|
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 ... |
116-694 |
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: 905.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 116 QPYQWLSYQEVAKRAEFLGSGLLQHDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADI 195
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 196 CTVIVDKphkailllehverketpglklvilmepfddalrergkkcGVDIKSMQAIEDSGQENHRVPVPPRPDDLSIVCF 275
Cdd:cd05927 81 SIVFCDA---------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 276 TSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTCADVHFSYLPLAHMFERMVQSVVYCHGGRVGFFQGDIRLLSDDM 355
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 356 KALRPTIFPVVPRLLNRMYDKIFH--QADTSLKRWLLEFAAKRKQAEVRSGIIRNNSIWDELFFNKIQASLGGHVRMIVT 433
Cdd:cd05927 202 KALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 434 GAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYW--TSKGEGEICVK 511
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDakDPNPRGEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 512 GPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGD 591
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 592 SLKAFLVGIVVPDPEVMPCWAQKK-GIEGNYQELCKSKELKKAILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLL 670
Cdd:cd05927 442 SLKSFLVAIVVPDPDVLKEWAASKgGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLL 521
|
570 580
....*....|....*....|....
gi 1937369599 671 TPTLKAKRPELREYFKKQIEELYS 694
Cdd:cd05927 522 TPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
79-694 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 701.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 79 TQLLTHY--YDDARTMYQVFRRGLSISGNGPCLGFRKPEQ----PYQWLSYQEVAKRAEFLGSGLLQHDCKVGteQFIGV 152
Cdd:PLN02736 31 LKLVSRFpdHPEIGTLHDNFVYAVETFRDYKYLGTRIRVDgtvgEYKWMTYGEAGTARTAIGSGLVQHGIPKG--ACVGL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 153 FAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIVdKPHKAILLLEHVerKETPGLKLVILMEPFDD 232
Cdd:PLN02736 109 YFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCL--SEIPSVRLIVVVGGADE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 233 ALRERGKKCGVDIKSMQAIEDSGQENHRVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESqwAPtc 312
Cdd:PLN02736 186 PLPSLPSGTGVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKF--YP-- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 313 ADVHFSYLPLAHMFERMVQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTS--LKRWLL 390
Cdd:PLN02736 262 SDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESggLKERLF 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 391 EFAAKRKQAEVRSGiiRNNS-IWDELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF 469
Cdd:PLN02736 342 NAAYNAKKQALENG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 470 TTPGDWTSGHVGAPLPCNHIKLVDAEELNYwTSKGE----GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWL 545
Cdd:PLN02736 420 MDEGDNLSGHVGSPNPACEVKLVDVPEMNY-TSEDQpyprGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWL 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 546 PEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAFLVGIVVPDPEVMPCWAQKKGIE-GNYQEL 624
Cdd:PLN02736 499 PGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQL 578
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 625 CKSKELKKAILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 694
Cdd:PLN02736 579 CNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYA 648
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
86-694 |
1.09e-174 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 511.95 E-value: 1.09e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 86 YDDARTMYQVFRRGLSISGNGPCLGfRKPEQPYQWLSYQEVAKRAEFLGSGLLQHDCKVGteQFIGVFAQNRPEWIIAEL 165
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVALR-EKEDGIWQSLTWAEFAERVRALAAGLLALGVKPG--DRVAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 166 ACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIVDKPHKAILLLEHveRKETPGLKLVILMEPfddalreRGKKCGVDI 245
Cdd:COG1022 84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEV--RDELPSLRHIVVLDP-------RGLRDDPRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 246 KSMQAIEDSGQENH------RVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWAPTCADVHFSY 319
Cdd:COG1022 155 LSLDELLALGREVAdpaeleARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLER----LPLGPGDRTLSF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 320 LPLAHMFERMVQSVVYCHGGRVGFfQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTS--LKRWLLEFA---A 394
Cdd:COG1022 231 LPLAHVFERTVSYYALAAGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAggLKRKLFRWAlavG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 395 KRKQAEVRSGiiRNNSIW--------DELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAG 466
Cdd:COG1022 310 RRYARARLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 467 CTFTTPGDWTSGHVGAPLPCNHIKLvdAEElnywtskgeGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLP 546
Cdd:COG1022 387 ITVNRPGDNRIGTVGPPLPGVEVKI--AED---------GEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 547 EGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKaFLVGIVVPDPEVMPCWAQKKGIE-GNYQELC 625
Cdd:COG1022 456 DGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDGRP-FLAALIVPDFEALGEWAEENGLPyTSYAELA 534
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937369599 626 KSKELKKAILDDMVMLGKesGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 694
Cdd:COG1022 535 QDPEVRALIQEEVDRANA--GLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYA 601
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
116-681 |
2.71e-160 |
|
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: 469.77 E-value: 2.71e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 116 QPYQWLSYQEVAKRAEFLGSGLLQHDCKVGteQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADI 195
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPG--DRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 196 CTVIVDKPhkailllehverketpglklvilmepfddalrergkkcgvdiksmqaiedsgqenhrvpvpprpDDLSIVCF 275
Cdd:cd05907 79 KALFVEDP----------------------------------------------------------------DDLATIIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 276 TSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWAPTCADVHFSYLPLAHMFE-RMVQSVVYCHGGRVGFFQgDIRLLSDD 354
Cdd:cd05907 95 TSGTTGRPKGVMLSHRNILSNALALAER----LPATEGDRHLSFLPLAHVFErRAGLYVPLLAGARIYFAS-SAETLLDD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 355 MKALRPTIFPVVPRLLNRMYDKIFHQADTSLKRWLLEFAAkrkqaevrsgiirnnsiwdelffnkiqaslGGHVRMIVTG 434
Cdd:cd05907 170 LSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV------------------------------GGRLRFAASG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 435 AAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDaeelnywtskgEGEICVKGPN 514
Cdd:cd05907 220 GAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPN 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 515 VFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLK 594
Cdd:cd05907 288 VMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDGRP 367
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 595 aFLVGIVVPDPEVMPCWAQKKGIEG-NYQELCKSKELKKAILDDMVMLGKEsgLHSFEQVKAIYIHCDMFSVQNGLLTPT 673
Cdd:cd05907 368 -FLVALIVPDPEALEAWAEEHGIAYtDVAELAANPAVRAEIEAAVEAANAR--LSRYEQIKKFLLLPEPFTIENGELTPT 444
|
....*...
gi 1937369599 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 |
2.28e-151 |
|
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: 448.97 E-value: 2.28e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 117 PYQWLSYQEVAKRAEFLGSGLlqhdCKVG--TEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTAD 194
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGL----VELGlkPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 195 ICTVIVDkphkailllehverketpglklvilmepfddalrergkkcgvdiksmqaiedsgqenhrvpvpPRPDDLSIVC 274
Cdd:cd17639 78 CSAIFTD---------------------------------------------------------------GKPDDLACIM 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 275 FTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTcaDVHFSYLPLAHMFERMVQSVVYCHGGRVGFfqGDIRLLSD- 353
Cdd:cd17639 95 YTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGPD--DRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDk 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 354 -------DMKALRPTIFPVVPRLLNRMYDKIFHQADTS--LKRWLLEFAAKRKQAEVRSGIirNNSIWDELFFNKIQASL 424
Cdd:cd17639 171 skrgckgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMggLKRTLFWTAYQSKLKALKEGP--GTPLLDELVFKKVRAAL 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 425 GGHVRMIVTGAAPASPTVLGFLrAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYWTSKG 504
Cdd:cd17639 249 GGRLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDKP 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 505 E--GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEP 582
Cdd:cd17639 328 PprGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPL 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 583 VAQIYVHGDSLKAFLVGIVVPDPEVMPCWAQKKG-IEGNYQELCKSKELKKAILDDMVMLGKESGLHSFEQVKAIYIHCD 661
Cdd:cd17639 408 VNNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGvINSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDE 487
|
570
....*....|....*..
gi 1937369599 662 MFSVQNGLLTPTLKAKR 678
Cdd:cd17639 488 EWTPENGLVTAAQKLKR 504
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
87-693 |
1.65e-149 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 449.86 E-value: 1.65e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 87 DDARTMYQVFRRGLSISGNGPCLGFR-----KPEQpYQWLSYQEVAKRAEFLGSGLlqHDCKVGTEQFIGVFAQNRPEWI 161
Cdd:PLN02614 42 EGMDSCWDVFRMSVEKYPNNPMLGRReivdgKPGK-YVWQTYQEVYDIVIKLGNSL--RSVGVKDEAKCGIYGANSPEWI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 162 IAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIVDKphKAILLLEHVERKETPGLKLVILMEPFDDALRERGKKC 241
Cdd:PLN02614 119 ISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEE--KKISELFKTCPNSTEYMKTVVSFGGVSREQKEEAETF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 242 GVDIKSMQAIEDSGQ-ENHRVPVPpRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTES-QWAPTCADVHFSY 319
Cdd:PLN02614 197 GLVIYAWDEFLKLGEgKQYDLPIK-KKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSaNAALTVKDVYLSY 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 320 LPLAHMFERMVQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTS--LKRWLLEFAAKRK 397
Cdd:PLN02614 276 LPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGgfLKKFVFDSAFSYK 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 398 QAEVRSGI--IRNNSIWDELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDW 475
Cdd:PLN02614 356 FGNMKKGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDEL 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 476 TS-GHVGAPLPCNHIKLVDAEELNY--WTSKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKI 552
Cdd:PLN02614 436 DMlGTVGPPVPNVDIRLESVPEMEYdaLASTPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKI 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 553 IDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAFLVGIVVPDPEVMPCWAQKKGIEGNYQELCKSKELKK 632
Cdd:PLN02614 515 IDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKE 594
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937369599 633 AILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 693
Cdd:PLN02614 595 FILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMY 655
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
117-694 |
1.46e-148 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 446.98 E-value: 1.46e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 117 PYQWLSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADIC 196
Cdd:PLN02861 74 PYVWLTYKEVYDAAIRIGSAIRSRGVNPGDR--CGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 197 TVIV-DKPHKAILlleHVERKETPGLKLVILMEPFDDALRERGKKCGVDIKSMQAIEDSGQENHRVPvPPRPDDLSIVCF 275
Cdd:PLN02861 152 IAFVqESKISSIL---SCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLDCELP-PKQKTDICTIMY 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 276 TSGTTGNPKGAMLTHGNVVADF---SGFLKVTESqwAPTCADVHFSYLPLAHMFERMVQSVVYCHGGRVGFFQGDIRLLS 352
Cdd:PLN02861 228 TSGTTGEPKGVILTNRAIIAEVlstDHLLKVTDR--VATEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQGDIRYLM 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 353 DDMKALRPTIFPVVPRLLNRMYDKIFH--QADTSLKRWLLEFAAKRKQAEVRSGIIRNNS--IWDELFFNKIQASLGGHV 428
Cdd:PLN02861 306 EDVQALKPTIFCGVPRVYDRIYTGIMQkiSSGGMLRKKLFDFAYNYKLGNLRKGLKQEEAspRLDRLVFDKIKEGLGGRV 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 429 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCtFTTPGDWTS--GHVGAPLPCNHIKLVDAEELNY--WTSKG 504
Cdd:PLN02861 386 RLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGC-FTSIANVFSmvGTVGVPMTTIEARLESVPEMGYdaLSDVP 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 505 EGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVA 584
Cdd:PLN02861 465 RGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIA 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 585 QIYVHGDSLKAFLVGIVVPDPEVMPCWAQKKGIEGNYQELCKSKELKKAILDDMVMLGKESGLHSFEQVKAIYIHCDMFS 664
Cdd:PLN02861 544 SIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFD 623
|
570 580 590
....*....|....*....|....*....|
gi 1937369599 665 VQNGLLTPTLKAKRPELREYFKKQIEELYS 694
Cdd:PLN02861 624 IERDLITPTFKLKRPQLLKYYKDCIDQLYS 653
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
88-693 |
8.48e-147 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 442.72 E-value: 8.48e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 88 DARTMYQVFRRGLSISGNGPCLGFRKPEQ----PYQWLSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIA 163
Cdd:PLN02430 40 DITTAWDIFSKSVEKYPDNKMLGWRRIVDgkvgPYMWKTYKEVYEEVLQIGSALRASGAEPGSR--VGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 164 ELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV-DKPHKAILlleHVERKETPGLKLVILMEPFDDALRERGKKCG 242
Cdd:PLN02430 118 MEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVqDKKIKELL---EPDCKSAKRLKAIVSFTSVTEEESDKASQIG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 243 VDIKSMQAIEDSGQENHRVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTESQWapTCADVHFSY 319
Cdd:PLN02430 195 VKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGvdlFMEQFEDKM--THDDVYLSF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 320 LPLAHMFERMVQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFH--QADTSLKRWLLEFAAKRK 397
Cdd:PLN02430 273 LPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYKYK 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 398 QAEVRSGIIRNNS--IWDELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDW 475
Cdd:PLN02430 353 LAWMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEM 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 476 TS-GHVGAPLPCNHIKLVDAEELNYwTSKGE---GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLK 551
Cdd:PLN02430 433 CMlGTVGAPAVYNELRLEEVPEMGY-DPLGEpprGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLK 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 552 IIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAFLVGIVVPDPEVMPCWAQKKGIEGNYQELCKSKELK 631
Cdd:PLN02430 511 IIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELK 590
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937369599 632 KAILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 693
Cdd:PLN02430 591 EHILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMY 652
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
79-694 |
2.94e-134 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 411.43 E-value: 2.94e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 79 TQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRK---PEQ---------------PYQWLSYQEVAKRAEFLGSGLLQ- 139
Cdd:PLN02387 47 PELVETPWEGATTLAALFEQSCKKYSDKRLLGTRKlisREFetssdgrkfeklhlgEYEWITYGQVFERVCNFASGLVAl 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 140 -HDckvgTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIVD-KPHKAILLLEhvERKE 217
Cdd:PLN02387 127 gHN----KEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDsKQLKKLIDIS--SQLE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 218 TpgLKLVILME-PFDDALRERGKKCGVDIKSMQAIEDSGQENHRVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD 296
Cdd:PLN02387 201 T--VKRVIYMDdEGVDSDSSLSGSSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVAT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 297 FSGFLKVTesqwaPTCA--DVHFSYLPLAHMFERMVQSVVYCHGGRVGFfqGDIRLLSD-----------DMKALRPTIF 363
Cdd:PLN02387 279 VAGVMTVV-----PKLGknDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDtsnkikkgtkgDASALKPTLM 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 364 PVVPRLLNRMYDKIFHQADTS--LKRWLLEFAAKRKQAEVR------SGIIRnnSIWDELFFNKIQASLGGHVRMIVTGA 435
Cdd:PLN02387 352 TAVPAILDRVRDGVRKKVDAKggLAKKLFDIAYKRRLAAIEgswfgaWGLEK--LLWDALVFKKIRAVLGGRIRFMLSGG 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 436 APASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYWTSKG---EGEICVKG 512
Cdd:PLN02387 430 APLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLISDKpmpRGEIVIGG 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 513 PNVFKGYLKDEDRTKEA--LDSDG--WLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYV 588
Cdd:PLN02387 510 PSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIMV 589
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 589 HGDSLKAFLVGIVVPDPEVMPCWAQKKGIE-GNYQELCKSKELKKAILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQN 667
Cdd:PLN02387 590 HADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPAKIKLLPEPWTPES 669
|
650 660
....*....|....*....|....*..
gi 1937369599 668 GLLTPTLKAKRPELREYFKKQIEELYS 694
Cdd:PLN02387 670 GLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
117-563 |
3.61e-126 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 380.89 E-value: 3.61e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 117 PYQWLSYQEVAKRAEFLGSGLLQHDCKVGteQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADIC 196
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRALGVGKG--DRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 197 TVIVDKPHKAILLLEHVERKETPGLKLVILMEPFDDALRergkkcgvdiksMQAIEDSGQENHRVPVPPRPDDLSIVCFT 276
Cdd:pfam00501 96 VLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEP------------LPEEAKPADVPPPPPPPPDPDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 277 SGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTCADVHFSYLPLAHMFER-MVQSVVYCHGGRVGFFQGDIRL----L 351
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALdpaaL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 352 SDDMKALRPTIFPVVPRLLNRmydkifhqadtslkrwllefaakrkqaevrsgIIRNNSIWDELFfnkiqaslgGHVRMI 431
Cdd:pfam00501 244 LELIERYKVTVLYGVPTLLNM--------------------------------LLEAGAPKRALL---------SSLRLV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 432 VTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDW---TSGHVGAPLPCNHIKLVDAEELNYWTSKGEGEI 508
Cdd:pfam00501 283 LSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGEL 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1937369599 509 CVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLA 563
Cdd:pfam00501 363 CVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
60-693 |
1.77e-101 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 325.78 E-value: 1.77e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 60 QSEEVEDSGGARRSVI--------GDCTQLLTHYYDdARTMYQVFRRGLSISGNGPCLGFRK--------------PEQP 117
Cdd:PTZ00216 32 QNVPVPGTETENASAIyriagvtdEEHERLRNEWYY-GPNFLQRLERICKERGDRRALAYRPvervekevvkdadgKERT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 118 Y--------QWLSYQEVAKRAEFLGSGL----LQHDCKVGteqfigVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGS 185
Cdd:PTZ00216 111 MevthfnetRYITYAELWERIVNFGRGLaelgLTKGSNVA------IYEETRWEWLASIYGIWSQSMVAATVYANLGEDA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 186 IRYIINTADiCTVIVDKPHKAILLLEHVERKETPGLKLVILmepfdDALRERGKKCGVDIKSMQAIEDSG---QENHRVP 262
Cdd:PTZ00216 185 LAYALRETE-CKAIVCNGKNVPNLLRLMKSGGMPNTTIIYL-----DSLPASVDTEGCRLVAWTDVVAKGhsaGSHHPLN 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 263 VPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF-LKVTESQWAPTCADVHFSYLPLAHMFERMVQSVVYCHGGRV 341
Cdd:PTZ00216 259 IPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALeDRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLARGALI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 342 GFfqGDIRLLSD-------DMKALRPTIFPVVPRllnrmydkIFhqaDT-------------SLKRWLLEFAAKRKQAEV 401
Cdd:PTZ00216 339 GF--GSPRTLTDtfarphgDLTEFRPVFLIGVPR--------IF---DTikkaveaklppvgSLKRRVFDHAYQSRLRAL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 402 RSGiiRNNSIWDELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCqVYEGYGQTE--CTAGCTFTtpGDWTSGH 479
Cdd:PTZ00216 406 KEG--KDTPYWNEKVFSAPRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTEtvCCGGIQRT--GDLEPNA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 480 VGAPLPCNHIKLVDAEELNYwTSKGE--GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKK 557
Cdd:PTZ00216 481 VGQLLKGVEMKLLDTEEYKH-TDTPEprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVK 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 558 HIFKLAQGEYVAPEKIENIYIRSEPVAQ----IYVHGDslKAFLVGIVVPD-PEVMPcWAQKKGIEGNYQELCKSKELKK 632
Cdd:PTZ00216 560 ALAKNCLGEYIALEALEALYGQNELVVPngvcVLVHPA--RSYICALVLTDeAKAMA-FAKEHGIEGEYPAILKDPEFQK 636
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937369599 633 AILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 693
Cdd:PTZ00216 637 KATESLQETARAAGRKSFEIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
118-678 |
4.30e-80 |
|
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: 263.95 E-value: 4.30e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 118 YQWLSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICT 197
Cdd:cd05932 4 VVEFTWGEVADKARRLAAALRALGLEPGSK--IALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 198 VIVDKphkaillLEHVERKE--TPGLKLVILMEPFDDALRERGKKcgvDIKSMQAIEDSgqenhrvPVPPRPDDLSIVCF 275
Cdd:cd05932 82 LFVGK-------LDDWKAMApgVPEGLISISLPPPSAANCQYQWD---DLIAQHPPLEE-------RPTRFPEQLATLIY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 276 TSGTTGNPKGAMLTHGNVVADFSGF---LKVTESqwaptcaDVHFSYLPLAHMFERMVQSVVYCHGGRVGFFQGDIRLLS 352
Cdd:cd05932 145 TSGTTGQPKGVMLTFGSFAWAAQAGiehIGTEEN-------DRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTFV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 353 DDMKALRPTIFPVVPRLL----NRMYDKIFHQadtSLKRWLlefaakrkQAEVRSGIIRNnsiwdelffnKIQASLG-GH 427
Cdd:cd05932 218 EDVQRARPTLFFSVPRLWtkfqQGVQDKIPQQ---KLNLLL--------KIPVVNSLVKR----------KVLKGLGlDQ 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 428 VRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDaeelnywtskgEGE 507
Cdd:cd05932 277 CRLAGCGSAPVPPALLEWYRS-LGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 508 ICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIY 587
Cdd:cd05932 345 ILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVC 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 588 VHGDSLKAfLVGIVVPDPEvmpcwAQKKGIEGNYQELCKSkelKKAILDDMvmlgkESGLHSFEQVKAIYIHCDMFSVQN 667
Cdd:cd05932 425 VIGSGLPA-PLALVVLSEE-----ARLRADAFARAELEAS---LRAHLARV-----NSTLDSHEQLAGIVVVKDPWSIDN 490
|
570
....*....|.
gi 1937369599 668 GLLTPTLKAKR 678
Cdd:cd05932 491 GILTPTLKIKR 501
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
116-679 |
1.64e-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: 248.04 E-value: 1.64e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 116 QPYQWLSYQEVAKRAEFLGSGLLqhDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADI 195
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLR--SLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 196 CTVIVdkphkailllehverketpglklvilmepfddalrergkkcgvdiksmqaiedsgqENHrvpvpprPDDLSIVCF 275
Cdd:cd17640 79 VALVV--------------------------------------------------------END-------SDDLATIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 276 TSGTTGNPKGAMLTHGNVVADFSGFLKVTEsqwaPTCADVHFSYLPLAHMFERMVQSVVYCHGGRVGFfqGDIRLLSDDM 355
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLLHQIRSLSDIVP----PQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDDL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 356 KALRPTIFPVVPRLLNRMYDKIFHQadtslkrwllefaaKRKQAEVRSGIIrnnsiwdeLFFnkiqaSLGGHVRMIVTGA 435
Cdd:cd17640 170 KRVKPHYIVSVPRLWESLYSGIQKQ--------------VSKSSPIKQFLF--------LFF-----LSGGIFKFGISGG 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 436 APASPTVLGFLRaALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYWTSKGEGEICVKGPNV 515
Cdd:cd17640 223 GALPPHVDTFFE-AIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQV 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 516 FKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKa 595
Cdd:cd17640 302 MKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQK- 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 596 FLVGIVVPDPEVMPCWAQKKG--IEGNYQELCKSKELKKAILDD-MVMLGKESGLHSFEQVKAIYIHCDMFsVQNGLLTP 672
Cdd:cd17640 381 RLGALIVPNFEELEKWAKESGvkLANDRSQLLASKKVLKLYKNEiKDEISNRPGFKSFEQIAPFALLEEPF-IENGEMTQ 459
|
....*..
gi 1937369599 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 |
2.39e-69 |
|
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: 237.64 E-value: 2.39e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 119 QW--LSYQEVAKRAEFLGSGLLqhdcKVGTEQF--IGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINT-- 192
Cdd:cd05933 5 KWhtLTYKEYYEACRQAAKAFL----KLGLERFhgVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETse 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 193 ADICTVIVDKPHKAILLLEHverkETPGLKLVI-LMEPFDDalrergKKCGVdiKSMQAIEDSG------QENHRVPVPp 265
Cdd:cd05933 81 ANILVVENQKQLQKILQIQD----KLPHLKAIIqYKEPLKE------KEPNL--YSWDEFMELGrsipdeQLDAIISSQ- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 266 RPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTCADVHFSYLPLAHMFERMVQS-VVYCHGGRVGFF 344
Cdd:cd05933 148 KPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIwLPIKVGGQVYFA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 345 QGDIR--LLSDDMKALRPTIFPVVPRLLNRMYDKI---FHQAdTSLKRWLLEFAaKRKQAEV-------RSGIIRNNSIW 412
Cdd:cd05933 228 QPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkavGAKS-GTLKRKIASWA-KGVGLETnlklmggESPSPLFYRLA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 413 DELFFNKIQASLG-GHVRMIVTGAAPASPTVLGFLrAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKL 491
Cdd:cd05933 306 KKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 492 V--DAEelnywtskGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVA 569
Cdd:cd05933 385 HnpDAD--------GIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 570 PEKIENIYIRSEP-VAQIYVHGDSLKaFLVGIVV------PD---------PEVMPcWAQKKGIEGNY-QELCKSKELK- 631
Cdd:cd05933 457 PVPIEDAVKKELPiISNAMLIGDKRK-FLSMLLTlkcevnPEtgepldeltEEAIE-FCRKLGSQATRvSEIAGGKDPKv 534
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937369599 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 |
5.87e-69 |
|
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: 232.78 E-value: 5.87e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 92 MYQVFRRGLSISGNGPCLGFRkpeqpYQWLSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELACYTYS 171
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG-----GRRLTYAELDARARRLAAALRALG--VGPGDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 172 MVVVPLYDTLGPGSIRYIINTADICTVIVdkphkailllehverketpglklvilmepfddalrergkkcgvdiksmqai 251
Cdd:COG0318 74 AVVVPLNPRLTAEELAYILEDSGARALVT--------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 252 edsgqenhrvpvpprpddlSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWAPTCADVHFSYLPLAHMFErMVQ 331
Cdd:COG0318 103 -------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAA----LGLTPGDVVLVALPLFHVFG-LTV 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 332 SVVYC--HGGRV----GFfqgDIRLLSDDMKALRPTIFPVVPRLLNRMYDKI-FHQADTSlkrwllefaakrkqaevrsg 404
Cdd:COG0318 159 GLLAPllAGATLvllpRF---DPERVLELIERERVTVLFGVPTMLARLLRHPeFARYDLS-------------------- 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 405 iirnnsiwdelffnkiqaslggHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGA 482
Cdd:COG0318 216 ----------------------SLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGR 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 483 PLPCNHIKLVDAE--ELnywtSKGE-GEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHI 559
Cdd:COG0318 274 PLPGVEVRIVDEDgrEL----PPGEvGEIVVRGPNVMKGYWNDPEATAEAFR-DGWLRTGDLGRLDEDGYLYIVGRKKDM 348
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1937369599 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 |
4.41e-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: 231.19 E-value: 4.41e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGSGLlQHDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:cd17632 68 ITYAELWERVGAVAAAH-DPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 201 DKPHKAiLLLEHVERKETPGLKLVILMEPFDDA-------LRERGKKCGVDIKSMQAIEDSGQE---NHRVPVPPRPDDL 270
Cdd:cd17632 147 SAEHLD-LAVEAVLEGGTPPRLVVFDHRPEVDAhraalesARERLAAVGIPVTTLTLIAVRGRDlppAPLFRPEPDDDPL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 271 SIVCFTSGTTGNPKGAMLTHgNVVADFsgFLKVTESQWAPTCADVHFSYLPLAHMFERMVQSVVYCHGGrVGFFQG--DI 348
Cdd:cd17632 226 ALLIYTSGSTGTPKGAMYTE-RLVATF--WLKVSSIQDIRPPASITLNFMPMSHIAGRISLYGTLARGG-TAYFAAasDM 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 349 RLLSDDMKALRPTIFPVVPRLLNRMYDKifHQADtsLKRWL-----LEFAAKRKQAEVRsgiirnnsiwdelffnkiQAS 423
Cdd:cd17632 302 STLFDDLALVRPTELFLVPRVCDMLFQR--YQAE--LDRRSvagadAETLAERVKAELR------------------ERV 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 424 LGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTtpgdwtSGHVGAPlPCNHIKLVDAEELNYWTSK 503
Cdd:cd17632 360 LGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE--AGAVIL------DGVIVRP-PVLDYKLVDVPELGYFRTD 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 504 G---EGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRS 580
Cdd:cd17632 431 RphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFAAS 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 581 EPVAQIYVHGDSLKAFLVGIVVPDPEVmpcwaqkkgiegnyQELCKSKELKKAILDDMVMLGKESGLHSFEQVKAIYIHC 660
Cdd:cd17632 511 PLVRQIFVYGNSERAYLLAVVVPTQDA--------------LAGEDTARLRAALAESLQRIAREAGLQSYEIPRDFLIET 576
|
570
....*....|.
gi 1937369599 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 |
3.06e-63 |
|
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: 220.37 E-value: 3.06e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 118 YQWLSYQEVAKRAEFLGSGLlqHDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICT 197
Cdd:cd17641 9 WQEFTWADYADRVRAFALGL--LALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 198 VIVDKPHKAILLLEHveRKETPGLKLVILMEP------FDDALRergkkcgvdikSMQAIEDSGQENHRVPvpP------ 265
Cdd:cd17641 87 VIAEDEEQVDKLLEI--ADRIPSVRYVIYCDPrgmrkyDDPRLI-----------SFEDVVALGRALDRRD--Pglyere 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 266 ----RPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESqwAPTcaDVHFSYLPLAHMFERM---VQSVVycHG 338
Cdd:cd17641 152 vaagKGEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPL--GPG--DEYVSVLPLPWIGEQMysvGQALV--CG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 339 GRVGFFQgDIRLLSDDMKALRPTIFPVVPRLLN--------RMYDKifhqadTSLKRWL--------LEFAAKRKQAEVR 402
Cdd:cd17641 226 FIVNFPE-EPETMMEDLREIGPTFVLLPPRVWEgiaadvraRMMDA------TPFKRFMfelgmklgLRALDRGKRGRPV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 403 SGIIRNNS-IWDELFFNKIQASLG-GHVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTEcTAGCTFTTP-GDWTSGH 479
Cdd:cd17641 299 SLWLRLASwLADALLFRPLRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTE-LAGAYTVHRdGDVDPDT 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 480 VGAPLPCNHIKLVDaeelnywtskgEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHI 559
Cdd:cd17641 377 VGVPFPGTEVRIDE-----------VGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDV 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 560 FKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSlKAFLVGIVVPDPEVMPCWAQKKGIE-GNYQELCKSKELKKAILDDM 638
Cdd:cd17641 446 GTTSDGTRFSPQFIENKLKFSPYIAEAVVLGAG-RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEV 524
|
....*.
gi 1937369599 639 VMLGKE 644
Cdd:cd17641 525 EKVNAS 530
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
93-598 |
8.68e-60 |
|
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: 208.19 E-value: 8.68e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 93 YQVFRRGLSISGNGPCLGFRKpeqpyQWLSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSM 172
Cdd:cd05936 2 ADLLEEAARRFPDKTALIFMG-----RKLTYRELDALAEAFAAGLQNLGVQPGDR--VALMLPNCPQFPIAYFGALKAGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 173 VVVPLYDTLGPGSIRYIINTAdictvivdkphkailllehverketpGLKLVILMEPFDDALrergkkcgvdiksmqaie 252
Cdd:cd05936 75 VVVPLNPLYTPRELEHILNDS--------------------------GAKALIVAVSFTDLL------------------ 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 253 dSGQENHRVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTcaDVHFSYLPLAHMFErmvQS 332
Cdd:cd05936 111 -AAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEGD--DVVLAALPLFHVFG---LT 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 333 VVYCHGGRVGFFQ------GDIRLLsDDMKALRPTIFPVVPRllnrMYDKIFHQADtslkrwllefaakrkqaevrsgii 406
Cdd:cd05936 185 VALLLPLALGATIvliprfRPIGVL-KEIRKHRVTIFPGVPT----MYIALLNAPE------------------------ 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 407 rnnsiwdelfFNKIQASlggHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT-SGHVGAPLP 485
Cdd:cd05936 236 ----------FKKRDFS---SLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRkPGSIGIPLP 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 486 CNHIKLVDAE--ELnywtSKGE-GEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFkL 562
Cdd:cd05936 303 GTEVKIVDDDgeEL----PPGEvGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMI-I 376
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1937369599 563 AQGEYVAPEKIENIYIRSEPVAQIYV-------HGDSLKAFLV 598
Cdd:cd05936 377 VGGFNVYPREVEEVLYEHPAVAEAAVvgvpdpySGEAVKAFVV 419
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
121-606 |
9.09e-60 |
|
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: 208.07 E-value: 9.09e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGsgLLQHDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:cd05914 8 LTYKDLADNIAKFA--LLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 201 DKPhkailllehverketpglklvilmepfddalrergkkcgvdiksmqaiedsgqenhrvpvpprpDDLSIVCFTSGTT 280
Cdd:cd05914 86 SDE----------------------------------------------------------------DDVALINYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 281 GNPKGAMLTHGNVVADFSG---FLKVTESqwaptcaDVHFSYLPLAHMFERMVQSVVYCHGGRVGFFQGDI---RLLSDD 354
Cdd:cd05914 102 GNSKGVMLTYRNIVSNVDGvkeVVLLGKG-------DKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIpsaKIIALA 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 355 MKALRPTIfpVVPRLLNRMYDKIFHQADTSLKRWLLEFAAKrkqaevrsgIIRNNSIWdELFFNKIQASLGGHVRMIVTG 434
Cdd:cd05914 175 FAQVTPTL--GVPVPLVIEKIFKMDIIPKLTLKKFKFKLAK---------KINNRKIR-KLAFKKVHEAFGGNIKEFVIG 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 435 AAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEElnywtSKGEGEICVKGPN 514
Cdd:cd05914 243 GAKINPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDP-----ATGEGEIIVRGPN 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 515 VFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVA--QIYVHGDS 592
Cdd:cd05914 317 VMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLesLVVVQEKK 396
|
490
....*....|....
gi 1937369599 593 LKAflvgIVVPDPE 606
Cdd:cd05914 397 LVA----LAYIDPD 406
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
121-598 |
2.64e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 208.22 E-value: 2.64e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGKGDR--VAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 201 -------DKP-HKAILLLEHVERKETP-GLKLVILMEPFDDALRergkkcgvdiksmqaiedSGQENHRVPvPPRPDDLS 271
Cdd:PRK07656 109 lglflgvDYSaTTRLPALEHVVICETEeDDPHTEKMKTFTDFLA------------------AGDPAERAP-EVDPDDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 272 IVCFTSGTTGNPKGAMLTHGNV---VADFSGFLKVTESqwaptcaDVHFSYLPLAHMFERMVqSVVYC--HGGRV---GF 343
Cdd:PRK07656 170 DILFTSGTTGRPKGAMLTHRQLlsnAADWAEYLGLTEG-------DRYLAANPFFHVFGYKA-GVNAPlmRGATIlplPV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 344 FQGD--IRLLSDDmkalRPTIFPVVPRLLNRMYDkifhqadtslkrwllefAAKRKQAEVRSgiirnnsiwdelffnkiq 421
Cdd:PRK07656 242 FDPDevFRLIETE----RITVLPGPPTMYNSLLQ-----------------HPDRSAEDLSS------------------ 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 422 aslgghVRMIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGCTFTTPGD---WTSGHVGAPLPCNHIKLVDaeEL 497
Cdd:PRK07656 283 ------LRLAVTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIAGVENKIVN--EL 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 498 NYWTSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENI 576
Cdd:PRK07656 355 GEEVPVGEvGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IVGGFNVYPAEVEEV 433
|
490 500
....*....|....*....|....*....
gi 1937369599 577 YIRSEPVAQIYV-------HGDSLKAFLV 598
Cdd:PRK07656 434 LYEHPAVAEAAVigvpderLGEVGKAYVV 462
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
269-606 |
1.32e-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: 201.36 E-value: 1.32e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 269 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWAPTCADVHFSYLPLAHMFerMVQSVVYC--HGGRVGFFQG 346
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS----GGLTEGDVFLSTLPLFHIG--GLFGLLGAllAGGTVVLLPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 347 -DIRLLSDDMKALRPTIFPVVPRLLNRmydkifhqadtslkrwLLEFAAKRKQAevrsgiirnnsiwdelffnkiQASLg 425
Cdd:cd04433 75 fDPEAALELIEREKVTILLGVPTLLAR----------------LLKAPESAGYD---------------------LSSL- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 426 ghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT--SGHVGAPLPCNHIKLVDaEELNYWTSK 503
Cdd:cd04433 117 ---RALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVD-PDGGELPPG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 504 GEGEICVKGPNVFKGYLKDEDRTkEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSEPV 583
Cdd:cd04433 193 EIGELVVRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPGV 270
|
330 340
....*....|....*....|...
gi 1937369599 584 AQIYVHGdslkaflvgivVPDPE 606
Cdd:cd04433 271 AEAAVVG-----------VPDPE 282
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
121-598 |
1.24e-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: 183.57 E-value: 1.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGSGLLQHDCKVGteQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKG--DVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 201 DKPhkailLLEHVER--KETPGLKLVILMEPFDDALRergkkcgvDIKSMQAIEDSGQENHRVPVPPR-PDDLSIVCFTS 277
Cdd:cd05911 89 DPD-----GLEKVKEaaKELGPKDKIIVLDDKPDGVL--------SIEDLLSPTLGEEDEDLPPPLKDgKDDTAAILYSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 278 GTTGNPKGAMLTHGNVVADFS---GFLKVTESQwaptcADVHFSYLPLAHMF--ERMVQSVVYchGGRV----GFFqgdi 348
Cdd:cd05911 156 GTTGLPKGVCLSHRNLIANLSqvqTFLYGNDGS-----NDVILGFLPLYHIYglFTTLASLLN--GATViimpKFD---- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 349 rllSDDMKAL----RPTIFPVVPRLLNRMydkifhqadtslkrwllefaakrkqaeVRSGIirnnsiwdelfFNKIQASl 424
Cdd:cd05911 225 ---SELFLDLiekyKITFLYLVPPIAAAL---------------------------AKSPL-----------LDKYDLS- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 425 ggHVRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYWTSK 503
Cdd:cd05911 263 --SLRVILSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 504 GEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIyIRSEP- 582
Cdd:cd05911 341 EPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAV-LLEHPg 418
|
490 500
....*....|....*....|...
gi 1937369599 583 -----VAQIY--VHGDSLKAFLV 598
Cdd:cd05911 419 vadaaVIGIPdeVSGELPRAYVV 441
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
86-605 |
2.25e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 178.07 E-value: 2.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 86 YDDARTMYQVFRRGLSISGNGPCLGFRKPEqpyqwLSYQEVAKRAEFLGSGLLqhDCKVGTEQFIGVFAQNRPEWIIAEL 165
Cdd:PRK06187 2 QDYPLTIGRILRHGARKHPDKEAVYFDGRR-----TTYAELDERVNRLANALR--ALGVKKGDRVAVFDWNSHEYLEAYF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 166 ACytySM---VVVPLYDTLGPGSIRYIINTADICTVIVDKPhkailLLEHVE--RKETPGLKLVILMEPFDDALrergkk 240
Cdd:PRK06187 75 AV---PKigaVLHPINIRLKPEEIAYILNDAEDRVVLVDSE-----FVPLLAaiLPQLPTVRTVIVEGDGPAAP------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 241 CGVDIKSMQAIEDsGQENHRVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVvadFSGFLKVTES-QWapTCADVHFSY 319
Cdd:PRK06187 141 LAPEVGEYEELLA-AASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNL---FLHSLAVCAWlKL--SRDDVYLVI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 320 LPLAHMFERMVqsvvychgGRVGFFQG---------DIRLLSDDMKALRPTIFPVVPRLLNRMydkifHQADTSLKRWLl 390
Cdd:PRK06187 215 VPMFHVHAWGL--------PYLALMAGakqviprrfDPENLLDLIETERVTFFFAVPTIWQML-----LKAPRAYFVDF- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 391 efaakrkqaevrsgiirnnsiwdelffnkiqaslgGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFT 470
Cdd:PRK06187 281 -----------------------------------SSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVL 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 471 TPGDWTSGH------VGAPLPCNHIKLVDAEELNYWTSKGE-GEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGK 543
Cdd:PRK06187 326 PPEDQLPGQwtkrrsAGRPLPGVEARIVDDDGDELPPDGGEvGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGY 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937369599 544 WLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIyirsepvaqIYVHGDSLKAFLVGivVPDP 605
Cdd:PRK06187 405 IDEDGYLYITDRIKDVIISG-GENIYPRELEDA---------LYGHPAVAEVAVIG--VPDE 454
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
233-694 |
7.38e-45 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 171.83 E-value: 7.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 233 ALRERGKKCGVDIksMQAIEDSGQENHRVPVP-PRPDDLSIVCFTSGTTGNPKGAMLTHGNV------VADFSGFLKvte 305
Cdd:PTZ00342 270 DLKEKAKKLGISI--ILFDDMTKNKTTNYKIQnEDPDFITSIVYTSGTSGKPKGVMLSNKNLyntvvpLCKHSIFKK--- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 306 sqWAPtcaDVHFSYLPLAHMFERMVQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQAD--T 383
Cdd:PTZ00342 345 --YNP---KTHLSYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINnlP 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 384 SLKRWLLE--FAAKRkqaevrsgiiRNNSIWDELFF-------NKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQV 454
Cdd:PTZ00342 420 PLKRFLVKkiLSLRK----------SNNNGGFSKFLegithisSKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNY 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 455 YEGYGQTEcTAGCTFTTPG-DWTSGHVGAPL-PCNHIKLVDAEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEALDS 532
Cdd:PTZ00342 490 YQGYGLTE-TTGPIFVQHAdDNNTESIGGPIsPNTKYKVRTWETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTE 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 533 DGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHG-DSLKAFLVGIVVPDPEVMPCW 611
Cdd:PTZ00342 569 DGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGdDSMDGPLAIISVDKYLLFKCL 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 612 A-----QKKGI-EGNYQELCKSKELKKAILDDMV---MLG--KESGLHSFEQVKAIYIHCDMFSVQNgLLTPTLKAKRPE 680
Cdd:PTZ00342 649 KddnmlESTGInEKNYLEKLTDETINNNIYVDYVkgkMLEvyKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKRFY 727
|
490
....*....|....*..
gi 1937369599 681 L-REY--FKKQIEELYS 694
Cdd:PTZ00342 728 VfKDYafFIDQVKKIYK 744
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
121-609 |
6.26e-41 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 155.53 E-value: 6.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLgSGLLQHDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIv 200
Cdd:cd05941 12 ITYADLVARAARL-ANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 201 dkphkailllehverketpglklvilmepfDDALrergkkcgvdiksmqaiedsgqenhrvpvpprpddlsiVCFTSGTT 280
Cdd:cd05941 90 ------------------------------DPAL--------------------------------------ILYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 281 GNPKGAMLTHGNVVADfsgfLKVTESQWAPTCADVHFSYLPLAHmfermVQSVV-------YChGGRV---GFFQGDIRL 350
Cdd:cd05941 102 GRPKGVVLTHANLAAN----VRALVDAWRWTEDDVLLHVLPLHH-----VHGLVnallcplFA-GASVeflPKFDPKEVA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 351 LSDDMKALrpTIFPVVPRllnrMYDKIFHQADTSLKrwllEFAAKRKQAEvrsgiirnnsiwdelffnkiqaslgGHVRM 430
Cdd:cd05941 172 ISRLMPSI--TVFMGVPT----IYTRLLQYYEAHFT----DPQFARAAAA-------------------------ERLRL 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 431 IVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTTP--GDWTSGHVGAPLPCNHIKLVDAEELNYWTSKGEGEI 508
Cdd:cd05941 217 MVSGSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEI 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 509 CVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKK-HIFKlAQGEYVAPEKIENIYIRSEPVAQIY 587
Cdd:cd05941 295 QVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEIERVLLAHPGVSECA 373
|
490 500
....*....|....*....|....*
gi 1937369599 588 VHGDSLKAF---LVGIVVPDPEVMP 609
Cdd:cd05941 374 VIGVPDPDWgerVVAVVVLRAGAAA 398
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
121-576 |
3.69e-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: 154.31 E-value: 3.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGSGLlqHDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTAdictviv 200
Cdd:cd05904 33 LTYAELERRVRRLAAGL--AKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDS------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 201 dKPHKAILLLEHVERKETPGLKLVILMEPFDDALRergkkcgvdIKSMQAIEDSGQenhrVPVPP-RPDDLSIVCFTSGT 279
Cdd:cd05904 104 -GAKLAFTTAELAEKLASLALPVVLLDSAEFDSLS---------FSDLLFEADEAE----PPVVViKQDDVAALLYSSGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 280 TGNPKGAMLTHGNVVADFSGFLKVTESQWAPTcaDVHFSYLPLAHMFermvqsvvychgGRVGFFQGDIRL--------- 350
Cdd:cd05904 170 TGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSE--DVFLCVLPMFHIY------------GLSSFALGLLRLgatvvvmpr 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 351 --LSDDMKAL---RPTIFPVVPRLLnrmydkifhqadtslkrwllefAAKRKQAEVRSGIIRnnsiwdelffnkiqaSLg 425
Cdd:cd05904 236 fdLEELLAAIeryKVTHLPVVPPIV----------------------LALVKSPIVDKYDLS---------------SL- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 426 ghvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFTTP---GDWTSGHVGAPLPCNHIKLVDAEELNYWT 501
Cdd:cd05904 278 ---RQIMSGAAPLGKELIeAFRAKFPNVDLGQGYGMTESTGVVAMCFApekDRAKYGSVGRLVPNVEAKIVDPETGESLP 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937369599 502 SKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENI 576
Cdd:cd05904 355 PNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEAL 428
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
96-605 |
4.64e-40 |
|
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: 152.76 E-value: 4.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 96 FRRGLSISGNGPCLGFRKPEqpyqwLSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVV 175
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRS-----LTYAELDERVNRLAHALRALGVAKGDR--VAVLSKNSPEFLELLFAAARLGAVFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 176 PLYDTLGPGSIRYIINTAdictvivdkphkailllehverketpGLKLVIlmepfddalrergkkcgvdiksmqaiedsg 255
Cdd:cd17631 74 PLNFRLTPPEVAYILADS--------------------------GAKVLF------------------------------ 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 256 qenhrvpvpprpDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLkvteSQWAPTCADVHFSYLPLAHMFE-RMVQSVV 334
Cdd:cd17631 98 ------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNAL----AALDLGPDDVLLVVAPLFHIGGlGVFTLPT 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 335 YCHGGRV----GFfqgDIRLLSDDMKALRPTIFPVVPRLLNRMYDK-IFHQADTSlkrwllefaakrkqaevrsgiirnn 409
Cdd:cd17631 162 LLRGGTVvilrKF---DPETVLDLIERHRVTSFFLVPTMIQALLQHpRFATTDLS------------------------- 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 410 siwdelffnkiqaSLgghvRMIVTGAAPASPTVLGFLRAAlGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPCN 487
Cdd:cd17631 214 -------------SL----RAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHRRklGSAGRPVFFV 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 488 HIKLVDAE--ELnywtSKGE-GEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQ 564
Cdd:cd17631 276 EVRIVDPDgrEV----PPGEvGEIVVRGPHVMAGYWNRPEATAAAFR-DGWFHTGDLGRLDEDGYLYIVDRKKDMII-SG 349
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1937369599 565 GEYVAPEKIENIyirsepvaqIYVHGDSLKAFLVGivVPDP 605
Cdd:cd17631 350 GENVYPAEVEDV---------LYEHPAVAEVAVIG--VPDE 379
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
121-576 |
9.32e-39 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 150.17 E-value: 9.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGSgLLQHDCKVGteQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:cd05909 8 LTYRKLLTGAIALAR-KLAKMTKEG--ENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 201 DKPHKAILLLEHVERKETPgLKLVILmepfdDALRER---GKKCGVDIKSMQAIEDSGQENHRVPVppRPDDLSIVCFTS 277
Cdd:cd05909 85 SKQFIEKLKLHHLFDVEYD-ARIVYL-----EDLRAKiskADKCKAFLAGKFPPKWLLRIFGVAPV--QPDDPAVILFTS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 278 GTTGNPKGAMLTHGNVVADFSGFLKVTEsqwaPTCADVHFSYLPLAHMFermvqsvvychggrvGFFQGDIRLLSDDMKA 357
Cdd:cd05909 157 GSEGLPKGVVLSHKNLLANVEQITAIFD----PNPEDVVFGALPFFHSF---------------GLTGCLWLPLLSGIKV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 358 L---RPTIFPVVPRLLnrmYDK---IFHQADTSLKRWllefaAKRKQAEVRSGIirnnsiwdelffnkiqaslgghvRMI 431
Cdd:cd05909 218 VfhpNPLDYKKIPELI---YDKkatILLGTPTFLRGY-----ARAAHPEDFSSL-----------------------RLV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 432 VTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPCNHIKLVDAEELNYWTSKGEGEICV 510
Cdd:cd05909 267 VAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLV 346
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937369599 511 KGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENI 576
Cdd:cd05909 347 RGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDI 410
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
120-683 |
2.19e-37 |
|
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: 146.30 E-value: 2.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 120 WLSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVI 199
Cdd:cd05926 14 ALTYADLAELVDDLARQLAALGIKKGDR--VAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 200 VDKPHkailLLEHVERKETPGLKLVILMepFDDALRERgkkcgVDIKSMQAIEDSGQENHRVPVPPRPDDLSIVCFTSGT 279
Cdd:cd05926 92 TPKGE----LGPASRAASKLGLAILELA--LDVGVLIR-----APSAESLSNLLADKKNAKSEGVPLPDDLALILHTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 280 TGNPKGAMLTHGNVVADFSGFLKVtesqWAPTCADVHFSYLPLAHMFERMVQ--SVVYChGGRV----GFfqgDIRLLSD 353
Cdd:cd05926 161 TGRPKGVPLTHRNLAASATNITNT----YKLTPDDRTLVVMPLFHVHGLVASllSTLAA-GGSVvlppRF---SASTFWP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 354 DMKALRPTIFPVVPRLlnrmydkifHQAdtslkrwLLEFAAKRKQAEVrsgiirnnsiwdelffnkiqaslgGHVRMIVT 433
Cdd:cd05926 233 DVRDYNATWYTAVPTI---------HQI-------LLNRPEPNPESPP------------------------PKLRFIRS 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 434 GAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTP---GDWTSGHVGAPLPcNHIKLVDaEELNYWTSKGEGEICV 510
Cdd:cd05926 273 CSASLPPAVLEALEATFGAPVLEAYGMTE-AAHQMTSNPlppGPRKPGSVGKPVG-VEVRILD-EDGEILPPGVVGEICL 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 511 KGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQIYVHG 590
Cdd:cd05926 350 RGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVLLSHPAVLEAVAFG 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 591 dslkaflvgivVPDP---EVMPCWAQKKGiegnyqelcKSKELKKAILDDMvmlgkESGLHSFEQVKAIYIhcdmfsVQN 667
Cdd:cd05926 429 -----------VPDEkygEEVAAAVVLRE---------GASVTEEELRAFC-----RKHLAAFKVPKKVYF------VDE 477
|
570
....*....|....*.
gi 1937369599 668 GLLTPTLKAKRPELRE 683
Cdd:cd05926 478 LPKTATGKIQRRKVAE 493
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
255-604 |
5.10e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 143.60 E-value: 5.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 255 GQENHRVPVP-PRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgflkVTESQ-WAPTCAD---VHFSYLPLAHMFE-R 328
Cdd:PRK05605 205 GGDGSDVSHPrPTPDDVALILYTSGTTGKPKGAQLTHRNLFAN------AAQGKaWVPGLGDgpeRVLAALPMFHAYGlT 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 329 MVQSV-VYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLlnrmYDKIfhqadtslkrwlLEFAAKRkqaevrsGIir 407
Cdd:PRK05605 279 LCLTLaVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPL----YEKI------------AEAAEER-------GV-- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 408 nnsiwdelffnkiqaSLGGhVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECT---AGCTFTTpgDWTSGHVGAPL 484
Cdd:PRK05605 334 ---------------DLSG-VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpiiVGNPMSD--DRRPGYVGVPF 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 485 PCNHIKLVDAEELNYWTSKGE-GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLA 563
Cdd:PRK05605 396 PDTEVRIVDPEDPDETMPDGEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELI-IT 473
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1937369599 564 QGEYVAPEKIEniyirsEPVAQiyvHGDSLKAFLVGIVVPD 604
Cdd:PRK05605 474 GGFNVYPAEVE------EVLRE---HPGVEDAAVVGLPRED 505
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
123-615 |
9.35e-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: 134.50 E-value: 9.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 123 YQEVAKRAEFLgsgllqHDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIVDK 202
Cdd:TIGR01923 6 DCEAAHLAKAL------KAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 203 PhkailllehverketpglklvilmepfddaLRERGkkcgVDIKSMQAIEDSGQENHRVPVPPRPDDLSIVCFTSGTTGN 282
Cdd:TIGR01923 80 L------------------------------LEEKD----FQADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 283 PKGAMLTHGNVVADFSGF---LKVTESqwaptcaDVHFSYLPLAHMFErmvQSVVY---CHGGRVGFFQGDIRLLsDDMK 356
Cdd:TIGR01923 126 PKAVPHTFRNHYASAVGSkenLGFTED-------DNWLLSLPLYHISG---LSILFrwlIEGATLRIVDKFNQLL-EMIA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 357 ALRPTIFPVVPRLLNRMYDKIFHqaDTSLKRWLLefaakrkqaevrsgiirnnsiwdelffnkiqaslGGhvrmivtGAA 436
Cdd:TIGR01923 195 NERVTHISLVPTQLNRLLDEGGH--NENLRKILL----------------------------------GG-------SAI 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 437 PASptvlgFLRAAL--GCQVYEGYGQTE-CTAGCTFTTPGDWTSGHVGAPLPCNHIKL-VDAEElnywtskGEGEICVKG 512
Cdd:TIGR01923 232 PAP-----LIEEAQqyGLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIkVDNKE-------GHGEIMVKG 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 513 PNVFKGYLKDEDRTkEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYV--HG 590
Cdd:TIGR01923 300 ANLMKGYLYQGELT-PAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVVvpKP 377
|
490 500 510
....*....|....*....|....*....|
gi 1937369599 591 DSL-----KAFLVGIVVPDPEVMPCWAQKK 615
Cdd:TIGR01923 378 DAEwgqvpVAYIVSESDISQAKLIAYLTEK 407
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
137-606 |
2.59e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 134.16 E-value: 2.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 137 LLQHDCKVGteQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADictvivdkphkailllehverk 216
Cdd:PRK09088 39 LRRRGCVDG--ERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAE---------------------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 217 etPGLKLvilmepfDDALRERGKKCGVDIKSMQAIEDSGQENHRVPVPPrpDDLSIVCFTSGTTGNPKGAMLTHGN---V 293
Cdd:PRK09088 95 --PRLLL-------GDDAVAAGRTDVEDLAAFIASADALEPADTPSIPP--ERVSLILFTSGTSGQPKGVMLSERNlqqT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 294 VADFSGFLKVtesqwaptcaDVHFSYLPLAHMFE--RMVQSV--VYCHGGRV----GFFQG-DIRLLSDdmKALRPTIFP 364
Cdd:PRK09088 164 AHNFGVLGRV----------DAHSSFLCDAPMFHiiGLITSVrpVLAVGGSIlvsnGFEPKrTLGRLGD--PALGITHYF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 365 VVPRllnrMYDKIFHQADtslkrwlleFAAkrkqaevrsgiirnnsiwdelffnkiqASLGgHVRMIVTGAAP-ASPTVL 443
Cdd:PRK09088 232 CVPQ----MAQAFRAQPG---------FDA---------------------------AALR-HLTALFTGGAPhAAEDIL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 444 GFLraALGCQVYEGYGQTEctAGCTFTTPGDWT-----SGHVGAPLPCNHIKLVDAEELNywTSKGE-GEICVKGPNVFK 517
Cdd:PRK09088 271 GWL--DDGIPMVDGFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVVDDQGND--CPAGVpGELLLRGPNLSP 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 518 GYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIEniyirsepvAQIYVHGDSLKAFL 597
Cdd:PRK09088 345 GYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIE---------AVLADHPGIRECAV 414
|
....*....
gi 1937369599 598 VGivVPDPE 606
Cdd:PRK09088 415 VG--MADAQ 421
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
262-598 |
2.64e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 135.28 E-value: 2.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 262 PVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTCaDVHFSYLPLAHMFERMVQSVVYCHGGRV 341
Cdd:PRK05677 201 EANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEGC-EILIAPLPLYHIYAFTFHCMAMMLIGNH 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 342 GFFQGDIRLLSDDMKALRPTIFPVVPRLlNRMydkifhqadtslkrwlleFAAkrkqaevrsgiIRNNSIWDELFFNKIQ 421
Cdd:PRK05677 280 NILISNPRDLPAMVKELGKWKFSGFVGL-NTL------------------FVA-----------LCNNEAFRKLDFSALK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 422 ASLGGHvrMIVTGAAPASptvlgfLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVD--AEELny 499
Cdd:PRK05677 330 LTLSGG--MALQLATAER------WKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDddGNEL-- 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 500 wtSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYI 578
Cdd:PRK05677 400 --PLGEvGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVSGFNVYPNELEDVLA 476
|
330 340
....*....|....*....|....*..
gi 1937369599 579 RSEPVAQ---IYV----HGDSLKAFLV 598
Cdd:PRK05677 477 ALPGVLQcaaIGVpdekSGEAIKVFVV 503
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
93-636 |
8.98e-33 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 133.70 E-value: 8.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 93 YQVFRRGLSISGNGPCLGFRKPEQPYQWLSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELACYTYSM 172
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRALG--VKKGDRVAIYLPNIPEAVIAMLACARIGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 173 VVVPLYDTLGPGSIRYIINTADICTVIVD----KPHKAILLLEHVE--RKETPGLKLVILMEPFDDALRERGkkcgvDIK 246
Cdd:COG0365 90 VHSPVFPGFGAEALADRIEDAEAKVLITAdgglRGGKVIDLKEKVDeaLEELPSLEHVIVVGRTGADVPMEG-----DLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 247 SMQAIEDSGQENHRVPVPPrpDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsGFLKVTESQWAPTCADVHFS-------- 318
Cdd:COG0365 165 WDELLAAASAEFEPEPTDA--DDPLFILYTSGTTGKPKGVVHTHGGYLV---HAATTAKYVLDLKPGDVFWCtadigwat 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 319 ------YLPLAH-----MFERmvqSVVYCHGGRVgffqgdIRLLSDdmkaLRPTIFPVVPRLLnRMydkifhqadtsLKR 387
Cdd:COG0365 240 ghsyivYGPLLNgatvvLYEG---RPDFPDPGRL------WELIEK----YGVTVFFTAPTAI-RA-----------LMK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 388 WLLEFAAKRKQAevrsgiirnnsiwdelffnkiqaslggHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECtaGC 467
Cdd:COG0365 295 AGDEPLKKYDLS---------------------------SLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTET--GG 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 468 TFTTPGDWTS---GHVGAPLPCNHIKLVDAE--ELnywTSKGEGEICVKG--PNVFKGYLKDEDRTKEAL--DSDGWLHT 538
Cdd:COG0365 346 IFISNLPGLPvkpGSMGKPVPGYDVAVVDEDgnPV---PPGEEGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRT 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 539 GDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQIYVhgdslkaflVGivVPDP---EVMPCWAQ-K 614
Cdd:COG0365 423 GDGARRDEDGYFWILGRSDDVINVS-GHRIGTAEIESALVSHPAVAEAAV---------VG--VPDEirgQVVKAFVVlK 490
|
570 580
....*....|....*....|..
gi 1937369599 615 KGIEGnyqelckSKELKKAILD 636
Cdd:COG0365 491 PGVEP-------SDELAKELQA 505
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
259-605 |
5.78e-32 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 131.15 E-value: 5.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 259 HRVP-VPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSgflkvTESQWAPTCA------DVHFSYLPLAHMFERMVQ 331
Cdd:PRK08751 198 HSMPtLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQ-----QAHQWLAGTGkleegcEVVITALPLYHIFALTAN 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 332 SVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLlNRMYDKIFhqadtslkrwllefaakrkqaevrsgiirNNSI 411
Cdd:PRK08751 273 GLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGV-NTLFNGLL-----------------------------NTPG 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 412 WDELFFNKIQASLGGHvrMIVTGAapasptVLGFLRAALGCQVYEGYGQTECT-AGCTFTTPGDWTSGHVGAPLPCNHIK 490
Cdd:PRK08751 323 FDQIDFSSLKMTLGGG--MAVQRS------VAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDAC 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 491 LVDaeELNYWTSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVA 569
Cdd:PRK08751 395 IKD--DAGTVLAIGEiGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-LVSGFNVY 471
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1937369599 570 PEKIENIYIRSEPVAQIYVHG----DSLKAFLVGIVVPDP 605
Cdd:PRK08751 472 PNEIEDVIAMMPGVLEVAAVGvpdeKSGEIVKVVIVKKDP 511
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
267-598 |
7.59e-32 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 130.94 E-value: 7.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgflkVTESQWA--PTCADVH---FSYLPLAHMFERMVQSVVYCHGGRV 341
Cdd:PRK08974 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLAN------LEQAKAAygPLLHPGKelvVTALPLYHIFALTVNCLLFIELGGQ 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 342 GFF---QGDIRLLSDDMKALRPTIFPVVPRLLNRmydkifhqadtslkrWLlefaakrkqaevrsgiirNNSIWDELFFN 418
Cdd:PRK08974 279 NLLitnPRDIPGFVKELKKYPFTAITGVNTLFNA---------------LL------------------NNEEFQELDFS 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 419 KIQASLGGhvrmivtgAAPASPTVLGFLRAALGCQVYEGYGQTECT---AGCTFTTPGdwTSGHVGAPLPCNHIKLVDaE 495
Cdd:PRK08974 326 SLKLSVGG--------GMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVNPYDLDY--YSGSIGLPVPSTEIKLVD-D 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 496 ELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIEN 575
Cdd:PRK08974 395 DGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMI-LVSGFNVYPNEIED 472
|
330 340 350
....*....|....*....|....*....|
gi 1937369599 576 IYIRSEPVAQIY-------VHGDSLKAFLV 598
Cdd:PRK08974 473 VVMLHPKVLEVAavgvpseVSGEAVKIFVV 502
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
122-606 |
1.35e-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: 129.57 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 122 SYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLgpgSIRYIINTADICT-VIV 200
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYG--LKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIY---NERELDHSLNISKpTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 201 DKPHKAILLLEHVERKeTPGLKLVILMEPFDDAlreRGKKCGVDIKSMQAIEDSGQENHRVPVPPRPDDLSIVCFTSGTT 280
Cdd:cd17642 121 FCSKKGLQKVLNVQKK-LKIIKTIIILDSKEDY---KGYQCLYTFITQNLPPGFNEYDFKPPSFDRDEQVALIMNSSGST 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 281 GNPKGAMLTHGNVVADFSGFLKVT-ESQWAPTCADVhfSYLPLAHMFERMVQSVVYCHGGRVGffqgdirllsddmkalr 359
Cdd:cd17642 197 GLPKGVQLTHKNIVARFSHARDPIfGNQIIPDTAIL--TVIPFHHGFGMFTTLGYLICGFRVV----------------- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 360 ptifpvvprLLNRMYDKIFHQA-------DTSLKRWLLEFAAKrkqaevrSGIIrnnsiwdelffNKIQASlggHVRMIV 432
Cdd:cd17642 258 ---------LMYKFEEELFLRSlqdykvqSALLVPTLFAFFAK-------STLV-----------DKYDLS---NLHEIA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 433 TGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYWTSKGEGEICVK 511
Cdd:cd17642 308 SGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVK 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 512 GPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYVHGd 591
Cdd:cd17642 388 GPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQHPKIFDAGVAG- 465
|
490
....*....|....*
gi 1937369599 592 slkaflvgivVPDPE 606
Cdd:cd17642 466 ----------IPDED 470
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
121-590 |
2.30e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 129.51 E-value: 2.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQPGDR--VGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVIC 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 201 DKPHK-----AILL-----LEHVERKET-----PGLKLVILMEPFD-------DALRERGKkcGVdikSMQAIEDSGQEN 258
Cdd:PRK12583 124 ADAFKtsdyhAMLQellpgLAEGQPGALacerlPELRGVVSLAPAPppgflawHELQARGE--TV---SREALAERQASL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 259 HRvpvpprpDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSG-FLKVTESQwaPTCADVhfsylPLAHMFErMVQSVVY 335
Cdd:PRK12583 199 DR-------DDPINIQYTSGTTGFPKGATLSHHNILnnGYFVAeSLGLTEHD--RLCVPV-----PLYHCFG-MVLANLG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 336 C--HGGRVGF----FQGDIRLLSddMKALRPTIFPVVPRL-LNRMYDKIFHQADTSlkrwllefaakrkqaEVRSGIIrn 408
Cdd:PRK12583 264 CmtVGACLVYpneaFDPLATLQA--VEEERCTALYGVPTMfIAELDHPQRGNFDLS---------------SLRTGIM-- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 409 nsiwdelffnkiqaslgghvrmivtGAAPASPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGD-----WTSghVGA 482
Cdd:PRK12583 325 -------------------------AGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSLQTTAADdlerrVET--VGR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 483 PLPCNHIKLVDAEELNywTSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFk 561
Cdd:PRK12583 378 TQPHLEVKVVDPDGAT--VPRGEiGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMI- 454
|
490 500
....*....|....*....|....*....
gi 1937369599 562 LAQGEYVAPEKIENIYIRSEPVAQIYVHG 590
Cdd:PRK12583 455 IRGGENIYPREIEEFLFTHPAVADVQVFG 483
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
117-557 |
6.27e-31 |
|
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: 127.78 E-value: 6.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 117 PYQWLSYQEVAKRAEFLGSGLLQHDCKVGtEQFIGVFAQNRpEWIIAELACYTYSMVVVPLydtlGPGSIRYIINTAdic 196
Cdd:cd05906 36 SEEFQSYQDLLEDARRLAAGLRQLGLRPG-DSVILQFDDNE-DFIPAFWACVLAGFVPAPL----TVPPTYDEPNAR--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 197 tvivdkphkaILLLEHVerKETPGLKLVI----LMEPFDDALRERGKkCGVDIKSMQAIEDSGQENHRVPvpPRPDDLSI 272
Cdd:cd05906 107 ----------LRKLRHI--WQLLGSPVVLtdaeLVAEFAGLETLSGL-PGIRVLSIEELLDTAADHDLPQ--SRPDDLAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 273 VCFTSGTTGNPKGAMLTHGNVVADFSGflKVTESQWAPtcADVHFSYLPLAHmfermVQSVVYCHggrvgffQGDIRLLS 352
Cdd:cd05906 172 LMLTSGSTGFPKAVPLTHRNILARSAG--KIQHNGLTP--QDVFLNWVPLDH-----VGGLVELH-------LRAVYLGC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 353 DDMKALRPTIFPVVPRLLNRMyDKifHQADTSlkrWLLEFA-AK-RKQAEVRSGiirnnSIWDelffnkiqasLGGHVRM 430
Cdd:cd05906 236 QQVHVPTEEILADPLRWLDLI-DR--YRVTIT---WAPNFAfALlNDLLEEIED-----GTWD----------LSSLRYL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 431 IVTGAAPASPTVLGFLRAALGCQVYE-----GYGQTECTAGCTFTTP---GDWTSGH----VGAPLPCNHIKLVDAEelN 498
Cdd:cd05906 295 VNAGEAVVAKTIRRLLRLLEPYGLPPdairpAFGMTETCSGVIYSRSfptYDHSQALefvsLGRPIPGVSMRIVDDE--G 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 499 YWTSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGkWLPEGTLKIIDRKK 557
Cdd:cd05906 373 QLLPEGEvGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| 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 1937369599 268 DDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF---LKVTESqwaptcaDVHFSYLPLAHM--FERMVQSVVYchGGRVG 342
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSalnLGLTED-------DNWLCALPLFHIsgLSILMRSVIY--GMTVY 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 343 FFQG-DIRLLSDDMKALRPTIFPVVPRLLNRMYdKIFHQADTSlkrwllefaakrkqaevrsgiirnnsiwdelffnkiq 421
Cdd:cd05912 148 LVDKfDAEQVLHLINSGKVTIISVVPTMLQRLL-EILGEGYPN------------------------------------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 422 aslggHVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTE-CTAGCTFTtPGDWTS--GHVGAPLPCNHIKLVDAEELN 498
Cdd:cd05912 190 -----NLRCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTEtCSQIVTLS-PEDALNkiGSAGKPLFPVELKIEDDGQPP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 499 YwtskGEGEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYI 578
Cdd:cd05912 263 Y----EVGEILLKGPNVTKGYLNRPDATEESFE-NGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLL 336
|
330 340 350
....*....|....*....|....*....|....*
gi 1937369599 579 RSEPVAQIYVhgdslkaflVGIvvPDPEvmpcWAQ 613
Cdd:cd05912 337 SHPAIKEAGV---------VGI--PDDK----WGQ 356
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
119-615 |
1.35e-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: 125.10 E-value: 1.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 119 QWlSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADiCTV 198
Cdd:cd05934 3 RW-TYAELLRESARIAAALAALGIRPGDR--VALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSG-AQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 199 IVdkphkailllehverketpglklvilmepfddalrergkkcgVDIKSMQaiedsgqenhrvpvpprpddlsivcFTSG 278
Cdd:cd05934 79 VV------------------------------------------VDPASIL-------------------------YTSG 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 279 TTGNPKGAMLTHGNVVadFSGflKVTESQWAPTCADVHFSYLPLAHM---FERMVQSVVycHGGRV--------GFFQGD 347
Cdd:cd05934 92 TTGPPKGVVITHANLT--FAG--YYSARRFGLGEDDVYLTVLPLFHInaqAVSVLAALS--VGATLvllprfsaSRFWSD 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 348 IRllsdDMKALRPTIFPVVPRLLNRmydkifhQADtslkrwllefAAKRKQAEVRsgiirnnsiwdelffnkiqaslggh 427
Cdd:cd05934 166 VR----RYGATVTNYLGAMLSYLLA-------QPP----------SPDDRAHRLR------------------------- 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 428 vrmiVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEelNYWTSKGE-G 506
Cdd:cd05934 200 ----AAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDD--GQELPAGEpG 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 507 EICVK---GPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSEPV 583
Cdd:cd05934 274 ELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVERAILRHPAV 351
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1937369599 584 AQIYVHG-------DSLKAFLVgiVVP----DPEVMPCWAQKK 615
Cdd:cd05934 352 REAAVVAvpdevgeDEVKAVVV--LRPgetlDPEELFAFCEGQ 392
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
173-575 |
1.58e-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: 341246 [Multi-domain] Cd Length: 457 Bit Score: 125.25 E-value: 1.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 173 VVVPLYDTLGPGSIRYIINTADIctvivdkphkailllehverketpglKLVILMEPFDDALRERGKKCGVDIKSMQAIE 252
Cdd:cd05922 48 VFVPLNPTLKESVLRYLVADAGG--------------------------RIVLADAGAADRLRDALPASPDPGTVLDADG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 253 DSGQENHRVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTESQWAPTCADVHFSY-LPLAHMFER 328
Cdd:cd05922 102 IRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSiaeYLGITADDRALTVLPLSYDYgLSVLNTHLL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 329 MVQSVVYCHGGRVGffqgdiRLLSDDMKALRPTIFPVVPRLLnrmydkifhqadtslkrwllefaakrkqaevrsgiirn 408
Cdd:cd05922 182 RGATLVLTNDGVLD------DAFWEDLREHGATGLAGVPSTY-------------------------------------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 409 nSIWDELFFNKIQASlggHVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFTTPG--DWTSGHVGAPLP 485
Cdd:cd05922 218 -AMLTRLGFDPAKLP---SLRYLTQAGGRLPQETIARLRELLpGAQVYVMYGQTEATRRMTYLPPEriLEKPGSIGLAIP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 486 CNHIKLVDAEELNywTSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAq 564
Cdd:cd05922 294 GGEFEILDDDGTP--TPPGEpGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF- 370
|
410
....*....|.
gi 1937369599 565 GEYVAPEKIEN 575
Cdd:cd05922 371 GNRISPTEIEA 381
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-628 |
2.22e-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: 122.77 E-value: 2.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSGF-LKVTESQwaPTCADVhfsylPLAHMFErMVQSVVYC--HGGRV 341
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVnnGYFIGErLGLTEQD--RLCIPV-----PLFHCFG-SVLGVLACltHGATM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 342 GF----FqgDIRLLSDDMKALRPTIFPVVPRllnrMYDKIFHQADtslkrwLLEFAAKRkqaeVRSGIIrnnsiwdelff 417
Cdd:cd05917 73 VFpspsF--DPLAVLEAIEKEKCTALHGVPT----MFIAELEHPD------FDKFDLSS----LRTGIM----------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 418 nkiqaslgghvrmivtGAAPASPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGDWTS---GHVGAPLPCNHIKLVD 493
Cdd:cd05917 126 ----------------AGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDSIEkrvNTVGRIMPHTEAKIVD 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 494 AEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKI 573
Cdd:cd05917 190 PEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGENIYPREI 268
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937369599 574 ENIyirsepvaqIYVHGDSLKAFLVGivVPDP----EVMPCWAQKKG---IEGNYQELCKSK 628
Cdd:cd05917 269 EEF---------LHTHPKVSDVQVVG--VPDErygeEVCAWIRLKEGaelTEEDIKAYCKGK 319
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
121-606 |
2.84e-30 |
|
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: 124.56 E-value: 2.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELACY----TYsmvvVPLYDTLGPGSIRYIINTADIC 196
Cdd:cd05930 13 LTYAELDARANRLARYLRERG--VGPGDLVAVLLERSLEMVVAILAVLkagaAY----VPLDPSYPAERLAYILEDSGAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 197 TVIVDkphkailllehverketpglklvilmepfddalrergkkcgvdiksmqaiedsgqenhrvpvpprPDDLSIVCFT 276
Cdd:cd05930 87 LVLTD-----------------------------------------------------------------PDDLAYVIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 277 SGTTGNPKGAMLTHGNVV---ADFSGFLKVTES----QWAPTCADVHFS--YLPLAHmfermvqsvvychGGRV----GF 343
Cdd:cd05930 102 SGSTGKPKGVMVEHRGLVnllLWMQEAYPLTPGdrvlQFTSFSFDVSVWeiFGALLA-------------GATLvvlpEE 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 344 FQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTSLkrwllefaakrkqaevrsgiirnnsiwdelffnkiqas 423
Cdd:cd05930 169 VRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAALPSL-------------------------------------- 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 424 lgghvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFT--TPGDWTSGHV--GAPLPCNHIKLVDaEELN 498
Cdd:cd05930 211 -----RLVLVGGEALPPDLVrRWRELLPGARLVNLYGPTEATVDATYYrvPPDDEEDGRVpiGRPIPNTRVYVLD-ENLR 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 499 YWTSKGEGEICVKGPNVFKGYLKDEDRTKEA-----LDSDGWLH-TGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEK 572
Cdd:cd05930 285 PVPPGVPGELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIELGE 363
|
490 500 510
....*....|....*....|....*....|....*..
gi 1937369599 573 IENIYIRSEPVAQIYV---HGDSLKAFLVGIVVPDPE 606
Cdd:cd05930 364 IEAALLAHPGVREAAVvarEDGDGEKRLVAYVVPDEG 400
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
262-607 |
3.52e-30 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 125.52 E-value: 3.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 262 PVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADF--------SGFLKVTE-SQWAPTCAdvhfsyLPLAHMFERMVQS 332
Cdd:PRK07059 198 PVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqmeawlqPAFEKKPRpDQLNFVCA------LPLYHIFALTVCG 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 333 VVYCHGGRVGFF---QGDIRLLSDDMKALRPTIFPVVPRLLNRMYdkifhqadtslkrwllefaakrkqaevrsgiirNN 409
Cdd:PRK07059 272 LLGMRTGGRNILipnPRDIPGFIKELKKYQVHIFPAVNTLYNALL---------------------------------NN 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 410 SIWDELFFNKIQASLGGhvrmivtGAAPASPTVLGFLRAAlGCQVYEGYG--QTECTAGCTFTTPGDWTsGHVGAPLPCN 487
Cdd:PRK07059 319 PDFDKLDFSKLIVANGG-------GMAVQRPVAERWLEMT-GCPITEGYGlsETSPVATCNPVDATEFS-GTIGLPLPST 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 488 HIKLVDAE--ELnywtSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQ 564
Cdd:PRK07059 390 EVSIRDDDgnDL----PLGEpGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMI-LVS 464
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1937369599 565 GEYVAPEKIENIyIRSEP----VAQIYVH----GDSLKAFlvgIVVPDPEV 607
Cdd:PRK07059 465 GFNVYPNEIEEV-VASHPgvleVAAVGVPdehsGEAVKLF---VVKKDPAL 511
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
89-694 |
3.72e-30 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 127.66 E-value: 3.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 89 ARTMYQVFRRGLSISGNGPCLGFRKPEQPYQWLSYQEVAKRAEFLGSGLLQHDCKVGteQFIGVFAQNRPEWIIAELACY 168
Cdd:PTZ00297 426 VRSLGEMWERSVTRHSTFRCLGQTSESGESEWLTYGTVDARARELGSGLLALGVRPG--DVIGVDCEASRNIVILEVACA 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 169 TYSMVVVPLydtLGPGS-IRYIINTADICTVIVDKPHKAILLLEHVERKETpglklVILMEPFDDALRER-GKKCGVDIK 246
Cdd:PTZ00297 504 LYGFTTLPL---VGKGStMRTLIDEHKIKVVFADRNSVAAILTCRSRKLET-----VVYTHSFYDEDDHAvARDLNITLI 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 247 SMQAIEDSGQENhrvPVPPRP--DDLSIVCFTSGTTGNPKGAML-----THGNVVADFSGFLKvteSQWAPTCAD----V 315
Cdd:PTZ00297 576 PYEFVEQKGRLC---PVPLKEhvTTDTVFTYVVDNTTSASGDGLavvrvTHADVLRDISTLVM---TGVLPSSFKkhlmV 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 316 HFSylPLAHMFERMVQSVVYCHGGRVGffQGDIRLLSDDMKALRPTIFPVVPRLlnrmydkiFHQADTSLKR-------- 387
Cdd:PTZ00297 650 HFT--PFAMLFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSL--------FSTSRLQLSRanerysav 717
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 388 --WLLEfaakrKQAEVRSGII----RNNSIWDELFFNKIQASLGGHVRMIVTGAAPASPTV-----LGFLRAALGCQVYe 456
Cdd:PTZ00297 718 ysWLFE-----RAFQLRSRLInihrRDSSLLRFIFFRATQELLGGCVEKIVLCVSEESTSFsllehISVCYVPCLREVF- 791
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 457 gygQTECTAGCTFTtpgdwtsghvGAPLPCNHIKLVDAEELNYWTSKGEGEICVKGpnvfkgylkDEDRTKEAldsdgwl 536
Cdd:PTZ00297 792 ---FLPSEGVFCVD----------GTPAPSLQVDLEPFDEPSDGAGIGQLVLAKKG---------EPRRTLPI------- 842
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 537 htgdIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAfLVGIVVPDPEVMPC-WAQKK 615
Cdd:PTZ00297 843 ----AAQWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEFeWRQSH 917
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 616 GIEG--------NYQELckSKELKKAILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKK 687
Cdd:PTZ00297 918 CMGEgggparqlGWTEL--VAYASSLLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSS 995
|
....*..
gi 1937369599 688 QIEELYS 694
Cdd:PTZ00297 996 VIERFYS 1002
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
121-606 |
3.79e-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: 123.74 E-value: 3.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGSGLlqHDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:cd05935 2 LTYLELLEVVKKLASFL--SNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 201 dkphkaillleHVERketpglklvilmepfddalrergkkcgvdiksmqaiedsgqenhrvpvpprpDDLSIVCFTSGTT 280
Cdd:cd05935 80 -----------GSEL----------------------------------------------------DDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 281 GNPKGAMLTHGNVVADFSGflkvtESQWAP-TCADVHFSYLPLAHM--FERMVQSVVYCHGGRVGFFQGDIRLLSDDMKA 357
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQ-----SAVWTGlTPSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMARWDRETALELIEK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 358 LRPTIFPVVPRLLNrmydkifhqadtslkrwllefaakrkqaevrsgiirnnsiwDELFFNKIQASLGGHVRMIVTGAAP 437
Cdd:cd05935 172 YKVTFWTNIPTMLV-----------------------------------------DLLATPEFKTRDLSSLKVLTGGGAP 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 438 ASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYWTSKGEGEICVKGPNVFK 517
Cdd:cd05935 211 MPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFK 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 518 GYLKDEDRTKEALDSDG---WLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQIYV------ 588
Cdd:cd05935 291 GYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVisvpde 369
|
490
....*....|....*....
gi 1937369599 589 -HGDSLKAFlvgiVVPDPE 606
Cdd:cd05935 370 rVGEEVKAF----IVLRPE 384
|
|
| 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 1937369599 269 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSgflkvtesQWApTCADVHFS--YL---PLAHMFErmvqsvvYCHGGRVGF 343
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAA--------AWA-DCADLTEDdrYLiinPFFHTFG-------YKAGIVACL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 344 FQG---------DIRLLSDDMKALRPTIFPVVPRLlnrmYDKIFHQADtslkrwllefaakRKQAEVRSgiirnnsiwde 414
Cdd:cd17638 65 LTGatvvpvavfDVDAILEAIERERITVLPGPPTL----FQSLLDHPG-------------RKKFDLSS----------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 415 lffnkiqaslgghVRMIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGcTFTTPGD---WTSGHVGAPLPCNHIK 490
Cdd:cd17638 117 -------------LRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVA-TMCRPGDdaeTVATTCGRACPGFEVR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 491 LVDAeelnywtskgeGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAP 570
Cdd:cd17638 183 IADD-----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYP 250
|
330 340 350
....*....|....*....|....*....|....*.
gi 1937369599 571 EKIENIYIRSEPVAQIYV-------HGDSLKAFLVG 599
Cdd:cd17638 251 AEVEGALAEHPGVAQVAVigvpderMGEVGKAFVVA 286
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
89-557 |
6.20e-30 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 125.45 E-value: 6.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 89 ARTMYQVFRRGLSISGNGPCLGF-------RKPEQpyqwLSYqevakrAEFLG-----SGLLqHDCKVGTEQFIGVFAQN 156
Cdd:PRK07529 24 PASTYELLSRAAARHPDAPALSFlldadplDRPET----WTY------AELLAdvtrtANLL-HSLGVGPGDVVAFLLPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 157 RPEWIIAELACYTYSmVVVPLYDTLGPGSIRYIINTADICTVIVDKP-------HKAILLLEHVerketPGLKLVI---- 225
Cdd:PRK07529 93 LPETHFALWGGEAAG-IANPINPLLEPEQIAELLRAAGAKVLVTLGPfpgtdiwQKVAEVLAAL-----PELRTVVevdl 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 226 ---LMEPFDDALRERGKKCGVDIKSMQAIEDSGQENHRV-PVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsGFL 301
Cdd:PRK07529 167 aryLPGPKRLAVPLIRRKAHARILDFDAELARQPGDRLFsGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVAN--AWL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 302 KVTESQWAPTcaDVHFSYLPLAHMFERMVQSVVYCHGGR---VGFFQG--DIRLLSDDMK---ALRPTIFPVVPRLLNRM 373
Cdd:PRK07529 245 GALLLGLGPG--DTVFCGLPLFHVNALLVTGLAPLARGAhvvLATPQGyrGPGVIANFWKiveRYRINFLSGVPTVYAAL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 374 YDKIFHQADTSLkrwlLEFAAkrkqaevrsgiirnnsiwdelffnkiqaslgghvrmivTGAAPASPTVLGFLRAALGCQ 453
Cdd:PRK07529 323 LQVPVDGHDISS----LRYAL--------------------------------------CGAAPLPVEVFRRFEAATGVR 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 454 VYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLVDAEEL-NYW--TSKGE-GEICVKGPNVFKGYLkDEDRTKE 528
Cdd:PRK07529 361 IVEGYGLTEATCVSSVNPPdGERRIGSVGLRLPYQRVRVVILDDAgRYLrdCAVDEvGVLCIAGPNVFSGYL-EAAHNKG 439
|
490 500
....*....|....*....|....*....
gi 1937369599 529 ALDSDGWLHTGDIGKWLPEGTLKIIDRKK 557
Cdd:PRK07529 440 LWLEDGWLNTGDLGRIDADGYFWLTGRAK 468
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
122-588 |
6.64e-30 |
|
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: 122.76 E-value: 6.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 122 SYQEVAKRAEFLGSGLLQHdCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGS-IRYIINTADICTVIV 200
Cdd:TIGR01733 1 TYRELDERANRLARHLRAA-GGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPL-DPAYPAErLAFILEDAGARLLLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 201 DKPHkailllehveRKETPGLKLVILMEPFDDALrergkkcgvdiksmqAIEDSGQENHRvPVPPRPDDLSIVCFTSGTT 280
Cdd:TIGR01733 79 DSAL----------ASRLAGLVLPVILLDPLELA---------------ALDDAPAPPPP-DAPSGPDDLAYVIYTSGST 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 281 GNPKGAMLTHGNVVAdfsgFLKVTESQWAPTCADVHFSYLPLAH------MFermvqsVVYCHGGRVGFFQGDIRLlsDD 354
Cdd:TIGR01733 133 GRPKGVVVTHRSLVN----LLAWLARRYGLDPDDRVLQFASLSFdasveeIF------GALLAGATLVVPPEDEER--DD 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 355 MKALRptifpvvpRLLNRMYDKIFHQADTSLKRWLLEfaakrkqaevrsgiirnnsiwdelffnkiQASLGGHVRMIVTG 434
Cdd:TIGR01733 201 AALLA--------ALIAEHPVTVLNLTPSLLALLAAA-----------------------------LPPALASLRLVILG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 435 AAPASPTVLGFLRAALG-CQVYEGYGQTECTAGCT-FTTPGDWTSGHV----GAPLPCNHIKLVDaEELNYWTSKGEGEI 508
Cdd:TIGR01733 244 GEALTPALVDRWRARGPgARLINLYGPTETTVWSTaTLVDPDDAPRESpvpiGRPLANTRLYVLD-DDLRPVPVGVVGEL 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 509 CVKGPNVFKGYLKDEDRTKEA-LDSDGWL-------HTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRS 580
Cdd:TIGR01733 323 YIGGPGVARGYLNRPELTAERfVPDPFAGgdgarlyRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAALLRH 401
|
....*...
gi 1937369599 581 EPVAQIYV 588
Cdd:TIGR01733 402 PGVREAVV 409
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
119-550 |
1.11e-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: 126.12 E-value: 1.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 119 QWLSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELA------CYtysmvvVPLYDTLGPGSIRYIINT 192
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALG--VGPGDLVGVCLERSLEMVVALLAvlkagaAY------VPLDPAYPAERLAYMLED 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 193 ADICTVIVDkphkailllehverketpglklvilmepfdDALRERGKKCGVDIKSMQAIEDSGQENHRVPVPPRPDDLSI 272
Cdd:COG1020 572 AGARLVLTQ------------------------------SALAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLAY 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 273 VCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTES----QWAPTCADVHFS--YLPLahmfermvqsvvyCHGGRVGF 343
Cdd:COG1020 622 VIYTSGSTGRPKGVMVEHRALVnllAWMQRRYGLGPGdrvlQFASLSFDASVWeiFGAL-------------LSGATLVL 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 344 FQGDIRL----LSDDMKALRPTIFPVVPRLLNRmydkifhqadtslkrwLLEFAAKRkqaevrsgiirnnsiwdelffnk 419
Cdd:COG1020 689 APPEARRdpaaLAELLARHRVTVLNLTPSLLRA----------------LLDAAPEA----------------------- 729
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 420 iqaslGGHVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTF--TTPGDWTSGHV--GAPLPCNHIKLVDA 494
Cdd:COG1020 730 -----LPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTVDSTYyeVTPPDADGGSVpiGRPIANTRVYVLDA 804
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 495 EelnywtskGE-------GEICVKGPNVFKGYLKDEDRTKEA-----LDSDG--WLHTGDIGKWLPEGTL 550
Cdd:COG1020 805 H--------LQpvpvgvpGELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNL 866
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
261-578 |
1.89e-29 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 123.41 E-value: 1.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 261 VPVPP-RPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWA-PTCADVHFSYLPLAHMFermvqsvvychg 338
Cdd:PLN02574 190 VPKPViKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEyPGSDNVYLAALPMFHIY------------ 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 339 GRVGFFQGDIRL-----------LSDDMKAL---RPTIFPVVPRLLnrmydkifhqadTSLKRwllefAAKRKQAEVRsg 404
Cdd:PLN02574 258 GLSLFVVGLLSLgstivvmrrfdASDMVKVIdrfKVTHFPVVPPIL------------MALTK-----KAKGVCGEVL-- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 405 iirnnsiwdelffnkiqaslgGHVRMIVTGAAPAS-PTVLGFLRAALGCQVYEGYGQTECTAGCT--FTTPGDWTSGHVG 481
Cdd:PLN02574 319 ---------------------KSLKQVSCGAAPLSgKFIQDFVQTLPHVDFIQGYGMTESTAVGTrgFNTEKLSKYSSVG 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 482 APLPCNHIKLVDAEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFK 561
Cdd:PLN02574 378 LLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIK 457
|
330
....*....|....*..
gi 1937369599 562 LaQGEYVAPEKIENIYI 578
Cdd:PLN02574 458 Y-KGFQIAPADLEAVLI 473
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
112-606 |
4.49e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 122.38 E-value: 4.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 112 RKPEQPYQW-----LSYQEVAKRAEFLgSGLLQHDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSI 186
Cdd:PRK08314 22 RYPDKTAIVfygraISYRELLEEAERL-AGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 187 RYIINTADICTVIVD-------KPHKAILLLEHV-------ERKETPGLKLvilmePfdDALRERGKKCGVDIKSMQAIE 252
Cdd:PRK08314 101 AHYVTDSGARVAIVGselapkvAPAVGNLRLRHVivaqysdYLPAEPEIAV-----P--AWLRAEPPLQALAPGGVVAWK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 253 DSGQENHRV-PVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkvteSQWAP-TCADVHFSYLPLAHM--FER 328
Cdd:PRK08314 174 EALAAGLAPpPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGS-----VLWSNsTPESVVLAVLPLFHVtgMVH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 329 MVQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLL-NRMYDKIFHQADTSlkrwllefaakrkqaevrsgiir 407
Cdd:PRK08314 249 SMNAPIYAGATVVLMPRWDREAAARLIERYRVTHWTNIPTMVvDFLASPGLAERDLS----------------------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 408 nnsiwdelffnkiqaSLgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWT-SGHVGAPLPC 486
Cdd:PRK08314 306 ---------------SL----RYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTE-TMAQTHSNPPDRPkLQCLGIPTFG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 487 NHIKLVDAEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEA---LDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlA 563
Cdd:PRK08314 366 VDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMIN-A 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1937369599 564 QGEYVAPEKIENIYIRSEPVAQIYV-------HGDSLKAFlvgiVVPDPE 606
Cdd:PRK08314 445 SGFKVWPAEVENLLYKHPAIQEACViatpdprRGETVKAV----VVLRPE 490
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
121-588 |
3.49e-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: 117.87 E-value: 3.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGSGLLQhdCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADIctviv 200
Cdd:cd05903 2 LTYSELDTRADRLAAGLAA--LGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 201 dkphkailllehverketpglKLVILMEPFddalrergkkcgvdiksmqaiedsGQENHRvpvpPRPDDLSIVCFTSGTT 280
Cdd:cd05903 75 ---------------------KVFVVPERF------------------------RQFDPA----AMPDAVALLLFTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 281 GNPKGAMLTHGNVVADFSGFLKvtesQWAPTCADVHFSYLPLAHMfermvqsVVYCHGGRVGFFQGDIRLLSDDMKALRp 360
Cdd:cd05903 106 GEPKGVMHSHNTLSASIRQYAE----RLGLGPGDVFLVASPMAHQ-------TGFVYGFTLPLLLGAPVVLQDIWDPDK- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 361 tifpvVPRLLNRMYDKIFHQADTSLKRWL--LEFAAKRKQaevrsgiirnnsiwdelffnkiqaslggHVRMIVTGAAPA 438
Cdd:cd05903 174 -----ALALMREHGVTFMMGATPFLTDLLnaVEEAGEPLS----------------------------RLRTFVCGGATV 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 439 SPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGD----WTSGhvGAPLPCNHIKLVDAEELNYwTSKGEGEICVKGPN 514
Cdd:cd05903 221 PRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPedrrLYTD--GRPLPGVEIKVVDDTGATL-APGVEGELLSRGPS 297
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937369599 515 VFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYV 588
Cdd:cd05903 298 VFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAV 369
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
121-609 |
6.94e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 118.16 E-value: 6.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAE-----FLGSGLLQHDCkvgteqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADI 195
Cdd:PRK06188 38 LTYGQLADRISryiqaFEALGLGTGDA-------VALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 196 CTVIVDK---PHKAILLLEHVerketPGLKLVILMEPFDDalrergkkcGVDIKSMQAIEDsgqenHRVPVPP-RPDDLS 271
Cdd:PRK06188 111 STLIVDPapfVERALALLARV-----PSLKHVLTLGPVPD---------GVDLLAAAAKFG-----PAPLVAAaLPPDIA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 272 IVCFTSGTTGNPKGAMLTHGNVVADFSGFLkvTESQWAPtcadvHFSYL---PLAHMFERMVQSVVYcHGGRVGFFQG-D 347
Cdd:PRK06188 172 GLAYTGGTTGKPKGVMGTHRSIATMAQIQL--AEWEWPA-----DPRFLmctPLSHAGGAFFLPTLL-RGGTVIVLAKfD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 348 IRLLSDDMKALRPTIFPVVPRLLNRmydkifhqadtslkrwLLEFAAKRKqaevrsgiiRNNSiwdelffnkiqaSLggh 427
Cdd:PRK06188 244 PAEVLRAIEEQRITATFLVPTMIYA----------------LLDHPDLRT---------RDLS------------SL--- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 428 vRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHV------GAPLPCNHIKLVDAEELNywT 501
Cdd:PRK06188 284 -ETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLRVALLDEDGRE--V 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 502 SKGE-GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRS 580
Cdd:PRK06188 361 AQGEvGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMI-VTGGFNVFPREVEDVLAEH 438
|
490 500 510
....*....|....*....|....*....|....*.
gi 1937369599 581 EPVAQIYV-------HGDSLKAflvgIVVPDPEVMP 609
Cdd:PRK06188 439 PAVAQVAVigvpdekWGEAVTA----VVVLRPGAAV 470
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
123-590 |
7.10e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 117.76 E-value: 7.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 123 YQEVAKRAEFLGSGLLQHDCKVGteqfigVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIVDk 202
Cdd:PRK03640 34 HEAVVSVAGKLAALGVKKGDRVA------LLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITD- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 203 phkailllehverketpglklvilmEPFDDALRErgkKCGVDIKSMQAiedsGQENHRVPVPPRP-DDLSIVCFTSGTTG 281
Cdd:PRK03640 107 -------------------------DDFEAKLIP---GISVKFAELMN----GPKEEAEIQEEFDlDEVATIMYTSGTTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 282 NPKGAMLTHGNVVADFSGF---LKVTESQ-WapTCAdvhfsyLPLAHM--FERMVQSVVYchGGRVGFFQG-DIRLLSDD 354
Cdd:PRK03640 155 KPKGVIQTYGNHWWSAVGSalnLGLTEDDcW--LAA------VPIFHIsgLSILMRSVIY--GMRVVLVEKfDAEKINKL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 355 MKALRPTIFPVVPRLLNRMYDKIFhqadtslkrwllefaakrkqaevrsgiirnnsiwdelffnkiQASLGGHVRMIVTG 434
Cdd:PRK03640 225 LQTGGVTIISVVSTMLQRLLERLG------------------------------------------EGTYPSSFRCMLLG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 435 AAPASPTVLGFLRAAlGCQVYEGYGQTEcTAGCTFTTPGDWTS---GHVGAPL-PCNhIKLVDaeELNYWTSKGEGEICV 510
Cdd:PRK03640 263 GGPAPKPLLEQCKEK-GIPVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLfPCE-LKIEK--DGVVVPPFEEGEIVV 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 511 KGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYVHG 590
Cdd:PRK03640 338 KGPNVTKGYLNREDATRETFQ-DGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPGVAEAGVVG 415
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
269-588 |
1.14e-27 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 117.77 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 269 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTCADVhfSYLPLAHMF--ERMVQSVVYCHGGRVGFFQG 346
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMIGQVVTL--GLIPFFHIYgiTGICCATLRNKGKVVVMSRF 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 347 DIRLLSDDMKALRPTIFPVVPRLLNRMYdkifhqadtslkrwllefaakrkqaevrsgiirNNSIWDELFFNKIQaslgg 426
Cdd:PLN02330 263 ELRTFLNALITQEVSFAPIVPPIILNLV---------------------------------KNPIVEEFDLSKLK----- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 427 hVRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTagCTFTTPGDWTSGH-------VGAPLPCNHIKLVDAEELN 498
Cdd:PLN02330 305 -LQAIMTAAAPLAPELLtAFEAKFPGVQVQEAYGLTEHS--CITLTHGDPEKGHgiakknsVGFILPNLEVKFIDPDTGR 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 499 YWTSKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYI 578
Cdd:PLN02330 382 SLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAILL 460
|
330
....*....|
gi 1937369599 579 RSEPVAQIYV 588
Cdd:PLN02330 461 THPSVEDAAV 470
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
241-604 |
1.38e-27 |
|
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: 116.25 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 241 CGVDIKS----MQAIEDSGQENHRVPvPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSGF-LKVTESQ------ 307
Cdd:cd17653 75 VPLDAKLpsarIQAILRTSGATLLLT-TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLnyVSQPPArLDVGPGSrvaqvl 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 308 ----WAptCADVHFSYLplahmfermvqsvvyCHGGRVgFFQGDIRLLSDDMKALrpTIFPVVPRLLNrMYDkifhqaDT 383
Cdd:cd17653 154 siafDA--CIGEIFSTL---------------CNGGTL-VLADPSDPFAHVARTV--DALMSTPSILS-TLS------PQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 384 SLKRwllefaakrkqaevrsgiirnnsiwdelffnkiqaslgghVRMIVTGAAPASPTVLGflRAALGCQVYEGYGQTEC 463
Cdd:cd17653 207 DFPN----------------------------------------LKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTEC 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 464 TAGCTFT--TPGDWTsgHVGAPLPCNHIKLVDAEELNywTSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLH--- 537
Cdd:cd17653 245 TISSTMTelLPGQPV--TIGKPIPNSTCYILDADLQP--VPEGVvGEICISGVQVARGYLGNPALTASKFVPDPFWPgsr 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937369599 538 ---TGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQ---IYVHGDSLKAFlvgiVVPD 604
Cdd:cd17653 321 myrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEIEEVVLQSQPEVTqaaAIVVNGRLVAF----VTPE 388
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
119-606 |
1.97e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 116.50 E-value: 1.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 119 QWLSYQEVAKRAEFLgSGLLQHDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTV 198
Cdd:PRK06839 26 EEMTYKQLHEYVSKV-AAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 199 IVDKPHKAILLLehverketpgLKLVILMEPFddalrergkkcgVDIKSMQAIEDSGQENHrvpVPPRPDDLSIVCFTSG 278
Cdd:PRK06839 105 FVEKTFQNMALS----------MQKVSYVQRV------------ISITSLKEIEDRKIDNF---VEKNESASFIICYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 279 TTGNPKGAMLTHGNVvadfsgFLKVTESQWAP--TCADVHFSYLPLAHMfermvqsvvychgGRVGFFqgdirllsddmk 356
Cdd:PRK06839 160 TTGKPKGAVLTQENM------FWNALNNTFAIdlTMHDRSIVLLPLFHI-------------GGIGLF------------ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 357 ALrPTIFP----VVPRLLNRmyDKIFHQADTslKRWLLEFAAKRKQAEVRSGIIRNNSIWDelffnkiqaslggHVRMIV 432
Cdd:PRK06839 209 AF-PTLFAggviIVPRKFEP--TKALSMIEK--HKVTVVMGVPTIHQALINCSKFETTNLQ-------------SVRWFY 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 433 TGAAPAS-PTVLGFLRAalGCQVYEGYGQTEcTAGCTFTTPGD---WTSGHVGAPLPCNHIKLVDaEELNYWTSKGEGEI 508
Cdd:PRK06839 271 NGGAPCPeELMREFIDR--GFLFGQGFGMTE-TSPTVFMLSEEdarRKVGSIGKPVLFCDYELID-ENKNKVEVGEVGEL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 509 CVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIyirsepvaqIYV 588
Cdd:PRK06839 347 LIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQV---------INK 415
|
490
....*....|....*...
gi 1937369599 589 HGDSLKAFLVGivVPDPE 606
Cdd:PRK06839 416 LSDVYEVAVVG--RQHVK 431
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
122-576 |
3.59e-27 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 116.39 E-value: 3.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 122 SYQEVAKRAEFLGSGLLQHDCKVGTeqfigVFAQNRPEW---IIAELACYTYSMVVVPLYDTLGPGSIRYIIN----TAD 194
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGD-----RVAFQLPGWcefTIIYLACLKVGAVSVPLLPSWREAELVWVLNkcqaKMF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 195 ICTVIVDK--PHKAILLLehveRKETPGLKLVILMEPFDDALRergkkcgvDIKSMQAIEDSGQENHrvPVPPRPDDLSI 272
Cdd:PRK06087 126 FAPTLFKQtrPVDLILPL----QNQLPQLQQIVGVDKLAPATS--------SLSLSQIIADYEPLTT--AITTHGDELAA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 273 VCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAptcaDVHFSYLPLAHmfermvqSVVYCHGGRVGFFQGDIRLLS 352
Cdd:PRK06087 192 VLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQ----DVFMMPAPLGH-------ATGFLHGVTAPFLIGARSVLL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 353 DDMKALRPTifpvvpRLLNRmydkifhQADTslkrWLL---EFaakrkqaevrsgiirnnsIWDELffNKIQASlGGHV- 428
Cdd:PRK06087 261 DIFTPDACL------ALLEQ-------QRCT----CMLgatPF------------------IYDLL--NLLEKQ-PADLs 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 429 --RMIVTGAAPASPTVLgflRAAL--GCQVYEGYGQTECTAGcTFTTPGD---WTSGHVGAPLPCNHIKLVDaEELNYWT 501
Cdd:PRK06087 303 alRFFLCGGTTIPKKVA---RECQqrGIKLLSVYGSTESSPH-AVVNLDDplsRFMHTDGYAAAGVEIKVVD-EARKTLP 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937369599 502 SKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENI 576
Cdd:PRK06087 378 PGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDI 451
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
112-605 |
4.47e-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: 4.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 112 RKPEQPYQWLSYQEVAKRAEFLGSGLlqHDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIIN 191
Cdd:cd12119 17 RTHEGEVHRYTYAEVAERARRLANAL--RRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 192 TADICTVIVDKPHKAIL-----LLEHVERketpglklVILMEPFDDALRERGKKCG-----VDIKSMQAIEDSGQENhrv 261
Cdd:cd12119 95 HAEDRVVFVDRDFLPLLeaiapRLPTVEH--------VVVMTDDAAMPEPAGVGVLayeelLAAESPEYDWPDFDEN--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 262 pvpprpdDLSIVCFTSGTTGNPKGAMLTHGNVV-----ADFSGFLKVTESqwaptcaDVhfsYLPLAHMFERMVQSVVYc 336
Cdd:cd12119 164 -------TAAAICYTSGTTGNPKGVVYSHRSLVlhamaALLTDGLGLSES-------DV---VLPVVPMFHVNAWGLPY- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 337 hggrVGFFQG----------DIRLLSDDMKALRPTIFPVVPRLlnrmydkifhqadtslkrWLLefaakrkqaeVRSGII 406
Cdd:cd12119 226 ----AAAMVGaklvlpgpylDPASLAELIEREGVTFAAGVPTV------------------WQG----------LLDHLE 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 407 RNNSiwdELFfnkiqaslggHVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPgdwTSGHV------ 480
Cdd:cd12119 274 ANGR---DLS----------SLRRVVIGGSAVPRSLIEAFEE-RGVRVIHAWGMTETSPLGTVARP---PSEHSnlsede 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 481 --------GAPLPCNHIKLVDAE--ELNyWTSKGEGEICVKGPNVFKGYLKDeDRTKEALDSDGWLHTGDIGKWLPEGTL 550
Cdd:cd12119 337 qlalrakqGRPVPGVELRIVDDDgrELP-WDGKAVGELQVRGPWVTKSYYKN-DEESEALTEDGWLRTGDVATIDEDGYL 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1937369599 551 KIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQIYVhgdslkaflvgIVVPDP 605
Cdd:cd12119 415 TITDRSKDVIKSG-GEWISSVELENAIMAHPAVAEAAV-----------IGVPHP 457
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
262-598 |
6.67e-27 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 115.69 E-value: 6.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 262 PVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTeSQWAP-------TCADVHFSYLPLAHMFErmvqsvv 334
Cdd:PRK12492 201 PVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACL-SQLGPdgqplmkEGQEVMIAPLPLYHIYA------- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 335 ychggrvgfFQGDIRLLsddMKALRPTIFPVVPRLLNRMYDKifhqadtsLKRWLLefaakrkqaevrSGIIRNNSIWDE 414
Cdd:PRK12492 273 ---------FTANCMCM---MVSGNHNVLITNPRDIPGFIKE--------LGKWRF------------SALLGLNTLFVA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 415 LF----FNKIQASlggHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHI 489
Cdd:PRK12492 321 LMdhpgFKDLDFS---ALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELARlGTVGIPVPGTAL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 490 KLVDAE--ELNYwtskGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGE 566
Cdd:PRK12492 398 KVIDDDgnELPL----GErGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLI-IVSGF 472
|
330 340 350
....*....|....*....|....*....|....*....
gi 1937369599 567 YVAPEKIENIYIRSEPVAQIYV-------HGDSLKAFLV 598
Cdd:PRK12492 473 NVYPNEIEDVVMAHPKVANCAAigvpderSGEAVKLFVV 511
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
254-605 |
8.97e-27 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 114.59 E-value: 8.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 254 SGQENHRVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgfLKVTESQWAPTCADVHFSYLPLAHMFERMVQS- 332
Cdd:PRK07514 142 AAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSN----ALTLVDYWRFTPDDVLIHALPIFHTHGLFVATn 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 333 VVYCHGGRVGFFQG-DIRLLSDDMKalRPTIFPVVPRLLNRMYdkifhqADTSLKRwllEFAAkrkqaevrsgiirnnsi 411
Cdd:PRK07514 218 VALLAGASMIFLPKfDPDAVLALMP--RATVMMGVPTFYTRLL------QEPRLTR---EAAA----------------- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 412 wdelffnkiqaslggHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTfTTP--GDWTSGHVGAPLPCNHI 489
Cdd:PRK07514 270 ---------------HMRLFISGSAPLLAETHREFQERTGHAILERYGMTE-TNMNT-SNPydGERRAGTVGFPLPGVSL 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 490 KLVDAE---ELnywtSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIfkLAQG 565
Cdd:PRK07514 333 RVTDPEtgaEL----PPGEiGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDL--IISG 406
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1937369599 566 EY-VAPEKIENiYIRSEP-VAQIYVHGDSLKAF---LVGIVVPDP 605
Cdd:PRK07514 407 GYnVYPKEVEG-EIDELPgVVESAVIGVPHPDFgegVTAVVVPKP 450
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
119-604 |
1.67e-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: 113.54 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 119 QWLSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTAdictv 198
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARG--VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDA----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 199 ivdkphKAILLLEhverketpglklvilmepfDDALRERGKKCGVDIksMQAIEDSGQENHRVPVPPRPDDLSIVCFTSG 278
Cdd:cd12116 84 ------EPALVLT-------------------DDALPDRLPAGLPVL--LLALAAAAAAPAAPRTPVSPDDLAYVIYTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 279 TTGNPKGAMLTHGNVVADFSGF------------LKVTesqwaPTCADVhfS----YLPLahmfermvqsvvyCHGGRVG 342
Cdd:cd12116 137 STGRPKGVVVSHRNLVNFLHSMrerlglgpgdrlLAVT-----TYAFDI--SllelLLPL-------------LAGARVV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 343 FFQGDI----RLLSDDMKALRPTIFpvvprllnrmydkifhQADTSLKRWLLEfaakrkqaevrSGiirnnsiWDELffn 418
Cdd:cd12116 197 IAPRETqrdpEALARLIEAHSITVM----------------QATPATWRMLLD-----------AG-------WQGR--- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 419 kiqaslgGHVRMIVTGAApaSPTVLGFLRAALGCQVYEGYGQTECT--AGCTFTTPGDwTSGHVGAPLPCNHIKLVDAee 496
Cdd:cd12116 240 -------AGLTALCGGEA--LPPDLAARLLSRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLDA-- 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 497 lnYWTS--KGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLH-------TGDIGKWLPEGTLKIIDRKKHIFKLaQGE 566
Cdd:cd12116 308 --ALRPvpPGVpGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQVKI-RGH 384
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1937369599 567 YVAPEKIENIYIRSEPVAQ--IYVHGDSLKAFLVGIVVPD 604
Cdd:cd12116 385 RIELGEIEAALAAHPGVAQaaVVVREDGGDRRLVAYVVLK 424
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
114-608 |
2.25e-26 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 114.14 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 114 PEQPYQWlSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVV---PLYDTlgpGSIRYII 190
Cdd:PRK08315 38 RDQGLRW-TYREFNEEVDALAKGLLALGIEKGDR--VGIWAPNVPEWVLTQFATAKIGAILVtinPAYRL---SELEYAL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 191 NTADICTVIVDKPHK-----AILL-----LEHVER-----KETPGLKLVIL--------MEPFDDaLRERGKkcGVDIKS 247
Cdd:PRK08315 112 NQSGCKALIAADGFKdsdyvAMLYelapeLATCEPgqlqsARLPELRRVIFlgdekhpgMLNFDE-LLALGR--AVDDAE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 248 MQAIEDSGQenhrvpvpprPDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsGFLkVTESQwAPTCAD-----VhfsylPL 322
Cdd:PRK08315 189 LAARQATLD----------PDDPINIQYTSGTTGFPKGATLTHRNILNN--GYF-IGEAM-KLTEEDrlcipV-----PL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 323 AHMFErMVQSVVYC--HGGRV-----GFfqgdirllsDDMKALR-------------PTIFPVVprlLNrmyDKIFHQAD 382
Cdd:PRK08315 250 YHCFG-MVLGNLACvtHGATMvypgeGF---------DPLATLAaveeerctalygvPTMFIAE---LD---HPDFARFD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 383 -TSLkrwllefaakrkqaevRSGIirnnsiwdelffnkiqaslgghvrMivtgAAPASPT-----VLGFLRAAlgcQVYE 456
Cdd:PRK08315 314 lSSL----------------RTGI------------------------M----AGSPCPIevmkrVIDKMHMS---EVTI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 457 GYGQTECTAGCTFTTPGD------WTsghVGAPLPCNHIKLVDAEelnywtsKGE-------GEICVKGPNVFKGYLKDE 523
Cdd:PRK08315 347 AYGMTETSPVSTQTRTDDplekrvTT---VGRALPHLEVKIVDPE-------TGEtvprgeqGELCTRGYSVMKGYWNDP 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 524 DRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIyirsepvaqIYVHGDSLKAFLVGivVP 603
Cdd:PRK08315 417 EKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEF---------LYTHPKIQDVQVVG--VP 484
|
....*....
gi 1937369599 604 DP----EVM 608
Cdd:PRK08315 485 DEkygeEVC 493
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
220-578 |
3.75e-26 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 113.15 E-value: 3.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 220 GLKLVILMEPFDDALRERGKKCGVDIKSMQAIED---------SGQENHRVPVPPRPDDLSIVCFTSGTTGNPKGAMLTH 290
Cdd:PLN02246 122 GAKLIITQSCYVDKLKGLAEDDGVTVVTIDDPPEgclhfseltQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTH 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 291 GNVVADFSGFLKVTESQWAPTCADVHFSYLPLAHMFErmVQSVVYChGGRVG--------FfqgDIRLLSDDMKALRPTI 362
Cdd:PLN02246 202 KGLVTSVAQQVDGENPNLYFHSDDVILCVLPMFHIYS--LNSVLLC-GLRVGaailimpkF---EIGALLELIQRHKVTI 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 363 FPVVPRLLnrmydkifhqadtslkrwlLEFAakrKQAEVRSgiirnnsiwDELffnkiqASlgghVRMIVTGAAPASPTV 442
Cdd:PLN02246 276 APFVPPIV-------------------LAIA---KSPVVEK---------YDL------SS----IRMVLSGAAPLGKEL 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 443 LGFLRAALGCQVY-EGYGQTE-------CTAgctFT-TPGDWTSGHVGAPLPCNHIKLVDAE---ELNYWTSkgeGEICV 510
Cdd:PLN02246 315 EDAFRAKLPNAVLgQGYGMTEagpvlamCLA---FAkEPFPVKSGSCGTVVRNAELKIVDPEtgaSLPRNQP---GEICI 388
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937369599 511 KGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYI 578
Cdd:PLN02246 389 RGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAELEALLI 455
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
156-598 |
4.05e-26 |
|
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: 111.66 E-value: 4.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 156 NRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIVDKphkailllehverketpglklvilmepfddalr 235
Cdd:cd05972 34 RVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA--------------------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 236 ergkkcgvdiksmqaiedsgqenhrvpvpprpDDLSIVCFTSGTTGNPKGAMLTHG---NVVADFSGFLKVTESQWAPTC 312
Cdd:cd05972 81 --------------------------------EDPALIYFTSGTTGLPKGVLHTHSyplGHIPTAAYWLGLRPDDIHWNI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 313 ADVHFSYLPLAHMFERMVQ--SVVYCHGGRvgffqgdirllsddMKALRptifpvVPRLLNRMYDKIFHQADTSLKRWLL 390
Cdd:cd05972 129 ADPGWAKGAWSSFFGPWLLgaTVFVYEGPR--------------FDAER------ILELLERYGVTSFCGPPTAYRMLIK 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 391 EFAAKRKQaevrsgiirnnsiwdelffnkiqaslgGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFT 470
Cdd:cd05972 189 QDLSSYKF---------------------------SHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNF 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 471 TPGDWTSGHVGAPLPCNHIKLVDAE--ELNYWTskgEGEICVKGPNV--FKGYLKDEDRTKEALdSDGWLHTGDIGKWLP 546
Cdd:cd05972 242 PDMPVKPGSMGRPTPGYDVAIIDDDgrELPPGE---EGDIAIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDRAYRDE 317
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1937369599 547 EGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSEPVAQIYV-------HGDSLKAFLV 598
Cdd:cd05972 318 DGYFWFVGRADDIIK-SSGYRIGPFEVESALLEHPAVAEAAVvgspdpvRGEVVKAFVV 375
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
259-609 |
4.73e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 112.01 E-value: 4.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 259 HRVPVPPrPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkvtESQWAPTCADVHFSYLPLAHMfermvqsvvycHG 338
Cdd:PRK07787 120 HRYPEPD-PDAPALIVYTSGTTGPPKGVVLSRRAIAADLDAL----AEAWQWTADDVLVHGLPLFHV-----------HG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 339 GRVGFFqGDIRLLSDDMKALRPTIFPVVPRLLNR---------MYDKIfhQADTSLKRwllefaakrkqaevrsgiirnn 409
Cdd:PRK07787 184 LVLGVL-GPLRIGNRFVHTGRPTPEAYAQALSEGgtlyfgvptVWSRI--AADPEAAR---------------------- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 410 siwdelffnkiqaSLGGhVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHI 489
Cdd:PRK07787 239 -------------ALRG-ARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVET 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 490 KLVDaEELNYWTSKGE--GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDR------KKHIFK 561
Cdd:PRK07787 305 RLVD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGGYR 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1937369599 562 LAQGEyvapekIENIYIRSEPVAQIYVHG---DSLKAFLVGIVVPDPEVMP 609
Cdd:PRK07787 384 IGAGE------IETALLGHPGVREAAVVGvpdDDLGQRIVAYVVGADDVAA 428
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
269-606 |
5.45e-25 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 106.59 E-value: 5.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 269 DLSIVCFTSGTTGNPKGAMLTHGNVVA---DFSGFLKVTEsqwaptcADVHFSYLPLAHMFERMVQSVVYCHGGR-VGFF 344
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAanlQLIHAMGLTE-------ADVYLNMLPLFHIAGLNLALATFHAGGAnVVME 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 345 QGDIRLLSDDMKALRPTIFPVVPRLLNRMYDkifhqadtslkrwllefAAKRKQAEVRSgiIRNnsiwdelffnkiqasl 424
Cdd:cd17637 74 KFDPAEALELIEEEKVTLMGSFPPILSNLLD-----------------AAEKSGVDLSS--LRH---------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 425 gghvrmiVTGAApaSPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDaeELNYWTSKG 504
Cdd:cd17637 119 -------VLGLD--APETIQRFEETTGATFWSLYGQTE-TSGLVTLSPYRERPGSAGRPGPLVRVRIVD--DNDRPVPAG 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 505 E-GEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRK--KHIFKlAQGEYVAPEKIENIYIRSE 581
Cdd:cd17637 187 EtGEIVVRGPLVFQGYWNLPELTAYTFR-NGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKVILEHP 264
|
330 340
....*....|....*....|....*
gi 1937369599 582 PVAQIYVHGdslkaflvgivVPDPE 606
Cdd:cd17637 265 AIAEVCVIG-----------VPDPK 278
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
256-598 |
2.20e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 107.81 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 256 QENHRVPVPPRPD-DLSIVCFTSGTTGNPKGAMLTHGNVVADfsgflKVTESQWAPTCAD---VHFSYLPLAHMF-ERMV 330
Cdd:PRK06710 193 EVNTGVEVPCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSN-----TLMGVQWLYNCKEgeeVVLGVLPFFHVYgMTAV 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 331 QSVVYCHGGRVGFF-QGDIRLLSDDMKALRPTIFPVVPRLLNRMydkifhqadtsLKRWLLefaakrKQAEVRSgiirnn 409
Cdd:PRK06710 268 MNLSIMQGYKMVLIpKFDMKMVFEAIKKHKVTLFPGAPTIYIAL-----------LNSPLL------KEYDISS------ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 410 siwdelffnkiqaslgghVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgctfTTPGDW-----TSGHVGAPL 484
Cdd:PRK06710 325 ------------------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSP----VTHSNFlwekrVPGSIGVPW 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 485 PCNHIKLVDAEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQ 564
Cdd:PRK06710 383 PDTEAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VAS 460
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1937369599 565 GEYVAPEKIENIYIRSEPVAQIYV-------HGDSLKAFLV 598
Cdd:PRK06710 461 GFNVYPREVEEVLYEHEKVQEVVTigvpdpyRGETVKAFVV 501
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
111-590 |
4.51e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 106.79 E-value: 4.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 111 FRKPEQPY-----QWLSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGS 185
Cdd:PRK07786 28 LMQPDAPAlrflgNTTTWRELDDRVAALAGALSRRG--VGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 186 IRYIINTADiCTVIVDKPHKAILLLEhvERKETPGLKLVILMEP--------FDDALRERGKKCG-VDIksmqaiedsgq 256
Cdd:PRK07786 106 IAFLVSDCG-AHVVVTEAALAPVATA--VRDIVPLLSTVVVAGGssddsvlgYEDLLAEAGPAHApVDI----------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 257 enhrvpvpprPDDL-SIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEsqwAPTCADVHFSYLPLAHMfeRMVQSVVy 335
Cdd:PRK07786 172 ----------PNDSpALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNG---ADINSDVGFVGVPLFHI--AGIGSML- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 336 chggrVGFFQGdirllsddmkalRPT-IFPVVPRLLNRMYDKIFHQADTSL----KRWLLEFAAKRKQAevrsgiiRNNS 410
Cdd:PRK07786 236 -----PGLLLG------------APTvIYPLGAFDPGQLLDVLEAEKVTGIflvpAQWQAVCAEQQARP-------RDLA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 411 IwdelffnkiqaslgghvRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAgCTFTTPGD---WTSGHVGAPLPC 486
Cdd:PRK07786 292 L-----------------RVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEMSP-VTCMLLGEdaiRKLGSVGKVIPT 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 487 NHIKLVDaEELNYwTSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSdGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQG 565
Cdd:PRK07786 354 VAARVVD-ENMND-VPVGEvGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGG 429
|
490 500
....*....|....*....|....*
gi 1937369599 566 EYVAPEKIENIYIRSEPVAQIYVHG 590
Cdd:PRK07786 430 ENIYCAEVENVLASHPDIVEVAVIG 454
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
111-588 |
1.05e-23 |
|
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: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 111 FRKPEQPY-----QWLSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLydtlGPGS 185
Cdd:cd17655 8 EKTPDHTAvvfedQTLTYRELNERANQLARTLREKG--VGPDTIVGIMAERSLEMIVGILGILKAGGAYLPI----DPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 186 ----IRYIINTADIctvivdkphkAILLLEHVERKETPGLKLVILMEpfDDALRERGKkcgvdiksmqaiedsgqENhrV 261
Cdd:cd17655 82 peerIQYILEDSGA----------DILLTQSHLQPPIAFIGLIDLLD--EDTIYHEES-----------------EN--L 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 262 PVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVadfsgflkvtesqwaptcadvhfsylplaHMFERMVQSVVYCHGGRV 341
Cdd:cd17655 131 EPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVV-----------------------------NLVEWANKVIYQGEHLRV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 342 GFFQGdirlLSDDMkalrpTIFPVVPRLL--NRMYdkIFHQADTSLKRWLLEFAAKRkqaevRSGIIR-NNSIWDELffN 418
Cdd:cd17655 182 ALFAS----ISFDA-----SVTEIFASLLsgNTLY--IVRKETVLDGQALTQYIRQN-----RITIIDlTPAHLKLL--D 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 419 KIQASLGGHVRMIVTGAAPASPTVLGFL--RAALGCQVYEGYGQTECTAGCTF--TTPGDWTSGHV--GAPLPCNHIKLV 492
Cdd:cd17655 244 AADDSEGLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETTVDASIyqYEPETDQQVSVpiGKPLGNTRIYIL 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 493 DAEElnYWTSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWL------HTGDIGKWLPEGTLKIIDRKKHIFKLaQG 565
Cdd:cd17655 324 DQYG--RPQPVGVaGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-RG 400
|
490 500
....*....|....*....|...
gi 1937369599 566 EYVAPEKIENIYIRSEPVAQIYV 588
Cdd:cd17655 401 YRIELGEIEARLLQHPDIKEAVV 423
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
120-557 |
1.10e-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: 105.78 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 120 WLSYQEVAKRAEFLGSGLLQHdCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGS---IRYIINTADIC 196
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAV-GKPGDR--VLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 197 TVIVDKPHKAiLLLEHVERKETPGLKLVILMEPFDDALRERGkkcgvdiksmqaiedsgqenhrVPVPPRPDDLSIVCFT 276
Cdd:cd05931 101 VVLTTAAALA-AVRAFAASRPAAGTPRLLVVDLLPDTSAADW----------------------PPPSPDPDDIAYLQYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 277 SGTTGNPKGAMLTHGNVVADFSGFLKvtesQWAPTCADVHFSYLPLAH-MfermvqsvvychgGRVG------FFQGDIR 349
Cdd:cd05931 158 SGSTGTPKGVVVTHRNLLANVRQIRR----AYGLDPGDVVVSWLPLYHdM-------------GLIGglltplYSGGPSV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 350 LLSddmkalrPTIFpvvprlLNRMYdkifhqadtslkRWL-----------------LEFAAKRKQAEVRSGIirnnsiw 412
Cdd:cd05931 221 LMS-------PAAF------LRRPL------------RWLrlisryratisaapnfaYDLCVRRVRDEDLEGL------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 413 dELffnkiqaslgGHVRMIVTGAAPASPTVL----------GFLRAAlgcqVYEGYGQTECTAGCTFTTPG--------- 473
Cdd:cd05931 269 -DL----------SSWRVALNGAEPVRPATLrrfaeafapfGFRPEA----FRPSYGLAEATLFVSGGPPGtgpvvlrvd 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 474 -DWTSGHV----------------GAPLPCNHIKLVDAEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKE------AL 530
Cdd:cd05931 334 rDALAGRAvavaaddpaarelvscGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaAT 413
|
490 500
....*....|....*....|....*..
gi 1937369599 531 DSDGWLHTGDIGkWLPEGTLKIIDRKK 557
Cdd:cd05931 414 DEGGWLRTGDLG-FLHDGELYITGRLK 439
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
269-685 |
1.76e-23 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 102.02 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 269 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkvTESQWAPTCADVHFSYLPLAHM--FERMVQSVVycHGGRVGFFQG 346
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAG----LHSRLGFGGGDSWLLSLPLYHVggLAILVRSLL--AGAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 347 DiRLLSDDMKALRPTIFPVVPRLLNRMYDKifHQADTSLKRwllefaakrkqaevrsgiirnnsiwdelffnkiqaslgg 426
Cdd:cd17630 75 N-QALAEDLAPPGVTHVSLVPTQLQRLLDS--GQGPAALKS--------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 427 hVRMIVTGAAPASPtvlGFLRAA--LGCQVYEGYGQTEcTAGCTFT-TPGDWTSGHVGAPLPCNHIKLVDaeelnywtsk 503
Cdd:cd17630 113 -LRAVLLGGAPIPP---ELLERAadRGIPLYTTYGMTE-TASQVATkRPDGFGRGGVGVLLPGRELRIVE---------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 504 gEGEICVKGPNVFKGYLKDedRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIEniyirsepv 583
Cdd:cd17630 178 -DGEIWVGGASLAMGYLRG--QLVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIE--------- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 584 AQIYVHGDSLKAFLVGivVPDPEvmpcWAQK---------KGIEGNYQELCKSKelkkailddmvmlgkesgLHSFEQVK 654
Cdd:cd17630 245 AALAAHPAVRDAFVVG--VPDEE----LGQRpvavivgrgPADPAELRAWLKDK------------------LARFKLPK 300
|
410 420 430
....*....|....*....|....*....|.
gi 1937369599 655 AIYIhcdmfsVQNGLLTPTLKAKRPELREYF 685
Cdd:cd17630 301 RIYP------VPELPRTGGGKVDRRALRAWL 325
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
162-574 |
2.22e-23 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 106.16 E-value: 2.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 162 IAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIVDKPhkailLLEHVERK----ETPGLKLVILMEPFDDALRER 237
Cdd:PRK08633 680 LANLALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVITSRK-----FLEKLKNKgfdlELPENVKVIYLEDLKAKISKV 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 238 GKKC-GVDIKSMQA--IEDSGQENhrvpvpPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD---FSGFLKVTESqwapt 311
Cdd:PRK08633 755 DKLTaLLAARLLPArlLKRLYGPT------FKPDDTATIIFSSGSEGEPKGVMLSHHNILSNieqISDVFNLRND----- 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 312 caDVHFSYLPLAHMFERMV-QSVVYCHGGRVGFFqgdirllSDDMKAL---------RPTIFPVVPRLLnRMYdkifhqa 381
Cdd:PRK08633 824 --DVILSSLPFFHSFGLTVtLWLPLLEGIKVVYH-------PDPTDALgiaklvakhRATILLGTPTFL-RLY------- 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 382 dtslkrwllefaakrkqaevrsgiIRNNSIWDELFfnkiqASLgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQT 461
Cdd:PRK08633 887 ------------------------LRNKKLHPLMF-----ASL----RLVVAGAEKLKPEVADAFEEKFGIRILEGYGAT 933
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 462 ECTAGCTFTTP-----GDWT-----SGHVGAPLPCNHIKLVDAEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEAL- 530
Cdd:PRK08633 934 ETSPVASVNLPdvlaaDFKRqtgskEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIk 1013
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1937369599 531 --DSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIE 574
Cdd:PRK08633 1014 diDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIG-GEMVPLGAVE 1058
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
266-606 |
2.75e-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: 103.78 E-value: 2.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 266 RPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKV----TESQWaptcadVHFSylplAHMFERMVQSVVY--CHGG 339
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRAlgltSESRV------LQFA----SYTFDVSILEIFTtlAAGG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 340 ---------RVGFFQGDIRllsdDMKA----LRPTifpvVPRLLNRmydkifhqadtslkrwllefaakrkqAEVRSgii 406
Cdd:cd05918 174 clcipseedRLNDLAGFIN----RLRVtwafLTPS----VARLLDP--------------------------EDVPS--- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 407 rnnsiwdelffnkiqaslgghVRMIVTGAAPASPTVLGflRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLP 485
Cdd:cd05918 217 ---------------------LRTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRPLG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 486 C--------NHIKLVdaeelnywtSKGE-GEICVKGPNVFKGYLKDEDRTKEA-LDSDGWLH------------TGDIGK 543
Cdd:cd05918 274 AtcwvvdpdNHDRLV---------PIGAvGELLIEGPILARGYLNDPEKTAAAfIEDPAWLKqegsgrgrrlyrTGDLVR 344
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937369599 544 WLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEP-----VAQIYVH-GDSLKAFLVGIVVPDPE 606
Cdd:cd05918 345 YNPDGSLEYVGRKDTQVKI-RGQRVELGEIEHHLRQSLPgakevVVEVVKPkDGSSSPQLVAFVVLDGS 412
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
112-569 |
3.84e-23 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 104.19 E-value: 3.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 112 RKPEQPYQWLSYQEVAKRAEFLGSGLLqhDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPL---YDTLG--PGSI 186
Cdd:PRK08180 61 RGADGGWRRLTYAEALERVRAIAQALL--DRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVspaYSLVSqdFGKL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 187 RYIINtadictvivdkphkailLLehverkeTPGLKLVILMEPFDDALRE-----------RGKKCGVDIKSMQAIEDSg 255
Cdd:PRK08180 139 RHVLE-----------------LL-------TPGLVFADDGAAFARALAAvvpadvevvavRGAVPGRAATPFAALLAT- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 256 qenhrvPVPP---------RPDDLSIVCFTSGTTGNPKGAMLTHGNVVA------DFSGFLKVTESqwaptcadVHFSYL 320
Cdd:PRK08180 194 ------PPTAavdaahaavGPDTIAKFLFTSGSTGLPKAVINTHRMLCAnqqmlaQTFPFLAEEPP--------VLVDWL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 321 PLAHMF--ERMVQSVVYcHGGR---------VGFFQGDIRLLsddmKALRPTIFPVVPRLlnrmydkifhqadtslkrWL 389
Cdd:PRK08180 260 PWNHTFggNHNLGIVLY-NGGTlyiddgkptPGGFDETLRNL----REISPTVYFNVPKG------------------WE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 390 LEFAAKRKQAEVRsgiirnnsiwdELFFNKiqaslgghVRMIVTGAAPASPTVLGFL----RAALGCQVY--EGYGQTEC 463
Cdd:PRK08180 317 MLVPALERDAALR-----------RRFFSR--------LKLLFYAGAALSQDVWDRLdrvaEATCGERIRmmTGLGMTET 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 464 TAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEelnywtskGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGK 543
Cdd:PRK08180 378 APSATFTTGPLSRAGNIGLPAPGCEVKLVPVG--------GKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVR 449
|
490 500 510
....*....|....*....|....*....|
gi 1937369599 544 WL----PEGTLKIIDRKKHIFKLAQGEYVA 569
Cdd:PRK08180 450 FVdpadPERGLMFDGRIAEDFKLSSGTWVS 479
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
121-605 |
7.17e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 103.09 E-value: 7.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:PRK08316 37 WTYAELDAAVNRVAAALLDLGLKKGDR--VAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 201 DKPhkailLLEHVERketpglklVILMEPFDDALRERGKKCGVDIKSMQAIED--SGQENHRVPVPPRPDDLSIVCFTSG 278
Cdd:PRK08316 115 DPA-----LAPTAEA--------ALALLPVDTLILSLVLGGREAPGGWLDFADwaEAGSVAEPDVELADDDLAQILYTSG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 279 TTGNPKGAMLTHGNVVADFSGflKVTESQWAPTCADVHfsYLPLAHMFERMV--QSVVYCHGGRVGFFQGDIRLLSDDMK 356
Cdd:PRK08316 182 TESLPKGAMLTHRALIAEYVS--CIVAGDMSADDIPLH--ALPLYHCAQLDVflGPYLYVGATNVILDAPDPELILRTIE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 357 ALRPTIF---PVVPRLLNRMYDkiFHQADTSlkrwllefaakrkqaevrsgiirnnsiwdelffnkiqaSLgghvRMIVT 433
Cdd:PRK08316 258 AERITSFfapPTVWISLLRHPD--FDTRDLS--------------------------------------SL----RKGYY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 434 GAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFTTPGDwtsgHVGAP----LPCNHI--KLVDA--EELnywtSKG 504
Cdd:PRK08316 294 GASIMPVEVLKELRERLpGLRFYNCYGQTEIAPLATVLGPEE----HLRRPgsagRPVLNVetRVVDDdgNDV----APG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 505 E-GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIyirsepv 583
Cdd:PRK08316 366 EvGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEA------- 436
|
490 500
....*....|....*....|..
gi 1937369599 584 aqIYVHGDSLKAFLVGivVPDP 605
Cdd:PRK08316 437 --LYTHPAVAEVAVIG--LPDP 454
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-584 |
9.39e-23 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 100.63 E-value: 9.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsGFLKVTESQWAPTcaDVHFSYLPLAHMFERMVQsvvychgGRVGFFQG 346
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYN--AWMLALNSLFDPD--DVLLCGLPLFHVNGSVVT-------LLTPLASG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 347 DIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTSLkrwllefaAKRKQAEVRSGIirnnsiwdelffnkiqaslgG 426
Cdd:cd05944 70 AHVVLAGPAGYRNPGLFDNFWKLVERYRITSLSTVPTVY--------AALLQVPVNADI--------------------S 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 427 HVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLV--DAEELNYWTSK 503
Cdd:cd05944 122 SLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKvlDGVGRLLRDCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 504 GE--GEICVKGPNVFKGYLKDEDRtKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSE 581
Cdd:cd05944 202 PDevGEICVAGPGVFGGYLYTEGN-KNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLRHP 279
|
...
gi 1937369599 582 PVA 584
Cdd:cd05944 280 AVA 282
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
121-605 |
1.35e-22 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 102.44 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGSGLLqhdcKVGTEQFIGVFAQ--NRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTV 198
Cdd:PRK13295 56 FTYRELAALVDRVAVGLA----RLGVGRGDVVSCQlpNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 199 IVDK-----PHKAIL--LlehveRKETPGLKLVILM-----EPFDDALRERGKKCGVDIksmQAIEDSgqenHRvpvpPR 266
Cdd:PRK13295 132 VVPKtfrgfDHAAMArrL-----RPELPALRHVVVVggdgaDSFEALLITPAWEQEPDA---PAILAR----LR----PG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVAD---FSGFLKVTESqwaptcaDVHFSYLPLAH----MFERMV-----QSVV 334
Cdd:PRK13295 196 PDDVTQLIYTSGTTGEPKGVMHTANTLMANivpYAERLGLGAD-------DVILMASPMAHqtgfMYGLMMpvmlgATAV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 335 YchggrvgffqGDIRllsDDMKALRptifpvvprlLNRMYDKIFHQADTSlkrWLLEFAakRKQAEVRSGIirnnsiwde 414
Cdd:PRK13295 269 L----------QDIW---DPARAAE----------LIRTEGVTFTMASTP---FLTDLT--RAVKESGRPV--------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 415 lffnkiqASLgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPGD---WTSGHVGAPLPCNHIKL 491
Cdd:PRK13295 312 -------SSL----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA-VTLTKLDDpdeRASTTDGCPLPGVEVRV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 492 VDAE--ELnywtSKGE-GEICVKGPNVFKGYLKDEDRTkeALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYV 568
Cdd:PRK13295 380 VDADgaPL----PAGQiGRLQVRGCSNFGGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENI 452
|
490 500 510
....*....|....*....|....*....|....*...
gi 1937369599 569 APEKIENIYIRSEPVAQiyvhgdslkaflVGIV-VPDP 605
Cdd:PRK13295 453 PVVEIEALLYRHPAIAQ------------VAIVaYPDE 478
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
156-598 |
3.35e-22 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 100.91 E-value: 3.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 156 NRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIVDKphKAILLLEHVERKETPGLKLVILMEPFDDALR 235
Cdd:PRK08008 71 NCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSA--QFYPMYRQIQQEDATPLRHICLTRVALPADD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 236 ERgkkcgVDIKSMQAiEDSGQENHRVPVppRPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLkvTESQWAPTCADV 315
Cdd:PRK08008 149 GV-----SSFTQLKA-QQPATLCYAPPL--STDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYY--SAWQCALRDDDV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 316 HFSYLPLAHMFermvqsvvychggrvgfFQgdirlLSDDMKAlrptiFPVVPRLLnrmydkifhqadtslkrwLLE-FAA 394
Cdd:PRK08008 217 YLTVMPAFHID-----------------CQ-----CTAAMAA-----FSAGATFV------------------LLEkYSA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 395 KRKQAEVRsgiirnnsiwdelffnKIQASLGGHVRMIVTG--AAPASPT--------VLGFLRAA----------LGCQV 454
Cdd:PRK08008 252 RAFWGQVC----------------KYRATITECIPMMIRTlmVQPPSANdrqhclreVMFYLNLSdqekdafeerFGVRL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 455 YEGYGQTECTAGCTFTTPGD---WTSghVGAPLPCNHIKLVDAEelNYWTSKGE-GEICVKG---PNVFKGYLKDEDRTK 527
Cdd:PRK08008 316 LTSYGMTETIVGIIGDRPGDkrrWPS--IGRPGFCYEAEIRDDH--NRPLPAGEiGEICIKGvpgKTIFKEYYLDPKATA 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937369599 528 EALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIyIRSEP-VAQIYVHG--DSL-----KAFLV 598
Cdd:PRK08008 392 KVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVELENI-IATHPkIQDIVVVGikDSIrdeaiKAFVV 468
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
112-606 |
3.83e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 100.89 E-value: 3.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 112 RKPEQP----Y-QWLSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSI 186
Cdd:PRK06178 45 ERPQRPaiifYgHVITYAELDELSDRFAALLRQRG--VGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 187 RYIINTADICTVIV-D------KPHKAILLLEHVErkeTPGLKLVILMEP---FDDALRERGKKCGVDIKSMQAIEDSGQ 256
Cdd:PRK06178 123 SYELNDAGAEVLLAlDqlapvvEQVRAETSLRHVI---VTSLADVLPAEPtlpLPDSLRAPRLAAAGAIDLLPALRACTA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 257 enhRVPVP-PRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPtcaDVHFSYLPlahMFermvqsvvy 335
Cdd:PRK06178 200 ---PVPLPpPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGED---SVFLSFLP---EF--------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 336 chggrvgFFQGDirllsdDMKALRPTIF--PVVprLLNRmYDkifhqADTSLKrwllefAAKRKQAEVRSGIIRNnsiWD 413
Cdd:PRK06178 262 -------WIAGE------NFGLLFPLFSgaTLV--LLAR-WD-----AVAFMA------AVERYRVTRTVMLVDN---AV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 414 ELF----FNKIQASLGGHVRmIVTGAAPASPTVLGFLRAALGCQVYEG-YGQTECTAGCTFTTpGDWTSGH--------V 480
Cdd:PRK06178 312 ELMdhprFAEYDLSSLRQVR-VVSFVKKLNPDYRQRWRALTGSVLAEAaWGMTETHTCDTFTA-GFQDDDFdllsqpvfV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 481 GAPLPCNHIKLVDAEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIF 560
Cdd:PRK06178 390 GLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEML 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1937369599 561 KLaQGEYVAPEKIENIYIRsepvaqiyvHGDSLKAFLVGivVPDPE 606
Cdd:PRK06178 469 KV-NGMSVFPSEVEALLGQ---------HPAVLGSAVVG--RPDPD 502
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
121-607 |
6.76e-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: 99.24 E-value: 6.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGSGLlqHDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:cd05945 17 LTYRELKERADALAAAL--ASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPALLIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 201 DkphkailllehverketpglklvilmepfddalrergkkcgvdiksmqaiedsgqenhrvpvpprPDDLSIVCFTSGTT 280
Cdd:cd05945 95 D-----------------------------------------------------------------GDDNAYIIFTSGST 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 281 GNPKGAMLTHGNVVAdfsgFLKVTESQWAPTCADVHFSYLPLAhmFERMVQSVVYC--HGGrvgffqgdirllsddmkal 358
Cdd:cd05945 110 GRPKGVQISHDNLVS----FTNWMLSDFPLGPGDVFLNQAPFS--FDLSVMDLYPAlaSGA------------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 359 rpTIFPVvPRLLNRMYdkifhqadtslkRWLLEFAAKRKQAEVRSgiirNNSIWDELF----FNkiQASLGGHVRMIVTG 434
Cdd:cd05945 165 --TLVPV-PRDATADP------------KQLFRFLAEHGITVWVS----TPSFAAMCLlsptFT--PESLPSLRHFLFCG 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 435 AAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFT--TP---GDWTSGHVGAPLPCNHIKLVDAEELNywTSKGE-GEI 508
Cdd:cd05945 224 EVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIevTPevlDGYDRLPIGYAKPGAKLVILDEDGRP--VPPGEkGEL 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 509 CVKGPNVFKGYLKDEDRTKEALDSD---GWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQ 585
Cdd:cd05945 302 VISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIELEEIEAALRQVPGVKE 380
|
490 500
....*....|....*....|....*.
gi 1937369599 586 IYV----HGDSlKAFLVGIVVPDPEV 607
Cdd:cd05945 381 AVVvpkyKGEK-VTELIAFVVPKPGA 405
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
220-574 |
1.19e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 99.30 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 220 GLKLVILMEPFDDA---LRERGKKcgvdiksMQAIEDSGQENHRVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD 296
Cdd:PRK07768 108 GAKAVVVGEPFLAAapvLEEKGIR-------VLTVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYAN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 297 FSGFlkVTESQWAPTcADVHFSYLPLAH-MfermvqsvvychgGRVGFfqgdirlLSDDMKA------LRPTIFPVVPRL 369
Cdd:PRK07768 181 AEAM--FVAAEFDVE-TDVMVSWLPLFHdM-------------GMVGF-------LTVPMYFgaelvkVTPMDFLRDPLL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 370 LNRMYDKifHQADT--------SLKRWLLEFAAKRKQAEVRSgiirnnsiwdelffnkiqaslgghVRMIVTGAAPASPT 441
Cdd:PRK07768 238 WAELISK--YRGTMtaapnfayALLARRLRRQAKPGAFDLSS------------------------LRFALNGAEPIDPA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 442 VL----------GFLRAALGCqvyeGYGQTECTAGCTFTTPGD--------------------WTSGHV------GAPLP 485
Cdd:PRK07768 292 DVedlldagarfGLRPEAILP----AYGMAEATLAVSFSPCGAglvvdevdadllaalrravpATKGNTrrlatlGPPLP 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 486 CNHIKLVDaEELNYWTSKGEGEICVKGPNVFKGYLkDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqG 565
Cdd:PRK07768 368 GLEVRVVD-EDGQVLPPRGVGVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-G 444
|
....*....
gi 1937369599 566 EYVAPEKIE 574
Cdd:PRK07768 445 RNIYPTDIE 453
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
121-576 |
1.38e-21 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 100.43 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGsGLLQHDCKVGteQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:PRK06814 659 LTYRKLLTGAFVLG-RKLKKNTPPG--ENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 201 DKP--HKA--------------ILLLEHVERKETPGLKLVILMEPFddalRERGKKCGVDiksmqaiedsgqenhrvpvp 264
Cdd:PRK06814 736 SRAfiEKArlgpliealefgirIIYLEDVRAQIGLADKIKGLLAGR----FPLVYFCNRD-------------------- 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 265 prPDDLSIVCFTSGTTGNPKGAMLTHGNVVA---------DFSGflkvtesqwaptcADVHFSYLPLAHMFermvqsvvy 335
Cdd:PRK06814 792 --PDDPAVILFTSGSEGTPKGVVLSHRNLLAnraqvaariDFSP-------------EDKVFNALPVFHSF--------- 847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 336 chggrvGFFQGDIRLLSDDMKAL---RPTIFPVVPRLLnrmYD---KIFHQADTSLkrwllefaakrkqaevrSGIIRNN 409
Cdd:PRK06814 848 ------GLTGGLVLPLLSGVKVFlypSPLHYRIIPELI---YDtnaTILFGTDTFL-----------------NGYARYA 901
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 410 SIWDelFFNkiqaslgghVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHI 489
Cdd:PRK06814 902 HPYD--FRS---------LRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEY 970
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 490 KLVDAEELNywtsKGeGEICVKGPNVFKGYLKDED-RTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYV 568
Cdd:PRK06814 971 RLEPVPGID----EG-GRLFVRGPNVMLGYLRAENpGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMI 1043
|
....*...
gi 1937369599 569 APEKIENI 576
Cdd:PRK06814 1044 SLAAVEEL 1051
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
121-613 |
1.99e-21 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 98.42 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGSGLLQHDCKVGteQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGLLPG--DRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 201 DKphkailllehverkETPGLKLVILMEPFDDALRERGKKCGVDIKSMQAIEDSGQENHRVPVPP--RPDDLSIVcFTSG 278
Cdd:PRK05852 122 DA--------------DGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTPATSTPEglRPDDAMIM-FTGG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 279 TTGNPKGAMLTHGNVVADFSGFlkVTESQWAPTCADVhfSYLPLAH---MFERMVQSVVycHGGRV-----GFFQGdiRL 350
Cdd:PRK05852 187 TTGLPKMVPWTHANIASSVRAI--ITGYRLSPRDATV--AVMPLYHghgLIAALLATLA--SGGAVllparGRFSA--HT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 351 LSDDMKALRPTIFPVVPRLlnrmydkifHQAdtslkrwLLEFAAKRKQAEVRSGIirnnsiwdelffnkiqaslgghvRM 430
Cdd:PRK05852 259 FWDDIKAVGATWYTAVPTI---------HQI-------LLERAATEPSGRKPAAL-----------------------RF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 431 IVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTfTTPGDWtSGHVGAPLPCN---------HIKLV--DAEELny 499
Cdd:PRK05852 300 IRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVT-TTQIEG-IGQTENPVVSTglvgrstgaQIRIVgsDGLPL-- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 500 wTSKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIR 579
Cdd:PRK05852 376 -PAGAVGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLAS 452
|
490 500 510
....*....|....*....|....*....|....*.
gi 1937369599 580 SEPVAQIYVHG--DSLKAFLVGIVVPDPEVMPCWAQ 613
Cdd:PRK05852 453 HPNVMEAAVFGvpDQLYGEAVAAVIVPRESAPPTAE 488
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
121-609 |
1.10e-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: 95.80 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGSGLlqHDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:cd12114 13 LTYGELAERARRVAGAL--KAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 201 DKPHkailLLEHVERketpglklvilmepfDDALRERGkkcgvdiksmQAIEDSGQEnhrVPVPPRPDDLSIVCFTSGTT 280
Cdd:cd12114 91 DGPD----AQLDVAV---------------FDVLILDL----------DALAAPAPP---PPVDVAPDDLAYVIFTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 281 GNPKGAMLTHG---NVVADfsgflkvTESQWAPTCADVHFSYLPLAHMFermvqSV-----VYCHGGRVgffqgdirlls 352
Cdd:cd12114 139 GTPKGVMISHRaalNTILD-------INRRFAVGPDDRVLALSSLSFDL-----SVydifgALSAGATL----------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 353 ddmkalrptifpVVPRllnrmydkifHQADTSLKRWllefaakrKQAEVRSGIirnnSIWdelffNKIQASLGghvrMIV 432
Cdd:cd12114 196 ------------VLPD----------EARRRDPAHW--------AELIERHGV----TLW-----NSVPALLE----MLL 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 433 TgAAPASPTVLGFLRAAL-------------------GCQVYEGYGQTECTAGCTF----TTPGDWTSGHVGAPLPCNHI 489
Cdd:cd12114 233 D-VLEAAQALLPSLRLVLlsgdwipldlparlralapDARLISLGGATEASIWSIYhpidEVPPDWRSIPYGRPLANQRY 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 490 KLVDA--EELNYWTskgEGEICVKGPNVFKGYLKDEDRTKEAL--DSDG--WLHTGDIGKWLPEGTLKIIDRKKHIFKLa 563
Cdd:cd12114 312 RVLDPrgRDCPDWV---PGELWIGGRGVALGYLGDPELTAARFvtHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKV- 387
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1937369599 564 QGEYVAPEKIENIYIRSEPVAQ--IYVHGDSLKAFLVGIVVPDPEVMP 609
Cdd:cd12114 388 RGYRIELGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPDNDGTP 435
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
112-605 |
3.31e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 94.57 E-value: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 112 RKPEQPY-----QWLSYQEVAKRAEfLGSGLLqHDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSI 186
Cdd:PRK06145 14 RTPDRAAlvyrdQEISYAEFHQRIL-QAAGML-HARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 187 RYIINTADICTVIVDKPHKAILLLEHverketpglklvilmepfddalrergKKCGVDIKSMQAIEDSGQENHRVP--VP 264
Cdd:PRK06145 92 AYILGDAGAKLLLVDEEFDAIVALET--------------------------PKIVIDAAAQADSRRLAQGGLEIPpqAA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 265 PRPDDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTESqwaptcaDVHFSYLPLAHMFERMVQSV-VYCHGGR 340
Cdd:PRK06145 146 VAPTDLVRLMYTSGTTDRPKGVMHSYGNLHwksIDHVIALGLTAS-------ERLLVVGPLYHVGAFDLPGIaVLWVGGT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 341 VGF---FQGDIRLLSDDMKALRPTIFpvVPRLLNRMY---DKifHQADTSLKRWLLefAAKRKQAEVRsgiIRNnsiwde 414
Cdd:PRK06145 219 LRIhreFDPEAVLAAIERHRLTCAWM--APVMLSRVLtvpDR--DRFDLDSLAWCI--GGGEKTPESR---IRD------ 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 415 lffnkiqaslgghvrmivtgaapasptvlgFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPcnHIKLV 492
Cdd:PRK06145 284 ------------------------------FTRVFTRARYIDAYGLTETCSGDTLMEAGREIEkiGSTGRALA--HVEIR 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 493 DAEELNYWTSKG-EGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPE 571
Cdd:PRK06145 332 IADGAGRWLPPNmKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASS 409
|
490 500 510
....*....|....*....|....*....|....*..
gi 1937369599 572 KIEN-IYIRSE--PVAQIYVHGDSLKAFLVGIVVPDP 605
Cdd:PRK06145 410 EVERvIYELPEvaEAAVIGVHDDRWGERITAVVVLNP 446
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
107-693 |
4.18e-20 |
|
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: 94.42 E-value: 4.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 107 PCLGFRKPEQPYQWLSYQEVAKRAEFLGSGLLQHDCKVgtEQFIGVFAQNRPEWIIAELACYTysmVVVPLydtlGPGSI 186
Cdd:cd05921 12 TWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGLSA--ERPLLILSGNSIEHALMALAAMY---AGVPA----APVSP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 187 RYIINTADIctvivDKphkaillLEHVERKETPGLKLVILMEPFDDALRE-----------RGKKCGVDIKSM------Q 249
Cdd:cd05921 83 AYSLMSQDL-----AK-------LKHLFELLKPGLVFAQDAAPFARALAAifplgtplvvsRNAVAGRGAISFaelaatP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 250 AIEDSGQENHRVpvppRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWA------PTCADvhfsYLPLA 323
Cdd:cd05921 151 PTAAVDAAFAAV----GPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQT----YPffgeepPVLVD----WLPWN 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 324 HMF--ERMVQSVVYcHGGRV---------GFFQGDIRLLSDDMkalrPTIFPVVPR----LLNRMYDkifhqaDTSLKRw 388
Cdd:cd05921 219 HTFggNHNFNLVLY-NGGTLyiddgkpmpGGFEETLRNLREIS----PTVYFNVPAgwemLVAALEK------DEALRR- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 389 llEFAAKRKQAEVrSGIIRNNSIWDELFFNKIQaSLGGHVRMivtgaapasptvlgflraalgcqvYEGYGQTECTAGCT 468
Cdd:cd05921 287 --RFFKRLKLMFY-AGAGLSQDVWDRLQALAVA-TVGERIPM------------------------MAGLGATETAPTAT 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 469 FTTPGDWTSGHVGAPLPCNHIKLVdaeelnywTSKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWL--- 545
Cdd:cd05921 339 FTHWPTERSGLIGLPAPGTELKLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpd 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 546 -PEGTLKIIDRKKHIFKLAQGEYVA--PekieniyIRSEPVAQI--YVHgDSL-----KAFLVGIVVPDPevMPCWAQKK 615
Cdd:cd05921 411 dPAKGLVFDGRVAEDFKLASGTWVSvgP-------LRARAVAACapLVH-DAVvagedRAEVGALVFPDL--LACRRLVG 480
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937369599 616 GIEGNYQELCKSKELKKAILDDMVMLGKESGlHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 693
Cdd:cd05921 481 LQEASDAEVLRHAKVRAAFRDRLAALNGEAT-GSSSRIARALLLDEPPSIDKGEITDKGYINQRAVLERRAALVERLY 557
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
121-607 |
5.81e-20 |
|
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: 93.42 E-value: 5.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELA------CYtysmvvVPLYDTLGPGSIRYIINTAD 194
Cdd:cd12117 23 LTYAELNERANRLARRLRAAG--VGPGDVVGVLAERSPELVVALLAvlkagaAY------VPLDPELPAERLAFMLADAG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 195 ICTVIVDKPhkailllehverketpglklvilmepfddaLRERGKKCGVDIKSMQAIEDSGQENhrVPVPPRPDDLSIVC 274
Cdd:cd12117 95 AKVLLTDRS------------------------------LAGRAGGLEVAVVIDEALDAGPAGN--PAVPVSPDDLAYVM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 275 FTSGTTGNPKGAMLTHGNVVAdfsgflKVTESQWAPTCADVHFSYL-PL---AHMFErmvqsvVY---CHGGRVgffqgd 347
Cdd:cd12117 143 YTSGSTGRPKGVAVTHRGVVR------LVKNTNYVTLGPDDRVLQTsPLafdASTFE------IWgalLNGARL------ 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 348 iRLLSDDmkalrptifpvVPRLLNRMYDKIFHQADTSLkrWLLefAAkrkqaevrsgiirnnsiwdelFFNKI----QAS 423
Cdd:cd12117 205 -VLAPKG-----------TLLDPDALGALIAEEGVTVL--WLT--AA---------------------LFNQLadedPEC 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 424 LGGhVRMIVTGAAPASPT-VLGFLRAALGCQVYEGYGQTECTagcTFTT-----PGDWTSGHV--GAPLPCNHIKLVDAe 495
Cdd:cd12117 248 FAG-LRELLTGGEVVSPPhVRRVLAACPGLRLVNGYGPTENT---TFTTshvvtELDEVAGSIpiGRPIANTRVYVLDE- 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 496 elnywtsKG-------EGEICVKGPNVFKGYLKDEDRTKEALDSDGWL------HTGDIGKWLPEGTLKIIDRKKHIFKL 562
Cdd:cd12117 323 -------DGrpvppgvPGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI 395
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1937369599 563 aQGEYVAPEKIENIYIRSEPVAQIYV---HGDSLKAFLVGIVVPDPEV 607
Cdd:cd12117 396 -RGFRIELGEIEAALRAHPGVREAVVvvrEDAGGDKRLVAYVVAEGAL 442
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
268-598 |
8.22e-20 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 92.52 E-value: 8.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 268 DDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSG--FLKVTESqwaptcaDVHFSylpLAHMFermvqsVVYCHGGRVGF 343
Cdd:cd05919 91 DDIAYLLYSSGTTGPPKGVMHAHRDPLlfADAMAreALGLTPG-------DRVFS---SAKMF------FGYGLGNSLWF 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 344 --FQGDIRLLSDD----------MKALRPTIFPVVPRllnrMYDKIFHQADTSlkrwllefaakrkQAEVRSgiIRnnsi 411
Cdd:cd05919 155 plAVGASAVLNPGwptaervlatLARFRPTVLYGVPT----FYANLLDSCAGS-------------PDALRS--LR---- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 412 wdelffnkiqaslgghvrmIVTGAAPASPTVLG-FLRAALGCQVYEGYGQTEctAGCTFTT--PGDWTSGHVGAPLPCNH 488
Cdd:cd05919 212 -------------------LCVSAGEALPRGLGeRWMEHFGGPILDGIGATE--VGHIFLSnrPGAWRLGSTGRPVPGYE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 489 IKLVDaEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYV 568
Cdd:cd05919 271 IRLVD-EEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWV 347
|
330 340 350
....*....|....*....|....*....|....*..
gi 1937369599 569 APEKIENIYIRSEPVAQIYV----HGDSL---KAFLV 598
Cdd:cd05919 348 SPVEVESLIIQHPAVAEAAVvavpESTGLsrlTAFVV 384
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
118-605 |
1.27e-19 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 92.94 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 118 YQWLSYQeVAKRAEFLGSgllqhdCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICT 197
Cdd:cd05970 50 FAELADY-SDKTANFFKA------MGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 198 VIVDKPHKailLLEHVE--RKETPGLKLVI-----LMEPFDDaLRERGKKCGVDIKSMQAiedsgqenhrvPVPPRPDDL 270
Cdd:cd05970 123 IVAIAEDN---IPEEIEkaAPECPSKPKLVwvgdpVPEGWID-FRKLIKNASPDFERPTA-----------NSYPCGEDI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 271 SIVCFTSGTTGNPKgaMLTHGNV--------------VADFSGFLKVTESQWAPTC-ADVHFSYLPLAHMFermvqsvVY 335
Cdd:cd05970 188 LLVYFSSGTTGMPK--MVEHDFTyplghivtakywqnVREGGLHLTVADTGWGKAVwGKIYGQWIAGAAVF-------VY 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 336 CHGgrvgffQGDIRLLSDDMKALRPTIF---PVVPRLLNRmydkifhqadTSLKRWLLefaakrkqaevrSGIirnnsiw 412
Cdd:cd05970 259 DYD------KFDPKALLEKLSKYGVTTFcapPTIYRFLIR----------EDLSRYDL------------SSL------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 413 delffnkiqaslgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPG-DWTSGHVGAPLPCNHIKL 491
Cdd:cd05970 304 ----------------RYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTL-TIATFPWmEPKPGSMGKPAPGYEIDL 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 492 VDAEELNYWTSKgEGEICV---KGPNV--FKGYLKDEDRTKEALdSDGWLHTGDIGkWLPE-GTLKIIDRKKHIFKlAQG 565
Cdd:cd05970 367 IDREGRSCEAGE-EGEIVIrtsKGKPVglFGGYYKDAEKTAEVW-HDGYYHTGDAA-WMDEdGYLWFVGRTDDLIK-SSG 442
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1937369599 566 EYVAPEKIENIYIRSEPVAQIYVHGdslkaflvgivVPDP 605
Cdd:cd05970 443 YRIGPFEVESALIQHPAVLECAVTG-----------VPDP 471
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
121-609 |
3.22e-19 |
|
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: 90.84 E-value: 3.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAG--VGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 201 DkphkailllehverketpglklvilmepfddalrergkkcgvdiksmqaiedsgqenhrvpvpprPDDLSIVCFTSGTT 280
Cdd:cd12115 103 D-----------------------------------------------------------------PDDLAYVIYTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 281 GNPKGAMLTHGNVVA------------DFSGFLKVTesqwaPTCADvhfsyLPLAHMFermvqsVVYCHGGRVGFFQGDI 348
Cdd:cd12115 118 GRPKGVAIEHRNAAAflqwaaaafsaeELAGVLAST-----SICFD-----LSVFELF------GPLATGGKVVLADNVL 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 349 RLLsDDMKALRPTIFPVVPrllnrmydkifhqadtSLKRWLLEFaakrkqaevrsgiirnnsiwdelffNKIQASlgghV 428
Cdd:cd12115 182 ALP-DLPAAAEVTLINTVP----------------SAAAELLRH-------------------------DALPAS----V 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 429 RMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFT--TPGDWTSGHVGAPLPCNHIKLVDaEELNYWTSKGE 505
Cdd:cd12115 216 RVVNLAGEPLPRDLVQRLYARLqVERVVNLYGPSEDTTYSTVApvPPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVP 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 506 GEICVKGPNVFKGYLKDEDRTKEALDSDGWL------HTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIR 579
Cdd:cd12115 295 GELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAALRS 373
|
490 500 510
....*....|....*....|....*....|...
gi 1937369599 580 SEPVAQ--IYVHGDSL-KAFLVGIVVPDPEVMP 609
Cdd:cd12115 374 IPGVREavVVAIGDAAgERRLVAYIVAEPGAAG 406
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
267-604 |
6.24e-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: 90.22 E-value: 6.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF--------LKVTESQWAPTCADVHFSYLPLAhmfermvqsvvYCHG 338
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWrreyeldsFPVRLLQMASFSFDVFAGDFARS-----------LLNG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 339 GRVGFFQGDIRL----LSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTSLKRWLLEFAAKRKQAEvrsgiirnnsiWde 414
Cdd:cd17650 161 GTLVICPDEVKLdpaaLYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQ-----------D-- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 415 lfFNKIQASLGGHVRMIvtgaapaspTVLGFLRAALGCQVYEGYGQTECTAGctfTTPgdwtsghVGAPLPCNHIKLVDa 494
Cdd:cd17650 228 --FKTLAARFGQGMRII---------NSYGVTEATIDSTYYEEGRDPLGDSA---NVP-------IGRPLPNTAMYVLD- 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 495 EELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGW------LHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYV 568
Cdd:cd17650 286 ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI-RGFRI 364
|
330 340 350
....*....|....*....|....*....|....*....
gi 1937369599 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 ... |
260-635 |
1.44e-18 |
|
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: 89.03 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 260 RVPVPPRPDDLSIVCFTSGTTGNPKGAMLTH----GNVVADFSGFlkvtesQWAPTCADVHFS-------------YLP- 321
Cdd:cd05971 80 SALVTDGSDDPALIIYTSGTTGPPKGALHAHrvllGHLPGVQFPF------NLFPRDGDLYWTpadwawigglldvLLPs 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 322 -------LAHMFERmvqsvvychggrvgfFQGD--IRLLSD---DMKALRPTIFpvvprllnrmydKIFHQADTSLKRWL 389
Cdd:cd05971 154 lyfgvpvLAHRMTK---------------FDPKaaLDLMSRygvTTAFLPPTAL------------KMMRQQGEQLKHAQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 390 LEfaakrkqaevrsgiirnnsiwdelffnkiqaslgghVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEC---TAG 466
Cdd:cd05971 207 VK------------------------------------LRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECnlvIGN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 467 CTFTTPGDwtSGHVGAPLPCNHIKLVDAEElNYWTSKGEGEICVKGPN--VFKGYLKDEDRTKEALDSDgWLHTGDIGKW 544
Cdd:cd05971 251 CSALFPIK--PGSMGKPIPGHRVAIVDDNG-TPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKMAGD-WLLTGDLGRK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 545 LPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRsepvaqiyvHGDSLKAFLVGIvvPDP---EVMPCWAQKKGIEGNY 621
Cdd:cd05971 327 DSDGYFWYVGRDDDVITSS-GYRIGPAEIEECLLK---------HPAVLMAAVVGI--PDPirgEIVKAFVVLNPGETPS 394
|
410
....*....|....*
gi 1937369599 622 QELCKS-KELKKAIL 635
Cdd:cd05971 395 DALAREiQELVKTRL 409
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
267-682 |
1.70e-18 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 89.47 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVAD------FSGFlkvTESqwaptcaDVHFSYLPLAH-------MFERMVQSv 333
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSALIVQslakiaIVGY---GED-------DVYLHTAPLCHigglssaLAMLMVGA- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 334 vyCHggrVGFFQGDIRLLSDDMKALRPTIFPVVPRLLnrmydkifhqADtslkrwLLEFAAKRKQAEVRSGiirnnsiwd 413
Cdd:PLN02860 240 --CH---VLLPKFDAKAALQAIKQHNVTSMITVPAMM----------AD------LISLTRKSMTWKVFPS--------- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 414 elffnkiqaslgghVRMIVTGAAPASP-----TVLGFLRAALgcqvYEGYGQTECTAGCTFTTPGDWT------------ 476
Cdd:PLN02860 290 --------------VRKILNGGGSLSSrllpdAKKLFPNAKL----FSAYGMTEACSSLTFMTLHDPTlespkqtlqtvn 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 477 -----SGH------VGAPLPcnHIKL-VDAEElnywtSKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKW 544
Cdd:PLN02860 352 qtkssSVHqpqgvcVGKPAP--HVELkIGLDE-----SSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWI 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 545 LPEGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSEPVAQIYVHGdslkaflvgivVPDPE----VMPC--------WA 612
Cdd:PLN02860 425 DKAGNLWLIGRSNDRIK-TGGENVYPEEVEAVLSQHPGVASVVVVG-----------VPDSRltemVVACvrlrdgwiWS 492
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 613 QKkgiegNYQELCKSKELKKAILDDMVmlgKESGLHSFEQVKAIYIHCDMFSvqnglLTPTLKAKRPELR 682
Cdd:PLN02860 493 DN-----EKENAKKNLTLSSETLRHHC---REKNLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEVR 549
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
120-610 |
2.84e-18 |
|
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: 88.51 E-value: 2.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 120 WLSYQEVAKRAEFLGSGLLqhDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVI 199
Cdd:cd12118 29 RYTWRQTYDRCRRLASALA--ALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 200 VDKPHKailllehverketpglklvilmepFDDALrergkkcgvdiksmqAIEDSGQEnhrvPVPPRPDDLSIVC-FTSG 278
Cdd:cd12118 107 VDREFE------------------------YEDLL---------------AEGDPDFE----WIPPADEWDPIALnYTSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 279 TTGNPKGAMLTH--------GNVVAdfsgflkvtesqWAptcADVHFSYLPLAHMFermvQSVVYCHGGRVGFFQG---- 346
Cdd:cd12118 144 TTGRPKGVVYHHrgaylnalANILE------------WE---MKQHPVYLWTLPMF----HCNGWCFPWTVAAVGGtnvc 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 347 ----DIRLLSDDMKALRPTIFPVVPRLLNrmydkifhqadtslkrwllefaakrkqaevrsgIIRNNSIWDelffnkiQA 422
Cdd:cd12118 205 lrkvDAKAIYDLIEKHKVTHFCGAPTVLN---------------------------------MLANAPPSD-------AR 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 423 SLGGHVRMIVTGAAPaSPTVLgFLRAALGCQVYEGYGQTEcTAG----CTF-----TTPGDWTS--------GHVGAplp 485
Cdd:cd12118 245 PLPHRVHVMTAGAPP-PAAVL-AKMEELGFDVTHVYGLTE-TYGpatvCAWkpewdELPTEERArlkarqgvRYVGL--- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 486 cNHIKLVDAEELNYWTSKGE--GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLA 563
Cdd:cd12118 319 -EEVDVLDPETMKPVPRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-IS 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1937369599 564 QGEYVAPEKIENIyirsepvaqIYVHGDSLKAFLVGivVPDP---EVmPC 610
Cdd:cd12118 396 GGENISSVEVEGV---------LYKHPAVLEAAVVA--RPDEkwgEV-PC 433
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
121-628 |
3.44e-18 |
|
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: 88.19 E-value: 3.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGSGLLQhdCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIIN--------- 191
Cdd:cd05959 30 LTYAELEAEARRVAGALRA--LGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEdsrarvvvv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 192 TADICTVIVDKPHKAILLLEHVERKE-TPGLKLVILMEPFDDALRERGKkcgvdiksmqaiedsgqenhrvPVPPRPDDL 270
Cdd:cd05959 108 SGELAPVLAAALTKSEHTLVVLIVSGgAGPEAGALLLAELVAAEAEQLK----------------------PAATHADDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 271 SIVCFTSGTTGNPKGAMLTHGN--VVADFSG--FLKVTESqwaptcaDVHFSYLPLAH--------MFERMVQSVVYCHG 338
Cdd:cd05959 166 AFWLYSSGSTGRPKGVVHLHADiyWTAELYArnVLGIRED-------DVCFSAAKLFFayglgnslTFPLSVGATTVLMP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 339 GRVgffqgDIRLLSDDMKALRPTIFPVVPRLLNRMydkifhqadtslkrwlleFAAKRKQAEVRSGIirnnsiwdelffn 418
Cdd:cd05959 239 ERP-----TPAAVFKRIRRYRPTVFFGVPTLYAAM------------------LAAPNLPSRDLSSL------------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 419 kiqaslgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTF--TTPGDWTSGHVGAPLPCNHIKLVDaEE 496
Cdd:cd05959 283 ----------RLCVSAGEALPAEVGERWKARFGLDILDGIGSTE--MLHIFlsNRPGRVRYGTTGKPVPGYEVELRD-ED 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 497 LNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEALDSdGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAPEKIENI 576
Cdd:cd05959 350 GGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQG-EWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSPFEVESA 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1937369599 577 YIRSEPVAQIYVHG-------DSLKAFlvgiVVPDPEVMPCWAQKKGIegnyQELCKSK 628
Cdd:cd05959 428 LVQHPAVLEAAVVGvededglTKPKAF----VVLRPGYEDSEALEEEL----KEFVKDR 478
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
121-606 |
1.94e-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: 85.97 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfigVFAQ--NRPEWIIAELACYtySMVVVPLYdTLgPG----SIRYIINTAD 194
Cdd:COG1021 51 LSYAELDRRADRLAAGLLALGLRPGDR----VVVQlpNVAEFVIVFFALF--RAGAIPVF-AL-PAhrraEISHFAEQSE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 195 ICTVIVDKPHkaiLLLEHVE-----RKETPGLKLVILMEPFDDALrergkkcgvdikSMQAIEDSGQEnHRVPVPPrPDD 269
Cdd:COG1021 123 AVAYIIPDRH---RGFDYRAlarelQAEVPSLRHVLVVGDAGEFT------------SLDALLAAPAD-LSEPRPD-PDD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 270 lsiVCF---TSGTTGNPKGAMLTHgnvvADFsgFLKVTESqwAPTCA----DVHFSYLPLAHMFErM----VQSVVYcHG 338
Cdd:COG1021 186 ---VAFfqlSGGTTGLPKLIPRTH----DDY--LYSVRAS--AEICGldadTVYLAALPAAHNFP-LsspgVLGVLY-AG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 339 GRVgffqgdirLLSDDMKALrpTIFPVVPRllnrmydkifHQAD-TSL-----KRWLlEFAAKRKQAevrsgiirnnsiw 412
Cdd:COG1021 253 GTV--------VLAPDPSPD--TAFPLIER----------ERVTvTALvpplaLLWL-DAAERSRYD------------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 413 deLffnkiqASLgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctaG-CTFTTPGD--WTSGH-VGAPL-PCN 487
Cdd:COG1021 299 --L------SSL----RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---GlVNYTRLDDpeEVILTtQGRPIsPDD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 488 HIKLVDAEELNywTSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKK-HIFKlaQG 565
Cdd:COG1021 364 EVRIVDEDGNP--VPPGEvGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKdQINR--GG 439
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1937369599 566 EYVAPEKIENiyirsepvaQIYVHGDSLKAFLVGivVPDPE 606
Cdd:COG1021 440 EKIAAEEVEN---------LLLAHPAVHDAAVVA--MPDEY 469
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
267-583 |
2.83e-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: 85.23 E-value: 2.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESqwapTCADVHFSYLPLAHmfermvqsvvychggRVGFFQG 346
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEW----KTKDRILSWMPLTH---------------DMGLIAF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 347 DIRLLSDDMKA-LRPT-IFPVVPRLlnrmydkifhqadtslkrWLLEfAAKRKQAEVRSGIIRNNSIWDELFFNKIQASL 424
Cdd:cd05908 166 HLAPLIAGMNQyLMPTrLFIRRPIL------------------WLKK-ASEHKATIVSSPNFGYKYFLKTLKPEKANDWD 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 425 GGHVRMIVTGAAPASP----------TVLGFLRAAlgcqVYEGYGQTECTAGCTF------------------------- 469
Cdd:cd05908 227 LSSIRMILNGAEPIDYelchefldhmSKYGLKRNA----ILPVYGLAEASVGASLpkaqspfktitlgrrhvthgepepe 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 470 ---TTPGDWTSGHVGAPLPCNHIKLVDaeELNYWTSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGkWL 545
Cdd:cd05908 303 vdkKDSECLTFVEVGKPIDETDIRICD--EDNKILPDGYiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FI 379
|
330 340 350
....*....|....*....|....*....|....*...
gi 1937369599 546 PEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPV 583
Cdd:cd05908 380 RNGRLVITGREKDII-FVNGQNVYPHDIERIAEELEGV 416
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
269-576 |
3.02e-17 |
|
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: 83.85 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 269 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKvteSQWAPTCADVHFSYLPLAHMFE--RMVQSVVYcHGGRVGFfqG 346
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQK---EGLNWVVGDVTYLPLPATHIGGlwWILTCLIH-GGLCVTG--G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 347 DIRLLSDDMKAL---RPTIFPVVPRLLNRMydkifhqadTSLKRWLLEFAAKrkqaevrsgiirnnsiwdelffnkiqas 423
Cdd:cd17635 76 ENTTYKSLFKILttnAVTTTCLVPTLLSKL---------VSELKSANATVPS---------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 424 lgghVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDAEELNYwTS 502
Cdd:cd17635 119 ----LRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLPTDDDSIEiNAVGRPYPGVDVYLAATDGIAG-PS 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937369599 503 KGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENI 576
Cdd:cd17635 194 ASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERI 265
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
259-594 |
4.76e-17 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 85.53 E-value: 4.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 259 HRVPVPPRPDDLSIVCFTSGTTGNPKGAMLTH----GNV-----VADFsgflkvtesqwapTCADVHFSYLPLAHMFerm 329
Cdd:PRK08043 356 RLAQVKQQPEDAALILFTSGSEGHPKGVVHSHksllANVeqiktIADF-------------TPNDRFMSALPLFHSF--- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 330 vqsvvychGGRVGffqgdirLLSDDMKALRPTIFP------VVPRLLnrmYDK----IFhqaDTSlkRWLLEFAakrkqa 399
Cdd:PRK08043 420 --------GLTVG-------LFTPLLTGAEVFLYPsplhyrIVPELV---YDRnctvLF---GTS--TFLGNYA------ 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 400 evrsgiiRNNSIWDelFFnkiqaslggHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGH 479
Cdd:PRK08043 471 -------RFANPYD--FA---------RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGT 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 480 VGAPLPCnhiklVDAEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTK-EALDSD--------GWLHTGDIGKWLPEGTL 550
Cdd:PRK08043 533 VGRILPG-----MDARLLSVPGIEQGGRLQLKGPNIMNGYLRVEKPGVlEVPTAEnargemerGWYDTGDIVRFDEQGFV 607
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1937369599 551 KIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQiyvHGDSLK 594
Cdd:PRK08043 608 QIQGRAKRFAKIA-GEMVSLEMVEQLALGVSPDKQ---HATAIK 647
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
121-590 |
7.40e-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: 84.10 E-value: 7.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGSGLLQHDCKVGteQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRPG--QRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 201 dkphkaillleHVERKETPGLKLVILMEPFDDALRERGKKCgvdiKSMQAIEDSgqenhrvpvPPRPDDLSIVCFTSGTT 280
Cdd:cd05923 107 -----------AVDAQVMDAIFQSGVRVLALSDLVGLGEPE----SAGPLIEDP---------PREPEQPAFVFYTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 281 GNPKGAMLTHgNVVADFSGFLkVTESQWAPTCADVHFSYLPLAHMfermvqsvvychggrVGFFQgdirLLSDDMkALRP 360
Cdd:cd05923 163 GLPKGAVIPQ-RAAESRVLFM-STQAGLRHGRHNVVLGLMPLYHV---------------IGFFA----VLVAAL-ALDG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 361 TIFPVvprllnrmydKIFHQADtslkrwllefAAKRKQAEVRSGIIRNNSIWDELFFNKIQASLG-GHVRMIVTGAAPAS 439
Cdd:cd05923 221 TYVVV----------EEFDPAD----------ALKLIEQERVTSLFATPTHLDALAAAAEFAGLKlSSLRHVTFAGATMP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 440 PTVLGFLRAALGCQVYEGYGQTECTagcTFTTPGDWTSGHVGAPLPCNHIKLVD-AEELNYWTSKG-EGEICVK--GPNV 515
Cdd:cd05923 281 DAVLERVNQHLPGEKVNIYGTTEAM---NSLYMRDARTGTEMRPGFFSEVRIVRiGGSPDEALANGeEGELIVAaaADAA 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937369599 516 FKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYVHG 590
Cdd:cd05923 358 FTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIG 430
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
27-604 |
8.64e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 85.21 E-value: 8.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 27 ATTLVSMGALAAILAYW--LTHRPKAlQPPCNL----LMQSEEVEDSGGARRsvigdctqlLTHYYDDARTMYQVFRRGL 100
Cdd:PRK12467 453 ATDLFEATTIERLATHWrnLLEAIVA-EPRRRLgelpLLDAEERARELVRWN---------APATEYAPDCVHQLIEAQA 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 101 SISGNGPCLGFRKpeqpyQWLSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDT 180
Cdd:PRK12467 523 RQHPERPALVFGE-----QVLSYAELNRQANRLAHVLIAAG--VGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPE 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 181 LGPGSIRYIINTADICTVIVDkPHKAILLlehverkETP-GLKLVILMEPFDdalrergkkcgvdiksmqaiEDSGQENH 259
Cdd:PRK12467 596 YPQDRLAYMLDDSGVRLLLTQ-SHLLAQL-------PVPaGLRSLCLDEPAD--------------------LLCGYSGH 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 260 RVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVvadfSGFLKVTESQWAPTCADVHFSYLPLAHMFERMVQSVVYCHGG 339
Cdd:PRK12467 648 NPEVALDPDNLAYVIYTSGSTGQPKGVAISHGAL----ANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGA 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 340 RVgffqgdirLLSDDMKALRPTIFpvvprllnrmYDKIFHQADTSLKrwllefaakrkqaevrsgiiRNNSIWDELFFNK 419
Cdd:PRK12467 724 TL--------HLLPPDCARDAEAF----------AALMADQGVTVLK--------------------IVPSHLQALLQAS 765
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 420 IQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTT----PGDWTSGHVGAPLPCNHIKLVDAe 495
Cdd:PRK12467 766 RVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYElsdeERDFGNVPIGQPLANLGLYILDH- 844
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 496 ELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEALDSD------GWLH-TGDIGKWLPEGTLKIIDRKKHIFKLaQGEYV 568
Cdd:PRK12467 845 YLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDpfgadgGRLYrTGDLARYRADGVIEYLGRMDHQVKI-RGFRI 923
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1937369599 569 APEKIENIYIRSEPVAQIYV------HGDSLKAFLVGIVVPD 604
Cdd:PRK12467 924 ELGEIEARLLAQPGVREAVVlaqpgdAGLQLVAYLVPAAVAD 965
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
421-626 |
1.16e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 83.92 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 421 QASLGGHVRMIVTGAAPasPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGD-WTSghvgapLPCN------------ 487
Cdd:PLN03102 296 LSPRSGPVHVLTGGSPP--PAALVKKVQRLGFQVMHAYGLTEATGPVLFCEWQDeWNR------LPENqqmelkarqgvs 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 488 HIKLVDAEELNYWT-------SKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIF 560
Cdd:PLN03102 368 ILGLADVDVKNKETqesvprdGKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937369599 561 kLAQGEYVAPEKIENIyirsepvaqIYVHGDSLKAFLVGIVVPDPEVMPCW--AQKKGIEGNYQELCK 626
Cdd:PLN03102 447 -ISGGENISSVEVENV---------LYKYPKVLETAVVAMPHPTWGETPCAfvVLEKGETTKEDRVDK 504
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
94-614 |
1.49e-16 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 83.29 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 94 QVFRRGLSISGNGPCLGFRKPEQpyQWLSYQEVAKRAEFLGSGLlqHD-CKVGTEQFIGVFAQNRPEWIIAELACYTYSM 172
Cdd:PRK05620 14 RILEYGSTVHGDTTVTTWGGAEQ--EQTTFAAIGARAAALAHAL--HDeLGITGDQRVGSMMYNCAEHLEVLFAVACMGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 173 VVVPLYDTLGPGSIRYIINTADIcTVIVDKPHKAILLLEHVerKETPGLKLVILMEPFDDALRERGKKCGVDIKSMQAIE 252
Cdd:PRK05620 90 VFNPLNKQLMNDQIVHIINHAED-EVIVADPRLAEQLGEIL--KECPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 253 DSGQENHRVPVPPRpDDLSIVCFTSGTTGNPKGAMLTHGNVVADfSGFLKVTESqWAPTCADVHFSYLPLAHMFERMVQS 332
Cdd:PRK05620 167 DGRSTVYDWPELDE-TTAAAICYSTGTTGAPKGVVYSHRSLYLQ-SLSLRTTDS-LAVTHGESFLCCVPIYHVLSWGVPL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 333 VVYCHGGrvgffqgdirllsddmkalrPTIFP----VVPRLLnrmydkifHQADTSLKRwllefaakrkqaeVRSGIirn 408
Cdd:PRK05620 244 AAFMSGT--------------------PLVFPgpdlSAPTLA--------KIIATAMPR-------------VAHGV--- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 409 NSIWDELFFNKIQ-----ASLgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGA- 482
Cdd:PRK05620 280 PTLWIQLMVHYLKnpperMSL----QEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEARWa 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 483 --------PLPCNHiKLVDAEELNYWTSKGEGEICVKGPNVFKGYLKDE----------------DRTKEALDSDGWLHT 538
Cdd:PRK05620 356 yrvsqgrfPASLEY-RIVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRT 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937369599 539 GDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSEPVaqiyvhgdsLKAFLVGIvvPDPEvmpcWAQK 614
Cdd:PRK05620 435 GDVGSVTRDGFLTIHDRARDVIR-SGGEWIYSAQLENYIMAAPEV---------VECAVIGY--PDDK----WGER 494
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
121-606 |
3.66e-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: 81.94 E-value: 3.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:cd17646 24 LTYRELDERANRLAHLLRARG--VGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 201 DkphkailllehverketpglklvilmepfdDALRERGKKcGVDIKSMQAIEDSGQENHRVPVPPRPDDLSIVCFTSGTT 280
Cdd:cd17646 102 T------------------------------ADLAARLPA-GGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGST 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 281 GNPKGAMLTHGNVVADFSGF---LKVTES----QWAPTCADVhfsylPLAHMFERMVQS---VVYCHGGRvgffqGDIRL 350
Cdd:cd17646 151 GRPKGVMVTHAGIVNRLLWMqdeYPLGPGdrvlQKTPLSFDV-----SVWELFWPLVAGarlVVARPGGH-----RDPAY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 351 LSDDMKALRPTIFPVVPRLLnrmydkifhqadtslkrwllefaakrkqaevrsgiirnnsiwdELFFNKIQASLGGHVRM 430
Cdd:cd17646 221 LAALIREHGVTTCHFVPSML-------------------------------------------RVFLAEPAAGSCASLRR 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 431 IVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHV--GAPLPCNHIKLVDAEeLNYWTSKGEGE 507
Cdd:cd17646 258 VFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVThWPVRGPAETPSVpiGRPVPNTRLYVLDDA-LRPVPVGVPGE 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 508 ICVKGPNVFKGYLKDEDRTKEALDSDGWLH------TGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSE 581
Cdd:cd17646 337 LYLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKI-RGFRVEPGEIEAALAAHP 415
|
490 500
....*....|....*....|....*...
gi 1937369599 582 PVAQIYV---HGDSLKAFLVGIVVPDPE 606
Cdd:cd17646 416 AVTHAVVvarAAPAGAARLVGYVVPAAG 443
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
262-609 |
4.77e-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: 81.62 E-value: 4.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 262 PVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVV-------ADFSGFLKVTESQWAPTCADVH----FSYLplahmfermv 330
Cdd:cd17651 130 DPALDADDLAYVIYTSGSTGRPKGVVMPHRSLAnlvawqaRASSLGPGARTLQFAGLGFDVSvqeiFSTL---------- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 331 qsvvyCHGGRVGFFQGDIRLLSDDMKALrptifpvvprLLNRMYDKIFhqADTSLKRWLLEfAAKRKQAEvrsgiirnns 410
Cdd:cd17651 200 -----CAGATLVLPPEEVRTDPPALAAW----------LDEQRISRVF--LPTVALRALAE-HGRPLGVR---------- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 411 iwdelffnkiqaslGGHVRMIVTG--AAPASPTVLGFLRAALGCQVYEGYGQTE---CTAGCTFTTPGDWTS-GHVGAPL 484
Cdd:cd17651 252 --------------LAALRYLLTGgeQLVLTEDLREFCAGLPGLRLHNHYGPTEthvVTALSLPGDPAAWPApPPIGRPI 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 485 PCNHIKLVDAeelnywtsKGE-------GEICVKGPNVFKGYLKDEDRTKEALDSDGWL------HTGDIGKWLPEGTLK 551
Cdd:cd17651 318 DNTRVYVLDA--------ALRpvppgvpGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELE 389
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937369599 552 IIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYV------HGDslkAFLVGIVVPDPEVMP 609
Cdd:cd17651 390 FLGRADDQVKI-RGFRIELGEIEAALARHPGVREAVVlaredrPGE---KRLVAYVVGDPEAPV 449
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
88-588 |
5.98e-16 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 81.34 E-value: 5.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 88 DARTMYQVFRRGLSISGNGPCLGFRKpeqpyQWLSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELAC 167
Cdd:PRK06155 19 SERTLPAMLARQAERYPDRPLLVFGG-----TRWTYAEAARAAAAAAHALAAAGVKRGDR--VALMCGNRIEFLDVFLGC 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 168 YTYSMVVVPLYDTLGPGSIRYIINTADICTVIVDKPHKAilLLEHVERKETPGLKLVILmepfdDALRERGKKCGVDIKS 247
Cdd:PRK06155 92 AWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLA--ALEAADPGDLPLPAVWLL-----DAPASVSVPAGWSTAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 248 MQAIEDSGQenhrvPVPPRPDDLSIVCFTSGTTGNPKGAMLTHG-------NVVADfsgfLKVTESqwaptcaDVHFSYL 320
Cdd:PRK06155 165 LPPLDAPAP-----AAAVQPGDTAAILYTSGTTGPSKGVCCPHAqfywwgrNSAED----LEIGAD-------DVLYTTL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 321 PLAH------MFERMVQSVVYCHGGRV---GFFqgdirllsDDMKALRPTIF----PVVPRLLnrmydkifhqadtslkr 387
Cdd:PRK06155 229 PLFHtnalnaFFQALLAGATYVLEPRFsasGFW--------PAVRRHGATVTyllgAMVSILL----------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 388 wllefaAKRKQAEVRsgiirnnsiwdelffnkiqaslgGH-VRMIVTGAAPASptVLGFLRAALGCQVYEGYGQTECTAG 466
Cdd:PRK06155 284 ------SQPARESDR-----------------------AHrVRVALGPGVPAA--LHAAFRERFGVDLLDGYGSTETNFV 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 467 CtFTTPGDWTSGHVGAPLPCNHIKLVDAEELNywTSKGE-GEICVKG--PNVF-KGYLKDEDRTKEALdSDGWLHTGDIG 542
Cdd:PRK06155 333 I-AVTHGSQRPGSMGRLAPGFEARVVDEHDQE--LPDGEpGELLLRAdePFAFaTGYFGMPEKTVEAW-RNLWFHTGDRV 408
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1937369599 543 KWLPEGTLKIIDRKKHIFKlAQGEYVAPEKIENIyIRSEP-VAQIYV 588
Cdd:PRK06155 409 VRDADGWFRFVDRIKDAIR-RRGENISSFEVEQV-LLSHPaVAAAAV 453
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
266-606 |
1.15e-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: 80.04 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 266 RPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkvTESQWAPTCADV----H-----FS----YLPLAHmfermvqs 332
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA----TQRWFGFNEDDVwtlfHsyafdFSvweiWGALLH-------- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 333 vvychGGRVGFFQGDIRLLSDDMkalrptifpvvPRLLNRMYDKIFHQADTSLKRWLlefaakrkQAEVRsgiirnnsiw 412
Cdd:cd17643 159 -----GGRLVVVPYEVARSPEDF-----------ARLLRDEGVTVLNQTPSAFYQLV--------EAADR---------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 413 delfFNKIQASLgghvRMIVTGAAPASPTVLGFLRAALGC---QVYEGYGQTECTAGCTFT--TPGDW---TSGHVGAPL 484
Cdd:cd17643 205 ----DGRDPLAL----RYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFRplDAADLpaaAASPIGRPL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 485 PCNHIKLVDAEeLNYWTSKGEGEICVKGPNVFKGYLKDEDRTKE-------ALDSDGWLHTGDIGKWLPEGTLKIIDRKK 557
Cdd:cd17643 277 PGLRVYVLDAD-GRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRLPDGELEYLGRAD 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1937369599 558 HIFKLaQGEYVAPEKIENIYIRSEPVAQIYV---HGDSLKAFLVGIVVPDPE 606
Cdd:cd17643 356 EQVKI-RGFRIELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVADDG 406
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
107-568 |
3.05e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 79.32 E-value: 3.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 107 PCLGFRKPEQ-PYQWLSYQEVAKRAEFLGSGLLqhDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLydtlgpgS 185
Cdd:PRK12582 66 PWLAQREPGHgQWRKVTYGEAKRAVDALAQALL--DLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPV-------S 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 186 IRYIINTADIctvivDKphkaillLEHVERKETPGLKLVILMEPFDDALRERGKKcGVDIKSMQAIEDSGQENH---RVP 262
Cdd:PRK12582 137 PAYSLMSHDH-----AK-------LKHLFDLVKPRVVFAQSGAPFARALAALDLL-DVTVVHVTGPGEGIASIAfadLAA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 263 VPPR-----------PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVT-ESQWAPTcaDVHFSYLPLAHMFERMV 330
Cdd:PRK12582 204 TPPTaavaaaiaaitPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRpREPDPPP--PVSLDWMPWNHTMGGNA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 331 Q--------SVVYCHGGR--VGFFQGDIRLLSDdmkaLRPTIFPVVPRLLNRMYDKIfhQADTSLKRWLLefaaKRKQAE 400
Cdd:PRK12582 282 NfngllwggGTLYIDDGKplPGMFEETIRNLRE----ISPTVYGNVPAGYAMLAEAM--EKDDALRRSFF----KNLRLM 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 401 VRSGIIRNNSIWDELFFNKIQASlgGHvrMIVtgaapasptvlgflraalgcqVYEGYGQTEcTAGCTFTTpgDWTS--- 477
Cdd:PRK12582 352 AYGGATLSDDLYERMQALAVRTT--GH--RIP---------------------FYTGYGATE-TAPTTTGT--HWDTerv 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 478 GHVGAPLPCNHIKLVDAEElNYwtskgegEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWL----PEGTLKII 553
Cdd:PRK12582 404 GLIGLPLPGVELKLAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdpddPEKGLIFD 475
|
490
....*....|....*
gi 1937369599 554 DRKKHIFKLAQGEYV 568
Cdd:PRK12582 476 GRVAEDFKLSTGTWV 490
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
457-613 |
3.65e-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: 77.34 E-value: 3.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 457 GYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAE--ELnywtSKGE-GEICVKGPNVFKGYLkDEDRTKEALDSD 533
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDgrEV----PDGEvGEIVARGPTVMAGYW-NRPEVNARRTRG 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 534 GWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqgeyvapekIENIY-------IRSEP-VAQIYVhgdslkaflvgIVVPDP 605
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSG---------AENIYpaevercLRQHPaVADAAV-----------IGVPDP 276
|
....*...
gi 1937369599 606 EvmpcWAQ 613
Cdd:cd17636 277 R----WAQ 280
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
121-609 |
5.08e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 78.25 E-value: 5.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADiCTVIV 200
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQG--VRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGR-ARWLV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 201 DKPH-KAILL---LEHVERKETPGLKLVILMEPFDDALRERGKKCGVdiksmQAIEDSGQENHRV-PVPPRPDDLSIVCF 275
Cdd:PRK06164 113 VWPGfKGIDFaaiLAAVPPDALPPLRAIAVVDDAADATPAPAPGARV-----QLFALPDPAPPAAaGERAADPDAGALLF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 276 T-SGTTGNPK------GAMLTHGNVVADFSGFlkvtesqwAPtcADVHFSYLPLahmfermvqSVVYCHGGRVGFFQGDI 348
Cdd:PRK06164 188 TtSGTTSGPKlvlhrqATLLRHARAIARAYGY--------DP--GAVLLAALPF---------CGVFGFSTLLGALAGGA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 349 RLLSDDmkalrptIF--PVVPRLL-----------NRMYDKIFHQADTSLkrwllEFAAKRkqaevRSGIIRNNSIWDEL 415
Cdd:PRK06164 249 PLVCEP-------VFdaARTARALrrhrvthtfgnDEMLRRILDTAGERA-----DFPSAR-----LFGFASFAPALGEL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 416 ffnkiqaslgghvrmivtgaaPASPTVLGFLRAALgcqvyegYGQTECTA---GCTFTTPgdWTSGHVGAPLPCN---HI 489
Cdd:PRK06164 312 ---------------------AALARARGVPLTGL-------YGSSEVQAlvaLQPATDP--VSVRIEGGGRPASpeaRV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 490 KLVDAEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVA 569
Cdd:PRK06164 362 RARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVN 440
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1937369599 570 PEKIENIYIRSEPVAQIYVHGDSL--KAFLVGIVVPDPEVMP 609
Cdd:PRK06164 441 PAEIEHALEALPGVAAAQVVGATRdgKTVPVAFVIPTDGASP 482
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
265-603 |
7.83e-15 |
|
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: 77.50 E-value: 7.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 265 PRPDDLSIVCFTSGTTGNPKGAMLTHGNvvadFSGFLKVTESQWAPTCADVHFSYLPLAHMFERM--VQSVVychggrvg 342
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGT----FAAQIDALRQLYGIRPGEVDLATFPLFALFGPAlgLTSVI-------- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 343 ffqgdirllsDDMKALRPtifpvvprllnrmydkifhqADTSlKRWLLEFAAkrkQAEVrSGIIRNNSIWDEL--FFNKI 420
Cdd:cd05910 150 ----------PDMDPTRP--------------------ARAD-PQKLVGAIR---QYGV-SIVFGSPALLERVarYCAQH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 421 QASLGGhVRMIVTGAAPASPTVLGFLRAAL--GCQVYEGYGQTECTAGCT------FTTPGDWTSGH----VGAPLPCNH 488
Cdd:cd05910 195 GITLPS-LRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrelLATTTAATSGGagtcVGRPIPGVR 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 489 IKLV--DAEELNYWTSKGE------GEICVKGPNVFKGYLKDEDRTKEALDSDG----WLHTGDIGKWLPEGTLKIIDRK 556
Cdd:cd05910 274 VRIIeiDDEPIAEWDDTLElprgeiGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRK 353
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1937369599 557 KHIFKLAQGEYVapekieniyirSEPVAQIY-VHGDSLKAFLVGIVVP 603
Cdd:cd05910 354 AHRVITTGGTLY-----------TEPVERVFnTHPGVRRSALVGVGKP 390
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
420-588 |
2.27e-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: 75.68 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 420 IQASLGG---HVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTfTTPGD-WTSGHVGAPLPCNHIKLVDAE 495
Cdd:cd05974 191 IQQDLASfdvKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVG-NSPGQpVKAGSMGRPLPGYRVALLDPD 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 496 ElnywTSKGEGEICV-----KGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAP 570
Cdd:cd05974 270 G----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SSDYRISP 343
|
170
....*....|....*...
gi 1937369599 571 EKIENIYIRSEPVAQIYV 588
Cdd:cd05974 344 FELESVLIEHPAVAEAAV 361
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
119-599 |
4.40e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 76.53 E-value: 4.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 119 QWLSYQEVAKRAEFLGSGLLqhDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGS-IRYIINTADICT 197
Cdd:PRK12316 2027 QHLSYAELDSRANRLAHRLR--ARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPL-DPNYPAErLAYMLEDSGAAL 2103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 198 VIVDkphkailllEHVERKETPGLKLVILmePFDDALrergkkcgvdiksmqAIEDSGQENHRVPVPprPDDLSIVCFTS 277
Cdd:PRK12316 2104 LLTQ---------RHLLERLPLPAGVARL--PLDRDA---------------EWADYPDTAPAVQLA--GENLAYVIYTS 2155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 278 GTTGNPKGAMLTHGNVVAdfsgFLKVTESQWAPTCADVHFSYLPLAhmFERMVQSVVY--CHGGRVgffqgdirLLSDDM 355
Cdd:PRK12316 2156 GSTGLPKGVAVSHGALVA----HCQAAGERYELSPADCELQFMSFS--FDGAHEQWFHplLNGARV--------LIRDDE 2221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 356 KalrptifpvvpRLLNRMYDKIFHQADTslkrwLLEFAAKRKQAEVRSGIIRNNSIwdelffnkiqaslggHVRMIVTGA 435
Cdd:PRK12316 2222 L-----------WDPEQLYDEMERHGVT-----ILDFPPVYLQQLAEHAERDGRPP---------------AVRVYCFGG 2270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 436 APASPTVLGFLRAALGCQ-VYEGYGQTEctagcTFTTPGDWTSGH----------VGAPLPCNHIKLVDAeELNYWTSKG 504
Cdd:PRK12316 2271 EAVPAASLRLAWEALRPVyLFNGYGPTE-----AVVTPLLWKCRPqdpcgaayvpIGRALGNRRAYILDA-DLNLLAPGM 2344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 505 EGEICVKGPNVFKGYLKDEDRTKEALDSDGWLH-------TGDIGKWLPEGTLKIIDRKKHI-----FKLAQGEYVApEK 572
Cdd:PRK12316 2345 AGELYLGGEGLARGYLNRPGLTAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQvkirgFRIELGEIEA-RL 2423
|
490 500
....*....|....*....|....*...
gi 1937369599 573 IENIYIRSEPV-AQIYVHGDSLKAFLVG 599
Cdd:PRK12316 2424 QAHPAVREAVVvAQDGASGKQLVAYVVP 2451
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
121-293 |
2.24e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 73.00 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGPGDH--VGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 201 DKPhkailLLEHVE--RKETPGLKLVILMEPFDDALRERGkkcGVDIKSMQAIEDSGqenhRVPVPPRPDDLSIVCfTSG 278
Cdd:PRK07798 107 ERE-----FAPRVAevLPRLPKLRTLVVVEDGSGNDLLPG---AVDYEDALAAGSPE----RDFGERSPDDLYLLY-TGG 173
|
170
....*....|....*
gi 1937369599 279 TTGNPKGAMLTHGNV 293
Cdd:PRK07798 174 TTGMPKGVMWRQEDI 188
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
262-603 |
4.52e-13 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 72.24 E-value: 4.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 262 PVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGfLKvteSQWAPTCADVHFSYLPLAHMFERM--VQSVVychgg 339
Cdd:PRK09274 168 MADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEA-LR---EDYGIEPGEIDLPTFPLFALFGPAlgMTSVI----- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 340 rvgffqgdirllsDDMKALRP-TIFPvvprllnrmyDKIFHQAD----TSLkrwlleFAA-----KRKQAEVRSGIIRNN 409
Cdd:PRK09274 239 -------------PDMDPTRPaTVDP----------AKLFAAIErygvTNL------FGSpalleRLGRYGEANGIKLPS 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 410 siwdelffnkiqaslgghVRMIVTGAAPASPTVLGFLRAAL--GCQVYEGYGQTECTAGCT-------FTTPGDWTSGH- 479
Cdd:PRK09274 290 ------------------LRRVISAGAPVPIAVIERFRAMLppDAEILTPYGATEALPISSiesreilFATRAATDNGAg 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 480 --VGAPLPCNHIKLV--DAEELNYWT-----SKGE-GEICVKGPNVFKGYLKDEDRTKEA--LDSDG--WLHTGDIGkWL 545
Cdd:PRK09274 352 icVGRPVDGVEVRIIaiSDAPIPEWDdalrlATGEiGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLG-YL 430
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 546 -PEGTLKIIDRKKHIFKLAQGEYVapekieniyirSEPVAQIY-VHGDSLKAFLVGIVVP 603
Cdd:PRK09274 431 dAQGRLWFCGRKAHRVETAGGTLY-----------TIPCERIFnTHPGVKRSALVGVGVP 479
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
421-610 |
4.70e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 72.29 E-value: 4.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 421 QASLGGHVRMIVTGAAPAsPTVLGFLRAAlGCQVYEGYGQTEcTAG----CTFTtpGDWTS----------GHVGAPLPC 486
Cdd:PRK08162 292 RAGIDHPVHAMVAGAAPP-AAVIAKMEEI-GFDLTHVYGLTE-TYGpatvCAWQ--PEWDAlplderaqlkARQGVRYPL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 487 -NHIKLVDAEELNYWTSKGE--GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLA 563
Cdd:PRK08162 367 qEGVTVLDPDTMQPVPADGEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDII-IS 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1937369599 564 QGEYVAPEKIENIyirsepvaqIYVHgdslKAFLVGIVV--PDP---EVmPC 610
Cdd:PRK08162 445 GGENISSIEVEDV---------LYRH----PAVLVAAVVakPDPkwgEV-PC 482
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
429-606 |
5.48e-13 |
|
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: 71.59 E-value: 5.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 429 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHVGAPL-PCNHIKLVDaEELNYWTSKGEG 506
Cdd:cd05920 258 RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTrLDDPDEVIIHTQGRPMsPDDEIRVVD-EEGNPVPPGEEG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 507 EICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENiyirsepvaQI 586
Cdd:cd05920 337 ELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVEN---------LL 406
|
170 180
....*....|....*....|
gi 1937369599 587 YVHGDSLKAFLVGivVPDPE 606
Cdd:cd05920 407 LRHPAVHDAAVVA--MPDEL 424
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
130-605 |
5.80e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 72.00 E-value: 5.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 130 AEFLGSGLLQHDCkvgteqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV--DKPhkai 207
Cdd:PRK07470 47 AALAARGVRKGDR-------ILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMIChaDFP---- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 208 lllEHVE--RKETPGLKLVIlmePFDDALRERGKKCGVDIKSMQAIEDSGQENhrvpvpprpDDLSIVCFTSGTTGNPKG 285
Cdd:PRK07470 116 ---EHAAavRAASPDLTHVV---AIGGARAGLDYEALVARHLGARVANAAVDH---------DDPCWFFFTSGTTGRPKA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 286 AMLTHG-------NVVADFsgFLKVTEsqwaptcADVHFSYLPLAHM--FERMVQSVvycHGGRVGFFQGDiRLLSDDMK 356
Cdd:PRK07470 181 AVLTHGqmafvitNHLADL--MPGTTE-------QDASLVVAPLSHGagIHQLCQVA---RGAATVLLPSE-RFDPAEVW 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 357 AL----RPTIFPVVPRLLNRMY-DKIFHQADTSlkrwllefaakrkqaevrsgiirnnsiwdelffnkiqaSLgghvRMI 431
Cdd:PRK07470 248 ALverhRVTNLFTVPTILKMLVeHPAVDRYDHS--------------------------------------SL----RYV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 432 VTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-----GDWTSGHVGaplPCNH------IKLVDAE--ELn 498
Cdd:PRK07470 286 IYAGAPMYRADQKRALAKLGKVLVQYFGLGEVTGNITVLPPalhdaEDGPDARIG---TCGFertgmeVQIQDDEgrEL- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 499 ywtSKGE-GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENiy 577
Cdd:PRK07470 362 ---PPGEtGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPREIEE-- 434
|
490 500
....*....|....*....|....*...
gi 1937369599 578 irsepvaQIYVHGDSLKAFLVGivVPDP 605
Cdd:PRK07470 435 -------KLLTHPAVSEVAVLG--VPDP 453
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
268-609 |
5.86e-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: 71.36 E-value: 5.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 268 DDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF----LKVTESqwaptcaDVHFSYLPLAHMFERMVQSVVYCHGGR--V 341
Cdd:cd05958 97 DDICILAFTSGTTGAPKATMHFHRDPLASADRYavnvLRLRED-------DRFVGSPPLAFTFGLGGVLLFPFGVGAsgV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 342 GFFQGDIRLLSDDMKALRPTIFPVVPRllnrMYDKIFHQADTSlkrwllefaakrkqaevrsgiirnnsiwdelffnkiq 421
Cdd:cd05958 170 LLEEATPDLLLSAIARYKPTVLFTAPT----AYRAMLAHPDAA------------------------------------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 422 ASLGGHVRMIVTgAAPASPTVLGFL-RAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNyw 500
Cdd:cd05958 209 GPDLSSLRKCVS-AGEALPAALHRAwKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVDDEGNP-- 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 501 TSKGE-GEICVKGPNvfkGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIR 579
Cdd:cd05958 286 VPDGTiGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQ 361
|
330 340 350
....*....|....*....|....*....|...
gi 1937369599 580 SEPVAQIYVHGDSLKAFLV---GIVVPDPEVMP 609
Cdd:cd05958 362 HPAVAECAVVGHPDESRGVvvkAFVVLRPGVIP 394
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
427-598 |
6.18e-13 |
|
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: 71.73 E-value: 6.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 427 HVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDaEELNYWTSKGEG 506
Cdd:cd05928 292 SLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIID-DNGNVLPPGTEG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 507 EICVK-GPN----VFKGYLKDEDRTKEALDSDGWLhTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSE 581
Cdd:cd05928 371 DIGIRvKPIrpfgLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYRIGPFEVESALIEHP 448
|
170 180
....*....|....*....|....
gi 1937369599 582 PVAQIYV-------HGDSLKAFLV 598
Cdd:cd05928 449 AVVESAVvsspdpiRGEVVKAFVV 472
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
150-607 |
8.39e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 71.25 E-value: 8.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 150 IGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIVDKPHKAIL--LLEHVERKETPGLKLVILM 227
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLdgLDPGVRVINVDSPAWADEL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 228 EPFDDALRErgkkcgvdiksmqaiedsgqenhrvPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVTESQ 307
Cdd:PRK07867 137 AAHRDAEPP-------------------------FRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVA--SAGVMLAQRFG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 308 WAPTcaDVHFSYLPLAHMFERMVQ-SVVYCHGGRV---------GFFqgdirllsDDMKALRPTIFPVVPRLLN------ 371
Cdd:PRK07867 190 LGPD--DVCYVSMPLFHSNAVMAGwAVALAAGASIalrrkfsasGFL--------PDVRRYGATYANYVGKPLSyvlatp 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 372 -RMYDkifhqADTSLKrwllefaakrkqaevrsgiirnnsiwdelffnkiqaslgghvrmIVTGAAPASPTVLGFlRAAL 450
Cdd:PRK07867 260 eRPDD-----ADNPLR--------------------------------------------IVYGNEGAPGDIARF-ARRF 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 451 GCQVYEGYGQTEctAGCTFTTPGDWTSGHVGaPLPCNhIKLVDAE----------ELNYWTSKGE--GEIC-VKGPNVFK 517
Cdd:PRK07867 290 GCVVVDGFGSTE--GGVAITRTPDTPPGALG-PLPPG-VAIVDPDtgtecppaedADGRLLNADEaiGELVnTAGPGGFE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 518 GYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYVHGdslkafl 597
Cdd:PRK07867 366 GYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPIERILLRYPDATEVAVYA------- 436
|
490
....*....|
gi 1937369599 598 vgivVPDPEV 607
Cdd:PRK07867 437 ----VPDPVV 442
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
267-578 |
1.17e-12 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 71.00 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWAPTCADVHFSYLPLAHMFermvqsvvychggrvGFfqG 346
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKF----FSPKEDDVMMSFLPPFHAY---------------GF--N 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 347 DIRLLSddMKALRPTIF---PVVPRLLNRMYDK---IFHQADTSLKRWLLEFAAKRKQA--EVRSGIIRNNSIWDELFfn 418
Cdd:PRK06334 241 SCTLFP--LLSGVPVVFaynPLYPKKIVEMIDEakvTFLGSTPVFFDYILKTAKKQESClpSLRFVVIGGDAFKDSLY-- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 419 kiqaslgghvrmivTGAAPASPTVlgflraalgcQVYEGYGQTECTAGCTFTT---PGDwtSGHVGAPLPCNHIKLVdAE 495
Cdd:PRK06334 317 --------------QEALKTFPHI----------QLRQGYGTTECSPVITINTvnsPKH--ESCVGMPIRGMDVLIV-SE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 496 ELNYWTSKGE-GEICVKGPNVFKGYL-KDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKI 573
Cdd:PRK06334 370 ETKVPVSSGEtGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSLEAL 448
|
....*
gi 1937369599 574 ENIYI 578
Cdd:PRK06334 449 ESILM 453
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
271-584 |
1.20e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 70.89 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 271 SIVCFTSGTTGNPKGAMLTHGNvvadfsgflkvtesqwaptcadvhfsylplahmfermvqSVVYCHGGRvgffqgdirl 350
Cdd:PRK07008 179 SSLCYTSGTTGNPKGALYSHRS---------------------------------------TVLHAYGAA---------- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 351 LSDDMK-ALRPTIFPVVPrllnrmydkIFHqadtsLKRWLLEFAAKRKQAE-VRSG-IIRNNSIWDELFFNKIQASLG-- 425
Cdd:PRK07008 210 LPDAMGlSARDAVLPVVP---------MFH-----VNAWGLPYSAPLTGAKlVLPGpDLDGKSLYELIEAERVTFSAGvp 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 426 -------GHV----------RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPgdwTSGHVGAPLPCNH 488
Cdd:PRK07008 276 tvwlgllNHMreaglrfstlRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLCKL---KWKHSQLPLDEQR 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 489 --------------IKLVDAE--ELNyWTSKGEGEICVKGPNVFKGYLKDEDrtkEALDsDGWLHTGDIGKWLPEGTLKI 552
Cdd:PRK07008 353 kllekqgrviygvdMKIVGDDgrELP-WDGKAFGDLQVRGPWVIDRYFRGDA---SPLV-DGWFPTGDVATIDADGFMQI 427
|
330 340 350
....*....|....*....|....*....|..
gi 1937369599 553 IDRKKHIFKlAQGEYVAPEKIENIYIRSEPVA 584
Cdd:PRK07008 428 TDRSKDVIK-SGGEWISSIDIENVAVAHPAVA 458
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
121-606 |
1.55e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 70.49 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:PRK13391 25 VTYRELDERSNRLAHLFRSLGLKRGDH--VAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALIT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 201 DKPHKAI--LLLEHVerketPGLKLVILMEPFDDalrergkkcgvdiksMQAIEDSGQENHRVPVPPRPDDL--SIVCFT 276
Cdd:PRK13391 103 SAAKLDVarALLKQC-----PGVRHRLVLDGDGE---------------LEGFVGYAEAVAGLPATPIADESlgTDMLYS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 277 SGTTGNPKG--AMLTHGNVVaDFSGFLKVTESQWAPTCADVHFSYLPLAHMFERMVQSVVYCHGGRV----GFfqgdirl 350
Cdd:PRK13391 163 SGTTGRPKGikRPLPEQPPD-TPLPLTAFLQRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVivmeHF------- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 351 lsDDMKAL------RPTIFPVVPRLLNRMydkifhqadtsLKrwLLEfaAKRKQAEVRSgiirnnsiwdelffnkiqasl 424
Cdd:PRK13391 235 --DAEQYLalieeyGVTHTQLVPTMFSRM-----------LK--LPE--EVRDKYDLSS--------------------- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 425 gghVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCN-HIKLVDAEELnywt 501
Cdd:PRK13391 277 ---LEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATE-GLGFTACDSEEWLAhpGTVGRAMFGDlHILDDDGAEL---- 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 502 SKGE-GEICVKGPNVFKgYLKDEDRTKEALDSDG-WLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIR 579
Cdd:PRK13391 349 PPGEpGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMI-ISGGVNIYPQEAENLLIT 426
|
490 500
....*....|....*....|....*..
gi 1937369599 580 SEPVAQIYVHGdslkaflvgivVPDPE 606
Cdd:PRK13391 427 HPKVADAAVFG-----------VPNED 442
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
86-639 |
4.34e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 70.19 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 86 YDDARTMYQVFRRGLSISGNGPCLGFRKpeqpyQWLSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAEL 165
Cdd:PRK12467 1570 YPLARLVHQLIEDQAAATPEAVALVFGE-----QELTYGELNRRANRLAHRLIALG--VGPEVLVGIAVERSLEMVVGLL 1642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 166 ACYTYSMVVVPLYDTLGPGSIRYIINTADIctvivdkphkAILLLEHVERKETP---GLKLVILmEPFDDALrergkkcg 242
Cdd:PRK12467 1643 AILKAGGAYVPLDPEYPRERLAYMIEDSGI----------ELLLTQSHLQARLPlpdGLRSLVL-DQEDDWL-------- 1703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 243 vdiksmqaiedSGQENHRVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFsgflKVTESQWAPTCADVHFSYLPL 322
Cdd:PRK12467 1704 -----------EGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRL----CATQEAYQLSAADVVLQFTSF 1768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 323 AhmFERMVQSVVY--CHGGRVgffqgdirLLSDDMKALRPTIFpvvPRLLNRMYDKIFHQADTSLKRwLLEFAAkrKQAE 400
Cdd:PRK12467 1769 A--FDVSVWELFWplINGARL--------VIAPPGAHRDPEQL---IQLIERQQVTTLHFVPSMLQQ-LLQMDE--QVEH 1832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 401 VRSgiirnnsiwdelffnkiqaslgghVRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAG-----CTFTTPGD 474
Cdd:PRK12467 1833 PLS------------------------LRRVVCGGEALEVEALRPWLERLPdTGLFNLYGPTETAVDvthwtCRRKDLEG 1888
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 475 WTSGHVGAPLPCNHIKLVDAeELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEAL------DSDGWLH-TGDIGKWLPE 547
Cdd:PRK12467 1889 RDSVPIGQPIANLSTYILDA-SLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgTVGSRLYrTGDLARYRAD 1967
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 548 GTLKIIDRKKHIFKLaQGEYVAPEKIENiYIRSEP----VAQIYVHGDSLKAfLVGIVVPDPEVMPCWAQKKgieGNYQE 623
Cdd:PRK12467 1968 GVIEYLGRIDHQVKI-RGFRIELGEIEA-RLREQGgvreAVVIAQDGANGKQ-LVAYVVPTDPGLVDDDEAQ---VALRA 2041
|
570
....*....|....*.
gi 1937369599 624 LCKsKELKKAILDDMV 639
Cdd:PRK12467 2042 ILK-NHLKASLPEYMV 2056
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
262-598 |
4.48e-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: 4.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 262 PVPPRPDDLSIVCFTSGTTGNPKGAMLTHGN--VVADFSG--FLKVTESQWAPTCADVHFSY-LPLAHMFERMVQSVVYC 336
Cdd:TIGR02262 155 PAATQADDPAFWLYSSGSTGMPKGVVHTHSNpyWTAELYArnTLGIREDDVCFSAAKLFFAYgLGNALTFPMSVGATTVL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 337 HGGR---VGFFqgdirllsDDMKALRPTIFPVVPRLLNRMYdkifhqADTSLKrwllefaaKRKQAEVRsgiirnnsiwd 413
Cdd:TIGR02262 235 MGERptpDAVF--------DRLRRHQPTIFYGVPTLYAAML------ADPNLP--------SEDQVRLR----------- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 414 elffnkiqaslgghvrmIVTGAAPASPTVLGF-LRAALGCQVYEGYGQTEctAGCTFTT--PGDWTSGHVGAPLPCNHIK 490
Cdd:TIGR02262 282 -----------------LCTSAGEALPAEVGQrWQARFGVDIVDGIGSTE--MLHIFLSnlPGDVRYGTSGKPVPGYRLR 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 491 LVDaeELNYWTSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSdGWLHTGDigKWL--PEGTLKIIDRKKHIFKLAqGEY 567
Cdd:TIGR02262 343 LVG--DGGQDVADGEpGELLISGPSSATMYWNNRAKSRDTFQG-EWTRSGD--KYVrnDDGSYTYAGRTDDMLKVS-GIY 416
|
330 340 350
....*....|....*....|....*....|....*...
gi 1937369599 568 VAPEKIENIYIRSEPVAQIYVHG----DSL---KAFLV 598
Cdd:TIGR02262 417 VSPFEIESALIQHPAVLEAAVVGvadeDGLikpKAFVV 454
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
440-588 |
5.32e-12 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 68.36 E-value: 5.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 440 PTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTSGhVGAPLPCNHIKLVDaeelnywtskgeGEICVKGPNVFKGY 519
Cdd:PRK09029 253 PVELTEQAEQQGIRCWCGYGLTE-MASTVCAKRADGLAG-VGSPLPGREVKLVD------------GEIWLRGASLALGY 318
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937369599 520 LKDeDRTKEALDSDGWLHTGDIGKWLpEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYV 588
Cdd:PRK09029 319 WRQ-GQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQVFV 384
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
86-598 |
5.34e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 69.60 E-value: 5.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 86 YDDARTMYQVFRRGLSISGNGPCLGFRKpeqpyQWLSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAEL 165
Cdd:PRK12316 3053 YPLERGVHRLFEEQVERTPDAVALAFGE-----QRLSYAELNRRANRLAHRLIERG--VGPDVLVGVAVERSLEMVVGLL 3125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 166 ACYTYSMVVVPLYDTLGPGSIRYIINTADIcTVIVDKPHKAILLLEHVErketpglklVILMEPFDDALRErgkkcgvdi 245
Cdd:PRK12316 3126 AILKAGGAYVPLDPEYPEERLAYMLEDSGA-QLLLSQSHLRLPLAQGVQ---------VLDLDRGDENYAE--------- 3186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 246 ksmqaiedsgqenHRVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNvvadFSGFLKVTESQWAPTCADVHFSYLPLAHM 325
Cdd:PRK12316 3187 -------------ANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSA----LSNHLCWMQQAYGLGVGDRVLQFTTFSFD 3249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 326 FERMVQSVVYCHGGRVgfFQGDIRLLSDdmkalrptifpvvPRLLNRMYDKifHQADTSLKRWllefaakrkqaevrsgi 405
Cdd:PRK12316 3250 VFVEELFWPLMSGARV--VLAGPEDWRD-------------PALLVELINS--EGVDVLHAYP----------------- 3295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 406 irnnSIWDELFFNKIQASLGGHVRMIVTGAAPASPtvlGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGH--VGAP 483
Cdd:PRK12316 3296 ----SMLQAFLEEEDAHRCTSLKRIVCGGEALPAD---LQQQVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRP 3368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 484 LPCNHIKLVDAeELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGW------LHTGDIGKWLPEGTLKIIDRKK 557
Cdd:PRK12316 3369 IANRACYILDG-SLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVD 3447
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1937369599 558 HIFKLaQGEYVAPEKIENIYIRSEPV---AQIYVHGDSLKAFLV 598
Cdd:PRK12316 3448 HQVKI-RGFRIELGEIEARLLEHPWVreaVVLAVDGRQLVAYVV 3490
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
255-606 |
5.54e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 68.80 E-value: 5.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 255 GQENHRVPVPPRPDdlSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLkvtesqwaptcadvhfSYLPLaHMFERMVQSVV 334
Cdd:PRK07788 196 GSSTAPLPKPPKPG--GIVILTSGTTGTPKGAPRPEPSPLAPLAGLL----------------SRVPF-RAGETTLLPAP 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 335 YCHGgrVGFFQGDIRLlsddmkALRPTIfpVVPRLL---NRMYDKIFHQAD------TSLKRwLLEFAAKRKQA-EVRSg 404
Cdd:PRK07788 257 MFHA--TGWAHLTLAM------ALGSTV--VLRRRFdpeATLEDIAKHKATalvvvpVMLSR-ILDLGPEVLAKyDTSS- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 405 iirnnsiwdelffnkiqaslgghVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECtAGCTFTTPGDWT--SGHVGA 482
Cdd:PRK07788 325 -----------------------LKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEV-AFATIATPEDLAeaPGTVGR 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 483 PLPCNHIKLVDAE--ELnywtSKGE-GEICVKGPNVFKGYLkdEDRTKEALdsDGWLHTGDIGKWLPEGTLKIIDRKKHI 559
Cdd:PRK07788 381 PPKGVTVKILDENgnEV----PRGVvGRIFVGNGFPFEGYT--DGRDKQII--DGLLSSGDVGYFDEDGLLFVDGRDDDM 452
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1937369599 560 FkLAQGEYVAPEKIENIYIRSEPVAQIYVHGdslkaflvgivVPDPE 606
Cdd:PRK07788 453 I-VSGGENVFPAEVEDLLAGHPDVVEAAVIG-----------VDDEE 487
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
274-590 |
6.03e-12 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 68.62 E-value: 6.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 274 CFTSGTTGNPKGAMLTH-GNVVadfsgflkvtesqwaptcadvhfsylplahmfermvQSVVYCHGGRVGFFQGDirlls 352
Cdd:PRK06018 183 CYTSGTTGDPKGVLYSHrSNVL------------------------------------HALMANNGDALGTSAAD----- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 353 ddmkalrpTIFPVVPrllnrmydkIFHQadtslKRWLLEFAAKRKQAE-VRSGI-IRNNSIWDELFFNKIQASLG----- 425
Cdd:PRK06018 222 --------TMLPVVP---------LFHA-----NSWGIAFSAPSMGTKlVMPGAkLDGASVYELLDTEKVTFTAGvptvw 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 426 --------------GHVRMIVTGAApASPTvlGFLRA--ALGCQVYEGYGQTECTAGCTFTT--------PGDWTSGHV- 480
Cdd:PRK06018 280 lmllqymekeglklPHLKMVVCGGS-AMPR--SMIKAfeDMGVEVRHAWGMTEMSPLGTLAAlkppfsklPGDARLDVLq 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 481 --GAPLPCNHIKLVD--AEELNyWTSKGEGEICVKGPNVFKGYLKDEDrtkEALDSDGWLHTGDIGKWLPEGTLKIIDRK 556
Cdd:PRK06018 357 kqGYPPFGVEMKITDdaGKELP-WDGKTFGRLKVRGPAVAAAYYRVDG---EILDDDGFFDTGDVATIDAYGYMRITDRS 432
|
330 340 350
....*....|....*....|....*....|....
gi 1937369599 557 KHIFKlAQGEYVAPEKIENIYIRSEPVAQIYVHG 590
Cdd:PRK06018 433 KDVIK-SGGEWISSIDLENLAVGHPKVAEAAVIG 465
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
119-639 |
1.83e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 68.06 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 119 QWLSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGS-IRYIINTAdict 197
Cdd:PRK12316 4575 EKLTYAELNRRANRLAHALIARG--VGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPL-DPEYPRErLAYMMEDS---- 4647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 198 vivdkphKAILLLEHveRKETPGLklvilmePFDDalrergkkcGVDIKSMQAIED-SGQENHRVPVPPRPDDLSIVCFT 276
Cdd:PRK12316 4648 -------GAALLLTQ--SHLLQRL-------PIPD---------GLASLALDRDEDwEGFPAHDPAVRLHPDNLAYVIYT 4702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 277 SGTTGNPKGAMLTHGNVVAdfsgFLKVTESQWAPTCADVHFSYLPLAhmFERMVQSV--VYCHGGRVgffqgdirLLSDD 354
Cdd:PRK12316 4703 SGSTGRPKGVAVSHGSLVN----HLHATGERYELTPDDRVLQFMSFS--FDGSHEGLyhPLINGASV--------VIRDD 4768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 355 MKALRPTIFpvvpRLLNRMYDKIFHQADTSLKRWLLEFAAKRKQAEVRsgiirnnsiwdelffnkiQASLGGHvrmivtG 434
Cdd:PRK12316 4769 SLWDPERLY----AEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLR------------------VYCFGGE------A 4820
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 435 AAPASPTVLgfLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSG----HVGAPLPCNHIKLVDaEELNYWTSKGEGEIC 509
Cdd:PRK12316 4821 VAQASYDLA--WRALKPVYLFNGYGPTETTVTVLlWKARDGDACGaaymPIGTPLGNRSGYVLD-GQLNPLPVGVAGELY 4897
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 510 VKGPNVFKGYLKDEDRTKEALDSD------GWLH-TGDIGKWLPEGTLKIIDRKKHI-----FKLAQGEYVAPEKiENIY 577
Cdd:PRK12316 4898 LGGEGVARGYLERPALTAERFVPDpfgapgGRLYrTGDLARYRADGVIDYLGRVDHQvkirgFRIELGEIEARLR-EHPA 4976
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937369599 578 IRSEPVaqIYVHGdSLKAFLVGIVVP-DPEVMPCWAQKKGIEGNYQELckskeLKKAILDDMV 639
Cdd:PRK12316 4977 VREAVV--IAQEG-AVGKQLVGYVVPqDPALADADEAQAELRDELKAA-----LRERLPEYMV 5031
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
271-636 |
3.06e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 66.19 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 271 SIVCFTSGTTGNPKG--------AMLTHGN-VVADFSGFLKVTESqwaptcaDVHFSYLPLAHMFERMVQSVVYCHGGRV 341
Cdd:PRK13390 151 AVMLYSSGTTGFPKGiqpdlpgrDVDAPGDpIVAIARAFYDISES-------DIYYSSAPIYHAAPLRWCSMVHALGGTV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 342 GFFQG-DIRLLSDDMKALRPTIFPVVPRLLNRMYdkifhqadtslkrwllefaakRKQAEVRSGiirnnsiWDelffnki 420
Cdd:PRK13390 224 VLAKRfDAQATLGHVERYRITVTQMVPTMFVRLL---------------------KLDADVRTR-------YD------- 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 421 QASLgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVG-APLPCNHIKLVDAEEL 497
Cdd:PRK13390 269 VSSL----RAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGrSVLGDLHICDDDGNEL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 498 nywtSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDG--WLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIE 574
Cdd:PRK13390 344 ----PAGRiGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQETE 418
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937369599 575 NIYIRSEPVAQIYVHGdslkaflvgivVPDPEVmpcWAQKKGIEGNYQELCKSKELKKAILD 636
Cdd:PRK13390 419 NALTMHPAVHDVAVIG-----------VPDPEM---GEQVKAVIQLVEGIRGSDELARELID 466
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
121-609 |
3.33e-11 |
|
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: 65.74 E-value: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGSGLLqhDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGS-IRYIINTADictvi 199
Cdd:cd17652 13 LTYAELNARANRLARLLA--ARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPL-DPAYPAErIAYMLADAR----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 200 vdkphkAILLLEHverketpglklvilmepfddalrergkkcgvdiksmqaiedsgqenhrvpvpprPDDLSIVCFTSGT 279
Cdd:cd17652 85 ------PALLLTT------------------------------------------------------PDNLAYVIYTSGS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 280 TGNPKGAMLTH---GNVVADFSGFLKVTE----SQWAPTCADVHFSYLPLAhmfermvqsvvYCHGGRVGFFQGDIRL-- 350
Cdd:cd17652 105 TGRPKGVVVTHrglANLAAAQIAAFDVGPgsrvLQFASPSFDASVWELLMA-----------LLAGATLVLAPAEELLpg 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 351 --LSDDMKALRPTIFPVVPRLLNRMYDkifhqadtslkrwllefaakrkqaevrsgiirnnsiwDELffnkiqasLGGHV 428
Cdd:cd17652 174 epLADLLREHRITHVTLPPAALAALPP-------------------------------------DDL--------PDLRT 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 429 rMIVTGAAPASPTVLgflRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLVDAeELNYWTSKGEGE 507
Cdd:cd17652 209 -LVVAGEACPAELVD---RWAPGRRMINAYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYVLDA-RLRPVPPGVPGE 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 508 ICVKGPNVFKGYLKDEDRTKEALDSD------GWLH-TGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRS 580
Cdd:cd17652 284 LYIAGAGLARGYLNRPGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKI-RGFRIELGEVEAALTEH 362
|
490 500 510
....*....|....*....|....*....|..
gi 1937369599 581 EPVAQ--IYVHGDSL-KAFLVGIVVPDPEVMP 609
Cdd:cd17652 363 PGVAEavVVVRDDRPgDKRLVAYVVPAPGAAP 394
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
121-606 |
3.53e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 66.08 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGSGLLQHDCKVGteQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREG--DVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 201 dkpHKAILLLEHVERKETP-GLKLVILM-------EPFDDALrergkkcgvdiksmqaiedSGQENHRVPVPPRPDDLSi 272
Cdd:PRK08276 90 ---SAALADTAAELAAELPaGVPLLLVVagpvpgfRSYEEAL-------------------AAQPDTPIADETAGADML- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 273 vcFTSGTTGNPKGAM--LTHGNVVADFSGFLKVTeSQWAPTCAD-VHFSYLPLAH----MFERMVQSvvycHGGRV---- 341
Cdd:PRK08276 147 --YSSGTTGRPKGIKrpLPGLDPDEAPGMMLALL-GFGMYGGPDsVYLSPAPLYHtaplRFGMSALA----LGGTVvvme 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 342 GFfqgdirllsDDMKAL------RPTIFPVVPRLLNRMydkifhqadtsLKrwLLEfaakrkqaEVRSGiirnnsiWDel 415
Cdd:PRK08276 220 KF---------DAEEALalieryRVTHSQLVPTMFVRM-----------LK--LPE--------EVRAR-------YD-- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 416 ffnkiQASLgghvRMIVTGAAPASPTVLgflRAAL---GCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCN-HI 489
Cdd:PRK08276 261 -----VSSL----RVAIHAAAPCPVEVK---RAMIdwwGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGEvRI 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 490 KLVDAEELnywtSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGkWLPE-GTLKIIDRKKHIFkLAQGEY 567
Cdd:PRK08276 328 LDEDGNEL----PPGEiGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVG-YLDEdGYLYLTDRKSDMI-ISGGVN 401
|
490 500 510
....*....|....*....|....*....|....*....
gi 1937369599 568 VAPEKIENIYIRSEPVAQIYVHGdslkaflvgivVPDPE 606
Cdd:PRK08276 402 IYPQEIENLLVTHPKVADVAVFG-----------VPDEE 429
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
109-607 |
4.62e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 65.82 E-value: 4.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 109 LGFRKPEQPYQWLSY-QEVAKRAEFLgSGLLQHDCKVgteqFIGVFAQNRPEWII----AELACYTysmvVVPLYDTLGP 183
Cdd:PRK13388 18 IAVRYGDRTWTWREVlAEAAARAAAL-IALADPDRPL----HVGVLLGNTPEMLFwlaaAALGGYV----LVGLNTTRRG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 184 GSIRYIINTADICTVIVDKPHKAilLLEHVErkeTPGLKLVILMEPfddALRERgkkcgvdiksmqaIEDSGQEN-HRvp 262
Cdd:PRK13388 89 AALAADIRRADCQLLVTDAEHRP--LLDGLD---LPGVRVLDVDTP---AYAEL-------------VAAAGALTpHR-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 263 vPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVteSQWAPTCADVHFSYLPLAHMFERMVQ-SVVYCHGGRV 341
Cdd:PRK13388 146 -EVDAMDPFMLIFTSGTTGAPKAVRCSHGRLA--FAGRALT--ERFGLTRDDVCYVSMPLFHSNAVMAGwAPAVASGAAV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 342 gffqgdirllsddmkALRPTifpvvprllnrmydkifhqadtslkrwlleFAAKRKQAEVRSgiirnnsiWDELFFNKIQ 421
Cdd:PRK13388 221 ---------------ALPAK------------------------------FSASGFLDDVRR--------YGATYFNYVG 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 422 ASLGghvRMIVTGAAP---ASPTVLGFLRAA-----------LGCQVYEGYGQTEctAGCTFTTPGDWTSGHVGAPLP-- 485
Cdd:PRK13388 248 KPLA---YILATPERPddaDNPLRVAFGNEAsprdiaefsrrFGCQVEDGYGSSE--GAVIVVREPGTPPGSIGRGAPgv 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 486 ----------C------NHIKLVDAEElnywtskGEGEICVK-GPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEG 548
Cdd:PRK13388 323 aiynpetlteCavarfdAHGALLNADE-------AIGELVNTaGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRDADG 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1937369599 549 TLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYVHGdslkaflvgivVPDPEV 607
Cdd:PRK13388 395 WIYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYA-----------VPDERV 441
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
86-606 |
5.26e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 66.52 E-value: 5.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 86 YDDARTMYQVFRRGLSISGNGPCLGFRKpeqpyQWLSYQEVAKRAEFLGSGLLQhdCKVGTEQFIGVFAQNRPEWIIAEL 165
Cdd:PRK12316 507 YPLQRGVHRLFEEQVERTPEAPALAFGE-----ETLDYAELNRRANRLAHALIE--RGVGPDVLVGVAMERSIEMVVALL 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 166 ACYTYSMVVVPLYDTLGPGSIRYIINTADIctvivdkphkAILLLEHVERKETP---GLKLVILMEPfddalrergkkcg 242
Cdd:PRK12316 580 AILKAGGAYVPLDPEYPAERLAYMLEDSGV----------QLLLSQSHLGRKLPlaaGVQVLDLDRP------------- 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 243 vdiksmqAIEDSGQENHRVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKV-------TESQWAPTCADV 315
Cdd:PRK12316 637 -------AAWLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAyglgvgdTVLQKTPFSFDV 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 316 HFS--YLPLAhmfermvqsvvycHGGR-VGFFQGDIRllsdDMKALrptifpvvPRLLNRmydkifHQADTslkrwlLEF 392
Cdd:PRK12316 710 SVWefFWPLM-------------SGARlVVAAPGDHR----DPAKL--------VELINR------EGVDT------LHF 752
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 393 AAKRKQAEVRSGIIrnnsiwdelffnkiqASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP 472
Cdd:PRK12316 753 VPSMLQAFLQDEDV---------------ASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTC 817
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 473 GDWTSGHV--GAPLPCNHIKLVDAeELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEAL------DSDGWLHTGDIGKW 544
Cdd:PRK12316 818 VEEGGDSVpiGRPIANLACYILDA-NLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFvpspfvAGERMYRTGDLARY 896
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937369599 545 LPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAfLVGIVVPDPE 606
Cdd:PRK12316 897 RADGVIEYAGRIDHQVKL-RGLRIELGEIEARLLEHPWVREAAVLAVDGKQ-LVGYVVLESE 956
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
121-607 |
6.57e-11 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 65.41 E-value: 6.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:PRK05857 42 LRYRELVAEVGGLAADLRAQSVSRGSR--VLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 201 DKPHKailllehVERKETPGLKLVILMEPFDDALRERGKKCGVDIKSMQAIEDSGQenhrvpvpprpDDLSIVCFTSGTT 280
Cdd:PRK05857 120 APGSK-------MASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNADQGS-----------EDPLAMIFTSGTT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 281 GNPKGAMLTHGNVVAdFSGFLKVTESQWAPTCA-DVHFSYLPLAHMfeRMVQSVVYC--HGGR--VGFFQGD--IRLLSD 353
Cdd:PRK05857 182 GEPKAVLLANRTFFA-VPDILQKEGLNWVTWVVgETTYSPLPATHI--GGLWWILTClmHGGLcvTGGENTTslLEILTT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 354 DMKALRPtifpVVPRLLNRMYDKIfhqadtslkrwllefaakrkqaevrsgiirnnsiwdelffnKIQASLGGHVRMIVT 433
Cdd:PRK05857 259 NAVATTC----LVPTLLSKLVSEL-----------------------------------------KSANATVPSLRLVGY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 434 GAAPASPTVLGFLRAA--LGCQVYeGYGQTECTAGCTFTTPGDWT---SGHVGAPLPCNHIKLVDAEELNYWTSKGE--- 505
Cdd:PRK05857 294 GGSRAIAADVRFIEATgvRTAQVY-GLSETGCTALCLPTDDGSIVkieAGAVGRPYPGVDVYLAATDGIGPTAPGAGpsa 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 506 --GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIyirSEPV 583
Cdd:PRK05857 373 sfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGGVNIAPDEVDRI---AEGV 447
|
490 500 510
....*....|....*....|....*....|
gi 1937369599 584 AQI-----YVHGDSLKAFLVGI-VVPDPEV 607
Cdd:PRK05857 448 SGVreaacYEIPDEEFGALVGLaVVASAEL 477
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
429-607 |
7.75e-11 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 65.10 E-value: 7.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 429 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCNHIKLVDAE--ELnywtSKG 504
Cdd:PRK12406 274 RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE-SGAVTFATSEDALShpGTVGKAAPGAELRFVDEDgrPL----PQG 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 505 E-GEICVKGPNV--FKGYLKDEDRTkeALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSE 581
Cdd:PRK12406 349 EiGEIYSRIAGNpdFTYHNKPEKRA--EIDRGGFITSGDVGYLDADGYLFLCDRKRDMV-ISGGVNIYPAEIEAVLHAVP 425
|
170 180
....*....|....*....|....*....
gi 1937369599 582 PVAQIYVHGDSLKAF---LVGIVVPDPEV 607
Cdd:PRK12406 426 GVHDCAVFGIPDAEFgeaLMAVVEPQPGA 454
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
121-635 |
8.41e-11 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 64.92 E-value: 8.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGSGLLQHDCKVGTEQFIgvFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADiCTVIV 200
Cdd:PRK04319 74 YTYKELKELSNKFANVLKELGVEKGDRVFI--FMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSE-AKVLI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 201 DKPhkaiLLLEHVERKETPGLKLVILMepfdDALRERGKKCgVDIKSMQAiedsgQENHRVPVPP-RPDDLSIVCFTSGT 279
Cdd:PRK04319 151 TTP----ALLERKPADDLPSLKHVLLV----GEDVEEGPGT-LDFNALME-----QASDEFDIEWtDREDGAILHYTSGS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 280 TGNPKGAMLTHGNVVADF-SGF----LKVTESQWaptC-ADVHF----SY---LPLAHmferMVQSVVYchGGRvgfFQG 346
Cdd:PRK04319 217 TGKPKGVLHVHNAMLQHYqTGKyvldLHEDDVYW---CtADPGWvtgtSYgifAPWLN----GATNVID--GGR---FSP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 347 D--IRLLSDdmkaLRPTIF---PVVPRLLNRMYDKIFHQADTSlkrwllefaakrkqaevrsgiirnnsiwdelffnkiq 421
Cdd:PRK04319 285 ErwYRILED----YKVTVWytaPTAIRMLMGAGDDLVKKYDLS------------------------------------- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 422 aslggHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPCNHIKLVDAEElNYW 500
Cdd:PRK04319 324 -----SLRHILSVGEPLNPEVVRWGMKVFGLPIHDNWWMTETGGIMIANYPAmDIKPGSMGKPLPGIEAAIVDDQG-NEL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 501 TSKGEGEICVKG--PNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYI 578
Cdd:PRK04319 398 PPNRMGNLAIKKgwPSMMRGIWNNPEKYESYF-AGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTS-GERVGPFEVESKLM 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937369599 579 RSEPVAQIYVhgdslkaflvgIVVPDP---EVMPCW-AQKKGIEGnyqelckSKELKKAIL 635
Cdd:PRK04319 476 EHPAVAEAGV-----------IGKPDPvrgEIIKAFvALRPGYEP-------SEELKEEIR 518
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
264-598 |
1.06e-10 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 64.87 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 264 PPRPDDLSIVC-FTSGTTGNPKGAMLTH-GNVVADFSGFLKvtesqWAPTCADVHFSYLPLAHmfermvqsvvyCHGGrv 341
Cdd:PLN02479 190 PPADEWQSIALgYTSGTTASPKGVVLHHrGAYLMALSNALI-----WGMNEGAVYLWTLPMFH-----------CNGW-- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 342 gFFQGDIRLLSDDMKALRPTIFPVVprllnrmYDKIFHQADTslkrwllEFAAkrkqAEVRSGIIRNNSIWDELFfnkiq 421
Cdd:PLN02479 252 -CFTWTLAALCGTNICLRQVTAKAI-------YSAIANYGVT-------HFCA----APVVLNTIVNAPKSETIL----- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 422 aSLGGHVRMIVTGAAPaSPTVLgFLRAALGCQVYEGYGQTEcTAG----CTFTTPGDWTSGHVGAPLPCNH-IKLVDAEE 496
Cdd:PLN02479 308 -PLPRVVHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSE-TYGpstvCAWKPEWDSLPPEEQARLNARQgVRYIGLEG 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 497 LNYWTSKGE----------GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGE 566
Cdd:PLN02479 384 LDVVDTKTMkpvpadgktmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGGE 461
|
330 340 350
....*....|....*....|....*....|..
gi 1937369599 567 YVAPEKIENIyirsepvaqIYVHGDSLKAFLV 598
Cdd:PLN02479 462 NISSLEVENV---------VYTHPAVLEASVV 484
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
435-606 |
1.14e-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: 64.32 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 435 AAPASPTVLGFLRAALGCQVYEGYGQTECTaGCTFTTPGDWTS--GHVGAPLPCN-HIKLVDAEELnywtSKGE-GEICV 510
Cdd:cd05929 253 AAPCPPWVKEQWIDWGGPIIWEYYGGTEGQ-GLTIINGEEWLThpGSVGRAVLGKvHILDEDGNEV----PPGEiGEVYF 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 511 KGPNVFKgYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRsepvaqiyvHG 590
Cdd:cd05929 328 ANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIA---------HP 396
|
170
....*....|....*.
gi 1937369599 591 DSLKAFLVGivVPDPE 606
Cdd:cd05929 397 KVLDAAVVG--VPDEE 410
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
119-613 |
1.23e-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: 64.31 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 119 QWLSYQEVAKRAEFLGSGLLQHdcKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIIntadictv 198
Cdd:cd17649 11 QSLSYAELDARANRLAHRLRAL--GVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 199 ivdkphkailllehverketpglklvilmepfddalrergkkcgvdiksmqaiEDSGqenHRVPVPPRPDDLSIVCFTSG 278
Cdd:cd17649 81 -----------------------------------------------------EDSG---AGLLLTHHPRQLAYVIYTSG 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 279 TTGNPKGAMLTHGNVVAdfsgFLKVTESQWAPTCADV--HFSYLPLAHMFERMVQSVVycHGGRVgffqgdirllsddmk 356
Cdd:cd17649 105 STGTPKGVAVSHGPLAA----HCQATAERYGLTPGDRelQFASFNFDGAHEQLLPPLI--CGACV--------------- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 357 ALRPTIFPVVPRLLNRMYDK----IFHQADTSLKRWLLEFAAKrkqaevrsgiirnnsiwdelffnkiQASLGGHVRMIV 432
Cdd:cd17649 164 VLRPDELWASADELAEMVRElgvtVLDLPPAYLQQLAEEADRT-------------------------GDGRPPSLRLYI 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 433 TGAAPASPTvlgFLRAALGCQVY--EGYGQTECTAGCT-FTTPGD----WTSGHVGAPLPCNHIKLVDAeELNYWTSKGE 505
Cdd:cd17649 219 FGGEALSPE---LLRRWLKAPVRlfNAYGPTEATVTPLvWKCEAGaaraGASMPIGRPLGGRSAYILDA-DLNPVPVGVT 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 506 GEICVKGPNVFKGYLKDEDRTKEAL--DSDG-----WLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYI 578
Cdd:cd17649 295 GELYIGGEGLARGYLGRPELTAERFvpDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-RGFRIELGEIEAALL 373
|
490 500 510
....*....|....*....|....*....|....*....
gi 1937369599 579 RSEPVAQIYV---HGDSLKAfLVGIVVP-DPEVMPCWAQ 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 |
2.70e-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: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSG--FLKVTESQwaptcADVHFSYLPLAHMFERMVQSVVYCHGGRV 341
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVnlrTSLSEryFGRDNGDE-----AVLFFSNYVFDFFVEQMTLALLNGQKLVV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 342 --GFFQGDIRLLSDDMKALRPTIFPVVPRLLnRMYDkiFHQAdTSLKRWLL---EFAAKRkqaevrsgiirnnsiwdelf 416
Cdd:cd17648 168 ppDEMRFDPDRFYAYINREKVTYLSGTPSVL-QQYD--LARL-PHLKRVDAageEFTAPV-------------------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 417 FNKIQASLGGhvrmivtgaapasptvlgflraalgcQVYEGYGQTEC--TAGCTFTTPGDWTSGHVGAPLPCNHIKLVDA 494
Cdd:cd17648 224 FEKLRSRFAG--------------------------LIINAYGPTETtvTNHKRFFPGDQRFDKSLGRPVRNTKCYVLND 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 495 EeLNYWTSKGEGEICVKGPNVFKGYLKDEDRTKE-------------ALDSDGWLH-TGDIGKWLPEGTLKIIDRKKHIF 560
Cdd:cd17648 278 A-MKRVPVGAVGELYLGGDGVARGYLNRPELTAErflpnpfqteqerARGRNARLYkTGDLVRWLPSGELEYLGRNDFQV 356
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1937369599 561 KLaQGEYVAPEKIENIY-----IRSEPVAQIYVHGDSLKA---FLVGIVVPDPEVMP 609
Cdd:cd17648 357 KI-RGQRIEPGEVEAALasypgVRECAVVAKEDASQAQSRiqkYLVGYYLPEPGHVP 412
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
121-557 |
3.10e-10 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 63.10 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGS-------IRYIINTA 193
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALGLKPGDR--VALIAETDGDFVEAFFACQYAGLVPVPLPLPMGFGGresyiaqLRGMLASA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 194 DICTVIVDKphkaiLLLEHVErKETPGLKLVILMEPFDDALRERGkkcGVDIKsmqaiedsgqenhrvpvPPRPDDLSIV 273
Cdd:PRK09192 128 QPAAIITPD-----ELLPWVN-EATHGNPLLHVLSHAWFKALPEA---DVALP-----------------RPTPDDIAYL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 274 CFTSGTTGNPKGAMLTHGNVVADFSGF----LKVTEsqwaptcADVHFSYLPLAH-MfermvqsvvychgGRVGFF---- 344
Cdd:PRK09192 182 QYSSGSTRFPRGVIITHRALMANLRAIshdgLKVRP-------GDRCVSWLPFYHdM-------------GLVGFLltpv 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 345 --QgdirlLSDDMkaLRPTIFPVVP----RLLNR-----MYDKIFHqadtslkrwlLEFAAKRkqAEVRSGIIRNNSIWd 413
Cdd:PRK09192 242 atQ-----LSVDY--LPTRDFARRPlqwlDLISRnrgtiSYSPPFG----------YELCARR--VNSKDLAELDLSCW- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 414 elffnkiqaslgghvRMIVTGAAPASPTVL----------GF-LRAALGCqvyegYGQTECTAGCTFTTPG--------- 473
Cdd:PRK09192 302 ---------------RVAGIGADMIRPDVLhqfaeafapaGFdDKAFMPS-----YGLAEATLAVSFSPLGsgivveevd 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 474 -DWTSGH------------------VGAPLPCNHIKLVDA--EELNywtSKGEGEICVKGPNVFKGYLKDEDRTKeALDS 532
Cdd:PRK09192 362 rDRLEYQgkavapgaetrrvrtfvnCGKALPGHEIEIRNEagMPLP---ERVVGHICVRGPSLMSGYFRDEESQD-VLAA 437
|
490 500
....*....|....*....|....*
gi 1937369599 533 DGWLHTGDIGkWLPEGTLKIIDRKK 557
Cdd:PRK09192 438 DGWLDTGDLG-YLLDGYLYITGRAK 461
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
267-609 |
5.23e-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: 5.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVTESQWAPTCADVHFSYLPLAhmFERMVQSVV--YCHGGRVGFF 344
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLV----NLCEWHRPYFGVTPADKSLVYASFS--FDASAWEIFphLTAGAALHVV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 345 QGDIRLlsdDMKALrptifpvvprllnrmyDKIFHQADTSLKRWLLEFAAKRKQAEvrsgiirNNSIwdelffnkiqasl 424
Cdd:cd17645 177 PSERRL---DLDAL----------------NDYFNQEGITISFLPTGAAEQFMQLD-------NQSL------------- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 425 gghvRMIVTGAapaspTVLGFLRAAlGCQVYEGYGQTECTAGCT-FTTPGDWTSGHVGAPLPCNHIKLVDaEELNYWTSK 503
Cdd:cd17645 218 ----RVLLTGG-----DKLKKIERK-GYKLVNNYGPTENTVVATsFEIDKPYANIPIGKPIDNTRVYILD-EALQLQPIG 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 504 GEGEICVKGPNVFKGYLKDEDRTKEALDSDGWL------HTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIY 577
Cdd:cd17645 287 VAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIEPFL 365
|
330 340 350
....*....|....*....|....*....|....*
gi 1937369599 578 IRSEPV---AQIYVHGDSLKAFLVGIVVPDPEVMP 609
Cdd:cd17645 366 MNHPLIelaAVLAKEDADGRKYLVAYVTAPEEIPH 400
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
267-609 |
9.39e-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: 61.30 E-value: 9.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKV---TES----QWAPTCADVHFSYLplahmfermvqSVVYCHGG 339
Cdd:cd17644 105 PENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEygiTSSdrvlQFASIAFDVAAEEI-----------YVTLLSGA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 340 RVgffqgdirllsddmkALRPT-IFPVVPRllnrMYDKIfhqadtslkrwllefaaKRKQAEVRSgiiRNNSIWDELFFN 418
Cdd:cd17644 174 TL---------------VLRPEeMRSSLED----FVQYI-----------------QQWQLTVLS---LPPAYWHLLVLE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 419 KIQASLGG--HVRMIVTGAAPASPTVLGFLRAALG--CQVYEGYGQTECTAGCTFTTPGDWTSGH-----VGAPLPCNHI 489
Cdd:cd17644 215 LLLSTIDLpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIANTQV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 490 KLVDaEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLH--------TGDIGKWLPEGTLKIIDRKKHIFK 561
Cdd:cd17644 295 YILD-ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVK 373
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1937369599 562 LaQGEYVAPEKIENIYIRSEPVAQ--IYVHGDSL-KAFLVGIVVPDPEVMP 609
Cdd:cd17644 374 I-RGFRIELGEIEAVLSQHNDVKTavVIVREDQPgNKRLVAYIVPHYEESP 423
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
268-598 |
1.13e-08 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 58.50 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 268 DDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF----LKVTESQWAPTCADVHFSY-------LPLAHMFERMVQSVVYc 336
Cdd:PRK06060 145 DALAYATYTSGTTGPPKAAIHRHADPLTFVDAMcrkaLRLTPEDTGLCSARMYFAYglgnsvwFPLATGGSAVINSAPV- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 337 hGGRVGffqgdiRLLSddmKALRPTIFPVVPRLLNRMYDKIfhQADTslkrwllefaakrkqaeVRSgiirnnsiwdelf 416
Cdd:PRK06060 224 -TPEAA------AILS---ARFGPSVLYGVPNFFARVIDSC--SPDS-----------------FRS------------- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 417 fnkiqaslgghVRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTEctAGCTFT--TPGDWTSGHVGAPLPCNHIKLVd 493
Cdd:PRK06060 262 -----------LRCVVSAGEALELGLAERLMEFFGgIPILDGIGSTE--VGQTFVsnRVDEWRLGTLGRVLPPYEIRVV- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 494 AEELNYWTSKGEGEICVKGPNVFKGYLkdeDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIfKLAQGEYVAPEKI 573
Cdd:PRK06060 328 APDGTTAGPGVEGDLWVRGPAIAKGYW---NRPDSPVANEGWLDTRDRVCIDSDGWVTYRCRADDT-EVIGGVNVDPREV 403
|
330 340 350
....*....|....*....|....*....|..
gi 1937369599 574 ENIYIRSEPVAQIYVHG-------DSLKAFLV 598
Cdd:PRK06060 404 ERLIIEDEAVAEAAVVAvrestgaSTLQAFLV 435
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
275-590 |
1.36e-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: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 275 FTSGTTGNPKGAMLTHGNVVADFsgflKVTESQWAPTCADVHFSYLPLAH-MFERMVQSVVYCHGGRVGFFQGDIRLLSD 353
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESF----VCNEDLFNISGEDAILAPGPLSHsLFLYGAISALYLGGTFIGQRKFNPKSWIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 354 DMKALRPTIFPVVPRLLnrmydkifhqadtslkrwllefaakrkQAEVRSGIIRNnsiwdelffnkiqaslggHVRMIVT 433
Cdd:cd17633 83 KINQYNATVIYLVPTML---------------------------QALARTLEPES------------------KIKSIFS 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 434 GAAPASPTVLGFLRAAL-GCQVYEGYGQTEcTAGCTFTTPGD-WTSGHVGAPLPCNHIKLVDAEelnywtSKGEGEICVK 511
Cdd:cd17633 118 SGQKLFESTKKKLKNIFpKANLIEFYGTSE-LSFITYNFNQEsRPPNSVGRPFPNVEIEIRNAD------GGEIGKIFVK 190
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937369599 512 GPNVFKGYLKDEDRTKealdsDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYVHG 590
Cdd:cd17633 191 SEMVFSGYVRGGFSNP-----DGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIEEAIVVG 263
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
254-609 |
2.26e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 56.59 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 254 SGQENHRVPVPPRP------------------DDLSIVCFTSGTTGNPKGAMLTHGNVVA------DFSGflkvTESQWA 309
Cdd:PRK07824 3 AGRAPALLPVPAQDerraallrdalrvgepidDDVALVVATSGTTGTPKGAMLTAAALTAsadathDRLG----GPGQWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 310 PTcadvhfsyLPLAHM--FERMVQSVVychGGRV--------GFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKifh 379
Cdd:PRK07824 79 LA--------LPAHHIagLQVLVRSVI---AGSEpveldvsaGFDPTALPRAVAELGGGRRYTSLVPMQLAKALDDP--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 380 QADTSLKrwllEFAAkrkqaevrsgiirnnsiwdelffnkiqaslgghvrmIVTGAAPASPTVlgfLRAA--LGCQVYEG 457
Cdd:PRK07824 145 AATAALA----ELDA------------------------------------VLVGGGPAPAPV---LDAAaaAGINVVRT 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 458 YGQTECTAGCTFTtpgdwtsghvGAPLPCNHIKLVDaeelnywtskgeGEICVKGPNVFKGYLKDEDrtKEALDSDGWLH 537
Cdd:PRK07824 182 YGMSETSGGCVYD----------GVPLDGVRVRVED------------GRIALGGPTLAKGYRNPVD--PDPFAEPGWFR 237
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937369599 538 TGDIGKwLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQIYVHG---DSLKAFLVGIVVPDPEVMP 609
Cdd:PRK07824 238 TDDLGA-LDDGVLTVLGRADDAISTG-GLTVLPQVVEAALATHPAVADCAVFGlpdDRLGQRVVAAVVGDGGPAP 310
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
422-606 |
3.48e-08 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 56.37 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 422 ASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEC-TAGCTFTTPGDWT-SGHVGAPLPCNHIKLVDaEELNy 499
Cdd:cd05973 201 ARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELgMVLANHHALEHPVhAGSAGRAMPGWRVAVLD-DDGD- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 500 wtSKGEGEICVKGPNV-------FKGYLKDEDRTKealdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEK 572
Cdd:cd05973 279 --ELGPGEPGRLAIDIansplmwFRGYQLPDTPAI----DGGYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFD 351
|
170 180 190
....*....|....*....|....*....|....
gi 1937369599 573 IENIYIRSEPVAQIYVhgdslkaflvgIVVPDPE 606
Cdd:cd05973 352 VESALIEHPAVAEAAV-----------IGVPDPE 374
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
255-576 |
4.51e-08 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 56.31 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 255 GQENHRVPVPPRPD-DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAptcADVHFSYLPLAH-Mfermvqs 332
Cdd:PRK05851 138 AHTNRSASLTPPDSgGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAA---TDVGCSWLPLYHdM------- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 333 vvychggrvgffqGDIRLLSDDMKA----LRPT-IFPVVP-RLLNrmydkifhqadtslkrWLLEFAAKRKQA-EVRSGI 405
Cdd:PRK05851 208 -------------GLAFLLTAALAGaplwLAPTtAFSASPfRWLS----------------WLSDSRATLTAApNFAYNL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 406 IRNNSiwdelffNKIQASLGGHVRMIVTGAAP----------ASPTVLGFLRAALGcqvyEGYGQTECTAGCTFTTPG-- 473
Cdd:PRK05851 259 IGKYA-------RRVSDVDLGALRVALNGGEPvdcdgferfaTAMAPFGFDAGAAA----PSYGLAESTCAVTVPVPGig 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 474 ---------DWTSGH----VGAPLPCNHIKLVDAEELNYWTSKGEGEICVKGPNVFKGYLKDedrtkEALDSDGWLHTGD 540
Cdd:PRK05851 328 lrvdevttdDGSGARrhavLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQ-----APIDPDDWFPTGD 402
|
330 340 350
....*....|....*....|....*....|....*.
gi 1937369599 541 IGkWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENI 576
Cdd:PRK05851 403 LG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERV 436
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
268-592 |
6.46e-08 |
|
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: 55.56 E-value: 6.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 268 DDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVTESQwapTCADVHFSYLPLAHM-FERMVQSVV--YCHGGRvgff 344
Cdd:cd17656 128 DDLLYIIYTSGTTGKPKGVQLEHKNMV----NLLHFEREK---TNINFSDKVLQFATCsFDVCYQEIFstLLSGGT---- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 345 qgdIRLLSDDMKALRPTIFPVVPRllnrmydkifHQADT-SLKRWLLEFAAKRKQAEVRsgiirnnsiwdelFFNKIQAS 423
Cdd:cd17656 197 ---LYIIREETKRDVEQLFDLVKR----------HNIEVvFLPVAFLKFIFSEREFINR-------------FPTCVKHI 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 424 LGGHVRMIVTgaapaSPTVLGFLRAalGCQVYEGYG--QTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDaEELNYW 500
Cdd:cd17656 251 ITAGEQLVIT-----NEFKEMLHEH--NVHLHNHYGpsETHVVTTYTINPEAEIPElPPIGKPISNTWIYILD-QEQQLQ 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 501 TSKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGW------LHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIE 574
Cdd:cd17656 323 PQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-RGYRIELGEIE 401
|
330 340
....*....|....*....|
gi 1937369599 575 NIYIRSEPVAQ--IYVHGDS 592
Cdd:cd17656 402 AQLLNHPGVSEavVLDKADD 421
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
429-605 |
8.74e-08 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 55.38 E-value: 8.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 429 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctaGCTFTTPGDWTSGHV----GAPL-PCNHIKLVDAE--ELnywt 501
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAE---GLVNYTRLDDSDERIfttqGRPMsPDDEVWVADADgnPL---- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 502 SKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHifklaQ----GEYVAPEKIENI 576
Cdd:PRK10946 376 PQGEvGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGEKIAAEEIENL 450
|
170 180
....*....|....*....|....*....
gi 1937369599 577 YIRsepvaqiyvHGDSLKAFLVGIvvPDP 605
Cdd:PRK10946 451 LLR---------HPAVIHAALVSM--EDE 468
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
121-585 |
1.65e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.17 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAEFLGSGLlQHDCKVGtEQFIGVFAQNrPEWIIAELACYTYSMVVVPLYDtlgPGSIRyiintadictviv 200
Cdd:PRK05691 41 LSYRDLDLRARTIAAAL-QARASFG-DRAVLLFPSG-PDYVAAFFGCLYAGVIAVPAYP---PESAR------------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 201 dkPHKAILLLEHVERKETpglKLVILMEPFDDALRERGKKCGVDIKSMQAIE--DSGQENHRVPVPPRPDDLSIVCFTSG 278
Cdd:PRK05691 102 --RHHQERLLSIIADAEP---RLLLTVADLRDSLLQMEELAAANAPELLCVDtlDPALAEAWQEPALQPDDIAFLQYTSG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 279 TTGNPKGAMLTHGNVVADfsgflkvtesQWAPTCA--------DVHFSYLPLAH---MFERMVQSV---VYCHGGRVGFF 344
Cdd:PRK05691 177 STALPKGVQVSHGNLVAN----------EQLIRHGfgidlnpdDVIVSWLPLYHdmgLIGGLLQPIfsgVPCVLMSPAYF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 345 QG-DIRLLsDDMKALRPTI-----FPVvpRLLN-RMYDKIFHQADtsLKRWLLEFAAkrkqaevrSGIIRNNSIwdELFF 417
Cdd:PRK05691 247 LErPLRWL-EAISEYGGTIsggpdFAY--RLCSeRVSESALERLD--LSRWRVAYSG--------SEPIRQDSL--ERFA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 418 NKIQ----------ASLG-GHVRMIVTGAAPA-SPTVLGFLRAALGCQVYEGyGQTECTAGCTFTTPGdwtsghvgaplp 485
Cdd:PRK05691 312 EKFAacgfdpdsffASYGlAEATLFVSGGRRGqGIPALELDAEALARNRAEP-GTGSVLMSCGRSQPG------------ 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 486 cNHIKLVDAEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEA---LDSDGWLHTGDIGkWLPEGTLKIIDRKKHIFkL 562
Cdd:PRK05691 379 -HAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfveHDGRTWLRTGDLG-FLRDGELFVTGRLKDML-I 455
|
490 500
....*....|....*....|...
gi 1937369599 563 AQGEYVAPEKIENIYIRSEPVAQ 585
Cdd:PRK05691 456 VRGHNLYPQDIEKTVEREVEVVR 478
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
269-606 |
1.74e-07 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 54.28 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 269 DLSIVCFTSGTTGNPKGAMLTH-----GNVVADFSGFLKVTesqwaptcaDVHFSYLPLAHMFERMVQ-SVVYCHGGRVG 342
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHrrawrGGAFFAGSGGALPS---------DVLYTCLPLYHSTALIVGwSACLASGATLV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 343 F---FQGdiRLLSDDMKALRPTIFPVVPRLLnrmydkifhqadtslkRWLLefAAKRKQAEVRsgiirnnsiwdelffNK 419
Cdd:cd05940 153 IrkkFSA--SNFWDDIRKYQATIFQYIGELC----------------RYLL--NQPPKPTERK---------------HK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 420 IQASLGGHVRmivtgaapasPTVLGFLRAALGC-QVYEGYGQTECTAGCT--FTTPGdwTSGHVGAPLPCNH-IKLV--- 492
Cdd:cd05940 198 VRMIFGNGLR----------PDIWEEFKERFGVpRIAEFYAATEGNSGFInfFGKPG--AIGRNPSLLRKVApLALVkyd 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 493 --------DAEELNYWTSKGE-----GEICVKGPnvFKGYLKDEDRTKEAL-----DSDGWLHTGDIGKWLPEGTLKIID 554
Cdd:cd05940 266 lesgepirDAEGRCIKVPRGEpglliSRINPLEP--FDGYTDPAATEKKILrdvfkKGDAWFNTGDLMRLDGEGFWYFVD 343
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1937369599 555 RKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYVHGDSL-----KAFLVGIVVPDPE 606
Cdd:cd05940 344 RLGDTFRW-KGENVSTTEVAAVLGAFPGVEEANVYGVQVpgtdgRAGMAAIVLQPNE 399
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
429-613 |
4.15e-07 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 53.07 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 429 RMIVTGAAPASPTVLGF-----LRAALGcqvyegYGQTEcTAG--CTFTtPGDWTSG--HVGAPLPCNHIKLvdaeelny 499
Cdd:PRK07445 233 RTILLGGAPAWPSLLEQarqlqLRLAPT------YGMTE-TASqiATLK-PDDFLAGnnSSGQVLPHAQITI-------- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 500 wTSKGEGEICVKGPNVFKGYLkdedrtKEALDSDGWLHTGDIGKWLPEGTLKIIDR--KKHIfklAQGEYVAPEKIENIY 577
Cdd:PRK07445 297 -PANQTGNITIQAQSLALGYY------PQILDSQGIFETDDLGYLDAQGYLHILGRnsQKII---TGGENVYPAEVEAAI 366
|
170 180 190
....*....|....*....|....*....|....*.
gi 1937369599 578 IRSEPVAQIYVHGdslkaflvgivVPDPEvmpcWAQ 613
Cdd:PRK07445 367 LATGLVQDVCVLG-----------LPDPH----WGE 387
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
417-605 |
1.08e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 51.70 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 417 FNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPGDWTSGHVGAPLPCNHIKLVDAEE 496
Cdd:PRK07638 245 LYKENRVIENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSF-VTALVDEESERRPNSVGRPFHNVQVRICNE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 497 LNYWTSKGE-GEICVKGPNVFKGYLKDEDRTKEaLDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIEN 575
Cdd:PRK07638 324 AGEEVQKGEiGTVYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIES 401
|
170 180 190
....*....|....*....|....*....|
gi 1937369599 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 |
1.62e-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: 51.28 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAptcaDVHFSYLPLAH---MFERMVQSVVycHGGRVGF 343
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNG----DRTYTCMPLYHgtaAFLGACNCLM--SGGTLAL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 344 ---FQgdIRLLSDDMKALRPTIFPVVPRLLnrmydkifhqadtslkRWLLEFAAkrkqaevrsgiirnnSIWDELffNKI 420
Cdd:cd05937 160 srkFS--ASQFWKDVRDSGATIIQYVGELC----------------RYLLSTPP---------------SPYDRD--HKV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 421 QASLGGHVRmivtgaapasPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKL-------- 491
Cdd:cd05937 205 RVAWGNGLR----------PDIWERFRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKFenqvvlvk 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 492 VDAEELNYW--TSKG---------EGEICVKGPNV----FKGYLKDEDRTKEAL------DSDGWLHTGDIGKWLPEGTL 550
Cdd:cd05937 275 MDPETDDPIrdPKTGfcvrapvgePGEMLGRVPFKnreaFQGYLHNEDATESKLvrdvfrKGDIYFRTGDLLRQDADGRW 354
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1937369599 551 KIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYVHG 590
Cdd:cd05937 355 YFLDRLGDTFRW-KSENVSTTEVADVLGAHPDIAEANVYG 393
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
267-598 |
2.23e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 51.32 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 267 PDDLSIVCFTSGTTGNPKGAMLT-HGNVVADFSG--FLKVTE----SQWAPTCADVHFSYLPLAHMFermvqsvvychGG 339
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEqRGMLNNQLSKvpYLALSEadviAQTASQSFDISVWQFLAAPLF-----------GA 3936
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 340 RVGFFQGDI----RLLSDDMKALRPTIFPVVPRLLNRMYDKIfHQADTSLkRWllefaakrkqaevrsgiirnnsiwdel 415
Cdd:PRK05691 3937 RVEIVPNAIahdpQGLLAHVQAQGITVLESVPSLIQGMLAED-RQALDGL-RW--------------------------- 3987
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 416 ffnkiqaslgghvrMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF------TTPGDWTSghVGAPLPCNHI 489
Cdd:PRK05691 3988 --------------MLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFfrvdlaSTRGSYLP--IGSPTDNNRL 4051
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 490 KLVDaEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEAL-------DSDGWLHTGDIGKWLPEGTLKIIDRKKHI--- 559
Cdd:PRK05691 4052 YLLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFvphpfgaPGERLYRTGDLARRRSDGVLEYVGRIDHQvki 4130
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1937369599 560 --FKLAQGEYVApEKIENIYIRSEPVA-QIYVHGDSLKAFLV 598
Cdd:PRK05691 4131 rgYRIELGEIEA-RLHEQAEVREAAVAvQEGVNGKHLVGYLV 4171
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
483-550 |
5.77e-06 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 49.51 E-value: 5.77e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937369599 483 PLPCNHIK-----LVDAEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEAL-DSDGW--LHTGDIGKwLPEGTL 550
Cdd:PRK04813 317 RLPIGYAKpdsplLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGY-LEDGLL 391
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
264-607 |
6.48e-06 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 49.37 E-value: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 264 PPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEsqW---------APTCADVHFSYLPLAHMferMVQSVV 334
Cdd:PRK13382 192 EPTGRKGRVILLTSGTTGTPKGARRSGPGGIGTLKAILDRTP--WraeeptvivAPMFHAWGFSQLVLAAS---LACTIV 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 335 YchggRVGFFQGDIRLLSDdmkALRPTIFPVVPRLLNRMYDKIfhqadtslkrwllefaakrkqAEVRSgiirnnsiwde 414
Cdd:PRK13382 267 T----RRRFDPEATLDLID---RHRATGLAVVPVMFDRIMDLP---------------------AEVRN----------- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 415 lffnkiqASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFT-TPGDWTSG--HVGAPLPCNHIKL 491
Cdd:PRK13382 308 -------RYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATE--AGMIATaTPADLRAApdTAGRPAEGTEIRI 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 492 VDAE--ELnywtSKGE-GEICVKGPNVFKGYlkDEDRTKEAldSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYV 568
Cdd:PRK13382 379 LDQDfrEV----PTGEvGTIFVRNDTQFDGY--TSGSTKDF--HDGFMASGDVGYLDENGRLFVVGRDDEMI-VSGGENV 449
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1937369599 569 APEKIENIYIRSEPVAQIYV-------HGDSLKAFlvgiVVPDPEV 607
Cdd:PRK13382 450 YPIEVEKTLATHPDVAEAAVigvddeqYGQRLAAF----VVLKPGA 491
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
122-609 |
1.08e-05 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 48.73 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 122 SYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPgsiryiintADICTVIVD 201
Cdd:cd17634 86 SYRELHREVCRFAGTLLDLGVKKGDR--VAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAP---------EAVAGRIID 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 202 -KPHKAILLLEHVERKETPGLKLVIlmepfDDALRERG---------KKCGVDIKSMQA--------IEDSGQENHrvPV 263
Cdd:cd17634 155 sSSRLLITADGGVRAGRSVPLKKNV-----DDALNPNVtsvehvivlKRTGSDIDWQEGrdlwwrdlIAKASPEHQ--PE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 264 PPRPDDLSIVCFTSGTTGNPKGAMLTHGnvvadfsGF-LKVTESqwaptcadvhfsylpLAHMFERMVQSVVYChGGRVG 342
Cdd:cd17634 228 AMNAEDPLFILYTSGTTGKPKGVLHTTG-------GYlVYAATT---------------MKYVFDYGPGDIYWC-TADVG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 343 FFQGDIRLLSDDMkALRPTIF-----PVVPRlLNRMYDKIFHQADTSLkrWLLEFAAKRKQAEVRSGIIRNNsiwdelff 417
Cdd:cd17634 285 WVTGHSYLLYGPL-ACGATTLlyegvPNWPT-PARMWQVVDKHGVNIL--YTAPTAIRALMAAGDDAIEGTD-------- 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 418 nkiQASLgghvRMIVTGAAPASPTVLGFLRAALG---CQVYEGYGQTECTAGCTFTTPG--DWTSGHVGAPLPCNHIKLV 492
Cdd:cd17634 353 ---RSSL----RILGSVGEPINPEAYEWYWKKIGkekCPVVDTWWQTETGGFMITPLPGaiELKAGSATRPVFGVQPAVV 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 493 DAEElNYWTSKGEGEICVKG--PNVFKGYLKDEDRTKEALDS--DGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYV 568
Cdd:cd17634 426 DNEG-HPQPGGTEGNLVITDpwPGQTRTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVA-GHRL 503
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1937369599 569 APEKIENIYIRSEPVAQIYVHG--DSLKA-FLVGIVVPDPEVMP 609
Cdd:cd17634 504 GTAEIESVLVAHPKVAEAAVVGipHAIKGqAPYAYVVLNHGVEP 547
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
121-324 |
1.81e-05 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 47.95 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 121 LSYQEVAKRAE-----FLGSGLLQHDCkvgteqfIGVFAQNRPEWIIAELACyTYSMVVVPLYDT-LGPGSIRYIINTAD 194
Cdd:PRK08279 63 ISYAELNARANryahwAAARGVGKGDV-------VALLMENRPEYLAAWLGL-AKLGAVVALLNTqQRGAVLAHSLNLVD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 195 ICTVIVDKPhkailLLEHVErkETPGLKLVILMEPFDDalRERGKKCGVDIKSMQAIEDSGQENHRVPVPPRPDDLSIVC 274
Cdd:PRK08279 135 AKHLIVGEE-----LVEAFE--EARADLARPPRLWVAG--GDTLDDPEGYEDLAAAAAGAPTTNPASRSGVTAKDTAFYI 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1937369599 275 FTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTESqwaptcaDVHFSYLPLAH 324
Cdd:PRK08279 206 YTSGTTGLPKAAVMSHMRWLkamGGFGGLLRLTPD-------DVLYCCLPLYH 251
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
265-614 |
1.88e-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: 47.38 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 265 PRPDDLSIVCfTSGTTGNPKGAMLTHGNV-VADFSGFLKVTESQWAPTCAD---------VHFSYLPLAH-------MFE 327
Cdd:cd05924 1 RSADDLYILY-TGGTTGMPKGVMWRQEDIfRMLMGGADFGTGEFTPSEDAHkaaaaaagtVMFPAPPLMHgtgswtaFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 328 RMVQSVVYCHGGRvgfFQGD--IRLLSDDmkalRPTIFPVVprllnrmydkifhqADtSLKRWLLEfaakrkqaEVRSGI 405
Cdd:cd05924 80 LLGGQTVVLPDDR---FDPEevWRTIEKH----KVTSMTIV--------------GD-AMARPLID--------ALRDAG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 406 IRNNSiwdelffnkiqaSLgghvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFTTPGdwtSGHVGAPL 484
Cdd:cd05924 130 PYDLS------------SL----FAISSGGALLSPEVKqGLLELVPNITLVDAFGSSETGFTGSGHSAG---SGPETGPF 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 485 -PCNHIKLVDAEELNYWT--SKGEGEICVKGpNVFKGYLKDEDRTKEA---LDSDGWLHTGDIGKWLPEGTLKIIDRKKH 558
Cdd:cd05924 191 tRANPDTVVLDDDGRVVPpgSGGVGWIARRG-HIPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGRGSV 269
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937369599 559 IFKLAqGEYVAPEKIEniyirsepvAQIYVHGDSLKAFLVGivVPDPEvmpcWAQK 614
Cdd:cd05924 270 CINTG-GEKVFPEEVE---------EALKSHPAVYDVLVVG--RPDER----WGQE 309
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
418-643 |
5.57e-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: 46.27 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 418 NKIQASLGGHVRMIVTGAAPASPTV----LGFLRA--ALGCQVYEGYGqTECTAGCTFTTPGDWTSGHVGAPLPCNHI-K 490
Cdd:cd05915 263 ESTGHRLKTLRRLVVGGSAAPRSLIarfeRMGVEVrqGYGLTETSPVV-VQNFVKSHLESLSEEEKLTLKAKTGLPIPlV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 491 LVDAEELNYWTSKGEGE----ICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGE 566
Cdd:cd05915 342 RLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG-GE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 567 YVAPEKIENIyirsepvaqIYVHGDSLKAFLVGivVPDP---EVMPCWAQKKGIEGNYQELCkskELKKAILDDMVMLGK 643
Cdd:cd05915 421 WISSVDLENA---------LMGHPKVKEAAVVA--IPHPkwqERPLAVVVPRGEKPTPEELN---EHLLKAGFAKWQLPD 486
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
233-325 |
6.30e-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: 46.13 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 233 ALRERGKKCGV--------DIKSMQAiEDSGQENHRVP----VPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVAdFSGF 300
Cdd:cd05938 98 ALRADGVSVWYlshtsnteGVISLLD-KVDAASDEPVPaslrAHVTIKSPALYIYTSGTTGLPKAARISHLRVLQ-CSGF 175
|
90 100
....*....|....*....|....*
gi 1937369599 301 LKVTesqwAPTCADVHFSYLPLAHM 325
Cdd:cd05938 176 LSLC----GVTADDVIYITLPLYHS 196
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
268-599 |
3.06e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.39 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 268 DDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgfLKVTESQWAPTCADVHFSYLPLAhmFErmvQSVVYCH-----GGRVG 342
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNTHAALAER----LQWMQATYALDDSDVLMQKAPIS--FD---VSVWECFwplitGCRLV 1343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 343 FF----QGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTSLKRWlleFAAkrkqAEVRSGIIRNNsiwdelffn 418
Cdd:PRK05691 1344 LAgpgeHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRL---FSG----GEALPAELRNR--------- 1407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 419 kiqaslgghvrmivtgaapasptVLGFLRAAlgcQVYEGYGQTECTAGCTF--TTPGDWTSGHVGAPLPCNHIKLVDAEe 496
Cdd:PRK05691 1408 -----------------------VLQRLPQV---QLHNRYGPTETAINVTHwqCQAEDGERSPIGRPLGNVLCRVLDAE- 1460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 497 LNYWTSKGEGEICVKGPNVFKGYLKDEDRTKE-----ALDSDG--WLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVA 569
Cdd:PRK05691 1461 LNLLPPGVAGELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL-RGFRVE 1539
|
330 340 350
....*....|....*....|....*....|..
gi 1937369599 570 PEKIENIYIRSEPVAQ--IYVHGDSLKAFLVG 599
Cdd:PRK05691 1540 PEEIQARLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
275-557 |
5.41e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 43.01 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 275 FTSGTTGNPKGAMLTHGNVVADF----SGFLKVTESQWAPTCADVhfSYLPLAHMFERMVQSVVYCHGGR-------VGF 343
Cdd:PRK05850 167 YTSGSTRTPAGVMVSHRNVIANFeqlmSDYFGDTGGVPPPDTTVV--SWLPFYHDMGLVLGVCAPILGGCpavltspVAF 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 344 FQGDIRLLSddMKALRPTIFPVVPrllnrmydkifhqadtslkRWLLEFAAKRKQAEVRSGIirnnsiwdELffnkiqas 423
Cdd:PRK05850 245 LQRPARWMQ--LLASNPHAFSAAP-------------------NFAFELAVRKTSDDDMAGL--------DL-------- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 424 lgGHVRMIVTGAAPASP-TVLGFLR--AALGCQ---VYEGYGQTECTAGCTFTTPGD-----------WTSGHV------ 480
Cdd:PRK05850 288 --GGVLGIISGSERVHPaTLKRFADrfAPFNLRetaIRPSYGLAEATVYVATREPGQppesvrfdyekLSAGHAkrcetg 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369599 481 -GAPLPCNH------IKLVDAEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEALD------SDG-----WLHTGDIG 542
Cdd:PRK05850 366 gGTPLVSYGsprsptVRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGatlvdpSPGtpegpWLRTGDLG 445
|
330
....*....|....*
gi 1937369599 543 kWLPEGTLKIIDRKK 557
Cdd:PRK05850 446 -FISEGELFIVGRIK 459
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
260-294 |
6.28e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 43.11 E-value: 6.28e-04
10 20 30
....*....|....*....|....*....|....*
gi 1937369599 260 RVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVV 294
Cdd:PRK10252 590 APLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIV 624
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
244-294 |
5.68e-03 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 39.88 E-value: 5.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1937369599 244 DIKSMQAIEDSGQENHRVpvppRPDDLSIVCFTSGTTGNPKGAMLTHGNVV 294
Cdd:PRK04813 123 ELKDIFATGNPYDFDHAV----KGDDNYYIIFTSGTTGKPKGVQISHDNLV 169
|
|
| |
