|
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 ... |
116-693 |
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: 908.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 116 QPYQWLSYQEVAKRAEFLGSGLLQHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADI 195
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 196 CTVIVDKphkatlllehverketpglklvilmepfedalrergkkcGVDIKSMQAIEDCGRENHHAPVPPRPDDLSIVCF 275
Cdd:cd05927 81 SIVFCDA---------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 276 TSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTCADVHFSYLPLAHMFERMVQSVVYCHGGRVGFFQGDIRLLSDDM 355
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 356 KALRPTIFPVVPRLLNRMYDKIFH--QADTSLKRWLLEFAAKRKQAEVRSGIIRNNSIWDELFFNKIQASLGGHVRMIVT 433
Cdd:cd05927 202 KALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 434 GAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYW--TCKGEGEICVK 511
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDakDPNPRGEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 512 GPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGD 591
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 592 SLKAFLVGIVVPDPEVMPSWAQKK-GIEGTYQELCMKKELKKAILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLL 670
Cdd:cd05927 442 SLKSFLVAIVVPDPDVLKEWAASKgGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLL 521
|
570 580
....*....|....*....|...
gi 1907081036 671 TPTLKAKRPELREYFKKQIEELY 693
Cdd:cd05927 522 TPTFKLKRPQLKKYYKKQIDEMY 544
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
79-693 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 697.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 79 TQLLTHY--YDDARTMYQVFRRGLSISGNGPCLGFRKPEQ----PYQWLSYQEVAKRAEFLGSGLLQHDCKVGteQFVGV 152
Cdd:PLN02736 31 LKLVSRFpdHPEIGTLHDNFVYAVETFRDYKYLGTRIRVDgtvgEYKWMTYGEAGTARTAIGSGLVQHGIPKG--ACVGL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 153 FAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIVdKPHKATLLLEHVerKETPGLKLVILMEPFED 232
Cdd:PLN02736 109 YFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCL--SEIPSVRLIVVVGGADE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 233 ALRERGKKCGVDIKSMQAIEDCGRENHHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESqwAPtc 312
Cdd:PLN02736 186 PLPSLPSGTGVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKF--YP-- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 313 ADVHFSYLPLAHMFERMVQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTS--LKRWLL 390
Cdd:PLN02736 262 SDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESggLKERLF 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 391 EFAAKRKQAEVRSGiiRNNS-IWDELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF 469
Cdd:PLN02736 342 NAAYNAKKQALENG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 470 TTPGDWTSGHVGAPLPCNHIKLVDAEELNYwTCKGE----GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWL 545
Cdd:PLN02736 420 MDEGDNLSGHVGSPNPACEVKLVDVPEMNY-TSEDQpyprGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWL 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 546 PEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKKGIE-GTYQEL 624
Cdd:PLN02736 499 PGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQL 578
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081036 625 CMKKELKKAILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 693
Cdd:PLN02736 579 CNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMY 647
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
86-693 |
1.51e-175 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 514.26 E-value: 1.51e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 86 YDDARTMYQVFRRGLSISGNGPCLGfRKPEQPYQWLSYQEVAKRAEFLGSGLLQHDCKVGteQFVGVFAQNRPEWIIAEL 165
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVALR-EKEDGIWQSLTWAEFAERVRALAAGLLALGVKPG--DRVAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 166 ACYTYSMVVVPLYDTLGPGSISYIINTADICTVIVDKPHKATLLLEHveRKETPGLKLVILMEPfedalreRGKKCGVDI 245
Cdd:COG1022 84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEV--RDELPSLRHIVVLDP-------RGLRDDPRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 246 KSMQAIEDCGRENHH------APVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWAPTCADVHFSY 319
Cdd:COG1022 155 LSLDELLALGREVADpaeleaRRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLER----LPLGPGDRTLSF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 320 LPLAHMFERMVQSVVYCHGGRVGFfQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTS--LKRWLLEFA---A 394
Cdd:COG1022 231 LPLAHVFERTVSYYALAAGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAggLKRKLFRWAlavG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 395 KRKQAEVRSGiiRNNSIW--------DELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAG 466
Cdd:COG1022 310 RRYARARLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 467 CTFTTPGDWTSGHVGAPLPCNHIKLvdAEElnywtckgeGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLP 546
Cdd:COG1022 387 ITVNRPGDNRIGTVGPPLPGVEVKI--AED---------GEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 547 EGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKaFLVGIVVPDPEVMPSWAQKKGIE-GTYQELC 625
Cdd:COG1022 456 DGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDGRP-FLAALIVPDFEALGEWAEENGLPyTSYAELA 534
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081036 626 MKKELKKAILDDMVMLGKesGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 693
Cdd:COG1022 535 QDPEVRALIQEEVDRANA--GLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALY 600
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
116-681 |
1.66e-159 |
|
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: 467.46 E-value: 1.66e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 116 QPYQWLSYQEVAKRAEFLGSGLLQHDCKVGteQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADI 195
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPG--DRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 196 CTVIVDKPhkatlllehverketpglklvilmepfedalrergkkcgvdiksmqaiedcgrenhhapvpprpDDLSIVCF 275
Cdd:cd05907 79 KALFVEDP----------------------------------------------------------------DDLATIIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 276 TSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWAPTCADVHFSYLPLAHMFE-RMVQSVVYCHGGRVGFFQgDIRLLSDD 354
Cdd:cd05907 95 TSGTTGRPKGVMLSHRNILSNALALAER----LPATEGDRHLSFLPLAHVFErRAGLYVPLLAGARIYFAS-SAETLLDD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 355 MKALRPTIFPVVPRLLNRMYDKIFHQADTSLKRWLLEFAAkrkqaevrsgiirnnsiwdelffnkiqaslGGHVRMIVTG 434
Cdd:cd05907 170 LSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV------------------------------GGRLRFAASG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 435 AAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDaeelnywtckgEGEICVKGPN 514
Cdd:cd05907 220 GAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPN 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 515 VFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLK 594
Cdd:cd05907 288 VMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDGRP 367
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 595 aFLVGIVVPDPEVMPSWAQKKGIEG-TYQELCMKKELKKAILDDMVMLGKEsgLHSFEQVKAIYIHCDMFSVQNGLLTPT 673
Cdd:cd05907 368 -FLVALIVPDPEALEAWAEEHGIAYtDVAELAANPAVRAEIEAAVEAANAR--LSRYEQIKKFLLLPEPFTIENGELTPT 444
|
....*...
gi 1907081036 674 LKAKRPEL 681
Cdd:cd05907 445 LKLKRPVI 452
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
117-678 |
1.34e-150 |
|
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: 447.05 E-value: 1.34e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 117 PYQWLSYQEVAKRAEFLGSGLlqhdCKVG--TEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTAD 194
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGL----VELGlkPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 195 ICTVIVDkphkatlllehverketpglklvilmepfedalrergkkcgvdiksmqaiedcgrenhhapvpPRPDDLSIVC 274
Cdd:cd17639 78 CSAIFTD---------------------------------------------------------------GKPDDLACIM 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 275 FTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTcaDVHFSYLPLAHMFERMVQSVVYCHGGRVGFfqGDIRLLSD- 353
Cdd:cd17639 95 YTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGPD--DRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDk 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 354 -------DMKALRPTIFPVVPRLLNRMYDKIFHQADTS--LKRWLLEFAAKRKQAEVRSGIirNNSIWDELFFNKIQASL 424
Cdd:cd17639 171 skrgckgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMggLKRTLFWTAYQSKLKALKEGP--GTPLLDELVFKKVRAAL 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 425 GGHVRMIVTGAAPASPTVLGFLrAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYWTCKG 504
Cdd:cd17639 249 GGRLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDKP 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 505 E--GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEP 582
Cdd:cd17639 328 PprGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPL 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 583 VAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKKG-IEGTYQELCMKKELKKAILDDMVMLGKESGLHSFEQVKAIYIHCD 661
Cdd:cd17639 408 VNNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGvINSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDE 487
|
570
....*....|....*..
gi 1907081036 662 MFSVQNGLLTPTLKAKR 678
Cdd:cd17639 488 EWTPENGLVTAAQKLKR 504
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
87-693 |
1.63e-147 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 444.85 E-value: 1.63e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 87 DDARTMYQVFRRGLSISGNGPCLGFR-----KPEQpYQWLSYQEVAKRAEFLGSGLlqHDCKVGTEQFVGVFAQNRPEWI 161
Cdd:PLN02614 42 EGMDSCWDVFRMSVEKYPNNPMLGRReivdgKPGK-YVWQTYQEVYDIVIKLGNSL--RSVGVKDEAKCGIYGANSPEWI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 162 IAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIVDKPHKATLLleHVERKETPGLKLVILMEPFEDALRERGKKC 241
Cdd:PLN02614 119 ISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKISELF--KTCPNSTEYMKTVVSFGGVSREQKEEAETF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 242 GVDIKSMQAIEDCGRENHHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTES-QWAPTCADVHFSYL 320
Cdd:PLN02614 197 GLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSaNAALTVKDVYLSYL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 321 PLAHMFERMVQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTS--LKRWLLEFAAKRKQ 398
Cdd:PLN02614 277 PLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGgfLKKFVFDSAFSYKF 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 399 AEVRSGI--IRNNSIWDELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT 476
Cdd:PLN02614 357 GNMKKGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELD 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 477 S-GHVGAPLPCNHIKLVDAEELNY--WTCKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKII 553
Cdd:PLN02614 437 MlGTVGPPVPNVDIRLESVPEMEYdaLASTPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKII 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 554 DRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKKGIEGTYQELCMKKELKKA 633
Cdd:PLN02614 516 DRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEF 595
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 634 ILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 693
Cdd:PLN02614 596 ILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMY 655
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
117-693 |
2.58e-146 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 441.20 E-value: 2.58e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 117 PYQWLSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADIC 196
Cdd:PLN02861 74 PYVWLTYKEVYDAAIRIGSAIRSRGVNPGDR--CGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 197 TVIVDKPHKATLLleHVERKETPGLKLVILMEPFEDALRERGKKCGVDIKSMQAIEDCGRENHHAPvPPRPDDLSIVCFT 276
Cdd:PLN02861 152 IAFVQESKISSIL--SCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLDCELP-PKQKTDICTIMYT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 277 SGTTGNPKGAMLTHGNVVADF---SGFLKVTESqwAPTCADVHFSYLPLAHMFERMVQSVVYCHGGRVGFFQGDIRLLSD 353
Cdd:PLN02861 229 SGTTGEPKGVILTNRAIIAEVlstDHLLKVTDR--VATEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQGDIRYLME 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 354 DMKALRPTIFPVVPRLLNRMYDKIFH--QADTSLKRWLLEFAAKRKQAEVRSGIIRNNS--IWDELFFNKIQASLGGHVR 429
Cdd:PLN02861 307 DVQALKPTIFCGVPRVYDRIYTGIMQkiSSGGMLRKKLFDFAYNYKLGNLRKGLKQEEAspRLDRLVFDKIKEGLGGRVR 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 430 MIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCtFTTPGDWTS--GHVGAPLPCNHIKLVDAEELNY--WTCKGE 505
Cdd:PLN02861 387 LLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGC-FTSIANVFSmvGTVGVPMTTIEARLESVPEMGYdaLSDVPR 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 506 GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQ 585
Cdd:PLN02861 466 GEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIAS 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 586 IYVHGDSLKAFLVGIVVPDPEVMPSWAQKKGIEGTYQELCMKKELKKAILDDMVMLGKESGLHSFEQVKAIYIHCDMFSV 665
Cdd:PLN02861 545 IWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDI 624
|
570 580
....*....|....*....|....*...
gi 1907081036 666 QNGLLTPTLKAKRPELREYFKKQIEELY 693
Cdd:PLN02861 625 ERDLITPTFKLKRPQLLKYYKDCIDQLY 652
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
88-693 |
4.08e-146 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 440.79 E-value: 4.08e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 88 DARTMYQVFRRGLSISGNGPCLGFRKPEQ----PYQWLSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIA 163
Cdd:PLN02430 40 DITTAWDIFSKSVEKYPDNKMLGWRRIVDgkvgPYMWKTYKEVYEEVLQIGSALRASGAEPGSR--VGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 164 ELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV-DKphKATLLLEhVERKETPGLKLVILMEPFEDALRERGKKCG 242
Cdd:PLN02430 118 MEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVqDK--KIKELLE-PDCKSAKRLKAIVSFTSVTEEESDKASQIG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 243 VDIKSMQAIEDCGRENHHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTESQWapTCADVHFSY 319
Cdd:PLN02430 195 VKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGvdlFMEQFEDKM--THDDVYLSF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 320 LPLAHMFERMVQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFH--QADTSLKRWLLEFAAKRK 397
Cdd:PLN02430 273 LPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYKYK 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 398 QAEVRSGIIRNNS--IWDELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDW 475
Cdd:PLN02430 353 LAWMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEM 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 476 TS-GHVGAPLPCNHIKLVDAEELNYwTCKGE---GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLK 551
Cdd:PLN02430 433 CMlGTVGAPAVYNELRLEEVPEMGY-DPLGEpprGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLK 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 552 IIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKKGIEGTYQELCMKKELK 631
Cdd:PLN02430 511 IIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELK 590
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081036 632 KAILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 693
Cdd:PLN02430 591 EHILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMY 652
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
59-693 |
9.55e-134 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 409.89 E-value: 9.55e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 59 KQSEEVEDGGG---ARRSviGGCTQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRK---PEQ---------------P 117
Cdd:PLN02387 26 KRGVPVDVGGEpgyAIRN--ARFPELVETPWEGATTLAALFEQSCKKYSDKRLLGTRKlisREFetssdgrkfeklhlgE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 118 YQWLSYQEVAKRAEFLGSGLLQ--HDckvgTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADI 195
Cdd:PLN02387 104 YEWITYGQVFERVCNFASGLVAlgHN----KEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 196 CTVIVDKPHKATLLlEHVERKETpgLKLVILMEPFEDALRERGKK-CGVDIKSMQAIEDCGRENHHAPVPPRPDDLSIVC 274
Cdd:PLN02387 180 TTVICDSKQLKKLI-DISSQLET--VKRVIYMDDEGVDSDSSLSGsSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIM 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 275 FTSGTTGNPKGAMLTHGNVVADFSGFLKVTesqwaPTCA--DVHFSYLPLAHMFERMVQSVVYCHGGRVGFfqGDIRLLS 352
Cdd:PLN02387 257 YTSGSTGLPKGVMMTHGNIVATVAGVMTVV-----PKLGknDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 353 D-----------DMKALRPTIFPVVPRLLNRMYDKIFHQADTS--LKRWLLEFAAKRKQAEVR------SGIIRnnSIWD 413
Cdd:PLN02387 330 DtsnkikkgtkgDASALKPTLMTAVPAILDRVRDGVRKKVDAKggLAKKLFDIAYKRRLAAIEgswfgaWGLEK--LLWD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 414 ELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVD 493
Cdd:PLN02387 408 ALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVS 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 494 AEELNYWTCKG---EGEICVKGPNVFKGYLKDEDRTKEA--LDSDG--WLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGE 566
Cdd:PLN02387 488 WEEGGYLISDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGE 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 567 YVAPEKIENIYIRSEPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKKGIE-GTYQELCMKKELKKAILDDMVMLGKES 645
Cdd:PLN02387 568 YVSLGKVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAA 647
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1907081036 646 GLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 693
Cdd:PLN02387 648 RLEKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLY 695
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
117-563 |
8.82e-126 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 379.73 E-value: 8.82e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 117 PYQWLSYQEVAKRAEFLGSGLLQHDCKVGteQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADIC 196
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRALGVGKG--DRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 197 TVIVDKPHKATLLLEHVERKETPGLKLVILMEPFEDALRergkkcgvdiksMQAIEDCGRENHHAPVPPRPDDLSIVCFT 276
Cdd:pfam00501 96 VLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEP------------LPEEAKPADVPPPPPPPPDPDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 277 SGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTCADVHFSYLPLAHMFER-MVQSVVYCHGGRVGFFQGDIRL----L 351
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALdpaaL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 352 SDDMKALRPTIFPVVPRLLNRmydkifhqadtslkrwllefaakrkqaevrsgIIRNNSIWDELFfnkiqaslgGHVRMI 431
Cdd:pfam00501 244 LELIERYKVTVLYGVPTLLNM--------------------------------LLEAGAPKRALL---------SSLRLV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 432 VTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDW---TSGHVGAPLPCNHIKLVDAEELNYWTCKGEGEI 508
Cdd:pfam00501 283 LSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGEL 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1907081036 509 CVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLA 563
Cdd:pfam00501 363 CVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
59-693 |
8.07e-100 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 321.54 E-value: 8.07e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 59 KQSEEVEDGGGARRSVI---GGCT----QLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRK--------------PEQP 117
Cdd:PTZ00216 31 PQNVPVPGTETENASAIyriAGVTdeehERLRNEWYYGPNFLQRLERICKERGDRRALAYRPvervekevvkdadgKERT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 118 Y--------QWLSYQEVAKRAEFLGSGL----LQHDCKVGteqfvgVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGS 185
Cdd:PTZ00216 111 MevthfnetRYITYAELWERIVNFGRGLaelgLTKGSNVA------IYEETRWEWLASIYGIWSQSMVAATVYANLGEDA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 186 ISYIINTADiCTVIVDKPHKATLLLEHVERKETPGLKLVILmepfeDALRERGKKCGVDIKSMQAIEDCGRE---NHHAP 262
Cdd:PTZ00216 185 LAYALRETE-CKAIVCNGKNVPNLLRLMKSGGMPNTTIIYL-----DSLPASVDTEGCRLVAWTDVVAKGHSagsHHPLN 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 263 VPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF-LKVTESQWAPTCADVHFSYLPLAHMFERMVQSVVYCHGGRV 341
Cdd:PTZ00216 259 IPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALeDRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLARGALI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 342 GFfqGDIRLLSD-------DMKALRPTIFPVVPRllnrmydkIFhqaDT-------------SLKRWLLEFAAKRKQAEV 401
Cdd:PTZ00216 339 GF--GSPRTLTDtfarphgDLTEFRPVFLIGVPR--------IF---DTikkaveaklppvgSLKRRVFDHAYQSRLRAL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 402 RSGiiRNNSIWDELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCqVYEGYGQTE--CTAGCTFTtpGDWTSGH 479
Cdd:PTZ00216 406 KEG--KDTPYWNEKVFSAPRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTEtvCCGGIQRT--GDLEPNA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 480 VGAPLPCNHIKLVDAEELNYwTCKGE--GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKK 557
Cdd:PTZ00216 481 VGQLLKGVEMKLLDTEEYKH-TDTPEprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVK 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 558 HIFKLAQGEYVAPEKIENIYIRSEPVAQ----IYVHGDslKAFLVGIVVPDPEVMPSWAQKKGIEGTYQELCMKKELKKA 633
Cdd:PTZ00216 560 ALAKNCLGEYIALEALEALYGQNELVVPngvcVLVHPA--RSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKK 637
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 634 ILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 693
Cdd:PTZ00216 638 ATESLQETARAAGRKSFEIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
118-678 |
1.08e-79 |
|
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: 262.79 E-value: 1.08e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 118 YQWLSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICT 197
Cdd:cd05932 4 VVEFTWGEVADKARRLAAALRALGLEPGSK--IALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 198 VIVDKphkatllLEHVERKET---PGLKLVILMEPfeDALRergkkcgvDIKSMQAIEDCGRENHHAPvPPRPDDLSIVC 274
Cdd:cd05932 82 LFVGK-------LDDWKAMAPgvpEGLISISLPPP--SAAN--------CQYQWDDLIAQHPPLEERP-TRFPEQLATLI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 275 FTSGTTGNPKGAMLTHGNVVADFSGF---LKVTESqwaptcaDVHFSYLPLAHMFERMVQSVVYCHGGRVGFFQGDIRLL 351
Cdd:cd05932 144 YTSGTTGQPKGVMLTFGSFAWAAQAGiehIGTEEN-------DRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 352 SDDMKALRPTIFPVVPRLL----NRMYDKIFHQadtSLKRWLlefaakrkQAEVRSGIIRNnsiwdelffnKIQASLG-G 426
Cdd:cd05932 217 VEDVQRARPTLFFSVPRLWtkfqQGVQDKIPQQ---KLNLLL--------KIPVVNSLVKR----------KVLKGLGlD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 427 HVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDaeelnywtckgEG 506
Cdd:cd05932 276 QCRLAGCGSAPVPPALLEWYRS-LGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 507 EICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQI 586
Cdd:cd05932 344 EILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMV 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 587 YVHGDSLKAfLVGIVVPDPEvmpswAQKKGIEGTYQELcmkKELKKAILDDMvmlgkESGLHSFEQVKAIYIHCDMFSVQ 666
Cdd:cd05932 424 CVIGSGLPA-PLALVVLSEE-----ARLRADAFARAEL---EASLRAHLARV-----NSTLDSHEQLAGIVVVKDPWSID 489
|
570
....*....|..
gi 1907081036 667 NGLLTPTLKAKR 678
Cdd:cd05932 490 NGILTPTLKIKR 501
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
116-679 |
5.07e-74 |
|
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: 246.50 E-value: 5.07e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 116 QPYQWLSYQEVAKRAEFLGSGLLqhDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADI 195
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLR--SLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 196 CTVIVdkphkatlllehverketpglklvilmepfedalrergkkcgvdiksmqaiedcgrENHhapvpprPDDLSIVCF 275
Cdd:cd17640 79 VALVV--------------------------------------------------------END-------SDDLATIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 276 TSGTTGNPKGAMLTHGNVVADFSGFLKVTEsqwaPTCADVHFSYLPLAHMFERMVQSVVYCHGGRVGFfqGDIRLLSDDM 355
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLLHQIRSLSDIVP----PQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDDL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 356 KALRPTIFPVVPRLLNRMYDKIFHQadtslkrwllefaaKRKQAEVRSGIIrnnsiwdeLFFnkiqaSLGGHVRMIVTGA 435
Cdd:cd17640 170 KRVKPHYIVSVPRLWESLYSGIQKQ--------------VSKSSPIKQFLF--------LFF-----LSGGIFKFGISGG 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 436 APASPTVLGFLRaALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYWTCKGEGEICVKGPNV 515
Cdd:cd17640 223 GALPPHVDTFFE-AIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQV 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 516 FKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKa 595
Cdd:cd17640 302 MKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQK- 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 596 FLVGIVVPDPEVMPSWAQKKGI---EGTYQELCMKKELKKAILDDMVMLGKESGLHSFEQVKAIYIHCDMFsVQNGLLTP 672
Cdd:cd17640 381 RLGALIVPNFEELEKWAKESGVklaNDRSQLLASKKVLKLYKNEIKDEISNRPGFKSFEQIAPFALLEEPF-IENGEMTQ 459
|
....*..
gi 1907081036 673 TLKAKRP 679
Cdd:cd17640 460 TMKIKRN 466
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
119-693 |
7.20e-71 |
|
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: 241.88 E-value: 7.20e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 119 QW--LSYQEVAKRAEFLGSGLLqhdcKVGTEQF--VGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTAD 194
Cdd:cd05933 5 KWhtLTYKEYYEACRQAAKAFL----KLGLERFhgVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 195 ICTVIVDKPHKATLLLEhvERKETPGLKLVI-LMEPFEDalrergKKCGVdiKSMQAIEDCGREnhhapVPP-------- 265
Cdd:cd05933 81 ANILVVENQKQLQKILQ--IQDKLPHLKAIIqYKEPLKE------KEPNL--YSWDEFMELGRS-----IPDeqldaiis 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 266 --RPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTCADVHFSYLPLAHMFERMVQS-VVYCHGGRVG 342
Cdd:cd05933 146 sqKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIwLPIKVGGQVY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 343 FFQGDIR--LLSDDMKALRPTIFPVVPRLLNRMYDKI---FHQAdTSLKRWLLEFAaKRKQAEV-------RSGIIRNNS 410
Cdd:cd05933 226 FAQPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkavGAKS-GTLKRKIASWA-KGVGLETnlklmggESPSPLFYR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 411 IWDELFFNKIQASLG-GHVRMIVTGAAPASPTVLGFLrAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHI 489
Cdd:cd05933 304 LAKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 490 KLVDAEelnywtCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVA 569
Cdd:cd05933 383 KIHNPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 570 PEKIENIYIRSEP-VAQIYVHGDSLKaFLVGIVV------PD---------PEVMpSWAQKKGIEGTY-QELCMKKELK- 631
Cdd:cd05933 457 PVPIEDAVKKELPiISNAMLIGDKRK-FLSMLLTlkcevnPEtgepldeltEEAI-EFCRKLGSQATRvSEIAGGKDPKv 534
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081036 632 -KAILDDMVMLGKESGLHSFEQVKAIYIHCDmFSVQNGLLTPTLKAKRPELREYFKKQIEELY 693
Cdd:cd05933 535 yEAIEEGIKRVNKKAISNAQKIQKWVILEKD-FSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
92-605 |
5.28e-68 |
|
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: 230.08 E-value: 5.28e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 92 MYQVFRRGLSISGNGPCLGFRkpeqpYQWLSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELACYTYS 171
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG-----GRRLTYAELDARARRLAAALRALG--VGPGDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 172 MVVVPLYDTLGPGSISYIINTADICTVIVdkphkatlllehverketpglklvilmepfedalrergkkcgvdiksmqai 251
Cdd:COG0318 74 AVVVPLNPRLTAEELAYILEDSGARALVT--------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 252 edcgrenhhapvpprpddlSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWAPTCADVHFSYLPLAHMFErMVQ 331
Cdd:COG0318 103 -------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAA----LGLTPGDVVLVALPLFHVFG-LTV 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 332 SVVYC--HGGRV----GFfqgDIRLLSDDMKALRPTIFPVVPRLLNRMYDKI-FHQADTSlkrwllefaakrkqaevrsg 404
Cdd:COG0318 159 GLLAPllAGATLvllpRF---DPERVLELIERERVTVLFGVPTMLARLLRHPeFARYDLS-------------------- 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 405 iirnnsiwdelffnkiqaslggHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGA 482
Cdd:COG0318 216 ----------------------SLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGR 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 483 PLPCNHIKLVDAE--ELNywtcKGE-GEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHI 559
Cdd:COG0318 274 PLPGVEVRIVDEDgrELP----PGEvGEIVVRGPNVMKGYWNDPEATAEAFR-DGWLRTGDLGRLDEDGYLYIVGRKKDM 348
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1907081036 560 FKLAqGEYVAPEKIENIYIRSEPVAQIYV-------HGDSLKAFlvgiVVPDP 605
Cdd:COG0318 349 IISG-GENVYPAEVEEVLAAHPGVAEAAVvgvpdekWGERVVAF----VVLRP 396
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
121-671 |
1.91e-67 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 232.35 E-value: 1.91e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLlQHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 200
Cdd:cd17632 68 ITYAELWERVGAVAAAH-DPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 DKPHKAtLLLEHVERKETPGLKLVILMEPFEDA-------LRERGKKCGVDIKSMQAIEDCGRENHHAPVP---PRPDDL 270
Cdd:cd17632 147 SAEHLD-LAVEAVLEGGTPPRLVVFDHRPEVDAhraalesARERLAAVGIPVTTLTLIAVRGRDLPPAPLFrpePDDDPL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 271 SIVCFTSGTTGNPKGAMLTHgNVVADFsgFLKVTESQWAPTCADVHFSYLPLAHMFERMVQSVVYCHGGrVGFFQG--DI 348
Cdd:cd17632 226 ALLIYTSGSTGTPKGAMYTE-RLVATF--WLKVSSIQDIRPPASITLNFMPMSHIAGRISLYGTLARGG-TAYFAAasDM 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 349 RLLSDDMKALRPTIFPVVPRLLNRMYDKifHQADtsLKRWL-----LEFAAKRKQAEVRsgiirnnsiwdelffnkiQAS 423
Cdd:cd17632 302 STLFDDLALVRPTELFLVPRVCDMLFQR--YQAE--LDRRSvagadAETLAERVKAELR------------------ERV 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 424 LGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTtpgdwtSGHVGAPlPCNHIKLVDAEELNYWTCK 503
Cdd:cd17632 360 LGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE--AGAVIL------DGVIVRP-PVLDYKLVDVPELGYFRTD 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 504 G---EGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRS 580
Cdd:cd17632 431 RphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFAAS 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 581 EPVAQIYVHGDSLKAFLVGIVVPDPEVMPSwaqkkgiEGTyqelcmkKELKKAILDDMVMLGKESGLHSFEQVKAIYIHC 660
Cdd:cd17632 511 PLVRQIFVYGNSERAYLLAVVVPTQDALAG-------EDT-------ARLRAALAESLQRIAREAGLQSYEIPRDFLIET 576
|
570
....*....|.
gi 1907081036 661 DMFSVQNGLLT 671
Cdd:cd17632 577 EPFTIANGLLS 587
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
118-644 |
7.47e-66 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 227.69 E-value: 7.47e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 118 YQWLSYQEVAKRAEFLGSGLlqHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICT 197
Cdd:cd17641 9 WQEFTWADYADRVRAFALGL--LALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 198 VIVDKPHKATLLLEHveRKETPGLKLVILMEPfedalreRGKKCGVDIK--SMQAIEDCGREnHHAPVPP---------R 266
Cdd:cd17641 87 VIAEDEEQVDKLLEI--ADRIPSVRYVIYCDP-------RGMRKYDDPRliSFEDVVALGRA-LDRRDPGlyerevaagK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESqwAPTcaDVHFSYLPLAHMFERM---VQSVVycHGGRVGF 343
Cdd:cd17641 157 GEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPL--GPG--DEYVSVLPLPWIGEQMysvGQALV--CGFIVNF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 344 FQgDIRLLSDDMKALRPTIFPVVPRLLN--------RMYDKifhqadTSLKRWL--------LEFAAKRKQAEVRSGIIR 407
Cdd:cd17641 231 PE-EPETMMEDLREIGPTFVLLPPRVWEgiaadvraRMMDA------TPFKRFMfelgmklgLRALDRGKRGRPVSLWLR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 408 NNS-IWDELFFNKIQASLG-GHVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTEcTAGCTFTTP-GDWTSGHVGAPL 484
Cdd:cd17641 304 LASwLADALLFRPLRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTE-LAGAYTVHRdGDVDPDTVGVPF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 485 PCNHIKLVDaeelnywtckgEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQ 564
Cdd:cd17641 382 PGTEVRIDE-----------VGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSD 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 565 GEYVAPEKIENIYIRSEPVAQIYVHGDSlKAFLVGIVVPDPEVMPSWAQKKGIE-GTYQELCMKKELKKAILDDMVMLGK 643
Cdd:cd17641 451 GTRFSPQFIENKLKFSPYIAEAVVLGAG-RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKVNA 529
|
.
gi 1907081036 644 E 644
Cdd:cd17641 530 S 530
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
121-606 |
3.64e-59 |
|
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: 206.52 E-value: 3.64e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGsgLLQHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 200
Cdd:cd05914 8 LTYKDLADNIAKFA--LLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 DKPhkatlllehverketpglklvilmepfedalrergkkcgvdiksmqaiedcgrenhhapvpprpDDLSIVCFTSGTT 280
Cdd:cd05914 86 SDE----------------------------------------------------------------DDVALINYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 281 GNPKGAMLTHGNVVADFSG---FLKVTESqwaptcaDVHFSYLPLAHMFERMVQSVVYCHGGRVGFFQGDI---RLLSDD 354
Cdd:cd05914 102 GNSKGVMLTYRNIVSNVDGvkeVVLLGKG-------DKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIpsaKIIALA 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 355 MKALRPTIfpVVPRLLNRMYDKIFHQADTSLKRWLLEFAAKrkqaevrsgIIRNNSIWdELFFNKIQASLGGHVRMIVTG 434
Cdd:cd05914 175 FAQVTPTL--GVPVPLVIEKIFKMDIIPKLTLKKFKFKLAK---------KINNRKIR-KLAFKKVHEAFGGNIKEFVIG 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 435 AAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNywtckGEGEICVKGPN 514
Cdd:cd05914 243 GAKINPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDPAT-----GEGEIIVRGPN 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 515 VFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVA--QIYVHGDS 592
Cdd:cd05914 317 VMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLesLVVVQEKK 396
|
490
....*....|....
gi 1907081036 593 LKAflvgIVVPDPE 606
Cdd:cd05914 397 LVA----LAYIDPD 406
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
121-598 |
5.42e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 207.45 E-value: 5.42e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 200
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGKGDR--VAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 -------DKP-HKATLLLEHVERKETP-GLKLVILMEPFEDALrERGKKcgvdiksmqaiedcgrENHHAPVppRPDDLS 271
Cdd:PRK07656 109 lglflgvDYSaTTRLPALEHVVICETEeDDPHTEKMKTFTDFL-AAGDP----------------AERAPEV--DPDDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 272 IVCFTSGTTGNPKGAMLTHGNV---VADFSGFLKVTESqwaptcaDVHFSYLPLAHMFERMVqSVVYC--HGGRV---GF 343
Cdd:PRK07656 170 DILFTSGTTGRPKGAMLTHRQLlsnAADWAEYLGLTEG-------DRYLAANPFFHVFGYKA-GVNAPlmRGATIlplPV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 344 FQGD--IRLLSDDmkalRPTIFPVVPRLLNRMYDkifhqadtslkrwllefAAKRKQAEVRSgiirnnsiwdelffnkiq 421
Cdd:PRK07656 242 FDPDevFRLIETE----RITVLPGPPTMYNSLLQ-----------------HPDRSAEDLSS------------------ 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 422 aslgghVRMIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGCTFTTPGD---WTSGHVGAPLPCNHIKLVDaeEL 497
Cdd:PRK07656 283 ------LRLAVTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIAGVENKIVN--EL 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 498 NYWTCKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENI 576
Cdd:PRK07656 355 GEEVPVGEvGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IVGGFNVYPAEVEEV 433
|
490 500
....*....|....*....|....*....
gi 1907081036 577 YIRSEPVAQIYV-------HGDSLKAFLV 598
Cdd:PRK07656 434 LYEHPAVAEAAVigvpderLGEVGKAYVV 462
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
93-598 |
1.68e-58 |
|
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: 204.72 E-value: 1.68e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 93 YQVFRRGLSISGNGPCLGFRKpeqpyQWLSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSM 172
Cdd:cd05936 2 ADLLEEAARRFPDKTALIFMG-----RKLTYRELDALAEAFAAGLQNLGVQPGDR--VALMLPNCPQFPIAYFGALKAGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 173 VVVPLYDTLGPGSISYIINTAdictvivdkphkatlllehverketpGLKLVILMEPFEDALRergkkcgvdiksmqaie 252
Cdd:cd05936 75 VVVPLNPLYTPRELEHILNDS--------------------------GAKALIVAVSFTDLLA----------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 253 dcGRENHHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTcaDVHFSYLPLAHMFErmvQS 332
Cdd:cd05936 112 --AGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEGD--DVVLAALPLFHVFG---LT 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 333 VVYCHGGRVGFFQ------GDIRLLsDDMKALRPTIFPVVPRllnrMYDKIFHQADtslkrwllefaakrkqaevrsgii 406
Cdd:cd05936 185 VALLLPLALGATIvliprfRPIGVL-KEIRKHRVTIFPGVPT----MYIALLNAPE------------------------ 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 407 rnnsiwdelfFNKIQASlggHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT-SGHVGAPLP 485
Cdd:cd05936 236 ----------FKKRDFS---SLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRkPGSIGIPLP 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 486 CNHIKLVDaEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQG 565
Cdd:cd05936 303 GTEVKIVD-DDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGG 379
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1907081036 566 EYVAPEKIENIYIRSEPVAQIYV-------HGDSLKAFLV 598
Cdd:cd05936 380 FNVYPREVEEVLYEHPAVAEAAVvgvpdpySGEAVKAFVV 419
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
269-606 |
8.03e-58 |
|
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: 199.05 E-value: 8.03e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 269 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWAPTCADVHFSYLPLAHMFerMVQSVVYC--HGGRVGFFQG 346
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS----GGLTEGDVFLSTLPLFHIG--GLFGLLGAllAGGTVVLLPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 347 -DIRLLSDDMKALRPTIFPVVPRLLNRmydkifhqadtslkrwLLEFAAKRKQAevrsgiirnnsiwdelffnkiQASLg 425
Cdd:cd04433 75 fDPEAALELIEREKVTILLGVPTLLAR----------------LLKAPESAGYD---------------------LSSL- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 426 ghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT--SGHVGAPLPCNHIKLVDAE--ELNYWt 501
Cdd:cd04433 117 ---RALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDPDggELPPG- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 502 ckGEGEICVKGPNVFKGYLKDEDRTkEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSE 581
Cdd:cd04433 193 --EIGELVVRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHP 268
|
330 340
....*....|....*....|....*
gi 1907081036 582 PVAQIYVHGdslkaflvgivVPDPE 606
Cdd:cd04433 269 GVAEAAVVG-----------VPDPE 282
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
121-598 |
3.29e-50 |
|
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: 182.41 E-value: 3.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLLQHDCKVGteQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 200
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKG--DVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 DKPHKATLLLehVERKETPGLKlVILMEPFEDALRergkkcgvDIKSMQAIEDCGRENHHAPVPPR-PDDLSIVCFTSGT 279
Cdd:cd05911 89 DPDGLEKVKE--AAKELGPKDK-IIVLDDKPDGVL--------SIEDLLSPTLGEEDEDLPPPLKDgKDDTAAILYSSGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 280 TGNPKGAMLTHGNVVADFS---GFLKVTESQwaptcADVHFSYLPLAHMF--ERMVQSVVYchGGRV----GFFqgdirl 350
Cdd:cd05911 158 TGLPKGVCLSHRNLIANLSqvqTFLYGNDGS-----NDVILGFLPLYHIYglFTTLASLLN--GATViimpKFD------ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 351 lSDDMKAL----RPTIFPVVPRLLNRMydkifhqadtslkrwllefaakrkqaeVRSGIirnnsiwdelfFNKIQASlgg 426
Cdd:cd05911 225 -SELFLDLiekyKITFLYLVPPIAAAL---------------------------AKSPL-----------LDKYDLS--- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 427 HVRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYWTCKGE 505
Cdd:cd05911 263 SLRVILSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEP 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 506 GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIyIRSEP--- 582
Cdd:cd05911 343 GEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAV-LLEHPgva 420
|
490 500
....*....|....*....|.
gi 1907081036 583 ---VAQIY--VHGDSLKAFLV 598
Cdd:cd05911 421 daaVIGIPdeVSGELPRAYVV 441
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
86-605 |
7.27e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 176.92 E-value: 7.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 86 YDDARTMYQVFRRGLSISGNGPCLGFRKPEqpyqwLSYQEVAKRAEFLGSGLLqhDCKVGTEQFVGVFAQNRPEWIIAEL 165
Cdd:PRK06187 2 QDYPLTIGRILRHGARKHPDKEAVYFDGRR-----TTYAELDERVNRLANALR--ALGVKKGDRVAVFDWNSHEYLEAYF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 166 ACytySM---VVVPLYDTLGPGSISYIINTADICTVIVDKPhkatlLLEHVE--RKETPGLKLVILMEPFEDALrergkk 240
Cdd:PRK06187 75 AV---PKigaVLHPINIRLKPEEIAYILNDAEDRVVLVDSE-----FVPLLAaiLPQLPTVRTVIVEGDGPAAP------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 241 CGVDIKSMQAIEDCGRENHHAPvPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVvadFSGFLKVTES-QWapTCADVHFSY 319
Cdd:PRK06187 141 LAPEVGEYEELLAAASDTFDFP-DIDENDAAAMLYTSGTTGHPKGVVLSHRNL---FLHSLAVCAWlKL--SRDDVYLVI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 320 LPLAHMFERMVqsvvychgGRVGFFQG---------DIRLLSDDMKALRPTIFPVVPRLLNRMydkifHQADTSLKRWLl 390
Cdd:PRK06187 215 VPMFHVHAWGL--------PYLALMAGakqviprrfDPENLLDLIETERVTFFFAVPTIWQML-----LKAPRAYFVDF- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 391 efaakrkqaevrsgiirnnsiwdelffnkiqaslgGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFT 470
Cdd:PRK06187 281 -----------------------------------SSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVL 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 471 TPGDWTSGH------VGAPLPCNHIKLVDAEELNYWTCKGE-GEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGK 543
Cdd:PRK06187 326 PPEDQLPGQwtkrrsAGRPLPGVEARIVDDDGDELPPDGGEvGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGY 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081036 544 WLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIyirsepvaqIYVHGDSLKAFLVGivVPDP 605
Cdd:PRK06187 405 IDEDGYLYITDRIKDVIISG-GENIYPRELEDA---------LYGHPAVAEVAVIG--VPDE 454
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
233-693 |
3.96e-42 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 163.74 E-value: 3.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 233 ALRERGKKCGVdikSMQAIEDCGREN--HHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNV------VADFSGFLKvt 304
Cdd:PTZ00342 270 DLKEKAKKLGI---SIILFDDMTKNKttNYKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLyntvvpLCKHSIFKK-- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 305 esqWAPtcaDVHFSYLPLAHMFERMVQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQAD-- 382
Cdd:PTZ00342 345 ---YNP---KTHLSYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINnl 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 383 TSLKRWLLE--FAAKRkqaevrsgiiRNNSIWDELFF-------NKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQ 453
Cdd:PTZ00342 419 PPLKRFLVKkiLSLRK----------SNNNGGFSKFLegithisSKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVN 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 454 VYEGYGQTEcTAGCTFTTPG-DWTSGHVGAPL-PCNHIKLVDAEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALD 531
Cdd:PTZ00342 489 YYQGYGLTE-TTGPIFVQHAdDNNTESIGGPIsPNTKYKVRTWETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFT 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 532 SDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHG-DSLKAFLvGIVVPDPEVM-- 608
Cdd:PTZ00342 568 EDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGdDSMDGPL-AIISVDKYLLfk 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 609 ----PSWAQKKGI-EGTYQELCMKKELKKAILDDMV---MLG--KESGLHSFEQVKAIYIHCDMFSVQNgLLTPTLKAKR 678
Cdd:PTZ00342 647 clkdDNMLESTGInEKNYLEKLTDETINNNIYVDYVkgkMLEvyKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKR 725
|
490
....*....|....*...
gi 1907081036 679 PEL-REY--FKKQIEELY 693
Cdd:PTZ00342 726 FYVfKDYafFIDQVKKIY 743
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
96-605 |
9.61e-41 |
|
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: 154.69 E-value: 9.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 96 FRRGLSISGNGPCLGFRKPEqpyqwLSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVV 175
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRS-----LTYAELDERVNRLAHALRALGVAKGDR--VAVLSKNSPEFLELLFAAARLGAVFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 176 PLYDTLGPGSISYIINTADictvivdkphkATLLLehverketpglklvilmepfedalrergkkcgvdiksmqaiedcg 255
Cdd:cd17631 74 PLNFRLTPPEVAYILADSG-----------AKVLF--------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 256 renhhapvpprpDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLkvteSQWAPTCADVHFSYLPLAHMFE-RMVQSVV 334
Cdd:cd17631 98 ------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNAL----AALDLGPDDVLLVVAPLFHIGGlGVFTLPT 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 335 YCHGGRV----GFfqgDIRLLSDDMKALRPTIFPVVPRLLNRMYDK-IFHQADTSlkrwllefaakrkqaevrsgiirnn 409
Cdd:cd17631 162 LLRGGTVvilrKF---DPETVLDLIERHRVTSFFLVPTMIQALLQHpRFATTDLS------------------------- 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 410 siwdelffnkiqaSLgghvRMIVTGAAPASPTVLGFLRAAlGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPCN 487
Cdd:cd17631 214 -------------SL----RAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHRRklGSAGRPVFFV 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 488 HIKLVDAE--ELNywtcKGE-GEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQ 564
Cdd:cd17631 276 EVRIVDPDgrEVP----PGEvGEIVVRGPHVMAGYWNRPEATAAAFR-DGWFHTGDLGRLDEDGYLYIVDRKKDMII-SG 349
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1907081036 565 GEYVAPEKIENIyirsepvaqIYVHGDSLKAFLVGivVPDP 605
Cdd:cd17631 350 GENVYPAEVEDV---------LYEHPAVAEVAVIG--VPDE 379
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
121-576 |
2.74e-40 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 154.70 E-value: 2.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLlqHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 200
Cdd:cd05904 33 LTYAELERRVRRLAAGL--AKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 DkphkatllLEHVERKETPGLKLVILMEPFEDalrergkkcgvdikSMQAIEDCGRENHHAPVPPR--PDDLSIVCFTSG 278
Cdd:cd05904 111 T--------AELAEKLASLALPVVLLDSAEFD--------------SLSFSDLLFEADEAEPPVVVikQDDVAALLYSSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 279 TTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTcaDVHFSYLPLAHMFermvqsvvychgGRVGFFQGDIRL-------- 350
Cdd:cd05904 169 TTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSE--DVFLCVLPMFHIY------------GLSSFALGLLRLgatvvvmp 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 351 ---LSDDMKAL---RPTIFPVVPRLLnrmydkifhqadtslkrwllefAAKRKQAEVRSGIIRnnsiwdelffnkiqaSL 424
Cdd:cd05904 235 rfdLEELLAAIeryKVTHLPVVPPIV----------------------LALVKSPIVDKYDLS---------------SL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 425 gghvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFTTP---GDWTSGHVGAPLPCNHIKLVDAEELNYW 500
Cdd:cd05904 278 ----RQIMSGAAPLGKELIeAFRAKFPNVDLGQGYGMTESTGVVAMCFApekDRAKYGSVGRLVPNVEAKIVDPETGESL 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081036 501 TCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENI 576
Cdd:cd05904 354 PPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEAL 428
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
121-609 |
7.80e-40 |
|
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: 152.06 E-value: 7.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLgSGLLQHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIv 200
Cdd:cd05941 12 ITYADLVARAARL-ANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 dkphkatlllehverketpglklvilmepfedalrergkkcgvdiksmqaiedcgrenhhapvpprpdDLSIVCFTSGTT 280
Cdd:cd05941 90 --------------------------------------------------------------------DPALILYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 281 GNPKGAMLTHGNVVADfsgfLKVTESQWAPTCADVHFSYLPLAHmfermVQSVV-------YChGGRV---GFFQGDIRL 350
Cdd:cd05941 102 GRPKGVVLTHANLAAN----VRALVDAWRWTEDDVLLHVLPLHH-----VHGLVnallcplFA-GASVeflPKFDPKEVA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 351 LSDDMKALrpTIFPVVPRllnrMYDKIFHQADTSLKrwllEFAAKRKQAEvrsgiirnnsiwdelffnkiqaslgGHVRM 430
Cdd:cd05941 172 ISRLMPSI--TVFMGVPT----IYTRLLQYYEAHFT----DPQFARAAAA-------------------------ERLRL 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 431 IVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTTP--GDWTSGHVGAPLPCNHIKLVDAEELNYWTCKGEGEI 508
Cdd:cd05941 217 MVSGSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEI 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 509 CVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKK-HIFKlAQGEYVAPEKIENIYIRSEPVAQIY 587
Cdd:cd05941 295 QVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEIERVLLAHPGVSECA 373
|
490 500
....*....|....*....|....*
gi 1907081036 588 VHGDSLKAF---LVGIVVPDPEVMP 609
Cdd:cd05941 374 VIGVPDPDWgerVVAVVVLRAGAAA 398
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
121-618 |
8.79e-38 |
|
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: 147.48 E-value: 8.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSgLLQHDCKVGteQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 200
Cdd:cd05909 8 LTYRKLLTGAIALAR-KLAKMTKEG--ENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 DKPHKATLLLEHVERKETPgLKLVILmepfEDaLRER---GKKCGVDIKSMQAIEDCGRENHHAPVppRPDDLSIVCFTS 277
Cdd:cd05909 85 SKQFIEKLKLHHLFDVEYD-ARIVYL----ED-LRAKiskADKCKAFLAGKFPPKWLLRIFGVAPV--QPDDPAVILFTS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 278 GTTGNPKGAMLTHGNVVADFSGFLKVTEsqwaPTCADVHFSYLPLAHMFermvqsvvychggrvGFFQGDIRLLSDDMKA 357
Cdd:cd05909 157 GSEGLPKGVVLSHKNLLANVEQITAIFD----PNPEDVVFGALPFFHSF---------------GLTGCLWLPLLSGIKV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 358 L---RPTIFPVVPRLLnrmYDK---IFHQADTSLKRWllefaAKRKQAEVRSGIirnnsiwdelffnkiqaslgghvRMI 431
Cdd:cd05909 218 VfhpNPLDYKKIPELI---YDKkatILLGTPTFLRGY-----ARAAHPEDFSSL-----------------------RLV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 432 VTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPCNHIKLVDAEELNYWTCKGEGEICV 510
Cdd:cd05909 267 VAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLV 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 511 KGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSEP----VAQI 586
Cdd:cd05909 347 RGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDILSEILPedneVAVV 424
|
490 500 510
....*....|....*....|....*....|....*.
gi 1907081036 587 YV----HGDSLKAFLVGIvVPDPEVMPSWAQKKGIE 618
Cdd:cd05909 425 SVpdgrKGEKIVLLTTTT-DTDPSSLNDILKNAGIS 459
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
91-604 |
1.64e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 144.76 E-value: 1.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 91 TMYQVFRRGLSISGNGPCLGFRKPEQPYQWLSYQeVAKRAEFLgsgllqHDCKVGTEQFVGVFAQNRPEWIIAELACYTY 170
Cdd:PRK05605 33 TLVDLYDNAVARFGDRPALDFFGATTTYAELGKQ-VRRAAAGL------RALGVRPGDRVAIVLPNCPQHIVAFYAVLRL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 171 SMVVV---PLYDT---LGP----GSISYII--NTADICTVIVDkphkaTLLLEHVER----KETPGLKLVILMEPFEDAL 234
Cdd:PRK05605 106 GAVVVehnPLYTAhelEHPfedhGARVAIVwdKVAPTVERLRR-----TTPLETIVSvnmiAAMPLLQRLALRLPIPALR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 235 RERGKKCG-----VDIKSMQAIEDcGRENHHAPVP-PRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgflkVTESQ- 307
Cdd:PRK05605 181 KARAALTGpapgtVPWETLVDAAI-GGDGSDVSHPrPTPDDVALILYTSGTTGKPKGAQLTHRNLFAN------AAQGKa 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 308 WAPTCAD---VHFSYLPLAHMFE-RMVQSV-VYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLlnrmYDKIfhqad 382
Cdd:PRK05605 254 WVPGLGDgpeRVLAALPMFHAYGlTLCLTLaVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPL----YEKI----- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 383 tslkrwlLEFAAKRkqaevrsGIirnnsiwdelffnkiqaSLGGhVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTE 462
Cdd:PRK05605 325 -------AEAAEER-------GV-----------------DLSG-VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 463 CT---AGCTFTTpgDWTSGHVGAPLPCNHIKLVDAEELNYWTCKGE-GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHT 538
Cdd:PRK05605 373 TSpiiVGNPMSD--DRRPGYVGVPFPDTEVRIVDPEDPDETMPDGEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRT 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081036 539 GDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIEniyirsEPVAQiyvHGDSLKAFLVGIVVPD 604
Cdd:PRK05605 450 GDVVVMEEDGFIRIVDRIKELI-ITGGFNVYPAEVE------EVLRE---HPGVEDAAVVGLPRED 505
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
120-683 |
1.79e-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: 143.61 E-value: 1.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 120 WLSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVI 199
Cdd:cd05926 14 ALTYADLAELVDDLARQLAALGIKKGDR--VAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 200 VDKPHkatlLLEHVERKETPGLklvilmepfedALRERGKKCGVDIKSMQAIEDCGRENHHAPV----PPRPDDLSIVCF 275
Cdd:cd05926 92 TPKGE----LGPASRAASKLGL-----------AILELALDVGVLIRAPSAESLSNLLADKKNAksegVPLPDDLALILH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 276 TSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWAPTCADVHFSYLPLAHMFERMVQ--SVVYChGGRV----GFfqgDIR 349
Cdd:cd05926 157 TSGTTGRPKGVPLTHRNLAASATNITNT----YKLTPDDRTLVVMPLFHVHGLVASllSTLAA-GGSVvlppRF---SAS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 350 LLSDDMKALRPTIFPVVPRLlnrmydkifHQAdtslkrwLLEFAAKRKQAEVrsgiirnnsiwdelffnkiqaslgGHVR 429
Cdd:cd05926 229 TFWPDVRDYNATWYTAVPTI---------HQI-------LLNRPEPNPESPP------------------------PKLR 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 430 MIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTP---GDWTSGHVGAPLPcNHIKLVDAEELnywTCK--G 504
Cdd:cd05926 269 FIRSCSASLPPAVLEALEATFGAPVLEAYGMTE-AAHQMTSNPlppGPRKPGSVGKPVG-VEVRILDEDGE---ILPpgV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 505 EGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPVA 584
Cdd:cd05926 344 VGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVLLSHPAVL 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 585 QIYVHGdslkaflvgivVPDP----EVMPSWAQKKGIEGTYQELcmKKELKKailddmvmlgkesGLHSFEQVKAIYIhc 660
Cdd:cd05926 423 EAVAFG-----------VPDEkygeEVAAAVVLREGASVTEEEL--RAFCRK-------------HLAAFKVPKKVYF-- 474
|
570 580
....*....|....*....|...
gi 1907081036 661 dmfsVQNGLLTPTLKAKRPELRE 683
Cdd:cd05926 475 ----VDELPKTATGKIQRRKVAE 493
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
123-615 |
7.45e-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: 134.88 E-value: 7.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 123 YQEVAKRAEFLgsgllqHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIVDK 202
Cdd:TIGR01923 6 DCEAAHLAKAL------KAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 203 P-HKATLLLEHVERKETPGLKLVILMEPFEDalrergkkcgvdiksmqaiedcgrenhhapvpprpDDLSIVCFTSGTTG 281
Cdd:TIGR01923 80 LlEEKDFQADSLDRIEAAGRYETSLSASFNM-----------------------------------DQIATLMFTSGTTG 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 282 NPKGAMLTHGNVVADFSGF---LKVTESqwaptcaDVHFSYLPLAHMFErmvQSVVY---CHGGRVGFFQGDIRLLsDDM 355
Cdd:TIGR01923 125 KPKAVPHTFRNHYASAVGSkenLGFTED-------DNWLLSLPLYHISG---LSILFrwlIEGATLRIVDKFNQLL-EMI 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 356 KALRPTIFPVVPRLLNRMYDKIFHqaDTSLKRWLLefaakrkqaevrsgiirnnsiwdelffnkiqaslGGhvrmivtGA 435
Cdd:TIGR01923 194 ANERVTHISLVPTQLNRLLDEGGH--NENLRKILL----------------------------------GG-------SA 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 436 APASptvlgFLRAAL--GCQVYEGYGQTE-CTAGCTFTTPGDWTSGHVGAPLPCNHIKL-VDAEElnywtckGEGEICVK 511
Cdd:TIGR01923 231 IPAP-----LIEEAQqyGLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIkVDNKE-------GHGEIMVK 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 512 GPNVFKGYLKDEDRTkEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYV--H 589
Cdd:TIGR01923 299 GANLMKGYLYQGELT-PAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVVvpK 376
|
490 500 510
....*....|....*....|....*....|.
gi 1907081036 590 GDSL-----KAFLVGIVVPDPEVMPSWAQKK 615
Cdd:TIGR01923 377 PDAEwgqvpVAYIVSESDISQAKLIAYLTEK 407
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
137-606 |
1.61e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 134.93 E-value: 1.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 137 LLQHDCKVGteQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADictvivdkphkATLLLEhverk 216
Cdd:PRK09088 39 LRRRGCVDG--ERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAE-----------PRLLLG----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 217 etpglklvilmepfeDALRERGKKCGVDIKSMQAIEDCGRENHHAPVPPrpDDLSIVCFTSGTTGNPKGAMLTHGN---V 293
Cdd:PRK09088 101 ---------------DDAVAAGRTDVEDLAAFIASADALEPADTPSIPP--ERVSLILFTSGTSGQPKGVMLSERNlqqT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 294 VADFSGFLKVtesqwaptcaDVHFSYLPLAHMFE--RMVQSV--VYCHGGRV----GFFQG-DIRLLSDdmKALRPTIFP 364
Cdd:PRK09088 164 AHNFGVLGRV----------DAHSSFLCDAPMFHiiGLITSVrpVLAVGGSIlvsnGFEPKrTLGRLGD--PALGITHYF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 365 VVPRllnrMYDKIFHQADtslkrwlleFAAkrkqaevrsgiirnnsiwdelffnkiqASLGgHVRMIVTGAAP-ASPTVL 443
Cdd:PRK09088 232 CVPQ----MAQAFRAQPG---------FDA---------------------------AALR-HLTALFTGGAPhAAEDIL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 444 GFLraALGCQVYEGYGQTEctAGCTFTTPGDWT-----SGHVGAPLPCNHIKLVDAEELNywtCK-GE-GEICVKGPNVF 516
Cdd:PRK09088 271 GWL--DDGIPMVDGFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVVDDQGND---CPaGVpGELLLRGPNLS 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 517 KGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIEniyirsepvAQIYVHGDSLKAF 596
Cdd:PRK09088 344 PGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIE---------AVLADHPGIRECA 413
|
490
....*....|
gi 1907081036 597 LVGivVPDPE 606
Cdd:PRK09088 414 VVG--MADAQ 421
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
255-598 |
1.86e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 135.66 E-value: 1.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 255 GRENHHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTCaDVHFSYLPLAHMFERMVQSVV 334
Cdd:PRK05677 194 GAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEGC-EILIAPLPLYHIYAFTFHCMA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 335 YCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLlNRMydkifhqadtslkrwlleFAAkrkqaevrsgiIRNNSIWDE 414
Cdd:PRK05677 273 MMLIGNHNILISNPRDLPAMVKELGKWKFSGFVGL-NTL------------------FVA-----------LCNNEAFRK 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 415 LFFNKIQASLGGHvrMIVTGAAPASptvlgfLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVD- 493
Cdd:PRK05677 323 LDFSALKLTLSGG--MALQLATAER------WKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDd 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 494 -AEELNYwtckGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPE 571
Cdd:PRK05677 395 dGNELPL----GEvGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVSGFNVYPN 469
|
330 340 350
....*....|....*....|....*....|....
gi 1907081036 572 KIENIYIRSEPVAQ---IYV----HGDSLKAFLV 598
Cdd:PRK05677 470 ELEDVLAALPGVLQcaaIGVpdekSGEAIKVFVV 503
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
117-557 |
8.27e-33 |
|
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: 133.56 E-value: 8.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 117 PYQWLSYQEVAKRAEFLGSGLLQHDCKVGtEQFVGVFAQNRpEWIIAELACYTYSMVVVPLydtlGPGSISYIINTAdic 196
Cdd:cd05906 36 SEEFQSYQDLLEDARRLAAGLRQLGLRPG-DSVILQFDDNE-DFIPAFWACVLAGFVPAPL----TVPPTYDEPNAR--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 197 tvivdkphkaTLLLEHVerKETPGLKLVI----LMEPFEDALRERGKkCGVDIKSMQAIEDCGREnHHAPvPPRPDDLSI 272
Cdd:cd05906 107 ----------LRKLRHI--WQLLGSPVVLtdaeLVAEFAGLETLSGL-PGIRVLSIEELLDTAAD-HDLP-QSRPDDLAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 273 VCFTSGTTGNPKGAMLTHGNVVADFSGflKVTESQWAPtcADVHFSYLPLAHmfermVQSVVYCHggrvgffQGDIRLLS 352
Cdd:cd05906 172 LMLTSGSTGFPKAVPLTHRNILARSAG--KIQHNGLTP--QDVFLNWVPLDH-----VGGLVELH-------LRAVYLGC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 353 DDMKALRPTIFPVVPRLLNRMyDKifHQADTSlkrWLLEFA-AK-RKQAEVRSGiirnnSIWDelffnkiqasLGGHVRM 430
Cdd:cd05906 236 QQVHVPTEEILADPLRWLDLI-DR--YRVTIT---WAPNFAfALlNDLLEEIED-----GTWD----------LSSLRYL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 431 IVTGAAPASPTVLGFLRAALGCQVYE-----GYGQTECTAGCTFTTP---GDWTSGH----VGAPLPCNHIKLVDAEEln 498
Cdd:cd05906 295 VNAGEAVVAKTIRRLLRLLEPYGLPPdairpAFGMTETCSGVIYSRSfptYDHSQALefvsLGRPIPGVSMRIVDDEG-- 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081036 499 ywTCKGEGEIC---VKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGkWLPEGTLKIIDRKK 557
Cdd:cd05906 373 --QLLPEGEVGrlqVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
93-634 |
7.91e-32 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 130.62 E-value: 7.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 93 YQVFRRGLSISGNGPCLGFRKPEQPYQWLSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELACYTYSM 172
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRALG--VKKGDRVAIYLPNIPEAVIAMLACARIGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 173 VVVPLYDTLGPGSISYIINTADICTVIVD----KPHKATLLLEHVE--RKETPGLKLVILMEPFEDALRERGkkcgvDIK 246
Cdd:COG0365 90 VHSPVFPGFGAEALADRIEDAEAKVLITAdgglRGGKVIDLKEKVDeaLEELPSLEHVIVVGRTGADVPMEG-----DLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 247 SMQAIEDCGREnhHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsGFLKVTESQWAPTCADVHFS-------- 318
Cdd:COG0365 165 WDELLAAASAE--FEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLV---HAATTAKYVLDLKPGDVFWCtadigwat 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 319 ------YLPLAH-----MFERmvqSVVYCHGGRVgffqgdIRLLSDdmkaLRPTIFPVVPRLLnRMydkifhqadtsLKR 387
Cdd:COG0365 240 ghsyivYGPLLNgatvvLYEG---RPDFPDPGRL------WELIEK----YGVTVFFTAPTAI-RA-----------LMK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 388 WLLEFAAKRKQAevrsgiirnnsiwdelffnkiqaslggHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECtaGC 467
Cdd:COG0365 295 AGDEPLKKYDLS---------------------------SLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTET--GG 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 468 TFTTPGDWTS---GHVGAPLPCNHIKLVDAEelnywtckG-------EGEICVKG--PNVFKGYLKDEDRTKEAL--DSD 533
Cdd:COG0365 346 IFISNLPGLPvkpGSMGKPVPGYDVAVVDED--------GnpvppgeEGELVIKGpwPGMFRGYWNDPERYRETYfgRFP 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 534 GWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQIYV----H---GDSLKAFlvgiVVPDPE 606
Cdd:COG0365 418 GWYRTGDGARRDEDGYFWILGRSDDVINVS-GHRIGTAEIESALVSHPAVAEAAVvgvpDeirGQVVKAF----VVLKPG 492
|
570 580
....*....|....*....|....*...
gi 1907081036 607 VMPSwaqkkgiegtyQELcmKKELKKAI 634
Cdd:COG0365 493 VEPS-----------DEL--AKELQAHV 507
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
121-610 |
9.59e-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: 128.80 E-value: 9.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELACY----TYsmvvVPLYDTLGPGSISYIINTAdic 196
Cdd:cd05930 13 LTYAELDARANRLARYLRERG--VGPGDLVAVLLERSLEMVVAILAVLkagaAY----VPLDPSYPAERLAYILEDS--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 197 tvivdkphKATLLLEHverketpglklvilmepfedalrergkkcgvdiksmqaiedcgrenhhapvpprPDDLSIVCFT 276
Cdd:cd05930 84 --------GAKLVLTD------------------------------------------------------PDDLAYVIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 277 SGTTGNPKGAMLTHGNVV---ADFSGFLKVTES----QWAPTCADVHFS--YLPLAHmfermvqsvvychGGRV----GF 343
Cdd:cd05930 102 SGSTGKPKGVMVEHRGLVnllLWMQEAYPLTPGdrvlQFTSFSFDVSVWeiFGALLA-------------GATLvvlpEE 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 344 FQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTSLkrwllefaakrkqaevrsgiirnnsiwdelffnkiqas 423
Cdd:cd05930 169 VRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAALPSL-------------------------------------- 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 424 lgghvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFT--TPGDWTSGHV--GAPLPCNHIKLVDaEELN 498
Cdd:cd05930 211 -----RLVLVGGEALPPDLVrRWRELLPGARLVNLYGPTEATVDATYYrvPPDDEEDGRVpiGRPIPNTRVYVLD-ENLR 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 499 YWTCKGEGEICVKGPNVFKGYLKDEDRTKEA-----LDSDGWLH-TGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEK 572
Cdd:cd05930 285 PVPPGVPGELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIELGE 363
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1907081036 573 IENIYIRSEPVAQIYV---HGDSLKAFLVGIVVPDPEVMPS 610
Cdd:cd05930 364 IEAALLAHPGVREAAVvarEDGDGEKRLVAYVVPDEGGELD 404
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
255-605 |
1.11e-31 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 130.38 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 255 GRENHHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSgflkvTESQWAPTCA------DVHFSYLPLAHMFER 328
Cdd:PRK08751 195 GRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQ-----QAHQWLAGTGkleegcEVVITALPLYHIFAL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 329 MVQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLlNRMYDKIFhqadtslkrwllefaakrkqaevrsgiirN 408
Cdd:PRK08751 270 TANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGV-NTLFNGLL-----------------------------N 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 409 NSIWDELFFNKIQASLGGHvrMIVTGAapasptVLGFLRAALGCQVYEGYGQTECT-AGCTFTTPGDWTSGHVGAPLPCN 487
Cdd:PRK08751 320 TPGFDQIDFSSLKMTLGGG--MAVQRS------VAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLPIPST 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 488 HIKLVDaeELNYWTCKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGE 566
Cdd:PRK08751 392 DACIKD--DAGTVLAIGEiGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-LVSGF 468
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1907081036 567 YVAPEKIENIYIRSEPVAQIYVHG----DSLKAFLVGIVVPDP 605
Cdd:PRK08751 469 NVYPNEIEDVIAMMPGVLEVAAVGvpdeKSGEIVKVVIVKKDP 511
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
267-598 |
1.44e-31 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 129.79 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgflkVTESQWA--PTCADVH---FSYLPLAHMFERMVQSVVYCHGGRV 341
Cdd:PRK08974 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLAN------LEQAKAAygPLLHPGKelvVTALPLYHIFALTVNCLLFIELGGQ 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 342 GFF---QGDIRLLSDDMKALRPTIFPVVPRLLNRmydkifhqadtslkrWLlefaakrkqaevrsgiirNNSIWDELFFN 418
Cdd:PRK08974 279 NLLitnPRDIPGFVKELKKYPFTAITGVNTLFNA---------------LL------------------NNEEFQELDFS 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 419 KIQASLGGhvrmivtgAAPASPTVLGFLRAALGCQVYEGYGQTECT---AGCTFTTPGdwTSGHVGAPLPCNHIKLVDaE 495
Cdd:PRK08974 326 SLKLSVGG--------GMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVNPYDLDY--YSGSIGLPVPSTEIKLVD-D 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 496 ELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIEN 575
Cdd:PRK08974 395 DGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMI-LVSGFNVYPNEIED 472
|
330 340 350
....*....|....*....|....*....|
gi 1907081036 576 IYIRSEPVAQIY-------VHGDSLKAFLV 598
Cdd:PRK08974 473 VVMLHPKVLEVAavgvpseVSGEAVKIFVV 502
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
112-606 |
5.22e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 128.15 E-value: 5.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 112 RKPEQPYQW-----LSYQEVAKRAEFLgSGLLQHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSI 186
Cdd:PRK08314 22 RYPDKTAIVfygraISYRELLEEAERL-AGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 187 SYIINTADICTVIVD-------KPHKATLLLEHV-------ERKETPGLKLvilmepfEDALRERGKKCGVDIKSMQAIE 252
Cdd:PRK08314 101 AHYVTDSGARVAIVGselapkvAPAVGNLRLRHVivaqysdYLPAEPEIAV-------PAWLRAEPPLQALAPGGVVAWK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 253 DCGRENHHA-PVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkvteSQWAP-TCADVHFSYLPLAHM--FER 328
Cdd:PRK08314 174 EALAAGLAPpPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGS-----VLWSNsTPESVVLAVLPLFHVtgMVH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 329 MVQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLL-NRMYDKIFHQADTSlkrwllefaakrkqaevrsgiir 407
Cdd:PRK08314 249 SMNAPIYAGATVVLMPRWDREAAARLIERYRVTHWTNIPTMVvDFLASPGLAERDLS----------------------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 408 nnsiwdelffnkiqaSLgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWT-SGHVGAPLPC 486
Cdd:PRK08314 306 ---------------SL----RYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTE-TMAQTHSNPPDRPkLQCLGIPTFG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 487 NHIKLVDAEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEA---LDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlA 563
Cdd:PRK08314 366 VDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMIN-A 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1907081036 564 QGEYVAPEKIENIYIRSEPVAQIYV-------HGDSLKAFlvgiVVPDPE 606
Cdd:PRK08314 445 SGFKVWPAEVENLLYKHPAIQEACViatpdprRGETVKAV----VVLRPE 490
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
268-613 |
6.41e-31 |
|
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: 125.54 E-value: 6.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 268 DDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF---LKVTESqwaptcaDVHFSYLPLAHM--FERMVQSVVYchGGRVG 342
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSalnLGLTED-------DNWLCALPLFHIsgLSILMRSVIY--GMTVY 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 343 FFQG-DIRLLSDDMKALRPTIFPVVPRLLNRMYdKIFHQADTSlkrwllefaakrkqaevrsgiirnnsiwdelffnkiq 421
Cdd:cd05912 148 LVDKfDAEQVLHLINSGKVTIISVVPTMLQRLL-EILGEGYPN------------------------------------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 422 aslggHVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTE-CTAGCTFTtPGDWTS--GHVGAPLPCNHIKLVDAEELN 498
Cdd:cd05912 190 -----NLRCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTEtCSQIVTLS-PEDALNkiGSAGKPLFPVELKIEDDGQPP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 499 YwtckGEGEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYI 578
Cdd:cd05912 263 Y----EVGEILLKGPNVTKGYLNRPDATEESFE-NGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLL 336
|
330 340 350
....*....|....*....|....*....|....*
gi 1907081036 579 RSEPVAQIYVhgdslkaflVGIvvPDPEvmpsWAQ 613
Cdd:cd05912 337 SHPAIKEAGV---------VGI--PDDK----WGQ 356
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
122-606 |
9.50e-31 |
|
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: 127.26 E-value: 9.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 122 SYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIVD 201
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYG--LKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 202 KphKATLLLEHVERKeTPGLKLVILMEPFEDAlreRGKKCGVDIKSMQAIEDCGRENHHAPVPPRPDDLSIVCFTSGTTG 281
Cdd:cd17642 124 K--KGLQKVLNVQKK-LKIIKTIIILDSKEDY---KGYQCLYTFITQNLPPGFNEYDFKPPSFDRDEQVALIMNSSGSTG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 282 NPKGAMLTHGNVVADFSGFLKVT-ESQWAPTCADVhfSYLPLAHMFERMVQSVVYCHGGRVGffqgdirllsddmkalrp 360
Cdd:cd17642 198 LPKGVQLTHKNIVARFSHARDPIfGNQIIPDTAIL--TVIPFHHGFGMFTTLGYLICGFRVV------------------ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 361 tifpvvprLLNRMYDKIFHQA-------DTSLKRWLLEFAAKrkqaevrSGIIrnnsiwdelffNKIQASlggHVRMIVT 433
Cdd:cd17642 258 --------LMYKFEEELFLRSlqdykvqSALLVPTLFAFFAK-------STLV-----------DKYDLS---NLHEIAS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 434 GAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYWTCKGEGEICVKG 512
Cdd:cd17642 309 GGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 513 PNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYVHGds 592
Cdd:cd17642 389 PMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQHPKIFDAGVAG-- 465
|
490
....*....|....
gi 1907081036 593 lkaflvgivVPDPE 606
Cdd:cd17642 466 ---------IPDED 470
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
89-557 |
1.20e-30 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 127.76 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 89 ARTMYQVFRRGLSISGNGPCLGF-------RKPEQpyqwLSYqevakrAEFLG-----SGLLqHDCKVGTEQFVGVFAQN 156
Cdd:PRK07529 24 PASTYELLSRAAARHPDAPALSFlldadplDRPET----WTY------AELLAdvtrtANLL-HSLGVGPGDVVAFLLPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 157 RPEWIIAELACYTYSmVVVPLYDTLGPGSISYIINTADICTVIVDKPHKATLLLEHVE--RKETPGLKLVI-------LM 227
Cdd:PRK07529 93 LPETHFALWGGEAAG-IANPINPLLEPEQIAELLRAAGAKVLVTLGPFPGTDIWQKVAevLAALPELRTVVevdlaryLP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 228 EPFEDALRERGKKCGVDIKSMQAIEDCGRENHH-APVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsGFLKVTES 306
Cdd:PRK07529 172 GPKRLAVPLIRRKAHARILDFDAELARQPGDRLfSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVAN--AWLGALLL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 307 QWAPTcaDVHFSYLPLAHMFERMVQSVVYCHGGR---VGFFQG--DIRLLSDDMK---ALRPTIFPVVPRLLNRMYDKIF 378
Cdd:PRK07529 250 GLGPG--DTVFCGLPLFHVNALLVTGLAPLARGAhvvLATPQGyrGPGVIANFWKiveRYRINFLSGVPTVYAALLQVPV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 379 HQADTSLkrwlLEFAAkrkqaevrsgiirnnsiwdelffnkiqaslgghvrmivTGAAPASPTVLGFLRAALGCQVYEGY 458
Cdd:PRK07529 328 DGHDISS----LRYAL--------------------------------------CGAAPLPVEVFRRFEAATGVRIVEGY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 459 GQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLVDAEEL-NYWT-C-KGE-GEICVKGPNVFKGYLkDEDRTKEALDSD 533
Cdd:PRK07529 366 GLTEATCVSSVNPPdGERRIGSVGLRLPYQRVRVVILDDAgRYLRdCaVDEvGVLCIAGPNVFSGYL-EAAHNKGLWLED 444
|
490 500
....*....|....*....|....
gi 1907081036 534 GWLHTGDIGKWLPEGTLKIIDRKK 557
Cdd:PRK07529 445 GWLNTGDLGRIDADGYFWLTGRAK 468
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
121-606 |
1.32e-30 |
|
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: 125.28 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLlqHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 200
Cdd:cd05935 2 LTYLELLEVVKKLASFL--SNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 dkphkatllleHVERketpglklvilmepfedalrergkkcgvdiksmqaiedcgrenhhapvpprpDDLSIVCFTSGTT 280
Cdd:cd05935 80 -----------GSEL----------------------------------------------------DDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 281 GNPKGAMLTHGNVVADFSGflkvtESQWAP-TCADVHFSYLPLAHM--FERMVQSVVYCHGGRVGFFQGDIRLLSDDMKA 357
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQ-----SAVWTGlTPSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMARWDRETALELIEK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 358 LRPTIFPVVPRLLNrmydkifhqadtslkrwllefaakrkqaevrsgiirnnsiwDELFFNKIQASLGGHVRMIVTGAAP 437
Cdd:cd05935 172 YKVTFWTNIPTMLV-----------------------------------------DLLATPEFKTRDLSSLKVLTGGGAP 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 438 ASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYWTCKGEGEICVKGPNVFK 517
Cdd:cd05935 211 MPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFK 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 518 GYLKDEDRTKEALDSDG---WLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQIYV------ 588
Cdd:cd05935 291 GYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVisvpde 369
|
490
....*....|....*....
gi 1907081036 589 -HGDSLKAFlvgiVVPDPE 606
Cdd:cd05935 370 rVGEEVKAF----IVLRPE 384
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
121-590 |
1.50e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 126.81 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 200
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQPGDR--VGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVIC 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 DKPHKAT--------LLLEHVERKET-------PGLKLVILMEPFE-------DALRERGKkcGVdikSMQAIEDcgren 258
Cdd:PRK12583 124 ADAFKTSdyhamlqeLLPGLAEGQPGalacerlPELRGVVSLAPAPppgflawHELQARGE--TV---SREALAE----- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 259 hhAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSG-FLKVTESQwaPTCADVhfsylPLAHMFErMVQSVVY 335
Cdd:PRK12583 194 --RQASLDRDDPINIQYTSGTTGFPKGATLSHHNILnnGYFVAeSLGLTEHD--RLCVPV-----PLYHCFG-MVLANLG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 336 C--HGGRVGF----FQGDIRLLSddMKALRPTIFPVVPRL-LNRMYDKIFHQADTSlkrwllefaakrkqaEVRSGIIrn 408
Cdd:PRK12583 264 CmtVGACLVYpneaFDPLATLQA--VEEERCTALYGVPTMfIAELDHPQRGNFDLS---------------SLRTGIM-- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 409 nsiwdelffnkiqaslgghvrmivtGAAPASPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGD-----WTSghVGA 482
Cdd:PRK12583 325 -------------------------AGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSLQTTAADdlerrVET--VGR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 483 PLPCNHIKLVDAEELNywTCKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFk 561
Cdd:PRK12583 378 TQPHLEVKVVDPDGAT--VPRGEiGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMI- 454
|
490 500
....*....|....*....|....*....
gi 1907081036 562 LAQGEYVAPEKIENIYIRSEPVAQIYVHG 590
Cdd:PRK12583 455 IRGGENIYPREIEEFLFTHPAVADVQVFG 483
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
119-606 |
2.02e-30 |
|
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: 124.33 E-value: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 119 QWlSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTV 198
Cdd:cd05934 3 RW-TYAELLRESARIAAALAALGIRPGDR--VALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 199 IVDkphkatlllehverketpglklvilmePFEdalrergkkcgvdiksmqaiedcgrenhhapvpprpddlsiVCFTSG 278
Cdd:cd05934 80 VVD---------------------------PAS-----------------------------------------ILYTSG 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 279 TTGNPKGAMLTHGNVVadFSGflKVTESQWAPTCADVHFSYLPLAHM---FERMVQSVVycHGGRV--------GFFQGD 347
Cdd:cd05934 92 TTGPPKGVVITHANLT--FAG--YYSARRFGLGEDDVYLTVLPLFHInaqAVSVLAALS--VGATLvllprfsaSRFWSD 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 348 IRllsdDMKALRPTIFPVVPRLLNRmydkifhQADtslkrwllefAAKRKQAEVRsgiirnnsiwdelffnkiqaslggh 427
Cdd:cd05934 166 VR----RYGATVTNYLGAMLSYLLA-------QPP----------SPDDRAHRLR------------------------- 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 428 vrmiVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEelNYWTCKGE-G 506
Cdd:cd05934 200 ----AAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDD--GQELPAGEpG 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 507 EICVK---GPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSEPV 583
Cdd:cd05934 274 ELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVERAILRHPAV 351
|
490 500 510
....*....|....*....|....*....|
gi 1907081036 584 AQIYVHG-------DSLKAFlvgIVVPDPE 606
Cdd:cd05934 352 REAAVVAvpdevgeDEVKAV---VVLRPGE 378
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
255-607 |
2.04e-30 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 126.29 E-value: 2.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 255 GRENHHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADF--------SGFLKVTE-SQWAPTCAdvhfsyLPLAHM 325
Cdd:PRK07059 191 GARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqmeawlqPAFEKKPRpDQLNFVCA------LPLYHI 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 326 FERMVQSVVYCHGGRVGFF---QGDIRLLSDDMKALRPTIFPVVPRLLNRMYdkifhqadtslkrwllefaakrkqaevr 402
Cdd:PRK07059 265 FALTVCGLLGMRTGGRNILipnPRDIPGFIKELKKYQVHIFPAVNTLYNALL---------------------------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 403 sgiirNNSIWDELFFNKIQASLGGhvrmivtGAAPASPTVLGFLRAAlGCQVYEGYG--QTECTAGCTFTTPGDWTsGHV 480
Cdd:PRK07059 317 -----NNPDFDKLDFSKLIVANGG-------GMAVQRPVAERWLEMT-GCPITEGYGlsETSPVATCNPVDATEFS-GTI 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 481 GAPLPCNHIKLVDAE--ELNYwtckGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKK 557
Cdd:PRK07059 383 GLPLPSTEVSIRDDDgnDLPL----GEpGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKK 458
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081036 558 HIFkLAQGEYVAPEKIENIyIRSEP----VAQIYVH----GDSLKAFlvgIVVPDPEV 607
Cdd:PRK07059 459 DMI-LVSGFNVYPNEIEEV-VASHPgvleVAAVGVPdehsGEAVKLF---VVKKDPAL 511
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
269-599 |
4.71e-30 |
|
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: 121.45 E-value: 4.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 269 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSgflkvtesQWApTCADVHFS--YL---PLAHMFErmvqsvvYCHGGRVGF 343
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAA--------AWA-DCADLTEDdrYLiinPFFHTFG-------YKAGIVACL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 344 FQG---------DIRLLSDDMKALRPTIFPVVPRLlnrmYDKIFHQADtslkrwllefaakRKQAEVRSgiirnnsiwde 414
Cdd:cd17638 65 LTGatvvpvavfDVDAILEAIERERITVLPGPPTL----FQSLLDHPG-------------RKKFDLSS----------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 415 lffnkiqaslgghVRMIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGcTFTTPGD---WTSGHVGAPLPCNHIK 490
Cdd:cd17638 117 -------------LRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVA-TMCRPGDdaeTVATTCGRACPGFEVR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 491 LVDAeelnywtckgeGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAP 570
Cdd:cd17638 183 IADD-----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYP 250
|
330 340 350
....*....|....*....|....*....|....*.
gi 1907081036 571 EKIENIYIRSEPVAQIYV-------HGDSLKAFLVG 599
Cdd:cd17638 251 AEVEGALAEHPGVAQVAVigvpderMGEVGKAFVVA 286
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
24-693 |
7.64e-30 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 126.89 E-value: 7.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 24 SLSATTLVsVGALAAVLAYWLTHRPKALQPPCNLLKQSEEVEDGGGarrsvigGCTQLLTHYYDD---ARTMYQVFRRGL 100
Cdd:PTZ00297 366 SFSFMSLV-LCAAVWLLRWAQNSSIHPLLSERPFLTVEALKEKGEE-------CFALNLPREYNPlagVRSLGEMWERSV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 101 SISGNGPCLGFRKPEQPYQWLSYQEVAKRAEFLGSGLLQHDCKVGteQFVGVFAQNRPEWIIAELACYTYSMVVVPLydt 180
Cdd:PTZ00297 438 TRHSTFRCLGQTSESGESEWLTYGTVDARARELGSGLLALGVRPG--DVIGVDCEASRNIVILEVACALYGFTTLPL--- 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 181 LGPGS-ISYIINTADICTVIVDKPHKATLLLEHVERKETpglklVILMEPFEDALRER-GKKCGVDIKSMQAIEDCGREn 258
Cdd:PTZ00297 513 VGKGStMRTLIDEHKIKVVFADRNSVAAILTCRSRKLET-----VVYTHSFYDEDDHAvARDLNITLIPYEFVEQKGRL- 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 259 hhAPVPPRP--DDLSIVCFTSGTTGNPKGAML-----THGNVVADFSGFLKvteSQWAPTCAD----VHFSylPLAHMFE 327
Cdd:PTZ00297 587 --CPVPLKEhvTTDTVFTYVVDNTTSASGDGLavvrvTHADVLRDISTLVM---TGVLPSSFKkhlmVHFT--PFAMLFN 659
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 328 RMVQSVVYCHGGRVGffQGDIRLLSDDMKALRPTIFPVVPRLlnrmydkiFHQADTSLKR----------WLLEfaakrK 397
Cdd:PTZ00297 660 RVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSL--------FSTSRLQLSRanerysavysWLFE-----R 724
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 398 QAEVRSGII----RNNSIWDELFFNKIQASLGGHVRMIVTGAAPASPTvlgflraalgcqvyegYGQTECTAGCTfttpg 473
Cdd:PTZ00297 725 AFQLRSRLInihrRDSSLLRFIFFRATQELLGGCVEKIVLCVSEESTS----------------FSLLEHISVCY----- 783
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 474 dwtsghvgAPLPCnhiklvdaeELNYWTCkgEGEICVKG---PNVFKGYLKDEDRTKEAldSDGWL---------HTGDI 541
Cdd:PTZ00297 784 --------VPCLR---------EVFFLPS--EGVFCVDGtpaPSLQVDLEPFDEPSDGA--GIGQLvlakkgeprRTLPI 842
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 542 -GKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAfLVGIVVPDPEVMP-SWAQKKGIE- 618
Cdd:PTZ00297 843 aAQWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEfEWRQSHCMGe 921
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 619 --GTYQELCMKKELKKA---ILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 693
Cdd:PTZ00297 922 ggGPARQLGWTELVAYAsslLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIERFY 1001
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-605 |
8.61e-30 |
|
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: 120.85 E-value: 8.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSGF-LKVTESQwaPTCADVhfsylPLAHMFErMVQSVVYC--HGGRV 341
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVnnGYFIGErLGLTEQD--RLCIPV-----PLFHCFG-SVLGVLACltHGATM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 342 GF----FqgDIRLLSDDMKALRPTIFPVVPRllnrMYDKIFHQADtslkrwLLEFAAKRkqaeVRSGIIrnnsiwdelff 417
Cdd:cd05917 73 VFpspsF--DPLAVLEAIEKEKCTALHGVPT----MFIAELEHPD------FDKFDLSS----LRTGIM----------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 418 nkiqaslgghvrmivtGAAPASPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGDWTS---GHVGAPLPCNHIKLVD 493
Cdd:cd05917 126 ----------------AGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDSIEkrvNTVGRIMPHTEAKIVD 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 494 AEelnywTCK----GE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYV 568
Cdd:cd05917 190 PE-----GGIvppvGVpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGENI 263
|
330 340 350
....*....|....*....|....*....|....*..
gi 1907081036 569 APEKIENIyirsepvaqIYVHGDSLKAFLVGivVPDP 605
Cdd:cd05917 264 YPREIEEF---------LHTHPKVSDVQVVG--VPDE 289
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
220-615 |
1.79e-29 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 122.16 E-value: 1.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 220 GLKLVILMEPFEDALRERGKKCGVDIKSMQAIEDCGRENHHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG 299
Cdd:cd05922 69 GGRIVLADAGAADRLRDALPASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 300 ---FLKVTESQWAPTCADVHFSY-LPLAHMFERMVQSVVYCHGGRVGffqgdiRLLSDDMKALRPTIFPVVPRLLnrmyd 375
Cdd:cd05922 149 iaeYLGITADDRALTVLPLSYDYgLSVLNTHLLRGATLVLTNDGVLD------DAFWEDLREHGATGLAGVPSTY----- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 376 kifhqadtslkrwllefaakrkqaevrsgiirnnSIWDELFFNKIQASlggHVRMIVTGAAPASPTVLGFLRAAL-GCQV 454
Cdd:cd05922 218 ----------------------------------AMLTRLGFDPAKLP---SLRYLTQAGGRLPQETIARLRELLpGAQV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 455 YEGYGQTECTAGCTFTTPG--DWTSGHVGAPLPCNHIKLVDAEELNYWTckGE-GEICVKGPNVFKGYLKDEDRTKEALD 531
Cdd:cd05922 261 YVMYGQTEATRRMTYLPPEriLEKPGSIGLAIPGGEFEILDDDGTPTPP--GEpGEIVHRGPNVMKGYWNDPPYRRKEGR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 532 SDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIyIRSEP---VAQIYVHGDSLKAFLVGIVVPDPEVM 608
Cdd:cd05922 339 GGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF-GNRISPTEIEAA-ARSIGliiEAAAVGLPDPLGEKLALFVTAPDKID 416
|
....*..
gi 1907081036 609 PSWAQKK 615
Cdd:cd05922 417 PKDVLRS 423
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
122-588 |
5.89e-29 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 119.68 E-value: 5.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 122 SYQEVAKRAEFLGSGLLQHdCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGS-ISYIINTADICTVIV 200
Cdd:TIGR01733 1 TYRELDERANRLARHLRAA-GGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPL-DPAYPAErLAFILEDAGARLLLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 DKPHkatlllehveRKETPGLKLVILMEPFEDALrergkkcgvdiksmqAIEDCGRENHhAPVPPRPDDLSIVCFTSGTT 280
Cdd:TIGR01733 79 DSAL----------ASRLAGLVLPVILLDPLELA---------------ALDDAPAPPP-PDAPSGPDDLAYVIYTSGST 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 281 GNPKGAMLTHGNVVAdfsgFLKVTESQWAPTCADVHFSYLPLAH------MFermvqsVVYCHGGRVGFFQGDIRLlsDD 354
Cdd:TIGR01733 133 GRPKGVVVTHRSLVN----LLAWLARRYGLDPDDRVLQFASLSFdasveeIF------GALLAGATLVVPPEDEER--DD 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 355 MKALRptifpvvpRLLNRMYDKIFHQADTSLKRWLLEfaakrkqaevrsgiirnnsiwdelffnkiQASLGGHVRMIVTG 434
Cdd:TIGR01733 201 AALLA--------ALIAEHPVTVLNLTPSLLALLAAA-----------------------------LPPALASLRLVILG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 435 AAPASPTVLGFLRAALG-CQVYEGYGQTECTAGCT-FTTPGDWTSGHV----GAPLPCNHIKLVDA--EELNYWtckGEG 506
Cdd:TIGR01733 244 GEALTPALVDRWRARGPgARLINLYGPTETTVWSTaTLVDPDDAPRESpvpiGRPLANTRLYVLDDdlRPVPVG---VVG 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 507 EICVKGPNVFKGYLKDEDRTKEA-LDSDGWL-------HTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYI 578
Cdd:TIGR01733 321 ELYIGGPGVARGYLNRPELTAERfVPDPFAGgdgarlyRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAALL 399
|
490
....*....|
gi 1907081036 579 RSEPVAQIYV 588
Cdd:TIGR01733 400 RHPGVREAVV 409
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
262-578 |
6.74e-29 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 121.87 E-value: 6.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 262 PVPP-RPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWA-PTCADVHFSYLPLAHMFermvqsvvychgG 339
Cdd:PLN02574 191 PKPViKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEyPGSDNVYLAALPMFHIY------------G 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 340 RVGFFQGDIRL-----------LSDDMKAL---RPTIFPVVPRLLnrmydkifhqadTSLKRwllefAAKRKQAEVRsgi 405
Cdd:PLN02574 259 LSLFVVGLLSLgstivvmrrfdASDMVKVIdrfKVTHFPVVPPIL------------MALTK-----KAKGVCGEVL--- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 406 irnnsiwdelffnkiqaslgGHVRMIVTGAAPAS-PTVLGFLRAALGCQVYEGYGQTECTAGCT--FTTPGDWTSGHVGA 482
Cdd:PLN02574 319 --------------------KSLKQVSCGAAPLSgKFIQDFVQTLPHVDFIQGYGMTESTAVGTrgFNTEKLSKYSSVGL 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 483 PLPCNHIKLVDAEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKL 562
Cdd:PLN02574 379 LAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY 458
|
330
....*....|....*.
gi 1907081036 563 aQGEYVAPEKIENIYI 578
Cdd:PLN02574 459 -KGFQIAPADLEAVLI 473
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
119-550 |
8.75e-29 |
|
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: 123.43 E-value: 8.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 119 QWLSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELA------CYtysmvvVPLYDTLGPGSISYIINT 192
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALG--VGPGDLVGVCLERSLEMVVALLAvlkagaAY------VPLDPAYPAERLAYMLED 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 193 ADICTVIVDKPHKATLllehverkETPGLKLVILmepfeDALrergkkcgvdiksmqAIEDCGRENhhAPVPPRPDDLSI 272
Cdd:COG1020 572 AGARLVLTQSALAARL--------PELGVPVLAL-----DAL---------------ALAAEPATN--PPVPVTPDDLAY 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 273 VCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTES----QWAPTCADVHFS--YLPLahmfermvqsvvyCHGGRVGF 343
Cdd:COG1020 622 VIYTSGSTGRPKGVMVEHRALVnllAWMQRRYGLGPGdrvlQFASLSFDASVWeiFGAL-------------LSGATLVL 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 344 FQGDIRL----LSDDMKALRPTIFPVVPRLLNRmydkifhqadtslkrwLLEFAAKRkqaevrsgiirnnsiwdelffnk 419
Cdd:COG1020 689 APPEARRdpaaLAELLARHRVTVLNLTPSLLRA----------------LLDAAPEA----------------------- 729
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 420 iqaslGGHVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTF--TTPGDWTSGHV--GAPLPCNHIKLVDA 494
Cdd:COG1020 730 -----LPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTVDSTYyeVTPPDADGGSVpiGRPIANTRVYVLDA 804
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 495 EelnywtckGE-------GEICVKGPNVFKGYLKDEDRTKEA-----LDSDG--WLHTGDIGKWLPEGTL 550
Cdd:COG1020 805 H--------LQpvpvgvpGELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNL 866
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
122-576 |
1.27e-28 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 121.01 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 122 SYQEVAKRAEFLGSGLLQHDCKVGTeqfvgVFAQNRPEW---IIAELACYTYSMVVVPLYDTLGPGSISYIIN----TAD 194
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGD-----RVAFQLPGWcefTIIYLACLKVGAVSVPLLPSWREAELVWVLNkcqaKMF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 195 ICTVIVDKPHKATLLLEhvERKETPGLKLVILMEPFEDALRergkkcgvDIKSMQAIEDcgRENHHAPVPPRPDDLSIVC 274
Cdd:PRK06087 126 FAPTLFKQTRPVDLILP--LQNQLPQLQQIVGVDKLAPATS--------SLSLSQIIAD--YEPLTTAITTHGDELAAVL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 275 FTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAptcaDVHFSYLPLAHmfermvqSVVYCHGGRVGFFQGDIRLLSDD 354
Cdd:PRK06087 194 FTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQ----DVFMMPAPLGH-------ATGFLHGVTAPFLIGARSVLLDI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 355 MKALRPTifpvvpRLLNRmydkifhQADTslkrWLL---EFaakrkqaevrsgiirnnsIWDELffNKIQASlGGHV--- 428
Cdd:PRK06087 263 FTPDACL------ALLEQ-------QRCT----CMLgatPF------------------IYDLL--NLLEKQ-PADLsal 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 429 RMIVTGAAPASPTVLgflRAAL--GCQVYEGYGQTECTAGcTFTTPGD---WTSGHVGAPLPCNHIKLVDaEELNYWTCK 503
Cdd:PRK06087 305 RFFLCGGTTIPKKVA---RECQqrGIKLLSVYGSTESSPH-AVVNLDDplsRFMHTDGYAAAGVEIKVVD-EARKTLPPG 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081036 504 GEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENI 576
Cdd:PRK06087 380 CEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDI 451
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
121-613 |
2.09e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 120.09 E-value: 2.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAE-----FLGSGLLQHDCkvgteqfVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADI 195
Cdd:PRK06188 38 LTYGQLADRISryiqaFEALGLGTGDA-------VALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 196 CTVIVDK---PHKATLLLEHVerketPGLKLVILMEPFEDalrergkkcGVDIKSMQAIEDcgrenhHAPVPP--RPDDL 270
Cdd:PRK06188 111 STLIVDPapfVERALALLARV-----PSLKHVLTLGPVPD---------GVDLLAAAAKFG------PAPLVAaaLPPDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 271 SIVCFTSGTTGNPKGAMLTHGNVVADFSGFLkvTESQWAPtcadvHFSYL---PLAHMFERMVQSVVYcHGGRVGFFQG- 346
Cdd:PRK06188 171 AGLAYTGGTTGKPKGVMGTHRSIATMAQIQL--AEWEWPA-----DPRFLmctPLSHAGGAFFLPTLL-RGGTVIVLAKf 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 347 DIRLLSDDMKALRPTIFPVVPRLLNRmydkifhqadtslkrwLLEFAAKRKqaevrsgiiRNNSiwdelffnkiqaSLgg 426
Cdd:PRK06188 243 DPAEVLRAIEEQRITATFLVPTMIYA----------------LLDHPDLRT---------RDLS------------SL-- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 427 hvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHV------GAPLPCNHIKLVDAEELNYW 500
Cdd:PRK06188 284 --ETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLRVALLDEDGREVA 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 501 TckGE-GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIR 579
Cdd:PRK06188 362 Q--GEvGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMI-VTGGFNVFPREVEDVLAE 437
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1907081036 580 SEPVAQIYV-------HGDSLKAflvgIVVPDPEVMPSWAQ 613
Cdd:PRK06188 438 HPAVAQVAVigvpdekWGEAVTA----VVVLRPGAAVDAAE 474
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
121-588 |
2.30e-28 |
|
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: 118.64 E-value: 2.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLLQhdCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADIctviv 200
Cdd:cd05903 2 LTYSELDTRADRLAAGLAA--LGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 dkphkatlllehverketpglKLVILMEPFedalrergkkcgvdiksmqaiedcgRENHHAPVPprpDDLSIVCFTSGTT 280
Cdd:cd05903 75 ---------------------KVFVVPERF-------------------------RQFDPAAMP---DAVALLLFTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 281 GNPKGAMLTHGNVVADFSGFLKvtesQWAPTCADVHFSYLPLAHMfermvqsVVYCHGGRVGFFQGDIRLLSDDMKALRp 360
Cdd:cd05903 106 GEPKGVMHSHNTLSASIRQYAE----RLGLGPGDVFLVASPMAHQ-------TGFVYGFTLPLLLGAPVVLQDIWDPDK- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 361 tifpvVPRLLNRMYDKIFHQADTSLKRWL--LEFAAKRKQaevrsgiirnnsiwdelffnkiqaslggHVRMIVTGAAPA 438
Cdd:cd05903 174 -----ALALMREHGVTFMMGATPFLTDLLnaVEEAGEPLS----------------------------RLRTFVCGGATV 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 439 SPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGD----WTSGhvGAPLPCNHIKLVDAEELNYwTCKGEGEICVKGPN 514
Cdd:cd05903 221 PRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPedrrLYTD--GRPLPGVEIKVVDDTGATL-APGVEGELLSRGPS 297
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081036 515 VFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYV 588
Cdd:cd05903 298 VFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAV 369
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
255-598 |
3.38e-28 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 119.54 E-value: 3.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 255 GRENHHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTeSQWAP-------TCADVHFSYLPLAHMFE 327
Cdd:PRK12492 194 GRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACL-SQLGPdgqplmkEGQEVMIAPLPLYHIYA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 328 rmvqsvvychggrvgfFQGDIRLLsddMKALRPTIFPVVPRLLNRMYDKifhqadtsLKRWLLefaakrkqaevrSGIIR 407
Cdd:PRK12492 273 ----------------FTANCMCM---MVSGNHNVLITNPRDIPGFIKE--------LGKWRF------------SALLG 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 408 NNSIWDELF----FNKIQASlggHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGA 482
Cdd:PRK12492 314 LNTLFVALMdhpgFKDLDFS---ALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELARlGTVGI 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 483 PLPCNHIKLVDAE--ELNYwtckGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHI 559
Cdd:PRK12492 391 PVPGTALKVIDDDgnELPL----GErGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDL 466
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1907081036 560 FkLAQGEYVAPEKIENIYIRSEPVAQIYV-------HGDSLKAFLV 598
Cdd:PRK12492 467 I-IVSGFNVYPNEIEDVVMAHPKVANCAAigvpderSGEAVKLFVV 511
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
123-590 |
1.03e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 117.37 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 123 YQEVAKRAEFLGSGLLQHDckvgteQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIVDk 202
Cdd:PRK03640 34 HEAVVSVAGKLAALGVKKG------DRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITD- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 203 phkatlllehverketpglklvilmEPFEDALRErgkKCGVDIKSMQAiedcGRENHHAPVPPRP-DDLSIVCFTSGTTG 281
Cdd:PRK03640 107 -------------------------DDFEAKLIP---GISVKFAELMN----GPKEEAEIQEEFDlDEVATIMYTSGTTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 282 NPKGAMLTHGNVVADFSGF---LKVTESQ-WapTCAdvhfsyLPLAHM--FERMVQSVVYchGGRVGFFQG-DIRLLSDD 354
Cdd:PRK03640 155 KPKGVIQTYGNHWWSAVGSalnLGLTEDDcW--LAA------VPIFHIsgLSILMRSVIY--GMRVVLVEKfDAEKINKL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 355 MKALRPTIFPVVPRLLNRMYDKIFhqadtslkrwllefaakrkqaevrsgiirnnsiwdelffnkiQASLGGHVRMIVTG 434
Cdd:PRK03640 225 LQTGGVTIISVVSTMLQRLLERLG------------------------------------------EGTYPSSFRCMLLG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 435 AAPASPTVLGFLRAAlGCQVYEGYGQTEcTAGCTFTTPGDWTS---GHVGAPL-PCNhIKLVDaeELNYWTCKGEGEICV 510
Cdd:PRK03640 263 GGPAPKPLLEQCKEK-GIPVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLfPCE-LKIEK--DGVVVPPFEEGEIVV 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 511 KGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYVHG 590
Cdd:PRK03640 338 KGPNVTKGYLNREDATRETFQ-DGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPGVAEAGVVG 415
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
119-606 |
1.19e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 117.27 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 119 QWLSYQEVAKRAEFLgSGLLQHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTV 198
Cdd:PRK06839 26 EEMTYKQLHEYVSKV-AAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 199 IVDKPHKATLLLehverketpgLKLVILMEPFedalrergkkcgVDIKSMQAIEDCGRENHhapVPPRPDDLSIVCFTSG 278
Cdd:PRK06839 105 FVEKTFQNMALS----------MQKVSYVQRV------------ISITSLKEIEDRKIDNF---VEKNESASFIICYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 279 TTGNPKGAMLTHGNVvadfsgFLKVTESQWAP--TCADVHFSYLPLAHMfermvqsvvychgGRVGFFqgdirllsddmk 356
Cdd:PRK06839 160 TTGKPKGAVLTQENM------FWNALNNTFAIdlTMHDRSIVLLPLFHI-------------GGIGLF------------ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 357 ALrPTIFP----VVPRLLNRmyDKIFHQADTslKRWLLEFAAKRKQAEVRSGIIRNNSIWDelffnkiqaslggHVRMIV 432
Cdd:PRK06839 209 AF-PTLFAggviIVPRKFEP--TKALSMIEK--HKVTVVMGVPTIHQALINCSKFETTNLQ-------------SVRWFY 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 433 TGAAPAS-PTVLGFLRAalGCQVYEGYGQTEcTAGCTFTTPGD---WTSGHVGAPLPCNHIKLVDaEELNYWTCKGEGEI 508
Cdd:PRK06839 271 NGGAPCPeELMREFIDR--GFLFGQGFGMTE-TSPTVFMLSEEdarRKVGSIGKPVLFCDYELID-ENKNKVEVGEVGEL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 509 CVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIyirsepvaqIYV 588
Cdd:PRK06839 347 LIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQV---------INK 415
|
490
....*....|....*...
gi 1907081036 589 HGDSLKAFLVGivVPDPE 606
Cdd:PRK06839 416 LSDVYEVAVVG--RQHVK 431
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
259-605 |
1.57e-27 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 116.90 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 259 HHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgfLKVTESQWAPTCADVHFSYLPLAHMFERMVQS-VVYCH 337
Cdd:PRK07514 147 DFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSN----ALTLVDYWRFTPDDVLIHALPIFHTHGLFVATnVALLA 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 338 GGRVGFFQG-DIRLLSDDMKalRPTIFPVVPRLLNRMYdkifhqADTSLKRwllEFAAkrkqaevrsgiirnnsiwdelf 416
Cdd:PRK07514 223 GASMIFLPKfDPDAVLALMP--RATVMMGVPTFYTRLL------QEPRLTR---EAAA---------------------- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 417 fnkiqaslggHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTfTTP--GDWTSGHVGAPLPCNHIKLVDA 494
Cdd:PRK07514 270 ----------HMRLFISGSAPLLAETHREFQERTGHAILERYGMTE-TNMNT-SNPydGERRAGTVGFPLPGVSLRVTDP 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 495 E---ELNywtcKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIfkLAQGEY-VA 569
Cdd:PRK07514 338 EtgaELP----PGEiGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDL--IISGGYnVY 411
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1907081036 570 PEKIENiYIRSEP-VAQIYVHGDSLKAF---LVGIVVPDP 605
Cdd:PRK07514 412 PKEVEG-EIDELPgVVESAVIGVPHPDFgegVTAVVVPKP 450
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
248-588 |
2.85e-27 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 116.62 E-value: 2.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 248 MQAIEDCGRENHHAPVppRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTCADVhfSYLPLAHMF- 326
Cdd:PLN02330 166 LEAADRAGDTSDNEEI--LQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMIGQVVTL--GLIPFFHIYg 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 327 -ERMVQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYdkifhqadtslkrwllefaakrkqaevrsgi 405
Cdd:PLN02330 242 iTGICCATLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLV------------------------------- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 406 irNNSIWDELFFNKIQaslgghVRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTagCTFTTPGDWTSGH----- 479
Cdd:PLN02330 291 --KNPIVEEFDLSKLK------LQAIMTAAAPLAPELLtAFEAKFPGVQVQEAYGLTEHS--CITLTHGDPEKGHgiakk 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 480 --VGAPLPCNHIKLVDAEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKK 557
Cdd:PLN02330 361 nsVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIK 440
|
330 340 350
....*....|....*....|....*....|.
gi 1907081036 558 HIFKLaQGEYVAPEKIENIYIRSEPVAQIYV 588
Cdd:PLN02330 441 ELIKY-KGFQVAPAELEAILLTHPSVEDAAV 470
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
112-605 |
4.51e-27 |
|
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: 115.81 E-value: 4.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 112 RKPEQPYQWLSYQEVAKRAEFLGSGLlqHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIIN 191
Cdd:cd12119 17 RTHEGEVHRYTYAEVAERARRLANAL--RRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 192 TADICTVIVDkphkATLL---------LEHVERketpglklVILMEPFEDALRERGKKcgvDIKSMQAIEDcgrenhHAP 262
Cdd:cd12119 95 HAEDRVVFVD----RDFLplleaiaprLPTVEH--------VVVMTDDAAMPEPAGVG---VLAYEELLAA------ESP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 263 VPPRPD----DLSIVCFTSGTTGNPKGAMLTHGNVV-----ADFSGFLKVTESqwaptcaDVhfsYLPLAHMFERMVQSV 333
Cdd:cd12119 154 EYDWPDfdenTAAAICYTSGTTGNPKGVVYSHRSLVlhamaALLTDGLGLSES-------DV---VLPVVPMFHVNAWGL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 334 VYchggrVGFFQG----------DIRLLSDDMKALRPTIFPVVPRLlnrmydkifhqadtslkrWLLefaakrkqaeVRS 403
Cdd:cd12119 224 PY-----AAAMVGaklvlpgpylDPASLAELIEREGVTFAAGVPTV------------------WQG----------LLD 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 404 GIIRNNSiwdELFfnkiqaslggHVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPgdwTSGHV--- 480
Cdd:cd12119 271 HLEANGR---DLS----------SLRRVVIGGSAVPRSLIEAFEE-RGVRVIHAWGMTETSPLGTVARP---PSEHSnls 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 481 -----------GAPLPCNHIKLVDAE--ELNyWTCKGEGEICVKGPNVFKGYLKDeDRTKEALDSDGWLHTGDIGKWLPE 547
Cdd:cd12119 334 edeqlalrakqGRPVPGVELRIVDDDgrELP-WDGKAVGELQVRGPWVTKSYYKN-DEESEALTEDGWLRTGDVATIDED 411
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081036 548 GTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQIYVhgdslkaflvgIVVPDP 605
Cdd:cd12119 412 GYLTITDRSKDVIKSG-GEWISSVELENAIMAHPAVAEAAV-----------IGVPHP 457
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
220-578 |
4.69e-27 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 115.85 E-value: 4.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 220 GLKLVILMEPFEDALRERGKKCGVDIKSM-QAIEDCGR--------ENHHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTH 290
Cdd:PLN02246 122 GAKLIITQSCYVDKLKGLAEDDGVTVVTIdDPPEGCLHfseltqadENELPEVEISPDDVVALPYSSGTTGLPKGVMLTH 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 291 GNVVADFSGFLKVTESQWAPTCADVHFSYLPLAHMFErmVQSVVYChGGRVG--------FfqgDIRLLSDDMKALRPTI 362
Cdd:PLN02246 202 KGLVTSVAQQVDGENPNLYFHSDDVILCVLPMFHIYS--LNSVLLC-GLRVGaailimpkF---EIGALLELIQRHKVTI 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 363 FPVVPRLLnrmydkifhqadtslkrwlLEFAakrKQAEVRSgiirnnsiwDELffnkiqASlgghVRMIVTGAAPASPTV 442
Cdd:PLN02246 276 APFVPPIV-------------------LAIA---KSPVVEK---------YDL------SS----IRMVLSGAAPLGKEL 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 443 LGFLRAALGCQVY-EGYGQTE-------CTAgctFT-TPGDWTSGHVGAPLPCNHIKLVDAE---ELNYWTCkgeGEICV 510
Cdd:PLN02246 315 EDAFRAKLPNAVLgQGYGMTEagpvlamCLA---FAkEPFPVKSGSCGTVVRNAELKIVDPEtgaSLPRNQP---GEICI 388
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081036 511 KGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYI 578
Cdd:PLN02246 389 RGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAELEALLI 455
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
114-608 |
9.33e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 115.29 E-value: 9.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 114 PEQPYQWlSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVV---PLYDTlgpGSISYII 190
Cdd:PRK08315 38 RDQGLRW-TYREFNEEVDALAKGLLALGIEKGDR--VGIWAPNVPEWVLTQFATAKIGAILVtinPAYRL---SELEYAL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 191 NTADICT-VIVDK--------------PHKATLLLEHVERKETPGLKLVILMepfeDALRERGkkcgvdIKSMQAIEDCG 255
Cdd:PRK08315 112 NQSGCKAlIAADGfkdsdyvamlyelaPELATCEPGQLQSARLPELRRVIFL----GDEKHPG------MLNFDELLALG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 256 RENHHAPVPPR-----PDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsGFLkVTESQwAPTCAD-----VhfsylPLAHM 325
Cdd:PRK08315 182 RAVDDAELAARqatldPDDPINIQYTSGTTGFPKGATLTHRNILNN--GYF-IGEAM-KLTEEDrlcipV-----PLYHC 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 326 FErMVQSVVYC--HGGRV-----GFfqgdirllsDDMKALR-------------PTIFPVVprlLNrmyDKIFHQAD-TS 384
Cdd:PRK08315 253 FG-MVLGNLACvtHGATMvypgeGF---------DPLATLAaveeerctalygvPTMFIAE---LD---HPDFARFDlSS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 385 LkrwllefaakrkqaevRSGIirnnsiwdelffnkiqaslgghvrMivtgAAPASPT-----VLGFLRAAlgcQVYEGYG 459
Cdd:PRK08315 317 L----------------RTGI------------------------M----AGSPCPIevmkrVIDKMHMS---EVTIAYG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 460 QTECTAGCTFTTPGD------WTsghVGAPLPCNHIKLVDAEelnywTCK----GE-GEICVKGPNVFKGYLKDEDRTKE 528
Cdd:PRK08315 350 MTETSPVSTQTRTDDplekrvTT---VGRALPHLEVKIVDPE-----TGEtvprGEqGELCTRGYSVMKGYWNDPEKTAE 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 529 ALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIyirsepvaqIYVHGDSLKAFLVGivVPDP--- 605
Cdd:PRK08315 422 AIDADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEF---------LYTHPKIQDVQVVG--VPDEkyg 489
|
....
gi 1907081036 606 -EVM 608
Cdd:PRK08315 490 eEVC 493
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
264-604 |
1.21e-26 |
|
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: 113.56 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 264 PPRPDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSGF-LKVTESQ----------WAptCADVHFSYLplahmfermv 330
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLnyVSQPPArLDVGPGSrvaqvlsiafDA--CIGEIFSTL---------- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 331 qsvvyCHGGRVgFFQGDIRLLSDDMKALrpTIFPVVPRLLNrMYDkifhqaDTSLKRwllefaakrkqaevrsgiirnns 410
Cdd:cd17653 169 -----CNGGTL-VLADPSDPFAHVARTV--DALMSTPSILS-TLS------PQDFPN----------------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 411 iwdelffnkiqaslgghVRMIVTGAAPASPTVLGflRAALGCQVYEGYGQTECTAGCTFT--TPGDWTsgHVGAPLPCNH 488
Cdd:cd17653 211 -----------------LKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTelLPGQPV--TIGKPIPNST 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 489 IKLVDAEELNYwTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLH------TGDIGKWLPEGTLKIIDRKKHIFKL 562
Cdd:cd17653 270 CYILDADLQPV-PEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPgsrmyrTGDYGRWTEDGGLEFLGREDNQVKV 348
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1907081036 563 aQGEYVAPEKIENIYIRSEPVAQ---IYVHGDSLKAFlvgiVVPD 604
Cdd:cd17653 349 -RGFRINLEEIEEVVLQSQPEVTqaaAIVVNGRLVAF----VTPE 388
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
260-610 |
3.08e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 112.78 E-value: 3.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 260 HAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkvtESQWAPTCADVHFSYLPLAHMfermvqsvvycHGG 339
Cdd:PRK07787 120 HRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDAL----AEAWQWTADDVLVHGLPLFHV-----------HGL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 340 RVGFFqGDIRLLSDDMKALRPTIFPVVPRLLNR---------MYDKIfhQADTSLKRwllefaakrkqaevrsgiirnns 410
Cdd:PRK07787 185 VLGVL-GPLRIGNRFVHTGRPTPEAYAQALSEGgtlyfgvptVWSRI--AADPEAAR----------------------- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 411 iwdelffnkiqaSLGGhVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIK 490
Cdd:PRK07787 239 ------------ALRG-ARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 491 LVDaEELNYWTCKGE--GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDR------KKHIFKL 562
Cdd:PRK07787 306 LVD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGGYRI 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1907081036 563 AQGEyvapekIENIYIRSEPVAQIYVHG---DSLKAFLVGIVVPDPEVMPS 610
Cdd:PRK07787 385 GAGE------IETALLGHPGVREAAVVGvpdDDLGQRIVAYVVGADDVAAD 429
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
119-604 |
8.36e-26 |
|
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: 111.23 E-value: 8.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 119 QWLSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTV 198
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARG--VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 199 IVDkphkatlllehverketpglklvilmepfeDALRERGKKCGVDIksMQAIEDCGRENHHAPVPPRPDDLSIVCFTSG 278
Cdd:cd12116 89 LTD------------------------------DALPDRLPAGLPVL--LLALAAAAAAPAAPRTPVSPDDLAYVIYTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 279 TTGNPKGAMLTHGNVVADFSGF------------LKVTesqwaPTCADVhfS----YLPLahmfermvqsvvyCHGGRVG 342
Cdd:cd12116 137 STGRPKGVVVSHRNLVNFLHSMrerlglgpgdrlLAVT-----TYAFDI--SllelLLPL-------------LAGARVV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 343 FFQGDI----RLLSDDMKALRPTIFpvvprllnrmydkifhQADTSLKRWLLEfaakrkqaevrSGiirnnsiWDELffn 418
Cdd:cd12116 197 IAPRETqrdpEALARLIEAHSITVM----------------QATPATWRMLLD-----------AG-------WQGR--- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 419 kiqaslgGHVRMIVTGAApaSPTVLGFLRAALGCQVYEGYGQTECT--AGCTFTTPGDwTSGHVGAPLPCNHIKLVDAEe 496
Cdd:cd12116 240 -------AGLTALCGGEA--LPPDLAARLLSRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLDAA- 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 497 lnywtckGE-------GEICVKGPNVFKGYLKDEDRTKEALDSDGWLH-------TGDIGKWLPEGTLKIIDRKKHIFKL 562
Cdd:cd12116 309 -------LRpvppgvpGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQVKI 381
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1907081036 563 aQGEYVAPEKIENIYIRSEPVAQ--IYVHGDSLKAFLVGIVVPD 604
Cdd:cd12116 382 -RGHRIELGEIEAALAAHPGVAQaaVVVREDGGDRRLVAYVVLK 424
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
111-590 |
1.03e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 111.79 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 111 FRKPEQPY-----QWLSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGS 185
Cdd:PRK07786 28 LMQPDAPAlrflgNTTTWRELDDRVAALAGALSRRG--VGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 186 ISYIINTADiCTVIVDKPHKATLLLEhvERKETPGLKLVILMEP--------FEDALRERGKKcgvdiksmqaiedcgre 257
Cdd:PRK07786 106 IAFLVSDCG-AHVVVTEAALAPVATA--VRDIVPLLSTVVVAGGssddsvlgYEDLLAEAGPA----------------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 258 nhHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEsqwAPTCADVHFSYLPLAHMfeRMVQSVVych 337
Cdd:PRK07786 166 --HAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNG---ADINSDVGFVGVPLFHI--AGIGSML--- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 338 ggrVGFFQGdirllsddmkalRPT-IFPVVPRLLNRMYDKIFHQADTSL----KRWLLEFAAKRKQAevrsgiiRNNSIw 412
Cdd:PRK07786 236 ---PGLLLG------------APTvIYPLGAFDPGQLLDVLEAEKVTGIflvpAQWQAVCAEQQARP-------RDLAL- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 413 delffnkiqaslgghvRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAgCTFTTPGD---WTSGHVGAPLPCNH 488
Cdd:PRK07786 293 ----------------RVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEMSP-VTCMLLGEdaiRKLGSVGKVIPTVA 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 489 IKLVDaEELNYwTCKGE-GEICVKGPNVFKGYLKDEDRTKEALDSdGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEY 567
Cdd:PRK07786 356 ARVVD-ENMND-VPVGEvGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGEN 431
|
490 500
....*....|....*....|...
gi 1907081036 568 VAPEKIENIYIRSEPVAQIYVHG 590
Cdd:PRK07786 432 IYCAEVENVLASHPDIVEVAVIG 454
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
121-598 |
1.80e-25 |
|
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: 109.73 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLLQHDCKVGteQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 200
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKG--DRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 DKphkatlllehverketpglklvilmepfedalrergkkcgvdiksmqaiedcgrenhhapvpprpDDLSIVCFTSGTT 280
Cdd:cd05972 79 DA-----------------------------------------------------------------EDPALIYFTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 281 GNPKGAMLTHG---NVVADFSGFLKVTESQWAPTCADVHFSYLPLAHMFERMVQ--SVVYCHGGRvgffqgdirllsddM 355
Cdd:cd05972 94 GLPKGVLHTHSyplGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLgaTVFVYEGPR--------------F 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 356 KALRptifpvVPRLLNRMYDKIFHQADTSLKRWLLEFAAKRKQaevrsgiirnnsiwdelffnkiqaslgGHVRMIVTGA 435
Cdd:cd05972 160 DAER------ILELLERYGVTSFCGPPTAYRMLIKQDLSSYKF---------------------------SHLRLVVSAG 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 436 APASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAE--ELNYWTckgEGEICVKGP 513
Cdd:cd05972 207 EPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDgrELPPGE---EGDIAIKLP 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 514 NV--FKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSEPVAQIYV--- 588
Cdd:cd05972 284 PPglFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVESALLEHPAVAEAAVvgs 361
|
490
....*....|....
gi 1907081036 589 ----HGDSLKAFLV 598
Cdd:cd05972 362 pdpvRGEVVKAFVV 375
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
112-569 |
8.86e-25 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 109.58 E-value: 8.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 112 RKPEQPYQWLSYQEVAKRAEFLGSGLLqhDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLydtlgpgSISYIIN 191
Cdd:PRK08180 61 RGADGGWRRLTYAEALERVRAIAQALL--DRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPV-------SPAYSLV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 192 TADIctvivDKphkatllLEHVERKETPGLKLVILMEPFEDALRE-----------RGKKCGVDIKSMQAIEDCGR---- 256
Cdd:PRK08180 132 SQDF-----GK-------LRHVLELLTPGLVFADDGAAFARALAAvvpadvevvavRGAVPGRAATPFAALLATPPtaav 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 257 ENHHAPVppRPDDLSIVCFTSGTTGNPKGAMLTHGNVVA------DFSGFLKVTESqwaptcadVHFSYLPLAHMF--ER 328
Cdd:PRK08180 200 DAAHAAV--GPDTIAKFLFTSGSTGLPKAVINTHRMLCAnqqmlaQTFPFLAEEPP--------VLVDWLPWNHTFggNH 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 329 MVQSVVYcHGGR---------VGFFQGDIRLLsddmKALRPTIFPVVPRLlnrmydkifhqadtslkrWLLEFAAKRKQA 399
Cdd:PRK08180 270 NLGIVLY-NGGTlyiddgkptPGGFDETLRNL----REISPTVYFNVPKG------------------WEMLVPALERDA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 400 EVRsgiirnnsiwdELFFNKiqaslgghVRMIVTGAAPASPTVLGFL----RAALGCQVY--EGYGQTECTAGCTFTTPG 473
Cdd:PRK08180 327 ALR-----------RRFFSR--------LKLLFYAGAALSQDVWDRLdrvaEATCGERIRmmTGLGMTETAPSATFTTGP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 474 DWTSGHVGAPLPCNHIKLVDAEelnywtckGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWL----PEGT 549
Cdd:PRK08180 388 LSRAGNIGLPAPGCEVKLVPVG--------GKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVdpadPERG 459
|
490 500
....*....|....*....|
gi 1907081036 550 LKIIDRKKHIFKLAQGEYVA 569
Cdd:PRK08180 460 LMFDGRIAEDFKLSSGTWVS 479
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
269-606 |
1.36e-24 |
|
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: 105.43 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 269 DLSIVCFTSGTTGNPKGAMLTHGNVVA---DFSGFLKVTEsqwaptcADVHFSYLPLAHMFERMVQSVVYCHGGR-VGFF 344
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAanlQLIHAMGLTE-------ADVYLNMLPLFHIAGLNLALATFHAGGAnVVME 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 345 QGDIRLLSDDMKALRPTIFPVVPRLLNRMYDkifhqadtslkrwllefAAKRKQAEVRSgiIRNnsiwdelffnkiqasl 424
Cdd:cd17637 74 KFDPAEALELIEEEKVTLMGSFPPILSNLLD-----------------AAEKSGVDLSS--LRH---------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 425 gghvrmiVTGAApaSPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDaeELNYWTCKG 504
Cdd:cd17637 119 -------VLGLD--APETIQRFEETTGATFWSLYGQTE-TSGLVTLSPYRERPGSAGRPGPLVRVRIVD--DNDRPVPAG 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 505 E-GEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRK--KHIFKlAQGEYVAPEKIENIYIRSE 581
Cdd:cd17637 187 EtGEIVVRGPLVFQGYWNLPELTAYTFR-NGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKVILEHP 264
|
330 340
....*....|....*....|....*
gi 1907081036 582 PVAQIYVHGdslkaflvgivVPDPE 606
Cdd:cd17637 265 AIAEVCVIG-----------VPDPK 278
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
112-606 |
8.33e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 106.28 E-value: 8.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 112 RKPEQP----Y-QWLSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSI 186
Cdd:PRK06178 45 ERPQRPaiifYgHVITYAELDELSDRFAALLRQRG--VGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 187 SYIINTADICTVIV-D------KPHKATLLLEHVErkeTPGLKLVILMEP---FEDALRERGKKCGVDIKSMQAIEDCGR 256
Cdd:PRK06178 123 SYELNDAGAEVLLAlDqlapvvEQVRAETSLRHVI---VTSLADVLPAEPtlpLPDSLRAPRLAAAGAIDLLPALRACTA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 257 ENhhAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPtcaDVHFSYLPlahMFermvqsvvyc 336
Cdd:PRK06178 200 PV--PLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGED---SVFLSFLP---EF---------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 337 hggrvgFFQGDirllsdDMKALRPTIF--PVVprLLNRmYDkifhqADTSLKrwllefAAKRKQAEVRSGIIRNnsiWDE 414
Cdd:PRK06178 262 ------WIAGE------NFGLLFPLFSgaTLV--LLAR-WD-----AVAFMA------AVERYRVTRTVMLVDN---AVE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 415 LF----FNKIQASLGGHVRmIVTGAAPASPTVLGFLRAALGCQVYEG-YGQTECTAGCTFTTpGDWTSGH--------VG 481
Cdd:PRK06178 313 LMdhprFAEYDLSSLRQVR-VVSFVKKLNPDYRQRWRALTGSVLAEAaWGMTETHTCDTFTA-GFQDDDFdllsqpvfVG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 482 APLPCNHIKLVDAEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFK 561
Cdd:PRK06178 391 LPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLK 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1907081036 562 LaQGEYVAPEKIENIYIRsepvaqiyvHGDSLKAFLVGivVPDPE 606
Cdd:PRK06178 470 V-NGMSVFPSEVEALLGQ---------HPAVLGSAVVG--RPDPD 502
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-584 |
9.35e-24 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 103.33 E-value: 9.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsGFLKVTESQWAPTcaDVHFSYLPLAHMFERMVQsvvychgGRVGFFQG 346
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYN--AWMLALNSLFDPD--DVLLCGLPLFHVNGSVVT-------LLTPLASG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 347 DIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTSLkrwllefaAKRKQAEVRSGIirnnsiwdelffnkiqaslgG 426
Cdd:cd05944 70 AHVVLAGPAGYRNPGLFDNFWKLVERYRITSLSTVPTVY--------AALLQVPVNADI--------------------S 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 427 HVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLV--DAEELNYWTCK 503
Cdd:cd05944 122 SLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKvlDGVGRLLRDCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 504 GE--GEICVKGPNVFKGYLKDEDRtKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSE 581
Cdd:cd05944 202 PDevGEICVAGPGVFGGYLYTEGN-KNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLRHP 279
|
...
gi 1907081036 582 PVA 584
Cdd:cd05944 280 AVA 282
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
162-574 |
9.56e-24 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 107.32 E-value: 9.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 162 IAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIVDKPhkatlLLEHVERK----ETPGLKLVILMEPFEDALRER 237
Cdd:PRK08633 680 LANLALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVITSRK-----FLEKLKNKgfdlELPENVKVIYLEDLKAKISKV 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 238 GKKC-GVDIKSMQA--IEDCGRENHHapvpprPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD---FSGFLKVTESqwapt 311
Cdd:PRK08633 755 DKLTaLLAARLLPArlLKRLYGPTFK------PDDTATIIFSSGSEGEPKGVMLSHHNILSNieqISDVFNLRND----- 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 312 caDVHFSYLPLAHMFERMV-QSVVYCHGGRVGFFqgdirllSDDMKAL---------RPTIFPVVPRLLnRMYdkifhqa 381
Cdd:PRK08633 824 --DVILSSLPFFHSFGLTVtLWLPLLEGIKVVYH-------PDPTDALgiaklvakhRATILLGTPTFL-RLY------- 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 382 dtslkrwllefaakrkqaevrsgiIRNNSIWDELFfnkiqASLgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQT 461
Cdd:PRK08633 887 ------------------------LRNKKLHPLMF-----ASL----RLVVAGAEKLKPEVADAFEEKFGIRILEGYGAT 933
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 462 ECTAGCTFTTP-----GDWT-----SGHVGAPLPCNHIKLVDAEelNYWTCKG--EGEICVKGPNVFKGYLKDEDRTKEA 529
Cdd:PRK08633 934 ETSPVASVNLPdvlaaDFKRqtgskEGSVGMPLPGVAVRIVDPE--TFEELPPgeDGLILIGGPQVMKGYLGDPEKTAEV 1011
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1907081036 530 L---DSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIE 574
Cdd:PRK08633 1012 IkdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIG-GEMVPLGAVE 1058
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
111-588 |
9.90e-24 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 105.10 E-value: 9.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 111 FRKPEQPY-----QWLSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLydtlGPGS 185
Cdd:cd17655 8 EKTPDHTAvvfedQTLTYRELNERANQLARTLREKG--VGPDTIVGIMAERSLEMIVGILGILKAGGAYLPI----DPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 186 ----ISYIINTADictvivdkphkATLLL--EHVERKETpGLKLVILMEpfEDALRERGKkcgvdiksmqaiedcgrENH 259
Cdd:cd17655 82 peerIQYILEDSG-----------ADILLtqSHLQPPIA-FIGLIDLLD--EDTIYHEES-----------------ENL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 260 HAPVppRPDDLSIVCFTSGTTGNPKGAMLTHGNVVadfsgflkvtesqwaptcadvhfsylplaHMFERMVQSVVYCHGG 339
Cdd:cd17655 131 EPVS--KSDDLAYVIYTSGSTGKPKGVMIEHRGVV-----------------------------NLVEWANKVIYQGEHL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 340 RVGFFQGdirlLSDDMkalrpTIFPVVPRLL--NRMYdkIFHQADTSLKRWLLEFAAKRkqaevRSGIIR-NNSIWDELf 416
Cdd:cd17655 180 RVALFAS----ISFDA-----SVTEIFASLLsgNTLY--IVRKETVLDGQALTQYIRQN-----RITIIDlTPAHLKLL- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 417 fNKIQASLGGHVRMIVTGAAPASPTVLGFL--RAALGCQVYEGYGQTECTAGCTF--TTPGDWTSGHV--GAPLPCNHIK 490
Cdd:cd17655 243 -DAADDSEGLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETTVDASIyqYEPETDQQVSVpiGKPLGNTRIY 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 491 LVDaEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWL------HTGDIGKWLPEGTLKIIDRKKHIFKLaQ 564
Cdd:cd17655 322 ILD-QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-R 399
|
490 500
....*....|....*....|....
gi 1907081036 565 GEYVAPEKIENIYIRSEPVAQIYV 588
Cdd:cd17655 400 GYRIELGEIEARLLQHPDIKEAVV 423
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
120-557 |
1.47e-23 |
|
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: 105.40 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 120 WLSYQEVAKRAEFLGSGLLQHdCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGS---ISYIINTADIC 196
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAV-GKPGDR--VLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 197 TVIVDKPHKAtLLLEHVERKETPGLKLVILMEPFEDALRERGkkcgvdiksmqaiedcgrenhhAPVPPRPDDLSIVCFT 276
Cdd:cd05931 101 VVLTTAAALA-AVRAFAASRPAAGTPRLLVVDLLPDTSAADW----------------------PPPSPDPDDIAYLQYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 277 SGTTGNPKGAMLTHGNVVADFSGFLKvtesQWAPTCADVHFSYLPLAH-MfermvqsvvychgGRVG------FFQGDIR 349
Cdd:cd05931 158 SGSTGTPKGVVVTHRNLLANVRQIRR----AYGLDPGDVVVSWLPLYHdM-------------GLIGglltplYSGGPSV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 350 LLSddmkalrPTIFpvvprlLNRMYdkifhqadtslkRWL-----------------LEFAAKRKQAEVRSGIirnnsiw 412
Cdd:cd05931 221 LMS-------PAAF------LRRPL------------RWLrlisryratisaapnfaYDLCVRRVRDEDLEGL------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 413 dELffnkiqaslgGHVRMIVTGAAPASPTVL----------GFLRAAlgcqVYEGYGQTECTAGCTFTTPG--------- 473
Cdd:cd05931 269 -DL----------SSWRVALNGAEPVRPATLrrfaeafapfGFRPEA----FRPSYGLAEATLFVSGGPPGtgpvvlrvd 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 474 -DWTSGHV----------------GAPLPCNHIKLVDAEelnywTCK-----GEGEICVKGPNVFKGYLKDEDRTKE--- 528
Cdd:cd05931 334 rDALAGRAvavaaddpaarelvscGRPLPDQEVRIVDPE-----TGRelpdgEVGEIWVRGPSVASGYWGRPEATAEtfg 408
|
490 500 510
....*....|....*....|....*....|..
gi 1907081036 529 ---ALDSDGWLHTGDIGkWLPEGTLKIIDRKK 557
Cdd:cd05931 409 alaATDEGGWLRTGDLG-FLHDGELYITGRLK 439
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
263-598 |
1.95e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 105.12 E-value: 1.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 263 VPPRPD-DLSIVCFTSGTTGNPKGAMLTHGNVVADfsgflKVTESQWAPTCAD---VHFSYLPLAHMF-ERMVQSVVYCH 337
Cdd:PRK06710 200 VPCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSN-----TLMGVQWLYNCKEgeeVVLGVLPFFHVYgMTAVMNLSIMQ 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 338 GGRVGFF-QGDIRLLSDDMKALRPTIFPVVPRLLNRMydkifhqadtsLKRWLLefaakrKQAEVRSgiirnnsiwdelf 416
Cdd:PRK06710 275 GYKMVLIpKFDMKMVFEAIKKHKVTLFPGAPTIYIAL-----------LNSPLL------KEYDISS------------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 417 fnkiqaslgghVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgctfTTPGDW-----TSGHVGAPLPCNHIKL 491
Cdd:PRK06710 325 -----------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSP----VTHSNFlwekrVPGSIGVPWPDTEAMI 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 492 VDAEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPE 571
Cdd:PRK06710 390 MSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPR 467
|
330 340 350
....*....|....*....|....*....|....
gi 1907081036 572 KIENIYIRSEPVAQIYV-------HGDSLKAFLV 598
Cdd:PRK06710 468 EVEEVLYEHEKVQEVVTigvpdpyRGETVKAFVV 501
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
269-685 |
3.15e-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: 101.25 E-value: 3.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 269 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkvTESQWAPTCADVHFSYLPLAHM--FERMVQSVVycHGGRVGFFQG 346
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAG----LHSRLGFGGGDSWLLSLPLYHVggLAILVRSLL--AGAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 347 DiRLLSDDMKALRPTIFPVVPRLLNRMYDKifHQADTSLKRwllefaakrkqaevrsgiirnnsiwdelffnkiqaslgg 426
Cdd:cd17630 75 N-QALAEDLAPPGVTHVSLVPTQLQRLLDS--GQGPAALKS--------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 427 hVRMIVTGAAPASPtvlGFLRAA--LGCQVYEGYGQTEcTAGCTFT-TPGDWTSGHVGAPLPCNHIKLVDaeelnywtck 503
Cdd:cd17630 113 -LRAVLLGGAPIPP---ELLERAadRGIPLYTTYGMTE-TASQVATkRPDGFGRGGVGVLLPGRELRIVE---------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 504 gEGEICVKGPNVFKGYLKDedRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIEniyirsepv 583
Cdd:cd17630 178 -DGEIWVGGASLAMGYLRG--QLVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIE--------- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 584 AQIYVHGDSLKAFLVGivVPDPEV--MPSWAQKKGIEGTYQEL--CMKKELKKailddmvmlgkesglhsFEQVKAIYIh 659
Cdd:cd17630 245 AALAAHPAVRDAFVVG--VPDEELgqRPVAVIVGRGPADPAELraWLKDKLAR-----------------FKLPKRIYP- 304
|
410 420
....*....|....*....|....*.
gi 1907081036 660 cdmfsVQNGLLTPTLKAKRPELREYF 685
Cdd:cd17630 305 -----VPELPRTGGGKVDRRALRAWL 325
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
121-605 |
7.50e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 102.70 E-value: 7.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 200
Cdd:PRK08316 37 WTYAELDAAVNRVAAALLDLGLKKGDR--VAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 DkphkaTLLLEHVERKETPGLKLVILMEPFEDaLRERGKKCgVDIKSMQAIEDcgreNHHAPVPPRPDDLSIVCFTSGTT 280
Cdd:PRK08316 115 D-----PALAPTAEAALALLPVDTLILSLVLG-GREAPGGW-LDFADWAEAGS----VAEPDVELADDDLAQILYTSGTE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 281 GNPKGAMLTHGNVVADFSGflKVTESQWAPTCADVHfsYLPLAHMFERMV--QSVVYCHGGRVGFFQGDIRLLSDDMKAL 358
Cdd:PRK08316 184 SLPKGAMLTHRALIAEYVS--CIVAGDMSADDIPLH--ALPLYHCAQLDVflGPYLYVGATNVILDAPDPELILRTIEAE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 359 RPTIF---PVVPRLLNRMYDkiFHQADTSlkrwllefaakrkqaevrsgiirnnsiwdelffnkiqaSLgghvRMIVTGA 435
Cdd:PRK08316 260 RITSFfapPTVWISLLRHPD--FDTRDLS--------------------------------------SL----RKGYYGA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 436 APASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFTTPGDwtsgHVGAP----LPCNHI--KLVDA--EELnywtCKGE- 505
Cdd:PRK08316 296 SIMPVEVLKELRERLpGLRFYNCYGQTEIAPLATVLGPEE----HLRRPgsagRPVLNVetRVVDDdgNDV----APGEv 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 506 GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIyirsepvaq 585
Cdd:PRK08316 368 GEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEA--------- 436
|
490 500
....*....|....*....|
gi 1907081036 586 IYVHGDSLKAFLVGivVPDP 605
Cdd:PRK08316 437 LYTHPAVAEVAVIG--LPDP 454
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
266-606 |
8.59e-23 |
|
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: 102.24 E-value: 8.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 266 RPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKV----TESQWaptcadVHFSylplAHMFERMVQSVVY--CHGG 339
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRAlgltSESRV------LQFA----SYTFDVSILEIFTtlAAGG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 340 ---------RVGFFQGDIRllsdDMKA----LRPTifpvVPRLLNRmydkifhqadtslkrwllefaakrkqAEVRSgii 406
Cdd:cd05918 174 clcipseedRLNDLAGFIN----RLRVtwafLTPS----VARLLDP--------------------------EDVPS--- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 407 rnnsiwdelffnkiqaslgghVRMIVTGAAPASPTVLGflRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLP 485
Cdd:cd05918 217 ---------------------LRTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRPLG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 486 C--------NHIKLVDaeelnywtcKGE-GEICVKGPNVFKGYLKDEDRTKEA-LDSDGWLH------------TGDIGK 543
Cdd:cd05918 274 AtcwvvdpdNHDRLVP---------IGAvGELLIEGPILARGYLNDPEKTAAAfIEDPAWLKqegsgrgrrlyrTGDLVR 344
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081036 544 WLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEP-----VAQIYVH-GDSLKAFLVGIVVPDPE 606
Cdd:cd05918 345 YNPDGSLEYVGRKDTQVKI-RGQRVELGEIEHHLRQSLPgakevVVEVVKPkDGSSSPQLVAFVVLDGS 412
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
121-605 |
1.04e-22 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 102.44 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLLqhDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 200
Cdd:PRK13295 56 FTYRELAALVDRVAVGLA--RLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 -------DKPHKATLLlehveRKETPGLKLVILM-----EPFEDALRERGKKCGVDIksmQAIEDCGRenhhapvpPRPD 268
Cdd:PRK13295 134 pktfrgfDHAAMARRL-----RPELPALRHVVVVggdgaDSFEALLITPAWEQEPDA---PAILARLR--------PGPD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 269 DLSIVCFTSGTTGNPKGAMLTHGNVVAD---FSGFLKVTESqwaptcaDVHFSYLPLAH----MFERMV-----QSVVYc 336
Cdd:PRK13295 198 DVTQLIYTSGTTGEPKGVMHTANTLMANivpYAERLGLGAD-------DVILMASPMAHqtgfMYGLMMpvmlgATAVL- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 337 hggrvgffqGDIRllsDDMKALRptifpvvprlLNRMYDKIFHQADTSlkrWLLEFAakRKQAEVRSGIirnnsiwdelf 416
Cdd:PRK13295 270 ---------QDIW---DPARAAE----------LIRTEGVTFTMASTP---FLTDLT--RAVKESGRPV----------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 417 fnkiqASLgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPGD---WTSGHVGAPLPCNHIKLVD 493
Cdd:PRK13295 312 -----SSL----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA-VTLTKLDDpdeRASTTDGCPLPGVEVRVVD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 494 AE--ELNYWTckgEGEICVKGPNVFKGYLKDEDRTkeALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPE 571
Cdd:PRK13295 382 ADgaPLPAGQ---IGRLQVRGCSNFGGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVV 455
|
490 500 510
....*....|....*....|....*....|....*
gi 1907081036 572 KIENIYIRSEPVAQiyvhgdslkaflVGIV-VPDP 605
Cdd:PRK13295 456 EIEALLYRHPAIAQ------------VAIVaYPDE 478
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
150-598 |
3.60e-22 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 100.53 E-value: 3.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 150 VGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIVDKphKATLLLEHVERKETPGLKLVILMEP 229
Cdd:PRK08008 65 VALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSA--QFYPMYRQIQQEDATPLRHICLTRV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 230 FEDAlrERGKKCGVDIKSMQAIEDCgrenhHAPvPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLkvTESQWA 309
Cdd:PRK08008 143 ALPA--DDGVSSFTQLKAQQPATLC-----YAP-PLSTDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYY--SAWQCA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 310 PTCADVHFSYLPLAHMFermvqsvvychggrvgfFQgdirlLSDDMKAlrptiFPVVPRLLnrmydkifhqadtslkrwL 389
Cdd:PRK08008 211 LRDDDVYLTVMPAFHID-----------------CQ-----CTAAMAA-----FSAGATFV------------------L 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 390 LE-FAAKRKQAEVRsgiirnnsiwdelffnKIQASLGGHVRMIVTG--AAPASPT--------VLGFLRAA--------- 449
Cdd:PRK08008 246 LEkYSARAFWGQVC----------------KYRATITECIPMMIRTlmVQPPSANdrqhclreVMFYLNLSdqekdafee 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 450 -LGCQVYEGYGQTECTAGCTFTTPGD---WTSghVGAPLPCNHIKLVDAEelNYWTCKGE-GEICVKG---PNVFKGYLK 521
Cdd:PRK08008 310 rFGVRLLTSYGMTETIVGIIGDRPGDkrrWPS--IGRPGFCYEAEIRDDH--NRPLPAGEiGEICIKGvpgKTIFKEYYL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 522 DEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIyIRSEP-VAQIYVHG--DSL----- 593
Cdd:PRK08008 386 DPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVELENI-IATHPkIQDIVVVGikDSIrdeai 463
|
....*
gi 1907081036 594 KAFLV 598
Cdd:PRK08008 464 KAFVV 468
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
267-639 |
8.95e-22 |
|
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: 98.86 E-value: 8.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgFLKVTESQWAPTCADVHFSYLPLAhmFERMVQSVVYC--HGGrvgff 344
Cdd:cd05945 96 GDDNAYIIFTSGSTGRPKGVQISHDNLVS----FTNWMLSDFPLGPGDVFLNQAPFS--FDLSVMDLYPAlaSGA----- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 345 qgdirllsddmkalrpTIFPVvPRLLNRMYdkifhqadtslkRWLLEFAAKRKQAEVRSgiirNNSIWDELF----FNki 420
Cdd:cd05945 165 ----------------TLVPV-PRDATADP------------KQLFRFLAEHGITVWVS----TPSFAAMCLlsptFT-- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 421 QASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFT--TP---GDWTSGHVGAPLPCNHIKLVDaE 495
Cdd:cd05945 210 PESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIevTPevlDGYDRLPIGYAKPGAKLVILD-E 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 496 ELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSD---GWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEK 572
Cdd:cd05945 289 DGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIELEE 367
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081036 573 IENIYIRSEPVAQIYV----HGDSlKAFLVGIVVPDPEVMPswAQKKGIegtyqelcmKKELKKAILDDMV 639
Cdd:cd05945 368 IEAALRQVPGVKEAVVvpkyKGEK-VTELIAFVVPKPGAEA--GLTKAI---------KAELAERLPPYMI 426
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
121-576 |
1.22e-21 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 100.43 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGsGLLQHDCKVGteQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 200
Cdd:PRK06814 659 LTYRKLLTGAFVLG-RKLKKNTPPG--ENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 DKP--HKATL--LLEHVERketpGLKLVILmEPFEDALRERGKKCGVDIKSMQAIEDCGRenhhapvppRPDDLSIVCFT 276
Cdd:PRK06814 736 SRAfiEKARLgpLIEALEF----GIRIIYL-EDVRAQIGLADKIKGLLAGRFPLVYFCNR---------DPDDPAVILFT 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 277 SGTTGNPKGAMLTHGNVVA---------DFSGflkvtesqwaptcADVHFSYLPLAHMFermvqsvvychggrvGFFQGD 347
Cdd:PRK06814 802 SGSEGTPKGVVLSHRNLLAnraqvaariDFSP-------------EDKVFNALPVFHSF---------------GLTGGL 853
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 348 IRLLSDDMKAL---RPTIFPVVPRLLnrmYD---KIFHQADTSLkrwllefaakrkqaevrSGIIRNNSIWDelFFNkiq 421
Cdd:PRK06814 854 VLPLLSGVKVFlypSPLHYRIIPELI---YDtnaTILFGTDTFL-----------------NGYARYAHPYD--FRS--- 908
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 422 aslgghVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNywt 501
Cdd:PRK06814 909 ------LRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGID--- 979
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081036 502 cKGeGEICVKGPNVFKGYLKDED-RTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENI 576
Cdd:PRK06814 980 -EG-GRLFVRGPNVMLGYLRAENpGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAVEEL 1051
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
118-605 |
1.68e-21 |
|
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: 98.72 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 118 YQWLSYQeVAKRAEFLGSgllqhdCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICT 197
Cdd:cd05970 50 FAELADY-SDKTANFFKA------MGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 198 VIVDKphkATLLLEHVE--RKETPGLKLVI-----LMEPFEDaLRERGKKCGVDIksmqaiedcgrENHHAPVPPRPDDL 270
Cdd:cd05970 123 IVAIA---EDNIPEEIEkaAPECPSKPKLVwvgdpVPEGWID-FRKLIKNASPDF-----------ERPTANSYPCGEDI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 271 SIVCFTSGTTGNPKgaMLTHGNV--------------VADFSGFLKVTESQWAPTC-ADVHFSYLPLAHMFermvqsvVY 335
Cdd:cd05970 188 LLVYFSSGTTGMPK--MVEHDFTyplghivtakywqnVREGGLHLTVADTGWGKAVwGKIYGQWIAGAAVF-------VY 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 336 CHGgrvgffQGDIRLLSDDMKALRPTIF---PVVPRLLNRmydkifhqadTSLKRWLLefaakrkqaevrSGIirnnsiw 412
Cdd:cd05970 259 DYD------KFDPKALLEKLSKYGVTTFcapPTIYRFLIR----------EDLSRYDL------------SSL------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 413 delffnkiqaslgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPG-DWTSGHVGAPLPCNHIKL 491
Cdd:cd05970 304 ----------------RYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTL-TIATFPWmEPKPGSMGKPAPGYEIDL 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 492 VDAEELnywTCKG--EGEICV---KGPNV--FKGYLKDEDRTKEALdSDGWLHTGDIGkWLPE-GTLKIIDRKKHIFKlA 563
Cdd:cd05970 367 IDREGR---SCEAgeEGEIVIrtsKGKPVglFGGYYKDAEKTAEVW-HDGYYHTGDAA-WMDEdGYLWFVGRTDDLIK-S 440
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1907081036 564 QGEYVAPEKIENIYIRSEPVAQIYVHGdslkaflvgivVPDP 605
Cdd:cd05970 441 SGYRIGPFEVESALIQHPAVLECAVTG-----------VPDP 471
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
107-605 |
1.93e-21 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 98.66 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 107 PCLGFRKPEQPYQWLSYQEVAKRAEFLGSGLLQHDCKVgtEQFVGVFAQNRPEWIIAELACYTysmVVVPLydtlGPGSI 186
Cdd:cd05921 12 TWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGLSA--ERPLLILSGNSIEHALMALAAMY---AGVPA----APVSP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 187 SYIINTADIctvivDKphkatllLEHVERKETPGLKLVILMEPFEDALRERgKKCGVDIKSMQAIEDCGRENHHAPV--- 263
Cdd:cd05921 83 AYSLMSQDL-----AK-------LKHLFELLKPGLVFAQDAAPFARALAAI-FPLGTPLVVSRNAVAGRGAISFAELaat 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 264 PPR-----------PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWA------PTCADvhfsYLPLAHMF 326
Cdd:cd05921 150 PPTaavdaafaavgPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQT----YPffgeepPVLVD----WLPWNHTF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 327 --ERMVQSVVYcHGGRV---------GFFQGDIRLLSDDMkalrPTIFPVVPR----LLNRMYDkifhqaDTSLKRwllE 391
Cdd:cd05921 222 ggNHNFNLVLY-NGGTLyiddgkpmpGGFEETLRNLREIS----PTVYFNVPAgwemLVAALEK------DEALRR---R 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 392 FAAKRKQAEVrSGIIRNNSIWDELFFNKIQaSLGGHVRMivtgaapasptvlgflraalgcqvYEGYGQTECTAGCTFTT 471
Cdd:cd05921 288 FFKRLKLMFY-AGAGLSQDVWDRLQALAVA-TVGERIPM------------------------MAGLGATETAPTATFTH 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 472 PGDWTSGHVGAPLPCNHIKLVdaeelnywTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWL----PE 547
Cdd:cd05921 342 WPTERSGLIGLPAPGTELKLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpddPA 413
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081036 548 GTLKIIDRKKHIFKLAQGEYVA--PekieniyIRSEPVAQI--YVHgDSL-----KAFLVGIVVPDP 605
Cdd:cd05921 414 KGLVFDGRVAEDFKLASGTWVSvgP-------LRARAVAACapLVH-DAVvagedRAEVGALVFPDL 472
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
220-574 |
4.06e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 97.76 E-value: 4.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 220 GLKLVILMEPFEDA---LRERGKKcgvdiksMQAIEDCGRENHHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD 296
Cdd:PRK07768 108 GAKAVVVGEPFLAAapvLEEKGIR-------VLTVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYAN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 297 FSGFlkVTESQWAPTcADVHFSYLPLAH-MfermvqsvvychgGRVGFfqgdirlLSDDMKA------LRPTIFPVVPRL 369
Cdd:PRK07768 181 AEAM--FVAAEFDVE-TDVMVSWLPLFHdM-------------GMVGF-------LTVPMYFgaelvkVTPMDFLRDPLL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 370 LNRMYDKifHQADT--------SLKRWLLEFAAKRKQAEVRSgiirnnsiwdelffnkiqaslgghVRMIVTGAAPASPT 441
Cdd:PRK07768 238 WAELISK--YRGTMtaapnfayALLARRLRRQAKPGAFDLSS------------------------LRFALNGAEPIDPA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 442 VL----------GFLRAALGCqvyeGYGQTECTAGCTFTTPGD--------------------WTSGHV------GAPLP 485
Cdd:PRK07768 292 DVedlldagarfGLRPEAILP----AYGMAEATLAVSFSPCGAglvvdevdadllaalrravpATKGNTrrlatlGPPLP 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 486 CNHIKLVDaEELNYWTCKGEGEICVKGPNVFKGYLkDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqG 565
Cdd:PRK07768 368 GLEVRVVD-EDGQVLPPRGVGVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-G 444
|
....*....
gi 1907081036 566 EYVAPEKIE 574
Cdd:PRK07768 445 RNIYPTDIE 453
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
112-605 |
4.59e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 97.26 E-value: 4.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 112 RKPEQPY-----QWLSYQEVAKRAEfLGSGLLqHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSI 186
Cdd:PRK06145 14 RTPDRAAlvyrdQEISYAEFHQRIL-QAAGML-HARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 187 SYIINTADICTVIVDKPHKATLLLEHverketpglKLVILMEPFEDALRERGKKcgvdiksmqaiedcgrenhHAPVPP- 265
Cdd:PRK06145 92 AYILGDAGAKLLLVDEEFDAIVALET---------PKIVIDAAAQADSRRLAQG-------------------GLEIPPq 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 266 ---RPDDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTESqwaptcaDVHFSYLPLAHMFERMVQSV-VYCHG 338
Cdd:PRK06145 144 aavAPTDLVRLMYTSGTTDRPKGVMHSYGNLHwksIDHVIALGLTAS-------ERLLVVGPLYHVGAFDLPGIaVLWVG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 339 GRVGF---FQGDIRLLSDDMKALRPTIFpvVPRLLNRMY---DKifHQADTSLKRWLLefAAKRKQAEVRsgiIRNnsiw 412
Cdd:PRK06145 217 GTLRIhreFDPEAVLAAIERHRLTCAWM--APVMLSRVLtvpDR--DRFDLDSLAWCI--GGGEKTPESR---IRD---- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 413 delffnkiqaslgghvrmivtgaapasptvlgFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPcnHIK 490
Cdd:PRK06145 284 --------------------------------FTRVFTRARYIDAYGLTETCSGDTLMEAGREIEkiGSTGRALA--HVE 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 491 LVDAEELNYWTCKG-EGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVA 569
Cdd:PRK06145 330 IRIADGAGRWLPPNmKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIA 407
|
490 500 510
....*....|....*....|....*....|....*....
gi 1907081036 570 PEKIEN-IYIRSE--PVAQIYVHGDSLKAFLVGIVVPDP 605
Cdd:PRK06145 408 SSEVERvIYELPEvaEAAVIGVHDDRWGERITAVVVLNP 446
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
121-609 |
1.75e-20 |
|
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: 95.03 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLlqHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 200
Cdd:cd12114 13 LTYGELAERARRVAGAL--KAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 DKPHkatlLLEHVERKETPGLKLVilmepFEDALRERgkkcgvdiksmqaiedcgrenhhAPVPPRPDDLSIVCFTSGTT 280
Cdd:cd12114 91 DGPD----AQLDVAVFDVLILDLD-----ALAAPAPP-----------------------PPVDVAPDDLAYVIFTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 281 GNPKGAMLTHG---NVVADfsgflkvTESQWAPTCADVHFSYLPLAHMFermvqSV-----VYCHGGRVgffqgdirlls 352
Cdd:cd12114 139 GTPKGVMISHRaalNTILD-------INRRFAVGPDDRVLALSSLSFDL-----SVydifgALSAGATL----------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 353 ddmkalrptifpVVPRllnrmydkifHQADTSLKRWllefaakrKQAEVRSGIirnnSIWdelffNKIQASLGghvrMIV 432
Cdd:cd12114 196 ------------VLPD----------EARRRDPAHW--------AELIERHGV----TLW-----NSVPALLE----MLL 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 433 TgAAPASPTVLGFLRAAL-------------------GCQVYEGYGQTECTAGCTF----TTPGDWTSGHVGAPLPCNHI 489
Cdd:cd12114 233 D-VLEAAQALLPSLRLVLlsgdwipldlparlralapDARLISLGGATEASIWSIYhpidEVPPDWRSIPYGRPLANQRY 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 490 KLVDA--EELNYWTckgEGEICVKGPNVFKGYLKDEDRTKEAL--DSDG--WLHTGDIGKWLPEGTLKIIDRKKHIFKLa 563
Cdd:cd12114 312 RVLDPrgRDCPDWV---PGELWIGGRGVALGYLGDPELTAARFvtHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKV- 387
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1907081036 564 QGEYVAPEKIENIYIRSEPVAQ--IYVHGDSLKAFLVGIVVPDPEVMP 609
Cdd:cd12114 388 RGYRIELGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPDNDGTP 435
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
121-610 |
3.62e-20 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 94.57 E-value: 3.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLLQHDCKVGteQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 200
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGLLPG--DRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 DKphkatlllehverkETPGLKLVILMEPFEDALReRGKKCGVDIKSMQAIEDCGRENHHAPVPP---RPDDLSIVcFTS 277
Cdd:PRK05852 122 DA--------------DGPHDRAEPTTRWWPLTVN-VGGDSGPSGGTLSVHLDAATEPTPATSTPeglRPDDAMIM-FTG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 278 GTTGNPKGAMLTHGNVVADFSGFlkVTESQWAPTCADVhfSYLPLAH---MFERMVQSVVycHGGRV-----GFFQGdiR 349
Cdd:PRK05852 186 GTTGLPKMVPWTHANIASSVRAI--ITGYRLSPRDATV--AVMPLYHghgLIAALLATLA--SGGAVllparGRFSA--H 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 350 LLSDDMKALRPTIFPVVPRLlnrmydkifHQAdtslkrwLLEFAAKRKQAEVRSGIirnnsiwdelffnkiqaslgghvR 429
Cdd:PRK05852 258 TFWDDIKAVGATWYTAVPTI---------HQI-------LLERAATEPSGRKPAAL-----------------------R 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 430 MIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTfTTPGDWtSGHVGAPLPCN---------HIKLV--DAEELn 498
Cdd:PRK05852 299 FIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVT-TTQIEG-IGQTENPVVSTglvgrstgaQIRIVgsDGLPL- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 499 ywTCKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYI 578
Cdd:PRK05852 376 --PAGAVGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLA 451
|
490 500 510
....*....|....*....|....*....|....*
gi 1907081036 579 RSEPVAQIYVHGDSLKAF---LVGIVVPDPEVMPS 610
Cdd:PRK05852 452 SHPNVMEAAVFGVPDQLYgeaVAAVIVPRESAPPT 486
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
249-610 |
3.95e-20 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 93.68 E-value: 3.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 249 QAIEDCGRENHHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSG--FLKVTESqwaptcaDVHFSylpLAH 324
Cdd:cd05919 72 DDYAYIARDCEARLVVTSADDIAYLLYSSGTTGPPKGVMHAHRDPLlfADAMAreALGLTPG-------DRVFS---SAK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 325 MFermvqsVVYCHGGRVGF--FQGDIRLLSDD----------MKALRPTIFPVVPRllnrMYDKIFHQADTSlkrwllef 392
Cdd:cd05919 142 MF------FGYGLGNSLWFplAVGASAVLNPGwptaervlatLARFRPTVLYGVPT----FYANLLDSCAGS-------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 393 aakrkQAEVRSgiIRnnsiwdelffnkiqaslgghvrmIVTGAAPASPTVLG-FLRAALGCQVYEGYGQTEctAGCTFTT 471
Cdd:cd05919 204 -----PDALRS--LR-----------------------LCVSAGEALPRGLGeRWMEHFGGPILDGIGATE--VGHIFLS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 472 --PGDWTSGHVGAPLPCNHIKLVDaEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGT 549
Cdd:cd05919 252 nrPGAWRLGSTGRPVPGYEIRLVD-EEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGW 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081036 550 LKIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQIYV----HGDSL---KAFlvgiVVPDPEVMPS 610
Cdd:cd05919 330 YTHAGRADDMLKVG-GQWVSPVEVESLIIQHPAVAEAAVvavpESTGLsrlTAF----VVLKSPAAPQ 392
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
120-624 |
1.27e-19 |
|
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: 92.75 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 120 WLSYQEVAKRAEFLGSGLLqhDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVI 199
Cdd:cd12118 29 RYTWRQTYDRCRRLASALA--ALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 200 VDKPHKatlllehverketpglklvilmepFEDALrERGKKcgvdiksmqaiedcgrenHHAPVPPRPDDLSIVC-FTSG 278
Cdd:cd12118 107 VDREFE------------------------YEDLL-AEGDP------------------DFEWIPPADEWDPIALnYTSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 279 TTGNPKGAMLTH--------GNVVAdfsgflkvtesqWAptcADVHFSYLPLAHMFermvQSVVYCHGGRVGFFQG---- 346
Cdd:cd12118 144 TTGRPKGVVYHHrgaylnalANILE------------WE---MKQHPVYLWTLPMF----HCNGWCFPWTVAAVGGtnvc 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 347 ----DIRLLSDDMKALRPTIFPVVPRLLNrmydkifhqadtslkrwllefaakrkqaevrsgIIRNNSIWDelffnkiQA 422
Cdd:cd12118 205 lrkvDAKAIYDLIEKHKVTHFCGAPTVLN---------------------------------MLANAPPSD-------AR 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 423 SLGGHVRMIVTGAAPaSPTVLgFLRAALGCQVYEGYGQTEcTAG----CTFTTPGDWTSGHVGAPLPC----NHIKLVDA 494
Cdd:cd12118 245 PLPHRVHVMTAGAPP-PAAVL-AKMEELGFDVTHVYGLTE-TYGpatvCAWKPEWDELPTEERARLKArqgvRYVGLEEV 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 495 EELNYWTCK-----GE--GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEY 567
Cdd:cd12118 322 DVLDPETMKpvprdGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGGEN 399
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081036 568 VAPEKIENIyirsepvaqIYVHGDSLKAFLVGivVPDP---EVMPSW-AQKKGIEGTYQEL 624
Cdd:cd12118 400 ISSVEVEGV---------LYKHPAVLEAAVVA--RPDEkwgEVPCAFvELKEGAKVTEEEI 449
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
121-607 |
5.13e-19 |
|
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: 90.72 E-value: 5.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELA------CYtysmvvVPLYDTLGPGSISYIINTAD 194
Cdd:cd12117 23 LTYAELNERANRLARRLRAAG--VGPGDVVGVLAERSPELVVALLAvlkagaAY------VPLDPELPAERLAFMLADAG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 195 ICTVIVDKPhkatlllehverketpglklvilmepfedaLRERGKKCGVDIKSMQAIEDCGRENhhAPVPPRPDDLSIVC 274
Cdd:cd12117 95 AKVLLTDRS------------------------------LAGRAGGLEVAVVIDEALDAGPAGN--PAVPVSPDDLAYVM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 275 FTSGTTGNPKGAMLTHGNVVAdfsgflKVTESQWAPTCADVHFSYL-PL---AHMFERMVQSVvycHGGRVgffqgdiRL 350
Cdd:cd12117 143 YTSGSTGRPKGVAVTHRGVVR------LVKNTNYVTLGPDDRVLQTsPLafdASTFEIWGALL---NGARL-------VL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 351 LSDDmkalrptifpvVPRLLNRMYDKIFHQADTSLkrWLLefAAkrkqaevrsgiirnnsiwdelFFNKI----QASLGG 426
Cdd:cd12117 207 APKG-----------TLLDPDALGALIAEEGVTVL--WLT--AA---------------------LFNQLadedPECFAG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 427 hVRMIVTGAAPASPT-VLGFLRAALGCQVYEGYGQTECTagcTFTT-----PGDWTSGHV--GAPLPCNHIKLVDAeeln 498
Cdd:cd12117 251 -LRELLTGGEVVSPPhVRRVLAACPGLRLVNGYGPTENT---TFTTshvvtELDEVAGSIpiGRPIANTRVYVLDE---- 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 499 ywtcKG-------EGEICVKGPNVFKGYLKDEDRTKEALDSDGWL------HTGDIGKWLPEGTLKIIDRKKHIFKLaQG 565
Cdd:cd12117 323 ----DGrpvppgvPGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI-RG 397
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1907081036 566 EYVAPEKIENIYIRSEPVAQIYV---HGDSLKAFLVGIVVPDPEV 607
Cdd:cd12117 398 FRIELGEIEAALRAHPGVREAVVvvrEDAGGDKRLVAYVVAEGAL 442
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
267-604 |
7.74e-19 |
|
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: 89.83 E-value: 7.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF--------LKVTESQWAPTCADVHFSYLPLAhmfermvqsvvYCHG 338
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWrreyeldsFPVRLLQMASFSFDVFAGDFARS-----------LLNG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 339 GRVGFFQGDIRL----LSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTSLKRWLLEFAAKRKQAEvrsgiirnnsiWde 414
Cdd:cd17650 161 GTLVICPDEVKLdpaaLYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQ-----------D-- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 415 lfFNKIQASLGGHVRMIvtgaapaspTVLGFLRAALGCQVYEGYGQTECTAGctfTTPgdwtsghVGAPLPCNHIKLVDa 494
Cdd:cd17650 228 --FKTLAARFGQGMRII---------NSYGVTEATIDSTYYEEGRDPLGDSA---NVP-------IGRPLPNTAMYVLD- 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 495 EELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGW------LHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYV 568
Cdd:cd17650 286 ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI-RGFRI 364
|
330 340 350
....*....|....*....|....*....|....*....
gi 1907081036 569 APEKIENIYIRSEPVAQIYV---HGDSLKAFLVGIVVPD 604
Cdd:cd17650 365 ELGEIESQLARHPAIDEAVVavrEDKGGEARLCAYVVAA 403
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
267-631 |
7.90e-19 |
|
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: 89.80 E-value: 7.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 267 PDDLSIVCFTSGTTGNPKGAMLTH----GNVVADFSGFlkvtesQWAPTCADVHFS-------------YLP-------- 321
Cdd:cd05971 87 SDDPALIIYTSGTTGPPKGALHAHrvllGHLPGVQFPF------NLFPRDGDLYWTpadwawigglldvLLPslyfgvpv 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 322 LAHMFERmvqsvvychggrvgfFQGD--IRLLSD---DMKALRPTIFpvvprllnrmydKIFHQADTSLKRWLLEfaakr 396
Cdd:cd05971 161 LAHRMTK---------------FDPKaaLDLMSRygvTTAFLPPTAL------------KMMRQQGEQLKHAQVK----- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 397 kqaevrsgiirnnsiwdelffnkiqaslgghVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEC---TAGCTFTTPG 473
Cdd:cd05971 209 -------------------------------LRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECnlvIGNCSALFPI 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 474 DwtSGHVGAPLPCNHIKLVDAeelnywtcKGE-------GEICVKGPN--VFKGYLKDEDRTKEALDSDgWLHTGDIGKW 544
Cdd:cd05971 258 K--PGSMGKPIPGHRVAIVDD--------NGTplppgevGEIAVELPDpvAFLGYWNNPSATEKKMAGD-WLLTGDLGRK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 545 LPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRsepvaqiyvHGDSLKAFLVGIvvPDP---EVMPSWAQKKGIEGTY 621
Cdd:cd05971 327 DSDGYFWYVGRDDDVITSS-GYRIGPAEIEECLLK---------HPAVLMAAVVGI--PDPirgEIVKAFVVLNPGETPS 394
|
410
....*....|
gi 1907081036 622 QELcmKKELK 631
Cdd:cd05971 395 DAL--AREIQ 402
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
121-609 |
2.43e-18 |
|
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: 88.14 E-value: 2.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 200
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAG--VGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 DkphkatlllehverketpglklvilmepfedalrergkkcgvdiksmqaiedcgrenhhapvpprPDDLSIVCFTSGTT 280
Cdd:cd12115 103 D-----------------------------------------------------------------PDDLAYVIYTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 281 GNPKGAMLTHGNVVA------------DFSGFLKVTesqwaPTCADvhfsyLPLAHMFermvqsVVYCHGGRVGFFQGDI 348
Cdd:cd12115 118 GRPKGVAIEHRNAAAflqwaaaafsaeELAGVLAST-----SICFD-----LSVFELF------GPLATGGKVVLADNVL 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 349 RLLsDDMKALRPTIFPVVPrllnrmydkifhqadtSLKRWLLEFaakrkqaevrsgiirnnsiwdelffNKIQASlgghV 428
Cdd:cd12115 182 ALP-DLPAAAEVTLINTVP----------------SAAAELLRH-------------------------DALPAS----V 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 429 RMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFT--TPGDWTSGHVGAPLPCNHIKLVDaEELNYWTCKGE 505
Cdd:cd12115 216 RVVNLAGEPLPRDLVQRLYARLqVERVVNLYGPSEDTTYSTVApvPPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVP 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 506 GEICVKGPNVFKGYLKDEDRTKEALDSDGWL------HTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIR 579
Cdd:cd12115 295 GELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAALRS 373
|
490 500 510
....*....|....*....|....*....|...
gi 1907081036 580 SEPVAQ--IYVHGDSL-KAFLVGIVVPDPEVMP 609
Cdd:cd12115 374 IPGVREavVVAIGDAAgERRLVAYIVAEPGAAG 406
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
121-606 |
1.20e-17 |
|
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: 86.74 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfvgVFAQ--NRPEWIIAELACYtySMVVVPLYdTLgPG----SISYIINTAD 194
Cdd:COG1021 51 LSYAELDRRADRLAAGLLALGLRPGDR----VVVQlpNVAEFVIVFFALF--RAGAIPVF-AL-PAhrraEISHFAEQSE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 195 ICTVIVDKPHkatLLLEHVE-----RKETPGLKLVILmepfedalrergkkCGvDIKSMQAIEDCGRENHHAPVP-PRPD 268
Cdd:COG1021 123 AVAYIIPDRH---RGFDYRAlarelQAEVPSLRHVLV--------------VG-DAGEFTSLDALLAAPADLSEPrPDPD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 269 DlsiVCF---TSGTTGNPKGAMLTHgnvvADFsgFLKVTESqwAPTCA----DVHFSYLPLAHMFErM----VQSVVYcH 337
Cdd:COG1021 185 D---VAFfqlSGGTTGLPKLIPRTH----DDY--LYSVRAS--AEICGldadTVYLAALPAAHNFP-LsspgVLGVLY-A 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 338 GGRVgffqgdirLLSDDMKALrpTIFPVVPRllnrmydkifHQAD-TSL-----KRWLlEFAAKRKQAevrsgiirnnsi 411
Cdd:COG1021 252 GGTV--------VLAPDPSPD--TAFPLIER----------ERVTvTALvpplaLLWL-DAAERSRYD------------ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 412 wdeLffnkiqASLgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctaG-CTFTTPGD--WTSGH-VGAPL-PC 486
Cdd:COG1021 299 ---L------SSL----RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---GlVNYTRLDDpeEVILTtQGRPIsPD 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 487 NHIKLVDAEelnywtckGE-------GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKK-H 558
Cdd:COG1021 363 DEVRIVDED--------GNpvppgevGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKdQ 434
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1907081036 559 IFKlaQGEYVAPEKIENiyirsepvaQIYVHGDSLKAFLVGivVPDPE 606
Cdd:COG1021 435 INR--GGEKIAAEEVEN---------LLLAHPAVHDAAVVA--MPDEY 469
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
27-639 |
1.32e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 87.91 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 27 ATTLVSVGALAAVLAYW--LTHRPKAlQPPCNL----LKQSEEVEDGGGARRsviggctqlLTHYYDDARTMYQVFRRGL 100
Cdd:PRK12467 453 ATDLFEATTIERLATHWrnLLEAIVA-EPRRRLgelpLLDAEERARELVRWN---------APATEYAPDCVHQLIEAQA 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 101 SISGNGPCLGFRKpeqpyQWLSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDT 180
Cdd:PRK12467 523 RQHPERPALVFGE-----QVLSYAELNRQANRLAHVLIAAG--VGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPE 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 181 LGPGSISYIINTADICTVIVDkPHKATLLlehverkETP-GLKLVILMEPfedalrergkkcgvdiksmqAIEDCGRENH 259
Cdd:PRK12467 596 YPQDRLAYMLDDSGVRLLLTQ-SHLLAQL-------PVPaGLRSLCLDEP--------------------ADLLCGYSGH 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 260 HAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVvadfSGFLKVTESQWAPTCADVHFSYLPLAHMFERMVQSVVYCHGG 339
Cdd:PRK12467 648 NPEVALDPDNLAYVIYTSGSTGQPKGVAISHGAL----ANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGA 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 340 RVgffqgdirLLSDDMKALRPTIFpvvprllnrmYDKIFHQADTSLKrwllefaakrkqaevrsgiiRNNSIWDELFFNK 419
Cdd:PRK12467 724 TL--------HLLPPDCARDAEAF----------AALMADQGVTVLK--------------------IVPSHLQALLQAS 765
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 420 IQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTT----PGDWTSGHVGAPLPCNHIKLVDAe 495
Cdd:PRK12467 766 RVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYElsdeERDFGNVPIGQPLANLGLYILDH- 844
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 496 ELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSD------GWLH-TGDIGKWLPEGTLKIIDRKKHIFKLaQGEYV 568
Cdd:PRK12467 845 YLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDpfgadgGRLYrTGDLARYRADGVIEYLGRMDHQVKI-RGFRI 923
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081036 569 APEKIENIYIRSEPVAQIYV------HGDSLKAFLVGIVVPDpevmpswaqkkGIEGTYQELCMKKELKKAILDDMV 639
Cdd:PRK12467 924 ELGEIEARLLAQPGVREAVVlaqpgdAGLQLVAYLVPAAVAD-----------GAEHQATRDELKAQLRQVLPDYMV 989
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
121-610 |
1.85e-17 |
|
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: 85.88 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLLQhdCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIIN--------- 191
Cdd:cd05959 30 LTYAELEAEARRVAGALRA--LGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEdsrarvvvv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 192 TADICTVIVDKPHKATLLLEHVERKE-TPGLKLVILMEPFEDALRERGKkcgvdiksmqaiedcgrenhhaPVPPRPDDL 270
Cdd:cd05959 108 SGELAPVLAAALTKSEHTLVVLIVSGgAGPEAGALLLAELVAAEAEQLK----------------------PAATHADDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 271 SIVCFTSGTTGNPKGAMLTHGN--VVADFSG--FLKVTESqwaptcaDVHFSYLPLAH--------MFERMVQSVVYCHG 338
Cdd:cd05959 166 AFWLYSSGSTGRPKGVVHLHADiyWTAELYArnVLGIRED-------DVCFSAAKLFFayglgnslTFPLSVGATTVLMP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 339 GRVgffqgDIRLLSDDMKALRPTIFPVVPRLLNRMydkifhqadtslkrwlleFAAKRKQAEVRSGIirnnsiwdelffn 418
Cdd:cd05959 239 ERP-----TPAAVFKRIRRYRPTVFFGVPTLYAAM------------------LAAPNLPSRDLSSL------------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 419 kiqaslgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTF--TTPGDWTSGHVGAPLPCNHIKLVDaEE 496
Cdd:cd05959 283 ----------RLCVSAGEALPAEVGERWKARFGLDILDGIGSTE--MLHIFlsNRPGRVRYGTTGKPVPGYEVELRD-ED 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 497 LNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSdGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAPEKIENI 576
Cdd:cd05959 350 GGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQG-EWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSPFEVESA 427
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1907081036 577 YIRSEPVAQIYVHG-------DSLKAFlvgiVVPDPEVMPS 610
Cdd:cd05959 428 LVQHPAVLEAAVVGvededglTKPKAF----VVLRPGYEDS 464
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
121-590 |
2.03e-17 |
|
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: 85.64 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLLQHDCKVGteQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 200
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRPG--QRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 dkphkatllleHVERKETPGLKLVILMEPFEDALRERGKKCgVDIKSMqaiedcgrenhhAPVPPRPDDLSIVCFTSGTT 280
Cdd:cd05923 107 -----------AVDAQVMDAIFQSGVRVLALSDLVGLGEPE-SAGPLI------------EDPPREPEQPAFVFYTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 281 GNPKGAMLTHgNVVADFSGFLkVTESQWAPTCADVHFSYLPLAHMfermvqsvvychggrVGFFQgdirLLSDDMkALRP 360
Cdd:cd05923 163 GLPKGAVIPQ-RAAESRVLFM-STQAGLRHGRHNVVLGLMPLYHV---------------IGFFA----VLVAAL-ALDG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 361 TIFPVvprllnrmydKIFHQADtslkrwllefAAKRKQAEVRSGIIRNNSIWDELFFNKIQASLG-GHVRMIVTGAAPAS 439
Cdd:cd05923 221 TYVVV----------EEFDPAD----------ALKLIEQERVTSLFATPTHLDALAAAAEFAGLKlSSLRHVTFAGATMP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 440 PTVLGFLRAALGCQVYEGYGQTECTagcTFTTPGDWTSGHVGAPLPCNHIKLVD-AEELNYWTCKG-EGEICVK--GPNV 515
Cdd:cd05923 281 DAVLERVNQHLPGEKVNIYGTTEAM---NSLYMRDARTGTEMRPGFFSEVRIVRiGGSPDEALANGeEGELIVAaaADAA 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907081036 516 FKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYVHG 590
Cdd:cd05923 358 FTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIG 430
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
259-594 |
2.69e-17 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 86.30 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 259 HHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTH----GNV-----VADFsgflkvtesqwapTCADVHFSYLPLAHMFerm 329
Cdd:PRK08043 356 RLAQVKQQPEDAALILFTSGSEGHPKGVVHSHksllANVeqiktIADF-------------TPNDRFMSALPLFHSF--- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 330 vqsvvychGGRVGffqgdirLLSDDMKALRPTIFP------VVPRLLnrmYDK----IFhqaDTSlkRWLLEFAakrkqa 399
Cdd:PRK08043 420 --------GLTVG-------LFTPLLTGAEVFLYPsplhyrIVPELV---YDRnctvLF---GTS--TFLGNYA------ 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 400 evrsgiiRNNSIWDelFFnkiqaslggHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGH 479
Cdd:PRK08043 471 -------RFANPYD--FA---------RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGT 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 480 VGAPLPCnhiklVDAEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTK-EALDSD--------GWLHTGDIGKWLPEGTL 550
Cdd:PRK08043 533 VGRILPG-----MDARLLSVPGIEQGGRLQLKGPNIMNGYLRVEKPGVlEVPTAEnargemerGWYDTGDIVRFDEQGFV 607
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1907081036 551 KIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQiyvHGDSLK 594
Cdd:PRK08043 608 QIQGRAKRFAKIA-GEMVSLEMVEQLALGVSPDKQ---HATAIK 647
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
107-568 |
2.98e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 85.87 E-value: 2.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 107 PCLGFRKPEQ-PYQWLSYQEVAKRAEFLGSGLLqhDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLydtlgpgS 185
Cdd:PRK12582 66 PWLAQREPGHgQWRKVTYGEAKRAVDALAQALL--DLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPV-------S 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 186 ISYIINTADIctvivDKphkatllLEHVERKETPGLKLVILMEPFEDALRERGKKcGVDIKSMQAIEDCGRENHHAPV-- 263
Cdd:PRK12582 137 PAYSLMSHDH-----AK-------LKHLFDLVKPRVVFAQSGAPFARALAALDLL-DVTVVHVTGPGEGIASIAFADLaa 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 264 -PPR-----------PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVT-ESQWAPTcaDVHFSYLPLAHMFERMV 330
Cdd:PRK12582 204 tPPTaavaaaiaaitPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRpREPDPPP--PVSLDWMPWNHTMGGNA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 331 Q--------SVVYCHGGR--VGFFQGDIRLLSDdmkaLRPTIFPVVPRLLNRMYDKIfhQADTSLKRWLLefaaKRKQAE 400
Cdd:PRK12582 282 NfngllwggGTLYIDDGKplPGMFEETIRNLRE----ISPTVYGNVPAGYAMLAEAM--EKDDALRRSFF----KNLRLM 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 401 VRSGIIRNNSIWDELFFNKIQASlgGHvrMIVtgaapasptvlgflraalgcqVYEGYGQTEcTAGCTFTTpgDWTS--- 477
Cdd:PRK12582 352 AYGGATLSDDLYERMQALAVRTT--GH--RIP---------------------FYTGYGATE-TAPTTTGT--HWDTerv 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 478 GHVGAPLPCNHIKLVDAEElNYwtckgegEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWL----PEGTLKII 553
Cdd:PRK12582 404 GLIGLPLPGVELKLAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdpddPEKGLIFD 475
|
490
....*....|....*
gi 1907081036 554 DRKKHIFKLAQGEYV 568
Cdd:PRK12582 476 GRVAEDFKLSTGTWV 490
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
88-588 |
3.54e-17 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 85.20 E-value: 3.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 88 DARTMYQVFRRGLSISGNGPCLGFRKpeqpyQWLSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELAC 167
Cdd:PRK06155 19 SERTLPAMLARQAERYPDRPLLVFGG-----TRWTYAEAARAAAAAAHALAAAGVKRGDR--VALMCGNRIEFLDVFLGC 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 168 YTYSMVVVPLYDTLGPGSISYIINTADICTVIVDkphkATLL--LEHVERKETPGLKLVILmepfeDALRERGKKCGVDI 245
Cdd:PRK06155 92 AWLGAIAVPINTALRGPQLEHILRNSGARLLVVE----AALLaaLEAADPGDLPLPAVWLL-----DAPASVSVPAGWST 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 246 KSMQAIEDCGrenhhAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHG-------NVVADfsgfLKVTESqwaptcaDVHFS 318
Cdd:PRK06155 163 APLPPLDAPA-----PAAAVQPGDTAAILYTSGTTGPSKGVCCPHAqfywwgrNSAED----LEIGAD-------DVLYT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 319 YLPLAH------MFERMVQSVVYCHGGRV---GFFqgdirllsDDMKALRPTIF----PVVPRLLnrmydkifhqadtsl 385
Cdd:PRK06155 227 TLPLFHtnalnaFFQALLAGATYVLEPRFsasGFW--------PAVRRHGATVTyllgAMVSILL--------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 386 krwllefaAKRKQAEVRsgiirnnsiwdelffnkiqaslgGH-VRMIVTGAAPASptVLGFLRAALGCQVYEGYGQTECT 464
Cdd:PRK06155 284 --------SQPARESDR-----------------------AHrVRVALGPGVPAA--LHAAFRERFGVDLLDGYGSTETN 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 465 AGCtFTTPGDWTSGHVGAPLPCNHIKLVDAE--ELNywtcKGE-GEICVKG--PNVF-KGYLKDEDRTKEALdSDGWLHT 538
Cdd:PRK06155 331 FVI-AVTHGSQRPGSMGRLAPGFEARVVDEHdqELP----DGEpGELLLRAdePFAFaTGYFGMPEKTVEAW-RNLWFHT 404
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1907081036 539 GDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAPEKIENIyIRSEP-VAQIYV 588
Cdd:PRK06155 405 GDRVVRDADGWFRFVDRIKDAIR-RRGENISSFEVEQV-LLSHPaVAAAAV 453
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
267-583 |
6.39e-17 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 84.08 E-value: 6.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESqwapTCADVHFSYLPLAHmfermvqsvvychggRVGFFQG 346
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEW----KTKDRILSWMPLTH---------------DMGLIAF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 347 DIRLLSDDMKA-LRPT-IFPVVPRLlnrmydkifhqadtslkrWLLEfAAKRKQAEVRSGIIRNNSIWDELFFNKIQASL 424
Cdd:cd05908 166 HLAPLIAGMNQyLMPTrLFIRRPIL------------------WLKK-ASEHKATIVSSPNFGYKYFLKTLKPEKANDWD 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 425 GGHVRMIVTGAAPASP----------TVLGFLRAAlgcqVYEGYGQTECTAGCTF------------------------- 469
Cdd:cd05908 227 LSSIRMILNGAEPIDYelchefldhmSKYGLKRNA----ILPVYGLAEASVGASLpkaqspfktitlgrrhvthgepepe 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 470 ---TTPGDWTSGHVGAPLPCNHIKLVDaeELNYWTCKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGkWL 545
Cdd:cd05908 303 vdkKDSECLTFVEVGKPIDETDIRICD--EDNKILPDGYiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FI 379
|
330 340 350
....*....|....*....|....*....|....*...
gi 1907081036 546 PEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPV 583
Cdd:cd05908 380 RNGRLVITGREKDII-FVNGQNVYPHDIERIAEELEGV 416
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
267-590 |
6.84e-17 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 84.47 E-value: 6.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVAD------FSGFlkvTESqwaptcaDVHFSYLPLAH-------MFERMVQSv 333
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSALIVQslakiaIVGY---GED-------DVYLHTAPLCHigglssaLAMLMVGA- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 334 vyCHggrVGFFQGDIRLLSDDMKALRPTIFPVVPRLLnrmydkifhqADtslkrwLLEFAAKRKQAEVRSGiirnnsiwd 413
Cdd:PLN02860 240 --CH---VLLPKFDAKAALQAIKQHNVTSMITVPAMM----------AD------LISLTRKSMTWKVFPS--------- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 414 elffnkiqaslgghVRMIVTGAAPASP-----TVLGFLRAALgcqvYEGYGQTECTAGCTFTTPGDWT------------ 476
Cdd:PLN02860 290 --------------VRKILNGGGSLSSrllpdAKKLFPNAKL----FSAYGMTEACSSLTFMTLHDPTlespkqtlqtvn 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 477 -----SGH------VGAPLPcnHIKL-VDAEELNYwtckgEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKW 544
Cdd:PLN02860 352 qtkssSVHqpqgvcVGKPAP--HVELkIGLDESSR-----VGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWI 424
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1907081036 545 LPEGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSEPVAQIYVHG 590
Cdd:PLN02860 425 DKAGNLWLIGRSNDRIK-TGGENVYPEEVEAVLSQHPGVASVVVVG 469
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
269-576 |
1.03e-16 |
|
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: 81.92 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 269 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKvteSQWAPTCADVHFSYLPLAHMFE--RMVQSVVYcHGGRVGFfqG 346
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQK---EGLNWVVGDVTYLPLPATHIGGlwWILTCLIH-GGLCVTG--G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 347 DIRLLSDDMKAL---RPTIFPVVPRLLNRMydkifhqadTSLKRWLLEFAAKrkqaevrsgiirnnsiwdelffnkiqas 423
Cdd:cd17635 76 ENTTYKSLFKILttnAVTTTCLVPTLLSKL---------VSELKSANATVPS---------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 424 lgghVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDAEELNYWTc 502
Cdd:cd17635 119 ----LRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLPTDDDSIEiNAVGRPYPGVDVYLAATDGIAGPS- 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081036 503 KGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENI 576
Cdd:cd17635 194 ASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERI 265
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
121-610 |
1.12e-16 |
|
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: 83.55 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIIntADICTVIV 200
Cdd:cd17651 21 LTYAELDRRANRLAHRLRARG--VGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFML--ADAGPVLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 dkphkatlLLEHVERKETPG-LKLVILMEPFEDAlrergkkcgvdiksmqaieDCGRENHhaPVPPRPDDLSIVCFTSGT 279
Cdd:cd17651 97 --------LTHPALAGELAVeLVAVTLLDQPGAA-------------------AGADAEP--DPALDADDLAYVIYTSGS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 280 TGNPKGAMLTHGNVV-------ADFSGFLKVTESQWAPTCADVH----FSYLplahmfermvqsvvyCHGGRVGFFQGDI 348
Cdd:cd17651 148 TGRPKGVVMPHRSLAnlvawqaRASSLGPGARTLQFAGLGFDVSvqeiFSTL---------------CAGATLVLPPEEV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 349 RLLSDDMKALrptifpvvprLLNRMYDKIFhqADTSLKRWLLEfAAKRKQAEvrsgiirnnsiwdelffnkiqaslGGHV 428
Cdd:cd17651 213 RTDPPALAAW----------LDEQRISRVF--LPTVALRALAE-HGRPLGVR------------------------LAAL 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 429 RMIVTG--AAPASPTVLGFLRAALGCQVYEGYGQTE---CTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDAeelnywtc 502
Cdd:cd17651 256 RYLLTGgeQLVLTEDLREFCAGLPGLRLHNHYGPTEthvVTALSLPGDPAAWPApPPIGRPIDNTRVYVLDA-------- 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 503 KGE-------GEICVKGPNVFKGYLKDEDRTKEALDSDGWL------HTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVA 569
Cdd:cd17651 328 ALRpvppgvpGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGFRIE 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1907081036 570 PEKIENIYIRSEPVAQIYV------HGDslkAFLVGIVVPDPEVMPS 610
Cdd:cd17651 407 LGEIEAALARHPGVREAVVlaredrPGE---KRLVAYVVGDPEAPVD 450
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
121-606 |
4.99e-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: 81.17 E-value: 4.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 200
Cdd:cd17646 24 LTYRELDERANRLAHLLRARG--VGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 DkphkatlllehverketpglklvilmepfeDALRERGKKcGVDIKSMQAIEDCGRENHHAPVPPRPDDLSIVCFTSGTT 280
Cdd:cd17646 102 T------------------------------ADLAARLPA-GGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGST 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 281 GNPKGAMLTHGNVVADFSGF---LKVTES----QWAPTCADVhfsylPLAHMFERMVQS---VVYCHGGRvgffqGDIRL 350
Cdd:cd17646 151 GRPKGVMVTHAGIVNRLLWMqdeYPLGPGdrvlQKTPLSFDV-----SVWELFWPLVAGarlVVARPGGH-----RDPAY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 351 LSDDMKALRPTIFPVVPRLLnrmydkifhqadtslkrwllefaakrkqaevrsgiirnnsiwdELFFNKIQASLGGHVRM 430
Cdd:cd17646 221 LAALIREHGVTTCHFVPSML-------------------------------------------RVFLAEPAAGSCASLRR 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 431 IVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHV--GAPLPCNHIKLVDAEeLNYWTCKGEGE 507
Cdd:cd17646 258 VFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVThWPVRGPAETPSVpiGRPVPNTRLYVLDDA-LRPVPVGVPGE 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 508 ICVKGPNVFKGYLKDEDRTKEALDSDGWLH------TGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSE 581
Cdd:cd17646 337 LYLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKI-RGFRVEPGEIEAALAAHP 415
|
490 500
....*....|....*....|....*...
gi 1907081036 582 PVAQIYV---HGDSLKAFLVGIVVPDPE 606
Cdd:cd17646 416 AVTHAVVvarAAPAGAARLVGYVVPAAG 443
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
121-609 |
1.02e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 80.56 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADiCTVIV 200
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQG--VRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGR-ARWLV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 DKPHKATL----LLEHVERKETPGLKLVILMEPFEDALRERGKKCGVdiksmQAIEDCGRENHHA-PVPPRPDDLSIVCF 275
Cdd:PRK06164 113 VWPGFKGIdfaaILAAVPPDALPPLRAIAVVDDAADATPAPAPGARV-----QLFALPDPAPPAAaGERAADPDAGALLF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 276 T-SGTTGNPK------GAMLTHGNVVADFSGFlkvtesqwAPtcADVHFSYLPLahmfermvqSVVYCHGGRVGFFQGDI 348
Cdd:PRK06164 188 TtSGTTSGPKlvlhrqATLLRHARAIARAYGY--------DP--GAVLLAALPF---------CGVFGFSTLLGALAGGA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 349 RLLSDDmkalrptIF--PVVPRLL-----------NRMYDKIFHQADTSLkrwllEFAAKRkqaevRSGIIRNNSIWDEL 415
Cdd:PRK06164 249 PLVCEP-------VFdaARTARALrrhrvthtfgnDEMLRRILDTAGERA-----DFPSAR-----LFGFASFAPALGEL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 416 ffnkiqaslgghvrmivtgaaPASPTVLGFLRAALgcqvyegYGQTECTA---GCTFTTPgdWTSGHVGAPLPCN---HI 489
Cdd:PRK06164 312 ---------------------AALARARGVPLTGL-------YGSSEVQAlvaLQPATDP--VSVRIEGGGRPASpeaRV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 490 KLVDAEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVA 569
Cdd:PRK06164 362 RARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVN 440
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1907081036 570 PEKIENIYIRSEPVAQIYVHGDSL--KAFLVGIVVPDPEVMP 609
Cdd:PRK06164 441 PAEIEHALEALPGVAAAQVVGATRdgKTVPVAFVIPTDGASP 482
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
94-614 |
1.02e-15 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 80.60 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 94 QVFRRGLSISGNGPCLGFRKPEQpyQWLSYQEVAKRAEFLGSGLlqHD-CKVGTEQFVGVFAQNRPEWIIAELACYTYSM 172
Cdd:PRK05620 14 RILEYGSTVHGDTTVTTWGGAEQ--EQTTFAAIGARAAALAHAL--HDeLGITGDQRVGSMMYNCAEHLEVLFAVACMGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 173 VVVPLYDTLGPGSISYIINTADIcTVIVDKPHKATLLLEHVerKETPGLKLVILMEPFEDALRERGKKCGVDIKSMQAIE 252
Cdd:PRK05620 90 VFNPLNKQLMNDQIVHIINHAED-EVIVADPRLAEQLGEIL--KECPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 253 DcGRENHHA-PVPPRpDDLSIVCFTSGTTGNPKGAMLTHGNVVADfSGFLKVTESqWAPTCADVHFSYLPLAHMFERMVQ 331
Cdd:PRK05620 167 D-GRSTVYDwPELDE-TTAAAICYSTGTTGAPKGVVYSHRSLYLQ-SLSLRTTDS-LAVTHGESFLCCVPIYHVLSWGVP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 332 SVVYCHGGrvgffqgdirllsddmkalrPTIFP----VVPRLLnrmydkifHQADTSLKRwllefaakrkqaeVRSGIir 407
Cdd:PRK05620 243 LAAFMSGT--------------------PLVFPgpdlSAPTLA--------KIIATAMPR-------------VAHGV-- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 408 nNSIWDELFFNKIQ-----ASLgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGA 482
Cdd:PRK05620 280 -PTLWIQLMVHYLKnpperMSL----QEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEARW 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 483 ---------PLPCNHiKLVDAEELNYWTCKGEGEICVKGPNVFKGYLKDE----------------DRTKEALDSDGWLH 537
Cdd:PRK05620 355 ayrvsqgrfPASLEY-RIVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLR 433
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081036 538 TGDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSEPVaqiyvhgdsLKAFLVGIvvPDPEvmpsWAQK 614
Cdd:PRK05620 434 TGDVGSVTRDGFLTIHDRARDVIR-SGGEWIYSAQLENYIMAAPEV---------VECAVIGY--PDDK----WGER 494
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
144-605 |
1.46e-15 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 80.45 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 144 VGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIVDKPHKATL--LLEHVERKET-PG 220
Cdd:PLN03102 61 ITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAreVLHLLSSEDSnLN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 221 LKLVILME------PFE-----DALRERGKKCGVDIKSMQAIEDcgrenHHAPVPprpddlsiVCFTSGTTGNPKGAMLT 289
Cdd:PLN03102 141 LPVIFIHEidfpkrPSSeeldyECLIQRGEPTPSLVARMFRIQD-----EHDPIS--------LNYTSGTTADPKGVVIS 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 290 H-GNVVADFSGFLKvtesqWAPTCADVHFSYLPLAHmfermvqsvvyCHGGRVGF---FQGDIRLLSDDMKAlrPTIFPV 365
Cdd:PLN03102 208 HrGAYLSTLSAIIG-----WEMGTCPVYLWTLPMFH-----------CNGWTFTWgtaARGGTSVCMRHVTA--PEIYKN 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 366 VprllnRMYDKIFHQADTSLKRWLLEfaAKRKQAEVRSGIIRnnsiwdelffnkiqaslgghvrmIVTGAAPAsPTVLGF 445
Cdd:PLN03102 270 I-----EMHNVTHMCCVPTVFNILLK--GNSLDLSPRSGPVH-----------------------VLTGGSPP-PAALVK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 446 LRAALGCQVYEGYGQTECTAGCTFTTPGD-WTSghvgapLPCN------------HIKLVDAEELNYWTC-------KGE 505
Cdd:PLN03102 319 KVQRLGFQVMHAYGLTEATGPVLFCEWQDeWNR------LPENqqmelkarqgvsILGLADVDVKNKETQesvprdgKTM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 506 GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIyirsepvaq 585
Cdd:PLN03102 393 GEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVENV--------- 461
|
490 500
....*....|....*....|
gi 1907081036 586 IYVHGDSLKAFLVGIvvPDP 605
Cdd:PLN03102 462 LYKYPKVLETAVVAM--PHP 479
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
266-606 |
2.00e-15 |
|
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: 79.27 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 266 RPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkvTESQWAPTCADV----H-----FS----YLPLAHmfermvqs 332
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA----TQRWFGFNEDDVwtlfHsyafdFSvweiWGALLH-------- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 333 vvychGGRVGFFQGDIRLLSDDMkalrptifpvvPRLLNRMYDKIFHQADTSLKRWLlefaakrkQAEVRsgiirnnsiw 412
Cdd:cd17643 159 -----GGRLVVVPYEVARSPEDF-----------ARLLRDEGVTVLNQTPSAFYQLV--------EAADR---------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 413 delfFNKIQASLgghvRMIVTGAAPASPTVLGFLRAALGC---QVYEGYGQTECTAGCTFT--TPGDW---TSGHVGAPL 484
Cdd:cd17643 205 ----DGRDPLAL----RYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFRplDAADLpaaAASPIGRPL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 485 PCNHIKLVDAEeLNYWTCKGEGEICVKGPNVFKGYLKDEDRTKE-------ALDSDGWLHTGDIGKWLPEGTLKIIDRKK 557
Cdd:cd17643 277 PGLRVYVLDAD-GRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRLPDGELEYLGRAD 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1907081036 558 HIFKLaQGEYVAPEKIENIYIRSEPVAQIYV---HGDSLKAFLVGIVVPDPE 606
Cdd:cd17643 356 EQVKI-RGFRIELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVADDG 406
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
457-613 |
9.64e-15 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 75.80 E-value: 9.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 457 GYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAE--ELNywtcKGE-GEICVKGPNVFKGYLkDEDRTKEALDSD 533
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDgrEVP----DGEvGEIVARGPTVMAGYW-NRPEVNARRTRG 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 534 GWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqgeyvapekIENIY-------IRSEP-VAQIYVhgdslkaflvgIVVPDp 605
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSG---------AENIYpaevercLRQHPaVADAAV-----------IGVPD- 275
|
....*...
gi 1907081036 606 evmPSWAQ 613
Cdd:cd17636 276 ---PRWAQ 280
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
265-603 |
1.47e-14 |
|
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: 76.73 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 265 PRPDDLSIVCFTSGTTGNPKGAMLTHGNvvadFSGFLKVTESQWAPTCADVHFSYLPLAHMFERM--VQSVVychggrvg 342
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGT----FAAQIDALRQLYGIRPGEVDLATFPLFALFGPAlgLTSVI-------- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 343 ffqgdirllsDDMKALRPtifpvvprllnrmydkifhqADTSlKRWLLEFAAkrkQAEVrSGIIRNNSIWDEL--FFNKI 420
Cdd:cd05910 150 ----------PDMDPTRP--------------------ARAD-PQKLVGAIR---QYGV-SIVFGSPALLERVarYCAQH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 421 QASLGGhVRMIVTGAAPASPTVLGFLRAAL--GCQVYEGYGQTECTAGCT------FTTPGDWTSGH----VGAPLPCNH 488
Cdd:cd05910 195 GITLPS-LRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrelLATTTAATSGGagtcVGRPIPGVR 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 489 IKLV--DAEELNYWTCKGE------GEICVKGPNVFKGYLKDEDRTKEALDSDG----WLHTGDIGKWLPEGTLKIIDRK 556
Cdd:cd05910 274 VRIIeiDDEPIAEWDDTLElprgeiGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRK 353
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1907081036 557 KHIFKLAQGEYVapekieniyirSEPVAQIY-VHGDSLKAFLVGIVVP 603
Cdd:cd05910 354 AHRVITTGGTLY-----------TEPVERVFnTHPGVRRSALVGVGKP 390
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
152-605 |
2.33e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 76.23 E-value: 2.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 152 VFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV--DKPhkatlllEHVE--RKETPGLKLVIlm 227
Cdd:PRK07470 62 VHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMIChaDFP-------EHAAavRAASPDLTHVV-- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 228 ePFEDALRERGkkcgvdiksmqaIEDCGRENHHAPVPPRP---DDLSIVCFTSGTTGNPKGAMLTHG-------NVVADF 297
Cdd:PRK07470 133 -AIGGARAGLD------------YEALVARHLGARVANAAvdhDDPCWFFFTSGTTGRPKAAVLTHGqmafvitNHLADL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 298 sgFLKVTEsqwaptcADVHFSYLPLAHM--FERMVQSVvycHGGRVGFFQGDiRLLSDDMKAL----RPTIFPVVPRLLN 371
Cdd:PRK07470 200 --MPGTTE-------QDASLVVAPLSHGagIHQLCQVA---RGAATVLLPSE-RFDPAEVWALverhRVTNLFTVPTILK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 372 RMY-DKIFHQADTSlkrwllefaakrkqaevrsgiirnnsiwdelffnkiqaSLgghvRMIVTGAAPASPTVLGFLRAAL 450
Cdd:PRK07470 267 MLVeHPAVDRYDHS--------------------------------------SL----RYVIYAGAPMYRADQKRALAKL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 451 GCQVYEGYGQTECTAGCTFTTP-----GDWTSGHVGaplPCNH------IKLVDAE--ELNywtcKGE-GEICVKGPNVF 516
Cdd:PRK07470 305 GKVLVQYFGLGEVTGNITVLPPalhdaEDGPDARIG---TCGFertgmeVQIQDDEgrELP----PGEtGEICVIGPAVF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 517 KGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENiyirsepvaQIYVHGDSLKAF 596
Cdd:PRK07470 378 AGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPREIEE---------KLLTHPAVSEVA 446
|
....*....
gi 1907081036 597 LVGivVPDP 605
Cdd:PRK07470 447 VLG--VPDP 453
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
119-599 |
2.53e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 77.30 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 119 QWLSYQEVAKRAEFLGSGLLqhDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGS-ISYIINTADICT 197
Cdd:PRK12316 2027 QHLSYAELDSRANRLAHRLR--ARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPL-DPNYPAErLAYMLEDSGAAL 2103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 198 VIVDKPHKATLLLehverketPGLKLVILMEPfEDALRERgkkcgvdiksmqaiedcgrENHHAPVPPRPDDLSIVCFTS 277
Cdd:PRK12316 2104 LLTQRHLLERLPL--------PAGVARLPLDR-DAEWADY-------------------PDTAPAVQLAGENLAYVIYTS 2155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 278 GTTGNPKGAMLTHGNVVAdfsgFLKVTESQWAPTCADVHFSYLPLAhmFERMVQSVVY--CHGGRVgffqgdirLLSDDM 355
Cdd:PRK12316 2156 GSTGLPKGVAVSHGALVA----HCQAAGERYELSPADCELQFMSFS--FDGAHEQWFHplLNGARV--------LIRDDE 2221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 356 KalrptifpvvpRLLNRMYDKIFHQADTslkrwLLEFAAKRKQAEVRSGIIRNNSIwdelffnkiqaslggHVRMIVTGA 435
Cdd:PRK12316 2222 L-----------WDPEQLYDEMERHGVT-----ILDFPPVYLQQLAEHAERDGRPP---------------AVRVYCFGG 2270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 436 APASPTVLGFLRAALGCQ-VYEGYGQTEctagcTFTTPGDWTSGH----------VGAPLPCNHIKLVDAeELNYWTCKG 504
Cdd:PRK12316 2271 EAVPAASLRLAWEALRPVyLFNGYGPTE-----AVVTPLLWKCRPqdpcgaayvpIGRALGNRRAYILDA-DLNLLAPGM 2344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 505 EGEICVKGPNVFKGYLKDEDRTKEALDSDGWLH-------TGDIGKWLPEGTLKIIDRKKHI-----FKLAQGEYVApEK 572
Cdd:PRK12316 2345 AGELYLGGEGLARGYLNRPGLTAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQvkirgFRIELGEIEA-RL 2423
|
490 500
....*....|....*....|....*...
gi 1907081036 573 IENIYIRSEPV-AQIYVHGDSLKAFLVG 599
Cdd:PRK12316 2424 QAHPAVREAVVvAQDGASGKQLVAYVVP 2451
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
420-588 |
5.10e-14 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 74.91 E-value: 5.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 420 IQASLGG---HVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTfTTPGD-WTSGHVGAPLPCNHIKLVDAE 495
Cdd:cd05974 191 IQQDLASfdvKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVG-NSPGQpVKAGSMGRPLPGYRVALLDPD 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 496 ElnywTCKGEGEICV-----KGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAP 570
Cdd:cd05974 270 G----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SSDYRISP 343
|
170
....*....|....*...
gi 1907081036 571 EKIENIYIRSEPVAQIYV 588
Cdd:cd05974 344 FELESVLIEHPAVAEAAV 361
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
119-639 |
6.24e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 76.15 E-value: 6.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 119 QWLSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGS-ISYIINTAdict 197
Cdd:PRK12316 4575 EKLTYAELNRRANRLAHALIARG--VGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPL-DPEYPRErLAYMMEDS---- 4647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 198 vivdkphKATLLLEHveRKETPGLklvilmePFEDalrergkkcGVDIKSMQAIED-CGRENHHAPVPPRPDDLSIVCFT 276
Cdd:PRK12316 4648 -------GAALLLTQ--SHLLQRL-------PIPD---------GLASLALDRDEDwEGFPAHDPAVRLHPDNLAYVIYT 4702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 277 SGTTGNPKGAMLTHGNVVAdfsgFLKVTESQWAPTCADVHFSYLPLAhmFERMVQSV--VYCHGGRVgffqgdirLLSDD 354
Cdd:PRK12316 4703 SGSTGRPKGVAVSHGSLVN----HLHATGERYELTPDDRVLQFMSFS--FDGSHEGLyhPLINGASV--------VIRDD 4768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 355 MKALRPTIFpvvpRLLNRMYDKIFHQADTSLKRWLLEFAAKRKQAEVRsgiirnnsiwdelffnkiQASLGGHvrmivtG 434
Cdd:PRK12316 4769 SLWDPERLY----AEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLR------------------VYCFGGE------A 4820
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 435 AAPASPTVLgfLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSG----HVGAPLPCNHIKLVDaEELNYWTCKGEGEIC 509
Cdd:PRK12316 4821 VAQASYDLA--WRALKPVYLFNGYGPTETTVTVLlWKARDGDACGaaymPIGTPLGNRSGYVLD-GQLNPLPVGVAGELY 4897
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 510 VKGPNVFKGYLKDEDRTKEALDSD------GWLH-TGDIGKWLPEGTLKIIDRKKHI-----FKLAQGEYVAPEKiENIY 577
Cdd:PRK12316 4898 LGGEGVARGYLERPALTAERFVPDpfgapgGRLYrTGDLARYRADGVIDYLGRVDHQvkirgFRIELGEIEARLR-EHPA 4976
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081036 578 IRSEPVaqIYVHGdSLKAFLVGIVVP-DPEVMPSWAQKKGIEGTyqelcMKKELKKAILDDMV 639
Cdd:PRK12316 4977 VREAVV--IAQEG-AVGKQLVGYVVPqDPALADADEAQAELRDE-----LKAALRERLPEYMV 5031
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
86-639 |
9.59e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 75.58 E-value: 9.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 86 YDDARTMYQVFRRGLSISGNGPCLGFRKpeqpyQWLSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAEL 165
Cdd:PRK12467 1570 YPLARLVHQLIEDQAAATPEAVALVFGE-----QELTYGELNRRANRLAHRLIALG--VGPEVLVGIAVERSLEMVVGLL 1642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 166 ACYTYSMVVVPLYDTLGPGSISYIINTADIctvivdkphkaTLLLEH---VERKETP-GLKLVILmEPFEDALRergkkc 241
Cdd:PRK12467 1643 AILKAGGAYVPLDPEYPRERLAYMIEDSGI-----------ELLLTQshlQARLPLPdGLRSLVL-DQEDDWLE------ 1704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 242 gvdiksmqaiedcGRENHHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFsgflKVTESQWAPTCADVHFSYLP 321
Cdd:PRK12467 1705 -------------GYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRL----CATQEAYQLSAADVVLQFTS 1767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 322 LAhmFERMVQSVVY--CHGGRVgffqgdirLLSDDMKALRPTIFpvvPRLLNRMYDKIFHQADTSLKRwLLEFAAkrKQA 399
Cdd:PRK12467 1768 FA--FDVSVWELFWplINGARL--------VIAPPGAHRDPEQL---IQLIERQQVTTLHFVPSMLQQ-LLQMDE--QVE 1831
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 400 EVRSgiirnnsiwdelffnkiqaslgghVRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAG-----CTFTTPG 473
Cdd:PRK12467 1832 HPLS------------------------LRRVVCGGEALEVEALRPWLERLPdTGLFNLYGPTETAVDvthwtCRRKDLE 1887
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 474 DWTSGHVGAPLPCNHIKLVDAeELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEAL------DSDGWLH-TGDIGKWLP 546
Cdd:PRK12467 1888 GRDSVPIGQPIANLSTYILDA-SLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgTVGSRLYrTGDLARYRA 1966
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 547 EGTLKIIDRKKHIFKLaQGEYVAPEKIENiYIRSEP----VAQIYVHGDSLKAfLVGIVVPDPEVMPSWAQKKgieGTYQ 622
Cdd:PRK12467 1967 DGVIEYLGRIDHQVKI-RGFRIELGEIEA-RLREQGgvreAVVIAQDGANGKQ-LVAYVVPTDPGLVDDDEAQ---VALR 2040
|
570
....*....|....*..
gi 1907081036 623 ELcMKKELKKAILDDMV 639
Cdd:PRK12467 2041 AI-LKNHLKASLPEYMV 2056
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
107-610 |
3.60e-13 |
|
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: 72.13 E-value: 3.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 107 PCLgfRKPEQPYqwlSYQEVAKRAEFLGSGLLqHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSI 186
Cdd:cd05958 2 TCL--RSPEREW---TYRDLLALANRIANVLV-GELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 187 SYIINTADICTVIVDkphkatlllehverketpglklvilmepfeDALRERgkkcgvdiksmqaiedcgrenhhapvppr 266
Cdd:cd05958 76 AYILDKARITVALCA------------------------------HALTAS----------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 267 pDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF----LKVTESqwaptcaDVHFSYLPLAHMFERMVQSVVYCHGGR-- 340
Cdd:cd05958 97 -DDICILAFTSGTTGAPKATMHFHRDPLASADRYavnvLRLRED-------DRFVGSPPLAFTFGLGGVLLFPFGVGAsg 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 341 VGFFQGDIRLLSDDMKALRPTIFPVVPRllnrMYDKIFHQADTSlkrwllefaakrkqaevrsgiirnnsiwdelffnki 420
Cdd:cd05958 169 VLLEEATPDLLLSAIARYKPTVLFTAPT----AYRAMLAHPDAA------------------------------------ 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 421 qASLGGHVRMIVTgAAPASPTVLGFL-RAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNy 499
Cdd:cd05958 209 -GPDLSSLRKCVS-AGEALPAALHRAwKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVDDEGNP- 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 500 wTCKGE-GEICVKGPNvfkGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYI 578
Cdd:cd05958 286 -VPDGTiGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLL 360
|
490 500 510
....*....|....*....|....*....|....*
gi 1907081036 579 RSEPVAQIYVHGDSLKAFLV---GIVVPDPEVMPS 610
Cdd:cd05958 361 QHPAVAECAVVGHPDESRGVvvkAFVVLRPGVIPG 395
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
150-607 |
6.40e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 71.64 E-value: 6.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 150 VGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIVDKPHKATL--LLEHVERKETPGLKLVILM 227
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLdgLDPGVRVINVDSPAWADEL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 228 EPFEDALRErgkkcgvdiksmqaiedcgrenhhaPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVTESQ 307
Cdd:PRK07867 137 AAHRDAEPP-------------------------FRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVA--SAGVMLAQRFG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 308 WAPTcaDVHFSYLPLAHMFERMVQ-SVVYCHGGRV---------GFFqgdirllsDDMKALRPTIFPVVPRLLN------ 371
Cdd:PRK07867 190 LGPD--DVCYVSMPLFHSNAVMAGwAVALAAGASIalrrkfsasGFL--------PDVRRYGATYANYVGKPLSyvlatp 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 372 -RMYDkifhqADTSLKrwllefaakrkqaevrsgiirnnsiwdelffnkiqaslgghvrmIVTGAAPASPTVLGFlRAAL 450
Cdd:PRK07867 260 eRPDD-----ADNPLR--------------------------------------------IVYGNEGAPGDIARF-ARRF 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 451 GCQVYEGYGQTEctAGCTFTTPGDWTSGHVGaPLPCNhIKLVDAE--------------ELNYWTCKGEgEICVKGPNVF 516
Cdd:PRK07867 290 GCVVVDGFGSTE--GGVAITRTPDTPPGALG-PLPPG-VAIVDPDtgtecppaedadgrLLNADEAIGE-LVNTAGPGGF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 517 KGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYVHGdslkaf 596
Cdd:PRK07867 365 EGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPIERILLRYPDATEVAVYA------ 436
|
490
....*....|.
gi 1907081036 597 lvgivVPDPEV 607
Cdd:PRK07867 437 -----VPDPVV 442
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
261-624 |
1.12e-12 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 71.08 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 261 APVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGfLKvteSQWAPTCADVHFSYLPLAHMFERM--VQSVVychg 338
Cdd:PRK09274 167 PMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEA-LR---EDYGIEPGEIDLPTFPLFALFGPAlgMTSVI---- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 339 grvgffqgdirllsDDMKALRP-TIFPvvprllnrmyDKIFHQAD----TSLkrwlleFAA-----KRKQAEVRSGIIRN 408
Cdd:PRK09274 239 --------------PDMDPTRPaTVDP----------AKLFAAIErygvTNL------FGSpalleRLGRYGEANGIKLP 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 409 NsiwdelffnkiqaslgghVRMIVTGAAPASPTVLGFLRAAL--GCQVYEGYGQTECTAGCT-------FTTPGDWTSGH 479
Cdd:PRK09274 289 S------------------LRRVISAGAPVPIAVIERFRAMLppDAEILTPYGATEALPISSiesreilFATRAATDNGA 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 480 ---VGAPLPCNHIKLV--DAEELNYWT-----CKGE-GEICVKGPNVFKGYLKDEDRTKEA--LDSDG--WLHTGDIGkW 544
Cdd:PRK09274 351 gicVGRPVDGVEVRIIaiSDAPIPEWDdalrlATGEiGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLG-Y 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 545 L-PEGTLKIIDRKKHIFKLAQGEYVapekieniyirSEPVAQIY-VHGDSLKAFLVGIVVPD---P----EVMPSWAQKK 615
Cdd:PRK09274 430 LdAQGRLWFCGRKAHRVETAGGTLY-----------TIPCERIFnTHPGVKRSALVGVGVPGaqrPvlcvELEPGVACSK 498
|
....*....
gi 1907081036 616 giEGTYQEL 624
Cdd:PRK09274 499 --SALYQEL 505
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
429-606 |
1.58e-12 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 70.43 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 429 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHVGAPL-PCNHIKLVDAEELNywTCKGE- 505
Cdd:cd05920 258 RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTrLDDPDEVIIHTQGRPMsPDDEIRVVDEEGNP--VPPGEe 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 506 GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENiyirsepvaQ 585
Cdd:cd05920 336 GELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVEN---------L 405
|
170 180
....*....|....*....|.
gi 1907081036 586 IYVHGDSLKAFLVGivVPDPE 606
Cdd:cd05920 406 LLRHPAVHDAAVVA--MPDEL 424
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
121-606 |
1.91e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 70.11 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 200
Cdd:PRK13391 25 VTYRELDERSNRLAHLFRSLGLKRGDH--VAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALIT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 DKPHK--ATLLLEHVerketPGLKLVILMEPFEDalRERgkkcgvdiksMQAIEDCGRENHHAPVP--PRPDDLsivCFT 276
Cdd:PRK13391 103 SAAKLdvARALLKQC-----PGVRHRLVLDGDGE--LEG----------FVGYAEAVAGLPATPIAdeSLGTDM---LYS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 277 SGTTGNPKG--AMLTHGNVVaDFSGFLKVTESQWAPTCADVHFSYLPLAHMFERMVQSVVYCHGGRV----GFfqgdirl 350
Cdd:PRK13391 163 SGTTGRPKGikRPLPEQPPD-TPLPLTAFLQRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVivmeHF------- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 351 lsDDMKAL------RPTIFPVVPRLLNRMydkifhqadtsLKrwLLEfaAKRKQAEVRSgiirnnsiwdelffnkiqasl 424
Cdd:PRK13391 235 --DAEQYLalieeyGVTHTQLVPTMFSRM-----------LK--LPE--EVRDKYDLSS--------------------- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 425 gghVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCN-HIKLVDAEELNywt 501
Cdd:PRK13391 277 ---LEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATE-GLGFTACDSEEWLAhpGTVGRAMFGDlHILDDDGAELP--- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 502 cKGE-GEICVKGPNVFKgYLKDEDRTKEALDSDG-WLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIR 579
Cdd:PRK13391 350 -PGEpGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMI-ISGGVNIYPQEAENLLIT 426
|
490 500
....*....|....*....|....*..
gi 1907081036 580 SEPVAQIYVHGdslkaflvgivVPDPE 606
Cdd:PRK13391 427 HPKVADAAVFG-----------VPNED 442
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
271-686 |
1.99e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 70.12 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 271 SIVCFTSGTTGNPKGAMLTHGNvvadfsgflkvtesqwaptcadvhfsylplahmfermvqSVVYCHGGRvgffqgdirl 350
Cdd:PRK07008 179 SSLCYTSGTTGNPKGALYSHRS---------------------------------------TVLHAYGAA---------- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 351 LSDDMK-ALRPTIFPVVPrllnrmydkIFHqadtsLKRWLLEFAAKRKQAE-VRSG-IIRNNSIWDELFFNKIQASLG-- 425
Cdd:PRK07008 210 LPDAMGlSARDAVLPVVP---------MFH-----VNAWGLPYSAPLTGAKlVLPGpDLDGKSLYELIEAERVTFSAGvp 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 426 -------GHV----------RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPgdwTSGHVGAPLPCNH 488
Cdd:PRK07008 276 tvwlgllNHMreaglrfstlRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLCKL---KWKHSQLPLDEQR 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 489 --------------IKLVDAE--ELNyWTCKGEGEICVKGPNVFKGYLKDEDrtkEALDsDGWLHTGDIGKWLPEGTLKI 552
Cdd:PRK07008 353 kllekqgrviygvdMKIVGDDgrELP-WDGKAFGDLQVRGPWVIDRYFRGDA---SPLV-DGWFPTGDVATIDADGFMQI 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 553 IDRKKHIFKlAQGEYVAPEKIENIYIRSEPVAQIYVhgdslkaflvgIVVPDPEvmpsW--------AQKKGIEGTYQEL 624
Cdd:PRK07008 428 TDRSKDVIK-SGGEWISSIDIENVAVAHPAVAEAAC-----------IACAHPK----WderpllvvVKRPGAEVTREEL 491
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907081036 625 CMKKELKKA---ILDDMVMlgkesglhsfeqVKAIyihcdmfsvqngLLTPTLKAKRPELREYFK 686
Cdd:PRK07008 492 LAFYEGKVAkwwIPDDVVF------------VDAI------------PHTATGKLQKLKLREQFR 532
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
427-598 |
2.04e-12 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 70.19 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 427 HVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDaEELNYWTCKGEG 506
Cdd:cd05928 292 SLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIID-DNGNVLPPGTEG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 507 EICVK-GPN----VFKGYLKDEDRTKEALDSDGWLhTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSE 581
Cdd:cd05928 371 DIGIRvKPIrpfgLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYRIGPFEVESALIEHP 448
|
170 180
....*....|....*....|....
gi 1907081036 582 PVAQIYV-------HGDSLKAFLV 598
Cdd:cd05928 449 AVVESAVvsspdpiRGEVVKAFVV 472
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
86-639 |
2.23e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 71.14 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 86 YDDARTMYQVFRRGLSISGNGPCLGFRKpeqpyQWLSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAEL 165
Cdd:PRK12316 3053 YPLERGVHRLFEEQVERTPDAVALAFGE-----QRLSYAELNRRANRLAHRLIERG--VGPDVLVGVAVERSLEMVVGLL 3125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 166 ACYTYSMVVVPLYDTLGPGSISYIINTADIcTVIVDKPHkatLLLEHVERKEtpglklVILMEPFEDALRErgkkcgvdi 245
Cdd:PRK12316 3126 AILKAGGAYVPLDPEYPEERLAYMLEDSGA-QLLLSQSH---LRLPLAQGVQ------VLDLDRGDENYAE--------- 3186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 246 ksmqaiedcgrenHHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNvvadFSGFLKVTESQWAPTCADVHFSYLPLAHM 325
Cdd:PRK12316 3187 -------------ANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSA----LSNHLCWMQQAYGLGVGDRVLQFTTFSFD 3249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 326 FERMVQSVVYCHGGRVgfFQGDIRLLSDdmkalrptifpvvPRLLNRMYDKifHQADTSLKRWllefaakrkqaevrsgi 405
Cdd:PRK12316 3250 VFVEELFWPLMSGARV--VLAGPEDWRD-------------PALLVELINS--EGVDVLHAYP----------------- 3295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 406 irnnSIWDELFFNKIQASLGGHVRMIVTGAAPASPtvlGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGH--VGAP 483
Cdd:PRK12316 3296 ----SMLQAFLEEEDAHRCTSLKRIVCGGEALPAD---LQQQVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRP 3368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 484 LPCNHIKLVDAeELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGW------LHTGDIGKWLPEGTLKIIDRKK 557
Cdd:PRK12316 3369 IANRACYILDG-SLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVD 3447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 558 HIFKLaQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAfLVGIVVPDPEvmpswaqkkgiEGTYQELcMKKELKKAILDD 637
Cdd:PRK12316 3448 HQVKI-RGFRIELGEIEARLLEHPWVREAVVLAVDGRQ-LVAYVVPEDE-----------AGDLREA-LKAHLKASLPEY 3513
|
..
gi 1907081036 638 MV 639
Cdd:PRK12316 3514 MV 3515
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
109-607 |
2.71e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 69.67 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 109 LGFRKPEQPYQWLSY-QEVAKRAEFLgSGLLQHDCKVgteqFVGVFAQNRPEWII----AELACYTysmvVVPLYDTLGP 183
Cdd:PRK13388 18 IAVRYGDRTWTWREVlAEAAARAAAL-IALADPDRPL----HVGVLLGNTPEMLFwlaaAALGGYV----LVGLNTTRRG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 184 GSISYIINTADICTVIVDKPHKAtlLLEHVErkeTPGLKLVILMEPfedALRERgkkcgvdiksmqaIEDCGRENHHAPV 263
Cdd:PRK13388 89 AALAADIRRADCQLLVTDAEHRP--LLDGLD---LPGVRVLDVDTP---AYAEL-------------VAAAGALTPHREV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 264 PPrpDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVteSQWAPTCADVHFSYLPLAHMFERMVQ-SVVYCHGGRVg 342
Cdd:PRK13388 148 DA--MDPFMLIFTSGTTGAPKAVRCSHGRLA--FAGRALT--ERFGLTRDDVCYVSMPLFHSNAVMAGwAPAVASGAAV- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 343 ffqgdirllsddmkALRPTifpvvprllnrmydkifhqadtslkrwlleFAAKRKQAEVRSgiirnnsiWDELFFNKIQA 422
Cdd:PRK13388 221 --------------ALPAK------------------------------FSASGFLDDVRR--------YGATYFNYVGK 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 423 SLGghvRMIVTGAAP---ASPTVLGFLRAA-----------LGCQVYEGYGQTEctAGCTFTTPGDWTSGHVGAPLPcnH 488
Cdd:PRK13388 249 PLA---YILATPERPddaDNPLRVAFGNEAsprdiaefsrrFGCQVEDGYGSSE--GAVIVVREPGTPPGSIGRGAP--G 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 489 IKLVDAEELNywTC---------------KGEGEICVK-GPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKI 552
Cdd:PRK13388 322 VAIYNPETLT--ECavarfdahgallnadEAIGELVNTaGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYF 398
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1907081036 553 IDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYVHGdslkaflvgivVPDPEV 607
Cdd:PRK13388 399 AGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYA-----------VPDERV 441
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
121-293 |
3.00e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 69.53 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 200
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGPGDH--VGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 DK---PHKATLLlehverKETPGLKLVILMEpfeDALRERGKKCGVDIKSMQAIEDCGREnhhaPVPPRPDDLSIVCfTS 277
Cdd:PRK07798 107 ERefaPRVAEVL------PRLPKLRTLVVVE---DGSGNDLLPGAVDYEDALAAGSPERD----FGERSPDDLYLLY-TG 172
|
170
....*....|....*.
gi 1907081036 278 GTTGNPKGAMLTHGNV 293
Cdd:PRK07798 173 GTTGMPKGVMWRQEDI 188
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
504-559 |
3.86e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 69.21 E-value: 3.86e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081036 504 GE--GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHI 559
Cdd:PRK08162 385 GEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDI 441
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
261-598 |
4.29e-12 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 69.10 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 261 APVPPRPDDLSIVCFTSGTTGNPKGAMLTHGN--VVADFSG--FLKVTESQWAPTCADVHFSY-LPLAHMFERMVQSVVY 335
Cdd:TIGR02262 154 KPAATQADDPAFWLYSSGSTGMPKGVVHTHSNpyWTAELYArnTLGIREDDVCFSAAKLFFAYgLGNALTFPMSVGATTV 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 336 CHGGR---VGFFqgdirllsDDMKALRPTIFPVVPRLLNRMYdkifhqADTSLKrwllefaaKRKQAEVRsgiirnnsiw 412
Cdd:TIGR02262 234 LMGERptpDAVF--------DRLRRHQPTIFYGVPTLYAAML------ADPNLP--------SEDQVRLR---------- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 413 delffnkiqaslgghvrmIVTGAAPASPTVLGF-LRAALGCQVYEGYGQTEctAGCTFTT--PGDWTSGHVGAPLPCNHI 489
Cdd:TIGR02262 282 ------------------LCTSAGEALPAEVGQrWQARFGVDIVDGIGSTE--MLHIFLSnlPGDVRYGTSGKPVPGYRL 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 490 KLVDaeELNYWTCKGE-GEICVKGPNVFKGYLKDEDRTKEALDSdGWLHTGDigKWL--PEGTLKIIDRKKHIFKLAqGE 566
Cdd:TIGR02262 342 RLVG--DGGQDVADGEpGELLISGPSSATMYWNNRAKSRDTFQG-EWTRSGD--KYVrnDDGSYTYAGRTDDMLKVS-GI 415
|
330 340 350
....*....|....*....|....*....|....*....
gi 1907081036 567 YVAPEKIENIYIRSEPVAQIYVHG----DSL---KAFLV 598
Cdd:TIGR02262 416 YVSPFEIESALIQHPAVLEAAVVGvadeDGLikpKAFVV 454
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
121-613 |
4.43e-12 |
|
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: 68.82 E-value: 4.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLLqhDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGS-ISYIINTADictvi 199
Cdd:cd17652 13 LTYAELNARANRLARLLA--ARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPL-DPAYPAErIAYMLADAR----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 200 vdkphkATLLLEHverketpglklvilmepfedalrergkkcgvdiksmqaiedcgrenhhapvpprPDDLSIVCFTSGT 279
Cdd:cd17652 85 ------PALLLTT------------------------------------------------------PDNLAYVIYTSGS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 280 TGNPKGAMLTH---GNVVADFSGFLKVTE----SQWAPTCADVHFSYLPLAhmfermvqsvvYCHGGRVGFFQGDIRL-- 350
Cdd:cd17652 105 TGRPKGVVVTHrglANLAAAQIAAFDVGPgsrvLQFASPSFDASVWELLMA-----------LLAGATLVLAPAEELLpg 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 351 --LSDDMKALRPTIFPVVPRLLNRMYDkifhqadtslkrwllefaakrkqaevrsgiirnnsiwDELffnkiqasLGGHV 428
Cdd:cd17652 174 epLADLLREHRITHVTLPPAALAALPP-------------------------------------DDL--------PDLRT 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 429 rMIVTGAAPASPTVLgflRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLVDAeELNYWTCKGEGE 507
Cdd:cd17652 209 -LVVAGEACPAELVD---RWAPGRRMINAYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYVLDA-RLRPVPPGVPGE 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 508 ICVKGPNVFKGYLKDEDRTKEALDSD------GWLH-TGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRS 580
Cdd:cd17652 284 LYIAGAGLARGYLNRPGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKI-RGFRIELGEVEAALTEH 362
|
490 500 510
....*....|....*....|....*....|....*.
gi 1907081036 581 EPVAQ--IYVHGDSL-KAFLVGIVVPDPEVMPSWAQ 613
Cdd:cd17652 363 PGVAEavVVVRDDRPgDKRLVAYVVPAPGAAPTAAE 398
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
440-588 |
5.71e-12 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 68.36 E-value: 5.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 440 PTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTSGhVGAPLPCNHIKLVDaeelnywtckgeGEICVKGPNVFKGY 519
Cdd:PRK09029 253 PVELTEQAEQQGIRCWCGYGLTE-MASTVCAKRADGLAG-VGSPLPGREVKLVD------------GEIWLRGASLALGY 318
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081036 520 LKDeDRTKEALDSDGWLHTGDIGKWLpEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYV 588
Cdd:PRK09029 319 WRQ-GQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQVFV 384
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
267-578 |
7.18e-12 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 68.30 E-value: 7.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWAPTCADVHFSYLPLAHMFermvqsvvychggrvGFfqG 346
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKF----FSPKEDDVMMSFLPPFHAY---------------GF--N 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 347 DIRLLSddMKALRPTIF---PVVPRLLNRMYDK---IFHQADTSLKRWLLEFAAKRKQA--EVRSGIIRNNSIWDELFfn 418
Cdd:PRK06334 241 SCTLFP--LLSGVPVVFaynPLYPKKIVEMIDEakvTFLGSTPVFFDYILKTAKKQESClpSLRFVVIGGDAFKDSLY-- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 419 kiqaslgghvrmivTGAAPASPTVlgflraalgcQVYEGYGQTECTAGCTFTT---PGDwtSGHVGAPLPCNHIKLVdAE 495
Cdd:PRK06334 317 --------------QEALKTFPHI----------QLRQGYGTTECSPVITINTvnsPKH--ESCVGMPIRGMDVLIV-SE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 496 ELNYWTCKGE-GEICVKGPNVFKGYL-KDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKI 573
Cdd:PRK06334 370 ETKVPVSSGEtGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSLEAL 448
|
....*
gi 1907081036 574 ENIYI 578
Cdd:PRK06334 449 ESILM 453
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
274-590 |
1.22e-11 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 67.85 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 274 CFTSGTTGNPKGAMLTH-GNVVadfsgflkvtesqwaptcadvhfsylplahmfermvQSVVYCHGGRVGFFQGDirlls 352
Cdd:PRK06018 183 CYTSGTTGDPKGVLYSHrSNVL------------------------------------HALMANNGDALGTSAAD----- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 353 ddmkalrpTIFPVVPrllnrmydkIFHQadtslKRWLLEFAAKRKQAE-VRSGI-IRNNSIWDELFFNKIQASLG----- 425
Cdd:PRK06018 222 --------TMLPVVP---------LFHA-----NSWGIAFSAPSMGTKlVMPGAkLDGASVYELLDTEKVTFTAGvptvw 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 426 --------------GHVRMIVTGAApASPTvlGFLRA--ALGCQVYEGYGQTECTAGCTFTT--------PGDWTSGHV- 480
Cdd:PRK06018 280 lmllqymekeglklPHLKMVVCGGS-AMPR--SMIKAfeDMGVEVRHAWGMTEMSPLGTLAAlkppfsklPGDARLDVLq 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 481 --GAPLPCNHIKLVD--AEELNyWTCKGEGEICVKGPNVFKGYLKDEDrtkEALDSDGWLHTGDIGKWLPEGTLKIIDRK 556
Cdd:PRK06018 357 kqGYPPFGVEMKITDdaGKELP-WDGKTFGRLKVRGPAVAAAYYRVDG---EILDDDGFFDTGDVATIDAYGYMRITDRS 432
|
330 340 350
....*....|....*....|....*....|....
gi 1907081036 557 KHIFKlAQGEYVAPEKIENIYIRSEPVAQIYVHG 590
Cdd:PRK06018 433 KDVIK-SGGEWISSIDLENLAVGHPKVAEAAVIG 465
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
255-606 |
1.84e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 67.26 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 255 GRENHHAPVPPRPDdlSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLkvtesqwaptcadvhfSYLPLaHMFERMVQSVV 334
Cdd:PRK07788 196 GSSTAPLPKPPKPG--GIVILTSGTTGTPKGAPRPEPSPLAPLAGLL----------------SRVPF-RAGETTLLPAP 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 335 YCHGgrVGFFQGDIRLlsddmkALRPTIfpVVPRLL---NRMYDKIFHQAD------TSLKRwLLEFAAKRKQA-EVRSg 404
Cdd:PRK07788 257 MFHA--TGWAHLTLAM------ALGSTV--VLRRRFdpeATLEDIAKHKATalvvvpVMLSR-ILDLGPEVLAKyDTSS- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 405 iirnnsiwdelffnkiqaslgghVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECtAGCTFTTPGDWT--SGHVGA 482
Cdd:PRK07788 325 -----------------------LKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEV-AFATIATPEDLAeaPGTVGR 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 483 PLPCNHIKLVDAE--ELNywtcKGE-GEICVKGPNVFKGYLkdEDRTKEALdsDGWLHTGDIGKWLPEGTLKIIDRKKHI 559
Cdd:PRK07788 381 PPKGVTVKILDENgnEVP----RGVvGRIFVGNGFPFEGYT--DGRDKQII--DGLLSSGDVGYFDEDGLLFVDGRDDDM 452
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1907081036 560 FkLAQGEYVAPEKIENIYIRSEPVAQIYVHGdslkaflvgivVPDPE 606
Cdd:PRK07788 453 I-VSGGENVFPAEVEDLLAGHPDVVEAAVIG-----------VDDEE 487
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
121-607 |
2.01e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 66.96 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLlqHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIv 200
Cdd:PRK13390 25 VSYRQLDDDSAALARVL--YDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLV- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 dkphkATLLLEHVERKETPGLKLVILM-------EPFEDALRERGKKCgvdiksmqAIEDCGrenhhapvpprpddlSIV 273
Cdd:PRK13390 102 -----ASAALDGLAAKVGADLPLRLSFggeidgfGSFEAALAGAGPRL--------TEQPCG---------------AVM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 274 CFTSGTTGNPKG--------AMLTHGN-VVADFSGFLKVTESqwaptcaDVHFSYLPLAHMFERMVQSVVYCHGGRVGFF 344
Cdd:PRK13390 154 LYSSGTTGFPKGiqpdlpgrDVDAPGDpIVAIARAFYDISES-------DIYYSSAPIYHAAPLRWCSMVHALGGTVVLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 345 QG-DIRLLSDDMKALRPTIFPVVPRLLNRMYdkifhqadtslkrwllefaakRKQAEVRSGiirnnsiWDelffnkiQAS 423
Cdd:PRK13390 227 KRfDAQATLGHVERYRITVTQMVPTMFVRLL---------------------KLDADVRTR-------YD-------VSS 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 424 LgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVG-APLPCNHIKLVDAEELNyw 500
Cdd:PRK13390 272 L----RAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGrSVLGDLHICDDDGNELP-- 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 501 tcKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDG--WLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIY 577
Cdd:PRK13390 345 --AGRiGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQETENAL 421
|
490 500 510
....*....|....*....|....*....|
gi 1907081036 578 IRSEPVAQIYVHGdslkaflvgivVPDPEV 607
Cdd:PRK13390 422 TMHPAVHDVAVIG-----------VPDPEM 440
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
118-598 |
2.41e-11 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 66.79 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 118 YQWLsyqEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICT 197
Cdd:PLN02479 46 YTWA---QTYQRCRRLASALAKRS--IGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 198 VIVDKP--HKATLLLEHVERKETPGLKLVILM---------EPFEDALReRGKkcgvdIKSMQAIEDCGREnhHAPVPPR 266
Cdd:PLN02479 121 VMVDQEffTLAEEALKILAEKKKSSFKPPLLIvigdptcdpKSLQYALG-KGA-----IEYEKFLETGDPE--FAWKPPA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 267 PDDLSIVC-FTSGTTGNPKGAMLTH-GNVVADFSGFLKvtesqWAPTCADVHFSYLPLAHmfermvqsvvyCHGGrvgFF 344
Cdd:PLN02479 193 DEWQSIALgYTSGTTASPKGVVLHHrGAYLMALSNALI-----WGMNEGAVYLWTLPMFH-----------CNGW---CF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 345 QGDIRLLSDDMKALRPTIFPVVprllnrmYDKIFHQADTslkrwllEFAAkrkqAEVRSGIIRNNSIWDELFfnkiqaSL 424
Cdd:PLN02479 254 TWTLAALCGTNICLRQVTAKAI-------YSAIANYGVT-------HFCA----APVVLNTIVNAPKSETIL------PL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 425 GGHVRMIVTGAAPaSPTVLgFLRAALGCQVYEGYGQTEcTAG----CTFTTPGDWTSGHVGAPLPCNH---------IKL 491
Cdd:PLN02479 310 PRVVHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSE-TYGpstvCAWKPEWDSLPPEEQARLNARQgvryiglegLDV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 492 VDAEELNYWTCKGE--GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVA 569
Cdd:PLN02479 387 VDTKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGGENIS 464
|
490 500
....*....|....*....|....*....
gi 1907081036 570 PEKIENIyirsepvaqIYVHGDSLKAFLV 598
Cdd:PLN02479 465 SLEVENV---------VYTHPAVLEASVV 484
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
86-613 |
4.04e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 66.90 E-value: 4.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 86 YDDARTMYQVFRRGLSISGNGPCLGFRKpeqpyQWLSYQEVAKRAEFLGSGLLQhdCKVGTEQFVGVFAQNRPEWIIAEL 165
Cdd:PRK12316 507 YPLQRGVHRLFEEQVERTPEAPALAFGE-----ETLDYAELNRRANRLAHALIE--RGVGPDVLVGVAMERSIEMVVALL 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 166 ACYTYSMVVVPLYDTLGPGSISYIINTADIctvivdkphkATLLLEHVERKETP---GLKLVILMEP--FEDALRERGKK 240
Cdd:PRK12316 580 AILKAGGAYVPLDPEYPAERLAYMLEDSGV----------QLLLSQSHLGRKLPlaaGVQVLDLDRPaaWLEGYSEENPG 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 241 CGVDiksmqaiedcgrenhhapvpprPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKV-------TESQWAPTCA 313
Cdd:PRK12316 650 TELN----------------------PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAyglgvgdTVLQKTPFSF 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 314 DVHFS--YLPLAhmfermvqsvvycHGGR-VGFFQGDIRllsdDMKALrptifpvvPRLLNRmydkifHQADTslkrwlL 390
Cdd:PRK12316 708 DVSVWefFWPLM-------------SGARlVVAAPGDHR----DPAKL--------VELINR------EGVDT------L 750
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 391 EFAAKRKQAEVRSGIIrnnsiwdelffnkiqASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFT 470
Cdd:PRK12316 751 HFVPSMLQAFLQDEDV---------------ASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHW 815
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 471 TPGDWTSGHV--GAPLPCNHIKLVDAeELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEAL------DSDGWLHTGDIG 542
Cdd:PRK12316 816 TCVEEGGDSVpiGRPIANLACYILDA-NLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFvpspfvAGERMYRTGDLA 894
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081036 543 KWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAfLVGIVVPD------PEVMPSWAQ 613
Cdd:PRK12316 895 RYRADGVIEYAGRIDHQVKL-RGLRIELGEIEARLLEHPWVREAAVLAVDGKQ-LVGYVVLEseggdwREALKAHLA 969
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
429-610 |
6.92e-11 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 65.10 E-value: 6.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 429 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCNHIKLVDAE--ELNywtcKG 504
Cdd:PRK12406 274 RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE-SGAVTFATSEDALShpGTVGKAAPGAELRFVDEDgrPLP----QG 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 505 E-GEICVKGPNV--FKGYLKDEDRTkeALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSE 581
Cdd:PRK12406 349 EiGEIYSRIAGNpdFTYHNKPEKRA--EIDRGGFITSGDVGYLDADGYLFLCDRKRDMV-ISGGVNIYPAEIEAVLHAVP 425
|
170 180 190
....*....|....*....|....*....|..
gi 1907081036 582 PVAQIYVHGDSLKAF---LVGIVVPDPEVMPS 610
Cdd:PRK12406 426 GVHDCAVFGIPDAEFgeaLMAVVEPQPGATLD 457
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
121-614 |
6.92e-11 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 65.41 E-value: 6.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 200
Cdd:PRK05857 42 LRYRELVAEVGGLAADLRAQSVSRGSR--VLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 DKPHKatlllehVERKETPGLKLVILMEPFEDALRERGKKCGVDIKSMQAIEDCGrenhhapvpprPDDLSIVCFTSGTT 280
Cdd:PRK05857 120 APGSK-------MASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNADQG-----------SEDPLAMIFTSGTT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 281 GNPKGAMLTHGNVVAdFSGFLKVTESQWAPTCA-DVHFSYLPLAHMfeRMVQSVVYC--HGGR--VGFFQGD--IRLLSD 353
Cdd:PRK05857 182 GEPKAVLLANRTFFA-VPDILQKEGLNWVTWVVgETTYSPLPATHI--GGLWWILTClmHGGLcvTGGENTTslLEILTT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 354 DMKALRPtifpVVPRLLNRMYDKIfhqadtslkrwllefaakrkqaevrsgiirnnsiwdelffnKIQASLGGHVRMIVT 433
Cdd:PRK05857 259 NAVATTC----LVPTLLSKLVSEL-----------------------------------------KSANATVPSLRLVGY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 434 GAAPASPTVLGFLRAA--LGCQVYeGYGQTECTAGCTFTTPGDWT---SGHVGAPLPCNHIKLVDAEELNYWTCKGE--- 505
Cdd:PRK05857 294 GGSRAIAADVRFIEATgvRTAQVY-GLSETGCTALCLPTDDGSIVkieAGAVGRPYPGVDVYLAATDGIGPTAPGAGpsa 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 506 --GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIyirSEPV 583
Cdd:PRK05857 373 sfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGGVNIAPDEVDRI---AEGV 447
|
490 500 510
....*....|....*....|....*....|....*..
gi 1907081036 584 AQI-----YVHGDSLKAFLVGI-VVPDPEVMPSWAQK 614
Cdd:PRK05857 448 SGVreaacYEIPDEEFGALVGLaVVASAELDESAARA 484
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
121-606 |
1.10e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 64.54 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLLQHDCKVGteQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 200
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREG--DVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 DKPHKATL--LLEHVERketpGLKLVILM-------EPFEDALrergkkcgvDIKSMQAIEDcgrenhhapVPPRPDDLs 271
Cdd:PRK08276 90 SAALADTAaeLAAELPA----GVPLLLVVagpvpgfRSYEEAL---------AAQPDTPIAD---------ETAGADML- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 272 ivcFTSGTTGNPKGAM--LTHGNVVADFSGFLKVTeSQWAPTCAD-VHFSYLPLAH----MFERMVQSvvycHGGRV--- 341
Cdd:PRK08276 147 ---YSSGTTGRPKGIKrpLPGLDPDEAPGMMLALL-GFGMYGGPDsVYLSPAPLYHtaplRFGMSALA----LGGTVvvm 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 342 -GFfqgdirllsDDMKAL------RPTIFPVVPRLLNRMydkifhqadtsLKrwLLEfaakrkqaEVRSGiirnnsiWDe 414
Cdd:PRK08276 219 eKF---------DAEEALalieryRVTHSQLVPTMFVRM-----------LK--LPE--------EVRAR-------YD- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 415 lffnkiQASLgghvRMIVTGAAPASPTVLgflRAAL---GCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCN-H 488
Cdd:PRK08276 261 ------VSSL----RVAIHAAAPCPVEVK---RAMIdwwGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGEvR 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 489 IKLVDAEELNywtcKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGkWLPE-GTLKIIDRKKHIFkLAQGE 566
Cdd:PRK08276 327 ILDEDGNELP----PGEiGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVG-YLDEdGYLYLTDRKSDMI-ISGGV 400
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1907081036 567 YVAPEKIENIYIRSEPVAQIYVHGdslkaflvgivVPDPE 606
Cdd:PRK08276 401 NIYPQEIENLLVTHPKVADVAVFG-----------VPDEE 429
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
435-606 |
1.80e-10 |
|
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: 63.94 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 435 AAPASPTVLGFLRAALGCQVYEGYGQTECTaGCTFTTPGDWTS--GHVGAPLPCN-HIKLVDAEELNYWTckgEGEICVK 511
Cdd:cd05929 253 AAPCPPWVKEQWIDWGGPIIWEYYGGTEGQ-GLTIINGEEWLThpGSVGRAVLGKvHILDEDGNEVPPGE---IGEVYFA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 512 GPNVFKgYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRsepvaqiyvHGD 591
Cdd:cd05929 329 NGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIA---------HPK 397
|
170
....*....|....*
gi 1907081036 592 SLKAFLVGivVPDPE 606
Cdd:cd05929 398 VLDAAVVG--VPDEE 410
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
119-613 |
2.44e-10 |
|
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: 63.16 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 119 QWLSYQEVAKRAEFLGSGLLQHdcKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIIntadictv 198
Cdd:cd17649 11 QSLSYAELDARANRLAHRLRAL--GVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 199 ivdkphkatlllehverkETPGLKLVIlmepfedalrergkkcgvdiksmqaiedcgreNHHapvpprPDDLSIVCFTSG 278
Cdd:cd17649 81 ------------------EDSGAGLLL--------------------------------THH------PRQLAYVIYTSG 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 279 TTGNPKGAMLTHGNVVAdfsgFLKVTESQWAPTCADV--HFSYLPLAHMFERMVQSVVycHGGRVgffqgdirllsddmk 356
Cdd:cd17649 105 STGTPKGVAVSHGPLAA----HCQATAERYGLTPGDRelQFASFNFDGAHEQLLPPLI--CGACV--------------- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 357 ALRPTIFPVVPRLLNRMYDK----IFHQADTSLKRWLLEFAAKrkqaevrsgiirnnsiwdelffnkiQASLGGHVRMIV 432
Cdd:cd17649 164 VLRPDELWASADELAEMVRElgvtVLDLPPAYLQQLAEEADRT-------------------------GDGRPPSLRLYI 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 433 TGAAPASPTvlgFLRAALGCQVY--EGYGQTECTAGCT-FTTPGD----WTSGHVGAPLPCNHIKLVDAeELNYWTCKGE 505
Cdd:cd17649 219 FGGEALSPE---LLRRWLKAPVRlfNAYGPTEATVTPLvWKCEAGaaraGASMPIGRPLGGRSAYILDA-DLNPVPVGVT 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 506 GEICVKGPNVFKGYLKDEDRTKEAL--DSDG-----WLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYI 578
Cdd:cd17649 295 GELYIGGEGLARGYLGRPELTAERFvpDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-RGFRIELGEIEAALL 373
|
490 500 510
....*....|....*....|....*....|....*....
gi 1907081036 579 RSEPVAQIYV---HGDSLKAfLVGIVVP-DPEVMPSWAQ 613
Cdd:cd17649 374 EHPGVREAAVvalDGAGGKQ-LVAYVVLrAAAAQPELRA 411
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
267-609 |
2.67e-10 |
|
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: 63.19 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSG--FLKVTESQwaptcADVHFSYLPLAHMFERMVQSVVYCHGGRV 341
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVnlrTSLSEryFGRDNGDE-----AVLFFSNYVFDFFVEQMTLALLNGQKLVV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 342 --GFFQGDIRLLSDDMKALRPTIFPVVPRLLnRMYDkiFHQAdTSLKRWLL---EFAAKRkqaevrsgiirnnsiwdelf 416
Cdd:cd17648 168 ppDEMRFDPDRFYAYINREKVTYLSGTPSVL-QQYD--LARL-PHLKRVDAageEFTAPV-------------------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 417 FNKIQASLGGhvrmivtgaapasptvlgflraalgcQVYEGYGQTEC--TAGCTFTTPGDWTSGHVGAPLPCNHIKLVDA 494
Cdd:cd17648 224 FEKLRSRFAG--------------------------LIINAYGPTETtvTNHKRFFPGDQRFDKSLGRPVRNTKCYVLND 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 495 EeLNYWTCKGEGEICVKGPNVFKGYLKDEDRTKE-------------ALDSDGWLH-TGDIGKWLPEGTLKIIDRKKHIF 560
Cdd:cd17648 278 A-MKRVPVGAVGELYLGGDGVARGYLNRPELTAErflpnpfqteqerARGRNARLYkTGDLVRWLPSGELEYLGRNDFQV 356
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081036 561 KLaQGEYVAPEKIENIY-----IRSEPVAQIYVHGDSLKA---FLVGIVVPDPEVMP 609
Cdd:cd17648 357 KI-RGQRIEPGEVEAALasypgVRECAVVAKEDASQAQSRiqkYLVGYYLPEPGHVP 412
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
121-557 |
2.99e-10 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 63.49 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGS-ISYI------INTA 193
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALGLKPGDR--VALIAETDGDFVEAFFACQYAGLVPVPLPLPMGFGGrESYIaqlrgmLASA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 194 DICTVIVDKphkatLLLEHVErKETPGLKLVILMEPFEDALRERGkkcGVDIKsmqaiedcgrenhhapvPPRPDDLSIV 273
Cdd:PRK09192 128 QPAAIITPD-----ELLPWVN-EATHGNPLLHVLSHAWFKALPEA---DVALP-----------------RPTPDDIAYL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 274 CFTSGTTGNPKGAMLTHGNVVADFSGF----LKVTEsqwaptcADVHFSYLPLAH-MfermvqsvvychgGRVGFF---- 344
Cdd:PRK09192 182 QYSSGSTRFPRGVIITHRALMANLRAIshdgLKVRP-------GDRCVSWLPFYHdM-------------GLVGFLltpv 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 345 --QgdirlLSDDMkaLRPTIFPVVP----RLLNR-----MYDKIFHqadtslkrwlLEFAAKRkqAEVRSGIIRNNSIWd 413
Cdd:PRK09192 242 atQ-----LSVDY--LPTRDFARRPlqwlDLISRnrgtiSYSPPFG----------YELCARR--VNSKDLAELDLSCW- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 414 elffnkiqaslgghvRMIVTGAAPASPTVL----------GF-LRAALGCqvyegYGQTECTAGCTFTTPG--------- 473
Cdd:PRK09192 302 ---------------RVAGIGADMIRPDVLhqfaeafapaGFdDKAFMPS-----YGLAEATLAVSFSPLGsgivveevd 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 474 -DWTSGH------------------VGAPLPCNHIKLVDA--EELNYwtcKGEGEICVKGPNVFKGYLKDEDRTKeALDS 532
Cdd:PRK09192 362 rDRLEYQgkavapgaetrrvrtfvnCGKALPGHEIEIRNEagMPLPE---RVVGHICVRGPSLMSGYFRDEESQD-VLAA 437
|
490 500
....*....|....*....|....*
gi 1907081036 533 DGWLHTGDIGkWLPEGTLKIIDRKK 557
Cdd:PRK09192 438 DGWLDTGDLG-YLLDGYLYITGRAK 461
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
267-610 |
3.53e-10 |
|
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: 62.84 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKV---TES----QWAPTCADVHFSYLplahmfermvqSVVYCHGG 339
Cdd:cd17644 105 PENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEygiTSSdrvlQFASIAFDVAAEEI-----------YVTLLSGA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 340 RVgffqgdirllsddmkALRPT-IFPVVPRllnrMYDKIfhqadtslkrwllefaaKRKQAEVRSgiiRNNSIWDELFFN 418
Cdd:cd17644 174 TL---------------VLRPEeMRSSLED----FVQYI-----------------QQWQLTVLS---LPPAYWHLLVLE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 419 KIQASLGG--HVRMIVTGAAPASPTVLGFLRAALG--CQVYEGYGQTECTAGCTFTTPGDWTSGH-----VGAPLPCNHI 489
Cdd:cd17644 215 LLLSTIDLpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIANTQV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 490 KLVDaEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLH--------TGDIGKWLPEGTLKIIDRKKHIFK 561
Cdd:cd17644 295 YILD-ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVK 373
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1907081036 562 LaQGEYVAPEKIENIYIRSEPVAQ--IYVHGDSL-KAFLVGIVVPDPEVMPS 610
Cdd:cd17644 374 I-RGFRIELGEIEAVLSQHNDVKTavVIVREDQPgNKRLVAYIVPHYEESPS 424
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
267-614 |
4.55e-10 |
|
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: 62.19 E-value: 4.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVTESQWAPTCADVHFSYLPLAhmFERMVQSVV--YCHGGRVGFF 344
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLV----NLCEWHRPYFGVTPADKSLVYASFS--FDASAWEIFphLTAGAALHVV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 345 QGDIRLlsdDMKALrptifpvvprllnrmyDKIFHQADTSLKRWLLEFAAKRKQAEvrsgiirNNSIwdelffnkiqasl 424
Cdd:cd17645 177 PSERRL---DLDAL----------------NDYFNQEGITISFLPTGAAEQFMQLD-------NQSL------------- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 425 gghvRMIVTGAapaspTVLGFLRAAlGCQVYEGYGQTECTAGCT-FTTPGDWTSGHVGAPLPCNHIKLVDaEELNYWTCK 503
Cdd:cd17645 218 ----RVLLTGG-----DKLKKIERK-GYKLVNNYGPTENTVVATsFEIDKPYANIPIGKPIDNTRVYILD-EALQLQPIG 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 504 GEGEICVKGPNVFKGYLKDEDRTKEALDSDGWL------HTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIY 577
Cdd:cd17645 287 VAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIEPFL 365
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1907081036 578 IRSEPV---AQIYVHGDSLKAFLVGIVVP----DPEVMPSWAQK 614
Cdd:cd17645 366 MNHPLIelaAVLAKEDADGRKYLVAYVTApeeiPHEELREWLKN 409
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
121-635 |
7.07e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 62.22 E-value: 7.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLLQHDCKVGTEQFVgvFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADiCTVIV 200
Cdd:PRK04319 74 YTYKELKELSNKFANVLKELGVEKGDRVFI--FMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSE-AKVLI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 DKPhkatLLLEHVERKETPGLKLVILMepfeDALRERGKKCgVDIKSM--QAIEDCgrenhhAPVPPRPDDLSIVCFTSG 278
Cdd:PRK04319 151 TTP----ALLERKPADDLPSLKHVLLV----GEDVEEGPGT-LDFNALmeQASDEF------DIEWTDREDGAILHYTSG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 279 TTGNPKGAMLTHGNVVADF-SGF----LKVTESQWaptC-ADVHF----SY---LPLAHmferMVQSVVYchGGRvgfFQ 345
Cdd:PRK04319 216 STGKPKGVLHVHNAMLQHYqTGKyvldLHEDDVYW---CtADPGWvtgtSYgifAPWLN----GATNVID--GGR---FS 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 346 GD--IRLLSDdmkaLRPTIF---PVVPRLLNRMYDKIFHQADTSlkrwllefaakrkqaevrsgiirnnsiwdelffnki 420
Cdd:PRK04319 284 PErwYRILED----YKVTVWytaPTAIRMLMGAGDDLVKKYDLS------------------------------------ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 421 qaslggHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPCNHIKLVDAEElNY 499
Cdd:PRK04319 324 ------SLRHILSVGEPLNPEVVRWGMKVFGLPIHDNWWMTETGGIMIANYPAmDIKPGSMGKPLPGIEAAIVDDQG-NE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 500 WTCKGEGEICVKG--PNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIY 577
Cdd:PRK04319 397 LPPNRMGNLAIKKgwPSMMRGIWNNPEKYESYF-AGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTS-GERVGPFEVESKL 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081036 578 IRSEPVAQIYVhgdslkaflvgIVVPDP---EVMPSW-AQKKGIEGTyqelcmkKELKKAIL 635
Cdd:PRK04319 475 MEHPAVAEAGV-----------IGKPDPvrgEIIKAFvALRPGYEPS-------EELKEEIR 518
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
268-592 |
5.87e-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: 59.02 E-value: 5.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 268 DDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVTESQwapTCADVHFSYLPLAHM-FERMVQSVV--YCHGGRvgff 344
Cdd:cd17656 128 DDLLYIIYTSGTTGKPKGVQLEHKNMV----NLLHFEREK---TNINFSDKVLQFATCsFDVCYQEIFstLLSGGT---- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 345 qgdIRLLSDDMKALRPTIFPVVPRllnrmydkifHQADT-SLKRWLLEFAAKRKQAEVRsgiirnnsiwdelFFNKIQAS 423
Cdd:cd17656 197 ---LYIIREETKRDVEQLFDLVKR----------HNIEVvFLPVAFLKFIFSEREFINR-------------FPTCVKHI 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 424 LGGHVRMIVTgaapaSPTVLGFLRAalGCQVYEGYG--QTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDaEELNYW 500
Cdd:cd17656 251 ITAGEQLVIT-----NEFKEMLHEH--NVHLHNHYGpsETHVVTTYTINPEAEIPElPPIGKPISNTWIYILD-QEQQLQ 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 501 TCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGW------LHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIE 574
Cdd:cd17656 323 PQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-RGYRIELGEIE 401
|
330 340
....*....|....*....|
gi 1907081036 575 NIYIRSEPVAQ--IYVHGDS 592
Cdd:cd17656 402 AQLLNHPGVSEavVLDKADD 421
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
275-590 |
1.48e-08 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 57.03 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 275 FTSGTTGNPKGAMLTHGNVVADFsgflKVTESQWAPTCADVHFSYLPLAH-MFERMVQSVVYCHGGRVGFFQGDIRLLSD 353
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESF----VCNEDLFNISGEDAILAPGPLSHsLFLYGAISALYLGGTFIGQRKFNPKSWIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 354 DMKALRPTIFPVVPRLLnrmydkifhqadtslkrwllefaakrkQAEVRSGIIRNnsiwdelffnkiqaslggHVRMIVT 433
Cdd:cd17633 83 KINQYNATVIYLVPTML---------------------------QALARTLEPES------------------KIKSIFS 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 434 GAAPASPTVLGFLRAAL-GCQVYEGYGQTEcTAGCTFTTPGD-WTSGHVGAPLPCNHIKLVDAEElnywtcKGEGEICVK 511
Cdd:cd17633 118 SGQKLFESTKKKLKNIFpKANLIEFYGTSE-LSFITYNFNQEsRPPNSVGRPFPNVEIEIRNADG------GEIGKIFVK 190
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081036 512 GPNVFKGYLKDEDRTKealdsDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYVHG 590
Cdd:cd17633 191 SEMVFSGYVRGGFSNP-----DGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIEEAIVVG 263
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
268-613 |
1.57e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 56.98 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 268 DDLSIVCFTSGTTGNPKGAMLTHGNVVA------DFSGflkvTESQWAPTcadvhfsyLPLAHM--FERMVQSVVychGG 339
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTAsadathDRLG----GPGQWLLA--------LPAHHIagLQVLVRSVI---AG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 340 RV--------GFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKifhQADTSLKrwllEFAAkrkqaevrsgiirnnsi 411
Cdd:PRK07824 100 SEpveldvsaGFDPTALPRAVAELGGGRRYTSLVPMQLAKALDDP---AATAALA----ELDA----------------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 412 wdelffnkiqaslgghvrmIVTGAAPASPTVlgfLRAA--LGCQVYEGYGQTECTAGCTFTtpgdwtsghvGAPLPCNHI 489
Cdd:PRK07824 156 -------------------VLVGGGPAPAPV---LDAAaaAGINVVRTYGMSETSGGCVYD----------GVPLDGVRV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 490 KLVDaeelnywtckgeGEICVKGPNVFKGYLKDEDrtKEALDSDGWLHTGDIGKwLPEGTLKIIDRKKHIFKLAqGEYVA 569
Cdd:PRK07824 204 RVED------------GRIALGGPTLAKGYRNPVD--PDPFAEPGWFRTDDLGA-LDDGVLTVLGRADDAISTG-GLTVL 267
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1907081036 570 PEKIENIYIRSEPVAQIYVHG---DSLKAFLVGIVVPDPEVMPSWAQ 613
Cdd:PRK07824 268 PQVVEAALATHPAVADCAVFGlpdDRLGQRVVAAVVGDGGPAPTLEA 314
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
268-598 |
4.80e-08 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 56.58 E-value: 4.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 268 DDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF----LKVTESQWAPTCADVHFSY-------LPLAHMFERMVQSVVYc 336
Cdd:PRK06060 145 DALAYATYTSGTTGPPKAAIHRHADPLTFVDAMcrkaLRLTPEDTGLCSARMYFAYglgnsvwFPLATGGSAVINSAPV- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 337 hGGRVGffqgdiRLLSddmKALRPTIFPVVPRLLNRMYDKIfhQADTslkrwllefaakrkqaeVRSgiirnnsiwdelf 416
Cdd:PRK06060 224 -TPEAA------AILS---ARFGPSVLYGVPNFFARVIDSC--SPDS-----------------FRS------------- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 417 fnkiqaslgghVRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTEctAGCTFT--TPGDWTSGHVGAPLPCNHIKLVd 493
Cdd:PRK06060 262 -----------LRCVVSAGEALELGLAERLMEFFGgIPILDGIGSTE--VGQTFVsnRVDEWRLGTLGRVLPPYEIRVV- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 494 AEELNYWTCKGEGEICVKGPNVFKGYLkdeDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIfKLAQGEYVAPEKI 573
Cdd:PRK06060 328 APDGTTAGPGVEGDLWVRGPAIAKGYW---NRPDSPVANEGWLDTRDRVCIDSDGWVTYRCRADDT-EVIGGVNVDPREV 403
|
330 340 350
....*....|....*....|....*....|..
gi 1907081036 574 ENIYIRSEPVAQIYVHG-------DSLKAFLV 598
Cdd:PRK06060 404 ERLIIEDEAVAEAAVVAvrestgaSTLQAFLV 435
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
255-576 |
5.79e-08 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 55.93 E-value: 5.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 255 GRENHHAPVPPRPD-DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAptcADVHFSYLPLAH-Mfermvqs 332
Cdd:PRK05851 138 AHTNRSASLTPPDSgGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAA---TDVGCSWLPLYHdM------- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 333 vvychggrvgffqGDIRLLSDDMKA----LRPT-IFPVVP-RLLNrmydkifhqadtslkrWLLEFAAKRKQA-EVRSGI 405
Cdd:PRK05851 208 -------------GLAFLLTAALAGaplwLAPTtAFSASPfRWLS----------------WLSDSRATLTAApNFAYNL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 406 IRNNSiwdelffNKIQASLGGHVRMIVTGAAP----------ASPTVLGFLRAALGcqvyEGYGQTECTAGCTFTTPG-- 473
Cdd:PRK05851 259 IGKYA-------RRVSDVDLGALRVALNGGEPvdcdgferfaTAMAPFGFDAGAAA----PSYGLAESTCAVTVPVPGig 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 474 ---------DWTSGH----VGAPLPCNHIKLVDAEELNYWTCKGEGEICVKGPNVFKGYLKDEdrtkeALDSDGWLHTGD 540
Cdd:PRK05851 328 lrvdevttdDGSGARrhavLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQA-----PIDPDDWFPTGD 402
|
330 340 350
....*....|....*....|....*....|....*.
gi 1907081036 541 IGkWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENI 576
Cdd:PRK05851 403 LG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERV 436
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
429-605 |
1.87e-07 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 54.23 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 429 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT---------FTT------PGD--WTSGHVGAPLPCNHIkl 491
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAEGLVNYTrlddsderiFTTqgrpmsPDDevWVADADGNPLPQGEV-- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 492 vdaeelnywtckgeGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHifklaQ----GEY 567
Cdd:PRK10946 381 --------------GRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGEK 441
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907081036 568 VAPEKIENIYIRsepvaqiyvHGDSLKAFLVGIvvPDP 605
Cdd:PRK10946 442 IAAEEIENLLLR---------HPAVIHAALVSM--EDE 468
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
429-613 |
2.78e-07 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 53.46 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 429 RMIVTGAAPASPTVLGF-----LRAALGcqvyegYGQTEcTAG--CTFTtPGDWTSG--HVGAPLPCNHIKLvdaeelny 499
Cdd:PRK07445 233 RTILLGGAPAWPSLLEQarqlqLRLAPT------YGMTE-TASqiATLK-PDDFLAGnnSSGQVLPHAQITI-------- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 500 wTCKGEGEICVKGPNVFKGYLkdedrtKEALDSDGWLHTGDIGKWLPEGTLKIIDR--KKHIfklAQGEYVAPEKIENIY 577
Cdd:PRK07445 297 -PANQTGNITIQAQSLALGYY------PQILDSQGIFETDDLGYLDAQGYLHILGRnsQKII---TGGENVYPAEVEAAI 366
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907081036 578 IRSEPVAQIYVHGdslkaflvgivVPDPEvmpsWAQ 613
Cdd:PRK07445 367 LATGLVQDVCVLG-----------LPDPH----WGE 387
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
121-324 |
1.04e-06 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 51.80 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAE-----FLGSGLLQHDCkvgteqfVGVFAQNRPEWIIAELACyTYSMVVVPLYDT-LGPGSISYIINTAD 194
Cdd:PRK08279 63 ISYAELNARANryahwAAARGVGKGDV-------VALLMENRPEYLAAWLGL-AKLGAVVALLNTqQRGAVLAHSLNLVD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 195 ICTVIVDKPhkatlLLEHVErkETPGLKLVILMEPFEDalRERGKKCGVDIKSMQAIEDCGRENHHAPVPPRPDDLSIVC 274
Cdd:PRK08279 135 AKHLIVGEE-----LVEAFE--EARADLARPPRLWVAG--GDTLDDPEGYEDLAAAAAGAPTTNPASRSGVTAKDTAFYI 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907081036 275 FTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTESqwaptcaDVHFSYLPLAH 324
Cdd:PRK08279 206 YTSGTTGLPKAAVMSHMRWLkamGGFGGLLRLTPD-------DVLYCCLPLYH 251
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
121-585 |
1.18e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 52.48 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLlQHDCKVGtEQFVGVFAQNrPEWIIAELACYTYSMVVVPLYDtlgPGSisyiintadictviv 200
Cdd:PRK05691 41 LSYRDLDLRARTIAAAL-QARASFG-DRAVLLFPSG-PDYVAAFFGCLYAGVIAVPAYP---PES--------------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 DKPHKATLLLEHVERKETpglKLVILMEPFEDALRERGKKCGVDIKSMQAI---EDCGRENHHAPVPPrPDDLSIVCFTS 277
Cdd:PRK05691 100 ARRHHQERLLSIIADAEP---RLLLTVADLRDSLLQMEELAAANAPELLCVdtlDPALAEAWQEPALQ-PDDIAFLQYTS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 278 GTTGNPKGAMLTHGNVVADfsgflkvtesQWAPTCA--------DVHFSYLPLAH---MFERMVQSV---VYCHGGRVGF 343
Cdd:PRK05691 176 GSTALPKGVQVSHGNLVAN----------EQLIRHGfgidlnpdDVIVSWLPLYHdmgLIGGLLQPIfsgVPCVLMSPAY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 344 FQG-DIRLLsDDMKALRPTI-----FPVvpRLLN-RMYDKIFHQADtsLKRWLLEFAAkrkqaevrSGIIRNNSIwdELF 416
Cdd:PRK05691 246 FLErPLRWL-EAISEYGGTIsggpdFAY--RLCSeRVSESALERLD--LSRWRVAYSG--------SEPIRQDSL--ERF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 417 FNKIQ----------ASLG-GHVRMIVTGAAPA-SPTVLGFLRAALGCQVYEGyGQTECTAGCTFTTPGdwtsghvgapl 484
Cdd:PRK05691 311 AEKFAacgfdpdsffASYGlAEATLFVSGGRRGqGIPALELDAEALARNRAEP-GTGSVLMSCGRSQPG----------- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 485 pcNHIKLVDAEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEA---LDSDGWLHTGDIGkWLPEGTLKIIDRKKHIFk 561
Cdd:PRK05691 379 --HAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfveHDGRTWLRTGDLG-FLRDGELFVTGRLKDML- 454
|
490 500
....*....|....*....|....
gi 1907081036 562 LAQGEYVAPEKIENIYIRSEPVAQ 585
Cdd:PRK05691 455 IVRGHNLYPQDIEKTVEREVEVVR 478
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
267-598 |
2.17e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 51.32 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 267 PDDLSIVCFTSGTTGNPKGAMLT-HGNVVADFSG--FLKVTE----SQWAPTCADVHFSYLPLAHMFermvqsvvychGG 339
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEqRGMLNNQLSKvpYLALSEadviAQTASQSFDISVWQFLAAPLF-----------GA 3936
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 340 RVGFFQGDI----RLLSDDMKALRPTIFPVVPRLLNRMYDKIfHQADTSLkRWllefaakrkqaevrsgiirnnsiwdel 415
Cdd:PRK05691 3937 RVEIVPNAIahdpQGLLAHVQAQGITVLESVPSLIQGMLAED-RQALDGL-RW--------------------------- 3987
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 416 ffnkiqaslgghvrMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF------TTPGDWTSghVGAPLPCNHI 489
Cdd:PRK05691 3988 --------------MLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFfrvdlaSTRGSYLP--IGSPTDNNRL 4051
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 490 KLVDaEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEAL-------DSDGWLHTGDIGKWLPEGTLKIIDRKKHI--- 559
Cdd:PRK05691 4052 YLLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFvphpfgaPGERLYRTGDLARRRSDGVLEYVGRIDHQvki 4130
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1907081036 560 --FKLAQGEYVApEKIENIYIRSEPVA-QIYVHGDSLKAFLV 598
Cdd:PRK05691 4131 rgYRIELGEIEA-RLHEQAEVREAAVAvQEGVNGKHLVGYLV 4171
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
417-605 |
2.29e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 50.55 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 417 FNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPGDWTSGHVGAPLPCNHIKLVDAEE 496
Cdd:PRK07638 245 LYKENRVIENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSF-VTALVDEESERRPNSVGRPFHNVQVRICNE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 497 LNYWTCKGE-GEICVKGPNVFKGYLKDEDRTKEaLDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIEN 575
Cdd:PRK07638 324 AGEEVQKGEiGTVYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIES 401
|
170 180 190
....*....|....*....|....*....|
gi 1907081036 576 IYIRSEPVAQIYVHGdslkaflvgivVPDP 605
Cdd:PRK07638 402 VLHEHPAVDEIVVIG-----------VPDS 420
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
267-590 |
3.53e-06 |
|
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: 50.12 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAptcaDVHFSYLPLAH---MFERMVQSVVycHGGRVGF 343
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNG----DRTYTCMPLYHgtaAFLGACNCLM--SGGTLAL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 344 ---FQgdIRLLSDDMKALRPTIFPVVPRLLnrmydkifhqadtslkRWLLEFAAkrkqaevrsgiirnnSIWDELffNKI 420
Cdd:cd05937 160 srkFS--ASQFWKDVRDSGATIIQYVGELC----------------RYLLSTPP---------------SPYDRD--HKV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 421 QASLGGHVRmivtgaapasPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKL-------- 491
Cdd:cd05937 205 RVAWGNGLR----------PDIWERFRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKFenqvvlvk 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 492 VDAEELNYWT------CK----GE-GEICVKGPNV----FKGYLKDEDRTKEAL------DSDGWLHTGDIGKWLPEGTL 550
Cdd:cd05937 275 MDPETDDPIRdpktgfCVrapvGEpGEMLGRVPFKnreaFQGYLHNEDATESKLvrdvfrKGDIYFRTGDLLRQDADGRW 354
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1907081036 551 KIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYVHG 590
Cdd:cd05937 355 YFLDRLGDTFRW-KSENVSTTEVADVLGAHPDIAEANVYG 393
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
122-610 |
3.84e-06 |
|
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: 50.27 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 122 SYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSI-SYIINTADICTVIV 200
Cdd:cd17634 86 SYRELHREVCRFAGTLLDLGVKKGDR--VAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVaGRIIDSSSRLLITA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 DkphkatlllEHVERKETPGLKLVIlmepfEDALRERG---------KKCGVDIKSMQA--------IEDCGREnhHAPV 263
Cdd:cd17634 164 D---------GGVRAGRSVPLKKNV-----DDALNPNVtsvehvivlKRTGSDIDWQEGrdlwwrdlIAKASPE--HQPE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 264 PPRPDDLSIVCFTSGTTGNPKGAMLTHGnvvadfsGF-LKVTESqwaptcadvhfsylpLAHMFERMVQSVVYChGGRVG 342
Cdd:cd17634 228 AMNAEDPLFILYTSGTTGKPKGVLHTTG-------GYlVYAATT---------------MKYVFDYGPGDIYWC-TADVG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 343 FFQGDIRLLSDDMkALRPTIF-----PVVPRlLNRMYDKIFHQADTSLkrWLLEFAAKRKQAEVRSGIIRNNsiwdelff 417
Cdd:cd17634 285 WVTGHSYLLYGPL-ACGATTLlyegvPNWPT-PARMWQVVDKHGVNIL--YTAPTAIRALMAAGDDAIEGTD-------- 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 418 nkiQASLgghvRMIVTGAAPASPTVLGFLRAALG---CQVYEGYGQTECTAGCTFTTPG--DWTSGHVGAPLPCNHIKLV 492
Cdd:cd17634 353 ---RSSL----RILGSVGEPINPEAYEWYWKKIGkekCPVVDTWWQTETGGFMITPLPGaiELKAGSATRPVFGVQPAVV 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 493 DAEElNYWTCKGEGEICVKG--PNVFKGYLKDEDRTKEALDS--DGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYV 568
Cdd:cd17634 426 DNEG-HPQPGGTEGNLVITDpwPGQTRTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVA-GHRL 503
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1907081036 569 APEKIENIYIRSEPVAQIYVHG--DSLKA-FLVGIVVPDPEVMPS 610
Cdd:cd17634 504 GTAEIESVLVAHPKVAEAAVVGipHAIKGqAPYAYVVLNHGVEPS 548
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
264-607 |
9.31e-06 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 48.99 E-value: 9.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 264 PPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEsqW---------APTCADVHFSYLPLAHMferMVQSVV 334
Cdd:PRK13382 192 EPTGRKGRVILLTSGTTGTPKGARRSGPGGIGTLKAILDRTP--WraeeptvivAPMFHAWGFSQLVLAAS---LACTIV 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 335 YchggRVGFFQGDIRLLSDdmkALRPTIFPVVPRLLNRMYDKIfhqadtslkrwllefaakrkqAEVRSgiirnnsiwde 414
Cdd:PRK13382 267 T----RRRFDPEATLDLID---RHRATGLAVVPVMFDRIMDLP---------------------AEVRN----------- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 415 lffnkiqASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFT-TPGDWTSG--HVGAPLPCNHIKL 491
Cdd:PRK13382 308 -------RYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATE--AGMIATaTPADLRAApdTAGRPAEGTEIRI 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 492 VDAE--ELNywtcKGE-GEICVKGPNVFKGYlkDEDRTKEAldSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYV 568
Cdd:PRK13382 379 LDQDfrEVP----TGEvGTIFVRNDTQFDGY--TSGSTKDF--HDGFMASGDVGYLDENGRLFVVGRDDEMI-VSGGENV 449
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1907081036 569 APEKIENIYIRSEPVAQIYV-------HGDSLKAFlvgiVVPDPEV 607
Cdd:PRK13382 450 YPIEVEKTLATHPDVAEAAVigvddeqYGQRLAAF----VVLKPGA 491
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
483-550 |
1.10e-05 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 48.35 E-value: 1.10e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081036 483 PLPCNHIK-----LVDAEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEAL-DSDGW--LHTGDIGKwLPEGTL 550
Cdd:PRK04813 317 RLPIGYAKpdsplLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGY-LEDGLL 391
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
418-643 |
3.65e-05 |
|
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: 47.04 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 418 NKIQASLGGHVRMIVTGAAPASPTV----LGFLRA--ALGCQVYEGYGqTECTAGCTFTTPGDWTSGHVGAPLPCNHI-K 490
Cdd:cd05915 263 ESTGHRLKTLRRLVVGGSAAPRSLIarfeRMGVEVrqGYGLTETSPVV-VQNFVKSHLESLSEEEKLTLKAKTGLPIPlV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 491 LVDAEELNYWTCKGEGE----ICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGE 566
Cdd:cd05915 342 RLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG-GE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 567 YVAPEKIENIyirsepvaqIYVHGDSLKAFLVGivVPDP---EVMPSWAQKKGIEGTYQELCmkkELKKAILDDMVMLGK 643
Cdd:cd05915 421 WISSVDLENA---------LMGHPKVKEAAVVA--IPHPkwqERPLAVVVPRGEKPTPEELN---EHLLKAGFAKWQLPD 486
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
265-614 |
7.31e-05 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 45.45 E-value: 7.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 265 PRPDDLSIVCfTSGTTGNPKGAMLTHGNV-VADFSGFLKVTESQWAPTCAD---------VHFSYLPLAH-------MFE 327
Cdd:cd05924 1 RSADDLYILY-TGGTTGMPKGVMWRQEDIfRMLMGGADFGTGEFTPSEDAHkaaaaaagtVMFPAPPLMHgtgswtaFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 328 RMVQSVVYCHGGRvgfFQGD--IRLLSDDmkalRPTIFPVVprllnrmydkifhqADtSLKRWLLEfaakrkqaEVRSGI 405
Cdd:cd05924 80 LLGGQTVVLPDDR---FDPEevWRTIEKH----KVTSMTIV--------------GD-AMARPLID--------ALRDAG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 406 IRNNSiwdelffnkiqaSLgghvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFTTPGdwtSGHVGAPL 484
Cdd:cd05924 130 PYDLS------------SL----FAISSGGALLSPEVKqGLLELVPNITLVDAFGSSETGFTGSGHSAG---SGPETGPF 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 485 -PCNHIKLVDAEELNYWTCK--GEGEICVKGpNVFKGYLKDEDRTKEA---LDSDGWLHTGDIGKWLPEGTLKIIDRKKH 558
Cdd:cd05924 191 tRANPDTVVLDDDGRVVPPGsgGVGWIARRG-HIPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGRGSV 269
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081036 559 IFKLAqGEYVAPEKIEniyirsepvAQIYVHGDSLKAFLVGivVPDPEvmpsWAQK 614
Cdd:cd05924 270 CINTG-GEKVFPEEVE---------EALKSHPAVYDVLVVG--RPDER----WGQE 309
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
233-325 |
7.88e-05 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 45.75 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 233 ALRERGKKCGVDIKSM--QAIEDCGRENHHAPVPPRPDDLS---------IVCFTSGTTGNPKGAMLTHGNVVAdFSGFL 301
Cdd:cd05938 98 ALRADGVSVWYLSHTSntEGVISLLDKVDAASDEPVPASLRahvtikspaLYIYTSGTTGLPKAARISHLRVLQ-CSGFL 176
|
90 100
....*....|....*....|....
gi 1907081036 302 KVTesqwAPTCADVHFSYLPLAHM 325
Cdd:cd05938 177 SLC----GVTADDVIYITLPLYHS 196
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
121-599 |
1.68e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 45.16 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 121 LSYQEVAKRAEFLGSGLlqHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTAdictviv 200
Cdd:PRK05691 1157 LDYAELHAQANRLAHYL--RDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADS------- 1227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 201 dkphKATLLLEHVERKEtpglklvilmepfedALRERGKKCGVDIKSMQAiedcgrENH--HAP-VPPRPDDLSIVCFTS 277
Cdd:PRK05691 1228 ----GVELLLTQSHLLE---------------RLPQAEGVSAIALDSLHL------DSWpsQAPgLHLHGDNLAYVIYTS 1282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 278 GTTGNPKGAMLTHGNVVADfsgfLKVTESQWAPTCADVHFSYLPLAhmFErmvQSVVYCH-----GGRVGFF----QGDI 348
Cdd:PRK05691 1283 GSTGQPKGVGNTHAALAER----LQWMQATYALDDSDVLMQKAPIS--FD---VSVWECFwplitGCRLVLAgpgeHRDP 1353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 349 RLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTSLKRWlleFAAkrkqAEVRSGIIRNNsiwdelffnkiqaslgghv 428
Cdd:PRK05691 1354 QRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRL---FSG----GEALPAELRNR------------------- 1407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 429 rmivtgaapasptVLGFLRAAlgcQVYEGYGQTECTAGCTF--TTPGDWTSGHVGAPLPCNHIKLVDAEeLNYWTCKGEG 506
Cdd:PRK05691 1408 -------------VLQRLPQV---QLHNRYGPTETAINVTHwqCQAEDGERSPIGRPLGNVLCRVLDAE-LNLLPPGVAG 1470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 507 EICVKGPNVFKGYLKDEDRTKE-----ALDSDG--WLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIR 579
Cdd:PRK05691 1471 ELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL-RGFRVEPEEIQARLLA 1549
|
490 500
....*....|....*....|..
gi 1907081036 580 SEPVAQ--IYVHGDSLKAFLVG 599
Cdd:PRK05691 1550 QPGVAQaaVLVREGAAGAQLVG 1571
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
261-557 |
5.65e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 43.01 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 261 APVPPRPDDLSIVCF---TSGTTGNPKGAMLTHGNVVADF----SGFLKVTESQWAPTCADVhfSYLPLAHMFERMVQSV 333
Cdd:PRK05850 150 RGSDARPRDLPSTAYlqyTSGSTRTPAGVMVSHRNVIANFeqlmSDYFGDTGGVPPPDTTVV--SWLPFYHDMGLVLGVC 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 334 VYCHGGR-------VGFFQGDIRLLSddMKALRPTIFPVVPrllnrmydkifhqadtslkRWLLEFAAKRKQAEVRSGIi 406
Cdd:PRK05850 228 APILGGCpavltspVAFLQRPARWMQ--LLASNPHAFSAAP-------------------NFAFELAVRKTSDDDMAGL- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 407 rnnsiwdELffnkiqaslgGHVRMIVTGAAPASP-TVLGFLR--AALGCQ---VYEGYGQTECTAGCTFTTPGD------ 474
Cdd:PRK05850 286 -------DL----------GGVLGIISGSERVHPaTLKRFADrfAPFNLRetaIRPSYGLAEATVYVATREPGQppesvr 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081036 475 -----WTSGHV-------GAPLPCNH------IKLVDAEelnywTCK-----GEGEICVKGPNVFKGYLKDEDRTKEALD 531
Cdd:PRK05850 349 fdyekLSAGHAkrcetggGTPLVSYGsprsptVRIVDPD-----TCIecpagTVGEIWVHGDNVAAGYWQKPEETERTFG 423
|
330 340 350
....*....|....*....|....*....|....*..
gi 1907081036 532 ------SDG-----WLHTGDIGkWLPEGTLKIIDRKK 557
Cdd:PRK05850 424 atlvdpSPGtpegpWLRTGDLG-FISEGELFIVGRIK 459
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
263-294 |
7.39e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 43.11 E-value: 7.39e-04
10 20 30
....*....|....*....|....*....|..
gi 1907081036 263 VPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVV 294
Cdd:PRK10252 593 QLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIV 624
|
|
| |
