdd:cd05930 361 LGEIEAALLAHPGVREAAVvarEDGDGEKRLVAYVVPDEGG 401
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
186-554 |
2.16e-32 |
|
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: 129.69 E-value: 2.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 186 GLKIIVVMDAYGSELVERGQRCGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSA 265
Cdd:TIGR01733 72 GARLLLTDSALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAW 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 266 FVKATENTvnpcPDDTLISFLPLAHMFervveCVM-----LCHGAK--------IGFFQGDIRLLMDDLKVlqpTVFPVV 332
Cdd:TIGR01733 152 LARRYGLD----PDDRVLQFASLSFDA-----SVEeifgaLLAGATlvvppedeERDDAALLAALIAEHPV---TVLNLT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 333 PrllnrmfdrifgqanttlkrwlldfaskrkeaelrsgiirnnSLWDRLIFHKVQSSLGgrVRLMVTGA-APVSATVLTF 411
Cdd:TIGR01733 220 P------------------------------------------SLLALLAAALPPALAS--LRLVILGGeALTPALVDRW 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 412 LRAALGCQFYEGYGQTECTAGCCLT-----MPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYL 486
Cdd:TIGR01733 256 RARGPGARLINLYGPTETTVWSTATlvdpdDAPRESPVPIGRPLANTRLYVLD-DDLRPVPVGVVGELYIGGPGVARGYL 334
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 557878740 487 KDPAKTAE--------ALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFV 554
Cdd:TIGR01733 335 NRPELTAErfvpdpfaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAALLRHPGVREAVV 409
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
235-574 |
1.37e-31 |
|
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: 127.79 E-value: 1.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 235 DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVEC-VMLCHGAKI------ 307
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLG----EDDVYLTVLPLFHINAQAVSVlAALSVGATLvllprf 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 308 --GFFQGDIRllmddlkVLQPTVF---PVVPRLLNRMFDRIFGQANttlkrwlldfaskrkeaelrsgiirnnslwdrli 382
Cdd:cd05934 158 saSRFWSDVR-------RYGATVTnylGAMLSYLLAQPPSPDDRAH---------------------------------- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 383 fhkvqsslggRVRLmVTGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEE 462
Cdd:cd05934 197 ----------RLRA-AYGAPNPPELHEEFEER-FGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVD-DD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 463 MNYMAAEGEGEVCVK---GPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKI 539
Cdd:cd05934 264 GQELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEV 341
|
330 340 350
....*....|....*....|....*....|....*....
gi 557878740 540 ENIYMRSEPVAQVFVHG----ESLQAFLIAIVVPDVETL 574
Cdd:cd05934 342 ERAILRHPAVREAAVVAvpdeVGEDEVKAVVVLRPGETL 380
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
230-581 |
2.08e-31 |
|
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: 127.43 E-value: 2.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 230 PPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATENTVNPCPDDTLISFLPLAhmFERVVECVM--LCHGAKI 307
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLN----YVSQPPARLDVGPGSRVAQVLSIA--FDACIGEIFstLCNGGTL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 308 gFFQGDIRLLMDDLKVLqpTVFPVVPRLLnrmfdrifgqanTTLKRWLLDfaskrkeaelrsgiirnnslwdrlifhkvq 387
Cdd:cd17653 175 -VLADPSDPFAHVARTV--DALMSTPSIL------------STLSPQDFP------------------------------ 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 388 sslggRVRLMVTGAAPVSATVLTflRAALGCQFYEGYGQTECTAGCCLT--MPGDWTagHVGAPMPCNLIKLVDVEEMNY 465
Cdd:cd17653 210 -----NLKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTelLPGQPV--TIGKPIPNSTCYILDADLQPV 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 466 MAAEgEGEVCVKGPNVFQGYLKDPAKTAEAL----DKDGWLH--TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKI 539
Cdd:cd17653 281 PEGV-VGEICISGVQVARGYLGNPALTASKFvpdpFWPGSRMyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEI 358
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 557878740 540 ENIYMRSEPVAQ---VFVHGEslqaFLIAIVVP---DVETLCSWAQKR 581
Cdd:cd17653 359 EEVVLQSQPEVTqaaAIVVNG----RLVAFVTPetvDVDGLRSELAKH 402
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
230-523 |
3.24e-31 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 128.07 E-value: 3.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 230 PPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAH---MFerVVECVMLCHGAK 306
Cdd:PRK07514 152 PRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFT----PDDVLIHALPIFHthgLF--VATNVALLAGAS 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 307 IGFFQG-DIRLLMDDLKvlQPTVFPVVP----RLL-NRMFDRifgqanttlkrwlldfaskrkeaelrsgiirnnslwdr 380
Cdd:PRK07514 226 MIFLPKfDPDAVLALMP--RATVMMGVPtfytRLLqEPRLTR-------------------------------------- 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 381 lifhkvqsSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctaGCCLTM-P--GDWTAGHVGAPMPCNLIKL 457
Cdd:PRK07514 266 --------EAAAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTE---TNMNTSnPydGERRAGTVGFPLPGVSLRV 334
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 557878740 458 VDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK 523
Cdd:PRK07514 335 TDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGK 400
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
221-564 |
1.97e-30 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 126.29 E-value: 1.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 221 GRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDC--------SAFVKatentvnPCPDDTLISF--LPLAH 290
Cdd:PRK07059 191 GARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqmeawlqPAFEK-------KPRPDQLNFVcaLPLYH 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 291 MFERVVECVMlchGAKIGffqG---------DIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfask 361
Cdd:PRK07059 264 IFALTVCGLL---GMRTG---GrnilipnprDIPGFIKELKKYQVHIFPAVNTLYNALL--------------------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 362 rkeaelrsgiirNNSLWDRLIFHKVQSSLGGrvrlmvtGAApVSATVLTFLRAALGCQFYEGYG--QTECTAGCCLTMPG 439
Cdd:PRK07059 317 ------------NNPDFDKLDFSKLIVANGG-------GMA-VQRPVAERWLEMTGCPITEGYGlsETSPVATCNPVDAT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 440 DWTaGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKII 519
Cdd:PRK07059 377 EFS-GTIGLPLPSTEVSIRD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIV 454
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 557878740 520 DRKKHIFkLAQGEYIAPEKIENIyMRSEP----VAQVFVH----GESLQAFLI 564
Cdd:PRK07059 455 DRKKDMI-LVSGFNVYPNEIEEV-VASHPgvleVAAVGVPdehsGEAVKLFVV 505
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
139-570 |
1.37e-29 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 125.42 E-value: 1.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 139 VIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLLLEGVENKLIPGLKIIVVMDaygseLVERgqrcgveVTSMKAME 218
Cdd:PRK08633 691 VPVNLNYTASEAALKSAIEQAQIKTVITSRKFLEKLKNKGFDLELPENVKVIYLED-----LKAK-------ISKVDKLT 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 219 DLGRA--------NRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDcsafVKATENTVNPCPDDTLISFLPLAH 290
Cdd:PRK08633 759 ALLAArllparllKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSN----IEQISDVFNLRNDDVILSSLPFFH 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 291 MFERVVECVM-LCHGAKIGFFQGDirllMDDLKVLQ-------------PTVFpvvprllnRMFDRifgqaNTTLKRwlL 356
Cdd:PRK08633 835 SFGLTVTLWLpLLEGIKVVYHPDP----TDALGIAKlvakhratillgtPTFL--------RLYLR-----NKKLHP--L 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 357 DFASkrkeaelrsgiirnnslwdrlifhkvqsslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLT 436
Cdd:PRK08633 896 MFAS---------------------------------LRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVN 942
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 437 MP-----GDWT-----AGHVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL---DKDGWLH 503
Cdd:PRK08633 943 LPdvlaaDFKRqtgskEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYV 1022
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557878740 504 TGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEniymrsEPVAQVFvHGESLQafLIAIVVPD 570
Cdd:PRK08633 1023 TGDKGHLDEDGFLTITDRYSRFAKIG-GEMVPLGAVE------EELAKAL-GGEEVV--FAVTAVPD 1079
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
235-554 |
6.66e-29 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 121.62 E-value: 6.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 235 DLAVICFTSGTTGNPKGAMVTHRNIVSD-CSAFVKATENTVNPCpddTLISFLPLAHMFERVVEC--VMLCHGAKIGFFQ 311
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTHRNLVANlCSSLFSVGPEMIGQV---VTLGLIPFFHIYGITGICcaTLRNKGKVVVMSR 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 312 GDIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeaelrsgiirNNSLWDRLIFHKVqsslg 391
Cdd:PLN02330 262 FELRTFLNALITQEVSFAPIVPPIILNLV---------------------------------KNPIVEEFDLSKL----- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 392 gRVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTagcCLTMP-GDWTAGH-------VGAPMPCNLIKLVDVEE 462
Cdd:PLN02330 304 -KLQAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEHS---CITLThGDPEKGHgiakknsVGFILPNLEVKFIDPDT 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 463 MNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 542
Cdd:PLN02330 380 GRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAI 458
|
330
....*....|..
gi 557878740 543 YMRSEPVAQVFV 554
Cdd:PLN02330 459 LLTHPSVEDAAV 470
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
239-594 |
1.70e-28 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 120.30 E-value: 1.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 239 ICFTSGTTGNPKGAMVTHRNIVSDcSAFVkaTENtVNPCPDDTLISFLPLAHMFErvveCVM-----LCHGAKI-----G 308
Cdd:PRK08315 204 IQYTSGTTGFPKGATLTHRNILNN-GYFI--GEA-MKLTEEDRLCIPVPLYHCFG----MVLgnlacVTHGATMvypgeG 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 309 FfqgdirllmDDLKVLQ-------------PTVFpvVPRLLNRMFDRifgqanttlkrwlLDFASkrkeaeLRSGI---- 371
Cdd:PRK08315 276 F---------DPLATLAaveeerctalygvPTMF--IAELDHPDFAR-------------FDLSS------LRTGImags 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 372 ---IRnnslwdrlIFHKVQSSLGgrvrlM--VTGAapvsatvltflraalgcqfyegYGQTECTAGCCLTMPGD------ 440
Cdd:PRK08315 326 pcpIE--------VMKRVIDKMH-----MseVTIA----------------------YGMTETSPVSTQTRTDDplekrv 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 441 WTaghVGAPMPCNLIKLVDvEEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKII 519
Cdd:PRK08315 371 TT---VGRALPHLEVKIVD-PETGETVPRGEqGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIV 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 520 DRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHGeslqafliaivVPDV---ETLCSWAQKR-GFEGSFEEL---CR 592
Cdd:PRK08315 447 GRIKDMI-IRGGENIYPREIEEFLYTHPKIQDVQVVG-----------VPDEkygEEVCAWIILRpGATLTEEDVrdfCR 514
|
..
gi 557878740 593 NK 594
Cdd:PRK08315 515 GK 516
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
139-541 |
1.89e-28 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 119.08 E-value: 1.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 139 VIVPLYDTLGNEAITYIVNKAELSLVFVDKPekaklllegvenklipglkiivvmdaYGSELVERGQRCGVEVTSMKAME 218
Cdd:cd05922 48 VFVPLNPTLKESVLRYLVADAGGRIVLADAG--------------------------AADRLRDALPASPDPGTVLDADG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 219 DLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVEC 298
Cdd:cd05922 102 IRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGIT----ADDRALTVLPLSYDYGLSVLN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 299 VMLCHGAKIgFFQGDIRL---LMDDLKVLQPTVFPVVPRLLNrMFDRIfgqanttlkrwlldfasKRKEAELrsgiirnN 375
Cdd:cd05922 178 THLLRGATL-VLTNDGVLddaFWEDLREHGATGLAGVPSTYA-MLTRL-----------------GFDPAKL-------P 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 376 SLwdRLIfhkvqSSLGGRVRlmvtgaapvSATVLTFLRAALGCQFYEGYGQTECTAGCClTMPGDWTA---GHVGAPMPC 452
Cdd:cd05922 232 SL--RYL-----TQAGGRLP---------QETIARLRELLPGAQVYVMYGQTEATRRMT-YLPPERILekpGSIGLAIPG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 453 NLIKLVDVEEMNYmaAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqG 531
Cdd:cd05922 295 GEFEILDDDGTPT--PPGEpGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF-G 371
|
410
....*....|
gi 557878740 532 EYIAPEKIEN 541
Cdd:cd05922 372 NRISPTEIEA 381
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
125-544 |
2.16e-28 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 119.85 E-value: 2.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 125 QWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAElSLVF-----VDKPEKAKLLLEGVENklIPGLKIIVVMDAYGSE 199
Cdd:PRK06087 86 EFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQ-AKMFfaptlFKQTRPVDLILPLQNQ--LPQLQQIVGVDKLAPA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 200 LVErgqrcgveVTSMKAMEDLGRANrrKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPD 279
Cdd:PRK06087 163 TSS--------LSLSQIIADYEPLT--TAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLT----WQ 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 280 DTLISFLPLAHmfervvecvmlchgaKIGFFQGDIR-LLMDDLKVLQPTVFPVVP-RLLNRmfDRIFGQANTTlkRWLLD 357
Cdd:PRK06087 229 DVFMMPAPLGH---------------ATGFLHGVTApFLIGARSVLLDIFTPDAClALLEQ--QRCTCMLGAT--PFIYD 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 358 FASKRKEAELRSgiirnnslwdrlifhkvqSSLggrvRLMVTGAAPVSATVLtflRAAL--GCQFYEGYGQTECT--AGC 433
Cdd:PRK06087 290 LLNLLEKQPADL------------------SAL----RFFLCGGTTIPKKVA---RECQqrGIKLLSVYGSTESSphAVV 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 434 CLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPN 513
Cdd:PRK06087 345 NLDDPLSRFMHTDGYAAAGVEIKVVD-EARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEA 423
|
410 420 430
....*....|....*....|....*....|.
gi 557878740 514 GTLKIIDRKKHIFkLAQGEYIAPEKIENIYM 544
Cdd:PRK06087 424 GYIKITGRKKDII-VRGGENISSREVEDILL 453
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
199-523 |
4.66e-28 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 118.92 E-value: 4.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 199 ELVERGQRCGVEVTSMkamEDLGRANRRKPKPPA-PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpc 277
Cdd:cd05906 134 GLETLSGLPGIRVLSI---EELLDTAADHDLPQSrPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLT---- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 278 PDDTLISFLPLAHmferVVECVMlCHGAkigffqgDIRLLMDDLKVLQPTVFPVVPRLLnRMFDRIfgQANTTlkrWLLD 357
Cdd:cd05906 207 PQDVFLNWVPLDH----VGGLVE-LHLR-------AVYLGCQQVHVPTEEILADPLRWL-DLIDRY--RVTIT---WAPN 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 358 FA-SKRKEAELRsgiiRNNSLWDrlifhkvQSSLggrvRLMVTGAAPVSA-TVLTFLR--AALGCQ---FYEGYGQTECT 430
Cdd:cd05906 269 FAfALLNDLLEE----IEDGTWD-------LSSL----RYLVNAGEAVVAkTIRRLLRllEPYGLPpdaIRPAFGMTETC 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 431 AGC--CLTMP-GDWTAGH----VGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLH 503
Cdd:cd05906 334 SGViySRSFPtYDHSQALefvsLGRPIPGVSMRIVD-DEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFR 412
|
330 340
....*....|....*....|
gi 557878740 504 TGDIGkWLPNGTLKIIDRKK 523
Cdd:cd05906 413 TGDLG-FLDNGNLTITGRTK 431
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
230-564 |
1.14e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 117.83 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 230 PPAPE-DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPcpDDTLISFLPLAHMF-ERVVECVMLCHGAKI 307
Cdd:PRK06710 201 PCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEG--EEVVLGVLPFFHVYgMTAVMNLSIMQGYKM 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 308 GFF-QGDIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqaNTTLkrwlldfaskRKEAELRSgiirnnslwdrlifhkv 386
Cdd:PRK06710 279 VLIpKFDMKMVFEAIKKHKVTLFPGAPTIYIALL-------NSPL----------LKEYDISS----------------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 387 qsslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPgdW---TAGHVGAPMPCNLIKLVDVEEM 463
Cdd:PRK06710 325 -------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFL--WekrVPGSIGVPWPDTEAMIMSLETG 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 464 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 543
Cdd:PRK06710 396 EALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREVEEVL 473
|
330 340
....*....|....*....|....*...
gi 557878740 544 MRSEPVAQVFV-------HGESLQAFLI 564
Cdd:PRK06710 474 YEHEKVQEVVTigvpdpyRGETVKAFVV 501
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
150-550 |
1.30e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 118.13 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 150 EAITYIVNKAELSLVFVDKPE-------KAKLLLEGVenkliPGLKIIVVMDayGSELVERGQRCGVEVTSMKAME---D 219
Cdd:PRK07529 119 EQIAELLRAAGAKVLVTLGPFpgtdiwqKVAEVLAAL-----PELRTVVEVD--LARYLPGPKRLAVPLIRRKAHArilD 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 220 LGRANRRKP-------KPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDC---SAFVKATentvnpcPDDTLISFLPLA 289
Cdd:PRK07529 192 FDAELARQPgdrlfsgRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAwlgALLLGLG-------PGDTVFCGLPLF 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 290 HMFERVVEC-VMLCHGAKIGFF--QG--DIRLLMDDLKVL---QPTVFPVVPRLLNRMFDRIFGQANTtlkrwlldfask 361
Cdd:PRK07529 265 HVNALLVTGlAPLARGAHVVLAtpQGyrGPGVIANFWKIVeryRINFLSGVPTVYAALLQVPVDGHDI------------ 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 362 rkeaelrsgiirnnslwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMP-GD 440
Cdd:PRK07529 333 --------------------------SSL----RYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPdGE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 441 WTAGHVGAPMPCNLIKLVDVEEM-NYM--AAEGE-GEVCVKGPNVFQGYLkDPAKTAEALDKDGWLHTGDIGKWLPNGTL 516
Cdd:PRK07529 383 RRIGSVGLRLPYQRVRVVILDDAgRYLrdCAVDEvGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDLGRIDADGYF 461
|
410 420 430
....*....|....*....|....*....|....
gi 557878740 517 KIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVA 550
Cdd:PRK07529 462 WLTGRAKDLI-IRGGHNIDPAAIEEALLRHPAVA 494
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
231-582 |
2.19e-27 |
|
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: 115.56 E-value: 2.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 231 PAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVvecvmlcHGAKIGFF 310
Cdd:cd05903 90 AMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLG----PGDVFLVASPMAHQTGFV-------YGFTLPLL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 311 QGDIRLLMDdlkVLQPTVfpvVPRLLNRmfDRI-FGQANTTLKRWLLDfaskrkeAELRSGiirnnslwDRLifhkvqss 389
Cdd:cd05903 159 LGAPVVLQD---IWDPDK---ALALMRE--HGVtFMMGATPFLTDLLN-------AVEEAG--------EPL-------- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 390 lgGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEC--TAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMA 467
Cdd:cd05903 208 --SRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECpgAVTSITPAPEDRRLYTDGRPLPGVEIKVVD-DTGATLA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 468 AEGEGEVCVKGPNVFQGYLKDPAKTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSE 547
Cdd:cd05903 285 PGVEGELLSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHP 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 557878740 548 PVAQVFVHG---ESLQAFLIAIVV------PDVETLCSWAQKRG 582
Cdd:cd05903 363 GVIEAAVVAlpdERLGERACAVVVtksgalLTFDELVAYLDRQG 406
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
233-570 |
2.31e-27 |
|
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: 116.10 E-value: 2.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 233 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLplAHMFE-RVVECVM-LCHGAKIGff 310
Cdd:cd05918 105 PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLT----SESRVLQFA--SYTFDvSILEIFTtLAAGGCLC-- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 311 qgdI---RLLMDDLkvlqptvfpvvPRLLNRMfdrifgQANTtlkrwlldfaskrkeAELRSGIIRnnslwdrLIFHKVQ 387
Cdd:cd05918 177 ---IpseEDRLNDL-----------AGFINRL------RVTW---------------AFLTPSVAR-------LLDPEDV 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 388 SSLggrvRLMVTGAAPVSATVLTflRAALGCQFYEGYGQTECTAGCCLTMPG-DWTAGHVGAPMPCNLIkLVDVEEMNYM 466
Cdd:cd05918 215 PSL----RTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRPLGATCW-VVDPDNHDRL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 467 AAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKD-GWLH------------TGDIGKWLPNGTLKIIDRKKHIFKLaQGE 532
Cdd:cd05918 288 VPIGAvGELLIEGPILARGYLNDPEKTAAAFIEDpAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKI-RGQ 366
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 557878740 533 YIAPEKIENIYMRSEP-----VAQVFVH-GESLQAFLIAIVVPD 570
Cdd:cd05918 367 RVELGEIEHHLRQSLPgakevVVEVVKPkDGSSSPQLVAFVVLD 410
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
234-557 |
4.22e-27 |
|
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: 114.37 E-value: 4.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 234 EDLAVICFTSGTTGNPKGAMVTHRNIvsdcSAFVKATENTVNPCPDDTLISFLPLAH------MFERVVE-CVMLCHGAk 306
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNH----WWSAIGSALNLGLTEDDNWLCALPLFHisglsiLMRSVIYgMTVYLVDK- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 307 igFFQGDIRLLMDDLKVlqpTVFPVVPRLLNRMFDRIFGQANTTLkrwlldfaskrkeaelrsgiirnnslwdrlifhkv 386
Cdd:cd05912 152 --FDAEQVLHLINSGKV---TIISVVPTMLQRLLEILGEGYPNNL----------------------------------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 387 qsslggrvRLMVTGAAPVSATVLTFLRAaLGCQFYEGYGQTEcTAGCCLTMPGDWTA---GHVGAPMPCNLIKLVDveem 463
Cdd:cd05912 192 --------RCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTE-TCSQIVTLSPEDALnkiGSAGKPLFPVELKIED---- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 464 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 543
Cdd:cd05912 258 DGQPPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVL 335
|
330
....*....|....
gi 557878740 544 MRSEPVAQVFVHGE 557
Cdd:cd05912 336 LSHPAIKEAGVVGI 349
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
228-542 |
6.63e-27 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 115.71 E-value: 6.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 228 PKPP-APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVK-ATENTVNPCPDDTLISFLPLAHMFERVVECV-MLCHG 304
Cdd:PLN02574 191 PKPViKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRfEASQYEYPGSDNVYLAALPMFHIYGLSLFVVgLLSLG 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 305 AKI----GFFQGDIRLLMDDLKVlqpTVFPVVPRLLNRMFDRIFGQANTTLKrwlldfaskrkeaelrsgiirnnslwdr 380
Cdd:PLN02574 271 STIvvmrRFDASDMVKVIDRFKV---THFPVVPPILMALTKKAKGVCGEVLK---------------------------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 381 lifhkvqsSLggrvRLMVTGAAPVSA-TVLTFLRAALGCQFYEGYGQTECTA----GCCLTMPGDWTAghVGAPMPCNLI 455
Cdd:PLN02574 320 --------SL----KQVSCGAAPLSGkFIQDFVQTLPHVDFIQGYGMTESTAvgtrGFNTEKLSKYSS--VGLLAPNMQA 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 456 KLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIA 535
Cdd:PLN02574 386 KVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQIA 464
|
....*..
gi 557878740 536 PEKIENI 542
Cdd:PLN02574 465 PADLEAV 471
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
126-569 |
1.41e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 114.31 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 126 WVIIEQGCFAySMVIVPLYDTLGNEAITYIVNKAELSLVFVDK---PEKAKLLLEGVenkliPGLKIIVVMDA--YGSEL 200
Cdd:PRK06188 76 LMAIGAAQLA-GLRRTALHPLGSLDDHAYVLEDAGISTLIVDPapfVERALALLARV-----PSLKHVLTLGPvpDGVDL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 201 vergqrcgvevtsmkamedLGRANRRKPKPP----APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATEntvnp 276
Cdd:PRK06188 150 -------------------LAAAAKFGPAPLvaaaLPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWE----- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 277 CPDDtlISFL---PLAHMFERVVECVMLCHGAKI---GFfqgDIRLLMDDLKVLQPTVFPVVPRLLNRmfdrifgqantt 350
Cdd:PRK06188 206 WPAD--PRFLmctPLSHAGGAFFLPTLLRGGTVIvlaKF---DPAEVLRAIEEQRITATFLVPTMIYA------------ 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 351 lkrwLLDFASKRKeAELrsgiirnnslwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECT 430
Cdd:PRK06188 269 ----LLDHPDLRT-RDL--------------------SSL----ETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 431 AGCCLTMPGDWTAGHV------GAPMPCNLIKLVDvEEMNYMAAeGE-GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLH 503
Cdd:PRK06188 320 MVITYLRKRDHDPDDPkrltscGRPTPGLRVALLD-EDGREVAQ-GEvGEICVRGPLVMDGYWNRPEETAEAF-RDGWLH 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557878740 504 TGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFV-------HGESLQafliAIVVP 569
Cdd:PRK06188 397 TGDVAREDEDGFYYIVDRKKDMI-VTGGFNVFPREVEDVLAEHPAVAQVAVigvpdekWGEAVT----AVVVL 464
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
233-594 |
2.65e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 113.71 E-value: 2.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 233 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDcSAFV----KATENtvnpcpdDTLISFLPLAHMFERVVeCVMLC--HGAK 306
Cdd:PRK12583 200 RDDPINIQYTSGTTGFPKGATLSHHNILNN-GYFVaeslGLTEH-------DRLCVPVPLYHCFGMVL-ANLGCmtVGAC 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 307 IgFFQGDirlLMDDLKVLQ-------------PTVFpvVPRLLNRMFDRifgqanttlkrwlLDFASkrkeaeLRSGIIr 373
Cdd:PRK12583 271 L-VYPNE---AFDPLATLQaveeerctalygvPTMF--IAELDHPQRGN-------------FDLSS------LRTGIM- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 374 nnslwdrlifhkvqsslggrvrlmvtGAAPVSATVLTFLRAALGC-QFYEGYGQTECTAGCCLTMPGD---WTAGHVGAP 449
Cdd:PRK12583 325 --------------------------AGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSLQTTAADdleRRVETVGRT 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 450 MPCNLIKLVDVEemNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkL 528
Cdd:PRK12583 379 QPHLEVKVVDPD--GATVPRGEiGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMI-I 455
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557878740 529 AQGEYIAPEKIENIYMRSEPVAQVFVHGeslqafliaivVPDV---ETLCSWAQKR-GFEGSFEEL---CRNK 594
Cdd:PRK12583 456 RGGENIYPREIEEFLFTHPAVADVQVFG-----------VPDEkygEEIVAWVRLHpGHAASEEELrefCKAR 517
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
233-612 |
7.69e-26 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 112.66 E-value: 7.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 233 PEDLAVICFTSGTTGNPKGAMVTHRNIVS------DCSAFVKATEntvnpcPddTLISFLPLAHMFERVVEC-VMLCHGA 305
Cdd:PRK08180 208 PDTIAKFLFTSGSTGLPKAVINTHRMLCAnqqmlaQTFPFLAEEP------P--VLVDWLPWNHTFGGNHNLgIVLYNGG 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 306 KI---------GFFQGDIRllmdDLKVLQPTVFPVVPR--------------LLNRMFDRifgqanttLKrwLLDFASkr 362
Cdd:PRK08180 280 TLyiddgkptpGGFDETLR----NLREISPTVYFNVPKgwemlvpalerdaaLRRRFFSR--------LK--LLFYAG-- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 363 keAELRSgiirnnSLWDRLifHKV-QSSLGGRVRLMVtgaapvsatvltflraalgcqfyeGYGQTEcTAGCCL--TMPG 439
Cdd:PRK08180 344 --AALSQ------DVWDRL--DRVaEATCGERIRMMT------------------------GLGMTE-TAPSATftTGPL 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 440 DwTAGHVGAPMPCNLIKLVDVEemnymaaeGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWL----PNGT 515
Cdd:PRK08180 389 S-RAGNIGLPAPGCEVKLVPVG--------GKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVdpadPERG 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 516 LKIIDRKKHIFKLAQGEYIA--PEKIENIYMRSEPVAQVFVHGESlQAFLIAIVVPDVEtLCSWAQKRGFEGSFEELCRN 593
Cdd:PRK08180 460 LMFDGRIAEDFKLSSGTWVSvgPLRARAVSAGAPLVQDVVITGHD-RDEIGLLVFPNLD-ACRRLAGLLADASLAEVLAH 537
|
410
....*....|....*....
gi 557878740 594 KDVKKAILEDMVRLGKDSG 612
Cdd:PRK08180 538 PAVRAAFRERLARLNAQAT 556
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
227-594 |
1.04e-25 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 111.24 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 227 KPKPPAPE-DLAVICFTSGTTGNPKGAMVTHRnivsdcSAFVKATENTV----NPCPddTLISFLPLAHmfervveCVML 301
Cdd:cd12118 125 EWIPPADEwDPIALNYTSGTTGRPKGVVYHHR------GAYLNALANILewemKQHP--VYLWTLPMFH-------CNGW 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 302 CHGAKIGFFQG--------DIRLLMDDLKVLQPTVFPVVPRLLNrmfdrifgqanttlkrwlldfaskrkeaelrsgIIR 373
Cdd:cd12118 190 CFPWTVAAVGGtnvclrkvDAKAIYDLIEKHKVTHFCGAPTVLN---------------------------------MLA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 374 NNSlwdrlifHKVQSSLGGRVRLMVTGAAPvSATVLtFLRAALGCQFYEGYGQTEcTAG---CCLTMPgDWTAGHV---- 446
Cdd:cd12118 237 NAP-------PSDARPLPHRVHVMTAGAPP-PAAVL-AKMEELGFDVTHVYGLTE-TYGpatVCAWKP-EWDELPTeera 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 447 ------GAPMPCNL-IKLVDVEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLK 517
Cdd:cd12118 306 rlkarqGVRYVGLEeVDVLDPETMKPVPRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 518 IIDRKKHIFkLAQGEYIAPEKIENIymrsepvaqVFVHGESLQAFLIAivVPD---VETLCSW-AQKRGFEGSFEEL--- 590
Cdd:cd12118 385 IKDRSKDII-ISGGENISSVEVEGV---------LYKHPAVLEAAVVA--RPDekwGEVPCAFvELKEGAKVTEEEIiaf 452
|
....
gi 557878740 591 CRNK 594
Cdd:cd12118 453 CREH 456
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
228-540 |
1.12e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 111.05 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 228 PKPPAPED-LAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPcpddtliSFLPLAHMFERV--VECV--MLC 302
Cdd:PRK09088 128 DTPSIPPErVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHS-------SFLCDAPMFHIIglITSVrpVLA 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 303 HGAKIGFFQGdirllmddlkvLQPTvfpvvpRLLNRMFDRIFGQANTtlkrwlldFASKRKEAELRSGIIRNNSLWDRLI 382
Cdd:PRK09088 201 VGGSILVSNG-----------FEPK------RTLGRLGDPALGITHY--------FCVPQMAQAFRAQPGFDAAALRHLT 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 383 fhkvqsslggrvrLMVTGAAP-VSATVLTFLraALGCQFYEGYGQTEctAGCCLTMPGDWT-----AGHVGAPMPCNLIK 456
Cdd:PRK09088 256 -------------ALFTGGAPhAAEDILGWL--DDGIPMVDGFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 457 LVDVEEMNYMAAEgEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAP 536
Cdd:PRK09088 319 VVDDQGNDCPAGV-PGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYP 396
|
....
gi 557878740 537 EKIE 540
Cdd:PRK09088 397 AEIE 400
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
139-569 |
1.53e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 111.18 E-value: 1.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 139 VIVPLYDTLGNEAITYIVNKAELSLVFVDkPEKAKLLLEGVENKlipglkiivVMDAYGSELVERGQrcgVEVTSMKAME 218
Cdd:PRK08316 87 VHVPVNFMLTGEELAYILDHSGARAFLVD-PALAPTAEAALALL---------PVDTLILSLVLGGR---EAPGGWLDFA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 219 DLGRANRRKPKPPAP--EDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVV 296
Cdd:PRK08316 154 DWAEAGSVAEPDVELadDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMS----ADDIPLHALPLYHCAQLDV 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 297 ecvmlchgakigffqgdirLLMDDLKVLQPTVFPVVPRLlNRMFDRIFGQANTTLkrwlldFASKrkeaelrsgiirnnS 376
Cdd:PRK08316 230 -------------------FLGPYLYVGATNVILDAPDP-ELILRTIEAERITSF------FAPP--------------T 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 377 LWDRLIFHKV-----QSSLggrvRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTAGCCLTMPGDwTAGHVG-AP 449
Cdd:PRK08316 270 VWISLLRHPDfdtrdLSSL----RKGYYGASIMPVEVLKELRERLpGLRFYNCYGQTEIAPLATVLGPEE-HLRRPGsAG 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 450 MPC-NL-IKLVDvEEMNYMAAeGE-GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIF 526
Cdd:PRK08316 345 RPVlNVeTRVVD-DDGNDVAP-GEvGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMI 421
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 557878740 527 KLAqGEYIAPEKIENIYMRSEPVAQVFV----HGESLQAfLIAIVVP 569
Cdd:PRK08316 422 KTG-GENVASREVEEALYTHPAVAEVAViglpDPKWIEA-VTAVVVP 466
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
235-572 |
6.10e-25 |
|
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: 106.20 E-value: 6.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 235 DLAVICFTSGTTGNPKGAMVTHRNIVsdCSAFvkATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAK---IGFFQ 311
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLI--AANL--QLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGAnvvMEKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 312 GDIRL-LMDDLKVlqpTVFPVVPRLLNRMFDRIfgqanttlkrwlldfasKRKEAELRSgiIRNnslwdrlifhkvqssl 390
Cdd:cd17637 77 PAEALeLIEEEKV---TLMGSFPPILSNLLDAA-----------------EKSGVDLSS--LRH---------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 391 ggrvrlmVTGA-APvsATVLTFLrAALGCQFYEGYGQTEcTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAE 469
Cdd:cd17637 119 -------VLGLdAP--ETIQRFE-ETTGATFWSLYGQTE-TSGLVTLSPYRERPGSAGRPGPLVRVRIVD-DNDRPVPAG 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 470 GEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRK--KHIFKlAQGEYIAPEKIENIYMRSE 547
Cdd:cd17637 187 ETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKVILEHP 264
|
330 340
....*....|....*....|....*
gi 557878740 548 PVAQVFVHGeslqafliaivVPDVE 572
Cdd:cd17637 265 AIAEVCVIG-----------VPDPK 278
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
186-556 |
1.58e-24 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 107.64 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 186 GLKIIVVMDAYGSELVERGQRCGVE----VTSMKAMEDLGRANRrkpKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIvs 261
Cdd:PRK06839 100 GTTVLFVEKTFQNMALSMQKVSYVQrvisITSLKEIEDRKIDNF---VEKNESASFIICYTSGTTGKPKGAVLTQENM-- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 262 dcsaFVKATEN--TVNPCPDDTLISFLPLAHMfervvecvmlchgAKIGFFQgdirllmddlkvlQPTVFP----VVPRL 335
Cdd:PRK06839 175 ----FWNALNNtfAIDLTMHDRSIVLLPLFHI-------------GGIGLFA-------------FPTLFAggviIVPRK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 336 LN-----RMFDR-----IFGQAntTLKRWLLDfASKRKEAELRSgiirnnslwdrlifhkvqsslggrVRLMVTGAAPVS 405
Cdd:PRK06839 225 FEptkalSMIEKhkvtvVMGVP--TIHQALIN-CSKFETTNLQS------------------------VRWFYNGGAPCP 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 406 ATVLTFLRAAlGCQFYEGYGQTECTAGCCLTMPGDW--TAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQ 483
Cdd:PRK06839 278 EELMREFIDR-GFLFGQGFGMTETSPTVFMLSEEDArrKVGSIGKPVLFCDYELID-ENKNKVEVGEVGELLIRGPNVMK 355
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557878740 484 GYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG 556
Cdd:PRK06839 356 EYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQVINKLSDVYEVAVVG 426
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
141-581 |
2.15e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 107.56 E-value: 2.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 141 VPLYDTLGNEAITYIVNKAELSLVFVDKPEKAklLLEGVENkLIPGLKIIVVMDAYGSELVergqrcgvevtsmKAMEDL 220
Cdd:PRK07786 95 VPVNFRLTPPEIAFLVSDCGAHVVVTEAALAP--VATAVRD-IVPLLSTVVVAGGSSDDSV-------------LGYEDL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 221 GRANRrKPKPPA--PEDL-AVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNpcpDDtlISFL--PLAHM--FE 293
Cdd:PRK07786 159 LAEAG-PAHAPVdiPNDSpALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADIN---SD--VGFVgvPLFHIagIG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 294 RVVECVMLchGAKIgffqgdirllmddlkVLQPTvfpvvprllnRMFDrifgqANTTLKRWlldfaskrkEAELRSGIIR 373
Cdd:PRK07786 233 SMLPGLLL--GAPT---------------VIYPL----------GAFD-----PGQLLDVL---------EAEKVTGIFL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 374 NNSLWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTAGCCLTMPGDWTA--GHVGAPM 450
Cdd:PRK07786 272 VPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEMSPVTCMLLGEDAIRklGSVGKVI 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 451 PCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQ 530
Cdd:PRK07786 352 PTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHSGDLVRQDEEGYVWVVDRKKDMI-ISG 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557878740 531 GEYIAPEKIENIYMRSEPVAQVFVHGESLQAF---LIAIVVPD-------VETLCSWAQKR 581
Cdd:PRK07786 429 GENIYCAEVENVLASHPDIVEVAVIGRADEKWgevPVAVAAVRnddaaltLEDLAEFLTDR 489
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
184-569 |
2.45e-24 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 107.45 E-value: 2.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 184 IPGLKIIVVMDAYGSELVERgqrcgveVTSMKAME---DLGR--ANRRkpkpPAPEDLAVICFTSGTTGNPKGAMVTHRN 258
Cdd:PRK13295 153 LPALRHVVVVGGDGADSFEA-------LLITPAWEqepDAPAilARLR----PGPDDVTQLIYTSGTTGEPKGVMHTANT 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 259 IVSDCSAFVKATENTvnpcPDDTLISFLPLAHMfervvecvmlchgakIGFFQGDIRLLMDDLK-VLQPTVFPVvprlln 337
Cdd:PRK13295 222 LMANIVPYAERLGLG----ADDVILMASPMAHQ---------------TGFMYGLMMPVMLGATaVLQDIWDPA------ 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 338 RMFDRI------FGQANTTlkrWLLDFASKRKEAElrsgiirnnslwdrlifhKVQSSLggrvRLMVTGAAPVSATVLTF 411
Cdd:PRK13295 277 RAAELIrtegvtFTMASTP---FLTDLTRAVKESG------------------RPVSSL----RTFLCAGAPIPGALVER 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 412 LRAALGCQFYEGYGQTECTAgCCLTMPGD---WTAGHVGAPMPCNLIKLVDVEEMNYMAAEgEGEVCVKGPNVFQGYLKD 488
Cdd:PRK13295 332 ARAALGAKIVSAWGMTENGA-VTLTKLDDpdeRASTTDGCPLPGVEVRVVDADGAPLPAGQ-IGRLQVRGCSNFGGYLKR 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 489 PAKTAEalDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG---ESLQAFLIA 565
Cdd:PRK13295 410 PQLNGT--DADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEALLYRHPAIAQVAIVAypdERLGERACA 486
|
....
gi 557878740 566 IVVP 569
Cdd:PRK13295 487 FVVP 490
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
234-564 |
2.98e-24 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 106.02 E-value: 2.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 234 EDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHM--FERVVECVMLCHGAKIGFFQ 311
Cdd:cd05935 84 DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLT----PSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMAR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 312 GDIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanTTLKRWLLDFASkrkeaelrsgiirnnslwdrlifhkvqsslg 391
Cdd:cd05935 160 WDRETALELIEKYKVTFWTNIPTMLVDLL--------ATPEFKTRDLSS------------------------------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 392 grVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAEGE 471
Cdd:cd05935 201 --LKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 472 GEVCVKGPNVFQGYLKDPAKTAEALDKDG---WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEP 548
Cdd:cd05935 279 GEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPA 357
|
330 340
....*....|....*....|...
gi 557878740 549 VAQVFV-------HGESLQAFLI 564
Cdd:cd05935 358 I*EVCVisvpderVGEEVKAFIV 380
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
198-570 |
6.02e-24 |
|
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: 105.45 E-value: 6.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 198 SELVERGQRCGVevTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATENTVNPC 277
Cdd:cd12116 92 DALPDRLPAGLP--VLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVN----FLHSMRERLGLG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 278 PDDTLISFLPLAhmFE-RVVECVM-LCHGAKIGFFQGDI----RLLMDDLKVLQPTVFpvvprllnrmfdrifgQANTTL 351
Cdd:cd12116 166 PGDRLLAVTTYA--FDiSLLELLLpLLAGARVVIAPRETqrdpEALARLIEAHSITVM----------------QATPAT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 352 KRWLLDfaskrkeaelrSGiirnnslWDRLifhkvqsslgGRVRLMVTGAA--PVSATVLTflraALGCQFYEGYGQTEC 429
Cdd:cd12116 228 WRMLLD-----------AG-------WQGR----------AGLTALCGGEAlpPDLAARLL----SRVGSLWNLYGPTET 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 430 T--AGCCLTMPGDwTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLH---- 503
Cdd:cd12116 276 TiwSTAARVTAAA-GPIPIGRPLANTQVYVLD-AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpgsr 353
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557878740 504 ---TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQ--VFVHGESLQAFLIAIVVPD 570
Cdd:cd12116 354 lyrTGDLVRRRADGRLEYLGRADGQVKI-RGHRIELGEIEAALAAHPGVAQaaVVVREDGGDRRLVAYVVLK 424
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
232-573 |
1.31e-23 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 104.25 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 232 APEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATENTVNPCPDDTLISFLPLAHMFervveCVM-----LCHGAk 306
Cdd:cd05945 95 DGDDNAYIIFTSGSTGRPKGVQISHDNLVS----FTNWMLSDFPLGPGDVFLNQAPFSFDL-----SVMdlypaLASGA- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 307 igffqgdirllmddlkvlqpTVFPVvPRLLNRMFDRIF-GQANTTLKRWLldfaskrkeaelrsgiiRNNSLWDRLIFHK 385
Cdd:cd05945 165 --------------------TLVPV-PRDATADPKQLFrFLAEHGITVWV-----------------STPSFAAMCLLSP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 386 --VQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTmpgDWT----AGH----VGAPMPCNLI 455
Cdd:cd05945 207 tfTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYI---EVTpevlDGYdrlpIGYAKPGAKL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 456 KLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKD---GWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGE 532
Cdd:cd05945 284 VILD-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGY 361
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 557878740 533 YIAPEKIENIYMRSEPVAQVFV----HGESLQAfLIAIVVPDVET 573
Cdd:cd05945 362 RIELEEIEAALRQVPGVKEAVVvpkyKGEKVTE-LIAFVVPKPGA 405
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
140-637 |
2.90e-23 |
|
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: 104.44 E-value: 2.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 140 IVPLYDTLGNE--AITYIVNKAELSLVFVDKPEKAKLLLEGVenkLIPGLKIIVVmdaygselveRGQRCGVEVTSMK-- 215
Cdd:cd05921 80 VSPAYSLMSQDlaKLKHLFELLKPGLVFAQDAAPFARALAAI---FPLGTPLVVS----------RNAVAGRGAISFAel 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 216 -AMEDLGRANRRKPKPpAPEDLAVICFTSGTTGNPKGAMVTHRNIVSdcSAFVKATENTVNPCPDDTLISFLPLAHMFer 294
Cdd:cd05921 147 aATPPTAAVDAAFAAV-GPDTVAKFLFTSGSTGLPKAVINTQRMLCA--NQAMLEQTYPFFGEEPPVLVDWLPWNHTF-- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 295 vvecvmlchGAKIGF-----------------FQGDIRLLMDDLKVLQPTVFPVVPR----LLNRMfdrifgQANTTLKR 353
Cdd:cd05921 222 ---------GGNHNFnlvlynggtlyiddgkpMPGGFEETLRNLREISPTVYFNVPAgwemLVAAL------EKDEALRR 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 354 WLLdfasKRKEAELRSGIIRNNSLWDRLIFHKVQSSlGGRVRlmvtgaapvsatvltflraalgcqFYEGYGQTECTAGC 433
Cdd:cd05921 287 RFF----KRLKLMFYAGAGLSQDVWDRLQALAVATV-GERIP------------------------MMAGLGATETAPTA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 434 CLTMPGDWTAGHVGAPMPCNLIKLVdveemnymAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWL-- 511
Cdd:cd05921 338 TFTHWPTERSGLIGLPAPGTELKLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdp 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 512 --PNGTLKIIDRKKHIFKLAQGEYIA--PEKIENIYMRSEPVAQVFVHGESlQAFLIAIVVPDVETLcsWAQKRGFEGSF 587
Cdd:cd05921 410 ddPAKGLVFDGRVAEDFKLASGTWVSvgPLRARAVAACAPLVHDAVVAGED-RAEVGALVFPDLLAC--RRLVGLQEASD 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 557878740 588 EELCRNKDVKKAILEDMVRLGKDSGLKPfEQVKGITLHPELFSIDNGLLT 637
Cdd:cd05921 487 AEVLRHAKVRAAFRDRLAALNGEATGSS-SRIARALLLDEPPSIDKGEIT 535
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
235-581 |
3.48e-23 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 100.87 E-value: 3.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 235 DLAVICFTSGTTGNPKGAMVTHRNIVSdcSAfvKATENTVNPCPDDTLISFLPLAHM--FERVVECVMLchGAKIGFFQG 312
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLA--SA--AGLHSRLGFGGGDSWLLSLPLYHVggLAILVRSLLA--GAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 313 DiRLLMDDLKVLQPTVFPVVPRLLNRMFDRifGQANTTLKRwlldfaskrkeaelrsgiirnnslwdrlifhkvqsslgg 392
Cdd:cd17630 75 N-QALAEDLAPPGVTHVSLVPTQLQRLLDS--GQGPAALKS--------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 393 rVRLMVTGAAPVSAtVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDveemnymaaegEG 472
Cdd:cd17630 113 -LRAVLLGGAPIPP-ELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVE-----------DG 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 473 EVCVKGPNVFQGYLKDPakTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQV 552
Cdd:cd17630 180 EIWVGGASLAMGYLRGQ--LVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAVRDA 256
|
330 340 350
....*....|....*....|....*....|....*.
gi 557878740 553 FVHG---ESLQAFLIAIVV----PDVETLCSWAQKR 581
Cdd:cd17630 257 FVVGvpdEELGQRPVAVIVgrgpADPAELRAWLKDK 292
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
139-590 |
1.04e-22 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 102.50 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 139 VIVPLYDTLGNEAITYIVNKAELSLVFVD----KPEKAKLLLEGVEN--KLIPGLKIIVVMDAYGSELVERGQRcgvevt 212
Cdd:COG0365 90 VHSPVFPGFGAEALADRIEDAEAKVLITAdgglRGGKVIDLKEKVDEalEELPSLEHVIVVGRTGADVPMEGDL------ 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 213 smkAMEDLgRANRRKPKPPAP---EDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKateNTVNPCPDDTLISFLPLA 289
Cdd:COG0365 164 ---DWDEL-LAAASAEFEPEPtdaDDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAK---YVLDLKPGDVFWCTADIG 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 290 ----HMFervveCVM--LCHGAKIGFFQGDI------RL--LMDDLKVlqpTVFPVVPRLLnRMfdrifgqanttLKRWL 355
Cdd:COG0365 237 watgHSY-----IVYgpLLNGATVVLYEGRPdfpdpgRLweLIEKYGV---TVFFTAPTAI-RA-----------LMKAG 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 356 LDFASKrkeaelrsgiirnnslWDRlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCL 435
Cdd:COG0365 297 DEPLKK----------------YDL-------SSL----RLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFIS 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 436 TMPGDWT-AGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKG--PNVFQGYLKDPAKTAEAL--DKDGWLHTGDIGKW 510
Cdd:COG0365 350 NLPGLPVkPGSMGKPVPGYDVAVVD-EDGNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDGARR 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 511 LPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPVAQVFV----HGESLQAfLIAIVVPdvetlcswaqKRGFEGS 586
Cdd:COG0365 429 DEDGYFWILGRSDDVINVS-GHRIGTAEIESALVSHPAVAEAAVvgvpDEIRGQV-VKAFVVL----------KPGVEPS 496
|
....
gi 557878740 587 fEEL 590
Cdd:COG0365 497 -DEL 499
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
198-574 |
1.09e-22 |
|
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: 103.78 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 198 SELVERGQRCGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATENTVNPC 277
Cdd:COG1020 581 SALAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVN----LLAWMQRRYGLG 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 278 PDDTLISFLPLAH------MFervvecVMLCHGAKIGFFQGDIRLLMDDLKVL----QPTVFPVVPRLLNRMFDrifgqa 347
Cdd:COG1020 657 PGDRVLQFASLSFdasvweIF------GALLSGATLVLAPPEARRDPAALAELlarhRVTVLNLTPSLLRALLD------ 724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 348 nttlkrwlldfaskrkeaelrsgiirnnSLWDRLifhkvqsslgGRVRLMVTG--AAPVsATVLTFLRAALGCQFYEGYG 425
Cdd:COG1020 725 ----------------------------AAPEAL----------PSLRLVLVGgeALPP-ELVRRWRARLPGARLVNLYG 765
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 426 QTECTAGCCL--TMPGDWTAGHV--GAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEA-----L 496
Cdd:COG1020 766 PTETTVDSTYyeVTPPDADGGSVpiGRPIANTRVYVLD-AHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERfvadpF 844
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 497 DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQ--VFVHGESLQA-FLIAIVVPDV 571
Cdd:COG1020 845 GFPGarLYRTGDLARWLPDGNLEFLGRADDQVKI-RGFRIELGEIEAALLQHPGVREavVVAREDAPGDkRLVAYVVPEA 923
|
...
gi 557878740 572 ETL 574
Cdd:COG1020 924 GAA 926
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
233-590 |
1.24e-22 |
|
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: 99.86 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 233 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVECVMLchgakigFFQG 312
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFD----PDDVLLCGLPLFHVNGSVVTLLTP-------LASG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 313 DIRLLMDDLKVLQPTVFPVVPRLLNRMfdRIfgQANTTLKRWLLDFASKRKEAELrsgiirnnslwdrlifhkvqSSLgg 392
Cdd:cd05944 70 AHVVLAGPAGYRNPGLFDNFWKLVERY--RI--TSLSTVPTVYAALLQVPVNADI--------------------SSL-- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 393 rvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMP-GDWTAGHVGAPMPCNLIKLVDVE-EMNYM--AA 468
Cdd:cd05944 124 --RFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKVLDgVGRLLrdCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 469 EGE-GEVCVKGPNVFQGYLKDPAKTaEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSE 547
Cdd:cd05944 202 PDEvGEICVAGPGVFGGYLYTEGNK-NAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLRHP 279
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 557878740 548 PVaqvfvhgeslqAFLIAIVVPDV---ETLCSWAQ-KRGFEGSFEEL 590
Cdd:cd05944 280 AV-----------AFAGAVGQPDAhagELPVAYVQlKPGAVVEEEEL 315
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
234-648 |
1.75e-22 |
|
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: 100.49 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 234 EDLAVICFTSGTTGNPKGAMVTHRNIVS---DCSAFVKATENTVNPCPDDT------LISFL-PLAHMFervveCVMLCH 303
Cdd:cd05972 81 EDPALIYFTSGTTGLPKGVLHTHSYPLGhipTAAYWLGLRPDDIHWNIADPgwakgaWSSFFgPWLLGA-----TVFVYE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 304 GAKIgffqgDIRLLMDDLKVLQPTVFPVVPrllnrmfdrifgqanTTLKRWL-LDFASKRKeaelrsgiirnnslwdrli 382
Cdd:cd05972 156 GPRF-----DAERILELLERYGVTSFCGPP---------------TAYRMLIkQDLSSYKF------------------- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 383 fhkvqsslgGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTA--GCCLTMPgdWTAGHVGAPMPCNLIKLVDv 460
Cdd:cd05972 197 ---------SHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLtvGNFPDMP--VKPGSMGRPTPGYDVAIID- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 461 EEMNYMAAEGEGEVCVKGPNV--FQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEK 538
Cdd:cd05972 265 DDGRELPPGEEGDIAIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 539 IENIYMRSEPVAQVFV-------HGESLQAFLIAivvpdvetlcswaqKRGFEGSfEELcrnkdvkkaiLEDMVRLGKdS 611
Cdd:cd05972 343 VESALLEHPAVAEAAVvgspdpvRGEVVKAFVVL--------------TSGYEPS-EEL----------AEELQGHVK-K 396
|
410 420 430
....*....|....*....|....*....|....*..
gi 557878740 612 GLKPFEQVKGITLHPELfsidngLLTPTMKAKRPELR 648
Cdd:cd05972 397 VLAPYKYPREIEFVEEL------PKTISGKIRRVELR 427
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
230-570 |
4.17e-22 |
|
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: 99.97 E-value: 4.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 230 PPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATeNTVNPCPDDTLISFLPL---AHMFERVVEcvmLCHGAK 306
Cdd:cd12117 132 PVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVR----LVKNT-NYVTLGPDDRVLQTSPLafdASTFEIWGA---LLNGAR 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 307 IgffqgdirllmddlkVLQPtvfPVVPRLLNRMFDRIFGQANTTLkrWLldfaskrkeaelrsgiirNNSLWdRLIFHKV 386
Cdd:cd12117 204 L---------------VLAP---KGTLLDPDALGALIAEEGVTVL--WL------------------TAALF-NQLADED 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 387 QSSLGGrVRLMVTGAAPVS-ATVLTFLRAALGCQFYEGYGQTECT--AGCCLTMPGDWTAGHV--GAPMPcNLIKLVdVE 461
Cdd:cd12117 245 PECFAG-LRELLTGGEVVSpPHVRRVLAACPGLRLVNGYGPTENTtfTTSHVVTELDEVAGSIpiGRPIA-NTRVYV-LD 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 462 EMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 534
Cdd:cd12117 322 EDGRPVPPGVpGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI-RGFRI 400
|
330 340 350
....*....|....*....|....*....|....*....
gi 557878740 535 APEKIENIYMRSEPVAQVFV---HGESLQAFLIAIVVPD 570
Cdd:cd12117 401 ELGEIEAALRAHPGVREAVVvvrEDAGGDKRLVAYVVAE 439
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
186-581 |
5.44e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 100.50 E-value: 5.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 186 GLKIIVVMDAYgSELVER-GQRCGVE---VTSMKAM-----------------------EDLGRANRRKPKP-----PAP 233
Cdd:PRK06178 130 GAEVLLALDQL-APVVEQvRAETSLRhviVTSLADVlpaeptlplpdslraprlaaagaIDLLPALRACTAPvplppPAL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 234 EDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATentVNPCPDDTLISFLPlahMFervvecvmlchgakigFFQGD 313
Cdd:PRK06178 209 DALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVA---VVGGEDSVFLSFLP---EF----------------WIAGE 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 314 irllmdDLKVLQPTVF--PVVprLLNRmfdrifgqanttlkrwlldfaskrkeaelrsgiirnnslWDRLIF------HK 385
Cdd:PRK06178 267 ------NFGLLFPLFSgaTLV--LLAR---------------------------------------WDAVAFmaaverYR 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 386 VQSSLG---GRVRLMVTGAapVSATVLTFL--------------------RAALGCQFYEG-YGQTEcTAGCcltmpGDW 441
Cdd:PRK06178 300 VTRTVMlvdNAVELMDHPR--FAEYDLSSLrqvrvvsfvkklnpdyrqrwRALTGSVLAEAaWGMTE-THTC-----DTF 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 442 TAG-------------HVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIG 508
Cdd:PRK06178 372 TAGfqdddfdllsqpvFVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIG 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 509 KWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFVHG---ESLQAFLIAIVVP------DVETLCSWAQ 579
Cdd:PRK06178 451 KIDEQGFLHYLGRRKEMLKV-NGMSVFPSEVEALLGQHPAVLGSAVVGrpdPDKGQVPVAFVQLkpgadlTAAALQAWCR 529
|
..
gi 557878740 580 KR 581
Cdd:PRK06178 530 EN 531
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
227-648 |
5.83e-22 |
|
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: 99.75 E-value: 5.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 227 KPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKateNTVNPCPDDTLISFLPLAHMFErvvecvmLCHGAK 306
Cdd:cd05959 156 KPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYAR---NVLGIREDDVCFSAAKLFFAYG-------LGNSLT 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 307 IGFFQGDIRLLM----------DDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeaelrsgiirNNS 376
Cdd:cd05959 226 FPLSVGATTVLMperptpaavfKRIRRYRPTVFFGVPTLYAAML---------------------------------AAP 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 377 LWdrlifhkvQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIK 456
Cdd:cd05959 273 NL--------PSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVE 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 457 LVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAP 536
Cdd:cd05959 345 LRD-EDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSP 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 537 EKIENIYMRSEPVAQVFVHGESLQAFLI---AIVVPdvetlcswaqKRGFEGSfeelcrnkdvkkAILEDMVRLGKDSGL 613
Cdd:cd05959 422 FEVESALVQHPAVLEAAVVGVEDEDGLTkpkAFVVL----------RPGYEDS------------EALEEELKEFVKDRL 479
|
410 420 430
....*....|....*....|....*....|....*
gi 557878740 614 KPFEQVKGITLHPELFSidngllTPTMKAKRPELR 648
Cdd:cd05959 480 APYKYPRWIVFVDELPK------TATGKIQRFKLR 508
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
234-565 |
1.18e-21 |
|
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: 98.30 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 234 EDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKateNTVNPCPDDTLISflpLAHMFErvveCVMLCHGAKIGFFQGD 313
Cdd:cd05919 91 DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAR---EALGLTPGDRVFS---SAKMFF----GYGLGNSLWFPLAVGA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 314 IRLLMDD----------LKVLQPTVFPVVPRLlnrmfdrifgqanttlkrwlldFASKRKEAELRSGIIRNnslwdrlif 383
Cdd:cd05919 161 SAVLNPGwptaervlatLARFRPTVLYGVPTF----------------------YANLLDSCAGSPDALRS--------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 384 hkvqsslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEM 463
Cdd:cd05919 210 ----------LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD-EEG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 464 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTaEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIY 543
Cdd:cd05919 279 HTIPPGEEGDLLVRGPSAAVGYWNNPEKS-RATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVESLI 356
|
330 340
....*....|....*....|....*....
gi 557878740 544 MRSEPVAQVFV------HGES-LQAFLIA 565
Cdd:cd05919 357 IQHPAVAEAAVvavpesTGLSrLTAFVVL 385
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
232-662 |
1.39e-21 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 99.10 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 232 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKAtentVNPCPDDTLISFLPLAHM--FERVVECVML--CHGAKI 307
Cdd:PLN02860 170 APDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAI----VGYGEDDVYLHTAPLCHIggLSSALAMLMVgaCHVLLP 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 308 GFfqgDIRLLMDDLKVLQPTVFPVVPRLL------NRMfdRIFGQANTTLKRWLldfaskrkeaelrSGiirNNSLWDRL 381
Cdd:PLN02860 246 KF---DAKAALQAIKQHNVTSMITVPAMMadlislTRK--SMTWKVFPSVRKIL-------------NG---GGSLSSRL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 382 IfhKVQSSLGGRVRLMVTGAAPVSATVLTFLRaaLGCQFYEGYGQTECTAGCCLTMPGDWTAGH-VGAPMPcnliklvDV 460
Cdd:PLN02860 305 L--PDAKKLFPNAKLFSAYGMTEACSSLTFMT--LHDPTLESPKQTLQTVNQTKSSSVHQPQGVcVGKPAP-------HV 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 461 EEMNYM-AAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKI 539
Cdd:PLN02860 374 ELKIGLdESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIK-TGGENVYPEEV 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 540 ENIYMRSEPVAQVFVHGeSLQAFLIAIVVPDVETLCSW--------AQKRGFEGSFEEL---CRNKdvkkailedmvrlg 608
Cdd:PLN02860 453 EAVLSQHPGVASVVVVG-VPDSRLTEMVVACVRLRDGWiwsdnekeNAKKNLTLSSETLrhhCREK-------------- 517
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 557878740 609 kdsGLKPFEQVKGITLHPELFSidnglLTPTMKAKRPELRNYFRSQIDDLYSTI 662
Cdd:PLN02860 518 ---NLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEVRREVLSHLQSLPSNL 563
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
232-648 |
1.67e-21 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 97.89 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 232 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDcsafVKATENTVNPCPDDTLISFLPlahmfervvecvmlchgAKIGFFQ 311
Cdd:cd05971 86 GSDDPALIIYTSGTTGPPKGALHAHRVLLGH----LPGVQFPFNLFPRDGDLYWTP-----------------ADWAWIG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 312 GdirlLMDdlkVLQPTVFPVVPRLLNRM--FDRifGQANTTLKRWLLDFASKRKEAeLRsgIIRnnslwdrliFHKVQSS 389
Cdd:cd05971 145 G----LLD---VLLPSLYFGVPVLAHRMtkFDP--KAALDLMSRYGVTTAFLPPTA-LK--MMR---------QQGEQLK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 390 LGG-RVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEC---TAGCCLTMPGDwtAGHVGAPMPCNLIKLVDvEEMNY 465
Cdd:cd05971 204 HAQvKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECnlvIGNCSALFPIK--PGSMGKPIPGHRVAIVD-DNGTP 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 466 MAAEGEGEVCVKGPN--VFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIY 543
Cdd:cd05971 281 LPPGEVGEIAVELPDpvAFLGYWNNPSATEKKM-AGDWLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAEIEECL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 544 MRSEPVAQVFV-------HGESLQAFliaIVVpdvetlcswaqKRGFEGSfEELCRNkdvkkaiLEDMVRlgkdSGLKPF 616
Cdd:cd05971 359 LKHPAVLMAAVvgipdpiRGEIVKAF---VVL-----------NPGETPS-DALARE-------IQELVK----TRLAAH 412
|
410 420 430
....*....|....*....|....*....|..
gi 557878740 617 EQVKGITLHPELfsidngLLTPTMKAKRPELR 648
Cdd:cd05971 413 EYPREIEFVNEL------PRTATGKIRRRELR 438
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
228-549 |
3.89e-21 |
|
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: 97.69 E-value: 3.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 228 PKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAH-Mfervvecvmlchgak 306
Cdd:cd05931 143 PPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLD----PGDVVVSWLPLYHdM--------------- 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 307 iGFFQGdirllmddlkVLQPTV--FPVV---PR-LLNRMFdrifgqanttlkRWL-----------------LDFASKRK 363
Cdd:cd05931 204 -GLIGG----------LLTPLYsgGPSVlmsPAaFLRRPL------------RWLrlisryratisaapnfaYDLCVRRV 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 364 EAELRSGIirnnslwdRLifhkvqsslgGRVRLMVTGAAPVSATVLT-FLRAALGCQF-----YEGYGQTECT------- 430
Cdd:cd05931 261 RDEDLEGL--------DL----------SSWRVALNGAEPVRPATLRrFAEAFAPFGFrpeafRPSYGLAEATlfvsggp 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 431 ---AGCCLTMPGDWTAGHV----------------GAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAK 491
Cdd:cd05931 323 pgtGPVVLRVDRDALAGRAvavaaddpaarelvscGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEA 402
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557878740 492 TAE------ALDKDGWLHTGDIGkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPV 549
Cdd:cd05931 403 TAEtfgalaATDEGGWLRTGDLG-FLHDGELYITGRLKDLIIVR-GRNHYPQDIEATAEEAHPA 464
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
230-570 |
4.47e-21 |
|
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: 97.03 E-value: 4.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 230 PPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATENTVNPCPDDTLISFLPLAhmFERVVECVM--LCHGAKI 307
Cdd:cd17651 132 ALDADDLAYVIYTSGSTGRPKGVVMPHRSLAN----LVAWQARASSLGPGARTLQFAGLG--FDVSVQEIFstLCAGATL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 308 GFFQGDIRllMDDlkvlqptvfpvvprllnrmfdrifgqanTTLKRWLldfaskrkeAELR-SGIIRNNSLWDRLIFH-K 385
Cdd:cd17651 206 VLPPEEVR--TDP----------------------------PALAAWL---------DEQRiSRVFLPTVALRALAEHgR 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 386 VQSSLGGRVRLMVTGAAPVSATVLT--FLRAALGCQFYEGYGQTECTAGCCLTMPGD---WTA-GHVGAPMPCNLIKLVD 459
Cdd:cd17651 247 PLGVRLAALRYLLTGGEQLVLTEDLreFCAGLPGLRLHNHYGPTETHVVTALSLPGDpaaWPApPPIGRPIDNTRVYVLD 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 460 vEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEY 533
Cdd:cd17651 327 -AALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGFR 404
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 557878740 534 IAPEKIENIYMRSEPVAQ--VFVHGE-SLQAFLIAIVVPD 570
Cdd:cd17651 405 IELGEIEAALARHPGVREavVLAREDrPGEKRLVAYVVGD 444
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
186-581 |
6.76e-21 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 96.18 E-value: 6.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 186 GLKIIVVMDAYGSELVErGQRCGVEvtsmkameDLGRANRRKPKPPAPEDL---AVICFTSGTTGNPKGAMVTHRNivsd 262
Cdd:PRK03640 99 EVKCLITDDDFEAKLIP-GISVKFA--------ELMNGPKEEAEIQEEFDLdevATIMYTSGTTGKPKGVIQTYGN---- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 263 csAFVKATENTVNP--CPDDTLISFLPLAH------MFERVVE-CVMLCH----GAKIgffqgdIRLLMDDlKVlqpTVF 329
Cdd:PRK03640 166 --HWWSAVGSALNLglTEDDCWLAAVPIFHisglsiLMRSVIYgMRVVLVekfdAEKI------NKLLQTG-GV---TII 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 330 PVVPRLLNRMFDRIfGQANTtlkrwlldfaskrkeaelrsgiirNNSLwdrlifhkvqsslggrvRLMVTGAAPVSATVL 409
Cdd:PRK03640 234 SVVSTMLQRLLERL-GEGTY------------------------PSSF-----------------RCMLLGGGPAPKPLL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 410 TFLRAAlGCQFYEGYGQTEcTAGCCLTMPGDWTA---GHVGAPM-PCNlIKLVDveEMNYMAAEGEGEVCVKGPNVFQGY 485
Cdd:PRK03640 272 EQCKEK-GIPVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLfPCE-LKIEK--DGVVVPPFEEGEIVVKGPNVTKGY 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 486 LKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQ----- 560
Cdd:PRK03640 347 LNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDkwgqv 424
|
410 420
....*....|....*....|...
gi 557878740 561 --AFLIAIVVPDVETLCSWAQKR 581
Cdd:PRK03640 425 pvAFVVKSGEVTEEELRHFCEEK 447
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
89-660 |
7.29e-21 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 98.00 E-value: 7.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 89 VTTLYEGFQRGIQVSNNGPCLGSRKPDQPYEWLSY--------------------------------KQWVIIEQGCFAY 136
Cdd:PTZ00297 426 VRSLGEMWERSVTRHSTFRCLGQTSESGESEWLTYgtvdararelgsgllalgvrpgdvigvdceasRNIVILEVACALY 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 137 SMVIVPLYDTlgNEAITYIVNKAELSLVFVDKPEKAKLL------LEGVENklipglkiivVMDAYGSELVERGQRCGVE 210
Cdd:PTZ00297 506 GFTTLPLVGK--GSTMRTLIDEHKIKVVFADRNSVAAILtcrsrkLETVVY----------THSFYDEDDHAVARDLNIT 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 211 VTSMKAMEDLGRANRRKPKPPAPED----LAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVkATENTVNPCPDDTLISFL 286
Cdd:PTZ00297 574 LIPYEFVEQKGRLCPVPLKEHVTTDtvftYVVDNTTSASGDGLAVVRVTHADVLRDISTLV-MTGVLPSSFKKHLMVHFT 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 287 PLAHMFERVVECVMLCHGAKIGffQGDIRLLMDDLKVLQPTVFPVVPRLlnrmfdriFGQANTTLKR----------WLL 356
Cdd:PTZ00297 653 PFAMLFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSL--------FSTSRLQLSRanerysavysWLF 722
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 357 DfaskrKEAELRSGII---RNNSLWDRLIFHK-VQSSLGGRVRLMVTGAAPVSATvltflraalgcqfyegYGQTECTAG 432
Cdd:PTZ00297 723 E-----RAFQLRSRLInihRRDSSLLRFIFFRaTQELLGGCVEKIVLCVSEESTS----------------FSLLEHISV 781
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 433 CCltmpgdwtaghvgapMPCnliklvdVEEMNYMAAEGEgeVCVKG---PNVfQGYLK---DPAKTAE----ALDKDGWL 502
Cdd:PTZ00297 782 CY---------------VPC-------LREVFFLPSEGV--FCVDGtpaPSL-QVDLEpfdEPSDGAGigqlVLAKKGEP 836
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 503 -HTGDIG-KWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAfLIAIVVPDVETL-CSWAQ 579
Cdd:PTZ00297 837 rRTLPIAaQWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVeFEWRQ 915
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 580 KRGFE---GSFEELCRNKDVKKA---ILEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRS 653
Cdd:PTZ00297 916 SHCMGeggGPARQLGWTELVAYAsslLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSS 995
|
....*..
gi 557878740 654 QIDDLYS 660
Cdd:PTZ00297 996 VIERFYS 1002
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
234-542 |
7.64e-21 |
|
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: 94.25 E-value: 7.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 234 EDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNpcpDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGD 313
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVV---GDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 314 IRL--LMDDLKVLQPTVFPVVPRLLNRMFDrifgqanttlkrwlldfaskrkeaELRSGIIRNNSLwdRLIfhkvqsslg 391
Cdd:cd17635 78 TTYksLFKILTTNAVTTTCLVPTLLSKLVS------------------------ELKSANATVPSL--RLI--------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 392 grvrlMVTGAAPVSATVLTFLRAALgCQFYEGYGQTECTAGCCL-TMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAeG 470
Cdd:cd17635 123 -----GYGGSRAIAADVRFIEATGL-TNTAQVYGLSETGTALCLpTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSA-S 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557878740 471 EGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 542
Cdd:cd17635 196 FGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERI 265
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
219-569 |
9.88e-21 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 96.11 E-value: 9.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 219 DLGRANRRKPKPPAPEDL----AVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFER 294
Cdd:PRK05852 157 HLDAATEPTPATSTPEGLrpddAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLS----PRDATVAVMPLYHGHGL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 295 VVECV-MLCHGAKI-----GFFQGdiRLLMDDLKVLQPTVFPVVPrllnrmfdrifgqantTLKRWLLDFA----SKRKE 364
Cdd:PRK05852 233 IAALLaTLASGGAVllparGRFSA--HTFWDDIKAVGATWYTAVP----------------TIHQILLERAatepSGRKP 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 365 AELRsgIIRNNSlwdrlifhkvqsslggrvrlmvtgaAPVSATVLTFLRAALGCQFYEGYGQTECT----------AGCC 434
Cdd:PRK05852 295 AALR--FIRSCS-------------------------APLTAETAQALQTEFAAPVVCAFGMTEAThqvtttqiegIGQT 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 435 LTmPGDWT--AGHVGAPMpcnlIKLVDVEEMNYMAAEgEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLP 512
Cdd:PRK05852 348 EN-PVVSTglVGRSTGAQ----IRIVGSDGLPLPAGA-VGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSA 420
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 513 NGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPVAQVFVHGESLQAF---LIAIVVP 569
Cdd:PRK05852 421 AGDLSIRGRIKELINRG-GEKISPERVEGVLASHPNVMEAAVFGVPDQLYgeaVAAVIVP 479
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
221-542 |
1.06e-20 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 97.34 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 221 GRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDC---SAFVKATentvnpcPDDTLISFLPLAHMFervve 297
Cdd:PRK06814 780 GRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRaqvAARIDFS-------PEDKVFNALPVFHSF----- 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 298 cvmlchgakiGFFQGDIRLLMDDLKVL---QPTVFPVVPRLLnrmFDR----IFGqANTTLKRWL-----LDFASkrkea 365
Cdd:PRK06814 848 ----------GLTGGLVLPLLSGVKVFlypSPLHYRIIPELI---YDTnatiLFG-TDTFLNGYAryahpYDFRS----- 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 366 elrsgiirnnslwdrlifhkvqsslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGH 445
Cdd:PRK06814 909 ----------------------------LRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGT 960
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 446 VGAPMPCNLIKLVDVEEMNymaaEGeGEVCVKGPNVFQGYLK-DPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKH 524
Cdd:PRK06814 961 VGRLLPGIEYRLEPVPGID----EG-GRLFVRGPNVMLGYLRaENPGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKR 1034
|
330
....*....|....*...
gi 557878740 525 IFKLAqGEYIAPEKIENI 542
Cdd:PRK06814 1035 FAKIA-GEMISLAAVEEL 1051
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
225-551 |
2.36e-20 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 95.55 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 225 RRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDTLISFLPLAHMFervvecvmlchG 304
Cdd:PRK08043 356 RLAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLL----ANVEQIKTIADFTPNDRFMSALPLFHSF-----------G 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 305 AKIGFFQGdirlLMDDLKVL---QPTVFPVVPRLLnrmFDR----IFGQAnTTLKRWL-----LDFAskrkeaelrsgii 372
Cdd:PRK08043 421 LTVGLFTP----LLTGAEVFlypSPLHYRIVPELV---YDRnctvLFGTS-TFLGNYArfanpYDFA------------- 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 373 rnnslwdrlifhkvqsslggRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPC 452
Cdd:PRK08043 480 --------------------RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPG 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 453 NLIKLVDVEEMnymaaEGEGEVCVKGPNVFQGYLK--DP-------AKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK 523
Cdd:PRK08043 540 MDARLLSVPGI-----EQGGRLQLKGPNIMNGYLRveKPgvlevptAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAK 614
|
330 340
....*....|....*....|....*...
gi 557878740 524 HIFKLAqGEYIAPEKIENIYMRSEPVAQ 551
Cdd:PRK08043 615 RFAKIA-GEMVSLEMVEQLALGVSPDKQ 641
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
139-556 |
2.85e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 94.57 E-value: 2.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 139 VIVPLYDTLGNEAITYIVNKAELSLVFVDKpekaklllegvENKLIPGLKI-IVVMDAYGSELVERGQRCGVEVTSMKam 217
Cdd:PRK06145 78 VFLPINYRLAADEVAYILGDAGAKLLLVDE-----------EFDAIVALETpKIVIDAAAQADSRRLAQGGLEIPPQA-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 218 edlgranrrkpkPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVnpcpDDTLISFLPLAHmferVVE 297
Cdd:PRK06145 145 ------------AVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTA----SERLLVVGPLYH----VGA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 298 C-----VMLCHGAKIGFFQG-DIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanTTLKRWLLDFASKRkeaelrsgi 371
Cdd:PRK06145 205 FdlpgiAVLWVGGTLRIHREfDPEAVLAAIERHRLTCAWMAPVMLSRVL--------TVPDRDRFDLDSLA--------- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 372 irnnslWdrlifhkvqsSLGGrvrlmvtGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDW--TAGHVGAP 449
Cdd:PRK06145 268 ------W----------CIGG-------GEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREieKIGSTGRA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 450 MPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLA 529
Cdd:PRK06145 325 LAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMI-IS 401
|
410 420
....*....|....*....|....*..
gi 557878740 530 QGEYIAPEKIENIYMRSEPVAQVFVHG 556
Cdd:PRK06145 402 GGENIASSEVERVIYELPEVAEAAVIG 428
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
186-549 |
2.89e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 94.68 E-value: 2.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 186 GLKIIVV---MDAYGSELVERGQRcGVEVTSMKAMEDLgranrrKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSD 262
Cdd:PRK07768 108 GAKAVVVgepFLAAAPVLEEKGIR-VLTVADLLAADPI------DPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYAN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 263 CSAFVKATENTVNpcpDDTLISFLPLAH-MfervvecvmlchgAKIGFFQGDIRLLMDDLKVlQPTVFPVVPRLLNRMFD 341
Cdd:PRK07768 181 AEAMFVAAEFDVE---TDVMVSWLPLFHdM-------------GMVGFLTVPMYFGAELVKV-TPMDFLRDPLLWAELIS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 342 RIFGQ-------ANTTLKRwLLDFASKRKEAELrsgiirnnslwdrlifhkvqSSLggrvRLMVTGAAPVS-ATVLTFLR 413
Cdd:PRK07768 244 KYRGTmtaapnfAYALLAR-RLRRQAKPGAFDL--------------------SSL----RFALNGAEPIDpADVEDLLD 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 414 A---------ALGCqfyeGYGQTECTAGCCLTMPGD--------------------WTAGHV------GAPMPCNLIKLV 458
Cdd:PRK07768 299 AgarfglrpeAILP----AYGMAEATLAVSFSPCGAglvvdevdadllaalrravpATKGNTrrlatlGPPLPGLEVRVV 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 459 DvEEMNYMAAEGEGEVCVKGPNVFQGYLkDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEK 538
Cdd:PRK07768 375 D-EDGQVLPPRGVGVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPTD 451
|
410
....*....|.
gi 557878740 539 IENIYMRSEPV 549
Cdd:PRK07768 452 IERAAARVEGV 462
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
150-592 |
9.36e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 93.09 E-value: 9.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 150 EAITYIVNKAELSLVFVDkPEKAKLLLEGVEnkLIPGLKIIVV---MDAYGselveRGQRCG-VEVTSMKAMEDLGRAnr 225
Cdd:PRK08162 105 ASIAFMLRHGEAKVLIVD-TEFAEVAREALA--LLPGPKPLVIdvdDPEYP-----GGRFIGaLDYEAFLASGDPDFA-- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 226 rkPKPPAPE-DLAVICFTSGTTGNPKGAMVTHRnivsdcSAFVKATENTV--NPCPDDTLISFLPLAHmfervveCVMLC 302
Cdd:PRK08162 175 --WTLPADEwDAIALNYTSGTTGNPKGVVYHHR------GAYLNALSNILawGMPKHPVYLWTLPMFH-------CNGWC 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 303 H--------GAKIGFFQGDIRLLMDDLKVLQPTVF---PVVPRLLnrmfdrifgqANTtlkrwlldfaskrkEAELRSGI 371
Cdd:PRK08162 240 FpwtvaaraGTNVCLRKVDPKLIFDLIREHGVTHYcgaPIVLSAL----------INA--------------PAEWRAGI 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 372 irnnslwdrlifhkvqsslGGRVRLMVTGAAPVSAtVLTFLRAAlGCQFYEGYGQTEC--TAGCCLTMPGdWTA------ 443
Cdd:PRK08162 296 -------------------DHPVHAMVAGAAPPAA-VIAKMEEI-GFDLTHVYGLTETygPATVCAWQPE-WDAlplder 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 444 ----GHVGAPMPC-NLIKLVDVEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTL 516
Cdd:PRK08162 354 aqlkARQGVRYPLqEGVTVLDPDTMQPVPADGEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYI 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 517 KIIDRKKHIFkLAQGEYIAPEKIENIYMRsepvaqvfvHgeslQAFLIAIVV--PDV---ETLCSWAQ-KRGFEGSFEEL 590
Cdd:PRK08162 433 KIKDRSKDII-ISGGENISSIEVEDVLYR---------H----PAVLVAAVVakPDPkwgEVPCAFVElKDGASATEEEI 498
|
....*
gi 557878740 591 ---CR 592
Cdd:PRK08162 499 iahCR 503
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
233-570 |
1.45e-19 |
|
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: 92.39 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 233 PEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATENTVNPCPDDTLISFLPLAhmFERVVECVM--LCHGAKIgff 310
Cdd:cd17655 136 SDDLAYVIYTSGSTGKPKGVMIEHRGVVN----LVEWANKVIYQGEHLRVALFASIS--FDASVTEIFasLLSGNTL--- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 311 qgdirllmddLKVLQPTVFPVVPrllnrmFDRIFGQANTTLkrwlldfaSKRKEAELRsgiirnnslwdrlIFHKVQSSL 390
Cdd:cd17655 207 ----------YIVRKETVLDGQA------LTQYIRQNRITI--------IDLTPAHLK-------------LLDAADDSE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 391 GGRVRLMVTGAAPVSATVLTFL--RAALGCQFYEGYGQTECTAGCC--LTMPGDWTAGHV--GAPMPCNLIKLVDvEEMN 464
Cdd:cd17655 250 GLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETTVDASiyQYEPETDQQVSVpiGKPLGNTRIYILD-QYGR 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 465 YMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 538
Cdd:cd17655 329 PQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-RGYRIELGE 407
|
330 340 350
....*....|....*....|....*....|....*
gi 557878740 539 IENIYMRSEPVAQ--VFVH-GESLQAFLIAIVVPD 570
Cdd:cd17655 408 IEARLLQHPDIKEavVIARkDEQGQNYLCAYIVSE 442
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
132-569 |
3.42e-19 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 91.38 E-value: 3.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 132 GCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVfVDKPEKAKLLLEGvenklIPGLKIIVVMDAYGSELVERGQRCGVEV 211
Cdd:TIGR03098 69 GAALAGGVFVPINPLLKAEQVAHILADCNVRLL-VTSSERLDLLHPA-----LPGCHDLRTLIIVGDPAHASEGHPGEEP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 212 TSMKAMEDLGRANRrkPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAhm 291
Cdd:TIGR03098 143 ASWPKLLALGDADP--PHPVIDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENR----PDDRLLAVLPLS-- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 292 fervvecvmlchgakigffqgdirllmddlkvlqptvfpvvprllnrmFDRIFGQANTTL----KRWLLDFASKRK---- 363
Cdd:TIGR03098 215 ------------------------------------------------FDYGFNQLTTAFyvgaTVVLHDYLLPRDvlka 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 364 -EAELRSGIIRNNSLWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALG-CQFYEGYGQTECTAGCCLTmPG-- 439
Cdd:TIGR03098 247 lEKHGITGLAAVPPLWAQLAQLDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPnARLFLMYGLTEAFRSTYLP-PEev 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 440 DWTAGHVGAPMPcNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDK----DGWLH-------TGDIG 508
Cdd:TIGR03098 326 DRRPDSIGKAIP-NAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPlppfPGELHlpelavwSGDTV 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 557878740 509 KWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPVAQVFVHG----ESLQAfLIAIVVP 569
Cdd:TIGR03098 405 RRDEEGFLYFVGRRDEMIKTS-GYRVSPTEVEEVAYATGLVAEAVAFGvpdpTLGQA-IVLVVTP 467
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
216-592 |
7.05e-19 |
|
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: 90.59 E-value: 7.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 216 AMEDLGRANRRKPKP-PAPEDLAVICFTSGTTGNPKGAMVTHRNIVsdCSAFVKATENTVNPcpDDTLISFLPLAHMFer 294
Cdd:COG1021 165 SLDALLAAPADLSEPrPDPDDVAFFQLSGGTTGLPKLIPRTHDDYL--YSVRASAEICGLDA--DTVYLAALPAAHNF-- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 295 vvecVMLCHGAkIGFFQ--GDIRL-----------LMDDLKVlqpTVFPVVPRLLNRMfdrifgqanttlkrwlLDFASK 361
Cdd:COG1021 239 ----PLSSPGV-LGVLYagGTVVLapdpspdtafpLIERERV---TVTALVPPLALLW----------------LDAAER 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 362 RKeAELrsgiirnnslwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctaG-CCLTMPGD 440
Cdd:COG1021 295 SR-YDL--------------------SSL----RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---GlVNYTRLDD 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 441 ---WTAGHVGAPM-PCNLIKLVDVEEMNymAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGT 515
Cdd:COG1021 347 peeVILTTQGRPIsPDDEVRIVDEDGNP--VPPGEvGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGY 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 516 LKIIDRKK-HIFKlaQGEYIAPEKIENIYMRSEPVAQVfvhgeslqafliAIV-VPDV---ETLCSWAQKRGFEGSFEEL 590
Cdd:COG1021 425 LVVEGRAKdQINR--GGEKIAAEEVENLLLAHPAVHDA------------AVVaMPDEylgERSCAFVVPRGEPLTLAEL 490
|
..
gi 557878740 591 CR 592
Cdd:COG1021 491 RR 492
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
198-592 |
3.26e-18 |
|
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: 87.95 E-value: 3.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 198 SELVERGQRCGV-----------------EVTSMKAMEDLGRANRR----KPKPPAPEDLAVICFTSGTTGNPKGAMVTH 256
Cdd:cd05923 93 AELIERGEMTAAviavdaqvmdaifqsgvRVLALSDLVGLGEPESAgpliEDPPREPEQPAFVFYTSGTTGLPKGAVIPQ 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 257 RNIVSdcSAFVKATENTVNPCPDDTLISFLPLAHMfervvecvmlchgakIGFFQgdirLLMDDLkVLQPTVFPVvprll 336
Cdd:cd05923 173 RAAES--RVLFMSTQAGLRHGRHNVVLGLMPLYHV---------------IGFFA----VLVAAL-ALDGTYVVV----- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 337 nRMFDRIFgqanttlkrwlldfASKRKEAELRSGIIRNNSLWDRLIFHKVQSSLG-GRVRLMVTGAAPVSATVLTFLRAA 415
Cdd:cd05923 226 -EEFDPAD--------------ALKLIEQERVTSLFATPTHLDALAAAAEFAGLKlSSLRHVTFAGATMPDAVLERVNQH 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 416 LGCQFYEGYGQTEctAGCCLTMPgDWTAGHVGAPMPCNLIKLVDV-EEMNYMAAEG-EGEVCVK--GPNVFQGYLKDPAK 491
Cdd:cd05923 291 LPGEKVNIYGTTE--AMNSLYMR-DARTGTEMRPGFFSEVRIVRIgGSPDEALANGeEGELIVAaaADAAFTGYLNQPEA 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 492 TAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG---ESLQAFLIAIVV 568
Cdd:cd05923 368 TAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIGvadERWGQSVTACVV 445
|
410 420
....*....|....*....|....
gi 557878740 569 PDVETLCswaqkrgfEGSFEELCR 592
Cdd:cd05923 446 PREGTLS--------ADELDQFCR 461
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
233-549 |
3.65e-18 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 87.93 E-value: 3.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 233 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVnpcpDDTLISFLPLAHMFErvvecVMLCHGAKIgfFQG 312
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKT----KDRILSWMPLTHDMG-----LIAFHLAPL--IAG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 313 DIRLLMddlkvlqPT-VFPVVPRLlnrmfdrifgqanttlkrWLLDfASKRKEAELRSGIIRNNSLWDRLIFHKVQSSLG 391
Cdd:cd05908 174 MNQYLM-------PTrLFIRRPIL------------------WLKK-ASEHKATIVSSPNFGYKYFLKTLKPEKANDWDL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 392 GRVRLMVTGAAPVSAT---VLTFLRAALGCQ---FYEGYGQTECTAGCCL----------------------------TM 437
Cdd:cd05908 228 SSIRMILNGAEPIDYElchEFLDHMSKYGLKrnaILPVYGLAEASVGASLpkaqspfktitlgrrhvthgepepevdkKD 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 438 PGDWTAGHVGAPMPCNLIKLVDveEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGkWLPNGTL 516
Cdd:cd05908 308 SECLTFVEVGKPIDETDIRICD--EDNKILPDGYiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIRNGRL 384
|
330 340 350
....*....|....*....|....*....|...
gi 557878740 517 KIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPV 549
Cdd:cd05908 385 VITGREKDII-FVNGQNVYPHDIERIAEELEGV 416
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
223-572 |
3.83e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 88.09 E-value: 3.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 223 ANRRKPKP--PAPEDLAVICFTSGTTGNPKGAMVTHRNIVsdCSAFVKATENTVNPcpDDTLISFLPLAHmferVVECVM 300
Cdd:PRK08314 177 AAGLAPPPhtAGPDDLAVLPYTSGTTGVPKGCMHTHRTVM--ANAVGSVLWSNSTP--ESVVLAVLPLFH----VTGMVH 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 301 LCHGAkigFFQGDIRLLMddlkvlqptvfP-----VVPRLLNRMfdRI-FGQANTTLkrwLLDFaskrkeaeLRSGIIRN 374
Cdd:PRK08314 249 SMNAP---IYAGATVVLM-----------PrwdreAAARLIERY--RVtHWTNIPTM---VVDF--------LASPGLAE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 375 NSLwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAG-----------CCLTMPgdwTA 443
Cdd:PRK08314 302 RDL----------SSL----RYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTETMAQthsnppdrpklQCLGIP---TF 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 444 GhVGApmpcnliKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEA---LDKDGWLHTGDIGKWLPNGTLKIID 520
Cdd:PRK08314 365 G-VDA-------RVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITD 436
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 557878740 521 RKKHIFKlAQGEYIAPEKIENIYMRSEPVAQVFV-------HGESLQAFliaiVVPDVE 572
Cdd:PRK08314 437 RLKRMIN-ASGFKVWPAEVENLLYKHPAIQEACViatpdprRGETVKAV----VVLRPE 490
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
208-570 |
4.92e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 89.25 E-value: 4.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 208 GVEVTSMKAMEDLGRANRRKPKPP-APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFL 286
Cdd:PRK12316 2119 GVARLPLDRDAEWADYPDTAPAVQlAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELS----PADCELQFM 2194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 287 PLAhmFERVVECVM--LCHGAkigffqgdiRLLMDDLKVLQPtvfpvvprllNRMFDRIFGQANTtlkrwLLDFASkrke 364
Cdd:PRK12316 2195 SFS--FDGAHEQWFhpLLNGA---------RVLIRDDELWDP----------EQLYDEMERHGVT-----ILDFPP---- 2244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 365 aelrsgiirnnSLWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQF-YEGYGQTECTA-----GCCLTMP 438
Cdd:PRK12316 2245 -----------VYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVYlFNGYGPTEAVVtpllwKCRPQDP 2313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 439 GDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLH-------TGDIGKWL 511
Cdd:PRK12316 2314 CGAAYVPIGRALGNRRAYILD-ADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSAsgerlyrTGDLARYR 2392
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557878740 512 PNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFV---HGESLQAfLIAIVVPD 570
Cdd:PRK12316 2393 ADGVVEYLGRIDHQVKI-RGFRIELGEIEARLQAHPAVREAVVvaqDGASGKQ-LVAYVVPD 2452
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
139-564 |
6.14e-18 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 87.43 E-value: 6.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 139 VIVPLYDTLGNEAITYIVNKAELSLVfVDKPEKAKLLLEGVENKLIPgLKIIVVMDAYGSElvERGqrcgveVTSMKAME 218
Cdd:PRK08008 88 IMVPINARLLREESAWILQNSQASLL-VTSAQFYPMYRQIQQEDATP-LRHICLTRVALPA--DDG------VSSFTQLK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 219 DLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSdcSAFVKATENTVNPcpDDTLISFLPLAHM-FERVVE 297
Cdd:PRK08008 158 AQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRF--AGYYSAWQCALRD--DDVYLTVMPAFHIdCQCTAA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 298 CVMLCHGAKIGF--------FQGDIRLLmddlkvlQPTVFPVVPRLLNRM-------FDRifgqaNTTLKRWL--LDFAS 360
Cdd:PRK08008 234 MAAFSAGATFVLlekysaraFWGQVCKY-------RATITECIPMMIRTLmvqppsaNDR-----QHCLREVMfyLNLSD 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 361 KRKEA-ELRSGiirnnslwdrlifhkvqsslggrVRLMVTgaapvsatvltflraalgcqfyegYGQTECTAGCCLTMPG 439
Cdd:PRK08008 302 QEKDAfEERFG-----------------------VRLLTS------------------------YGMTETIVGIIGDRPG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 440 D---WTAghVGAPMPCNLIKLVDveEMNYMAAEGE-GEVCVKG---PNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLP 512
Cdd:PRK08008 335 DkrrWPS--IGRPGFCYEAEIRD--DHNRPLPAGEiGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDE 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 557878740 513 NGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPVAQVFVHG-------ESLQAFLI 564
Cdd:PRK08008 411 EGFFYFVDRRCNMIKRG-GENVSCVELENIIATHPKIQDIVVVGikdsirdEAIKAFVV 468
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
198-571 |
7.23e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 88.68 E-value: 7.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 198 SELVERGQRC-GVEVTSMKAMEDL--GRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATENTV 274
Cdd:PRK12467 617 SHLLAQLPVPaGLRSLCLDEPADLlcGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALAN----YVCVIAERL 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 275 NPCPDDTLISFLPLAHMFERVVECVMLCHGAKIgffqgdirLLMDDLKVLQPTVFpvvprllnrmFDRIFGQANTTLKRw 354
Cdd:PRK12467 693 QLAADDSMLMVSTFAFDLGVTELFGALASGATL--------HLLPPDCARDAEAF----------AALMADQGVTVLKI- 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 355 lldfaskrkeaelrsgiirNNSLWDRLIFHKVQSSLGGRVRLMVTGAA-PVSATVLTFlRAALGCQFYEGYGQTECTAGC 433
Cdd:PRK12467 754 -------------------VPSHLQALLQASRVALPRPQRALVCGGEAlQVDLLARVR-ALGPGARLINHYGPTETTVGV 813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 434 ----CLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKD------GWLH 503
Cdd:PRK12467 814 styeLSDEERDFGNVPIGQPLANLGLYILD-HYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDpfgadgGRLY 892
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557878740 504 -TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFV--HGESLQAFLIAIVVPDV 571
Cdd:PRK12467 893 rTGDLARYRADGVIEYLGRMDHQVKI-RGFRIELGEIEARLLAQPGVREAVVlaQPGDAGLQLVAYLVPAA 962
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
233-583 |
1.10e-17 |
|
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: 85.98 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 233 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPcpddtlISFLPLAHMFERVVE---CVMLCHGAKIGF 309
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFP------VRLLQMASFSFDVFAgdfARSLLNGGTLVI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 310 FQGDIRL----LMDDLKVLQPTVFPVVPrllnrmfdrifgqantTLKRWLLDFASKRKE--AELRSGIIRNNSLWDRLiF 383
Cdd:cd17650 166 CPDEVKLdpaaLYDLILKSRITLMESTP----------------ALIRPVMAYVYRNGLdlSAMRLLIVGSDGCKAQD-F 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 384 HKVQSSLGGRVRLmvtgaapVSATVLTflRAALGCQFYEGYGQTECTAGcclTMPgdwtaghVGAPMPCNLIKLVDvEEM 463
Cdd:cd17650 229 KTLAARFGQGMRI-------INSYGVT--EATIDSTYYEEGRDPLGDSA---NVP-------IGRPLPNTAMYVLD-ERL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 464 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPE 537
Cdd:cd17650 289 QPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI-RGFRIELG 367
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 557878740 538 KIENIYMRSEPVAQVFV---HGESLQAFLIAIVVPDVETlcSWAQKRGF 583
Cdd:cd17650 368 EIESQLARHPAIDEAVVavrEDKGGEARLCAYVVAAATL--NTAELRAF 414
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
134-556 |
1.11e-17 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 86.78 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 134 FAYSM--------VIVPLYDTLGNEAITYIVNKAELSLVFVDKpekAKLLLEGVEnKLIPGLKIIVVMDAYGSELVErgQ 205
Cdd:cd05970 85 FWYSLlalhklgaIAIPATHQLTAKDIVYRIESADIKMIVAIA---EDNIPEEIE-KAAPECPSKPKLVWVGDPVPE--G 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 206 RCGVEVTSMKAMEDLGRanRRKPKPPAPEDLAVICFTSGTTGNPKgaMVTHRNIvsdcsafvkatentvnpcpddtlisf 285
Cdd:cd05970 159 WIDFRKLIKNASPDFER--PTANSYPCGEDILLVYFSSGTTGMPK--MVEHDFT-------------------------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 286 LPLAHMFErvvecVMLCHGAKigffQGDIRLLMDDLKVLQPtvfpvvprllnrMFDRIFGQANTTLKRWLLDFasKRKEA 365
Cdd:cd05970 209 YPLGHIVT-----AKYWQNVR----EGGLHLTVADTGWGKA------------VWGKIYGQWIAGAAVFVYDY--DKFDP 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 366 ELRSGIIRNN---------SLWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAgCCLT 436
Cdd:cd05970 266 KALLEKLSKYgvttfcappTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTL-TIAT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 437 MPG-DWTAGHVGAPMPCNLIKLVDVEEMNYMAAEgEGEVCV---KGPNV--FQGYLKDPAKTAEALdKDGWLHTGDIGKW 510
Cdd:cd05970 345 FPWmEPKPGSMGKPAPGYEIDLIDREGRSCEAGE-EGEIVIrtsKGKPVglFGGYYKDAEKTAEVW-HDGYYHTGDAAWM 422
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 557878740 511 LPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQVFVHG 556
Cdd:cd05970 423 DEDGYLWFVGRTDDLIK-SSGYRIGPFEVESALIQHPAVLECAVTG 467
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
233-573 |
2.55e-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: 85.05 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 233 PEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDTLISFLPLAHMFErVVEcvM---LCHGAKIGF 309
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHANVL----ALFAATQRWFGFNEDDVWTLFHSYAFDFS-VWE--IwgaLLHGGRLVV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 310 FQGDIRLLMDDLkvlqptvfpvvPRLLNRMFDRIFGQANTTLKRWLldfaskrkEAELRsgiirnnslwdrliFHKVQSS 389
Cdd:cd17643 165 VPYEVARSPEDF-----------ARLLRDEGVTVLNQTPSAFYQLV--------EAADR--------------DGRDPLA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 390 LggrvRLMVTGAAPVSATVLTFLRAALGC---QFYEGYGQTECTAGCCL-----TMPGDWTAGHVGAPMPCNLIKLVDvE 461
Cdd:cd17643 212 L----RYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFrpldaADLPAAAASPIGRPLPGLRVYVLD-A 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 462 EMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAE-------ALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 534
Cdd:cd17643 287 DGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI-RGFRI 365
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 557878740 535 APEKIENIYMRSEPVAQVFV---HGESLQAFLIAIVVPDVET 573
Cdd:cd17643 366 ELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVADDGA 407
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
139-556 |
3.04e-17 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 85.60 E-value: 3.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 139 VIVPLYDTLGNEAITYIVNKAELSLVFVDkPEKAKLLLEGVENklIPGLKIIVVMDAYGSELVERGQRCGVEVTSMKAME 218
Cdd:PRK05620 90 VFNPLNKQLMNDQIVHIINHAEDEVIVAD-PRLAEQLGEILKE--CPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 219 DlGRANRRkPKPPAPEDLAV-ICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNpcPDDTLISFLPLAHmfervve 297
Cdd:PRK05620 167 D-GRSTVY-DWPELDETTAAaICYSTGTTGAPKGVVYSHRSLYLQSLSLRTTDSLAVT--HGESFLCCVPIYH------- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 298 cvMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVprllnrmfdrifgqaNTTLKRwlldfaskrkeaeLRSGIirnNSL 377
Cdd:PRK05620 236 --VLSWGVPLAAFMSGTPLVFPGPDLSAPTLAKII---------------ATAMPR-------------VAHGV---PTL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 378 WDRLIFHKVQSSlGGRVRL--MVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAP------ 449
Cdd:PRK05620 283 WIQLMVHYLKNP-PERMSLqeIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEARWAyrvsqg 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 450 -MPCNLIKLVdVEEMNYMAA--EGEGEVCVKGPNVFQGYLKDPAKT----------------AEALDKDGWLHTGDIGKW 510
Cdd:PRK05620 362 rFPASLEYRI-VNDGQVMEStdRNEGEIQVRGNWVTASYYHSPTEEgggaastfrgedvedaNDRFTADGWLRTGDVGSV 440
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 557878740 511 LPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQVFVHG 556
Cdd:PRK05620 441 TRDGFLTIHDRARDVIR-SGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
233-581 |
1.10e-16 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 83.07 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 233 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAhmFERVV-ECVM-LCHGAkigff 310
Cdd:cd17652 92 PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVG----PGSRVLQFASPS--FDASVwELLMaLLAGA----- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 311 qgdiRLLMDDLKVLQPtvfpvvprllnrmfdrifGQAnttlkrwLLDFaskrkeaelrsgiirnnsLWDRLIFHKVQS-- 388
Cdd:cd17652 161 ----TLVLAPAEELLP------------------GEP-------LADL------------------LREHRITHVTLPpa 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 389 --------SLGGRVRLMVTGAAPVSATVLtflRAALGCQFYEGYGQTECTAgcCLTMPGDWTAGHV---GAPMPCNLIKL 457
Cdd:cd17652 194 alaalppdDLPDLRTLVVAGEACPAELVD---RWAPGRRMINAYGPTETTV--CATMAGPLPGGGVppiGRPVPGTRVYV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 458 VDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQ 530
Cdd:cd17652 269 LD-ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKI-R 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 531 GEYIAPEKIENIYMRSEPVAQ--VFVHGESL-QAFLIAIVV------PDVETLCSWAQKR 581
Cdd:cd17652 347 GFRIELGEVEAALTEHPGVAEavVVVRDDRPgDKRLVAYVVpapgaaPTAAELRAHLAER 406
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
134-604 |
1.35e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 83.53 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 134 FAYSM---VIVPLYDTLGNEAITYIVNKAELSLVFVDKP-----EKAKLLLEGVENKLIPGLKIIVVMD----AYGSE-- 199
Cdd:PLN03102 82 FAVPMagaVLNPINTRLDATSIAAILRHAKPKILFVDRSfeplaREVLHLLSSEDSNLNLPVIFIHEIDfpkrPSSEEld 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 200 ---LVERGQRCGVEVTSMKAMEDlgranrrkpkppaPEDLAVICFTSGTTGNPKGAMVTHRNI-VSDCSAFVKATENTvn 275
Cdd:PLN03102 162 yecLIQRGEPTPSLVARMFRIQD-------------EHDPISLNYTSGTTADPKGVVISHRGAyLSTLSAIIGWEMGT-- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 276 pCPddTLISFLPLAHmfervvecvmlCHGAKIGF---FQGDIRLLMDdlKVLQPTVFPVVprllnRMFDRIFGQANTTLK 352
Cdd:PLN03102 227 -CP--VYLWTLPMFH-----------CNGWTFTWgtaARGGTSVCMR--HVTAPEIYKNI-----EMHNVTHMCCVPTVF 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 353 RWLLdfaskrkeaelrsgiiRNNSLwdrlifhkVQSSLGGRVRLMVTGAAPVSATVLTFLRaaLGCQFYEGYGQTECTAG 432
Cdd:PLN03102 286 NILL----------------KGNSL--------DLSPRSGPVHVLTGGSPPPAALVKKVQR--LGFQVMHAYGLTEATGP 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 433 CCLTMPGD-WT------AGHVGAPMPCNLIKLVDVEEMNYMAAEGE-------GEVCVKGPNVFQGYLKDPAKTAEALdK 498
Cdd:PLN03102 340 VLFCEWQDeWNrlpenqQMELKARQGVSILGLADVDVKNKETQESVprdgktmGEIVIKGSSIMKGYLKNPKATSEAF-K 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 499 DGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIymrsepvaqVFVHGESLQAFLIAIVVPDV-ETLCSW 577
Cdd:PLN03102 419 HGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVENV---------LYKYPKVLETAVVAMPHPTWgETPCAF 488
|
490 500 510
....*....|....*....|....*....|..
gi 557878740 578 -AQKRGFEGSFEE----LCRNKDVKKAILEDM 604
Cdd:PLN03102 489 vVLEKGETTKEDRvdklVTRERDLIEYCRENL 520
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
208-570 |
1.79e-16 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 82.71 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 208 GVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSD----CSAFVKATENTV---NPCPDD 280
Cdd:cd17646 112 GGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRllwmQDEYPLGPGDRVlqkTPLSFD 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 281 TLIS--FLPLAHMfERVVECVMLCHGaKIGFFQGdirlLMDDLKVlqpTVFPVVPRLLnrmfdRIFGQanttlkrwlldf 358
Cdd:cd17646 192 VSVWelFWPLVAG-ARLVVARPGGHR-DPAYLAA----LIREHGV---TTCHFVPSML-----RVFLA------------ 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 359 askrkeaELRSGIIRNnslwdrlifhkvqsslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCL-TM 437
Cdd:cd17646 246 -------EPAAGSCAS-------------------LRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHwPV 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 438 PGDWTAGHV--GAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLH------TGDIGK 509
Cdd:cd17646 300 RGPAETPSVpiGRPVPNTRLYVLD-DALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLAR 378
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557878740 510 WLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFV---HGESLQAFLIAIVVPD 570
Cdd:cd17646 379 WRPDGALEFLGRSDDQVKI-RGFRVEPGEIEAALAAHPAVTHAVVvarAAPAGAARLVGYVVPA 441
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
232-569 |
1.99e-16 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 82.42 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 232 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAhmFERVVECVM--LCHGAkigf 309
Cdd:cd17649 92 HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLT----PGDRELQFASFN--FDGAHEQLLppLICGA---- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 310 fqgdiRLLMDDLKVLQPtvfpvvPRLLNRMFDR----IFGQANTTLKRWLLDFASkrkeaelrsgiirnnslwdrlifhk 385
Cdd:cd17649 162 -----CVVLRPDELWAS------ADELAEMVRElgvtVLDLPPAYLQQLAEEADR------------------------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 386 VQSSLGGRVRLMVTGAAPVSAtvlTFLRAALGC--QFYEGYGQTEC--TAGCCLTMPGDWTAGH---VGAPMPCNLIKLV 458
Cdd:cd17649 206 TGDGRPPSLRLYIFGGEALSP---ELLRRWLKApvRLFNAYGPTEAtvTPLVWKCEAGAARAGAsmpIGRPLGGRSAYIL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 459 DvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL--DKDG-----WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQG 531
Cdd:cd17649 283 D-ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFvpDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-RG 360
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 557878740 532 EYIAPEKIENIYMRSEPVAQVFVHGES--LQAFLIAIVVP 569
Cdd:cd17649 361 FRIELGEIEAALLEHPGVREAAVVALDgaGGKQLVAYVVL 400
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
74-581 |
3.33e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 82.10 E-value: 3.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 74 ALLDSDEPLVY--FYDDVTTLYEGFQRgiqvsnngpcLGSRKPDQPYEWL-SYKQWVIIEQGCFAYSMVIVPLYDTLGNE 150
Cdd:PRK06164 28 ALIDEDRPLSRaeLRALVDRLAAWLAA----------QGVRRGDRVAVWLpNCIEWVVLFLACARLGATVIAVNTRYRSH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 151 AITYIVNKAELSLVFVdKPEKAKL----LLEGVENKLIPGLKIIVVMDAYGSELVERGQRCGVEVTSMKAMEDLGRAnrr 226
Cdd:PRK06164 98 EVAHILGRGRARWLVV-WPGFKGIdfaaILAAVPPDALPPLRAIAVVDDAADATPAPAPGARVQLFALPDPAPPAAA--- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 227 kPKPPAPEDLAVICFT-SGTTGNPK------GAMVTHRNIVSDCSAFVkatentvnpcPDDTLISFLPLahmfervveCV 299
Cdd:PRK06164 174 -GERAADPDAGALLFTtSGTTSGPKlvlhrqATLLRHARAIARAYGYD----------PGAVLLAALPF---------CG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 300 MLCHGAKIGFFQGDIRLLMDDlkvlqptVF--PVVPRLL-----------NRMFDRIFGQANTTLkrwllDFASKRkeae 366
Cdd:PRK06164 234 VFGFSTLLGALAGGAPLVCEP-------VFdaARTARALrrhrvthtfgnDEMLRRILDTAGERA-----DFPSAR---- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 367 lrsgiirnnslwdRLIFHKVQSSLGGRVRLMVTGAAPvsatvLTFLraalgcqfyegYGQTECTA-GCCLTMPGDWTAGH 445
Cdd:PRK06164 298 -------------LFGFASFAPALGELAALARARGVP-----LTGL-----------YGSSEVQAlVALQPATDPVSVRI 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 446 V--GAPM-PCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRK 522
Cdd:PRK06164 349 EggGRPAsPEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRM 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557878740 523 KHIFKLAqGEYIAPEKIENIYMRSEPVAQVFVHGESLQ------AFLIAI--VVPDVETLCSWAQKR 581
Cdd:PRK06164 429 GDSLRLG-GFLVNPAEIEHALEALPGVAAAQVVGATRDgktvpvAFVIPTdgASPDEAGLMAACREA 494
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
235-565 |
3.63e-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: 81.61 E-value: 3.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 235 DLAVICFTSGTTGNPKGAMVTHRnivsDCSAFVKATENTVNPCPDDTLISFLPLAHMFerVVEC-----VMLChGAKIGF 309
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTHN----DYAYNVRASAEVCGLDQDTVYLAVLPAAHNF--PLACpgvlgTLLA-GGRVVL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 310 FQ----GDIRLLMDDLKVlqpTVFPVVPRLLnrmfdrifgqanttlKRWLlDFASKRKEAElrsgiirnnslwdrlifhk 385
Cdd:cd05920 213 APdpspDAAFPLIEREGV---TVTALVPALV---------------SLWL-DAAASRRADL------------------- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 386 vqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctaG-CCLTM---PGDWTAGHVGAPM-PCNLIKLVDv 460
Cdd:cd05920 255 --SSL----RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAE---GlLNYTRlddPDEVIIHTQGRPMsPDDEIRVVD- 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 461 EEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIE 540
Cdd:cd05920 325 EEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVE 403
|
330 340 350
....*....|....*....|....*....|..
gi 557878740 541 NIYMRSEPVAQVFV-------HGESLQAFLIA 565
Cdd:cd05920 404 NLLLRHPAVHDAAVvampdelLGERSCAFVVL 435
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
139-573 |
1.07e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 80.50 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 139 VIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAklLLEGVEnkliPGLKIIVVMDAYGSELVergqrcgvevtsmkame 218
Cdd:PRK07867 80 VPVGLNPTRRGAALARDIAHADCQLVLTESAHAE--LLDGLD----PGVRVINVDSPAWADEL----------------- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 219 DLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKatenTVNPCPDDTLISFLPLAHMFERVVE- 297
Cdd:PRK07867 137 AAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQ----RFGLGPDDVCYVSMPLFHSNAVMAGw 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 298 CVMLCHGAKI---------GFfqgdirllMDDLKVLQPTVFPVVPRLLNrmfdrifgqanttlkrWLLDFASKRKEAElr 368
Cdd:PRK07867 213 AVALAAGASIalrrkfsasGF--------LPDVRRYGATYANYVGKPLS----------------YVLATPERPDDAD-- 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 369 sgiirnNSLwdRLIFhkvqsslggrvrlmvtGAAPVSATVLTFlRAALGCQFYEGYGQTEctAGCCLTMPGDWTAGHVGA 448
Cdd:PRK07867 267 ------NPL--RIVY----------------GNEGAPGDIARF-ARRFGCVVVDGFGSTE--GGVAITRTPDTPPGALGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 449 PMPCnlIKLVDVE--------------EMNYMAAEGEgEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNG 514
Cdd:PRK07867 320 LPPG--VAIVDPDtgtecppaedadgrLLNADEAIGE-LVNTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADG 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 557878740 515 TLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFVHGeslqafliaivVPDVET 573
Cdd:PRK07867 396 YAYFAGRLGDWMRV-DGENLGTAPIERILLRYPDATEVAVYA-----------VPDPVV 442
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
233-637 |
1.16e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 80.48 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 233 PEDLAVICFTSGTTGNPKGAMVTHRNIvsdCSAfVKATENTVNPCPDD---TLISFLPLAHMFervvecvmlchGAKIGF 309
Cdd:PRK12582 219 PDTVAKYLFTSGSTGMPKAVINTQRMM---CAN-IAMQEQLRPREPDPpppVSLDWMPWNHTM-----------GGNANF 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 310 fQGDIR----LLMDDLKVLqPTVFPVVPRLLNRMFDRIFGQANTTLKrwLLDFASKRKEAELRSgiirnnslwdrliFHK 385
Cdd:PRK12582 284 -NGLLWgggtLYIDDGKPL-PGMFEETIRNLREISPTVYGNVPAGYA--MLAEAMEKDDALRRS-------------FFK 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 386 vqsslggRVRLMVTGAAPVSATVLTFLRA----ALGCQ--FYEGYGQTEcTAGccLTMPGDWTA---GHVGAPMPCNLIK 456
Cdd:PRK12582 347 -------NLRLMAYGGATLSDDLYERMQAlavrTTGHRipFYTGYGATE-TAP--TTTGTHWDTervGLIGLPLPGVELK 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 457 LVDVEEmNYmaaegegEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWL----PNGTLKIIDRKKHIFKLAQGE 532
Cdd:PRK12582 417 LAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdpddPEKGLIFDGRVAEDFKLSTGT 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 533 YIAPEKIE-NIYMRSEPVAQ-VFVHGESlQAFLIAIVVPDVETLCSWAQKRGfeGSFEELCRNKDVKKAILEDMVRLGKD 610
Cdd:PRK12582 489 WVSVGTLRpDAVAACSPVIHdAVVAGQD-RAFIGLLAWPNPAACRQLAGDPD--AAPEDVVKHPAVLAILREGLSAHNAE 565
|
410 420
....*....|....*....|....*..
gi 557878740 611 SGlKPFEQVKGITLHPELFSIDNGLLT 637
Cdd:PRK12582 566 AG-GSSSRIARALLMTEPPSIDAGEIT 591
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
228-570 |
3.72e-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: 78.47 E-value: 3.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 228 PKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAH------MFErvvecvML 301
Cdd:cd12114 120 PVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAVG----PDDRVLALSSLSFdlsvydIFG------AL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 302 CHGAKIGFFQGDIR----LLMDDLKVLQPTVFPVVPRLLNrMfdrifgqanttlkrwLLDfaskrkeaELRSGIIRNNSL 377
Cdd:cd12114 190 SAGATLVLPDEARRrdpaHWAELIERHGVTLWNSVPALLE-M---------------LLD--------VLEAAQALLPSL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 378 wdRLIFHK---VQSSLGGRVRLMVTGAAPVSatvltflraaLGcqfyegyGQTECTAGCCL----TMPGDWTAGHVGAPM 450
Cdd:cd12114 246 --RLVLLSgdwIPLDLPARLRALAPDARLIS----------LG-------GATEASIWSIYhpidEVPPDWRSIPYGRPL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 451 PCNLIKLVDveemnymaAEGE-------GEVCVKGPNVFQGYLKDPAKTAEAL--DKDG--WLHTGDIGKWLPNGTLKII 519
Cdd:cd12114 307 ANQRYRVLD--------PRGRdcpdwvpGELWIGGRGVALGYLGDPELTAARFvtHPDGerLYRTGDLGRYRPDGTLEFL 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 557878740 520 DRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQ--VFVHGESLQAFLIAIVVPD 570
Cdd:cd12114 379 GRRDGQVKV-RGYRIELGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPD 430
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
200-553 |
4.44e-15 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 78.40 E-value: 4.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 200 LVERGQRCGvevTSMKAMEDLGRANRRKPKPPA---PEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNP 276
Cdd:PRK09274 140 LVTVGGRLL---WGGTTLATLLRDGAAAPFPMAdlaPDDMAAILFTSGSTGTPKGVVYTHGMFE----AQIEALREDYGI 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 277 CPDDTLISFLPLahmfervvecvMLCHGAKIGFfqGDIRLLMDDLKVLQptvfpVVPRllnRMFDRIFGQANTTLkrwll 356
Cdd:PRK09274 213 EPGEIDLPTFPL-----------FALFGPALGM--TSVIPDMDPTRPAT-----VDPA---KLFAAIERYGVTNL----- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 357 dFASKrkeaelrsgiirnnSLWDRLIFHKVQS--SLGGrVRLMVTGAAPVSATVLTFLRAAL--GCQFYEGYGQTEC--- 429
Cdd:PRK09274 267 -FGSP--------------ALLERLGRYGEANgiKLPS-LRRVISAGAPVPIAVIERFRAMLppDAEILTPYGATEAlpi 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 430 ---TAGCCLTMPGDWT---AGH-VGAPMPCNLIKLVDVEEM-------NYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAE 494
Cdd:PRK09274 331 ssiESREILFATRAATdngAGIcVGRPVDGVEVRIIAISDApipewddALRLATGEiGEIVVAGPMVTRSYYNRPEATRL 410
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557878740 495 A--LDKDG--WLHTGDIGkWL-PNGTLKIIDRKKHIFKLAQGEYIapekieniymrSEPVAQVF 553
Cdd:PRK09274 411 AkiPDGQGdvWHRMGDLG-YLdAQGRLWFCGRKAHRVETAGGTLY-----------TIPCERIF 462
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
132-554 |
7.43e-15 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 77.88 E-value: 7.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 132 GCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDkpekAKLL--LEGVENKLIPgLKIIVVMDAYGSELVERGQRcgv 209
Cdd:PRK06155 90 GCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVE----AALLaaLEAADPGDLP-LPAVWLLDAPASVSVPAGWS--- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 210 eVTSMKAMedlgrANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTH-------RNIVSDcsafvkatentVNPCPDDTL 282
Cdd:PRK06155 162 -TAPLPPL-----DAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHaqfywwgRNSAED-----------LEIGADDVL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 283 ISFLPLAH-----MFERVvecvmLCHGAKI---------GFFqgdirllmDDLKVLQPTVF----PVVPRLLnrmfdrif 344
Cdd:PRK06155 225 YTTLPLFHtnalnAFFQA-----LLAGATYvleprfsasGFW--------PAVRRHGATVTyllgAMVSILL-------- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 345 gqanttlkrwlldfaSKRKEAELRSgiirnnslwdrlifHKVQSSLGGrvrlmvtgaaPVSATVLTFLRAALGCQFYEGY 424
Cdd:PRK06155 284 ---------------SQPARESDRA--------------HRVRVALGP----------GVPAALHAAFRERFGVDLLDGY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 425 GQTECTAGCCLTMPGDwTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKG--PNVF-QGYLKDPAKTAEALdKDGW 501
Cdd:PRK06155 325 GSTETNFVIAVTHGSQ-RPGSMGRLAPGFEARVVD-EHDQELPDGEPGELLLRAdePFAFaTGYFGMPEKTVEAW-RNLW 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 557878740 502 LHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIyMRSEP-VAQVFV 554
Cdd:PRK06155 402 FHTGDRVVRDADGWFRFVDRIKDAIR-RRGENISSFEVEQV-LLSHPaVAAAAV 453
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
233-580 |
9.05e-15 |
|
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: 77.21 E-value: 9.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 233 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNpcpDDTLI--SFLPLAHMFErvvecvMLCH---GAKI 307
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPA---DKSLVyaSFSFDASAWE------IFPHltaGAAL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 308 GFFQGDIRLLMDDLkvlqptvfpvvprllnrmfDRIFGQANTTLKRWLLDFASKRKEAElrsgiirNNSLwdrlifhkvq 387
Cdd:cd17645 174 HVVPSERRLDLDAL-------------------NDYFNQEGITISFLPTGAAEQFMQLD-------NQSL---------- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 388 sslggrvRLMVTGAAPVSATVLTflraalGCQFYEGYGQTECTAgCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMA 467
Cdd:cd17645 218 -------RVLLTGGDKLKKIERK------GYKLVNNYGPTENTV-VATSFEIDKPYANIPIGKPIDNTRVYILDEALQLQ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 468 AEG-EGEVCVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIE 540
Cdd:cd17645 284 PIGvAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIE 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 557878740 541 NIYMRSEPVAQVFV-------HGESLQAFLIAIVVPDVETLCSWAQK 580
Cdd:cd17645 363 PFLMNHPLIELAAVlakedadGRKYLVAYVTAPEEIPHEELREWLKN 409
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
232-569 |
1.82e-14 |
|
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: 75.98 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 232 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKateNTVNPCPDDTLISFLPLAHMFER-VVECVMLCHGAKIGFF 310
Cdd:cd05958 95 ASDDICILAFTSGTTGAPKATMHFHRDPLASADRYAV---NVLRLREDDRFVGSPPLAFTFGLgGVLLFPFGVGASGVLL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 311 QGDI-RLLMDDLKVLQPTVFPVVPRLLNRMfdrifgqanttlkrwlldFASKRKEAELRSGiirnnslwdrlifhkvqss 389
Cdd:cd05958 172 EEATpDLLLSAIARYKPTVLFTAPTAYRAM------------------LAHPDAAGPDLSS------------------- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 390 lggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAE 469
Cdd:cd05958 215 ----LRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD-DEGNPVPDG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 470 GEGEVCVKGPNvfqGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPV 549
Cdd:cd05958 290 TIGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQHPAV 365
|
330 340
....*....|....*....|...
gi 557878740 550 AQVFVHGESLQAFLI---AIVVP 569
Cdd:cd05958 366 AECAVVGHPDESRGVvvkAFVVL 388
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
423-579 |
2.12e-14 |
|
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: 74.65 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 423 GYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAeGE-GEVCVKGPNVFQGYLKDPAKTAEALdKDGW 501
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILD-EDGREVPD-GEvGEIVARGPTVMAGYWNRPEVNARRT-RGGW 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557878740 502 LHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIyMRSEP-VAQVFVhgeslqafliaIVVPDVetlcSWAQ 579
Cdd:cd17636 219 HHTNDLGRREPDGSLSFVGPKTRMIKSG-AENIYPAEVERC-LRQHPaVADAAV-----------IGVPDP----RWAQ 280
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
233-544 |
2.13e-14 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 76.39 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 233 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKAtentVNPCPDDTLISFLPLAHMFervvecvmlchgakiGFFQG 312
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKF----FSPKEDDVMMSFLPPFHAY---------------GFNSC 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 313 DIRLLMDDLkvlqPTVF---PVVPRLLNRMFDR----IFGQANTTLKrWLLDFASKRKEA--ELRSGIIRNNSLWDRLiF 383
Cdd:PRK06334 243 TLFPLLSGV----PVVFaynPLYPKKIVEMIDEakvtFLGSTPVFFD-YILKTAKKQESClpSLRFVVIGGDAFKDSL-Y 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 384 HKVQSslggrvrlmvtgaapvsatvlTFLRAALgcqfYEGYGQTECTAgcCLTMPGDWTAGH---VGAPMPCNLIKLVDv 460
Cdd:PRK06334 317 QEALK---------------------TFPHIQL----RQGYGTTECSP--VITINTVNSPKHescVGMPIRGMDVLIVS- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 461 EEMNYMAAEGE-GEVCVKGPNVFQGYL-KDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEK 538
Cdd:PRK06334 369 EETKVPVSSGEtGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSLEA 447
|
....*.
gi 557878740 539 IENIYM 544
Cdd:PRK06334 448 LESILM 453
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
233-583 |
2.40e-14 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 75.93 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 233 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNpcpdDTLISFLPLAhmFERVVE--CVMLCHGAKIgff 310
Cdd:cd17644 105 PENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSS----DRVLQFASIA--FDVAAEeiYVTLLSGATL--- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 311 qgdirllmddlkVLQPtvfpvvprllNRMFdrifgqanttlkRWLLDFASKRKEAELRSGIIrNNSLWDRLIFHKVQSSL 390
Cdd:cd17644 176 ------------VLRP----------EEMR------------SSLEDFVQYIQQWQLTVLSL-PPAYWHLLVLELLLSTI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 391 GG--RVRLMVTGAAPVSATVLTFLRAALG--CQFYEGYGQTECTAGCCLTMPGDWTAGH-----VGAPMPCNLIKLVDvE 461
Cdd:cd17644 221 DLpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIANTQVYILD-E 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 462 EMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLH--------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEY 533
Cdd:cd17644 300 NLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKI-RGFR 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 557878740 534 IAPEKIENIYMRSEPVAQVFV---HGESLQAFLIAIVVPDVETLCSWAQKRGF 583
Cdd:cd17644 379 IELGEIEAVLSQHNDVKTAVVivrEDQPGNKRLVAYIVPHYEESPSTVELRQF 431
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
150-624 |
2.86e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 75.90 E-value: 2.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 150 EAITYIVNKAELSLVFVD---KPekaklLLEGVENKLiPGLKIIVVM-DAygselvergQRCGVEVTSMKAMEDL-GRAN 224
Cdd:PRK07008 101 EQIAYIVNHAEDRYVLFDltfLP-----LVDALAPQC-PNVKGWVAMtDA---------AHLPAGSTPLLCYETLvGAQD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 225 RRKPKPPAPEDLAV-ICFTSGTTGNPKGAMVTHRNIVsdCSAFVKATENTVNPCPDDTLisfLPLAHMFErvVECVMLCH 303
Cdd:PRK07008 166 GDYDWPRFDENQASsLCYTSGTTGNPKGALYSHRSTV--LHAYGAALPDAMGLSARDAV---LPVVPMFH--VNAWGLPY 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 304 -----GAKIgffqgdirllmddlkvlqptVFPvvprllnrmfdrifGQAnttlkrwlLDFASKRK--EAELRSGIIRNNS 376
Cdd:PRK07008 239 sapltGAKL--------------------VLP--------------GPD--------LDGKSLYEliEAERVTFSAGVPT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 377 LWDRLIFHKVQSSLG-GRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECT---AGCCLT-----MPGD------W 441
Cdd:PRK07008 277 VWLGLLNHMREAGLRfSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSplgTLCKLKwkhsqLPLDeqrkllE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 442 TAGHV--GAPMpcnliKLVDvEEMNYMAAEGE--GEVCVKGPNVFQGYLKdpaKTAEALDkDGWLHTGDIGKWLPNGTLK 517
Cdd:PRK07008 357 KQGRViyGVDM-----KIVG-DDGRELPWDGKafGDLQVRGPWVIDRYFR---GDASPLV-DGWFPTGDVATIDADGFMQ 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 518 IIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAqvfvhgeslQAFLIAIVVP--DVETLCSWAQKRGFEGSFEELCRNKD 595
Cdd:PRK07008 427 ITDRSKDVIK-SGGEWISSIDIENVAVAHPAVA---------EAACIACAHPkwDERPLLVVVKRPGAEVTREELLAFYE 496
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 557878740 596 VKKA---ILEDMVRL--------GKDSGLKPFEQVKGITL 624
Cdd:PRK07008 497 GKVAkwwIPDDVVFVdaiphtatGKLQKLKLREQFRDYVL 536
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
230-574 |
3.68e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 76.53 E-value: 3.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 230 PPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAhmFERVVECVM--LCHGAki 307
Cdd:PRK12316 4690 RLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELT----PDDRVLQFMSFS--FDGSHEGLYhpLINGA-- 4761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 308 gffqgdiRLLMDDLKVLQPtvfpvvprllNRMFDRIFGQANTTlkrwlLDFASkrkeaelrsgiirnnSLWDRLIFHKVQ 387
Cdd:PRK12316 4762 -------SVVIRDDSLWDP----------ERLYAEIHEHRVTV-----LVFPP---------------VYLQQLAEHAER 4804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 388 SSLGGRVRLMVTG--AAPVSATVLTFlRAALGCQFYEGYGQTECTAG-CCLTMPGDWTAG----HVGAPMPCNLIKLVDV 460
Cdd:PRK12316 4805 DGEPPSLRVYCFGgeAVAQASYDLAW-RALKPVYLFNGYGPTETTVTvLLWKARDGDACGaaymPIGTPLGNRSGYVLDG 4883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 461 eEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAE-----ALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEY 533
Cdd:PRK12316 4884 -QLNPLPVGVAGELYLGGEGVARGYLERPALTAErfvpdPFGAPGgrLYRTGDLARYRADGVIDYLGRVDHQVKI-RGFR 4961
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 557878740 534 IAPEKIEnIYMRSEP-------VAQVFVHGeslqAFLIAIVVPDVETL 574
Cdd:PRK12316 4962 IELGEIE-ARLREHPavreavvIAQEGAVG----KQLVGYVVPQDPAL 5004
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
234-564 |
9.25e-14 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 74.42 E-value: 9.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 234 EDLAVICFTSGTTGNPKgaMVTHrnivSDCSAFVKA----------TENTVNPCPDDTLISFLPLAHMFERVVE--CVML 301
Cdd:cd05928 174 QEPMAIYFTSGTTGSPK--MAEH----SHSSLGLGLkvngrywldlTASDIMWNTSDTGWIKSAWSSLFEPWIQgaCVFV 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 302 CHGAKIgffqgDIRLLMDDLKVLQPTVFPVVPrllnrmfdrifgqantTLKRWLL--DFASkrkeaelrsgiirnnslwd 379
Cdd:cd05928 248 HHLPRF-----DPLVILKTLSSYPITTFCGAP----------------TVYRMLVqqDLSS------------------- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 380 rlifHKVQSslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLTMPG-DWTAGHVGAPMPCNLIKLV 458
Cdd:cd05928 288 ----YKFPS-----LQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTE-TGLICANFKGmKIKPGSMGKASPPYDVQII 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 459 DvEEMNYMAAEGEGEVCVK-GPN----VFQGYLKDPAKTAEALDKDGWLhTGDIGKWLPNGTLKIIDRKKHIFkLAQGEY 533
Cdd:cd05928 358 D-DNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYR 434
|
330 340 350
....*....|....*....|....*....|....*...
gi 557878740 534 IAPEKIENIYMRSEPVAQVFV-------HGESLQAFLI 564
Cdd:cd05928 435 IGPFEVESALIEHPAVVESAVvsspdpiRGEVVKAFVV 472
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
230-572 |
1.73e-13 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 72.98 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 230 PPAPEDLAVICFTSGTTGNPKGAMVTHRNI------VSDCSAFvkatenTVNpcpDDTLISfLPLAHmfervvecV---- 299
Cdd:PRK09029 131 AWQPQRLATMTLTSGSTGLPKAAVHTAQAHlasaegVLSLMPF------TAQ---DSWLLS-LPLFH--------Vsgqg 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 300 ----MLCHGAKIGFfqGDIRLLMDDLkvLQPTVFPVVPRLLNRMFDRifGQANTTLKRWLLdfaskrkeaelrsgiirnn 375
Cdd:PRK09029 193 ivwrWLYAGATLVV--RDKQPLEQAL--AGCTHASLVPTQLWRLLDN--RSEPLSLKAVLL------------------- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 376 slwdrlifhkvqsslGGrvrlmvtGAAPVSatvLTFLRAALGCQFYEGYGQTECTAGCClTMPGDWTAGhVGAPMPCNLI 455
Cdd:PRK09029 248 ---------------GG-------AAIPVE---LTEQAEQQGIRCWCGYGLTEMASTVC-AKRADGLAG-VGSPLPGREV 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 456 KLVDveemnymaaegeGEVCVKGPNVFQGYLKDpAKTAEALDKDGWLHTGDIGKWLpNGTLKIIDRKKHIFkLAQGEYIA 535
Cdd:PRK09029 301 KLVD------------GEIWLRGASLALGYWRQ-GQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQ 365
|
330 340 350
....*....|....*....|....*....|....*..
gi 557878740 536 PEKIENIYMRSEPVAQVFVhgeslqafliaIVVPDVE 572
Cdd:PRK09029 366 PEEIERVINQHPLVQQVFV-----------VPVADAE 391
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
218-570 |
3.08e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 72.77 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 218 EDLGRANRRKPKPPAPEDLAVIC---FTSGTTGNPKGAMVTHRNIvsdcsAFVkATENTVNPCPD----DTLISFLPLAH 290
Cdd:PRK07470 144 EALVARHLGARVANAAVDHDDPCwffFTSGTTGRPKAAVLTHGQM-----AFV-ITNHLADLMPGtteqDASLVVAPLSH 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 291 MfERVVECVMLCHGAKigffqgDIRLLMDDLKVlqPTVFPVVPRL-LNRMFdrifgQANTTLKRWLLDFASKRKEaelrs 369
Cdd:PRK07470 218 G-AGIHQLCQVARGAA------TVLLPSERFDP--AEVWALVERHrVTNLF-----TVPTILKMLVEHPAVDRYD----- 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 370 giirnnslwdrlifhkvQSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTaGC------CLTMPGDWTA 443
Cdd:PRK07470 279 -----------------HSSL----RYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVT-GNitvlppALHDAEDGPD 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 444 GHVGapmPCNL------IKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLK 517
Cdd:PRK07470 337 ARIG---TCGFertgmeVQIQD-DEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLY 411
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 557878740 518 IIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHGeslqafliaivVPD 570
Cdd:PRK07470 412 ITGRASDMY-ISGGSNVYPREIEEKLLTHPAVSEVAVLG-----------VPD 452
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
233-570 |
3.61e-13 |
|
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: 71.96 E-value: 3.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 233 PEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTvnpCPDD--------TLISF-LPLAHMFervvecVMLCH 303
Cdd:cd12115 104 PDDLAYVIYTSGSTGRPKGVAIEHRNAA----AFLQWAAAA---FSAEelagvlasTSICFdLSVFELF------GPLAT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 304 GAKIgffqgdirllmddlkVLQPTVFPvvprllnrmfdrifgqanttlkrwLLDFASkRKEAELrsgIIRNNSLWDRLIF 383
Cdd:cd12115 171 GGKV---------------VLADNVLA------------------------LPDLPA-AAEVTL---INTVPSAAAELLR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 384 HkvqSSLGGRVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTECT--AGCCLTMPGDWTAGHVGAPMPCNLIKLVDv 460
Cdd:cd12115 208 H---DALPASVRVVNLAGEPLPRDLVQRLYARLqVERVVNLYGPSEDTtySTVAPVPPGASGEVSIGRPLANTQAYVLD- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 461 EEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 534
Cdd:cd12115 284 RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRI 362
|
330 340 350
....*....|....*....|....*....|....*....
gi 557878740 535 APEKIENIYMRSEPVAQ--VFVHGESL-QAFLIAIVVPD 570
Cdd:cd12115 363 ELGEIEAALRSIPGVREavVVAIGDAAgERRLVAYIVAE 401
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
231-605 |
5.61e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 72.89 E-value: 5.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 231 PAPEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDTLISFLPLAhmFERVVECVM--LCHGAKIG 308
Cdd:PRK12467 1715 LAPQNLAYVIYTSGSTGRPKGAGNRHGALV----NRLCATQEAYQLSAADVVLQFTSFA--FDVSVWELFwpLINGARLV 1788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 309 FFQGDIRL----LMDDLKVLQPTVFPVVPRLLNRmfdrifgqanttlkrwLLDFAskrkEAELRSGIIRnnslwdRLIFh 384
Cdd:PRK12467 1789 IAPPGAHRdpeqLIQLIERQQVTTLHFVPSMLQQ----------------LLQMD----EQVEHPLSLR------RVVC- 1841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 385 kvqsslGGRvrlmvtgAAPVSATVLTFlrAALG-CQFYEGYGQTECTAG-----CCLTMPGDWTAGHVGAPMPcNLIKLV 458
Cdd:PRK12467 1842 ------GGE-------ALEVEALRPWL--ERLPdTGLFNLYGPTETAVDvthwtCRRKDLEGRDSVPIGQPIA-NLSTYI 1905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 459 DVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL------DKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQG 531
Cdd:PRK12467 1906 LDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgTVGSRLYrTGDLARYRADGVIEYLGRIDHQVKI-RG 1984
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557878740 532 EYIAPEKIENIYMRSEPVAQ--VFVHGESLQAFLIAIVVPDVETLCSWAQKRGfeGSFEELcrnKDVKKAILED-MV 605
Cdd:PRK12467 1985 FRIELGEIEARLREQGGVREavVIAQDGANGKQLVAYVVPTDPGLVDDDEAQV--ALRAIL---KNHLKASLPEyMV 2056
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
231-553 |
5.88e-13 |
|
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: 71.34 E-value: 5.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 231 PAPEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDTLISFLPLAHMFervvecvmlchGAKIGff 310
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFA----AQIDALRQLYGIRPGEVDLATFPLFALF-----------GPALG-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 311 qgdirllmddLKVLQPTVFPVVPrllnrmfdrifGQANttlKRWLLDFASKRKEaelrSGIIRNNSLWDRLIFHKVQSSL 390
Cdd:cd05910 145 ----------LTSVIPDMDPTRP-----------ARAD---PQKLVGAIRQYGV----SIVFGSPALLERVARYCAQHGI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 391 G-GRVRLMVTGAAPVSATVLTFLRAAL--GCQFYEGYGQTECTAGCC------LTMPGDWTAGH----VGAPMPCNLIKL 457
Cdd:cd05910 197 TlPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrelLATTTAATSGGagtcVGRPIPGVRVRI 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 458 VDVEEMNYMAAEGE--------GEVCVKGPNVFQGYLKDPAKTAEALDKDG----WLHTGDIGKWLPNGTLKIIDRKKHI 525
Cdd:cd05910 277 IEIDDEPIAEWDDTlelprgeiGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHR 356
|
330 340
....*....|....*....|....*...
gi 557878740 526 FKLAQGEYIapekieniymrSEPVAQVF 553
Cdd:cd05910 357 VITTGGTLY-----------TEPVERVF 373
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
227-552 |
1.62e-12 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 70.42 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 227 KPKPPAPEDLAVIcFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCPDDTLISFLPLAHM--FERVVECVMlcHG 304
Cdd:PRK05857 163 NADQGSEDPLAMI-FTSGTTGEPKAVLLANRTFFAVPDILQKEGLNWVTWVVGETTYSPLPATHIggLWWILTCLM--HG 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 305 AKI---GFFQGDIRLLMDDLKVLQPTVfpvVPRLLNRMFdrifgqanttlkrwlldfaskrkeAELRSGIIRNNSLwdrl 381
Cdd:PRK05857 240 GLCvtgGENTTSLLEILTTNAVATTCL---VPTLLSKLV------------------------SELKSANATVPSL---- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 382 ifhkvqsslggrvRLMVTGAAPVSATVLTFLRAA--LGCQFYeGYGQTECTAGCCLTMPGDWT---AGHVGAPMPCNLIK 456
Cdd:PRK05857 289 -------------RLVGYGGSRAIAADVRFIEATgvRTAQVY-GLSETGCTALCLPTDDGSIVkieAGAVGRPYPGVDVY 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 457 LVDVEEMNYMAAEGE-----GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQG 531
Cdd:PRK05857 355 LAATDGIGPTAPGAGpsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGG 432
|
330 340
....*....|....*....|.
gi 557878740 532 EYIAPEKIENIymrSEPVAQV 552
Cdd:PRK05857 433 VNIAPDEVDRI---AEGVSGV 450
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
376-554 |
1.63e-12 |
|
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: 69.90 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 376 SLWdRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLI 455
Cdd:cd05974 185 TVW-RMLIQQDLASFDVKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRV 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 456 KLVDVEEmnymAAEGEGEVCV-----KGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQ 530
Cdd:cd05974 264 ALLDPDG----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SS 337
|
170 180
....*....|....*....|....
gi 557878740 531 GEYIAPEKIENIYMRSEPVAQVFV 554
Cdd:cd05974 338 DYRISPFELESVLIEHPAVAEAAV 361
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
216-569 |
2.15e-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: 69.71 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 216 AMEDLGRANRRKPKPPAPEDLA--VICFTSGTTGNPKGAMVTHrnivsDCsafvkatentvNPCPDDTLISF-LPLAHMF 292
Cdd:cd05929 105 GLEDYEAAEGGSPETPIEDEAAgwKMLYSGGTTGRPKGIKRGL-----PG-----------GPPDNDTLMAAaLGFGPGA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 293 ERVVECVM-LCHGAKIGFFQGDIRL-----LM---DDLKVLQP------TVFPVVPRLLNRMfdrifgqanttLK----- 352
Cdd:cd05929 169 DSVYLSPApLYHAAPFRWSMTALFMggtlvLMekfDPEEFLRLieryrvTFAQFVPTMFVRL-----------LKlpeav 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 353 RWLLDFASkrkeaeLRSgiirnnslwdrlIFHkvqsslggrvrlmvtGAAPVSATVLTFLRAALGCQFYEGYGQTECTAG 432
Cdd:cd05929 238 RNAYDLSS------LKR------------VIH---------------AAAPCPPWVKEQWIDWGGPIIWEYYGGTEGQGL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 433 CCLTmPGDWTA--GHVGAPMPCNLiKLVDvEEMNYMAAEGEGEVCVKGPNVFQgYLKDPAKTAEALDKDGWLHTGDIGKW 510
Cdd:cd05929 285 TIIN-GEEWLThpGSVGRAVLGKV-HILD-EDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYL 360
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557878740 511 LPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG---ESLQAFLIAIVVP 569
Cdd:cd05929 361 DEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIAHPKVLDAAVVGvpdEELGQRVHAVVQP 421
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
394-563 |
4.55e-12 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 69.10 E-value: 4.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 394 VRLMVTGAAPvSATVLtFLRAALGCQFYEGYGQTEcTAG---CCLTMPgDW------TAGHVGAPMPCNLIKL-----VD 459
Cdd:PLN02479 313 VHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSE-TYGpstVCAWKP-EWdslppeEQARLNARQGVRYIGLegldvVD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 460 VEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPE 537
Cdd:PLN02479 389 TKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGGENISSL 466
|
170 180 190
....*....|....*....|....*....|...
gi 557878740 538 KIENIYMRSEPVAQVFV-------HGESLQAFL 563
Cdd:PLN02479 467 EVENVVYTHPAVLEASVvarpderWGESPCAFV 499
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
232-551 |
7.56e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 69.04 E-value: 7.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 232 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNpcPDDTLISFLPLAHmfervvecvmlchgaKIGFFQ 311
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLN--PDDVIVSWLPLYH---------------DMGLIG 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 312 GdirllmddlkVLQPtVFPVVPRLLnrMFDRIFGQANTtlkRWLldfaskrkEA--ELRSGIIRNNSLWDRLIFHKV-QS 388
Cdd:PRK05691 227 G----------LLQP-IFSGVPCVL--MSPAYFLERPL---RWL--------EAisEYGGTISGGPDFAYRLCSERVsES 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 389 SLGG----RVRLMVTGAAPVSATVL-TFLRAALGC-----QFYEGYGQTECT---AGC-------CLTMPGDWTAGHV-- 446
Cdd:PRK05691 283 ALERldlsRWRVAYSGSEPIRQDSLeRFAEKFAACgfdpdSFFASYGLAEATlfvSGGrrgqgipALELDAEALARNRae 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 447 ----------GAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEA-LDKDG--WLHTGDIGkWLPN 513
Cdd:PRK05691 363 pgtgsvlmscGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfVEHDGrtWLRTGDLG-FLRD 441
|
330 340 350
....*....|....*....|....*....|....*...
gi 557878740 514 GTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQ 551
Cdd:PRK05691 442 GELFVTGRLKDML-IVRGHNLYPQDIEKTVEREVEVVR 478
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
223-564 |
2.20e-11 |
|
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: 66.39 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 223 ANRRKpkppAPEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDtliSFLPLAH------MFERVV 296
Cdd:cd05973 81 ANRHK----LDSDPFVMMFTSGTTGLPKGVPVPLRALA----AFGAYLRDAVDLRPED---SFWNAADpgwaygLYYAIT 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 297 ECVMLCHGAKI---GFFQGDIRLLMDDLKVLQPTVFPVVPRLLnrmfdrifgqanttlkrwlldfaskrkeaeLRSGIir 373
Cdd:cd05973 150 GPLALGHPTILlegGFSVESTWRVIERLGVTNLAGSPTAYRLL------------------------------MAAGA-- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 374 nnslwdrlifhKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctagccLTMP--GDWTAGHV----- 446
Cdd:cd05973 198 -----------EVPARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTE------LGMVlaNHHALEHPvhags 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 447 -GAPMP---CNLIKLVDVEemnymAAEGE-GEVCVKGPNV----FQGYLKDPAKTAEAldkdGWLHTGDIGKWLPNGTLK 517
Cdd:cd05973 261 aGRAMPgwrVAVLDDDGDE-----LGPGEpGRLAIDIANSplmwFRGYQLPDTPAIDG----GYYLTGDTVEFDPDGSFS 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 557878740 518 IIDRKKHIFKLAqGEYIAPEKIENIYMRSEPVAQVFV-------HGESLQAFLI 564
Cdd:cd05973 332 FIGRADDVITMS-GYRIGPFDVESALIEHPAVAEAAVigvpdpeRTEVVKAFVV 384
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
143-556 |
2.40e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 66.64 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 143 LYDTLGNEAIT-----YIVNKAELSLVF--VDKPEKAKLLLegvenKLIPGLKIIVVMDAYGSelvergqrcgvevtsMK 215
Cdd:PRK13391 74 LYYTCVNSHLTpaeaaYIVDDSGARALItsAAKLDVARALL-----KQCPGVRHRLVLDGDGE---------------LE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 216 AMEDLGRANRRKPKPPAPEDL--AVICFTSGTTGNPKGamvthrnivsdcsafVKAtentvnPCPDDTLISFLPLAHMFE 293
Cdd:PRK13391 134 GFVGYAEAVAGLPATPIADESlgTDMLYSSGTTGRPKG---------------IKR------PLPEQPPDTPLPLTAFLQ 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 294 RVV----ECVMLC-----HGAKIGFFQGDIRL-----LMDD------LKVLQP---TVFPVVPRllnrMFDRIFGQANTT 350
Cdd:PRK13391 193 RLWgfrsDMVYLSpaplyHSAPQRAVMLVIRLggtviVMEHfdaeqyLALIEEygvTHTQLVPT----MFSRMLKLPEEV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 351 LKRWLLdfaskrkeaelrsgiirnnslwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEcT 430
Cdd:PRK13391 269 RDKYDL-------------------------------SSL----EVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATE-G 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 431 AGCCLTMPGDWTA--GHVGAPMpCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQgYLKDPAKTAEALDKDG-WLHTGDI 507
Cdd:PRK13391 313 LGFTACDSEEWLAhpGTVGRAM-FGDLHILD-DDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDI 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 557878740 508 GKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG 556
Cdd:PRK13391 390 GYVDEDGYLYLTDRAAFMI-ISGGVNIYPQEAENLLITHPKVADAAVFG 437
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
150-556 |
2.53e-11 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 66.70 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 150 EAITYIVNKAELSLVFVDK---PekaklLLEGVENKLiPGLKIIVVMdaygselverGQRCGVEVTSMK---AMED-LGR 222
Cdd:PRK06018 101 EQIAWIINHAEDRVVITDLtfvP-----ILEKIADKL-PSVERYVVL----------TDAAHMPQTTLKnavAYEEwIAE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 223 ANRRKPKPPAPEDLAV-ICFTSGTTGNPKGAMVTHRNIVsdCSAFVKATENTVNPCPDDTLISFLPLAH-------MFER 294
Cdd:PRK06018 165 ADGDFAWKTFDENTAAgMCYTSGTTGDPKGVLYSHRSNV--LHALMANNGDALGTSAADTMLPVVPLFHanswgiaFSAP 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 295 VVECVMLCHGAKIGffQGDIRLLMDDLKVlqpTVFPVVPrllnrmfdrifgqantTLKRWLLDF--ASKRKEAELRSGII 372
Cdd:PRK06018 243 SMGTKLVMPGAKLD--GASVYELLDTEKV---TFTAGVP----------------TVWLMLLQYmeKEGLKLPHLKMVVC 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 373 rnnslwdrlifhkvqsslGGrvrlmvtgaapvSATVLTFLRA--ALGCQFYEGYGQTECT---AGCCLTMPGDWTAGHV- 446
Cdd:PRK06018 302 ------------------GG------------SAMPRSMIKAfeDMGVEVRHAWGMTEMSplgTLAALKPPFSKLPGDAr 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 447 -------GAPMPCNLIKLVDvEEMNYMAAEGE--GEVCVKGPNVFQGYLKdpaKTAEALDKDGWLHTGDIGKWLPNGTLK 517
Cdd:PRK06018 352 ldvlqkqGYPPFGVEMKITD-DAGKELPWDGKtfGRLKVRGPAVAAAYYR---VDGEILDDDGFFDTGDVATIDAYGYMR 427
|
410 420 430
....*....|....*....|....*....|....*....
gi 557878740 518 IIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQVFVHG 556
Cdd:PRK06018 428 ITDRSKDVIK-SGGEWISSIDLENLAVGHPKVAEAAVIG 465
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
233-574 |
3.42e-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: 65.88 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 233 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpCPDDTLISFLPlAHMFERVVE--CVMLCHGAKIGFF 310
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGR---DNGDEAVLFFS-NYVFDFFVEqmTLALLNGQKLVVP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 311 QGDIRL-------LMDDLKVlqpTVFPVVPRLLNRM-FDRIfgqanTTLKRWLL---DFASKRkeaelrsgiirnnslwd 379
Cdd:cd17648 169 PDEMRFdpdrfyaYINREKV---TYLSGTPSVLQQYdLARL-----PHLKRVDAageEFTAPV----------------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 380 rliFHKVQSSLGGRVrlmVTGAAPVSATVLTFLRaalgcqFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIklvd 459
Cdd:cd17648 224 ---FEKLRSRFAGLI---INAYGPTETTVTNHKR------FFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAV---- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 460 veemnymaaegeGEVCVKGPNVFQGYLKDPAKTAE-------------ALDKDGWLH-TGDIGKWLPNGTLKIIDRKKHI 525
Cdd:cd17648 288 ------------GELYLGGDGVARGYLNRPELTAErflpnpfqteqerARGRNARLYkTGDLVRWLPSGELEYLGRNDFQ 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 557878740 526 FKLaQGEYIAPEKIENIYMRSEPVAQVFV--------HGESLQAFLIAIVVPDVETL 574
Cdd:cd17648 356 VKI-RGQRIEPGEVEAALASYPGVRECAVvakedasqAQSRIQKYLVGYYLPEPGHV 411
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
395-570 |
6.38e-11 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 65.40 E-value: 6.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 395 RLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctaG-CCLTMPGDwTAGHV----GAPM-PCNLIKLVDvEEMNYMAa 468
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAE---GlVNYTRLDD-SDERIfttqGRPMsPDDEVWVAD-ADGNPLP- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 469 EGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHifklaQ----GEYIAPEKIENIY 543
Cdd:PRK10946 377 QGEvGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGEKIAAEEIENLL 451
|
170 180
....*....|....*....|....*..
gi 557878740 544 MRsepvaqvfvHGESLQAFLIAIvvPD 570
Cdd:PRK10946 452 LR---------HPAVIHAALVSM--ED 467
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
235-556 |
8.70e-11 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 64.68 E-value: 8.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 235 DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVE-CVMLCHGAKIGF---F 310
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGAL----PSDVLYTCLPLYHSTALIVGwSACLASGATLVIrkkF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 311 QGdiRLLMDDLKVLQPTVFPVVPRLLnrmfdrifgqanttlkRWLLdfASKRKEAELRsgiirnnslwdrlifHKVQSSL 390
Cdd:cd05940 158 SA--SNFWDDIRKYQATIFQYIGELC----------------RYLL--NQPPKPTERK---------------HKVRMIF 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 391 GGRVRLMVTGaapvsatvlTFL-RAALGcQFYEGYGQTECTAGCCLTMPGDWTAGHVGA----PMPCNLIKlVDVEEMN- 464
Cdd:cd05940 203 GNGLRPDIWE---------EFKeRFGVP-RIAEFYAATEGNSGFINFFGKPGAIGRNPSllrkVAPLALVK-YDLESGEp 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 465 ------YMAAEGEGEV--CV-----KGPnvFQGYLkDPAKTAEAL------DKDGWLHTGDIGKWLPNGTLKIIDRKKHI 525
Cdd:cd05940 272 irdaegRCIKVPRGEPglLIsrinpLEP--FDGYT-DPAATEKKIlrdvfkKGDAWFNTGDLMRLDGEGFWYFVDRLGDT 348
|
330 340 350
....*....|....*....|....*....|.
gi 557878740 526 FKLaQGEYIAPEKIENIYMRSEPVAQVFVHG 556
Cdd:cd05940 349 FRW-KGENVSTTEVAAVLGAFPGVEEANVYG 378
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
233-580 |
1.84e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 64.80 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 233 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNpcpdDTLISFLPLAhmFERVVECVM--LCHGAKIGFF 310
Cdd:PRK12467 3236 GENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDAN----DRVLLFMSFS--FDGAQERFLwtLICGGCLVVR 3309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 311 QGDIRllmDDLKVLQptvfpvvprLLNRmfDRIfgqanTTlkrwlLDFASkrkeaelrsgiirnNSLWDRLIFHKVQSsl 390
Cdd:PRK12467 3310 DNDLW---DPEELWQ---------AIHA--HRI-----SI-----ACFPP--------------AYLQQFAEDAGGAD-- 3349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 391 GGRVRLMVTGAAPVSATVLTFLRAALG-CQFYEGYGQTECTAGCCL-TMPGDWTAGHVGAPMPCNLIKL---VDVEEMNY 465
Cdd:PRK12467 3350 CASLDIYVFGGEAVPPAAFEQVKRKLKpRGLTNGYGPTEAVVTVTLwKCGGDAVCEAPYAPIGRPVAGRsiyVLDGQLNP 3429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 466 MAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 538
Cdd:PRK12467 3430 VPVGVAGELYIGGVGLARGYHQRPSLTAERFVADpfsgsgGRLYrTGDLARYRADGVIEYLGRIDHQVKI-RGFRIELGE 3508
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 557878740 539 IENIYMRSEPVAQVFVHGESLQA--FLIAIVVPDVETlCSWAQK 580
Cdd:PRK12467 3509 IEARLLQHPSVREAVVLARDGAGgkQLVAYVVPADPQ-GDWRET 3551
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
388-572 |
2.40e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 63.38 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 388 SSLggrvRLMVTGAAPVSATVLtflRAAL---GCQFYEGYGQTEcTAGCCLTMPGDWTA--GHVGAPMPCNlIKLVDvEE 462
Cdd:PRK08276 262 SSL----RVAIHAAAPCPVEVK---RAMIdwwGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGE-VRILD-ED 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 463 MNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGkWL-PNGTLKIIDRKKHIFkLAQGEYIAPEKIEN 541
Cdd:PRK08276 332 GNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVG-YLdEDGYLYLTDRKSDMI-ISGGVNIYPQEIEN 409
|
170 180 190
....*....|....*....|....*....|.
gi 557878740 542 IYMRSEPVAQVFVHGeslqafliaivVPDVE 572
Cdd:PRK08276 410 LLVTHPKVADVAVFG-----------VPDEE 429
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
195-552 |
2.99e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 63.25 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 195 AYGSELvergQRCGVEVTSMkAMEDL---GRANRRKPKPPAP-EDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKAT 270
Cdd:PRK05851 114 SHGSHL----ERLRAVDSSV-TVHDLataAHTNRSASLTPPDsGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 271 ENTVnpcPDDTLISFLPLAH-MFERVVECVMLChGAKIGffqgdirllmddlkvLQPT-VFPVVP-RLLNrmfdrifgqa 347
Cdd:PRK05851 189 GLDA---ATDVGCSWLPLYHdMGLAFLLTAALA-GAPLW---------------LAPTtAFSASPfRWLS---------- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 348 nttlkrWLLDF-ASKRKEAELRSGIIRNNSlwdrlifHKVQSSLGGRVRLMVTGAAPVSATVLT-FLRAALGCQFYEG-- 423
Cdd:PRK05851 240 ------WLSDSrATLTAAPNFAYNLIGKYA-------RRVSDVDLGALRVALNGGEPVDCDGFErFATAMAPFGFDAGaa 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 424 ---YGQTECTagCCLTMP---------------GDWTAGH--VGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQ 483
Cdd:PRK05851 307 apsYGLAEST--CAVTVPvpgiglrvdevttddGSGARRHavLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMS 384
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557878740 484 GYLKDPAktaeaLDKDGWLHTGDIGkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIymrsepVAQV 552
Cdd:PRK05851 385 GYLGQAP-----IDPDDWFPTGDLG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERV------AAQV 440
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
150-570 |
3.15e-10 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 62.79 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 150 EAITYIVN--KAELSLVFVDkpekaklLLEGVENKLIPGLKIIVV------MDAYGSELVERGQRCGvevtsMKAMEDLG 221
Cdd:PRK12406 73 EEIAYILEdsGARVLIAHAD-------LLHGLASALPAGVTVLSVptppeiAAAYRISPALLTPPAG-----AIDWEGWL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 222 RANRRKPKPPAPEDLAVIcFTSGTTGNPKGamvthrnivsdcsafVKATentvNPCPDDTL--ISFLPLAHMFERVVECV 299
Cdd:PRK12406 141 AQQEPYDGPPVPQPQSMI-YTSGTTGHPKG---------------VRRA----APTPEQAAaaEQMRALIYGLKPGIRAL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 300 M---LCHGAKIGFFQGDIRLlmDDLKVLQP-----------------TVFpVVPRllnrMFDRifgqanttlkrwLLDFA 359
Cdd:PRK12406 201 LtgpLYHSAPNAYGLRAGRL--GGVLVLQPrfdpeellqlierhritHMH-MVPT----MFIR------------LLKLP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 360 SKRKEAelrsgiirnnslWDrlifhkvQSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLTMPG 439
Cdd:PRK12406 262 EEVRAK------------YD-------VSSL----RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE-SGAVTFATSE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 440 DWTA--GHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNV--FQgYLKDPAKTAEaLDKDGWLHTGDIGKWLPNGT 515
Cdd:PRK12406 318 DALShpGTVGKAAPGAELRFVD-EDGRPLPQGEIGEIYSRIAGNpdFT-YHNKPEKRAE-IDRGGFITSGDVGYLDADGY 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 557878740 516 LKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG---ESLQAFLIAIVVPD 570
Cdd:PRK12406 395 LFLCDRKRDMV-ISGGVNIYPAEIEAVLHAVPGVHDCAVFGipdAEFGEALMAVVEPQ 451
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
139-574 |
5.98e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 62.35 E-value: 5.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 139 VIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAklLLEGVEnklIPGLKIIVVMDAYGSELVERGQRCgvevtsmkame 218
Cdd:PRK13388 78 VLVGLNTTRRGAALAADIRRADCQLLVTDAEHRP--LLDGLD---LPGVRVLDVDTPAYAELVAAAGAL----------- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 219 dlgranrrKP-KPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMfervvE 297
Cdd:PRK13388 142 --------TPhREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLT----RDDVCYVSMPLFHS-----N 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 298 CVM------LCHGAKI---------GFfqgdirllMDDLKVLQPTVFPVVPRLL-------NRMFDrifgqANTTLKRWL 355
Cdd:PRK13388 205 AVMagwapaVASGAAValpakfsasGF--------LDDVRRYGATYFNYVGKPLayilatpERPDD-----ADNPLRVAF 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 356 LDFASKRKEAElrsgiirnnslwdrlifhkvqsslggrvrlmvtgaapvsatvltFLRAaLGCQFYEGYGQTEctAGCCL 435
Cdd:PRK13388 272 GNEASPRDIAE--------------------------------------------FSRR-FGCQVEDGYGSSE--GAVIV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 436 TMPGDWTAGHVGAPMPCnlIKLVDVEEM---------------NymAAEGEGE-VCVKGPNVFQGYLKDPAKTAEALdKD 499
Cdd:PRK13388 305 VREPGTPPGSIGRGAPG--VAIYNPETLtecavarfdahgallN--ADEAIGElVNTAGAGFFEGYYNNPEATAERM-RH 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557878740 500 GWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFVHG----ESLQAFLIAIVVPDVETL 574
Cdd:PRK13388 380 GMYWSGDLAYRDADGWIYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYAvpdeRVGDQVMAALVLRDGATF 457
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
234-572 |
3.27e-09 |
|
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: 59.80 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 234 EDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATENTVNPCPDDTLISFLPLAH--MFERVVECvmLCHGAKIGFFQ 311
Cdd:cd17656 128 DDLLYIIYTSGTTGKPKGVQLEHKNMVN----LLHFEREKTNINFSDKVLQFATCSFdvCYQEIFST--LLSGGTLYIIR 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 312 GDIRLLMDDLKVL------QPTVFPVVprLLNRMFDrifgqanttLKRWLLDFASKRKEAeLRSG--IIRNNSLWDRLIF 383
Cdd:cd17656 202 EETKRDVEQLFDLvkrhniEVVFLPVA--FLKFIFS---------EREFINRFPTCVKHI-ITAGeqLVITNEFKEMLHE 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 384 HkvqsslggrvrlmvtgaapvsatvltflraalGCQFYEGYGQTEC-TAGCCLTMPGDWTAGH--VGAPMPCNLIKLVDv 460
Cdd:cd17656 270 H--------------------------------NVHLHNHYGPSEThVVTTYTINPEAEIPELppIGKPISNTWIYILD- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 461 EEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 534
Cdd:cd17656 317 QEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-RGYRI 395
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 557878740 535 APEKIENIYMRSEPVAQ--VFVHGESL-QAFLIAIVVPDVE 572
Cdd:cd17656 396 ELGEIEAQLLNHPGVSEavVLDKADDKgEKYLCAYFVMEQE 436
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
230-540 |
5.29e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 59.25 E-value: 5.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 230 PPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFvkaTENTVNPCPDDTLISFLPLAH-MfervvecvmlchgAKIG 308
Cdd:PRK09192 172 RPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAI---SHDGLKVRPGDRCVSWLPFYHdM-------------GLVG 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 309 FFQGDI--RLLMDDLKVLQptvFPVVPRLLNRMFDR---------IFG------------QANTTLKRW----------- 354
Cdd:PRK09192 236 FLLTPVatQLSVDYLPTRD---FARRPLQWLDLISRnrgtisyspPFGyelcarrvnskdLAELDLSCWrvagigadmir 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 355 ---LLDFASKRKEA-----------------------ELRSGIIRNNSLWDRLIFHKVQSSLGGRVRlmvtgaaPVSATV 408
Cdd:PRK09192 313 pdvLHQFAEAFAPAgfddkafmpsyglaeatlavsfsPLGSGIVVEEVDRDRLEYQGKAVAPGAETR-------RVRTFV 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 409 LtflraalgcqfyegygqtectagcCltmpgdwtaghvGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKD 488
Cdd:PRK09192 386 N------------------------C------------GKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLMSGYFRD 428
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 557878740 489 PAkTAEALDKDGWLHTGDIGkWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIE 540
Cdd:PRK09192 429 EE-SQDVLAADGWLDTGDLG-YLLDGYLYITGRAKDLI-IINGRNIWPQDIE 477
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
231-574 |
5.85e-09 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 58.64 E-value: 5.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 231 PAPEDLAVICFTSGTTGNPKGAMVTHR----NIVSDCSAFvkatentvNPCPDDTLIsFLPLAHMFERVVECVM-LCHGA 305
Cdd:cd17654 115 RTDECLAYVIHTSGTTGTPKIVAVPHKcilpNIQHFRSLF--------NITSEDILF-LTSPLTFDPSVVEIFLsLSSGA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 306 KIgffqgdirllmddlkVLQPTVFPVVPRLLNRMFDRIFG----QANTTLKRwllDFASKRKEAELRSGIirnnslwdrl 381
Cdd:cd17654 186 TL---------------LIVPTSVKVLPSKLADILFKRHRitvlQATPTLFR---RFGSQSIKSTVLSAT---------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 382 ifhkvqSSLggRVrLMVTGAAPVSATVLTFLRAA-LGCQFYEGYGQTECTAGCCL-TMPGDWTAGHVGAPMPCNLIKLVD 459
Cdd:cd17654 238 ------SSL--RV-LALGGEPFPSLVILSSWRGKgNRTRIFNIYGITEVSCWALAyKVPEEDSPVQLGSPLLGTVIEVRD 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 460 VEemnymAAEGEGEVCVKGPNVfQGYLKDPAKTAEALdkdgWLHTGDIGKwLPNGTLKIIDRKKHIFKLAqGEYIAPEKI 539
Cdd:cd17654 309 QN-----GSEGTGQVFLGGLNR-VCILDDEVTVPKGT----MRATGDFVT-VKDGELFFLGRKDSQIKRR-GKRINLDLI 376
|
330 340 350
....*....|....*....|....*....|....*
gi 557878740 540 ENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETL 574
Cdd:cd17654 377 QQVIESCLGVESCAVTLSDQQRLIAFIVGESSSSR 411
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
208-572 |
1.02e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 58.82 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 208 GVEVTSMKA-MEDLGRANrrKPKPPAPEDLAVICFTSGTTGNPKGAMVTHrnivSDCSAFVKATENTVNPCPDDTLISFL 286
Cdd:PRK12316 3171 GVQVLDLDRgDENYAEAN--PAIRTMPENLAYVIYTSGSTGKPKGVGIRH----SALSNHLCWMQQAYGLGVGDRVLQFT 3244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 287 PLAHMFERVVECVMLCHGAKIgffqgdirllmddlkVLQPTVFPVVPRLLNRMFDRifGQANTTLKRWlldfaskrkeae 366
Cdd:PRK12316 3245 TFSFDVFVEELFWPLMSGARV---------------VLAGPEDWRDPALLVELINS--EGVDVLHAYP------------ 3295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 367 lrsgiirnnSLWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLtflRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGH- 445
Cdd:PRK12316 3296 ---------SMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQ---QVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAv 3363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 446 -VGAPMPCNLIKLVDVEeMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGW------LHTGDIGKWLPNGTLKI 518
Cdd:PRK12316 3364 pIGRPIANRACYILDGS-LEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEY 3442
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 557878740 519 IDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAfLIAIVVPDVE 572
Cdd:PRK12316 3443 IGRVDHQVKI-RGFRIELGEIEARLLEHPWVREAVVLAVDGRQ-LVAYVVPEDE 3494
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
185-556 |
1.71e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 57.59 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 185 PGLKIIVVMDAYGSELVERGqrcGVEVTSMKAMEDLGRAnrrkPKPPAPEDLAVICfTSGTTGNPKGAMVTHRNIVSdcS 264
Cdd:PRK07798 122 PKLRTLVVVEDGSGNDLLPG---AVDYEDALAAGSPERD----FGERSPDDLYLLY-TGGTTGMPKGVMWRQEDIFR--V 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 265 AFVKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAK-----IGFFQGdirllmddlkvlQPTVFPVVPRL---- 335
Cdd:PRK07798 192 LLGGRDFATGEPIEDEEELAKRAAAGPGMRRFPAPPLMHGAGqwaafAALFSG------------QTVVLLPDVRFdade 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 336 ---------LNRMFdrIFGQAnttLKRWLLDFASKRKEAELrsgiirnnslwdrlifhkvqSSLggrvRLMVTGAAPVSA 406
Cdd:PRK07798 260 vwrtierekVNVIT--IVGDA---MARPLLDALEARGPYDL--------------------SSL----FAIASGGALFSP 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 407 TVLTFLRAAL-GCQFYEGYGQTEctAGCCLTMPGDWTAGHVGAP--MPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQ 483
Cdd:PRK07798 311 SVKEALLELLpNVVLTDSIGSSE--TGFGGSGTVAKGAVHTGGPrfTIGPRTVVLDEDGNPVEPGSGEIGWIARRGHIPL 388
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557878740 484 GYLKDPAKTAEAL-DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIyMRSEP-VAQVFVHG 556
Cdd:PRK07798 389 GYYKDPEKTAETFpTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTG-GEKVFPEEVEEA-LKAHPdVADALVVG 463
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
218-573 |
3.14e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 56.86 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 218 EDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFV-----KATENTVNPCPddtlisflplahMF 292
Cdd:PRK07788 191 DDLIAGSSTAPLPKPPKPGGIVILTSGTTGTPKGAPRPEPSPLAPLAGLLsrvpfRAGETTLLPAP------------MF 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 293 ervvecvmlcHG-----AKIGFFQG---------DIRLLMDDLKVLQPTVFPVVPRLLNRMFDrifgqanttlkrwLLDF 358
Cdd:PRK07788 259 ----------HAtgwahLTLAMALGstvvlrrrfDPEATLEDIAKHKATALVVVPVMLSRILD-------------LGPE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 359 ASKRKEAelrsgiirnnslwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECtAGCCLTMP 438
Cdd:PRK07788 316 VLAKYDT----------------------SSL----KIIFVSGSALSPELATRALEAFGPVLYNLYGSTEV-AFATIATP 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 439 GDWTA--GHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAealdKDGWLHTGDIGKWLPNGTL 516
Cdd:PRK07788 369 EDLAEapGTVGRPPKGVTVKILD-ENGNEVPRGVVGRIFVGNGFPFEGYTDGRDKQI----IDGLLSSGDVGYFDEDGLL 443
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 557878740 517 KIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHGeslqafliaivVPDVET 573
Cdd:PRK07788 444 FVDGRDDDMI-VSGGENVFPAEVEDLLAGHPDVVEAAVIG-----------VDDEEF 488
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
239-570 |
5.28e-08 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 55.10 E-value: 5.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 239 ICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDTLISFLPLAH-MFERVVECVMLCHGAKIGFFQGDIRLL 317
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERSWI----ESFVCNEDLFNISGEDAILAPGPLSHsLFLYGAISALYLGGTFIGQRKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 318 MDDLKVLQPTVFPVVPRLLnrmfdrifgqanttlkrwlldfaskrkEAELRSGIIRnnslwdrlifHKVQSSLGGrvrlm 397
Cdd:cd17633 81 IRKINQYNATVIYLVPTML---------------------------QALARTLEPE----------SKIKSIFSS----- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 398 vtGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCnliklVDVEEMNymAAEGE-GEVCV 476
Cdd:cd17633 119 --GQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYNFNQESRPPNSVGRPFPN-----VEIEIRN--ADGGEiGKIFV 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 477 KGPNVFQGYLKdpaktAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG 556
Cdd:cd17633 190 KSEMVFSGYVR-----GGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIEEAIVVG 263
|
330
....*....|....*..
gi 557878740 557 ESLQAF---LIAIVVPD 570
Cdd:cd17633 264 IPDARFgeiAVALYSGD 280
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
446-604 |
5.53e-08 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 55.67 E-value: 5.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 446 VGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL-DKDGW--LHTGDIGKwLPNGTLKIIDRK 522
Cdd:PRK04813 320 IGYAKPDSPLLIID-EEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGY-LEDGLLFYQGRI 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 523 KHIFKLAqGEYIAPEKIENIYMRSEPVAQVFV----HGESLQAfLIAIVVPDvetlcswaqkrgfEGSFEelcRNKDVKK 598
Cdd:PRK04813 398 DFQIKLN-GYRIELEEIEQNLRQSSYVESAVVvpynKDHKVQY-LIAYVVPK-------------EEDFE---REFELTK 459
|
....*.
gi 557878740 599 AILEDM 604
Cdd:PRK04813 460 AIKKEL 465
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
234-565 |
5.87e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 56.33 E-value: 5.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 234 EDLAVICFTSGTTGNPKGAMVTHRNIVSDcsafVKATENTVNPCPDDTLISFLPLAhmFE-RVVECVM-LCHGAKIGFF- 310
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNTHAALAER----LQWMQATYALDDSDVLMQKAPIS--FDvSVWECFWpLITGCRLVLAg 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 311 ---QGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQANTTLKRwlLDFASKRKEAELRsgiirnnslwDRLIFHKVQ 387
Cdd:PRK05691 1347 pgeHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRR--LFSGGEALPAELR----------NRVLQRLPQ 1414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 388 SSLGGRvrlmvtgaapvsatvltflraalgcqfyegYGQTE----CTAGCCLTMPGDWTAghVGAPMPCNLIKLVDvEEM 463
Cdd:PRK05691 1415 VQLHNR------------------------------YGPTEtainVTHWQCQAEDGERSP--IGRPLGNVLCRVLD-AEL 1461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 464 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAE-----ALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAP 536
Cdd:PRK05691 1462 NLLPPGVAGELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL-RGFRVEP 1540
|
330 340 350
....*....|....*....|....*....|.
gi 557878740 537 EKIENIYMRSEPVAQ--VFVHGESLQAFLIA 565
Cdd:PRK05691 1541 EEIQARLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
209-290 |
7.70e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 55.33 E-value: 7.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 209 VEVTSMkameDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDC----SAFVKATENTvnPCPDDTLIS 284
Cdd:PRK05850 139 IEVDLL----DLDSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFeqlmSDYFGDTGGV--PPPDTTVVS 212
|
....*.
gi 557878740 285 FLPLAH 290
Cdd:PRK05850 213 WLPFYH 218
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
227-620 |
1.21e-07 |
|
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: 54.74 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 227 KPKPPAPE-DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCPddTLISFLPLAHmfervveCVMLCHGA 305
Cdd:cd05915 145 ADPVRVPErAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKD--VVLPVVPMFH-------VNAWCLPY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 306 KIGFFQGDIRLLMDdlkVLQPTVfpvvprllnrMFDRIFGQANTTL--KRWLLDFASKRKEAelrsgiirnnslwdrlif 383
Cdd:cd05915 216 AATLVGAKQVLPGP---RLDPAS----------LVELFDGEGVTFTagVPTVWLALADYLES------------------ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 384 hkVQSSLGGRVRLMVTGAAPvsATVLTFLRAALGCQFYEGYGQTEC--TAGCCLTMPgDWT------AGHVGAPMPCN-L 454
Cdd:cd05915 265 --TGHRLKTLRRLVVGGSAA--PRSLIARFERMGVEVRQGYGLTETspVVVQNFVKS-HLEslseeeKLTLKAKTGLPiP 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 455 IKLVDVEEMNYMAAEGEGE----VCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAq 530
Cdd:cd05915 340 LVRLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG- 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 531 GEYIAPEKIENIYMRSEPVAQVFVHGEslqafliaivvPDV---ETLCSWAQKRGFEGSFEEL---CRNKDVKKAILEDM 604
Cdd:cd05915 419 GEWISSVDLENALMGHPKVKEAAVVAI-----------PHPkwqERPLAVVVPRGEKPTPEELnehLLKAGFAKWQLPDA 487
|
410
....*....|....*.
gi 557878740 605 VRLGKDSGLKPFEQVK 620
Cdd:cd05915 488 YVFAEEIPRTSAGKFL 503
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
59-567 |
2.43e-07 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 53.88 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 59 MQSVEVAGSGGARRSALLDSDEPlVYFYDDVTT---LYEGFQR-GIQVSNNGPCLGSR----KPDQPyewlsykQWVIIE 130
Cdd:PRK06060 1 MRNGNLAGLLAEQASEAGWYDRP-AFYAADVVThgqIHDGAARlGEVLRNRGLSSGDRvllcLPDSP-------DLVQLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 131 QGCFAYSMvivplydtlgneaityivnkaelsLVFVDKPEKAKlllegvENKLIPGLKIIVVMDAYGSELVERGQRCGVe 210
Cdd:PRK06060 73 LACLARGV------------------------MAFLANPELHR------DDHALAARNTEPALVVTSDALRDRFQPSRV- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 211 VTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMvtHRNivSDCSAFVKAT-ENTVNPCPDDtlisflpla 289
Cdd:PRK06060 122 AEAAELMSEAARVAPGGYEPMGGDALAYATYTSGTTGPPKAAI--HRH--ADPLTFVDAMcRKALRLTPED--------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 290 hmfervvecVMLChGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPrllnrmfdrIFGQANTTLkrwlldfaSKRKEAELRS 369
Cdd:PRK06060 189 ---------TGLC-SARMYFAYGLGNSVWFPLATGGSAVINSAP---------VTPEAAAIL--------SARFGPSVLY 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 370 GIirnNSLWDRLIFHKVQSSLGGrVRLMVTGAAPVSATVLTFLRAALG-CQFYEGYGQTECTAGCCLTMPGDWTAGHVGA 448
Cdd:PRK06060 242 GV---PNFFARVIDSCSPDSFRS-LRCVVSAGEALELGLAERLMEFFGgIPILDGIGSTEVGQTFVSNRVDEWRLGTLGR 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 449 PMPCNLIKLVdVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTaeaLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIfKL 528
Cdd:PRK06060 318 VLPPYEIRVV-APDGTTAGPGVEGDLWVRGPAIAKGYWNRPDSP---VANEGWLDTRDRVCIDSDGWVTYRCRADDT-EV 392
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 557878740 529 AQGEYIAPEKIENIYMRSEPVAQVFVHG-------ESLQAFLIAIV 567
Cdd:PRK06060 393 IGGVNVDPREVERLIIEDEAVAEAAVVAvrestgaSTLQAFLVATS 438
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
231-556 |
4.76e-07 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 52.38 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 231 PAPEDLAVICfTSGTTGNPKGAMVTHRNIVSdcSAFVKATENTVNPCPDD---------TLISFLPLAHmfervvecvmL 301
Cdd:cd05924 1 RSADDLYILY-TGGTTGMPKGVMWRQEDIFR--MLMGGADFGTGEFTPSEdahkaaaaaAGTVMFPAPP----------L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 302 CHGAK-----IGFFQGDiRLLMDDLKVLQPTVFPVVPR-LLNRMFdrIFGQAnttLKRWLLDfaskrkeaELRSGiiRNN 375
Cdd:cd05924 68 MHGTGswtafGGLLGGQ-TVVLPDDRFDPEEVWRTIEKhKVTSMT--IVGDA---MARPLID--------ALRDA--GPY 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 376 SLwdrlifhkvqSSLggrvRLMVTGAAPVSATVLT-FLRAALGCQFYEGYGQTECTA-GCCLTMPGDWTAGHVGAPMPcn 453
Cdd:cd05924 132 DL----------SSL----FAISSGGALLSPEVKQgLLELVPNITLVDAFGSSETGFtGSGHSAGSGPETGPFTRANP-- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 454 LIKLVDvEEMNYM--AAEGEGEVCVKGpNVFQGYLKDPAKTAEAL-DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKL 528
Cdd:cd05924 196 DTVVLD-DDGRVVppGSGGVGWIARRG-HIPLGYYGDEAKTAETFpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINT 273
|
330 340
....*....|....*....|....*....
gi 557878740 529 AqGEYIAPEKIENIyMRSEP-VAQVFVHG 556
Cdd:cd05924 274 G-GEKVFPEEVEEA-LKSHPaVYDVLVVG 300
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
220-555 |
6.69e-07 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 52.74 E-value: 6.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 220 LGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIV------------SDCSAFVKATentvnPCPDDtlIS--- 284
Cdd:PRK10252 584 LAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVnrllwmqnhyplTADDVVLQKT-----PCSFD--VSvwe 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 285 -FLPlahmfervvecvMLChGAKIGFFQGD-------IRLLMDDLKVlqpTVFPVVPRLL----NRMFDRIFGQANTTLK 352
Cdd:PRK10252 657 fFWP------------FIA-GAKLVMAEPEahrdplaMQQFFAEYGV---TTTHFVPSMLaafvASLTPEGARQSCASLR 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 353 RWlldFASKRK-EAELRsgiirnnSLWDRLIfhkvqsslggrvrlmvtgAAPVsatvltflraalgcqfYEGYGQTECT- 430
Cdd:PRK10252 721 QV---FCSGEAlPADLC-------REWQQLT------------------GAPL----------------HNLYGPTEAAv 756
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 431 ------AGccltmpGDWTAGHVGAPMPCNL------IKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDK 498
Cdd:PRK10252 757 dvswypAF------GEELAAVRGSSVPIGYpvwntgLRILD-ARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIA 829
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557878740 499 DGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFVH 555
Cdd:PRK10252 830 DPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKI-RGQRIELGEIDRAMQALPDVEQAVTH 891
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
232-565 |
2.96e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 50.94 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 232 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFV--------KATENTVNPCPDDTLISFLPlAHMFERVVECV--ML 301
Cdd:PRK05691 3867 GPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVpylalseaDVIAQTASQSFDISVWQFLA-APLFGARVEIVpnAI 3945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 302 CHgakigffqgDIRLLMDDLKVLQPTVFPVVPRLLNRMF--DRifgQANTTLkRWLLDfaskrkeaelrsgiirnnslwd 379
Cdd:PRK05691 3946 AH---------DPQGLLAHVQAQGITVLESVPSLIQGMLaeDR---QALDGL-RWMLP---------------------- 3990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 380 rlifhkvqsslggrvrlmvTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCL-TMPGDWTAGH---VGAPMPCNLI 455
Cdd:PRK05691 3991 -------------------TGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFfRVDLASTRGSylpIGSPTDNNRL 4051
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 456 KLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGW-------LHTGDIGKWLPNGTLKIIDRKKHIFKL 528
Cdd:PRK05691 4052 YLLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRRSDGVLEYVGRIDHQVKI 4130
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 557878740 529 aQGEYIAPEKIENIYMRSEPV------AQVFVHGESLQAFLIA 565
Cdd:PRK05691 4131 -RGYRIELGEIEARLHEQAEVreaavaVQEGVNGKHLVGYLVP 4172
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
233-581 |
4.22e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 50.34 E-value: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 233 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATEntvnpcpddtlisfLPLAhmfERVVECVMLCHGAKIGFFQG 312
Cdd:PRK12316 654 PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYG--------------LGVG---DTVLQKTPFSFDVSVWEFFW 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 313 DirlLMDDLKVLqptvfpVVPRLLNRMFDRIFGQANTTLKRwLLDFASKRKEAELRSGiirnnslwdrlifhKVQSSLGg 392
Cdd:PRK12316 717 P---LMSGARLV------VAAPGDHRDPAKLVELINREGVD-TLHFVPSMLQAFLQDE--------------DVASCTS- 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 393 rVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTAGCCltmpgDWTAGH-------VGAPMPCNLIKLVDVeEMN 464
Cdd:PRK12316 772 -LRRIVCSGEALPADAQEQVFAKLpQAGLYNLYGPTEAAIDVT-----HWTCVEeggdsvpIGRPIANLACYILDA-NLE 844
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 465 YMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL------DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 538
Cdd:PRK12316 845 PVPVGVLGELYLAGRGLARGYHGRPGLTAERFvpspfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKL-RGLRIELGE 923
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 557878740 539 IENIYMRSEPVAQVFVHGESLQAfLIAIVVPD------VETLCSWAQKR 581
Cdd:PRK12316 924 IEARLLEHPWVREAAVLAVDGKQ-LVGYVVLEseggdwREALKAHLAAS 971
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
216-290 |
7.03e-06 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 49.10 E-value: 7.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 216 AMEDLGRANRRKPKPPAP-------EDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVkateNTVNPCPDDTLISFLPL 288
Cdd:PRK08279 174 GYEDLAAAAAGAPTTNPAsrsgvtaKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFG----GLLRLTPDDVLYCCLPL 249
|
..
gi 557878740 289 AH 290
Cdd:PRK08279 250 YH 251
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
199-291 |
8.48e-06 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 48.83 E-value: 8.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 199 ELVERGQRCGV--EVTSMKAMEDLGRANRRKPKPPAPEDL---------AVICFTSGTTGNPKGAMVTHRNIVSdCSAFV 267
Cdd:cd05938 98 ALRADGVSVWYlsHTSNTEGVISLLDKVDAASDEPVPASLrahvtikspALYIYTSGTTGLPKAARISHLRVLQ-CSGFL 176
|
90 100
....*....|....*....|....
gi 557878740 268 KATentvNPCPDDTLISFLPLAHM 291
Cdd:cd05938 177 SLC----GVTADDVIYITLPLYHS 196
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
230-572 |
1.59e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 48.08 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 230 PPAPEDL--AVICFTSGTTGNPKGAM--VTHRNIVSDCSAFVKATENTVNPCPDDTLISFLPLAHMFE-RVVECVMLCHG 304
Cdd:PRK13390 142 PRLTEQPcgAVMLYSSGTTGFPKGIQpdLPGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHAAPlRWCSMVHALGG 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 305 AKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskRKEAELRSGiirnnslwdrlifH 384
Cdd:PRK13390 222 TVVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLL---------------------KLDADVRTR-------------Y 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 385 KVQSslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLTMPGDWTA--GHVGAPMPCNLiKLVDvEE 462
Cdd:PRK13390 268 DVSS-----LRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGRSVLGDL-HICD-DD 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 463 MNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIE 540
Cdd:PRK13390 340 GNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQETE 418
|
330 340 350
....*....|....*....|....*....|..
gi 557878740 541 NIYMRSEPVAQVFVHGeslqafliaivVPDVE 572
Cdd:PRK13390 419 NALTMHPAVHDVAVIG-----------VPDPE 439
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
233-560 |
6.34e-05 |
|
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: 45.89 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 233 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFvkatENTVNPCPDDTLISFLPLAH---MFERVVECVMlcHGAKIGF 309
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLL----SHDLNLKNGDRTYTCMPLYHgtaAFLGACNCLM--SGGTLAL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 310 ---FQgdIRLLMDDLKVLQPTVFPVVPRLLnrmfdrifgqanttlkRWLLdfaskrkeaelrSGIIrnnSLWDRLifHKV 386
Cdd:cd05937 160 srkFS--ASQFWKDVRDSGATIIQYVGELC----------------RYLL------------STPP---SPYDRD--HKV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 387 QSSLGGRVRLMVTGAapvsatvltfLRAALGC-QFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVE---- 461
Cdd:cd05937 205 RVAWGNGLRPDIWER----------FRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKFENQVvlvk 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 462 -----EMNYM---------AAEGE-GEVCVKGPNV----FQGYLKDPAKTAEALDK------DGWLHTGDIGKWLPNGTL 516
Cdd:cd05937 275 mdpetDDPIRdpktgfcvrAPVGEpGEMLGRVPFKnreaFQGYLHNEDATESKLVRdvfrkgDIYFRTGDLLRQDADGRW 354
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 557878740 517 KIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFVHGESLQ 560
Cdd:cd05937 355 YFLDRLGDTFRW-KSENVSTTEVADVLGAHPDIAEANVYGVKVP 397
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
471-556 |
7.97e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 45.54 E-value: 7.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 471 EGEVCVKGPNVFQGYLKDpAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVA 550
Cdd:PRK07638 333 IGTVYVKSPQFFMGYIIG-GVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIESVLHEHPAVD 410
|
....*.
gi 557878740 551 QVFVHG 556
Cdd:PRK07638 411 EIVVIG 416
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
227-570 |
9.21e-05 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 45.04 E-value: 9.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 227 KPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSdcSAfvKATENTVNPcPDDTLISfLPLAHmfervvecvmlchgak 306
Cdd:PRK07824 28 RVGEPIDDDVALVVATSGTTGTPKGAMLTAAALTA--SA--DATHDRLGG-PGQWLLA-LPAHH---------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 307 IGFFQGDIRLLM---DDLKVLQPTVF--PVVPRLLNRM-FDRIF-GQANTTLKRWLLDFASKRKEAELRSGIIrnnslwd 379
Cdd:PRK07824 86 IAGLQVLVRSVIagsEPVELDVSAGFdpTALPRAVAELgGGRRYtSLVPMQLAKALDDPAATAALAELDAVLV------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 380 rlifhkvqsslggrvrlmvtGAAPVSATVLTflRA-ALGCQFYEGYGQTEcTAGCCLtmpgdwtagHVGAPMPCNLIKLV 458
Cdd:PRK07824 159 --------------------GGGPAPAPVLD--AAaAAGINVVRTYGMSE-TSGGCV---------YDGVPLDGVRVRVE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 459 DveemnymaaegeGEVCVKGPNVFQGY--LKDPAKTAEaldkDGWLHTGDIGKwLPNGTLKIIDRKKHIFKLAqGEYIAP 536
Cdd:PRK07824 207 D------------GRIALGGPTLAKGYrnPVDPDPFAE----PGWFRTDDLGA-LDDGVLTVLGRADDAISTG-GLTVLP 268
|
330 340 350
....*....|....*....|....*....|....*..
gi 557878740 537 EKIENIYMRSEPVAQVFVHG---ESLQAFLIAIVVPD 570
Cdd:PRK07824 269 QVVEAALATHPAVADCAVFGlpdDRLGQRVVAAVVGD 305
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
139-256 |
2.01e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 44.50 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 139 VIVPLYDTLGNEAITYIVNKAELSlVFVDKPEkaklLLEGVENKLIPGLKIIVVMDAYGSELvergqrcGVEVTSMKAME 218
Cdd:PRK04319 124 IVGPLFEAFMEEAVRDRLEDSEAK-VLITTPA----LLERKPADDLPSLKHVLLVGEDVEEG-------PGTLDFNALME 191
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 557878740 219 DlgrANRRKPKPP-APEDLAVICFTSGTTGNPKG------AMVTH 256
Cdd:PRK04319 192 Q---ASDEFDIEWtDREDGAILHYTSGSTGKPKGvlhvhnAMLQH 233
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
233-528 |
1.09e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.46 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 233 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKatenTVNPCPDDtlisflplahmfervveCVMlcHGAKIGFFQG 312
Cdd:PRK05691 2332 PQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIE----RFGMRADD-----------------CEL--HFYSINFDAA 2388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 313 DIRLLmddlkvlqptvfpvVPRLLN-RMFDRIFGQanttlkrWlldfaskrkEAELRSGIIRNNSLwDRLIFHKVQSS-- 389
Cdd:PRK05691 2389 SERLL--------------VPLLCGaRVVLRAQGQ-------W---------GAEEICQLIREQQV-SILGFTPSYGSql 2437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 390 ---LGGR-----VRLMVTGAAPVSATVLTFLRAALGCQ-FYEGYGQTE-------CTAGccLTMPGDWTAGHVGAPMPCN 453
Cdd:PRK05691 2438 aqwLAGQgeqlpVRMCITGGEALTGEHLQRIRQAFAPQlFFNAYGPTEtvvmplaCLAP--EQLEEGAASVPIGRVVGAR 2515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878740 454 LIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIF 526
Cdd:PRK05691 2516 VAYILD-ADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdggrlyrTGDLVRLRADGLVEYVGRIDHQV 2594
|
..
gi 557878740 527 KL 528
Cdd:PRK05691 2595 KI 2596
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
225-256 |
1.64e-03 |
|
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: 41.41 E-value: 1.64e-03
10 20 30
....*....|....*....|....*....|..
gi 557878740 225 RRKPKPPAPEDLAVICFTSGTTGNPKGAMVTH 256
Cdd:cd17634 223 EHQPEAMNAEDPLFILYTSGTTGKPKGVLHTT 254
|
|
| |
