|
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 ... |
141-718 |
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: 907.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 141 QPYQWLSYQEVAKRAEFLGSGLLQHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADI 220
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 221 CTVIVDKphkatlllehverketpglklvilmepfedalrergkkcGVDIKSMQAIEDCGRENHHAPVPPRPDDLSIVCF 300
Cdd:cd05927 81 SIVFCDA---------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 301 TSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDM 380
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 381 KALRPTIFPVVPRLLNRMYDKIFH--QADTSLKRWLLEFAAKRKQAEVRSGIIRNNSIWDELFFNKIQASLGGHVRMIVT 458
Cdd:cd05927 202 KALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 459 GAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYW--TCKGEGEICVK 536
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDakDPNPRGEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 537 GPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGD 616
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 617 SLKAFLVGIVVPDPEVMPSWAQKK-GIEGTYQELCMKKELKKAILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLL 695
Cdd:cd05927 442 SLKSFLVAIVVPDPDVLKEWAASKgGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLL 521
|
570 580
....*....|....*....|...
gi 75992911 696 TPTLKAKRPELREYFKKQIEELY 718
Cdd:cd05927 522 TPTFKLKRPQLKKYYKKQIDEMY 544
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
104-718 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 695.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 104 TQLLTHY--YDDARTMYQVFRRGLSISGNGPCLGFRKPEQ----PYQWLSYQEVAKRAEFLGSGLLQHDCKVGteQFVGV 177
Cdd:PLN02736 31 LKLVSRFpdHPEIGTLHDNFVYAVETFRDYKYLGTRIRVDgtvgEYKWMTYGEAGTARTAIGSGLVQHGIPKG--ACVGL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 178 FAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIVdKPHKATLLLEHVerKETPGLKLVILMEPFED 257
Cdd:PLN02736 109 YFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCL--SEIPSVRLIVVVGGADE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 258 ALRERGKKCGVDIKSMQAIEDCGRENHHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvIFPrq 337
Cdd:PLN02736 186 PLPSLPSGTGVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTK--FYP-- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 338 DDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTS--LKRWLL 415
Cdd:PLN02736 262 SDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESggLKERLF 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 416 EFAAKRKQAEVRSGiiRNNS-IWDELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF 494
Cdd:PLN02736 342 NAAYNAKKQALENG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 495 TTPGDWTSGHVGAPLPCNHIKLVDAEELNYwTCKGE----GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWL 570
Cdd:PLN02736 420 MDEGDNLSGHVGSPNPACEVKLVDVPEMNY-TSEDQpyprGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWL 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 571 PEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKKGIE-GTYQEL 649
Cdd:PLN02736 499 PGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQL 578
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75992911 650 CMKKELKKAILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 718
Cdd:PLN02736 579 CNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMY 647
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
111-718 |
1.25e-175 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 515.42 E-value: 1.25e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 111 YDDARTMYQVFRRGLSISGNGPCLGfRKPEQPYQWLSYQEVAKRAEFLGSGLLQHDCKVGteQFVGVFAQNRPEWIIAEL 190
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVALR-EKEDGIWQSLTWAEFAERVRALAAGLLALGVKPG--DRVAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 191 ACYTYSMVVVPLYDTLGPGSISYIINTADICTVIVDKPHKATLLLEHveRKETPGLKLVILMEPfedalreRGKKCGVDI 270
Cdd:COG1022 84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEV--RDELPSLRHIVVLDP-------RGLRDDPRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 271 KSMQAIEDCGRENHH------APVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekvIFPRQDDVLISF 344
Cdd:COG1022 155 LSLDELLALGREVADpaeleaRRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLER----LPLGPGDRTLSF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 345 LPLAHMFERVIQSVVYCHGGRVGFfQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTS--LKRWLLEFA---A 419
Cdd:COG1022 231 LPLAHVFERTVSYYALAAGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAggLKRKLFRWAlavG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 420 KRKQAEVRSGiiRNNSIW--------DELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAG 491
Cdd:COG1022 310 RRYARARLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 492 CTFTTPGDWTSGHVGAPLPCNHIKLvdAEElnywtckgeGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLP 571
Cdd:COG1022 387 ITVNRPGDNRIGTVGPPLPGVEVKI--AED---------GEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 572 EGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKaFLVGIVVPDPEVMPSWAQKKGIE-GTYQELC 650
Cdd:COG1022 456 DGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDGRP-FLAALIVPDFEALGEWAEENGLPyTSYAELA 534
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75992911 651 MKKELKKAILDDMVMLGKesGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 718
Cdd:COG1022 535 QDPEVRALIQEEVDRANA--GLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALY 600
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
141-706 |
2.14e-159 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 468.23 E-value: 2.14e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 141 QPYQWLSYQEVAKRAEFLGSGLLQHDCKVGteQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADI 220
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPG--DRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 221 CTVIVDKPhkatlllehverketpglklvilmepfedalrergkkcgvdiksmqaiedcgrenhhapvpprpDDLSIVCF 300
Cdd:cd05907 79 KALFVEDP----------------------------------------------------------------DDLATIIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 301 TSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAHMFERV-IQSVVYCHGGRVGFFQgDIRLLSDD 379
Cdd:cd05907 95 TSGTTGRPKGVMLSHRNILSNALALAERLP----ATEGDRHLSFLPLAHVFERRaGLYVPLLAGARIYFAS-SAETLLDD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 380 MKALRPTIFPVVPRLLNRMYDKIFHQADTSLKRWLLEFAAkrkqaevrsgiirnnsiwdelffnkiqaslGGHVRMIVTG 459
Cdd:cd05907 170 LSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV------------------------------GGRLRFAASG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 460 AAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDaeelnywtckgEGEICVKGPN 539
Cdd:cd05907 220 GAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPN 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 540 VFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLK 619
Cdd:cd05907 288 VMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDGRP 367
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 620 aFLVGIVVPDPEVMPSWAQKKGIEG-TYQELCMKKELKKAILDDMVMLGKEsgLHSFEQVKAIYIHCDMFSVQNGLLTPT 698
Cdd:cd05907 368 -FLVALIVPDPEALEAWAEEHGIAYtDVAELAANPAVRAEIEAAVEAANAR--LSRYEQIKKFLLLPEPFTIENGELTPT 444
|
....*...
gi 75992911 699 LKAKRPEL 706
Cdd:cd05907 445 LKLKRPVI 452
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
142-703 |
2.15e-152 |
|
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: 452.44 E-value: 2.15e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 142 PYQWLSYQEVAKRAEFLGSGLlqhdCKVG--TEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTAD 219
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGL----VELGlkPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 220 ICTVIVDkphkatlllehverketpglklvilmepfedalrergkkcgvdiksmqaiedcgrenhhapvpPRPDDLSIVC 299
Cdd:cd17639 78 CSAIFTD---------------------------------------------------------------GKPDDLACIM 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 300 FTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPrqDDVLISFLPLAHMFERVIQSVVYCHGGRVGFfqGDIRLLSD- 378
Cdd:cd17639 95 YTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGP--DDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDk 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 379 -------DMKALRPTIFPVVPRLLNRMYDKIFHQADT--SLKRWLLEFAAKRKQAEVRSGIirNNSIWDELFFNKIQASL 449
Cdd:cd17639 171 skrgckgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPmgGLKRTLFWTAYQSKLKALKEGP--GTPLLDELVFKKVRAAL 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 450 GGHVRMIVTGAAPASPTVLGFLrAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYWTCKG 529
Cdd:cd17639 249 GGRLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDKP 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 530 E--GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEP 607
Cdd:cd17639 328 PprGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPL 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 608 VAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKKG-IEGTYQELCMKKELKKAILDDMVMLGKESGLHSFEQVKAIYIHCD 686
Cdd:cd17639 408 VNNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGvINSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDE 487
|
570
....*....|....*..
gi 75992911 687 MFSVQNGLLTPTLKAKR 703
Cdd:cd17639 488 EWTPENGLVTAAQKLKR 504
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
142-718 |
8.56e-148 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 445.83 E-value: 8.56e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 142 PYQWLSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADIC 221
Cdd:PLN02861 74 PYVWLTYKEVYDAAIRIGSAIRSRGVNPGDR--CGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 222 TVIVDKPHKATLLleHVERKETPGLKLVILMEPFEDALRERGKKCGVDIKSMQAIEDCGRENHHAPvPPRPDDLSIVCFT 301
Cdd:PLN02861 152 IAFVQESKISSIL--SCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLDCELP-PKQKTDICTIMYT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 302 SGTTGNPKGAMLTHGNVVADF---SGFLKVTEKVIfpRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSD 378
Cdd:PLN02861 229 SGTTGEPKGVILTNRAIIAEVlstDHLLKVTDRVA--TEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQGDIRYLME 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 379 DMKALRPTIFPVVPRLLNRMYDKIFH--QADTSLKRWLLEFAAKRKQAEVRSGIIRNNS--IWDELFFNKIQASLGGHVR 454
Cdd:PLN02861 307 DVQALKPTIFCGVPRVYDRIYTGIMQkiSSGGMLRKKLFDFAYNYKLGNLRKGLKQEEAspRLDRLVFDKIKEGLGGRVR 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 455 MIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCtFTTPGDWTS--GHVGAPLPCNHIKLVDAEELNY--WTCKGE 530
Cdd:PLN02861 387 LLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGC-FTSIANVFSmvGTVGVPMTTIEARLESVPEMGYdaLSDVPR 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 531 GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQ 610
Cdd:PLN02861 466 GEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIAS 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 611 IYVHGDSLKAFLVGIVVPDPEVMPSWAQKKGIEGTYQELCMKKELKKAILDDMVMLGKESGLHSFEQVKAIYIHCDMFSV 690
Cdd:PLN02861 545 IWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDI 624
|
570 580
....*....|....*....|....*...
gi 75992911 691 QNGLLTPTLKAKRPELREYFKKQIEELY 718
Cdd:PLN02861 625 ERDLITPTFKLKRPQLLKYYKDCIDQLY 652
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
112-718 |
2.23e-146 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 442.54 E-value: 2.23e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 112 DDARTMYQVFRRGLSISGNGPCLGFR-----KPEQpYQWLSYQEVAKRAEFLGSGLlqHDCKVGTEQFVGVFAQNRPEWI 186
Cdd:PLN02614 42 EGMDSCWDVFRMSVEKYPNNPMLGRReivdgKPGK-YVWQTYQEVYDIVIKLGNSL--RSVGVKDEAKCGIYGANSPEWI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 187 IAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIVDKPHKATLLleHVERKETPGLKLVILMEPFEDALRERGKKC 266
Cdd:PLN02614 119 ISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKISELF--KTCPNSTEYMKTVVSFGGVSREQKEEAETF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 267 GVDIKSMQAIEDCGRENHHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTEKVIfpRQDDVLIS 343
Cdd:PLN02614 197 GLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGvirLLKSANAAL--TVKDVYLS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 344 FLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTS--LKRWLLEFAAKR 421
Cdd:PLN02614 275 YLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGgfLKKFVFDSAFSY 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 422 KQAEVRSGI--IRNNSIWDELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGD 499
Cdd:PLN02614 355 KFGNMKKGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDE 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 500 WTS-GHVGAPLPCNHIKLVDAEELNY--WTCKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLK 576
Cdd:PLN02614 435 LDMlGTVGPPVPNVDIRLESVPEMEYdaLASTPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMK 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 577 IIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKKGIEGTYQELCMKKELK 656
Cdd:PLN02614 514 IIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAK 593
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75992911 657 KAILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 718
Cdd:PLN02614 594 EFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMY 655
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
113-718 |
5.58e-146 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 441.18 E-value: 5.58e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 113 DARTMYQVFRRGLSISGNGPCLGFRKPEQ----PYQWLSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIA 188
Cdd:PLN02430 40 DITTAWDIFSKSVEKYPDNKMLGWRRIVDgkvgPYMWKTYKEVYEEVLQIGSALRASGAEPGSR--VGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 189 ELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV-DKphKATLLLEhVERKETPGLKLVILMEPFEDALRERGKKCG 267
Cdd:PLN02430 118 MEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVqDK--KIKELLE-PDCKSAKRLKAIVSFTSVTEEESDKASQIG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 268 VDIKSMQAIEDCGRENHHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTEKVIfpRQDDVLISF 344
Cdd:PLN02430 195 VKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGvdlFMEQFEDKM--THDDVYLSF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 345 LPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFH--QADTSLKRWLLEFAAKRK 422
Cdd:PLN02430 273 LPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYKYK 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 423 QAEVRSGIIRNNS--IWDELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDW 500
Cdd:PLN02430 353 LAWMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEM 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 501 TS-GHVGAPLPCNHIKLVDAEELNYwTCKGE---GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLK 576
Cdd:PLN02430 433 CMlGTVGAPAVYNELRLEEVPEMGY-DPLGEpprGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLK 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 577 IIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKKGIEGTYQELCMKKELK 656
Cdd:PLN02430 511 IIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELK 590
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75992911 657 KAILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 718
Cdd:PLN02430 591 EHILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMY 652
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
84-718 |
4.88e-134 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 411.43 E-value: 4.88e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 84 KQSEEVEDGGG---ARRSviGGCTQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRK---PEQ---------------P 142
Cdd:PLN02387 26 KRGVPVDVGGEpgyAIRN--ARFPELVETPWEGATTLAALFEQSCKKYSDKRLLGTRKlisREFetssdgrkfeklhlgE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 143 YQWLSYQEVAKRAEFLGSGLLQ--HDckvgTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADI 220
Cdd:PLN02387 104 YEWITYGQVFERVCNFASGLVAlgHN----KEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 221 CTVIVDKPHKATLLlEHVERKETpgLKLVILMEPFEDALRERGKK-CGVDIKSMQAIEDCGRENHHAPVPPRPDDLSIVC 299
Cdd:PLN02387 180 TTVICDSKQLKKLI-DISSQLET--VKRVIYMDDEGVDSDSSLSGsSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIM 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 300 FTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifpRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFfqGDIRLLSD- 378
Cdd:PLN02387 257 YTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKL---GKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDt 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 379 ----------DMKALRPTIFPVVPRLLNRMYDKIFHQADTS--LKRWLLEFAAKRKQAEVR------SGIIRnnSIWDEL 440
Cdd:PLN02387 332 snkikkgtkgDASALKPTLMTAVPAILDRVRDGVRKKVDAKggLAKKLFDIAYKRRLAAIEgswfgaWGLEK--LLWDAL 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 441 FFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAE 520
Cdd:PLN02387 410 VFKKIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWE 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 521 ELNYWTCKG---EGEICVKGPNVFKGYLKDEDRTKEA--LDSDG--WLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYV 593
Cdd:PLN02387 490 EGGYLISDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYV 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 594 APEKIENIYIRSEPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKKGIE-GTYQELCMKKELKKAILDDMVMLGKESGL 672
Cdd:PLN02387 570 SLGKVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARL 649
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 75992911 673 HSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 718
Cdd:PLN02387 650 EKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLY 695
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
142-588 |
2.94e-125 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 379.35 E-value: 2.94e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 142 PYQWLSYQEVAKRAEFLGSGLLQHDCKVGteQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADIC 221
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRALGVGKG--DRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 222 TVIVDKPHKATLLLEHVERKETPGLKLVILMEPFEDALRergkkcgvdiksMQAIEDCGRENHHAPVPPRPDDLSIVCFT 301
Cdd:pfam00501 96 VLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEP------------LPEEAKPADVPPPPPPPPDPDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 302 SGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERV-IQSVVYCHGGRVGFFQGDIRL----L 376
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSlGLLGPLLAGATVVLPPGFPALdpaaL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 377 SDDMKALRPTIFPVVPRLLNRmydkifhqadtslkrwllefaakrkqaevrsgIIRNNSIWDELFfnkiqaslgGHVRMI 456
Cdd:pfam00501 244 LELIERYKVTVLYGVPTLLNM--------------------------------LLEAGAPKRALL---------SSLRLV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 457 VTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDW---TSGHVGAPLPCNHIKLVDAEELNYWTCKGEGEI 533
Cdd:pfam00501 283 LSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGEL 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 75992911 534 CVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLA 588
Cdd:pfam00501 363 CVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
84-718 |
1.53e-100 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 324.24 E-value: 1.53e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 84 KQSEEVEDGGGARRSVI---GGCT----QLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRK--------------PEQP 142
Cdd:PTZ00216 31 PQNVPVPGTETENASAIyriAGVTdeehERLRNEWYYGPNFLQRLERICKERGDRRALAYRPvervekevvkdadgKERT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 143 Y--------QWLSYQEVAKRAEFLGSGL----LQHDCKVGteqfvgVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGS 210
Cdd:PTZ00216 111 MevthfnetRYITYAELWERIVNFGRGLaelgLTKGSNVA------IYEETRWEWLASIYGIWSQSMVAATVYANLGEDA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 211 ISYIINTADiCTVIVDKPHKATLLLEHVERKETPGLKLVILmepfeDALRERGKKCGVDIKSMQAIEDCGRE---NHHAP 287
Cdd:PTZ00216 185 LAYALRETE-CKAIVCNGKNVPNLLRLMKSGGMPNTTIIYL-----DSLPASVDTEGCRLVAWTDVVAKGHSagsHHPLN 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 288 VPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF-LKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRV 366
Cdd:PTZ00216 259 IPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALeDRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLARGALI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 367 GFfqGDIRLLSD-------DMKALRPTIFPVVPRllnrmydkIFhqaDT-------------SLKRWLLEFAAKRKQAEV 426
Cdd:PTZ00216 339 GF--GSPRTLTDtfarphgDLTEFRPVFLIGVPR--------IF---DTikkaveaklppvgSLKRRVFDHAYQSRLRAL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 427 RSGiiRNNSIWDELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCqVYEGYGQTE--CTAGCTFTtpGDWTSGH 504
Cdd:PTZ00216 406 KEG--KDTPYWNEKVFSAPRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTEtvCCGGIQRT--GDLEPNA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 505 VGAPLPCNHIKLVDAEELNYwTCKGE--GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKK 582
Cdd:PTZ00216 481 VGQLLKGVEMKLLDTEEYKH-TDTPEprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVK 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 583 HIFKLAQGEYVAPEKIENIYIRSEPVAQ----IYVHGDslKAFLVGIVVPDPEVMPSWAQKKGIEGTYQELCMKKELKKA 658
Cdd:PTZ00216 560 ALAKNCLGEYIALEALEALYGQNELVVPngvcVLVHPA--RSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKK 637
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 659 ILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 718
Cdd:PTZ00216 638 ATESLQETARAAGRKSFEIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
143-703 |
2.21e-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: 265.49 E-value: 2.21e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 143 YQWLSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICT 222
Cdd:cd05932 4 VVEFTWGEVADKARRLAAALRALGLEPGSK--IALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 223 VIVDKphkatllLEHVERKET---PGLKLVILMEPfeDALRergkkcgvDIKSMQAIEDCGRENHHAPvPPRPDDLSIVC 299
Cdd:cd05932 82 LFVGK-------LDDWKAMAPgvpEGLISISLPPP--SAAN--------CQYQWDDLIAQHPPLEERP-TRFPEQLATLI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 300 FTSGTTGNPKGAMLTHGNvvadFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDD 379
Cdd:cd05932 144 YTSGTTGQPKGVMLTFGS----FAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTFVED 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 380 MKALRPTIFPVVPRLL----NRMYDKIFHQadtSLKRWLlefaakrkQAEVRSGIIRNnsiwdelffnKIQASLG-GHVR 454
Cdd:cd05932 220 VQRARPTLFFSVPRLWtkfqQGVQDKIPQQ---KLNLLL--------KIPVVNSLVKR----------KVLKGLGlDQCR 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 455 MIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDaeelnywtckgEGEIC 534
Cdd:cd05932 279 LAGCGSAPVPPALLEWYRS-LGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEIL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 535 VKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVH 614
Cdd:cd05932 347 VRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVI 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 615 GDSLKAfLVGIVVPDPEvmpswAQKKGIEGTYQELcmkKELKKAILDDMvmlgkESGLHSFEQVKAIYIHCDMFSVQNGL 694
Cdd:cd05932 427 GSGLPA-PLALVVLSEE-----ARLRADAFARAEL---EASLRAHLARV-----NSTLDSHEQLAGIVVVKDPWSIDNGI 492
|
....*....
gi 75992911 695 LTPTLKAKR 703
Cdd:cd05932 493 LTPTLKIKR 501
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
141-704 |
5.00e-75 |
|
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: 249.97 E-value: 5.00e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 141 QPYQWLSYQEVAKRAEFLGSGLLqhDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADI 220
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLR--SLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 221 CTVIVdkphkatlllehverketpglklvilmepfedalrergkkcgvdiksmqaiedcgrENHhapvpprPDDLSIVCF 300
Cdd:cd17640 79 VALVV--------------------------------------------------------END-------SDDLATIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 301 TSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFfqGDIRLLSDDM 380
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLLHQIRSLSDIVP----PQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDDL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 381 KALRPTIFPVVPRLLNRMYDKIFHQadtslkrwllefaaKRKQAEVRSGIIrnnsiwdeLFFnkiqaSLGGHVRMIVTGA 460
Cdd:cd17640 170 KRVKPHYIVSVPRLWESLYSGIQKQ--------------VSKSSPIKQFLF--------LFF-----LSGGIFKFGISGG 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 461 APASPTVLGFLRaALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYWTCKGEGEICVKGPNV 540
Cdd:cd17640 223 GALPPHVDTFFE-AIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQV 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 541 FKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKa 620
Cdd:cd17640 302 MKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQK- 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 621 FLVGIVVPDPEVMPSWAQKKGI---EGTYQELCMKKELKKAILDDMVMLGKESGLHSFEQVKAIYIHCDMFsVQNGLLTP 697
Cdd:cd17640 381 RLGALIVPNFEELEKWAKESGVklaNDRSQLLASKKVLKLYKNEIKDEISNRPGFKSFEQIAPFALLEEPF-IENGEMTQ 459
|
....*..
gi 75992911 698 TLKAKRP 704
Cdd:cd17640 460 TMKIKRN 466
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
144-718 |
1.79e-70 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 241.11 E-value: 1.79e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 144 QW--LSYQEVAKRAEFLGSGLLqhdcKVGTEQF--VGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTAD 219
Cdd:cd05933 5 KWhtLTYKEYYEACRQAAKAFL----KLGLERFhgVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 220 ICTVIVDKPHKATLLLEhvERKETPGLKLVI-LMEPFEDalrergKKCGVdiKSMQAIEDCGREnhhapVPP-------- 290
Cdd:cd05933 81 ANILVVENQKQLQKILQ--IQDKLPHLKAIIqYKEPLKE------KEPNL--YSWDEFMELGRS-----IPDeqldaiis 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 291 --RPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQS-VVYCHGGRVG 367
Cdd:cd05933 146 sqKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIwLPIKVGGQVY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 368 FFQGDIR--LLSDDMKALRPTIFPVVPRLLNRMYDKI---FHQAdTSLKRWLLEFAaKRKQAEV-------RSGIIRNNS 435
Cdd:cd05933 226 FAQPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkavGAKS-GTLKRKIASWA-KGVGLETnlklmggESPSPLFYR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 436 IWDELFFNKIQASLG-GHVRMIVTGAAPASPTVLGFLrAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHI 514
Cdd:cd05933 304 LAKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 515 KLVDAEelnywtCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVA 594
Cdd:cd05933 383 KIHNPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 595 PEKIENIYIRSEP-VAQIYVHGDSLKaFLVGIVV------PD---------PEVMpSWAQKKGIEGTY-QELCMKKELK- 656
Cdd:cd05933 457 PVPIEDAVKKELPiISNAMLIGDKRK-FLSMLLTlkcevnPEtgepldeltEEAI-EFCRKLGSQATRvSEIAGGKDPKv 534
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75992911 657 -KAILDDMVMLGKESGLHSFEQVKAIYIHCDmFSVQNGLLTPTLKAKRPELREYFKKQIEELY 718
Cdd:cd05933 535 yEAIEEGIKRVNKKAISNAQKIQKWVILEKD-FSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
117-630 |
1.02e-68 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 232.39 E-value: 1.02e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 117 MYQVFRRGLSISGNGPCLGFRkpeqpYQWLSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELACYTYS 196
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG-----GRRLTYAELDARARRLAAALRALG--VGPGDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 197 MVVVPLYDTLGPGSISYIINTADICTVIVdkphkatlllehverketpglklvilmepfedalrergkkcgvdiksmqai 276
Cdd:COG0318 74 AVVVPLNPRLTAEELAYILEDSGARALVT--------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 277 edcgrenhhapvpprpddlSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAHMF---ER 353
Cdd:COG0318 103 -------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALG----LTPGDVVLVALPLFHVFgltVG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 354 VIQSVVycHGGRV----GFfqgDIRLLSDDMKALRPTIFPVVPRLLNRMYDKI-FHQADTSlkrwllefaakrkqaevrs 428
Cdd:COG0318 160 LLAPLL--AGATLvllpRF---DPERVLELIERERVTVLFGVPTMLARLLRHPeFARYDLS------------------- 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 429 giirnnsiwdelffnkiqaslggHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVG 506
Cdd:COG0318 216 -----------------------SLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVG 272
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 507 APLPCNHIKLVDAE--ELNywtcKGE-GEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKH 583
Cdd:COG0318 273 RPLPGVEVRIVDEDgrELP----PGEvGEIVVRGPNVMKGYWNDPEATAEAFR-DGWLRTGDLGRLDEDGYLYIVGRKKD 347
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 75992911 584 IFKLAqGEYVAPEKIENIYIRSEPVAQIYV-------HGDSLKAFlvgiVVPDP 630
Cdd:COG0318 348 MIISG-GENVYPAEVEEVLAAHPGVAEAAVvgvpdekWGERVVAF----VVLRP 396
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
146-696 |
3.77e-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: 231.96 E-value: 3.77e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLlQHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 225
Cdd:cd17632 68 ITYAELWERVGAVAAAH-DPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 DKPHKAtLLLEHVERKETPGLKLVILMEPFEDA-------LRERGKKCGVDIKSMQAIEDCGRENHHAPVP---PRPDDL 295
Cdd:cd17632 147 SAEHLD-LAVEAVLEGGTPPRLVVFDHRPEVDAhraalesARERLAAVGIPVTTLTLIAVRGRDLPPAPLFrpePDDDPL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 296 SIVCFTSGTTGNPKGAMLTHgNVVADFsgFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGrVGFFQG--DI 373
Cdd:cd17632 226 ALLIYTSGSTGTPKGAMYTE-RLVATF--WLKVSSIQDIRPPASITLNFMPMSHIAGRISLYGTLARGG-TAYFAAasDM 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 374 RLLSDDMKALRPTIFPVVPRLLNRMYDKifHQADtsLKRWL-----LEFAAKRKQAEVRsgiirnnsiwdelffnkiQAS 448
Cdd:cd17632 302 STLFDDLALVRPTELFLVPRVCDMLFQR--YQAE--LDRRSvagadAETLAERVKAELR------------------ERV 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 449 LGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTtpgdwtSGHVGAPlPCNHIKLVDAEELNYWTCK 528
Cdd:cd17632 360 LGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE--AGAVIL------DGVIVRP-PVLDYKLVDVPELGYFRTD 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 529 G---EGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRS 605
Cdd:cd17632 431 RphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFAAS 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 606 EPVAQIYVHGDSLKAFLVGIVVPDPEVMPSwaqkkgiEGTyqelcmkKELKKAILDDMVMLGKESGLHSFEQVKAIYIHC 685
Cdd:cd17632 511 PLVRQIFVYGNSERAYLLAVVVPTQDALAG-------EDT-------ARLRAALAESLQRIAREAGLQSYEIPRDFLIET 576
|
570
....*....|.
gi 75992911 686 DMFSVQNGLLT 696
Cdd:cd17632 577 EPFTIANGLLS 587
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
143-669 |
2.74e-66 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 229.23 E-value: 2.74e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 143 YQWLSYQEVAKRAEFLGSGLlqHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICT 222
Cdd:cd17641 9 WQEFTWADYADRVRAFALGL--LALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 223 VIVDKPHKATLLLEHveRKETPGLKLVILMEPfedalreRGKKCGVDIK--SMQAIEDCGREnHHAPVPP---------R 291
Cdd:cd17641 87 VIAEDEEQVDKLLEI--ADRIPSVRYVIYCDP-------RGMRKYDDPRliSFEDVVALGRA-LDRRDPGlyerevaagK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKvifpRQDDVLISFLPLAHMFER---VIQSVVycHGGRVGF 368
Cdd:cd17641 157 GEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPL----GPGDEYVSVLPLPWIGEQmysVGQALV--CGFIVNF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 369 FQgDIRLLSDDMKALRPTIFPVVPRLLN--------RMYDKifhqadTSLKRWL--------LEFAAKRKQAEVRSGIIR 432
Cdd:cd17641 231 PE-EPETMMEDLREIGPTFVLLPPRVWEgiaadvraRMMDA------TPFKRFMfelgmklgLRALDRGKRGRPVSLWLR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 433 NNS-IWDELFFNKIQASLG-GHVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTEcTAGCTFTTP-GDWTSGHVGAPL 509
Cdd:cd17641 304 LASwLADALLFRPLRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTE-LAGAYTVHRdGDVDPDTVGVPF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 510 PCNHIKLVDaeelnywtckgEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQ 589
Cdd:cd17641 382 PGTEVRIDE-----------VGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSD 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 590 GEYVAPEKIENIYIRSEPVAQIYVHGDSlKAFLVGIVVPDPEVMPSWAQKKGIE-GTYQELCMKKELKKAILDDMVMLGK 668
Cdd:cd17641 451 GTRFSPQFIENKLKFSPYIAEAVVLGAG-RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKVNA 529
|
.
gi 75992911 669 E 669
Cdd:cd17641 530 S 530
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
146-631 |
1.80e-61 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 213.46 E-value: 1.80e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGsgLLQHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 225
Cdd:cd05914 8 LTYKDLADNIAKFA--LLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 DKPhkatlllehverketpglklvilmepfedalrergkkcgvdiksmqaiedcgrenhhapvpprpDDLSIVCFTSGTT 305
Cdd:cd05914 86 SDE----------------------------------------------------------------DDVALINYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 306 GNPKGAMLTHGNVVADFSGfLKVTEKVifpRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDI---RLLSDDMKA 382
Cdd:cd05914 102 GNSKGVMLTYRNIVSNVDG-VKEVVLL---GKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIpsaKIIALAFAQ 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 383 LRPTIfpVVPRLLNRMYDKIFHQADTSLKRWLLEFAAKrkqaevrsgIIRNNSIWdELFFNKIQASLGGHVRMIVTGAAP 462
Cdd:cd05914 178 VTPTL--GVPVPLVIEKIFKMDIIPKLTLKKFKFKLAK---------KINNRKIR-KLAFKKVHEAFGGNIKEFVIGGAK 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 463 ASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNywtckGEGEICVKGPNVFK 542
Cdd:cd05914 246 INPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDPAT-----GEGEIIVRGPNVMK 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 543 GYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVA--QIYVHGDSLKA 620
Cdd:cd05914 320 GYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLesLVVVQEKKLVA 399
|
490
....*....|.
gi 75992911 621 flvgIVVPDPE 631
Cdd:cd05914 400 ----LAYIDPD 406
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
118-623 |
1.96e-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: 210.50 E-value: 1.96e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 118 YQVFRRGLSISGNGPCLGFRKpeqpyQWLSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSM 197
Cdd:cd05936 2 ADLLEEAARRFPDKTALIFMG-----RKLTYRELDALAEAFAAGLQNLGVQPGDR--VALMLPNCPQFPIAYFGALKAGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 198 VVVPLYDTLGPGSISYIINTAdictvivdkphkatlllehverketpGLKLVILMEPFEDALRergkkcgvdiksmqaie 277
Cdd:cd05936 75 VVVPLNPLYTPRELEHILNDS--------------------------GAKALIVAVSFTDLLA----------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 278 dcGRENHHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIfpRQDDVLISFLPLAHMFErviQS 357
Cdd:cd05936 112 --AGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLL--EGDDVVLAALPLFHVFG---LT 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 358 VVYCHGGRVGFFQ------GDIRLLsDDMKALRPTIFPVVPRllnrMYDKIFHQADtslkrwllefaakrkqaevrsgii 431
Cdd:cd05936 185 VALLLPLALGATIvliprfRPIGVL-KEIRKHRVTIFPGVPT----MYIALLNAPE------------------------ 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 432 rnnsiwdelfFNKIQASlggHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT-SGHVGAPLP 510
Cdd:cd05936 236 ----------FKKRDFS---SLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRkPGSIGIPLP 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 511 CNHIKLVDaEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQG 590
Cdd:cd05936 303 GTEVKIVD-DDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGG 379
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 75992911 591 EYVAPEKIENIYIRSEPVAQIYV-------HGDSLKAFLV 623
Cdd:cd05936 380 FNVYPREVEEVLYEHPAVAEAAVvgvpdpySGEAVKAFVV 419
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
146-623 |
3.03e-60 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 211.30 E-value: 3.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 225
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGKGDR--VAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 -------DKP-HKATLLLEHVERKETP-GLKLVILMEPFEDALrERGKKcgvdiksmqaiedcgrENHHAPVppRPDDLS 296
Cdd:PRK07656 109 lglflgvDYSaTTRLPALEHVVICETEeDDPHTEKMKTFTDFL-AAGDP----------------AERAPEV--DPDDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 297 IVCFTSGTTGNPKGAMLTHGNV---VADFSGFLKVTEKvifprqDDVLISfLPLAHMFerviqsvvychGGRVGF----- 368
Cdd:PRK07656 170 DILFTSGTTGRPKGAMLTHRQLlsnAADWAEYLGLTEG------DRYLAA-NPFFHVF-----------GYKAGVnaplm 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 369 ----------FQGD--IRLLSDDmkalRPTIFPVVPRLLNRMYDkifhqadtslkrwllefAAKRKQAEVRSgiirnnsi 436
Cdd:PRK07656 232 rgatilplpvFDPDevFRLIETE----RITVLPGPPTMYNSLLQ-----------------HPDRSAEDLSS-------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 437 wdelffnkiqaslgghVRMIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGCTFTTPGD---WTSGHVGAPLPCN 512
Cdd:PRK07656 283 ----------------LRLAVTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIAGV 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 513 HIKLVDaeELNYWTCKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGE 591
Cdd:PRK07656 347 ENKIVN--ELGEEVPVGEvGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IVGGF 423
|
490 500 510
....*....|....*....|....*....|....*....
gi 75992911 592 YVAPEKIENIYIRSEPVAQIYV-------HGDSLKAFLV 623
Cdd:PRK07656 424 NVYPAEVEEVLYEHPAVAEAAVigvpderLGEVGKAYVV 462
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
294-631 |
3.35e-59 |
|
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: 203.29 E-value: 3.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 294 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekvIFPRQDDVLISFLPLAHMFerVIQSVVYC--HGGRVGFFQG 371
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS----GGLTEGDVFLSTLPLFHIG--GLFGLLGAllAGGTVVLLPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 372 -DIRLLSDDMKALRPTIFPVVPRLLNRmydkifhqadtslkrwLLEFAAKRKQAevrsgiirnnsiwdelffnkiQASLg 450
Cdd:cd04433 75 fDPEAALELIEREKVTILLGVPTLLAR----------------LLKAPESAGYD---------------------LSSL- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 451 ghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT--SGHVGAPLPCNHIKLVDAE--ELNYWt 526
Cdd:cd04433 117 ---RALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDPDggELPPG- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 527 ckGEGEICVKGPNVFKGYLKDEDRTkEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSE 606
Cdd:cd04433 193 --EIGELVVRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHP 268
|
330 340
....*....|....*....|....*
gi 75992911 607 PVAQIYVHGdslkaflvgivVPDPE 631
Cdd:cd04433 269 GVAEAAVVG-----------VPDPE 282
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
146-623 |
1.11e-52 |
|
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: 189.73 E-value: 1.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLLQHDCKVGteQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 225
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKG--DVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 DKPHKATLLLehVERKETPGLKlVILMEPFEDALRergkkcgvDIKSMQAIEDCGRENHHAPVPPR-PDDLSIVCFTSGT 304
Cdd:cd05911 89 DPDGLEKVKE--AAKELGPKDK-IIVLDDKPDGVL--------SIEDLLSPTLGEEDEDLPPPLKDgKDDTAAILYSSGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 305 TGNPKGAMLTHGNVVADFSgFLKVTEKVIFPRqDDVLISFLPLAHMFErvIQSVVYC--HGGRV----GFFqgdirllSD 378
Cdd:cd05911 158 TGLPKGVCLSHRNLIANLS-QVQTFLYGNDGS-NDVILGFLPLYHIYG--LFTTLASllNGATViimpKFD-------SE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 379 DMKAL----RPTIFPVVPRLLNRMydkifhqadtslkrwllefaakrkqaeVRSGIirnnsiwdelfFNKIQASlggHVR 454
Cdd:cd05911 227 LFLDLiekyKITFLYLVPPIAAAL---------------------------AKSPL-----------LDKYDLS---SLR 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 455 MIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYWTCKGEGEI 533
Cdd:cd05911 266 VILSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEI 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 534 CVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIyIRSEP------ 607
Cdd:cd05911 346 CVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAV-LLEHPgvadaa 423
|
490
....*....|....*...
gi 75992911 608 VAQIY--VHGDSLKAFLV 623
Cdd:cd05911 424 VIGIPdeVSGELPRAYVV 441
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
111-630 |
3.01e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 181.15 E-value: 3.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 111 YDDARTMYQVFRRGLSISGNGPCLGFRKPEqpyqwLSYQEVAKRAEFLGSGLLqhDCKVGTEQFVGVFAQNRPEWIIAEL 190
Cdd:PRK06187 2 QDYPLTIGRILRHGARKHPDKEAVYFDGRR-----TTYAELDERVNRLANALR--ALGVKKGDRVAVFDWNSHEYLEAYF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 191 ACytySM---VVVPLYDTLGPGSISYIINTADICTVIVDKPhkatlLLEHVE--RKETPGLKLVILMEPFEDALrergkk 265
Cdd:PRK06187 75 AV---PKigaVLHPINIRLKPEEIAYILNDAEDRVVLVDSE-----FVPLLAaiLPQLPTVRTVIVEGDGPAAP------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 266 CGVDIKSMQAIEDCGRENHHAPvPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVvadFSGFLKVTEKVIFpRQDDVLISFL 345
Cdd:PRK06187 141 LAPEVGEYEELLAAASDTFDFP-DIDENDAAAMLYTSGTTGHPKGVVLSHRNL---FLHSLAVCAWLKL-SRDDVYLVIV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 346 PLAHmferviqsvvyCHG---GRVGFFQG---------DIRLLSDDMKALRPTIFPVVPRLLNRMydkifHQADTSLKRW 413
Cdd:PRK06187 216 PMFH-----------VHAwglPYLALMAGakqviprrfDPENLLDLIETERVTFFFAVPTIWQML-----LKAPRAYFVD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 414 LlefaakrkqaevrsgiirnnsiwdelffnkiqaslgGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT 493
Cdd:PRK06187 280 F------------------------------------SSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVS 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 494 FTTPGDWTSGH------VGAPLPCNHIKLVDAEELNYWTCKGE-GEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDI 566
Cdd:PRK06187 324 VLPPEDQLPGQwtkrrsAGRPLPGVEARIVDDDGDELPPDGGEvGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDV 402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75992911 567 GKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIyirsepvaqIYVHGDSLKAFLVGivVPDP 630
Cdd:PRK06187 403 GYIDEDGYLYITDRIKDVIISG-GENIYPRELEDA---------LYGHPAVAEVAVIG--VPDE 454
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
121-630 |
8.86e-42 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 157.77 E-value: 8.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 121 FRRGLSISGNGPCLGFRKPEqpyqwLSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVV 200
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRS-----LTYAELDERVNRLAHALRALGVAKGDR--VAVLSKNSPEFLELLFAAARLGAVFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 201 PLYDTLGPGSISYIINTADictvivdkphkATLLLehverketpglklvilmepfedalrergkkcgvdiksmqaiedcg 280
Cdd:cd17631 74 PLNFRLTPPEVAYILADSG-----------AKVLF--------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 281 renhhapvpprpDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekvIFPRQDDVLISFLPLAHMFE-RVIQSVV 359
Cdd:cd17631 98 ------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAA----LDLGPDDVLLVVAPLFHIGGlGVFTLPT 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 360 YCHGGRV----GFfqgDIRLLSDDMKALRPTIFPVVPRLLNRMYDK-IFHQADTSlkrwllefaakrkqaevrsgiirnn 434
Cdd:cd17631 162 LLRGGTVvilrKF---DPETVLDLIERHRVTSFFLVPTMIQALLQHpRFATTDLS------------------------- 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 435 siwdelffnkiqaSLgghvRMIVTGAAPASPTVLGFLRAAlGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPCN 512
Cdd:cd17631 214 -------------SL----RAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHRRklGSAGRPVFFV 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 513 HIKLVDAE--ELNywtcKGE-GEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQ 589
Cdd:cd17631 276 EVRIVDPDgrEVP----PGEvGEIVVRGPHVMAGYWNRPEATAAAFR-DGWFHTGDLGRLDEDGYLYIVDRKKDMII-SG 349
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 75992911 590 GEYVAPEKIENIyirsepvaqIYVHGDSLKAFLVGivVPDP 630
Cdd:cd17631 350 GENVYPAEVEDV---------LYEHPAVAEVAVIG--VPDE 379
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
146-601 |
4.34e-41 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 157.40 E-value: 4.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLlqHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 225
Cdd:cd05904 33 LTYAELERRVRRLAAGL--AKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 DkphkatllLEHVERKETPGLKLVILMEPFEDalrergkkcgvdikSMQAIEDCGRENHHAPVPPR--PDDLSIVCFTSG 303
Cdd:cd05904 111 T--------AELAEKLASLALPVVLLDSAEFD--------------SLSFSDLLFEADEAEPPVVVikQDDVAALLYSSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 304 TTGNPKGAMLTHGNVVADFSGFLKVTEKVifPRQDDVLISFLPLAHMFerviqsvvychgGRVGFFQGDIRL-------- 375
Cdd:cd05904 169 TTGRSKGVMLTHRNLIAMVAQFVAGEGSN--SDSEDVFLCVLPMFHIY------------GLSSFALGLLRLgatvvvmp 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 376 ---LSDDMKAL---RPTIFPVVPRLLnrmydkifhqadtslkrwllefAAKRKQAEVRSGIIRnnsiwdelffnkiqaSL 449
Cdd:cd05904 235 rfdLEELLAAIeryKVTHLPVVPPIV----------------------LALVKSPIVDKYDLS---------------SL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 450 gghvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFTTP---GDWTSGHVGAPLPCNHIKLVDAEELNYW 525
Cdd:cd05904 278 ----RQIMSGAAPLGKELIeAFRAKFPNVDLGQGYGMTESTGVVAMCFApekDRAKYGSVGRLVPNVEAKIVDPETGESL 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75992911 526 TCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENI 601
Cdd:cd05904 354 PPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEAL 428
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
258-718 |
1.87e-40 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 158.73 E-value: 1.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 258 ALRERGKKCGVdikSMQAIEDCGREN--HHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNV------VADFSGFLKVT 329
Cdd:PTZ00342 270 DLKEKAKKLGI---SIILFDDMTKNKttNYKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLyntvvpLCKHSIFKKYN 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 330 EKVIFprqddvliSFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQAD-- 407
Cdd:PTZ00342 347 PKTHL--------SYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINnl 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 408 TSLKRWLLE--FAAKRkqaevrsgiiRNNSIWDELFF-------NKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQ 478
Cdd:PTZ00342 419 PPLKRFLVKkiLSLRK----------SNNNGGFSKFLegithisSKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVN 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 479 VYEGYGQTEcTAGCTFTTPG-DWTSGHVGAPL-PCNHIKLVDAEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALD 556
Cdd:PTZ00342 489 YYQGYGLTE-TTGPIFVQHAdDNNTESIGGPIsPNTKYKVRTWETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFT 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 557 SDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHG-DSLKAFLvGIVVPDPEVM-- 633
Cdd:PTZ00342 568 EDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGdDSMDGPL-AIISVDKYLLfk 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 634 ----PSWAQKKGI-EGTYQELCMKKELKKAILDDMV---MLG--KESGLHSFEQVKAIYIHCDMFSVQNgLLTPTLKAKR 703
Cdd:PTZ00342 647 clkdDNMLESTGInEKNYLEKLTDETINNNIYVDYVkgkMLEvyKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKR 725
|
490
....*....|....*...
gi 75992911 704 PEL-REY--FKKQIEELY 718
Cdd:PTZ00342 726 FYVfKDYafFIDQVKKIY 743
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
146-634 |
2.76e-39 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 150.90 E-value: 2.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLgSGLLQHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIv 225
Cdd:cd05941 12 ITYADLVARAARL-ANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 dkphkatlllehverketpglklvilmepfedalrergkkcgvdiksmqaiedcgrenhhapvpprpdDLSIVCFTSGTT 305
Cdd:cd05941 90 --------------------------------------------------------------------DPALILYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 306 GNPKGAMLTHGNVVADFSGFLKVTEKvifpRQDDVLISFLPLAHMFERV--IQSVVYChGGRV---GFFQGDIRLLSDDM 380
Cdd:cd05941 102 GRPKGVVLTHANLAANVRALVDAWRW----TEDDVLLHVLPLHHVHGLVnaLLCPLFA-GASVeflPKFDPKEVAISRLM 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 381 KALrpTIFPVVPRllnrMYDKIFHQADTSLKrwllEFAAKRKQAEvrsgiirnnsiwdelffnkiqaslgGHVRMIVTGA 460
Cdd:cd05941 177 PSI--TVFMGVPT----IYTRLLQYYEAHFT----DPQFARAAAA-------------------------ERLRLMVSGS 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 461 APASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTTP--GDWTSGHVGAPLPCNHIKLVDAEELNYWTCKGEGEICVKGP 538
Cdd:cd05941 222 AALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGP 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 539 NVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKK-HIFKlAQGEYVAPEKIENIYIRSEPVAQIYVHGDS 617
Cdd:cd05941 300 SVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEIERVLLAHPGVSECAVIGVP 378
|
490 500
....*....|....*....|
gi 75992911 618 LKAF---LVGIVVPDPEVMP 634
Cdd:cd05941 379 DPDWgerVVAVVVLRAGAAA 398
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
146-601 |
6.42e-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: 150.94 E-value: 6.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSgLLQHDCKVGteQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 225
Cdd:cd05909 8 LTYRKLLTGAIALAR-KLAKMTKEG--ENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 DKPHKATLLLEHVERKETPgLKLVILmepfEDaLRER---GKKCGVDIKSMQAIEDCGRENHHAPVppRPDDLSIVCFTS 302
Cdd:cd05909 85 SKQFIEKLKLHHLFDVEYD-ARIVYL----ED-LRAKiskADKCKAFLAGKFPPKWLLRIFGVAPV--QPDDPAVILFTS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 303 GTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAHMFerviqsvvychggrvGFFQGDIRLLSDDMKA 382
Cdd:cd05909 157 GSEGLPKGVVLSHKNLLANVEQITAIFD----PNPEDVVFGALPFFHSF---------------GLTGCLWLPLLSGIKV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 383 L---RPTIFPVVPRLLnrmYDK---IFHQADTSLKRWllefaAKRKQAEVRSGIirnnsiwdelffnkiqaslgghvRMI 456
Cdd:cd05909 218 VfhpNPLDYKKIPELI---YDKkatILLGTPTFLRGY-----ARAAHPEDFSSL-----------------------RLV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 457 VTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPCNHIKLVDAEELNYWTCKGEGEICV 535
Cdd:cd05909 267 VAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLV 346
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75992911 536 KGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENI 601
Cdd:cd05909 347 RGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDI 410
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
148-640 |
5.94e-37 |
|
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: 144.13 E-value: 5.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 148 YQEVAKRAEFLgsgllqHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIVDK 227
Cdd:TIGR01923 6 DCEAAHLAKAL------KAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 228 P-HKATLLLEHVERKETPGLKLVILMEPFEDalrergkkcgvdiksmqaiedcgrenhhapvpprpDDLSIVCFTSGTTG 306
Cdd:TIGR01923 80 LlEEKDFQADSLDRIEAAGRYETSLSASFNM-----------------------------------DQIATLMFTSGTTG 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 307 NPKGAMLTHGNVVADFSGflkVTEKVIFPRQDDVLISfLPLAH------MFERVIQsvvychGGRVGFFQGDIRLLsDDM 380
Cdd:TIGR01923 125 KPKAVPHTFRNHYASAVG---SKENLGFTEDDNWLLS-LPLYHisglsiLFRWLIE------GATLRIVDKFNQLL-EMI 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 381 KALRPTIFPVVPRLLNRMYDKIFHqaDTSLKRWLLefaakrkqaevrsgiirnnsiwdelffnkiqaslGGhvrmivtGA 460
Cdd:TIGR01923 194 ANERVTHISLVPTQLNRLLDEGGH--NENLRKILL----------------------------------GG-------SA 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 461 APASptvlgFLRAAL--GCQVYEGYGQTE-CTAGCTFTTPGDWTSGHVGAPLPCNHIKL-VDAEElnywtckGEGEICVK 536
Cdd:TIGR01923 231 IPAP-----LIEEAQqyGLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIkVDNKE-------GHGEIMVK 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 537 GPNVFKGYLKDEDRTkEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYV--H 614
Cdd:TIGR01923 299 GANLMKGYLYQGELT-PAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVVvpK 376
|
490 500 510
....*....|....*....|....*....|.
gi 75992911 615 GDSL-----KAFLVGIVVPDPEVMPSWAQKK 640
Cdd:TIGR01923 377 PDAEwgqvpVAYIVSESDISQAKLIAYLTEK 407
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
116-629 |
6.94e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 146.30 E-value: 6.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 116 TMYQVFRRGLSISGNGPCLGFRKPEQPYQWLSYQeVAKRAEFLgsgllqHDCKVGTEQFVGVFAQNRPEWIIAELACYTY 195
Cdd:PRK05605 33 TLVDLYDNAVARFGDRPALDFFGATTTYAELGKQ-VRRAAAGL------RALGVRPGDRVAIVLPNCPQHIVAFYAVLRL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 196 SMVVV---PLYDT---LGP----GSISYII--NTADICTVIVDkphkaTLLLEHVER----KETPGLKLVILMEPFEDAL 259
Cdd:PRK05605 106 GAVVVehnPLYTAhelEHPfedhGARVAIVwdKVAPTVERLRR-----TTPLETIVSvnmiAAMPLLQRLALRLPIPALR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 260 RERGKKCG-----VDIKSMQAIEDcGRENHHAPVP-PRPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD-FSGFLKVTEkv 332
Cdd:PRK05605 181 KARAALTGpapgtVPWETLVDAAI-GGDGSDVSHPrPTPDDVALILYTSGTTGKPKGAQLTHRNLFANaAQGKAWVPG-- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 333 iFPRQDDVLISFLPLAHMF--ERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLlnrmYDKIfhqadtsl 410
Cdd:PRK05605 258 -LGDGPERVLAALPMFHAYglTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPL----YEKI-------- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 411 krwlLEFAAKRkqaevrsGIirnnsiwdelffnkiqaSLGGhVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECT- 489
Cdd:PRK05605 325 ----AEAAEER-------GV-----------------DLSG-VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSp 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 490 --AGCTFTTpgDWTSGHVGAPLPCNHIKLVDAEELNYWTCKGE-GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDI 566
Cdd:PRK05605 376 iiVGNPMSD--DRRPGYVGVPFPDTEVRIVDPEDPDETMPDGEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDV 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75992911 567 GKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIEniyirsEPVAQiyvHGDSLKAFLVGIVVPD 629
Cdd:PRK05605 453 VVMEEDGFIRIVDRIKELI-ITGGFNVYPAEVE------EVLRE---HPGVEDAAVVGLPRED 505
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
145-708 |
7.13e-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: 144.76 E-value: 7.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 145 WLSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVI 224
Cdd:cd05926 14 ALTYADLAELVDDLARQLAALGIKKGDR--VAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 225 VDKPHkatlLLEHVERKETPGLklvilmepfedALRERGKKCGVDIKSMQAIEDCGRENHHAPV----PPRPDDLSIVCF 300
Cdd:cd05926 92 TPKGE----LGPASRAASKLGL-----------AILELALDVGVLIRAPSAESLSNLLADKKNAksegVPLPDDLALILH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 301 TSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvIFPrqDDVLISFLPLAHmferVIQSVVYC-----HGGRV----GFfqg 371
Cdd:cd05926 157 TSGTTGRPKGVPLTHRNLAASATNITNTYK--LTP--DDRTLVVMPLFH----VHGLVASLlstlaAGGSVvlppRF--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 372 DIRLLSDDMKALRPTIFPVVPRLlnrmydkifHQAdtslkrwLLEFAAKRKQAEVrsgiirnnsiwdelffnkiqaslgG 451
Cdd:cd05926 226 SASTFWPDVRDYNATWYTAVPTI---------HQI-------LLNRPEPNPESPP------------------------P 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 452 HVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTP---GDWTSGHVGAPLPcNHIKLVDAEELnywTCK 528
Cdd:cd05926 266 KLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTE-AAHQMTSNPlppGPRKPGSVGKPVG-VEVRILDEDGE---ILP 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 529 --GEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSE 606
Cdd:cd05926 341 pgVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVLLSHP 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 607 PVAQIYVHGdslkaflvgivVPDP----EVMPSWAQKKGIEGTYQELcmKKELKKailddmvmlgkesGLHSFEQVKAIY 682
Cdd:cd05926 420 AVLEAVAFG-----------VPDEkygeEVAAAVVLREGASVTEEEL--RAFCRK-------------HLAAFKVPKKVY 473
|
570 580
....*....|....*....|....*.
gi 75992911 683 IhcdmfsVQNGLLTPTLKAKRPELRE 708
Cdd:cd05926 474 F------VDELPKTATGKIQRRKVAE 493
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
162-631 |
7.74e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 135.70 E-value: 7.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 162 LLQHDCKVGteQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADictvivdkphkATLLLEhverk 241
Cdd:PRK09088 39 LRRRGCVDG--ERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAE-----------PRLLLG----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 242 etpglklvilmepfeDALRERGKKCGVDIKSMQAIEDCGRENHHAPVPPrpDDLSIVCFTSGTTGNPKGAMLTHGNVVAD 321
Cdd:PRK09088 101 ---------------DDAVAAGRTDVEDLAAFIASADALEPADTPSIPP--ERVSLILFTSGTSGQPKGVMLSERNLQQT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 322 FSGFlKVTEKVifprqdDVLISFLPLAHMFERV--IQSV--VYCHGGRV----GFFQG-DIRLLSDdmKALRPTIFPVVP 392
Cdd:PRK09088 164 AHNF-GVLGRV------DAHSSFLCDAPMFHIIglITSVrpVLAVGGSIlvsnGFEPKrTLGRLGD--PALGITHYFCVP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 393 RllnrMYDKIFHQADtslkrwlleFAAkrkqaevrsgiirnnsiwdelffnkiqASLGgHVRMIVTGAAP-ASPTVLGFL 471
Cdd:PRK09088 235 Q----MAQAFRAQPG---------FDA---------------------------AALR-HLTALFTGGAPhAAEDILGWL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 472 raALGCQVYEGYGQTEctAGCTFTTPGDWT-----SGHVGAPLPCNHIKLVDAEELNywtCK-GE-GEICVKGPNVFKGY 544
Cdd:PRK09088 274 --DDGIPMVDGFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVVDDQGND---CPaGVpGELLLRGPNLSPGY 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 545 LKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIEniyirsepvAQIYVHGDSLKAFLVG 624
Cdd:PRK09088 347 WRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIE---------AVLADHPGIRECAVVG 416
|
....*..
gi 75992911 625 ivVPDPE 631
Cdd:PRK09088 417 --MADAQ 421
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
280-623 |
1.36e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 136.43 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 280 GRENHHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGfLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVV 359
Cdd:PRK05677 194 GAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQ-CRALMGSNLNEGCEILIAPLPLYHIYAFTFHCMA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 360 YCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLlNRMydkifhqadtslkrwlleFAAkrkqaevrsgiIRNNSIWDE 439
Cdd:PRK05677 273 MMLIGNHNILISNPRDLPAMVKELGKWKFSGFVGL-NTL------------------FVA-----------LCNNEAFRK 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 440 LFFNKIQASLGGHvrMIVTGAAPASptvlgfLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVD- 518
Cdd:PRK05677 323 LDFSALKLTLSGG--MALQLATAER------WKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDd 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 519 -AEELNYwtckGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPE 596
Cdd:PRK05677 395 dGNELPL----GEvGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVSGFNVYPN 469
|
330 340 350
....*....|....*....|....*....|....
gi 75992911 597 KIENIYIRSEPVAQ---IYV----HGDSLKAFLV 623
Cdd:PRK05677 470 ELEDVLAALPGVLQcaaIGVpdekSGEAIKVFVV 503
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
280-630 |
1.38e-32 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 133.08 E-value: 1.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 280 GRENHHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADF---SGFLKVTEKVifPRQDDVLISFLPLAHMFERVIQ 356
Cdd:PRK08751 195 GRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMqqaHQWLAGTGKL--EEGCEVVITALPLYHIFALTAN 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 357 SVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLlNRMYDKIFhqadtslkrwllefaakrkqaevrsgiirNNSI 436
Cdd:PRK08751 273 GLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGV-NTLFNGLL-----------------------------NTPG 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 437 WDELFFNKIQASLGGHvrMIVTGAapasptVLGFLRAALGCQVYEGYGQTECT-AGCTFTTPGDWTSGHVGAPLPCNHIK 515
Cdd:PRK08751 323 FDQIDFSSLKMTLGGG--MAVQRS------VAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDAC 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 516 LVDaeELNYWTCKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVA 594
Cdd:PRK08751 395 IKD--DAGTVLAIGEiGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-LVSGFNVY 471
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 75992911 595 PEKIENIYIRSEPVAQIYVHG----DSLKAFLVGIVVPDP 630
Cdd:PRK08751 472 PNEIEDVIAMMPGVLEVAAVGvpdeKSGEIVKVVIVKKDP 511
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
292-623 |
2.16e-32 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 132.49 E-value: 2.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPRQDDVLISfLPLAHMFERVIQSVVYCHGGRVGFF-- 369
Cdd:PRK08974 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGPLLHPGKELVVTA-LPLYHIFALTVNCLLFIELGGQNLLit 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 370 -QGDIRLLSDDMKALRPTIFPVVPRLLNRmydkifhqadtslkrWLlefaakrkqaevrsgiirNNSIWDELFFNKIQAS 448
Cdd:PRK08974 284 nPRDIPGFVKELKKYPFTAITGVNTLFNA---------------LL------------------NNEEFQELDFSSLKLS 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 449 LGGhvrmivtgAAPASPTVLGFLRAALGCQVYEGYGQTECT---AGCTFTTPGdwTSGHVGAPLPCNHIKLVDaEELNYW 525
Cdd:PRK08974 331 VGG--------GMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVNPYDLDY--YSGSIGLPVPSTEIKLVD-DDGNEV 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 526 TCKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRS 605
Cdd:PRK08974 400 PPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMI-LVSGFNVYPNEIEDVVMLH 477
|
330 340
....*....|....*....|....*
gi 75992911 606 EPVAQIY-------VHGDSLKAFLV 623
Cdd:PRK08974 478 PKVLEVAavgvpseVSGEAVKIFVV 502
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
146-635 |
2.70e-32 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 130.34 E-value: 2.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELACY----TYsmvvVPLYDTLGPGSISYIINTAdic 221
Cdd:cd05930 13 LTYAELDARANRLARYLRERG--VGPGDLVAVLLERSLEMVVAILAVLkagaAY----VPLDPSYPAERLAYILEDS--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 222 tvivdkphKATLLLEHverketpglklvilmepfedalrergkkcgvdiksmqaiedcgrenhhapvpprPDDLSIVCFT 301
Cdd:cd05930 84 --------GAKLVLTD------------------------------------------------------PDDLAYVIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 302 SGTTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPLAH------MFerviqsVVYCHGGRV----GFFQG 371
Cdd:cd05930 102 SGSTGKPKGVMVEHRGLVN----LLLWMQEAYPLTPGDRVLQFTSFSFdvsvweIF------GALLAGATLvvlpEEVRK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 372 DIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTSLkrwllefaakrkqaevrsgiirnnsiwdelffnkiqaslgg 451
Cdd:cd05930 172 DPEALADLLAEEGITVLHLTPSLLRLLLQELELAALPSL----------------------------------------- 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 452 hvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFT--TPGDWTSGHV--GAPLPCNHIKLVDaEELNYWT 526
Cdd:cd05930 211 --RLVLVGGEALPPDLVrRWRELLPGARLVNLYGPTEATVDATYYrvPPDDEEDGRVpiGRPIPNTRVYVLD-ENLRPVP 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 527 CKGEGEICVKGPNVFKGYLKDEDRTKEA-----LDSDGWLH-TGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIEN 600
Cdd:cd05930 288 PGVPGELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIELGEIEA 366
|
490 500 510
....*....|....*....|....*....|....*...
gi 75992911 601 IYIRSEPVAQIYV---HGDSLKAFLVGIVVPDPEVMPS 635
Cdd:cd05930 367 ALLAHPGVREAAVvarEDGDGEKRLVAYVVPDEGGELD 404
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
147-613 |
6.92e-32 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 128.54 E-value: 6.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 147 SYQEVAKRAEFLGSGLLQHdCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGS-ISYIINTADICTVIV 225
Cdd:TIGR01733 1 TYRELDERANRLARHLRAA-GGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPL-DPAYPAErLAFILEDAGARLLLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 DKPHkatlllehveRKETPGLKLVILMEPFEDALrergkkcgvdiksmqAIEDCGRENHhAPVPPRPDDLSIVCFTSGTT 305
Cdd:TIGR01733 79 DSAL----------ASRLAGLVLPVILLDPLELA---------------ALDDAPAPPP-PDAPSGPDDLAYVIYTSGST 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 306 GNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPLAH------MFerviqsVVYCHGGRVGFFQGDIRLlsDD 379
Cdd:TIGR01733 133 GRPKGVVVTHRSLVN----LLAWLARRYGLDPDDRVLQFASLSFdasveeIF------GALLAGATLVVPPEDEER--DD 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 380 MKALRptifpvvpRLLNRMYDKIFHQADTSLKRWLLEfaakrkqaevrsgiirnnsiwdelffnkiQASLGGHVRMIVTG 459
Cdd:TIGR01733 201 AALLA--------ALIAEHPVTVLNLTPSLLALLAAA-----------------------------LPPALASLRLVILG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 460 AAPASPTVLGFLRAALG-CQVYEGYGQTECTAGCT-FTTPGDWTSGHV----GAPLPCNHIKLVDA--EELNYWtckGEG 531
Cdd:TIGR01733 244 GEALTPALVDRWRARGPgARLINLYGPTETTVWSTaTLVDPDDAPRESpvpiGRPLANTRLYVLDDdlRPVPVG---VVG 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 532 EICVKGPNVFKGYLKDEDRTKEA-LDSDGWL-------HTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYI 603
Cdd:TIGR01733 321 ELYIGGPGVARGYLNRPELTAERfVPDPFAGgdgarlyRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAALL 399
|
490
....*....|
gi 75992911 604 RSEPVAQIYV 613
Cdd:TIGR01733 400 RHPGVREAVV 409
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
118-659 |
1.28e-31 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 130.23 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 118 YQVFRRGLSISGNGPCLGFRKPEQPYQWLSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELACYTYSM 197
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRALG--VKKGDRVAIYLPNIPEAVIAMLACARIGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 198 VVVPLYDTLGPGSISYIINTADICTVIVD----KPHKATLLLEHVE--RKETPGLKLVILMEPFEDALRERGkkcgvDIK 271
Cdd:COG0365 90 VHSPVFPGFGAEALADRIEDAEAKVLITAdgglRGGKVIDLKEKVDeaLEELPSLEHVIVVGRTGADVPMEG-----DLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 272 SMQAIEDCGREnhHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVTEKVIF-PRQDDVL--------- 341
Cdd:COG0365 165 WDELLAAASAE--FEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYL----VHAATTAKYVLdLKPGDVFwctadigwa 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 342 -----ISFLPLAH-----MFERVIqsvVYCHGGRVgffqgdIRLLSDdmkaLRPTIFPVVPRLLnRMydkifhqadtsLK 411
Cdd:COG0365 239 tghsyIVYGPLLNgatvvLYEGRP---DFPDPGRL------WELIEK----YGVTVFFTAPTAI-RA-----------LM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 412 RWLLEFAAKRKQAevrsgiirnnsiwdelffnkiqaslggHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECtaG 491
Cdd:COG0365 294 KAGDEPLKKYDLS---------------------------SLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTET--G 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 492 CTFTTPGDWTS---GHVGAPLPCNHIKLVDAEelnywtckG-------EGEICVKG--PNVFKGYLKDEDRTKEAL--DS 557
Cdd:COG0365 345 GIFISNLPGLPvkpGSMGKPVPGYDVAVVDED--------GnpvppgeEGELVIKGpwPGMFRGYWNDPERYRETYfgRF 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 558 DGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQIYV----H---GDSLKAFlvgiVVPDP 630
Cdd:COG0365 417 PGWYRTGDGARRDEDGYFWILGRSDDVINVS-GHRIGTAEIESALVSHPAVAEAAVvgvpDeirGQVVKAF----VVLKP 491
|
570 580
....*....|....*....|....*....
gi 75992911 631 EVMPSwaqkkgiegtyQELcmKKELKKAI 659
Cdd:COG0365 492 GVEPS-----------DEL--AKELQAHV 507
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
292-630 |
1.38e-31 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 126.24 E-value: 1.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSGF-LKVTEkvifprqDDVLISFLPLAHMFERVIqSVVYC--HGGRV 366
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVnnGYFIGErLGLTE-------QDRLCIPVPLFHCFGSVL-GVLACltHGATM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 367 GF----FqgDIRLLSDDMKALRPTIFPVVPRllnrMYDKIFHQADtslkrwLLEFAAKRkqaeVRSGIIrnnsiwdelff 442
Cdd:cd05917 73 VFpspsF--DPLAVLEAIEKEKCTALHGVPT----MFIAELEHPD------FDKFDLSS----LRTGIM----------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 443 nkiqaslgghvrmivtGAAPASPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGDWTS---GHVGAPLPCNHIKLVD 518
Cdd:cd05917 126 ----------------AGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDSIEkrvNTVGRIMPHTEAKIVD 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 519 AEelnywTCK----GE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYV 593
Cdd:cd05917 190 PE-----GGIvppvGVpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGENI 263
|
330 340 350
....*....|....*....|....*....|....*..
gi 75992911 594 APEKIENIyirsepvaqIYVHGDSLKAFLVGivVPDP 630
Cdd:cd05917 264 YPREIEEF---------LHTHPKVSDVQVVG--VPDE 289
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
49-718 |
1.96e-31 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 132.29 E-value: 1.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 49 SLSATTLVsVGALAAVLAYWLTHRPKALQPPCNLLKQSEEVEDGGGarrsvigGCTQLLTHYYDD---ARTMYQVFRRGL 125
Cdd:PTZ00297 366 SFSFMSLV-LCAAVWLLRWAQNSSIHPLLSERPFLTVEALKEKGEE-------CFALNLPREYNPlagVRSLGEMWERSV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 126 SISGNGPCLGFRKPEQPYQWLSYQEVAKRAEFLGSGLLQHDCKVGteQFVGVFAQNRPEWIIAELACYTYSMVVVPLydt 205
Cdd:PTZ00297 438 TRHSTFRCLGQTSESGESEWLTYGTVDARARELGSGLLALGVRPG--DVIGVDCEASRNIVILEVACALYGFTTLPL--- 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 206 LGPGS-ISYIINTADICTVIVDKPHKATLLLEHVERKETpglklVILMEPFEDALRER-GKKCGVDIKSMQAIEDCGREn 283
Cdd:PTZ00297 513 VGKGStMRTLIDEHKIKVVFADRNSVAAILTCRSRKLET-----VVYTHSFYDEDDHAvARDLNITLIPYEFVEQKGRL- 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 284 hhAPVPPRP--DDLSIVCFTSGTTGNPKGAML-----THGNVVADFSgFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQ 356
Cdd:PTZ00297 587 --CPVPLKEhvTTDTVFTYVVDNTTSASGDGLavvrvTHADVLRDIS-TLVMTGVLPSSFKKHLMVHFTPFAMLFNRVFV 663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 357 SVVYCHGGRVGffQGDIRLLSDDMKALRPTIFPVVPRLlnrmydkiFHQADTSLKR----------WLLEfaakrKQAEV 426
Cdd:PTZ00297 664 LGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSL--------FSTSRLQLSRanerysavysWLFE-----RAFQL 728
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 427 RSGII----RNNSIWDELFFNKIQASLGGHVRMIVTGAAPASPTvlgflraalgcqvyegYGQTECTAGCTfttpgdwts 502
Cdd:PTZ00297 729 RSRLInihrRDSSLLRFIFFRATQELLGGCVEKIVLCVSEESTS----------------FSLLEHISVCY--------- 783
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 503 ghvgAPLPCnhiklvdaeELNYWTCkgEGEICVKG---PNVFKGYLKDEDRTKEAldSDGWL---------HTGDI-GKW 569
Cdd:PTZ00297 784 ----VPCLR---------EVFFLPS--EGVFCVDGtpaPSLQVDLEPFDEPSDGA--GIGQLvlakkgeprRTLPIaAQW 846
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 570 LPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAfLVGIVVPDPEVMP-SWAQKKGIE---GT 645
Cdd:PTZ00297 847 KRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEfEWRQSHCMGeggGP 925
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75992911 646 YQELCMKKELKKA---ILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 718
Cdd:PTZ00297 926 ARQLGWTELVAYAsslLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIERFY 1001
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
142-582 |
2.39e-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: 129.32 E-value: 2.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 142 PYQWLSYQEVAKRAEFLGSGLLQHDCKVGtEQFVGVFAQNRpEWIIAELACYTYSMVVVPLydtlGPGSISYIINTAdic 221
Cdd:cd05906 36 SEEFQSYQDLLEDARRLAAGLRQLGLRPG-DSVILQFDDNE-DFIPAFWACVLAGFVPAPL----TVPPTYDEPNAR--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 222 tvivdkphkaTLLLEHVerKETPGLKLVI----LMEPFEDALRERGKkCGVDIKSMQAIEDCGREnHHAPvPPRPDDLSI 297
Cdd:cd05906 107 ----------LRKLRHI--WQLLGSPVVLtdaeLVAEFAGLETLSGL-PGIRVLSIEELLDTAAD-HDLP-QSRPDDLAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 298 VCFTSGTTGNPKGAMLTHGNVVADFSGflKVTEKVIFPrqDDVLISFLPLAHmfervIQSVVYCHggrvgffQGDIRLLS 377
Cdd:cd05906 172 LMLTSGSTGFPKAVPLTHRNILARSAG--KIQHNGLTP--QDVFLNWVPLDH-----VGGLVELH-------LRAVYLGC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 378 DDMKALRPTIFPVVPRLLNRMyDKifHQADTSlkrWLLEFA-AK-RKQAEVRSGiirnnSIWDelffnkiqasLGGHVRM 455
Cdd:cd05906 236 QQVHVPTEEILADPLRWLDLI-DR--YRVTIT---WAPNFAfALlNDLLEEIED-----GTWD----------LSSLRYL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 456 IVTGAAPASPTVLGFLRAALGCQVYE-----GYGQTECTAGCTFTTP---GDWTSGH----VGAPLPCNHIKLVDAEEln 523
Cdd:cd05906 295 VNAGEAVVAKTIRRLLRLLEPYGLPPdairpAFGMTETCSGVIYSRSfptYDHSQALefvsLGRPIPGVSMRIVDDEG-- 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75992911 524 ywTCKGEGEIC---VKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGkWLPEGTLKIIDRKK 582
Cdd:cd05906 373 --QLLPEGEVGrlqVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
245-603 |
2.96e-31 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 128.94 E-value: 2.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 245 GLKLVILMEPFEDALRERGKKCGVDIKSM-QAIEDCGR--------ENHHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTH 315
Cdd:PLN02246 122 GAKLIITQSCYVDKLKGLAEDDGVTVVTIdDPPEGCLHfseltqadENELPEVEISPDDVVALPYSSGTTGLPKGVMLTH 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 316 GNVVADfsgflkVTEKV------IFPRQDDVLISFLPLAHMFErvIQSVVYChGGRVG--------FfqgDIRLLSDDMK 381
Cdd:PLN02246 202 KGLVTS------VAQQVdgenpnLYFHSDDVILCVLPMFHIYS--LNSVLLC-GLRVGaailimpkF---EIGALLELIQ 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 382 ALRPTIFPVVPRLLnrmydkifhqadtslkrwlLEFAakrKQAEVRSgiirnnsiwDELffnkiqASlgghVRMIVTGAA 461
Cdd:PLN02246 270 RHKVTIAPFVPPIV-------------------LAIA---KSPVVEK---------YDL------SS----IRMVLSGAA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 462 PASPTVLGFLRAALGCQVY-EGYGQTE-------CTAgctFT-TPGDWTSGHVGAPLPCNHIKLVDAE---ELNYWTCkg 529
Cdd:PLN02246 309 PLGKELEDAFRAKLPNAVLgQGYGMTEagpvlamCLA---FAkEPFPVKSGSCGTVVRNAELKIVDPEtgaSLPRNQP-- 383
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75992911 530 eGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYI 603
Cdd:PLN02246 384 -GEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAELEALLI 455
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
293-638 |
3.10e-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: 126.69 E-value: 3.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 293 DDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF---LKVTEkvifprqDDVLISFLPLAHM--FERVIQSVVYchGGRVG 367
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSalnLGLTE-------DDNWLCALPLFHIsgLSILMRSVIY--GMTVY 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 368 FFQG-DIRLLSDDMKALRPTIFPVVPRLLNRMYdKIFHQADTSlkrwllefaakrkqaevrsgiirnnsiwdelffnkiq 446
Cdd:cd05912 148 LVDKfDAEQVLHLINSGKVTIISVVPTMLQRLL-EILGEGYPN------------------------------------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 447 aslggHVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTE-CTAGCTFTtPGDWTS--GHVGAPLPCNHIKLVDAEELN 523
Cdd:cd05912 190 -----NLRCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTEtCSQIVTLS-PEDALNkiGSAGKPLFPVELKIEDDGQPP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 524 YwtckGEGEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYI 603
Cdd:cd05912 263 Y----EVGEILLKGPNVTKGYLNRPDATEESFE-NGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLL 336
|
330 340 350
....*....|....*....|....*....|....*
gi 75992911 604 RSEPVAQIYVhgdslkaflVGIvvPDPEvmpsWAQ 638
Cdd:cd05912 337 SHPAIKEAGV---------VGI--PDDK----WGQ 356
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
147-631 |
3.48e-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: 128.80 E-value: 3.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 147 SYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIVD 226
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYG--LKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 227 KphKATLLLEHVERKeTPGLKLVILMEPFEDAlreRGKKCGVDIKSMQAIEDCGRENHHAPVPPRPDDLSIVCFTSGTTG 306
Cdd:cd17642 124 K--KGLQKVLNVQKK-LKIIKTIIILDSKEDY---KGYQCLYTFITQNLPPGFNEYDFKPPSFDRDEQVALIMNSSGSTG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 307 NPKGAMLTHGNVVADFSGflkvTEKVIF---PRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGffqgdirllsddmkal 383
Cdd:cd17642 198 LPKGVQLTHKNIVARFSH----ARDPIFgnqIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVV---------------- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 384 rptifpvvprLLNRMYDKIFHQA-------DTSLKRWLLEFAAKrkqaevrSGIIrnnsiwdelffNKIQASlggHVRMI 456
Cdd:cd17642 258 ----------LMYKFEEELFLRSlqdykvqSALLVPTLFAFFAK-------STLV-----------DKYDLS---NLHEI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 457 VTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYWTCKGEGEICV 535
Cdd:cd17642 307 ASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 536 KGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYVHG 615
Cdd:cd17642 387 KGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQHPKIFDAGVAG 465
|
490
....*....|....*.
gi 75992911 616 dslkaflvgivVPDPE 631
Cdd:cd17642 466 -----------IPDED 470
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
144-631 |
4.66e-31 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 126.25 E-value: 4.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 144 QWlSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTV 223
Cdd:cd05934 3 RW-TYAELLRESARIAAALAALGIRPGDR--VALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 224 IVDkphkatlllehverketpglklvilmePFEdalrergkkcgvdiksmqaiedcgrenhhapvpprpddlsiVCFTSG 303
Cdd:cd05934 80 VVD---------------------------PAS-----------------------------------------ILYTSG 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 304 TTGNPKGAMLTHGNVVadFSGFLKVTEKVIfpRQDDVLISFLPLAHM---FERVIQSVVycHGGRV--------GFFQGD 372
Cdd:cd05934 92 TTGPPKGVVITHANLT--FAGYYSARRFGL--GEDDVYLTVLPLFHInaqAVSVLAALS--VGATLvllprfsaSRFWSD 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 373 IRllsdDMKALRPTIFPVVPRLLNRmydkifhQADtslkrwllefAAKRKQAEVRsgiirnnsiwdelffnkiqaslggh 452
Cdd:cd05934 166 VR----RYGATVTNYLGAMLSYLLA-------QPP----------SPDDRAHRLR------------------------- 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 453 vrmiVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEelNYWTCKGE-G 531
Cdd:cd05934 200 ----AAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDD--GQELPAGEpG 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 532 EICVK---GPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSEPV 608
Cdd:cd05934 274 ELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVERAILRHPAV 351
|
490 500 510
....*....|....*....|....*....|
gi 75992911 609 AQIYVHG-------DSLKAFlvgIVVPDPE 631
Cdd:cd05934 352 REAAVVAvpdevgeDEVKAV---VVLRPGE 378
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
114-582 |
4.73e-31 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 129.30 E-value: 4.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 114 ARTMYQVFRRGLSISGNGPCLGF-------RKPEQpyqwLSYqevakrAEFLG-----SGLLqHDCKVGTEQFVGVFAQN 181
Cdd:PRK07529 24 PASTYELLSRAAARHPDAPALSFlldadplDRPET----WTY------AELLAdvtrtANLL-HSLGVGPGDVVAFLLPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 182 RPEWIIAELACYTYSmVVVPLYDTLGPGSISYIINTADICTVIVDKPHKATLLLEHVE--RKETPGLKLVI-------LM 252
Cdd:PRK07529 93 LPETHFALWGGEAAG-IANPINPLLEPEQIAELLRAAGAKVLVTLGPFPGTDIWQKVAevLAALPELRTVVevdlaryLP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 253 EPFEDALRERGKKCGVDIKSMQAIEDCGRENHH-APVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD-FSGFLkvte 330
Cdd:PRK07529 172 GPKRLAVPLIRRKAHARILDFDAELARQPGDRLfSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANaWLGAL---- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 331 kVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGR---VGFFQG--DIRLLSDDMK---ALRPTIFPVVPRLLNRMYDKI 402
Cdd:PRK07529 248 -LLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAhvvLATPQGyrGPGVIANFWKiveRYRINFLSGVPTVYAALLQVP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 403 FHQADTSLkrwlLEFAAkrkqaevrsgiirnnsiwdelffnkiqaslgghvrmivTGAAPASPTVLGFLRAALGCQVYEG 482
Cdd:PRK07529 327 VDGHDISS----LRYAL--------------------------------------CGAAPLPVEVFRRFEAATGVRIVEG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 483 YGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLVDAEEL-NYWT-C-KGE-GEICVKGPNVFKGYLkDEDRTKEALDS 557
Cdd:PRK07529 365 YGLTEATCVSSVNPPdGERRIGSVGLRLPYQRVRVVILDDAgRYLRdCaVDEvGVLCIAGPNVFSGYL-EAAHNKGLWLE 443
|
490 500
....*....|....*....|....*
gi 75992911 558 DGWLHTGDIGKWLPEGTLKIIDRKK 582
Cdd:PRK07529 444 DGWLNTGDLGRIDADGYFWLTGRAK 468
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
284-630 |
6.50e-31 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 127.30 E-value: 6.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 284 HHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGN------VVADFSGFlkvtekvifpRQDDVLISFLPLAH---MFerV 354
Cdd:PRK07514 147 DFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNllsnalTLVDYWRF----------TPDDVLIHALPIFHthgLF--V 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 355 IQSVVYCHGGRVGFFQG-DIRLLSDDMKalRPTIFPVVPRLLNRMYdkifhqADTSLKRwllEFAAkrkqaevrsgiirn 433
Cdd:PRK07514 215 ATNVALLAGASMIFLPKfDPDAVLALMP--RATVMMGVPTFYTRLL------QEPRLTR---EAAA-------------- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 434 nsiwdelffnkiqaslggHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTfTTP--GDWTSGHVGAPLPC 511
Cdd:PRK07514 270 ------------------HMRLFISGSAPLLAETHREFQERTGHAILERYGMTE-TNMNT-SNPydGERRAGTVGFPLPG 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 512 NHIKLVDAE---ELNywtcKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIfkL 587
Cdd:PRK07514 330 VSLRVTDPEtgaELP----PGEiGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDL--I 403
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 75992911 588 AQGEY-VAPEKIENiYIRSEP-VAQIYVHGDSLKAF---LVGIVVPDP 630
Cdd:PRK07514 404 ISGGYnVYPKEVEG-EIDELPgVVESAVIGVPHPDFgegVTAVVVPKP 450
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
146-615 |
1.05e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 127.58 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 225
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQPGDR--VGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVIC 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 DKPHKAT--------LLLEHVERKET-------PGLKLVILMEPFE-------DALRERGKkcGVdikSMQAIEDcgren 283
Cdd:PRK12583 124 ADAFKTSdyhamlqeLLPGLAEGQPGalacerlPELRGVVSLAPAPppgflawHELQARGE--TV---SREALAE----- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 284 hhAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSG-FLKVTEKvifprqdDVLISFLPLAHMFERVIqSVVY 360
Cdd:PRK12583 194 --RQASLDRDDPINIQYTSGTTGFPKGATLSHHNILnnGYFVAeSLGLTEH-------DRLCVPVPLYHCFGMVL-ANLG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 361 C--HGGRVGF----FQGDIRLLSddMKALRPTIFPVVPRL-LNRMYDKIFHQADTSlkrwllefaakrkqaEVRSGIIrn 433
Cdd:PRK12583 264 CmtVGACLVYpneaFDPLATLQA--VEEERCTALYGVPTMfIAELDHPQRGNFDLS---------------SLRTGIM-- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 434 nsiwdelffnkiqaslgghvrmivtGAAPASPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGD-----WTSghVGA 507
Cdd:PRK12583 325 -------------------------AGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSLQTTAADdlerrVET--VGR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 508 PLPCNHIKLVDAEELNywTCKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFk 586
Cdd:PRK12583 378 TQPHLEVKVVDPDGAT--VPRGEiGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMI- 454
|
490 500
....*....|....*....|....*....
gi 75992911 587 LAQGEYVAPEKIENIYIRSEPVAQIYVHG 615
Cdd:PRK12583 455 IRGGENIYPREIEEFLFTHPAVADVQVFG 483
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
280-632 |
1.34e-30 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 127.06 E-value: 1.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 280 GRENHHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADF--------SGFLKvtekvifPRQDDVLISF--LPLAH 349
Cdd:PRK07059 191 GARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqmeawlqPAFEK-------KPRPDQLNFVcaLPLYH 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 350 MFERVIQSVVYCHGGRVGFF---QGDIRLLSDDMKALRPTIFPVVPRLLNRMYdkifhqadtslkrwllefaakrkqaev 426
Cdd:PRK07059 264 IFALTVCGLLGMRTGGRNILipnPRDIPGFIKELKKYQVHIFPAVNTLYNALL--------------------------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 427 rsgiirNNSIWDELFFNKIQASLGGhvrmivtGAAPASPTVLGFLRAAlGCQVYEGYG--QTECTAGCTFTTPGDWTsGH 504
Cdd:PRK07059 317 ------NNPDFDKLDFSKLIVANGG-------GMAVQRPVAERWLEMT-GCPITEGYGlsETSPVATCNPVDATEFS-GT 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 505 VGAPLPCNHIKLVDAE--ELNYwtckGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRK 581
Cdd:PRK07059 382 IGLPLPSTEVSIRDDDgnDLPL----GEpGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRK 457
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 75992911 582 KHIFkLAQGEYVAPEKIENIyIRSEP----VAQIYVH----GDSLKAFlvgIVVPDPEV 632
Cdd:PRK07059 458 KDMI-LVSGFNVYPNEIEEV-VASHPgvleVAAVGVPdehsGEAVKLF---VVKKDPAL 511
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
294-624 |
1.70e-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: 122.61 E-value: 1.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 294 DLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTEkvifprqDDVLISFLPLAHMFErviqsvvYCHGGRVGFFQ 370
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLraaAAWADCADLTE-------DDRYLIINPFFHTFG-------YKAGIVACLLT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 371 G---------DIRLLSDDMKALRPTIFPVVPRLlnrmYDKIFHQADtslkrwllefaakRKQAEVRSgiirnnsiwdelf 441
Cdd:cd17638 67 GatvvpvavfDVDAILEAIERERITVLPGPPTL----FQSLLDHPG-------------RKKFDLSS------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 442 fnkiqaslgghVRMIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGcTFTTPGD---WTSGHVGAPLPCNHIKLV 517
Cdd:cd17638 117 -----------LRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVA-TMCRPGDdaeTVATTCGRACPGFEVRIA 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 518 DAeelnywtckgeGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEK 597
Cdd:cd17638 185 DD-----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAE 252
|
330 340 350
....*....|....*....|....*....|....
gi 75992911 598 IENIYIRSEPVAQIYV-------HGDSLKAFLVG 624
Cdd:cd17638 253 VEGALAEHPGVAQVAVigvpderMGEVGKAFVVA 286
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
137-631 |
4.70e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 125.46 E-value: 4.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 137 RKPEQPYQW-----LSYQEVAKRAEFLgSGLLQHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSI 211
Cdd:PRK08314 22 RYPDKTAIVfygraISYRELLEEAERL-AGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 212 SYIINTADICTVIVD-------KPHKATLLLEHV-------ERKETPGLKLvilmePfeDALRERGKKCGVDIKSMQAIE 277
Cdd:PRK08314 101 AHYVTDSGARVAIVGselapkvAPAVGNLRLRHVivaqysdYLPAEPEIAV-----P--AWLRAEPPLQALAPGGVVAWK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 278 DCGRENHHA-PVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD-FSGFLKVTEKVifprqDDVLISFLPLAHM--FER 353
Cdd:PRK08314 174 EALAAGLAPpPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANaVGSVLWSNSTP-----ESVVLAVLPLFHVtgMVH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 354 VIQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLL-NRMYDKIFHQADTSlkrwllefaakrkqaevrsgiir 432
Cdd:PRK08314 249 SMNAPIYAGATVVLMPRWDREAAARLIERYRVTHWTNIPTMVvDFLASPGLAERDLS----------------------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 433 nnsiwdelffnkiqaSLgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWT-SGHVGAPLPC 511
Cdd:PRK08314 306 ---------------SL----RYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTE-TMAQTHSNPPDRPkLQCLGIPTFG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 512 NHIKLVDAEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEA---LDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlA 588
Cdd:PRK08314 366 VDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMIN-A 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 75992911 589 QGEYVAPEKIENIYIRSEPVAQIYV-------HGDSLKAFlvgiVVPDPE 631
Cdd:PRK08314 445 SGFKVWPAEVENLLYKHPAIQEACViatpdprRGETVKAV----VVLRPE 490
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
280-623 |
7.66e-30 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 124.93 E-value: 7.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 280 GRENHHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKV------IFPRQDDVLISFLPLAHMFEr 353
Cdd:PRK12492 194 GRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLgpdgqpLMKEGQEVMIAPLPLYHIYA- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 354 viqsvvychggrvgfFQGDIRLLsddMKALRPTIFPVVPRLLNRMYDKifhqadtsLKRWLLefaakrkqaevrSGIIRN 433
Cdd:PRK12492 273 ---------------FTANCMCM---MVSGNHNVLITNPRDIPGFIKE--------LGKWRF------------SALLGL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 434 NSIWDELF----FNKIQASlggHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAP 508
Cdd:PRK12492 315 NTLFVALMdhpgFKDLDFS---ALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELARlGTVGIP 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 509 LPCNHIKLVDAE--ELNYwtckGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIF 585
Cdd:PRK12492 392 VPGTALKVIDDDgnELPL----GErGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLI 467
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 75992911 586 kLAQGEYVAPEKIENIYIRSEPVAQIYV-------HGDSLKAFLV 623
Cdd:PRK12492 468 -IVSGFNVYPNEIEDVVMAHPKVANCAAigvpderSGEAVKLFVV 511
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
146-631 |
2.50e-29 |
|
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: 121.43 E-value: 2.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLlqHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 225
Cdd:cd05935 2 LTYLELLEVVKKLASFL--SNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 dkphkatllleHVERketpglklvilmepfedalrergkkcgvdiksmqaiedcgrenhhapvpprpDDLSIVCFTSGTT 305
Cdd:cd05935 80 -----------GSEL----------------------------------------------------DDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 306 GNPKGAMLTHGNVVADFSGFLKVTEKVifprQDDVLISFLPLAHM--FERVIQSVVYCHGGRVGFFQGDIRLLSDDMKAL 383
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQSAVWTGLT----PSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMARWDRETALELIEKY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 384 RPTIFPVVPRLLNrmydkifhqadtslkrwllefaakrkqaevrsgiirnnsiwDELFFNKIQASLGGHVRMIVTGAAPA 463
Cdd:cd05935 173 KVTFWTNIPTMLV-----------------------------------------DLLATPEFKTRDLSSLKVLTGGGAPM 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 464 SPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYWTCKGEGEICVKGPNVFKG 543
Cdd:cd05935 212 PPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKG 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 544 YLKDEDRTKEALDSDG---WLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQIYV------- 613
Cdd:cd05935 292 YWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVisvpder 370
|
490
....*....|....*...
gi 75992911 614 HGDSLKAFlvgiVVPDPE 631
Cdd:cd05935 371 VGEEVKAF----IVLRPE 384
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
144-631 |
2.54e-29 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 122.66 E-value: 2.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 144 QWLSYQEVAKRAEFLgSGLLQHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTV 223
Cdd:PRK06839 26 EEMTYKQLHEYVSKV-AAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 224 IVDKPHKATLLLehverketpgLKLVILMEPFedalrergkkcgVDIKSMQAIEDCGRENHhapVPPRPDDLSIVCFTSG 303
Cdd:PRK06839 105 FVEKTFQNMALS----------MQKVSYVQRV------------ISITSLKEIEDRKIDNF---VEKNESASFIICYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 304 TTGNPKGAMLTHGNVvadfsgFLKVTEKV--IFPRQDDVLISFLPLAHMferviqsvvychgGRVGFFqgdirllsddmk 381
Cdd:PRK06839 160 TTGKPKGAVLTQENM------FWNALNNTfaIDLTMHDRSIVLLPLFHI-------------GGIGLF------------ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 382 ALrPTIFP----VVPRLLNRmyDKIFHQADTslKRWLLEFAAKRKQAEVRSGIIRNNSIWDelffnkiqaslggHVRMIV 457
Cdd:PRK06839 209 AF-PTLFAggviIVPRKFEP--TKALSMIEK--HKVTVVMGVPTIHQALINCSKFETTNLQ-------------SVRWFY 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 458 TGAAPAS-PTVLGFLRAalGCQVYEGYGQTEcTAGCTFTTPGD---WTSGHVGAPLPCNHIKLVDaEELNYWTCKGEGEI 533
Cdd:PRK06839 271 NGGAPCPeELMREFIDR--GFLFGQGFGMTE-TSPTVFMLSEEdarRKVGSIGKPVLFCDYELID-ENKNKVEVGEVGEL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 534 CVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIyirsepvaqIYV 613
Cdd:PRK06839 347 LIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQV---------INK 415
|
490
....*....|....*...
gi 75992911 614 HGDSLKAFLVGivVPDPE 631
Cdd:PRK06839 416 LSDVYEVAVVG--RQHVK 431
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
146-613 |
1.00e-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: 119.79 E-value: 1.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLLQhdCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADIctviv 225
Cdd:cd05903 2 LTYSELDTRADRLAAGLAA--LGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 dkphkatlllehverketpglKLVILMEPFedalrergkkcgvdiksmqaiedcgRENHHAPVPprpDDLSIVCFTSGTT 305
Cdd:cd05903 75 ---------------------KVFVVPERF-------------------------RQFDPAAMP---DAVALLLFTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 306 GNPKGAMLTHGNVVADFSGFLkvtEKVIFPRQDDVLISfLPLAHMferviqsVVYCHGGRVGFFQGDIRLLSDDMKALRp 385
Cdd:cd05903 106 GEPKGVMHSHNTLSASIRQYA---ERLGLGPGDVFLVA-SPMAHQ-------TGFVYGFTLPLLLGAPVVLQDIWDPDK- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 386 tifpvVPRLLNRMYDKIFHQADTSLKRWL--LEFAAKRKQaevrsgiirnnsiwdelffnkiqaslggHVRMIVTGAAPA 463
Cdd:cd05903 174 -----ALALMREHGVTFMMGATPFLTDLLnaVEEAGEPLS----------------------------RLRTFVCGGATV 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 464 SPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGD----WTSGhvGAPLPCNHIKLVDAEELNYwTCKGEGEICVKGPN 539
Cdd:cd05903 221 PRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPedrrLYTD--GRPLPGVEIKVVDDTGATL-APGVEGELLSRGPS 297
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75992911 540 VFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYV 613
Cdd:cd05903 298 VFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAV 369
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
273-613 |
3.77e-28 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 119.70 E-value: 3.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 273 MQAIEDCGRENHHAPVppRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADF-SGFLKVTEKVIfprQDDVLISFLPLAHMF 351
Cdd:PLN02330 166 LEAADRAGDTSDNEEI--LQTDLCALPFSSGTTGISKGVMLTHRNLVANLcSSLFSVGPEMI---GQVVTLGLIPFFHIY 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 352 --ERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYdkifhqadtslkrwllefaakrkqaevrsg 429
Cdd:PLN02330 241 giTGICCATLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLV------------------------------ 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 430 iirNNSIWDELFFNKIQaslgghVRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTagCTFTTPGDWTSGH---- 504
Cdd:PLN02330 291 ---KNPIVEEFDLSKLK------LQAIMTAAAPLAPELLtAFEAKFPGVQVQEAYGLTEHS--CITLTHGDPEKGHgiak 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 505 ---VGAPLPCNHIKLVDAEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRK 581
Cdd:PLN02330 360 knsVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRI 439
|
330 340 350
....*....|....*....|....*....|..
gi 75992911 582 KHIFKLaQGEYVAPEKIENIYIRSEPVAQIYV 613
Cdd:PLN02330 440 KELIKY-KGFQVAPAELEAILLTHPSVEDAAV 470
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
147-601 |
8.09e-28 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 118.70 E-value: 8.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 147 SYQEVAKRAEFLGSGLLQHDCKVGTeqfvgVFAQNRPEW---IIAELACYTYSMVVVPLYDTLGPGSISYIIN----TAD 219
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGD-----RVAFQLPGWcefTIIYLACLKVGAVSVPLLPSWREAELVWVLNkcqaKMF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 220 ICTVIVDKPHKATLLLEhvERKETPGLKLVILMEPFEDALRergkkcgvDIKSMQAIEDcgRENHHAPVPPRPDDLSIVC 299
Cdd:PRK06087 126 FAPTLFKQTRPVDLILP--LQNQLPQLQQIVGVDKLAPATS--------SLSLSQIIAD--YEPLTTAITTHGDELAAVL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 300 FTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifprQDDVLISFLPLAHmferviqSVVYCHGGRVGFFQGDIRLLSDD 379
Cdd:PRK06087 194 FTSGTEGLPKGVMLTHNNILASERAYCARLNLT----WQDVFMMPAPLGH-------ATGFLHGVTAPFLIGARSVLLDI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 380 MKALRPTifpvvpRLLNRmydkifhQADTslkrWLL---EFaakrkqaevrsgiirnnsIWDELffNKIQASlGGHV--- 453
Cdd:PRK06087 263 FTPDACL------ALLEQ-------QRCT----CMLgatPF------------------IYDLL--NLLEKQ-PADLsal 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 454 RMIVTGAAPASPTVLgflRAAL--GCQVYEGYGQTECTAGcTFTTPGD---WTSGHVGAPLPCNHIKLVDaEELNYWTCK 528
Cdd:PRK06087 305 RFFLCGGTTIPKKVA---RECQqrGIKLLSVYGSTESSPH-AVVNLDDplsRFMHTDGYAAAGVEIKVVD-EARKTLPPG 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75992911 529 GEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENI 601
Cdd:PRK06087 380 CEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDI 451
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
245-640 |
8.51e-28 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 117.16 E-value: 8.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 245 GLKLVILMEPFEDALRERGKKCGVDIKSMQAIEDCGRENHHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG 324
Cdd:cd05922 69 GGRIVLADAGAADRLRDALPASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 325 ---FLKVTEkvifprqDDVLISFLPLAhmferviqsvvYCHGGRV---GFFQGDIRLLSDDMkalrptifpVVPRLLnrm 398
Cdd:cd05922 149 iaeYLGITA-------DDRALTVLPLS-----------YDYGLSVlntHLLRGATLVLTNDG---------VLDDAF--- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 399 YDKIFHQADTSLkrwllefaakrkqaevrSGIIRNNSIWDELFFNKIQASlggHVRMIVTGAAPASPTVLGFLRAAL-GC 477
Cdd:cd05922 199 WEDLREHGATGL-----------------AGVPSTYAMLTRLGFDPAKLP---SLRYLTQAGGRLPQETIARLRELLpGA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 478 QVYEGYGQTECTAGCTFTTPG--DWTSGHVGAPLPCNHIKLVDAEELNYWTckGE-GEICVKGPNVFKGYLKDEDRTKEA 554
Cdd:cd05922 259 QVYVMYGQTEATRRMTYLPPEriLEKPGSIGLAIPGGEFEILDDDGTPTPP--GEpGEIVHRGPNVMKGYWNDPPYRRKE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 555 LDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIyIRSEP---VAQIYVHGDSLKAFLVGIVVPDPE 631
Cdd:cd05922 337 GRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF-GNRISPTEIEAA-ARSIGliiEAAAVGLPDPLGEKLALFVTAPDK 414
|
....*....
gi 75992911 632 VMPSWAQKK 640
Cdd:cd05922 415 IDPKDVLRS 423
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
146-638 |
1.17e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 117.78 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAE-----FLGSGLLQHDCkvgteqfVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADI 220
Cdd:PRK06188 38 LTYGQLADRISryiqaFEALGLGTGDA-------VALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 221 CTVIVDK---PHKATLLLEHVerketPGLKLVILMEPFEDalrergkkcGVDIKSMQAIEDcgrenhHAPVPP--RPDDL 295
Cdd:PRK06188 111 STLIVDPapfVERALALLARV-----PSLKHVLTLGPVPD---------GVDLLAAAAKFG------PAPLVAaaLPPDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 296 SIVCFTSGTTGNPKGAMLTHGNVV-------ADFSgflkvtekviFPRQddvlISFL---PLAH----MFERVIQsvvyc 361
Cdd:PRK06188 171 AGLAYTGGTTGKPKGVMGTHRSIAtmaqiqlAEWE----------WPAD----PRFLmctPLSHaggaFFLPTLL----- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 362 HGGRVGFFQG-DIRLLSDDMKALRPTIFPVVPRLLNRmydkifhqadtslkrwLLEFAAKRKqaevrsgiiRNNSiwdel 440
Cdd:PRK06188 232 RGGTVIVLAKfDPAEVLRAIEEQRITATFLVPTMIYA----------------LLDHPDLRT---------RDLS----- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 441 ffnkiqaSLgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHV------GAPLPCNHI 514
Cdd:PRK06188 282 -------SL----ETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLRV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 515 KLVDAEELNYWTckGE-GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYV 593
Cdd:PRK06188 351 ALLDEDGREVAQ--GEvGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMI-VTGGFNV 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 75992911 594 APEKIENIYIRSEPVAQIYV-------HGDSLKAflvgIVVPDPEVMPSWAQ 638
Cdd:PRK06188 427 FPREVEDVLAEHPAVAQVAVigvpdekWGEAVTA----VVVLRPGAAVDAAE 474
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
148-615 |
1.81e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 116.60 E-value: 1.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 148 YQEVAKRAEFLGSGLLQHDckvgteQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIVDk 227
Cdd:PRK03640 34 HEAVVSVAGKLAALGVKKG------DRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITD- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 228 phkatlllehverketpglklvilmEPFEDALRErgkKCGVDIKSMQAiedcGRENHHAPVPPRP-DDLSIVCFTSGTTG 306
Cdd:PRK03640 107 -------------------------DDFEAKLIP---GISVKFAELMN----GPKEEAEIQEEFDlDEVATIMYTSGTTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 307 NPKGAMLTHGNVVADFSGF---LKVTEKvifprqDDVLISfLPLAHM--FERVIQSVVYchGGRVGFFQG-DIRLLSDDM 380
Cdd:PRK03640 155 KPKGVIQTYGNHWWSAVGSalnLGLTED------DCWLAA-VPIFHIsgLSILMRSVIY--GMRVVLVEKfDAEKINKLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 381 KALRPTIFPVVPRLLNRMYDKIFhqadtslkrwllefaakrkqaevrsgiirnnsiwdelffnkiQASLGGHVRMIVTGA 460
Cdd:PRK03640 226 QTGGVTIISVVSTMLQRLLERLG------------------------------------------EGTYPSSFRCMLLGG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 461 APASPTVLGFLRAAlGCQVYEGYGQTEcTAGCTFTTPGDWTS---GHVGAPL-PCNhIKLVDaeELNYWTCKGEGEICVK 536
Cdd:PRK03640 264 GPAPKPLLEQCKEK-GIPVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLfPCE-LKIEK--DGVVVPPFEEGEIVVK 338
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75992911 537 GPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYVHG 615
Cdd:PRK03640 339 GPNVTKGYLNREDATRETFQ-DGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPGVAEAGVVG 415
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
139-633 |
2.84e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 116.83 E-value: 2.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 139 PEQPYQWlSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVV---PLYDTlgpGSISYII 215
Cdd:PRK08315 38 RDQGLRW-TYREFNEEVDALAKGLLALGIEKGDR--VGIWAPNVPEWVLTQFATAKIGAILVtinPAYRL---SELEYAL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 216 NTADICT-VIVDK--------------PHKATLLLEHVERKETPGLKLVILMepfeDALRERGkkcgvdIKSMQAIEDCG 280
Cdd:PRK08315 112 NQSGCKAlIAADGfkdsdyvamlyelaPELATCEPGQLQSARLPELRRVIFL----GDEKHPG------MLNFDELLALG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 281 RENHHAPVPPR-----PDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsGFLkVTEKVIFPRQDDVLISfLPLAHMFERVI 355
Cdd:PRK08315 182 RAVDDAELAARqatldPDDPINIQYTSGTTGFPKGATLTHRNILNN--GYF-IGEAMKLTEEDRLCIP-VPLYHCFGMVL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 356 qSVVYC--HGGRV-----GFfqgdirllsDDMKALR-------------PTIFPVVprlLNrmyDKIFHQAD-TSLkrwl 414
Cdd:PRK08315 258 -GNLACvtHGATMvypgeGF---------DPLATLAaveeerctalygvPTMFIAE---LD---HPDFARFDlSSL---- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 415 lefaakrkqaevRSGIirnnsiwdelffnkiqaslgghvrMivtgAAPASPT-----VLGFLRAAlgcQVYEGYGQTECT 489
Cdd:PRK08315 318 ------------RTGI------------------------M----AGSPCPIevmkrVIDKMHMS---EVTIAYGMTETS 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 490 AGCTFTTPGD------WTsghVGAPLPCNHIKLVDAEelnywTCK----GE-GEICVKGPNVFKGYLKDEDRTKEALDSD 558
Cdd:PRK08315 355 PVSTQTRTDDplekrvTT---VGRALPHLEVKIVDPE-----TGEtvprGEqGELCTRGYSVMKGYWNDPEKTAEAIDAD 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75992911 559 GWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIyirsepvaqIYVHGDSLKAFLVGivVPDP----EVM 633
Cdd:PRK08315 427 GWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEF---------LYTHPKIQDVQVVG--VPDEkygeEVC 493
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
137-594 |
4.61e-27 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 116.90 E-value: 4.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 137 RKPEQPYQWLSYQEVAKRAEFLGSGLLqhDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLydtlgpgSISYIIN 216
Cdd:PRK08180 61 RGADGGWRRLTYAEALERVRAIAQALL--DRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPV-------SPAYSLV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 217 TADIctvivDKphkatllLEHVERKETPGLKLVILMEPFEDALRE-----------RGKKCGVDIKSMQAIEDCGR---- 281
Cdd:PRK08180 132 SQDF-----GK-------LRHVLELLTPGLVFADDGAAFARALAAvvpadvevvavRGAVPGRAATPFAALLATPPtaav 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 282 ENHHAPVppRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekVIFPRQDD-VLISFLPLAHMF-ERVIQSVV 359
Cdd:PRK08180 200 DAAHAAV--GPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQT---FPFLAEEPpVLVDWLPWNHTFgGNHNLGIV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 360 YCHGGR---------VGFFQGDIRLLsddmKALRPTIFPVVPRLlnrmydkifhqadtslkrWLLEFAAKRKQAEVRsgi 430
Cdd:PRK08180 275 LYNGGTlyiddgkptPGGFDETLRNL----REISPTVYFNVPKG------------------WEMLVPALERDAALR--- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 431 irnnsiwdELFFNKiqaslgghVRMIVTGAAPASPTVLGFL----RAALGCQVY--EGYGQTECTAGCTFTTPGDWTSGH 504
Cdd:PRK08180 330 --------RRFFSR--------LKLLFYAGAALSQDVWDRLdrvaEATCGERIRmmTGLGMTETAPSATFTTGPLSRAGN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 505 VGAPLPCNHIKLVDAEelnywtckGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWL----PEGTLKIIDR 580
Cdd:PRK08180 394 IGLPAPGCEVKLVPVG--------GKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVdpadPERGLMFDGR 465
|
490
....*....|....
gi 75992911 581 KKHIFKLAQGEYVA 594
Cdd:PRK08180 466 IAEDFKLSSGTWVS 479
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
144-575 |
5.65e-27 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 118.04 E-value: 5.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 144 QWLSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELA------CYtysmvvVPLYDTLGPGSISYIINT 217
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALG--VGPGDLVGVCLERSLEMVVALLAvlkagaAY------VPLDPAYPAERLAYMLED 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 218 ADICTVIVDKPHKATLllehverkETPGLKLVILmepfeDALrergkkcgvdiksmqAIEDCGRENhhAPVPPRPDDLSI 297
Cdd:COG1020 572 AGARLVLTQSALAARL--------PELGVPVLAL-----DAL---------------ALAAEPATN--PPVPVTPDDLAY 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 298 VCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTEkvifprQDDVL----ISF--------LPLahmferviqsvvyCH 362
Cdd:COG1020 622 VIYTSGSTGRPKGVMVEHRALVnllAWMQRRYGLGP------GDRVLqfasLSFdasvweifGAL-------------LS 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 363 GGRVGFFQGDIRL----LSDDMKALRPTIFPVVPRLLNRmydkifhqadtslkrwLLEFAAKRkqaevrsgiirnnsiwd 438
Cdd:COG1020 683 GATLVLAPPEARRdpaaLAELLARHRVTVLNLTPSLLRA----------------LLDAAPEA----------------- 729
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 439 elffnkiqaslGGHVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTF--TTPGDWTSGHV--GAPLPCNH 513
Cdd:COG1020 730 -----------LPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTVDSTYyeVTPPDADGGSVpiGRPIANTR 798
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75992911 514 IKLVDAEelnywtckGE-------GEICVKGPNVFKGYLKDEDRTKEA-----LDSDG--WLHTGDIGKWLPEGTL 575
Cdd:COG1020 799 VYVLDAH--------LQpvpvgvpGELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNL 866
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
137-630 |
7.25e-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: 115.42 E-value: 7.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 137 RKPEQPYQWLSYQEVAKRAEFLGSGLlqHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIIN 216
Cdd:cd12119 17 RTHEGEVHRYTYAEVAERARRLANAL--RRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 217 TADICTVIVDkphkATLL---------LEHVERketpglklVILMEPFEDALRERGKKcgvDIKSMQAIEDcgrenhHAP 287
Cdd:cd12119 95 HAEDRVVFVD----RDFLplleaiaprLPTVEH--------VVVMTDDAAMPEPAGVG---VLAYEELLAA------ESP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 288 VPPRPD----DLSIVCFTSGTTGNPKGAMLTHGNVV--------ADFSGFlkvtekvifpRQDDVLISFLPLAHM----- 350
Cdd:cd12119 154 EYDWPDfdenTAAAICYTSGTTGNPKGVVYSHRSLVlhamaallTDGLGL----------SESDVVLPVVPMFHVnawgl 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 351 -FERVIQSVVYCHGGRvgFFQGDirLLSDDMKALRPTIFPVVPRLlnrmydkifhqadtslkrWLLefaakrkqaeVRSG 429
Cdd:cd12119 224 pYAAAMVGAKLVLPGP--YLDPA--SLAELIEREGVTFAAGVPTV------------------WQG----------LLDH 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 430 IIRNNSiwdELFfnkiqaslggHVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPgdwTSGHV---- 505
Cdd:cd12119 272 LEANGR---DLS----------SLRRVVIGGSAVPRSLIEAFEE-RGVRVIHAWGMTETSPLGTVARP---PSEHSnlse 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 506 ----------GAPLPCNHIKLVDAE--ELNyWTCKGEGEICVKGPNVFKGYLKDeDRTKEALDSDGWLHTGDIGKWLPEG 573
Cdd:cd12119 335 deqlalrakqGRPVPGVELRIVDDDgrELP-WDGKAVGELQVRGPWVTKSYYKN-DEESEALTEDGWLRTGDVATIDEDG 412
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 75992911 574 TLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQIYVhgdslkaflvgIVVPDP 630
Cdd:cd12119 413 YLTITDRSKDVIKSG-GEWISSVELENAIMAHPAVAEAAV-----------IGVPHP 457
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
187-599 |
8.12e-27 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 117.33 E-value: 8.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 187 IAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIVDKPhkatlLLEHVERK----ETPGLKLVILMEPFEDALRER 262
Cdd:PRK08633 680 LANLALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVITSRK-----FLEKLKNKgfdlELPENVKVIYLEDLKAKISKV 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 263 GKKC-GVDIKSMQA--IEDCGRENHHapvpprPDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgfLKVTEKVIFPRQDD 339
Cdd:PRK08633 755 DKLTaLLAARLLPArlLKRLYGPTFK------PDDTATIIFSSGSEGEPKGVMLSHHNILSN----IEQISDVFNLRNDD 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 340 VLISFLPLAHMFE-RVIQSVVYCHGGRVGFFqgdirllSDDMKAL---------RPTIFPVVPRLLnRMYdkifhqadts 409
Cdd:PRK08633 825 VILSSLPFFHSFGlTVTLWLPLLEGIKVVYH-------PDPTDALgiaklvakhRATILLGTPTFL-RLY---------- 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 410 lkrwllefaakrkqaevrsgiIRNNSIWDELFfnkiqASLgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECT 489
Cdd:PRK08633 887 ---------------------LRNKKLHPLMF-----ASL----RLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETS 936
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 490 AGCTFTTP-----GDWT-----SGHVGAPLPCNHIKLVDAEelNYWTCKG--EGEICVKGPNVFKGYLKDEDRTKEAL-- 555
Cdd:PRK08633 937 PVASVNLPdvlaaDFKRqtgskEGSVGMPLPGVAVRIVDPE--TFEELPPgeDGLILIGGPQVMKGYLGDPEKTAEVIkd 1014
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 75992911 556 -DSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIE 599
Cdd:PRK08633 1015 iDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIG-GEMVPLGAVE 1058
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
144-629 |
1.22e-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: 113.93 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 144 QWLSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTV 223
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARG--VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 224 IVDkphkatlllehverketpglklvilmepfeDALRERGKKCGVDIksMQAIEDCGRENHHAPVPPRPDDLSIVCFTSG 303
Cdd:cd12116 89 LTD------------------------------DALPDRLPAGLPVL--LLALAAAAAAPAAPRTPVSPDDLAYVIYTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 304 TTGNPKGAMLTHGNVVADFSGFlkvTEKVIFPRQDDVL--------IS----FLPLahmferviqsvvyCHGGRVGFFQG 371
Cdd:cd12116 137 STGRPKGVVVSHRNLVNFLHSM---RERLGLGPGDRLLavttyafdISllelLLPL-------------LAGARVVIAPR 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 372 DI----RLLSDDMKALRPTIFpvvprllnrmydkifhQADTSLKRWLLEfaakrkqaevrSGiirnnsiWDELffnkiqa 447
Cdd:cd12116 201 ETqrdpEALARLIEAHSITVM----------------QATPATWRMLLD-----------AG-------WQGR------- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 448 slgGHVRMIVTGAApaSPTVLGFLRAALGCQVYEGYGQTECT--AGCTFTTPGDwTSGHVGAPLPCNHIKLVDAEelnyw 525
Cdd:cd12116 240 ---AGLTALCGGEA--LPPDLAARLLSRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLDAA----- 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 526 tckGE-------GEICVKGPNVFKGYLKDEDRTKEALDSDGWLH-------TGDIGKWLPEGTLKIIDRKKHIFKLaQGE 591
Cdd:cd12116 309 ---LRpvppgvpGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQVKI-RGH 384
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 75992911 592 YVAPEKIENIYIRSEPVAQ--IYVHGDSLKAFLVGIVVPD 629
Cdd:cd12116 385 RIELGEIEAALAAHPGVAQaaVVVREDGGDRRLVAYVVLK 424
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
289-629 |
5.35e-26 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 111.63 E-value: 5.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 289 PPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPLAhmFERVIQSV--VYCHGGRV 366
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLN----YVSQPPARLDVGPGSRVAQVLSIA--FDACIGEIfsTLCNGGTL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 367 gFFQGDIRLLSDDMKALrpTIFPVVPRLLNrMYDkifhqaDTSLKRwllefaakrkqaevrsgiirnnsiwdelffnkiq 446
Cdd:cd17653 175 -VLADPSDPFAHVARTV--DALMSTPSILS-TLS------PQDFPN---------------------------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 447 aslgghVRMIVTGAAPASPTVLGflRAALGCQVYEGYGQTECTAGCTFT--TPGDWTsgHVGAPLPCNHIKLVDAEELNY 524
Cdd:cd17653 211 ------LKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTelLPGQPV--TIGKPIPNSTCYILDADLQPV 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 525 wTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLH------TGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKI 598
Cdd:cd17653 281 -PEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPgsrmyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEI 358
|
330 340 350
....*....|....*....|....*....|....
gi 75992911 599 ENIYIRSEPVAQ---IYVHGDSLKAFlvgiVVPD 629
Cdd:cd17653 359 EEVVLQSQPEVTqaaAIVVNGRLVAF----VTPE 388
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
287-603 |
6.16e-26 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 113.01 E-value: 6.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 287 PVPP-RPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKV-TEKVIFPRQDDVLISFLPLAHMFerviqsvvychgG 364
Cdd:PLN02574 191 PKPViKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFeASQYEYPGSDNVYLAALPMFHIY------------G 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 365 RVGFFQGDIRL-----------LSDDMKAL---RPTIFPVVPRLLnrmydkifhqadTSLKRwllefAAKRKQAEVRsgi 430
Cdd:PLN02574 259 LSLFVVGLLSLgstivvmrrfdASDMVKVIdrfKVTHFPVVPPIL------------MALTK-----KAKGVCGEVL--- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 431 irnnsiwdelffnkiqaslgGHVRMIVTGAAPAS-PTVLGFLRAALGCQVYEGYGQTECTAGCT--FTTPGDWTSGHVGA 507
Cdd:PLN02574 319 --------------------KSLKQVSCGAAPLSgKFIQDFVQTLPHVDFIQGYGMTESTAVGTrgFNTEKLSKYSSVGL 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 508 PLPCNHIKLVDAEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKL 587
Cdd:PLN02574 379 LAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY 458
|
330
....*....|....*.
gi 75992911 588 aQGEYVAPEKIENIYI 603
Cdd:PLN02574 459 -KGFQIAPADLEAVLI 473
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
285-635 |
6.95e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 111.62 E-value: 6.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 285 HAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifprQDDVLISFLPLAHMferviqsvvycHGG 364
Cdd:PRK07787 120 HRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWT----ADDVLVHGLPLFHV-----------HGL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 365 RVGFFqGDIRLLSDDMKALRPTIFPVVPRLLNR---------MYDKIfhQADTSLKRwllefaakrkqaevrsgiirnns 435
Cdd:PRK07787 185 VLGVL-GPLRIGNRFVHTGRPTPEAYAQALSEGgtlyfgvptVWSRI--AADPEAAR----------------------- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 436 iwdelffnkiqaSLGGhVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIK 515
Cdd:PRK07787 239 ------------ALRG-ARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 516 LVDaEELNYWTCKGE--GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDR------KKHIFKL 587
Cdd:PRK07787 306 LVD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGGYRI 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 75992911 588 AQGEyvapekIENIYIRSEPVAQIYVHG---DSLKAFLVGIVVPDPEVMPS 635
Cdd:PRK07787 385 GAGE------IETALLGHPGVREAAVVGvpdDDLGQRIVAYVVGADDVAAD 429
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
137-631 |
1.17e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 112.06 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 137 RKPEQP----Y-QWLSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSI 211
Cdd:PRK06178 45 ERPQRPaiifYgHVITYAELDELSDRFAALLRQRG--VGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 212 SYIINTADICTVIV-D------KPHKATLLLEHVErkeTPGLKLVILMEP---FEDALRERGKKCGVDIKSMQAIEDCGR 281
Cdd:PRK06178 123 SYELNDAGAEVLLAlDqlapvvEQVRAETSLRHVI---VTSLADVLPAEPtlpLPDSLRAPRLAAAGAIDLLPALRACTA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 282 ENhhAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifpRQDDVLISFLPlahMFerviqsvvyc 361
Cdd:PRK06178 200 PV--PLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVG---GEDSVFLSFLP---EF---------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 362 hggrvgFFQGDirllsdDMKALRPTIF--PVVprLLNRmYDkifhqADTSLKrwllefAAKRKQAEVRSGIIRNnsiWDE 439
Cdd:PRK06178 262 ------WIAGE------NFGLLFPLFSgaTLV--LLAR-WD-----AVAFMA------AVERYRVTRTVMLVDN---AVE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 440 LF----FNKIQASLGGHVRmIVTGAAPASPTVLGFLRAALGCQVYEG-YGQTECTAGCTFTTpGDWTSGH--------VG 506
Cdd:PRK06178 313 LMdhprFAEYDLSSLRQVR-VVSFVKKLNPDYRQRWRALTGSVLAEAaWGMTETHTCDTFTA-GFQDDDFdllsqpvfVG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 507 APLPCNHIKLVDAEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFK 586
Cdd:PRK06178 391 LPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLK 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 75992911 587 LaQGEYVAPEKIENIYIRsepvaqiyvHGDSLKAFLVGivVPDPE 631
Cdd:PRK06178 470 V-NGMSVFPSEVEALLGQ---------HPAVLGSAVVG--RPDPD 502
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
145-582 |
1.69e-25 |
|
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: 111.18 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 145 WLSYQEVAKRAEFLGSGLLQHdCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGS---ISYIINTADIC 221
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAV-GKPGDR--VLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 222 TVIVDKPHKAtLLLEHVERKETPGLKLVILMEPFEDALRERGkkcgvdiksmqaiedcgrenhhAPVPPRPDDLSIVCFT 301
Cdd:cd05931 101 VVLTTAAALA-AVRAFAASRPAAGTPRLLVVDLLPDTSAADW----------------------PPPSPDPDDIAYLQYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 302 SGTTGNPKGAMLTHGNVVADFSGFLkvteKVIFPRQDDVLISFLPLAH---MFERVIQSVVYchGGRVGFFQgdirllsd 378
Cdd:cd05931 158 SGSTGTPKGVVVTHRNLLANVRQIR----RAYGLDPGDVVVSWLPLYHdmgLIGGLLTPLYS--GGPSVLMS-------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 379 dmkalrPTIFpvvprlLNRMYdkifhqadtslkRWL-----------------LEFAAKRKQAEVRSGIirnnsiwdELf 441
Cdd:cd05931 224 ------PAAF------LRRPL------------RWLrlisryratisaapnfaYDLCVRRVRDEDLEGL--------DL- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 442 fnkiqaslgGHVRMIVTGAAPASPTVL----------GFLRAAlgcqVYEGYGQTECTAGCTFTTPG----------DWT 501
Cdd:cd05931 271 ---------SSWRVALNGAEPVRPATLrrfaeafapfGFRPEA----FRPSYGLAEATLFVSGGPPGtgpvvlrvdrDAL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 502 SGHV----------------GAPLPCNHIKLVDAEelnywTCK-----GEGEICVKGPNVFKGYLKDEDRTKE------A 554
Cdd:cd05931 338 AGRAvavaaddpaarelvscGRPLPDQEVRIVDPE-----TGRelpdgEVGEIWVRGPSVASGYWGRPEATAEtfgalaA 412
|
490 500
....*....|....*....|....*...
gi 75992911 555 LDSDGWLHTGDIGkWLPEGTLKIIDRKK 582
Cdd:cd05931 413 TDEGGWLRTGDLG-FLHDGELYITGRLK 439
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
146-623 |
2.74e-25 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 109.35 E-value: 2.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLLQHDCKVGteQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 225
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKG--DRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 DKphkatlllehverketpglklvilmepfedalrergkkcgvdiksmqaiedcgrenhhapvpprpDDLSIVCFTSGTT 305
Cdd:cd05972 79 DA-----------------------------------------------------------------EDPALIYFTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 306 GNPKGAMLTHG---NVVADFSGFLKVTEKVIFPRQDD------VLISFL-PLAHMFerviqSVVYCHGGRvgffqgdirl 375
Cdd:cd05972 94 GLPKGVLHTHSyplGHIPTAAYWLGLRPDDIHWNIADpgwakgAWSSFFgPWLLGA-----TVFVYEGPR---------- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 376 lsddMKALRptifpvVPRLLNRMYDKIFHQADTSLKRWLLEFAAKRKQaevrsgiirnnsiwdelffnkiqaslgGHVRM 455
Cdd:cd05972 159 ----FDAER------ILELLERYGVTSFCGPPTAYRMLIKQDLSSYKF---------------------------SHLRL 201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 456 IVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAE--ELNYWTckgEGEI 533
Cdd:cd05972 202 VVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDgrELPPGE---EGDI 278
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 534 CVKGPNV--FKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSEPVAQI 611
Cdd:cd05972 279 AIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVESALLEHPAVAEA 356
|
490
....*....|....*....
gi 75992911 612 YV-------HGDSLKAFLV 623
Cdd:cd05972 357 AVvgspdpvRGEVVKAFVV 375
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
132-630 |
4.98e-25 |
|
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: 110.21 E-value: 4.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 132 PCLGFRKPEQPYQWLSYQEVAKRAEFLGSGLLQHDCKVgtEQFVGVFAQNRPEWIIAELACYTysmVVVPLydtlGPGSI 211
Cdd:cd05921 12 TWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGLSA--ERPLLILSGNSIEHALMALAAMY---AGVPA----APVSP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 212 SYIINTADIctvivDKphkatllLEHVERKETPGLKLVILMEPFEDALRERgKKCGVDIKSMQAIEDCGRENHHAPV--- 288
Cdd:cd05921 83 AYSLMSQDL-----AK-------LKHLFELLKPGLVFAQDAAPFARALAAI-FPLGTPLVVSRNAVAGRGAISFAELaat 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 289 PPR-----------PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekviFPRQDD---VLISFLPLAHMF--E 352
Cdd:cd05921 150 PPTaavdaafaavgPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQT-----YPFFGEeppVLVDWLPWNHTFggN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 353 RVIQSVVYcHGGRV---------GFFQGDIRLLSDDMkalrPTIFPVVPR----LLNRMYDkifhqaDTSLKRwllEFAA 419
Cdd:cd05921 225 HNFNLVLY-NGGTLyiddgkpmpGGFEETLRNLREIS----PTVYFNVPAgwemLVAALEK------DEALRR---RFFK 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 420 KRKQAEVrSGIIRNNSIWDELFFNKIQaSLGGHVRMivtgaapasptvlgflraalgcqvYEGYGQTECTAGCTFTTPGD 499
Cdd:cd05921 291 RLKLMFY-AGAGLSQDVWDRLQALAVA-TVGERIPM------------------------MAGLGATETAPTATFTHWPT 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 500 WTSGHVGAPLPCNHIKLVdaeelnywTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWL----PEGTL 575
Cdd:cd05921 345 ERSGLIGLPAPGTELKLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpddPAKGL 416
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75992911 576 KIIDRKKHIFKLAQGEYVA--PekieniyIRSEPVAQI--YVHgDSL-----KAFLVGIVVPDP 630
Cdd:cd05921 417 VFDGRVAEDFKLASGTWVSvgP-------LRARAVAACapLVH-DAVvagedRAEVGALVFPDL 472
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
136-615 |
7.72e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 109.48 E-value: 7.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 136 FRKPEQPY-----QWLSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGS 210
Cdd:PRK07786 28 LMQPDAPAlrflgNTTTWRELDDRVAALAGALSRRG--VGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 211 ISYIINTADiCTVIVDKPHKATLLLEhvERKETPGLKLVILMEP--------FEDALRERGKKcgvdiksmqaiedcgre 282
Cdd:PRK07786 106 IAFLVSDCG-AHVVVTEAALAPVATA--VRDIVPLLSTVVVAGGssddsvlgYEDLLAEAGPA----------------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 283 nhHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkviFPRQDDVLISFLPLAHMfeRVIQSVVych 362
Cdd:PRK07786 166 --HAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNG---ADINSDVGFVGVPLFHI--AGIGSML--- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 363 ggrVGFFQGdirllsddmkalRPT-IFPVVPRLLNRMYDKIFHQADTSL----KRWLLEFAAKRKQAevrsgiiRNNSIw 437
Cdd:PRK07786 236 ---PGLLLG------------APTvIYPLGAFDPGQLLDVLEAEKVTGIflvpAQWQAVCAEQQARP-------RDLAL- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 438 delffnkiqaslgghvRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAgCTFTTPGD---WTSGHVGAPLPCNH 513
Cdd:PRK07786 293 ----------------RVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEMSP-VTCMLLGEdaiRKLGSVGKVIPTVA 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 514 IKLVDaEELNYwTCKGE-GEICVKGPNVFKGYLKDEDRTKEALDSdGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEY 592
Cdd:PRK07786 356 ARVVD-ENMND-VPVGEvGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGEN 431
|
490 500
....*....|....*....|...
gi 75992911 593 VAPEKIENIYIRSEPVAQIYVHG 615
Cdd:PRK07786 432 IYCAEVENVLASHPDIVEVAVIG 454
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
136-613 |
2.62e-24 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 107.03 E-value: 2.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 136 FRKPEQPY-----QWLSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLydtlGPGS 210
Cdd:cd17655 8 EKTPDHTAvvfedQTLTYRELNERANQLARTLREKG--VGPDTIVGIMAERSLEMIVGILGILKAGGAYLPI----DPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 211 ----ISYIINTADictvivdkphkATLLL--EHVERKETpGLKLVILMEpfEDALRERGKkcgvdiksmqaiedcgrENH 284
Cdd:cd17655 82 peerIQYILEDSG-----------ADILLtqSHLQPPIA-FIGLIDLLD--EDTIYHEES-----------------ENL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 285 HAPVppRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkvtEKVIFPRQDDVLISFLPLAhmFERVIQSvvychgg 364
Cdd:cd17655 131 EPVS--KSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWA----NKVIYQGEHLRVALFASIS--FDASVTE------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 365 rvgffqgdirllsddmkalrptIFPvvPRLL-NRMYdkIFHQADTSLKRWLLEFAAKRkqaevRSGIIR-NNSIWDELff 442
Cdd:cd17655 196 ----------------------IFA--SLLSgNTLY--IVRKETVLDGQALTQYIRQN-----RITIIDlTPAHLKLL-- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 443 NKIQASLGGHVRMIVTGAAPASPTVLGFL--RAALGCQVYEGYGQTECTAGCTF--TTPGDWTSGHV--GAPLPCNHIKL 516
Cdd:cd17655 243 DAADDSEGLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETTVDASIyqYEPETDQQVSVpiGKPLGNTRIYI 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 517 VDaEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWL------HTGDIGKWLPEGTLKIIDRKKHIFKLaQG 590
Cdd:cd17655 323 LD-QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-RG 400
|
490 500
....*....|....*....|...
gi 75992911 591 EYVAPEKIENIYIRSEPVAQIYV 613
Cdd:cd17655 401 YRIELGEIEARLLQHPDIKEAVV 423
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
292-609 |
3.94e-24 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 104.48 E-value: 3.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgfLKVTEKVIFPRQDDVLISFLPLAHMFERVIQsvvychgGRVGFFQG 371
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYN----AWMLALNSLFDPDDVLLCGLPLFHVNGSVVT-------LLTPLASG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 372 DIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTSLkrwllefaAKRKQAEVRSGIirnnsiwdelffnkiqaslgG 451
Cdd:cd05944 70 AHVVLAGPAGYRNPGLFDNFWKLVERYRITSLSTVPTVY--------AALLQVPVNADI--------------------S 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 452 HVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLV--DAEELNYWTCK 528
Cdd:cd05944 122 SLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKvlDGVGRLLRDCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 529 GE--GEICVKGPNVFKGYLKDEDRtKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSE 606
Cdd:cd05944 202 PDevGEICVAGPGVFGGYLYTEGN-KNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLRHP 279
|
...
gi 75992911 607 PVA 609
Cdd:cd05944 280 AVA 282
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
245-599 |
1.72e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 105.08 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 245 GLKLVILMEPFEDA---LRERGKKcgvdiksMQAIEDCGRENHHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD 321
Cdd:PRK07768 108 GAKAVVVGEPFLAAapvLEEKGIR-------VLTVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYAN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 322 FSGflkVTEKVIFPRQDDVLISFLPLAH-MferviqsvvychgGRVGFfqgdirlLSDDMKA------LRPTIFPVVPRL 394
Cdd:PRK07768 181 AEA---MFVAAEFDVETDVMVSWLPLFHdM-------------GMVGF-------LTVPMYFgaelvkVTPMDFLRDPLL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 395 LNRMYDKifHQADT--------SLKRWLLEFAAKRKQAEVRSgiirnnsiwdelffnkiqaslgghVRMIVTGAAPASPT 466
Cdd:PRK07768 238 WAELISK--YRGTMtaapnfayALLARRLRRQAKPGAFDLSS------------------------LRFALNGAEPIDPA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 467 VL----------GFLRAALGCqvyeGYGQTECTAGCTFTTPGD--------------------WTSGHV------GAPLP 510
Cdd:PRK07768 292 DVedlldagarfGLRPEAILP----AYGMAEATLAVSFSPCGAglvvdevdadllaalrravpATKGNTrrlatlGPPLP 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 511 CNHIKLVDaEELNYWTCKGEGEICVKGPNVFKGYLkDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqG 590
Cdd:PRK07768 368 GLEVRVVD-EDGQVLPPRGVGVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-G 444
|
....*....
gi 75992911 591 EYVAPEKIE 599
Cdd:PRK07768 445 RNIYPTDIE 453
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
294-635 |
2.73e-23 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 101.25 E-value: 2.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 294 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkVTEKVIFPRQDDVLISfLPLAHM--FERVIQSVVycHGGRVGFFQG 371
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAG---LHSRLGFGGGDSWLLS-LPLYHVggLAILVRSLL--AGAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 372 DiRLLSDDMKALRPTIFPVVPRLLNRMYDKifHQADTSLKRwllefaakrkqaevrsgiirnnsiwdelffnkiqaslgg 451
Cdd:cd17630 75 N-QALAEDLAPPGVTHVSLVPTQLQRLLDS--GQGPAALKS--------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 452 hVRMIVTGAAPASPtvlGFLRAA--LGCQVYEGYGQTEcTAGCTFT-TPGDWTSGHVGAPLPCNHIKLVDaeelnywtck 528
Cdd:cd17630 113 -LRAVLLGGAPIPP---ELLERAadRGIPLYTTYGMTE-TASQVATkRPDGFGRGGVGVLLPGRELRIVE---------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 529 gEGEICVKGPNVFKGYLKDedRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPV 608
Cdd:cd17630 178 -DGEIWVGGASLAMGYLRG--QLVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAV 253
|
330 340 350
....*....|....*....|....*....|
gi 75992911 609 AQIYVHG---DSLKAFLVGIVVPDPEVMPS 635
Cdd:cd17630 254 RDAFVVGvpdEELGQRPVAVIVGRGPADPA 283
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
146-630 |
3.40e-23 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 104.36 E-value: 3.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLLqhDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 225
Cdd:PRK13295 56 FTYRELAALVDRVAVGLA--RLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 -------DKPHKATLLlehveRKETPGLKLVILM-----EPFEDALRERGKKCGVDIksmQAIEDCGRenhhapvpPRPD 293
Cdd:PRK13295 134 pktfrgfDHAAMARRL-----RPELPALRHVVVVggdgaDSFEALLITPAWEQEPDA---PAILARLR--------PGPD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 294 DLSIVCFTSGTTGNPKGAMLTHGNVvadFSGFLKVTEKVIFpRQDDVLISFLPLAHMferviqsvvychggrVGFFQGDI 373
Cdd:PRK13295 198 DVTQLIYTSGTTGEPKGVMHTANTL---MANIVPYAERLGL-GADDVILMASPMAHQ---------------TGFMYGLM 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 374 RLLSDDMKALRPTIFPVVprllnRMYDKI------FHQADTSlkrWLLEFAakRKQAEVRSGIirnnsiwdelffnkiqA 447
Cdd:PRK13295 259 MPVMLGATAVLQDIWDPA-----RAAELIrtegvtFTMASTP---FLTDLT--RAVKESGRPV----------------S 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 448 SLgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPGD---WTSGHVGAPLPCNHIKLVDAE--EL 522
Cdd:PRK13295 313 SL----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA-VTLTKLDDpdeRASTTDGCPLPGVEVRVVDADgaPL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 523 NYWTckgEGEICVKGPNVFKGYLKDEDRTkeALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIY 602
Cdd:PRK13295 388 PAGQ---IGRLQVRGCSNFGGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEALL 461
|
490 500
....*....|....*....|....*....
gi 75992911 603 IRSEPVAQiyvhgdslkaflVGIV-VPDP 630
Cdd:PRK13295 462 YRHPAIAQ------------VAIVaYPDE 478
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
146-630 |
3.94e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 103.86 E-value: 3.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 225
Cdd:PRK08316 37 WTYAELDAAVNRVAAALLDLGLKKGDR--VAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 DkphkaTLLLEHVERKETPGLKLVILMEPFEDaLRERGKKCgVDIKSMQAIEDcgreNHHAPVPPRPDDLSIVCFTSGTT 305
Cdd:PRK08316 115 D-----PALAPTAEAALALLPVDTLILSLVLG-GREAPGGW-LDFADWAEAGS----VAEPDVELADDDLAQILYTSGTE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 306 GNPKGAMLTHGNVVADFSGFLKVTEKvifpRQDDVLISFLPLAHMFER--VIQSVVYCHGGRVGFFQGDIRLLSDDMKAL 383
Cdd:PRK08316 184 SLPKGAMLTHRALIAEYVSCIVAGDM----SADDIPLHALPLYHCAQLdvFLGPYLYVGATNVILDAPDPELILRTIEAE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 384 RPTIF---PVVPRLLNRMYDkiFHQADTSlkrwllefaakrkqaevrsgiirnnsiwdelffnkiqaSLgghvRMIVTGA 460
Cdd:PRK08316 260 RITSFfapPTVWISLLRHPD--FDTRDLS--------------------------------------SL----RKGYYGA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 461 APASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFTTPGDwtsgHVGAP----LPCNHI--KLVDA--EELnywtCKGE- 530
Cdd:PRK08316 296 SIMPVEVLKELRERLpGLRFYNCYGQTEIAPLATVLGPEE----HLRRPgsagRPVLNVetRVVDDdgNDV----APGEv 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 531 GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIyirsepvaq 610
Cdd:PRK08316 368 GEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEA--------- 436
|
490 500
....*....|....*....|
gi 75992911 611 IYVHGDSLKAFLVGivVPDP 630
Cdd:PRK08316 437 LYTHPAVAEVAVIG--LPDP 454
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
294-631 |
4.39e-23 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 100.81 E-value: 4.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 294 DLSIVCFTSGTTGNPKGAMLTHGNVVA---DFSGFLKVTEkvifprqDDVLISFLPLAHMFERVIQSVVYCHGGR-VGFF 369
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAanlQLIHAMGLTE-------ADVYLNMLPLFHIAGLNLALATFHAGGAnVVME 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 370 QGDIRLLSDDMKALRPTIFPVVPRLLNRMYDkifhqadtslkrwllefAAKRKQAEVRSgiIRNnsiwdelffnkiqasl 449
Cdd:cd17637 74 KFDPAEALELIEEEKVTLMGSFPPILSNLLD-----------------AAEKSGVDLSS--LRH---------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 450 gghvrmiVTGAApaSPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDaeELNYWTCKG 529
Cdd:cd17637 119 -------VLGLD--APETIQRFEETTGATFWSLYGQTE-TSGLVTLSPYRERPGSAGRPGPLVRVRIVD--DNDRPVPAG 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 530 E-GEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRK--KHIFKlAQGEYVAPEKIENIYIRSE 606
Cdd:cd17637 187 EtGEIVVRGPLVFQGYWNLPELTAYTFR-NGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKVILEHP 264
|
330 340
....*....|....*....|....*
gi 75992911 607 PVAQIYVHGdslkaflvgivVPDPE 631
Cdd:cd17637 265 AIAEVCVIG-----------VPDPK 278
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
146-601 |
1.22e-22 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 103.89 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGsGLLQHDCKVGteQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 225
Cdd:PRK06814 659 LTYRKLLTGAFVLG-RKLKKNTPPG--ENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 DKP--HKATL--LLEHVERketpGLKLVILmEPFEDALRERGKKCGVDIKSMQAIEDCGRenhhapvppRPDDLSIVCFT 301
Cdd:PRK06814 736 SRAfiEKARLgpLIEALEF----GIRIIYL-EDVRAQIGLADKIKGLLAGRFPLVYFCNR---------DPDDPAVILFT 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 302 SGTTGNPKGAMLTHGNVVADFSgflKVTEKVIFPRQDDVLiSFLPLAHMFerviqsvvychggrvGFFQGDIRLLSDDMK 381
Cdd:PRK06814 802 SGSEGTPKGVVLSHRNLLANRA---QVAARIDFSPEDKVF-NALPVFHSF---------------GLTGGLVLPLLSGVK 862
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 382 AL---RPTIFPVVPRLLnrmYD---KIFHQADTSLkrwllefaakrkqaevrSGIIRNNSIWDelFFNkiqaslgghVRM 455
Cdd:PRK06814 863 VFlypSPLHYRIIPELI---YDtnaTILFGTDTFL-----------------NGYARYAHPYD--FRS---------LRY 911
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 456 IVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNywtcKGeGEICV 535
Cdd:PRK06814 912 VFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGID----EG-GRLFV 986
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75992911 536 KGPNVFKGYLKDED-RTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENI 601
Cdd:PRK06814 987 RGPNVMLGYLRAENpGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAVEEL 1051
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
137-630 |
1.37e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 101.89 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 137 RKPEQPY-----QWLSYQEVAKRAEfLGSGLLqHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSI 211
Cdd:PRK06145 14 RTPDRAAlvyrdQEISYAEFHQRIL-QAAGML-HARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 212 SYIINTADICTVIVDKPHKATLLLEHverketpglKLVILMEPFEDALRERGKKcgvdiksmqaiedcgrenhHAPVPP- 290
Cdd:PRK06145 92 AYILGDAGAKLLLVDEEFDAIVALET---------PKIVIDAAAQADSRRLAQG-------------------GLEIPPq 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 291 ---RPDDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTekvifprQDDVLISFLPLAHMFERVIQSV-VYCHG 363
Cdd:PRK06145 144 aavAPTDLVRLMYTSGTTDRPKGVMHSYGNLHwksIDHVIALGLT-------ASERLLVVGPLYHVGAFDLPGIaVLWVG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 364 GRVGF---FQGDIRLLSDDMKALRPTIFpvVPRLLNRMY---DKifHQADTSLKRWLLefAAKRKQAEVRsgiIRNnsiw 437
Cdd:PRK06145 217 GTLRIhreFDPEAVLAAIERHRLTCAWM--APVMLSRVLtvpDR--DRFDLDSLAWCI--GGGEKTPESR---IRD---- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 438 delffnkiqaslgghvrmivtgaapasptvlgFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPcnHIK 515
Cdd:PRK06145 284 --------------------------------FTRVFTRARYIDAYGLTETCSGDTLMEAGREIEkiGSTGRALA--HVE 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 516 LVDAEELNYWTCKG-EGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVA 594
Cdd:PRK06145 330 IRIADGAGRWLPPNmKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIA 407
|
490 500 510
....*....|....*....|....*....|....*....
gi 75992911 595 PEKIEN-IYIRSE--PVAQIYVHGDSLKAFLVGIVVPDP 630
Cdd:PRK06145 408 SSEVERvIYELPEvaEAAVIGVHDDRWGERITAVVVLNP 446
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
288-623 |
1.67e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 102.03 E-value: 1.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 288 VPPRPD-DLSIVCFTSGTTGNPKGAMLTHGNVVADfsGFLKVTEKVIFPRQDDVLISFLPLAHMF-ERVIQSVVYCHGGR 365
Cdd:PRK06710 200 VPCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSN--TLMGVQWLYNCKEGEEVVLGVLPFFHVYgMTAVMNLSIMQGYK 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 366 VGFF-QGDIRLLSDDMKALRPTIFPVVPRLLNRMydkifhqadtsLKRWLLefaakrKQAEVRSgiirnnsiwdelffnk 444
Cdd:PRK06710 278 MVLIpKFDMKMVFEAIKKHKVTLFPGAPTIYIAL-----------LNSPLL------KEYDISS---------------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 445 iqaslgghVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgctfTTPGDW-----TSGHVGAPLPCNHIKLVDA 519
Cdd:PRK06710 325 --------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSP----VTHSNFlwekrVPGSIGVPWPDTEAMIMSL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 520 EELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIE 599
Cdd:PRK06710 393 ETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREVE 470
|
330 340 350
....*....|....*....|....*....|.
gi 75992911 600 NIYIRSEPVAQIYV-------HGDSLKAFLV 623
Cdd:PRK06710 471 EVLYEHEKVQEVVTigvpdpyRGETVKAFVV 501
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
175-623 |
7.17e-22 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 99.76 E-value: 7.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 175 VGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIVDKphKATLLLEHVERKETPGLKLVILMEP 254
Cdd:PRK08008 65 VALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSA--QFYPMYRQIQQEDATPLRHICLTRV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 255 FEDAlrERGKKCGVDIKSMQAIEDCgrenhHAPvPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVTEKVIf 334
Cdd:PRK08008 143 ALPA--DDGVSSFTQLKAQQPATLC-----YAP-PLSTDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYYSAWQCAL- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 335 pRQDDVLISFLPLAHMFerviqsvvychggrvgfFQgdirlLSDDMKAlrptiFPVVPRLLnrmydkifhqadtslkrwL 414
Cdd:PRK08008 212 -RDDDVYLTVMPAFHID-----------------CQ-----CTAAMAA-----FSAGATFV------------------L 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 415 LE-FAAKRKQAEVRsgiirnnsiwdelffnKIQASLGGHVRMIVTG--AAPASPT--------VLGFLRAA--------- 474
Cdd:PRK08008 246 LEkYSARAFWGQVC----------------KYRATITECIPMMIRTlmVQPPSANdrqhclreVMFYLNLSdqekdafee 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 475 -LGCQVYEGYGQTECTAGCTFTTPGD---WTSghVGAPLPCNHIKLVDAEelNYWTCKGE-GEICVKG---PNVFKGYLK 546
Cdd:PRK08008 310 rFGVRLLTSYGMTETIVGIIGDRPGDkrrWPS--IGRPGFCYEAEIRDDH--NRPLPAGEiGEICIKGvpgKTIFKEYYL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 547 DEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIyIRSEP-VAQIYVHG--DSL----- 618
Cdd:PRK08008 386 DPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVELENI-IATHPkIQDIVVVGikDSIrdeai 463
|
....*
gi 75992911 619 KAFLV 623
Cdd:PRK08008 464 KAFVV 468
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
291-631 |
7.86e-22 |
|
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: 99.54 E-value: 7.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 291 RPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkviFPRQDDVL----ISF-LPLAHMFerviqsVVYCHGG- 364
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALG---LTSESRVLqfasYTFdVSILEIF------TTLAAGGc 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 365 --------RVGFFQGDIRllsdDMKA----LRPTifpvVPRLLNRmydkifhqadtslkrwllefaakrkqAEVRSgiir 432
Cdd:cd05918 175 lcipseedRLNDLAGFIN----RLRVtwafLTPS----VARLLDP--------------------------EDVPS---- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 433 nnsiwdelffnkiqaslgghVRMIVTGAAPASPTVLGflRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPC 511
Cdd:cd05918 217 --------------------LRTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRPLGA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 512 --------NHIKLVDaeelnywtcKGE-GEICVKGPNVFKGYLKDEDRTKEA-LDSDGWLH------------TGDIGKW 569
Cdd:cd05918 275 tcwvvdpdNHDRLVP---------IGAvGELLIEGPILARGYLNDPEKTAAAfIEDPAWLKqegsgrgrrlyrTGDLVRY 345
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75992911 570 LPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEP-----VAQIYVH-GDSLKAFLVGIVVPDPE 631
Cdd:cd05918 346 NPDGSLEYVGRKDTQVKI-RGQRVELGEIEHHLRQSLPgakevVVEVVKPkDGSSSPQLVAFVVLDGS 412
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
292-664 |
4.74e-21 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 96.55 E-value: 4.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVVAdFS----GFLKVTEkvifprqDDVLISFLPLAhmFERVIQSVVYC--HGGr 365
Cdd:cd05945 96 GDDNAYIIFTSGSTGRPKGVQISHDNLVS-FTnwmlSDFPLGP-------GDVFLNQAPFS--FDLSVMDLYPAlaSGA- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 366 vgffqgdirllsddmkalrpTIFPVvPRLLNRMYdkifhqadtslkRWLLEFAAKRKQAEVRSgiirNNSIWDELF---- 441
Cdd:cd05945 165 --------------------TLVPV-PRDATADP------------KQLFRFLAEHGITVWVS----TPSFAAMCLlspt 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 442 FNkiQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFT--TP---GDWTSGHVGAPLPCNHIKL 516
Cdd:cd05945 208 FT--PESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIevTPevlDGYDRLPIGYAKPGAKLVI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 517 VDaEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSD---GWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYV 593
Cdd:cd05945 286 LD-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRI 363
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75992911 594 APEKIENIYIRSEPVAQIYV----HGDSlKAFLVGIVVPDPEVMPswAQKKGIegtyqelcmKKELKKAILDDMV 664
Cdd:cd05945 364 ELEEIEAALRQVPGVKEAVVvpkyKGEK-VTELIAFVVPKPGAEA--GLTKAI---------KAELAERLPPYMI 426
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
143-630 |
5.15e-21 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 97.18 E-value: 5.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 143 YQWLSYQeVAKRAEFLGSgllqhdCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICT 222
Cdd:cd05970 50 FAELADY-SDKTANFFKA------MGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 223 VIVDKphkATLLLEHVE--RKETPGLKLVI-----LMEPFEDaLRERGKKCGVDIksmqaiedcgrENHHAPVPPRPDDL 295
Cdd:cd05970 123 IVAIA---EDNIPEEIEkaAPECPSKPKLVwvgdpVPEGWID-FRKLIKNASPDF-----------ERPTANSYPCGEDI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 296 SIVCFTSGTTGNPKgaMLTHgnvvaDFSgflkvtekvifprqddvlisfLPLAHmfervIQSVVYCHGGRvgffQGDIRL 375
Cdd:cd05970 188 LLVYFSSGTTGMPK--MVEH-----DFT---------------------YPLGH-----IVTAKYWQNVR----EGGLHL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 376 LSDDM---KAlrptifpvvprllnrMYDKIFHQ-----------ADTSLKRWLLEFAAKRkqaEVRSgIIRNNSIWDELF 441
Cdd:cd05970 231 TVADTgwgKA---------------VWGKIYGQwiagaavfvydYDKFDPKALLEKLSKY---GVTT-FCAPPTIYRFLI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 442 FNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPG-DWTSGHVGAPLPCNHIKLVDAE 520
Cdd:cd05970 292 REDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTL-TIATFPWmEPKPGSMGKPAPGYEIDLIDRE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 521 ELnywTCKG--EGEICV---KGPNV--FKGYLKDEDRTKEALdSDGWLHTGDIGkWLPE-GTLKIIDRKKHIFKlAQGEY 592
Cdd:cd05970 371 GR---SCEAgeEGEIVIrtsKGKPVglFGGYYKDAEKTAEVW-HDGYYHTGDAA-WMDEdGYLWFVGRTDDLIK-SSGYR 444
|
490 500 510
....*....|....*....|....*....|....*...
gi 75992911 593 VAPEKIENIYIRSEPVAQIYVHGdslkaflvgivVPDP 630
Cdd:cd05970 445 IGPFEVESALIQHPAVLECAVTG-----------VPDP 471
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
274-635 |
8.32e-21 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 95.99 E-value: 8.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 274 QAIEDCGRENHHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHgnvvADFSGFLKVTEKVIFP-RQDDVLISflpLAHMFe 352
Cdd:cd05919 72 DDYAYIARDCEARLVVTSADDIAYLLYSSGTTGPPKGVMHAH----RDPLLFADAMAREALGlTPGDRVFS---SAKMF- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 353 rviqsVVYCHGGRVGF--FQGDIRLLSDD----------MKALRPTIFPVVPRllnrMYDKIFHQADTSlkrwllefaak 420
Cdd:cd05919 144 -----FGYGLGNSLWFplAVGASAVLNPGwptaervlatLARFRPTVLYGVPT----FYANLLDSCAGS----------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 421 rkQAEVRSgiIRnnsiwdelffnkiqaslgghvrmIVTGAAPASPTVLG-FLRAALGCQVYEGYGQTEctAGCTFTT--P 497
Cdd:cd05919 204 --PDALRS--LR-----------------------LCVSAGEALPRGLGeRWMEHFGGPILDGIGATE--VGHIFLSnrP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 498 GDWTSGHVGAPLPCNHIKLVDaEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKI 577
Cdd:cd05919 255 GAWRLGSTGRPVPGYEIRLVD-EEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTH 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75992911 578 IDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQIYV----HGDSL---KAFlvgiVVPDPEVMPS 635
Cdd:cd05919 333 AGRADDMLKVG-GQWVSPVEVESLIIQHPAVAEAAVvavpESTGLsrlTAF----VVLKSPAAPQ 392
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
145-649 |
1.09e-20 |
|
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: 95.83 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 145 WLSYQEVAKRAEFLGSGLLqhDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVI 224
Cdd:cd12118 29 RYTWRQTYDRCRRLASALA--ALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 225 VDKPHKatlllehverketpglklvilmepFEDALrERGKKcgvdiksmqaiedcgrenHHAPVPPRPDDLSIVC-FTSG 303
Cdd:cd12118 107 VDREFE------------------------YEDLL-AEGDP------------------DFEWIPPADEWDPIALnYTSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 304 TTGNPKGAMLTHGnvvadfSGFLKVTEKVIFPRQDD--VLISFLPLAHmferviqSVVYCHGGRVGFFQG--------DI 373
Cdd:cd12118 144 TTGRPKGVVYHHR------GAYLNALANILEWEMKQhpVYLWTLPMFH-------CNGWCFPWTVAAVGGtnvclrkvDA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 374 RLLSDDMKALRPTIFPVVPRLLNrmydkifhqadtslkrwllefaakrkqaevrsgIIRNNSIWDelffnkiQASLGGHV 453
Cdd:cd12118 211 KAIYDLIEKHKVTHFCGAPTVLN---------------------------------MLANAPPSD-------ARPLPHRV 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 454 RMIVTGAAPaSPTVLgFLRAALGCQVYEGYGQTEcTAG----CTFTTPGDWTSGHVGAPLPC----NHIKLVDAEELNYW 525
Cdd:cd12118 251 HVMTAGAPP-PAAVL-AKMEELGFDVTHVYGLTE-TYGpatvCAWKPEWDELPTEERARLKArqgvRYVGLEEVDVLDPE 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 526 TCK-----GE--GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKI 598
Cdd:cd12118 328 TMKpvprdGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENISSVEV 405
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 75992911 599 ENIyirsepvaqIYVHGDSLKAFLVGivVPDP---EVMPSW-AQKKGIEGTYQEL 649
Cdd:cd12118 406 EGV---------LYKHPAVLEAAVVA--RPDEkwgEVPCAFvELKEGAKVTEEEI 449
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
146-634 |
1.22e-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: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLlqHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 225
Cdd:cd12114 13 LTYGELAERARRVAGAL--KAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 DKPHkatlLLEHVERKETPGLKLVilmepFEDALRERgkkcgvdiksmqaiedcgrenhhAPVPPRPDDLSIVCFTSGTT 305
Cdd:cd12114 91 DGPD----AQLDVAVFDVLILDLD-----ALAAPAPP-----------------------PPVDVAPDDLAYVIFTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 306 GNPKGAMLTHG---NVVADFSGFLKVTEkvifprqDDVLISFLPLAHMFerviqSV-----VYCHGGRVgffqgdirlls 377
Cdd:cd12114 139 GTPKGVMISHRaalNTILDINRRFAVGP-------DDRVLALSSLSFDL-----SVydifgALSAGATL----------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 378 ddmkalrptifpVVPRllnrmydkifHQADTSLKRWllefaakrKQAEVRSGIirnnSIWdelffNKIQASLGghvrMIV 457
Cdd:cd12114 196 ------------VLPD----------EARRRDPAHW--------AELIERHGV----TLW-----NSVPALLE----MLL 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 458 TgAAPASPTVLGFLRAAL-------------------GCQVYEGYGQTECTAGCTF----TTPGDWTSGHVGAPLPCNHI 514
Cdd:cd12114 233 D-VLEAAQALLPSLRLVLlsgdwipldlparlralapDARLISLGGATEASIWSIYhpidEVPPDWRSIPYGRPLANQRY 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 515 KLVDA--EELNYWTckgEGEICVKGPNVFKGYLKDEDRTKEAL--DSDG--WLHTGDIGKWLPEGTLKIIDRKKHIFKLa 588
Cdd:cd12114 312 RVLDPrgRDCPDWV---PGELWIGGRGVALGYLGDPELTAARFvtHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKV- 387
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 75992911 589 QGEYVAPEKIENIYIRSEPVAQ--IYVHGDSLKAFLVGIVVPDPEVMP 634
Cdd:cd12114 388 RGYRIELGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPDNDGTP 435
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
146-635 |
3.14e-20 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 94.95 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLLQHDCKVGteQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 225
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGLLPG--DRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 DKphkatlllehverkETPGLKLVILMEPFEDALReRGKKCGVDIKSMQAIEDCGRENHHAPVPP---RPDDLSIVcFTS 302
Cdd:PRK05852 122 DA--------------DGPHDRAEPTTRWWPLTVN-VGGDSGPSGGTLSVHLDAATEPTPATSTPeglRPDDAMIM-FTG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 303 GTTGNPKGAMLTHGNVVADFSGFlkVTEKVIFPRqdDVLISFLPLAH---MFERVIQSVVycHGGRV-----GFFQGdiR 374
Cdd:PRK05852 186 GTTGLPKMVPWTHANIASSVRAI--ITGYRLSPR--DATVAVMPLYHghgLIAALLATLA--SGGAVllparGRFSA--H 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 375 LLSDDMKALRPTIFPVVPRLlnrmydkifHQAdtslkrwLLEFAAKRKQAEVRSGIirnnsiwdelffnkiqaslgghvR 454
Cdd:PRK05852 258 TFWDDIKAVGATWYTAVPTI---------HQI-------LLERAATEPSGRKPAAL-----------------------R 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 455 MIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTfTTPGDWtSGHVGAPLPCN---------HIKLV--DAEELn 523
Cdd:PRK05852 299 FIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVT-TTQIEG-IGQTENPVVSTglvgrstgaQIRIVgsDGLPL- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 524 ywTCKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYI 603
Cdd:PRK05852 376 --PAGAVGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLA 451
|
490 500 510
....*....|....*....|....*....|....*
gi 75992911 604 RSEPVAQIYVHGDSLKAF---LVGIVVPDPEVMPS 635
Cdd:PRK05852 452 SHPNVMEAAVFGVPDQLYgeaVAAVIVPRESAPPT 486
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
146-632 |
7.89e-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: 7.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELA------CYtysmvvVPLYDTLGPGSISYIINTAD 219
Cdd:cd12117 23 LTYAELNERANRLARRLRAAG--VGPGDVVGVLAERSPELVVALLAvlkagaAY------VPLDPELPAERLAFMLADAG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 220 ICTVIVDKPhkatlllehverketpglklvilmepfedaLRERGKKCGVDIKSMQAIEDCGRENhhAPVPPRPDDLSIVC 299
Cdd:cd12117 95 AKVLLTDRS------------------------------LAGRAGGLEVAVVIDEALDAGPAGN--PAVPVSPDDLAYVM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 300 FTSGTTGNPKGAMLTHGNVV--ADFSGFLKVTEkvifprqDDVLISFLPL---AHMFErviqsvVY---CHGGRVgffqg 371
Cdd:cd12117 143 YTSGSTGRPKGVAVTHRGVVrlVKNTNYVTLGP-------DDRVLQTSPLafdASTFE------IWgalLNGARL----- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 372 diRLLSDDmkalrptifpvVPRLLNRMYDKIFHQADTSLkrWLLefAAkrkqaevrsgiirnnsiwdelFFNKI----QA 447
Cdd:cd12117 205 --VLAPKG-----------TLLDPDALGALIAEEGVTVL--WLT--AA---------------------LFNQLadedPE 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 448 SLGGhVRMIVTGAAPASPT-VLGFLRAALGCQVYEGYGQTECTagcTFTT-----PGDWTSGHV--GAPLPCNHIKLVDA 519
Cdd:cd12117 247 CFAG-LRELLTGGEVVSPPhVRRVLAACPGLRLVNGYGPTENT---TFTTshvvtELDEVAGSIpiGRPIANTRVYVLDE 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 520 eelnywtcKG-------EGEICVKGPNVFKGYLKDEDRTKEALDSDGWL------HTGDIGKWLPEGTLKIIDRKKHIFK 586
Cdd:cd12117 323 --------DGrpvppgvPGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVK 394
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 75992911 587 LaQGEYVAPEKIENIYIRSEPVAQIYV---HGDSLKAFLVGIVVPDPEV 632
Cdd:cd12117 395 I-RGFRIELGEIEAALRAHPGVREAVVvvrEDAGGDKRLVAYVVAEGAL 442
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
292-656 |
9.74e-20 |
|
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: 92.50 E-value: 9.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 292 PDDLSIVCFTSGTTGNPKGAMLTH----GNVVADFSGFlkvtekVIFPRQDDVLIS-------------FLP-------- 346
Cdd:cd05971 87 SDDPALIIYTSGTTGPPKGALHAHrvllGHLPGVQFPF------NLFPRDGDLYWTpadwawigglldvLLPslyfgvpv 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 347 LAHMFERviqsvvychggrvgfFQGD--IRLLSD---DMKALRPTIFpvvprllnrmydKIFHQADTSLKRWLLEfaakr 421
Cdd:cd05971 161 LAHRMTK---------------FDPKaaLDLMSRygvTTAFLPPTAL------------KMMRQQGEQLKHAQVK----- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 422 kqaevrsgiirnnsiwdelffnkiqaslgghVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEC---TAGCTFTTPG 498
Cdd:cd05971 209 -------------------------------LRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECnlvIGNCSALFPI 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 499 DwtSGHVGAPLPCNHIKLVDAeelnywtcKGE-------GEICVKGPN--VFKGYLKDEDRTKEALDSDgWLHTGDIGKW 569
Cdd:cd05971 258 K--PGSMGKPIPGHRVAIVDD--------NGTplppgevGEIAVELPDpvAFLGYWNNPSATEKKMAGD-WLLTGDLGRK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 570 LPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRsepvaqiyvHGDSLKAFLVGIvvPDP---EVMPSWAQKKGIEGTY 646
Cdd:cd05971 327 DSDGYFWYVGRDDDVITSS-GYRIGPAEIEECLLK---------HPAVLMAAVVGI--PDPirgEIVKAFVVLNPGETPS 394
|
410
....*....|
gi 75992911 647 QELcmKKELK 656
Cdd:cd05971 395 DAL--AREIQ 402
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
292-629 |
8.46e-19 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 89.83 E-value: 8.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPRQDDVL--ISFLPLAHMFERVIqsvvyCHGGRVGFF 369
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQMasFSFDVFAGDFARSL-----LNGGTLVIC 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 370 QGDIRL----LSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTSLKRWLLEFAAKRKQAEvrsgiirnnsiWdelfFNKI 445
Cdd:cd17650 167 PDEVKLdpaaLYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQ-----------D----FKTL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 446 QASLGGHVRMIvtgaapaspTVLGFLRAALGCQVYEGYGQTECTAGctfTTPgdwtsghVGAPLPCNHIKLVDaEELNYW 525
Cdd:cd17650 232 AARFGQGMRII---------NSYGVTEATIDSTYYEEGRDPLGDSA---NVP-------IGRPLPNTAMYVLD-ERLQPQ 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 526 TCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGW------LHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIE 599
Cdd:cd17650 292 PVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI-RGFRIELGEIE 370
|
330 340 350
....*....|....*....|....*....|...
gi 75992911 600 NIYIRSEPVAQIYV---HGDSLKAFLVGIVVPD 629
Cdd:cd17650 371 SQLARHPAIDEAVVavrEDKGGEARLCAYVVAA 403
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
146-615 |
2.08e-18 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 89.11 E-value: 2.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLLQHDCKVGteQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 225
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRPG--QRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 dkphkatllleHVERKETPGLKLVILMEPFEDALRERGKKCgVDIKSMqaiedcgrenhhAPVPPRPDDLSIVCFTSGTT 305
Cdd:cd05923 107 -----------AVDAQVMDAIFQSGVRVLALSDLVGLGEPE-SAGPLI------------EDPPREPEQPAFVFYTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 306 GNPKGAMLTHgNVVADFSGFLKVTEKVIFPRQdDVLISFLPLAHMferviqsvvychggrVGFFQgdirLLSDDMkALRP 385
Cdd:cd05923 163 GLPKGAVIPQ-RAAESRVLFMSTQAGLRHGRH-NVVLGLMPLYHV---------------IGFFA----VLVAAL-ALDG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 386 TIFPVvprllnrmydKIFHQADtslkrwllefAAKRKQAEVRSGIIRNNSIWDELFFNKIQASLG-GHVRMIVTGAAPAS 464
Cdd:cd05923 221 TYVVV----------EEFDPAD----------ALKLIEQERVTSLFATPTHLDALAAAAEFAGLKlSSLRHVTFAGATMP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 465 PTVLGFLRAALGCQVYEGYGQTECTagcTFTTPGDWTSGHVGAPLPCNHIKLVD-AEELNYWTCKG-EGEICVK--GPNV 540
Cdd:cd05923 281 DAVLERVNQHLPGEKVNIYGTTEAM---NSLYMRDARTGTEMRPGFFSEVRIVRiGGSPDEALANGeEGELIVAaaADAA 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75992911 541 FKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYVHG 615
Cdd:cd05923 358 FTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIG 430
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
52-664 |
2.67e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 90.22 E-value: 2.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 52 ATTLVSVGALAAVLAYW--LTHRPKAlQPPCNL----LKQSEEVEDGGGARRsviggctqlLTHYYDDARTMYQVFRRGL 125
Cdd:PRK12467 453 ATDLFEATTIERLATHWrnLLEAIVA-EPRRRLgelpLLDAEERARELVRWN---------APATEYAPDCVHQLIEAQA 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 126 SISGNGPCLGFRKpeqpyQWLSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDT 205
Cdd:PRK12467 523 RQHPERPALVFGE-----QVLSYAELNRQANRLAHVLIAAG--VGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPE 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 206 LGPGSISYIINTADICTVIVDkPHKATLLlehverkETP-GLKLVILMEPfedalrergkkcgvdiksmqAIEDCGRENH 284
Cdd:PRK12467 596 YPQDRLAYMLDDSGVRLLLTQ-SHLLAQL-------PVPaGLRSLCLDEP--------------------ADLLCGYSGH 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 285 HAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVvadfSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGG 364
Cdd:PRK12467 648 NPEVALDPDNLAYVIYTSGSTGQPKGVAISHGAL----ANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGA 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 365 RVgffqgdirLLSDDMKALRPTIFpvvprllnrmYDKIFHQADTSLKrwllefaakrkqaevrsgiiRNNSIWDELFFNK 444
Cdd:PRK12467 724 TL--------HLLPPDCARDAEAF----------AALMADQGVTVLK--------------------IVPSHLQALLQAS 765
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 445 IQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTT----PGDWTSGHVGAPLPCNHIKLVDAe 520
Cdd:PRK12467 766 RVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYElsdeERDFGNVPIGQPLANLGLYILDH- 844
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 521 ELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSD------GWLH-TGDIGKWLPEGTLKIIDRKKHIFKLaQGEYV 593
Cdd:PRK12467 845 YLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDpfgadgGRLYrTGDLARYRADGVIEYLGRMDHQVKI-RGFRI 923
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75992911 594 APEKIENIYIRSEPVAQIYV------HGDSLKAFLVGIVVPDpevmpswaqkkGIEGTYQELCMKKELKKAILDDMV 664
Cdd:PRK12467 924 ELGEIEARLLAQPGVREAVVlaqpgdAGLQLVAYLVPAAVAD-----------GAEHQATRDELKAQLRQVLPDYMV 989
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
146-634 |
5.84e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 87.88 E-value: 5.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADiCTVIV 225
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQG--VRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGR-ARWLV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 DKPHKATL----LLEHVERKETPGLKLVILMEPFEDALRERGKKCGVdiksmQAIEDCGRENHHA-PVPPRPDDLSIVCF 300
Cdd:PRK06164 113 VWPGFKGIdfaaILAAVPPDALPPLRAIAVVDDAADATPAPAPGARV-----QLFALPDPAPPAAaGERAADPDAGALLF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 301 T-SGTTGNPK------GAMLTHGNVVADFSGFlkvtekvifpRQDDVLISFLPLahmferviqSVVYCHGGRVGFFQGDI 373
Cdd:PRK06164 188 TtSGTTSGPKlvlhrqATLLRHARAIARAYGY----------DPGAVLLAALPF---------CGVFGFSTLLGALAGGA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 374 RLLSDDmkalrptIF--PVVPRLL-----------NRMYDKIFHQADTSLkrwllEFAAKRkqaevRSGIIRNNSIWDEL 440
Cdd:PRK06164 249 PLVCEP-------VFdaARTARALrrhrvthtfgnDEMLRRILDTAGERA-----DFPSAR-----LFGFASFAPALGEL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 441 ffnkiqaslgghvrmivtgaaPASPTVLGFLRAALgcqvyegYGQTECTA---GCTFTTPgdWTSGHVGAPLPCN---HI 514
Cdd:PRK06164 312 ---------------------AALARARGVPLTGL-------YGSSEVQAlvaLQPATDP--VSVRIEGGGRPASpeaRV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 515 KLVDAEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVA 594
Cdd:PRK06164 362 RARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVN 440
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 75992911 595 PEKIENIYIRSEPVAQIYVHGDSL--KAFLVGIVVPDPEVMP 634
Cdd:PRK06164 441 PAEIEHALEALPGVAAAQVVGATRdgKTVPVAFVIPTDGASP 482
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
284-619 |
6.22e-18 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 88.23 E-value: 6.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 284 HHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTH----GNV-----VADFSgflkvtekvifPRqdDVLISFLPLAHMFerv 354
Cdd:PRK08043 356 RLAQVKQQPEDAALILFTSGSEGHPKGVVHSHksllANVeqiktIADFT-----------PN--DRFMSALPLFHSF--- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 355 iqsvvychGGRVGffqgdirLLSDDMKALRPTIFP------VVPRLLnrmYDK----IFhqaDTSlkRWLLEFAakrkqa 424
Cdd:PRK08043 420 --------GLTVG-------LFTPLLTGAEVFLYPsplhyrIVPELV---YDRnctvLF---GTS--TFLGNYA------ 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 425 evrsgiiRNNSIWDelFFnkiqaslggHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGH 504
Cdd:PRK08043 471 -------RFANPYD--FA---------RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGT 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 505 VGAPLPCnhiklVDAEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTK-EALDSD--------GWLHTGDIGKWLPEGTL 575
Cdd:PRK08043 533 VGRILPG-----MDARLLSVPGIEQGGRLQLKGPNIMNGYLRVEKPGVlEVPTAEnargemerGWYDTGDIVRFDEQGFV 607
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 75992911 576 KIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQiyvHGDSLK 619
Cdd:PRK08043 608 QIQGRAKRFAKIA-GEMVSLEMVEQLALGVSPDKQ---HATAIK 647
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
132-593 |
1.11e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 87.41 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 132 PCLGFRKPEQ-PYQWLSYQEVAKRAEFLGSGLLqhDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLydtlgpgS 210
Cdd:PRK12582 66 PWLAQREPGHgQWRKVTYGEAKRAVDALAQALL--DLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPV-------S 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 211 ISYIINTADIctvivDKphkatllLEHVERKETPGLKLVILMEPFEDALRERGKKcGVDIKSMQAIEDCGRENHHAPV-- 288
Cdd:PRK12582 137 PAYSLMSHDH-----AK-------LKHLFDLVKPRVVFAQSGAPFARALAALDLL-DVTVVHVTGPGEGIASIAFADLaa 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 289 -PPR-----------PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekviFPRQDD----VLISFLPLAHM-- 350
Cdd:PRK12582 204 tPPTaavaaaiaaitPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQL-----RPREPDppppVSLDWMPWNHTmg 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 351 ----FERVIQS--VVYCHGGR--VGFFQGDIRLLSDdmkaLRPTIFPVVPRLLNRMYDKIfhQADTSLKRWLLefaaKRK 422
Cdd:PRK12582 279 gnanFNGLLWGggTLYIDDGKplPGMFEETIRNLRE----ISPTVYGNVPAGYAMLAEAM--EKDDALRRSFF----KNL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 423 QAEVRSGIIRNNSIWDELFFNKIQASlgGHvrMIVtgaapasptvlgflraalgcqVYEGYGQTEcTAGCTFTTpgDWTS 502
Cdd:PRK12582 349 RLMAYGGATLSDDLYERMQALAVRTT--GH--RIP---------------------FYTGYGATE-TAPTTTGT--HWDT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 503 ---GHVGAPLPCNHIKLVDAEElNYwtckgegEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWL----PEGTL 575
Cdd:PRK12582 401 ervGLIGLPLPGVELKLAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdpddPEKGL 472
|
490
....*....|....*...
gi 75992911 576 KIIDRKKHIFKLAQGEYV 593
Cdd:PRK12582 473 IFDGRVAEDFKLSTGTWV 490
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
146-631 |
1.37e-17 |
|
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: 86.18 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 225
Cdd:cd17646 24 LTYRELDERANRLAHLLRARG--VGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 DkphkatlllehverketpglklvilmepfeDALRERGKKcGVDIKSMQAIEDCGRENHHAPVPPRPDDLSIVCFTSGTT 305
Cdd:cd17646 102 T------------------------------ADLAARLPA-GGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGST 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 306 GNPKGAMLTHGNVVADFSGF-----LKVTEKVIF--PRQDDVLIS--FLPLAHMfERViqsVVYCHGGRvgffqGDIRLL 376
Cdd:cd17646 151 GRPKGVMVTHAGIVNRLLWMqdeypLGPGDRVLQktPLSFDVSVWelFWPLVAG-ARL---VVARPGGH-----RDPAYL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 377 SDDMKALRPTIFPVVPRLLnrmydkifhqadtslkrwllefaakrkqaevrsgiirnnsiwdELFFNKIQASLGGHVRMI 456
Cdd:cd17646 222 AALIREHGVTTCHFVPSML-------------------------------------------RVFLAEPAAGSCASLRRV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 457 VTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHV--GAPLPCNHIKLVDAEeLNYWTCKGEGEI 533
Cdd:cd17646 259 FCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVThWPVRGPAETPSVpiGRPVPNTRLYVLDDA-LRPVPVGVPGEL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 534 CVKGPNVFKGYLKDEDRTKEALDSDGWLH------TGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEP 607
Cdd:cd17646 338 YLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKI-RGFRVEPGEIEAALAAHPA 416
|
490 500
....*....|....*....|....*..
gi 75992911 608 VAQIYV---HGDSLKAFLVGIVVPDPE 631
Cdd:cd17646 417 VTHAVVvarAAPAGAARLVGYVVPAAG 443
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
146-631 |
1.77e-17 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 86.35 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfvgVFAQ--NRPEWIIAELACYtySMVVVPLYdTLgPG----SISYIINTAD 219
Cdd:COG1021 51 LSYAELDRRADRLAAGLLALGLRPGDR----VVVQlpNVAEFVIVFFALF--RAGAIPVF-AL-PAhrraEISHFAEQSE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 220 ICTVIVDKPHkatLLLEHVE-----RKETPGLKLVILmepfedalrergkkCGvDIKSMQAIEDCGRENHHAPVP-PRPD 293
Cdd:COG1021 123 AVAYIIPDRH---RGFDYRAlarelQAEVPSLRHVLV--------------VG-DAGEFTSLDALLAAPADLSEPrPDPD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 294 DlsiVCF---TSGTTGNPKGAMLTHG----NVV--ADFSGFlkvtekvifpRQDDVLISFLPLAHMF---ERVIQSVVYc 361
Cdd:COG1021 185 D---VAFfqlSGGTTGLPKLIPRTHDdylySVRasAEICGL----------DADTVYLAALPAAHNFplsSPGVLGVLY- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 362 HGGRVgffqgdirLLSDDMKALrpTIFPVVPRllnrmydkifHQAD-TSL-----KRWLlEFAAKRKQAevrsgiirnns 435
Cdd:COG1021 251 AGGTV--------VLAPDPSPD--TAFPLIER----------ERVTvTALvpplaLLWL-DAAERSRYD----------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 436 iwdeLffnkiqASLgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctaG-CTFTTPGD--WTSGH-VGAPL-P 510
Cdd:COG1021 299 ----L------SSL----RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---GlVNYTRLDDpeEVILTtQGRPIsP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 511 CNHIKLVDAEelnywtckGE-------GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKK- 582
Cdd:COG1021 362 DDEVRIVDED--------GNpvppgevGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKd 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 75992911 583 HIFKlaQGEYVAPEKIENiyirsepvaQIYVHGDSLKAFLVGivVPDPE 631
Cdd:COG1021 434 QINR--GGEKIAAEEVEN---------LLLAHPAVHDAAVVA--MPDEY 469
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
292-615 |
2.00e-17 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 86.39 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfSGFLKVTekVIFPRQDDVLISFLPLAHMFErvIQSVVY------CHggr 365
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSALIV--QSLAKIA--IVGYGEDDVYLHTAPLCHIGG--LSSALAmlmvgaCH--- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 366 VGFFQGDIRLLSDDMKALRPTIFPVVPRLLnrmydkifhqADtslkrwLLEFAAKRKQAEVRSGiirnnsiwdelffnki 445
Cdd:PLN02860 242 VLLPKFDAKAALQAIKQHNVTSMITVPAMM----------AD------LISLTRKSMTWKVFPS---------------- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 446 qaslgghVRMIVTGAAPASP-----TVLGFLRAALgcqvYEGYGQTECTAGCTFTTPGDWT-----------------SG 503
Cdd:PLN02860 290 -------VRKILNGGGSLSSrllpdAKKLFPNAKL----FSAYGMTEACSSLTFMTLHDPTlespkqtlqtvnqtkssSV 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 504 H------VGAPLPcnHIKL-VDAEELNYwtckgEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLK 576
Cdd:PLN02860 359 HqpqgvcVGKPAP--HVELkIGLDESSR-----VGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLW 431
|
330 340 350
....*....|....*....|....*....|....*....
gi 75992911 577 IIDRKKHIFKlAQGEYVAPEKIENIYIRSEPVAQIYVHG 615
Cdd:PLN02860 432 LIGRSNDRIK-TGGENVYPEEVEAVLSQHPGVASVVVVG 469
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
291-631 |
2.95e-17 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 85.05 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 291 RPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkvTEKVIFPRQDDVLISFLPLAHMFerviqSV-----VYCHGGR 365
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA----TQRWFGFNEDDVWTLFHSYAFDF-----SVweiwgALLHGGR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 366 VGFFQGDIRLLSDDMkalrptifpvvPRLLNRMYDKIFHQADTSLKRWLlefaakrkQAEVRsgiirnnsiwdelfFNKI 445
Cdd:cd17643 162 LVVVPYEVARSPEDF-----------ARLLRDEGVTVLNQTPSAFYQLV--------EAADR--------------DGRD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 446 QASLgghvRMIVTGAAPASPTVLGFLRAALGC---QVYEGYGQTECTAGCTFT--TPGDW---TSGHVGAPLPCNHIKLV 517
Cdd:cd17643 209 PLAL----RYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFRplDAADLpaaAASPIGRPLPGLRVYVL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 518 DAEeLNYWTCKGEGEICVKGPNVFKGYLKDEDRTKE-------ALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQG 590
Cdd:cd17643 285 DAD-GRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI-RG 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 75992911 591 EYVAPEKIENIYIRSEPVAQIYV---HGDSLKAFLVGIVVPDPE 631
Cdd:cd17643 363 FRIELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVADDG 406
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
146-634 |
3.23e-17 |
|
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: 84.68 E-value: 3.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 225
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAG--VGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 DkphkatlllehverketpglklvilmepfedalrergkkcgvdiksmqaiedcgrenhhapvpprPDDLSIVCFTSGTT 305
Cdd:cd12115 103 D-----------------------------------------------------------------PDDLAYVIYTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 306 GNPKGAMLTHGNVVA------------DFSGFLKVTEkVIFprqdDVLI--SFLPLahmferviqsvvyCHGGRVGFFQG 371
Cdd:cd12115 118 GRPKGVAIEHRNAAAflqwaaaafsaeELAGVLASTS-ICF----DLSVfeLFGPL-------------ATGGKVVLADN 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 372 DIRLLsDDMKALRPTIFPVVPrllnrmydkifhqadtSLKRWLLEFaakrkqaevrsgiirnnsiwdelffNKIQASlgg 451
Cdd:cd12115 180 VLALP-DLPAAAEVTLINTVP----------------SAAAELLRH-------------------------DALPAS--- 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 452 hVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFT--TPGDWTSGHVGAPLPCNHIKLVDaEELNYWTCK 528
Cdd:cd12115 215 -VRVVNLAGEPLPRDLVQRLYARLqVERVVNLYGPSEDTTYSTVApvPPGASGEVSIGRPLANTQAYVLD-RALQPVPLG 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 529 GEGEICVKGPNVFKGYLKDEDRTKEALDSDGWL------HTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIY 602
Cdd:cd12115 293 VPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAAL 371
|
490 500 510
....*....|....*....|....*....|....*
gi 75992911 603 IRSEPVAQ--IYVHGDSL-KAFLVGIVVPDPEVMP 634
Cdd:cd12115 372 RSIPGVREavVVAIGDAAgERRLVAYIVAEPGAAG 406
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
146-635 |
4.29e-17 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 84.73 E-value: 4.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLLQhdCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIIN--------- 216
Cdd:cd05959 30 LTYAELEAEARRVAGALRA--LGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEdsrarvvvv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 217 TADICTVIVDKPHKATLLLEHVERKE-TPGLKLVILMEPFEDALRERGKkcgvdiksmqaiedcgrenhhaPVPPRPDDL 295
Cdd:cd05959 108 SGELAPVLAAALTKSEHTLVVLIVSGgAGPEAGALLLAELVAAEAEQLK----------------------PAATHADDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 296 SIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKvteKVIFPRQDDVLIS--------------FLPLAH------MFERVI 355
Cdd:cd05959 166 AFWLYSSGSTGRPKGVVHLHADIYWTAELYAR---NVLGIREDDVCFSaaklffayglgnslTFPLSVgattvlMPERPT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 356 QSVVYchggrvgffqgdirllsDDMKALRPTIFPVVPRLLNRMydkifhqadtslkrwlleFAAKRKQAEVRSGIirnns 435
Cdd:cd05959 243 PAAVF-----------------KRIRRYRPTVFFGVPTLYAAM------------------LAAPNLPSRDLSSL----- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 436 iwdelffnkiqaslgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTF--TTPGDWTSGHVGAPLPCNH 513
Cdd:cd05959 283 ------------------RLCVSAGEALPAEVGERWKARFGLDILDGIGSTE--MLHIFlsNRPGRVRYGTTGKPVPGYE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 514 IKLVDaEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSdGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYV 593
Cdd:cd05959 343 VELRD-EDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQG-EWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWV 419
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 75992911 594 APEKIENIYIRSEPVAQIYVHG-------DSLKAFlvgiVVPDPEVMPS 635
Cdd:cd05959 420 SPFEVESALVQHPAVLEAAVVGvededglTKPKAF----VVLRPGYEDS 464
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
292-608 |
4.30e-17 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 84.85 E-value: 4.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKvifpRQDDVLISFLPLAHmferviqsvvychggRVGFFQG 371
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEW----KTKDRILSWMPLTH---------------DMGLIAF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 372 DIRLLSDDMKA-LRPT-IFPVVPRLlnrmydkifhqadtslkrWLLEfAAKRKQAEVRSGIIRNNSIWDELFFNKIQASL 449
Cdd:cd05908 166 HLAPLIAGMNQyLMPTrLFIRRPIL------------------WLKK-ASEHKATIVSSPNFGYKYFLKTLKPEKANDWD 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 450 GGHVRMIVTGAAPASP----------TVLGFLRAAlgcqVYEGYGQTECTAGCTF------------------------- 494
Cdd:cd05908 227 LSSIRMILNGAEPIDYelchefldhmSKYGLKRNA----ILPVYGLAEASVGASLpkaqspfktitlgrrhvthgepepe 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 495 ---TTPGDWTSGHVGAPLPCNHIKLVDaeELNYWTCKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGkWL 570
Cdd:cd05908 303 vdkKDSECLTFVEVGKPIDETDIRICD--EDNKILPDGYiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FI 379
|
330 340 350
....*....|....*....|....*....|....*...
gi 75992911 571 PEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPV 608
Cdd:cd05908 380 RNGRLVITGREKDII-FVNGQNVYPHDIERIAEELEGV 416
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
294-601 |
4.64e-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: 83.08 E-value: 4.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 294 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIfprQDDVLISFLPLAHMFERV-IQSVVYCHGGRVGFfqGD 372
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWV---VGDVTYLPLPATHIGGLWwILTCLIHGGLCVTG--GE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 373 IRLLSDDMKAL---RPTIFPVVPRLLNRMydkifhqadTSLKRWLLEFAAKrkqaevrsgiirnnsiwdelffnkiqasl 449
Cdd:cd17635 77 NTTYKSLFKILttnAVTTTCLVPTLLSKL---------VSELKSANATVPS----------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 450 gghVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDAEELNYWTcK 528
Cdd:cd17635 119 ---LRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLPTDDDSIEiNAVGRPYPGVDVYLAATDGIAGPS-A 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75992911 529 GEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENI 601
Cdd:cd17635 195 SFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERI 265
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
113-613 |
5.38e-17 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 84.81 E-value: 5.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 113 DARTMYQVFRRGLSISGNGPCLGFRKpeqpyQWLSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELAC 192
Cdd:PRK06155 19 SERTLPAMLARQAERYPDRPLLVFGG-----TRWTYAEAARAAAAAAHALAAAGVKRGDR--VALMCGNRIEFLDVFLGC 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 193 YTYSMVVVPLYDTLGPGSISYIINTADICTVIVDkphkATLL--LEHVERKETPGLKLVILmepfeDALRERGKKCGVDI 270
Cdd:PRK06155 92 AWLGAIAVPINTALRGPQLEHILRNSGARLLVVE----AALLaaLEAADPGDLPLPAVWLL-----DAPASVSVPAGWST 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 271 KSMQAIEDCGrenhhAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHgnvvADFSGFLKVTEKVIFPRQDDVLISFLPLAH- 349
Cdd:PRK06155 163 APLPPLDAPA-----PAAAVQPGDTAAILYTSGTTGPSKGVCCPH----AQFYWWGRNSAEDLEIGADDVLYTTLPLFHt 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 350 ----MFervIQSVVycHGGRV---------GFFqgdirllsDDMKALRPTIF----PVVPRLLnrmydkifhqadtslkr 412
Cdd:PRK06155 234 nalnAF---FQALL--AGATYvleprfsasGFW--------PAVRRHGATVTyllgAMVSILL----------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 413 wllefaAKRKQAEVRsgiirnnsiwdelffnkiqaslgGH-VRMIVTGAAPASptVLGFLRAALGCQVYEGYGQTECTAG 491
Cdd:PRK06155 284 ------SQPARESDR-----------------------AHrVRVALGPGVPAA--LHAAFRERFGVDLLDGYGSTETNFV 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 492 CtFTTPGDWTSGHVGAPLPCNHIKLVDAE--ELNywtcKGE-GEICVKG--PNVF-KGYLKDEDRTKEALdSDGWLHTGD 565
Cdd:PRK06155 333 I-AVTHGSQRPGSMGRLAPGFEARVVDEHdqELP----DGEpGELLLRAdePFAFaTGYFGMPEKTVEAW-RNLWFHTGD 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 75992911 566 IGKWLPEGTLKIIDRKKHIFKlAQGEYVAPEKIENIyIRSEP-VAQIYV 613
Cdd:PRK06155 407 RVVRDADGWFRFVDRIKDAIR-RRGENISSFEVEQV-LLSHPaVAAAAV 453
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
132-635 |
2.78e-16 |
|
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: 81.76 E-value: 2.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 132 PCLgfRKPEQPYqwlSYQEVAKRAEFLGSGLLqHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSI 211
Cdd:cd05958 2 TCL--RSPEREW---TYRDLLALANRIANVLV-GELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 212 SYIINTADICTVIVDkphkatlllehverketpglklvilmepfeDALRERgkkcgvdiksmqaiedcgrenhhapvppr 291
Cdd:cd05958 76 AYILDKARITVALCA------------------------------HALTAS----------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 292 pDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkvTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGR--VGFF 369
Cdd:cd05958 97 -DDICILAFTSGTTGAPKATMHFHRDPLASADRY---AVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGAsgVLLE 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 370 QGDIRLLSDDMKALRPTIFPVVPRllnrMYDKIFHQADTSlkrwllefaakrkqaevrsgiirnnsiwdelffnkiqASL 449
Cdd:cd05958 173 EATPDLLLSAIARYKPTVLFTAPT----AYRAMLAHPDAA-------------------------------------GPD 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 450 GGHVRMIVTgAAPASPTVLGFL-RAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNywTCK 528
Cdd:cd05958 212 LSSLRKCVS-AGEALPAALHRAwKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVDDEGNP--VPD 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 529 GE-GEICVKGPNvfkGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSEP 607
Cdd:cd05958 289 GTiGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQHPA 364
|
490 500 510
....*....|....*....|....*....|.
gi 75992911 608 VAQIYVHGDSLKAFLV---GIVVPDPEVMPS 635
Cdd:cd05958 365 VAECAVVGHPDESRGVvvkAFVVLRPGVIPG 395
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
290-628 |
9.13e-16 |
|
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: 80.58 E-value: 9.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 290 PRPDDLSIVCFTSGTTGNPKGAMLTHGNvvadFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERV--IQSVVychggrvg 367
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGT----FAAQIDALRQLYGIRPGEVDLATFPLFALFGPAlgLTSVI-------- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 368 ffqgdirllsDDMKALRPtifpvvprllnrmydkifhqADTSlKRWLLEFAAkrkQAEVrSGIIRNNSIWDEL--FFNKI 445
Cdd:cd05910 150 ----------PDMDPTRP--------------------ARAD-PQKLVGAIR---QYGV-SIVFGSPALLERVarYCAQH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 446 QASLGGhVRMIVTGAAPASPTVLGFLRAAL--GCQVYEGYGQTECTAGCT------FTTPGDWTSGH----VGAPLPCNH 513
Cdd:cd05910 195 GITLPS-LRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrelLATTTAATSGGagtcVGRPIPGVR 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 514 IKLV--DAEELNYWTCKGE------GEICVKGPNVFKGYLKDEDRTKEALDSDG----WLHTGDIGKWLPEGTLKIIDRK 581
Cdd:cd05910 274 VRIIeiDDEPIAEWDDTLElprgeiGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRK 353
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 75992911 582 KHIFKLAQGEYVapekieniyirSEPVAQIY-VHGDSLKAFLVGIVVP 628
Cdd:cd05910 354 AHRVITTGGTLY-----------TEPVERVFnTHPGVRRSALVGVGKP 390
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
446-630 |
1.61e-15 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 80.06 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 446 QASLGGHVRMIVTGAAPasPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGD-WTSghvgapLPCN------------ 512
Cdd:PLN03102 296 LSPRSGPVHVLTGGSPP--PAALVKKVQRLGFQVMHAYGLTEATGPVLFCEWQDeWNR------LPENqqmelkarqgvs 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 513 HIKLVDAEELNYWTC-------KGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIF 585
Cdd:PLN03102 368 ILGLADVDVKNKETQesvprdgKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII 446
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 75992911 586 kLAQGEYVAPEKIENIyirsepvaqIYVHGDSLKAFLVGIvvPDP 630
Cdd:PLN03102 447 -ISGGENISSVEVENV---------LYKYPKVLETAVVAM--PHP 479
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
287-613 |
4.22e-15 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 78.37 E-value: 4.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 287 PVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkVTEKVIFPRQDDVLISfLPLAHmferVI-QSVVY---CH 362
Cdd:PRK09029 129 AVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEG---VLSLMPFTAQDSWLLS-LPLFH----VSgQGIVWrwlYA 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 363 GGRVGFfqGDIRLLSDDMK-----ALRPTifpVVPRLLNRmydkifHQADTSLKRWLLefaakrkqaevrsgiirnnsiw 437
Cdd:PRK09029 201 GATLVV--RDKQPLEQALAgcthaSLVPT---QLWRLLDN------RSEPLSLKAVLL---------------------- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 438 delffnkiqaslGGhvRMIvtgaapasPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTSGhVGAPLPCNHIKLV 517
Cdd:PRK09029 248 ------------GG--AAI--------PVELTEQAEQQGIRCWCGYGLTE-MASTVCAKRADGLAG-VGSPLPGREVKLV 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 518 DaeelnywtckgeGEICVKGPNVFKGYLKDeDRTKEALDSDGWLHTGDIGKWLpEGTLKIIDRKKHIFkLAQGEYVAPEK 597
Cdd:PRK09029 304 D------------GEIWLRGASLALGYWRQ-GQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEE 368
|
330
....*....|....*.
gi 75992911 598 IENIYIRSEPVAQIYV 613
Cdd:PRK09029 369 IERVINQHPLVQQVFV 384
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
119-639 |
4.86e-15 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 78.67 E-value: 4.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 119 QVFRRGLSISGNGPCLGFRKPEQpyQWLSYQEVAKRAEFLGSGLlqHD-CKVGTEQFVGVFAQNRPEWIIAELACYTYSM 197
Cdd:PRK05620 14 RILEYGSTVHGDTTVTTWGGAEQ--EQTTFAAIGARAAALAHAL--HDeLGITGDQRVGSMMYNCAEHLEVLFAVACMGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 198 VVVPLYDTLGPGSISYIINTADIcTVIVDKPHKATLLLEHVerKETPGLKLVILMEPFEDALRERGKKCGVDIKSMQAIE 277
Cdd:PRK05620 90 VFNPLNKQLMNDQIVHIINHAED-EVIVADPRLAEQLGEIL--KECPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 278 DcGRENHHA-PVPPRpDDLSIVCFTSGTTGNPKGAMLTHGNVVADfSGFLKVTEKviFPRQDDVliSFL---PLAHMFER 353
Cdd:PRK05620 167 D-GRSTVYDwPELDE-TTAAAICYSTGTTGAPKGVVYSHRSLYLQ-SLSLRTTDS--LAVTHGE--SFLccvPIYHVLSW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 354 VIQSVVYCHGGrvgffqgdirllsddmkalrPTIFP----VVPRLLnrmydkifHQADTSLKRwllefaakrkqaeVRSG 429
Cdd:PRK05620 240 GVPLAAFMSGT--------------------PLVFPgpdlSAPTLA--------KIIATAMPR-------------VAHG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 430 IirnNSIWDELFFNKIQ-----ASLgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGH 504
Cdd:PRK05620 279 V---PTLWIQLMVHYLKnpperMSL----QEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGE 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 505 VGA---------PLPCNHiKLVDAEELNYWTCKGEGEICVKGPNVFKGYLKDE----------------DRTKEALDSDG 559
Cdd:PRK05620 352 ARWayrvsqgrfPASLEY-RIVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADG 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 560 WLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSEPVaqiyvhgdsLKAFLVGIvvPDPEvmpsWAQK 639
Cdd:PRK05620 431 WLRTGDVGSVTRDGFLTIHDRARDVIR-SGGEWIYSAQLENYIMAAPEV---------VECAVIGY--PDDK----WGER 494
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
177-630 |
5.41e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 78.54 E-value: 5.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 177 VFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV--DKPhkatlllEHVE--RKETPGLKLVIlm 252
Cdd:PRK07470 62 VHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMIChaDFP-------EHAAavRAASPDLTHVV-- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 253 ePFEDALRERGkkcgvdiksmqaIEDCGRENHHAPVPPRP---DDLSIVCFTSGTTGNPKGAMLTHG-------NVVADf 322
Cdd:PRK07470 133 -AIGGARAGLD------------YEALVARHLGARVANAAvdhDDPCWFFFTSGTTGRPKAAVLTHGqmafvitNHLAD- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 323 sgflkvtekvIFP--RQDDVLISFLPLAHMfERVIQSVVYCHGGRVGFFQGDiRLLSDDMKAL----RPTIFPVVPRLLN 396
Cdd:PRK07470 199 ----------LMPgtTEQDASLVVAPLSHG-AGIHQLCQVARGAATVLLPSE-RFDPAEVWALverhRVTNLFTVPTILK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 397 RMY-DKIFHQADTSlkrwllefaakrkqaevrsgiirnnsiwdelffnkiqaSLgghvRMIVTGAAPASPTVLGFLRAAL 475
Cdd:PRK07470 267 MLVeHPAVDRYDHS--------------------------------------SL----RYVIYAGAPMYRADQKRALAKL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 476 GCQVYEGYGQTECTAGCTFTTP-----GDWTSGHVGaplPCNH------IKLVDAE--ELNywtcKGE-GEICVKGPNVF 541
Cdd:PRK07470 305 GKVLVQYFGLGEVTGNITVLPPalhdaEDGPDARIG---TCGFertgmeVQIQDDEgrELP----PGEtGEICVIGPAVF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 542 KGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENiyirsepvaQIYVHGDSLKAF 621
Cdd:PRK07470 378 AGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPREIEE---------KLLTHPAVSEVA 446
|
....*....
gi 75992911 622 LVGivVPDP 630
Cdd:PRK07470 447 VLG--VPDP 453
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
482-638 |
1.01e-14 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 75.80 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 482 GYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAE--ELNywtcKGE-GEICVKGPNVFKGYLkDEDRTKEALDSD 558
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDgrEVP----DGEvGEIVARGPTVMAGYW-NRPEVNARRTRG 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 559 GWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqgeyvapekIENIY-------IRSEP-VAQIYVhgdslkaflvgIVVPDp 630
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSG---------AENIYpaevercLRQHPaVADAAV-----------IGVPD- 275
|
....*...
gi 75992911 631 evmPSWAQ 638
Cdd:cd17636 276 ---PRWAQ 280
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
146-635 |
1.01e-14 |
|
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: 77.38 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIIntADICTVIV 225
Cdd:cd17651 21 LTYAELDRRANRLAHRLRARG--VGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFML--ADAGPVLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 dkphkatlLLEHVERKETPG-LKLVILMEPFEDAlrergkkcgvdiksmqaieDCGRENHhaPVPPRPDDLSIVCFTSGT 304
Cdd:cd17651 97 --------LTHPALAGELAVeLVAVTLLDQPGAA-------------------AGADAEP--DPALDADDLAYVIYTSGS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 305 TGNPKGAMLTHGNVVadfsGFLKVTEKVIFPRQDDVLISFLPLAhmFERVIQSV--VYCHGGRVGFFQGDIRLLSDDMKA 382
Cdd:cd17651 148 TGRPKGVVMPHRSLA----NLVAWQARASSLGPGARTLQFAGLG--FDVSVQEIfsTLCAGATLVLPPEEVRTDPPALAA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 383 LrptifpvvprLLNRMYDKIFhqADTSLKRWLLEfAAKRKQAEvrsgiirnnsiwdelffnkiqaslGGHVRMIVTG--A 460
Cdd:cd17651 222 W----------LDEQRISRVF--LPTVALRALAE-HGRPLGVR------------------------LAALRYLLTGgeQ 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 461 APASPTVLGFLRAALGCQVYEGYGQTE---CTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDAeelnywtcKGE------ 530
Cdd:cd17651 265 LVLTEDLREFCAGLPGLRLHNHYGPTEthvVTALSLPGDPAAWPApPPIGRPIDNTRVYVLDA--------ALRpvppgv 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 531 -GEICVKGPNVFKGYLKDEDRTKEALDSDGWL------HTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYI 603
Cdd:cd17651 337 pGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGFRIELGEIEAALA 415
|
490 500 510
....*....|....*....|....*....|....*...
gi 75992911 604 RSEPVAQIYV------HGDslkAFLVGIVVPDPEVMPS 635
Cdd:cd17651 416 RHPGVREAVVlaredrPGE---KRLVAYVVGDPEAPVD 450
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
445-613 |
4.72e-14 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 74.91 E-value: 4.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 445 IQASLGG---HVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTfTTPGD-WTSGHVGAPLPCNHIKLVDAE 520
Cdd:cd05974 191 IQQDLASfdvKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVG-NSPGQpVKAGSMGRPLPGYRVALLDPD 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 521 ElnywTCKGEGEICV-----KGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAP 595
Cdd:cd05974 270 G----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SSDYRISP 343
|
170
....*....|....*...
gi 75992911 596 EKIENIYIRSEPVAQIYV 613
Cdd:cd05974 344 FELESVLIEHPAVAEAAV 361
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
301-631 |
5.67e-14 |
|
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: 75.06 E-value: 5.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 301 TSGTTGNPKGAMLTHgnvvADFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERV---IQSVVYChGGRVgffqgdirLLS 377
Cdd:cd05920 147 SGGTTGTPKLIPRTH----NDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLAcpgVLGTLLA-GGRV--------VLA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 378 DDMKALrpTIFPVVPRllnrmyDKIFHqadTSL-----KRWLlEFAAKRkqaevrsgiirnnsiwdelffnkiQASLGGH 452
Cdd:cd05920 214 PDPSPD--AAFPLIER------EGVTV---TALvpalvSLWL-DAAASR------------------------RADLSSL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 453 vRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHVGAPL-PCNHIKLVDAEELNywTCKGE 530
Cdd:cd05920 258 -RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTrLDDPDEVIIHTQGRPMsPDDEIRVVDEEGNP--VPPGE 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 531 -GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENiyirsepva 609
Cdd:cd05920 335 eGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVEN--------- 404
|
330 340
....*....|....*....|..
gi 75992911 610 QIYVHGDSLKAFLVGivVPDPE 631
Cdd:cd05920 405 LLLRHPAVHDAAVVA--MPDEL 424
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
292-603 |
7.67e-14 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 74.85 E-value: 7.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAHMFerviqsvvychggrvGFfqG 371
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFS----PKEDDVMMSFLPPFHAY---------------GF--N 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 372 DIRLLSddMKALRPTIF---PVVPRLLNRMYDK---IFHQADTSLKRWLLEFAAKRKQA--EVRSGIIRNNSIWDELFfn 443
Cdd:PRK06334 241 SCTLFP--LLSGVPVVFaynPLYPKKIVEMIDEakvTFLGSTPVFFDYILKTAKKQESClpSLRFVVIGGDAFKDSLY-- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 444 kiqaslgghvrmivTGAAPASPTVlgflraalgcQVYEGYGQTECTAGCTFTT---PGDwtSGHVGAPLPCNHIKLVdAE 520
Cdd:PRK06334 317 --------------QEALKTFPHI----------QLRQGYGTTECSPVITINTvnsPKH--ESCVGMPIRGMDVLIV-SE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 521 ELNYWTCKGE-GEICVKGPNVFKGYL-KDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKI 598
Cdd:PRK06334 370 ETKVPVSSGEtGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSLEAL 448
|
....*
gi 75992911 599 ENIYI 603
Cdd:PRK06334 449 ESILM 453
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
144-664 |
1.28e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 74.99 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 144 QWLSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGS-ISYIINTAdict 222
Cdd:PRK12316 4575 EKLTYAELNRRANRLAHALIARG--VGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPL-DPEYPRErLAYMMEDS---- 4647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 223 vivdkphKATLLLEHveRKETPGLklvilmePFEDalrergkkcGVDIKSMQAIED-CGRENHHAPVPPRPDDLSIVCFT 301
Cdd:PRK12316 4648 -------GAALLLTQ--SHLLQRL-------PIPD---------GLASLALDRDEDwEGFPAHDPAVRLHPDNLAYVIYT 4702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 302 SGTTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPLAhmFERVIQSV--VYCHGGRVgffqgdirLLSDD 379
Cdd:PRK12316 4703 SGSTGRPKGVAVSHGSLVN----HLHATGERYELTPDDRVLQFMSFS--FDGSHEGLyhPLINGASV--------VIRDD 4768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 380 MKALRPTIFpvvpRLLNRMYDKIFHQADTSLKRWLLEFAAKRKQAEVRsgiirnnsiwdelffnkiQASLGGHvrmivtG 459
Cdd:PRK12316 4769 SLWDPERLY----AEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLR------------------VYCFGGE------A 4820
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 460 AAPASPTVLgfLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSG----HVGAPLPCNHIKLVDaEELNYWTCKGEGEIC 534
Cdd:PRK12316 4821 VAQASYDLA--WRALKPVYLFNGYGPTETTVTVLlWKARDGDACGaaymPIGTPLGNRSGYVLD-GQLNPLPVGVAGELY 4897
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 535 VKGPNVFKGYLKDEDRTKEALDSD------GWLH-TGDIGKWLPEGTLKIIDRKKHI-----FKLAQGEYVAPEKiENIY 602
Cdd:PRK12316 4898 LGGEGVARGYLERPALTAERFVPDpfgapgGRLYrTGDLARYRADGVIDYLGRVDHQvkirgFRIELGEIEARLR-EHPA 4976
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75992911 603 IRSEPVaqIYVHGdSLKAFLVGIVVP-DPEVMPSWAQKKGIEGTyqelcMKKELKKAILDDMV 664
Cdd:PRK12316 4977 VREAVV--IAQEG-AVGKQLVGYVVPqDPALADADEAQAELRDE-----LKAALRERLPEYMV 5031
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
111-664 |
2.68e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 74.04 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 111 YDDARTMYQVFRRGLSISGNGPCLGFRKpeqpyQWLSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAEL 190
Cdd:PRK12467 1570 YPLARLVHQLIEDQAAATPEAVALVFGE-----QELTYGELNRRANRLAHRLIALG--VGPEVLVGIAVERSLEMVVGLL 1642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 191 ACYTYSMVVVPLYDTLGPGSISYIINTADIctvivdkphkaTLLLEH---VERKETP-GLKLVILmEPFEDALRergkkc 266
Cdd:PRK12467 1643 AILKAGGAYVPLDPEYPRERLAYMIEDSGI-----------ELLLTQshlQARLPLPdGLRSLVL-DQEDDWLE------ 1704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 267 gvdiksmqaiedcGRENHHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFsgflKVTEKVIFPRQDDVLISFLP 346
Cdd:PRK12467 1705 -------------GYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRL----CATQEAYQLSAADVVLQFTS 1767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 347 LAhmFERVIQSVVY--CHGGRVgffqgdirLLSDDMKALRPTIFpvvPRLLNRMYDKIFHQADTSLKRwLLEFAAkrKQA 424
Cdd:PRK12467 1768 FA--FDVSVWELFWplINGARL--------VIAPPGAHRDPEQL---IQLIERQQVTTLHFVPSMLQQ-LLQMDE--QVE 1831
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 425 EVRSgiirnnsiwdelffnkiqaslgghVRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAG-----CTFTTPG 498
Cdd:PRK12467 1832 HPLS------------------------LRRVVCGGEALEVEALRPWLERLPdTGLFNLYGPTETAVDvthwtCRRKDLE 1887
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 499 DWTSGHVGAPLPCNHIKLVDAeELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEAL------DSDGWLH-TGDIGKWLP 571
Cdd:PRK12467 1888 GRDSVPIGQPIANLSTYILDA-SLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgTVGSRLYrTGDLARYRA 1966
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 572 EGTLKIIDRKKHIFKLaQGEYVAPEKIENiYIRSEP----VAQIYVHGDSLKAfLVGIVVPDPEVMPSWAQKKgieGTYQ 647
Cdd:PRK12467 1967 DGVIEYLGRIDHQVKI-RGFRIELGEIEA-RLREQGgvreAVVIAQDGANGKQ-LVAYVVPTDPGLVDDDEAQ---VALR 2040
|
570
....*....|....*..
gi 75992911 648 ELcMKKELKKAILDDMV 664
Cdd:PRK12467 2041 AI-LKNHLKASLPEYMV 2056
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
280-631 |
3.10e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 73.04 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 280 GRENHHAPVPPRPDdlSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLkvtEKVIFPRQDDVLISflplAHMFerviqsvv 359
Cdd:PRK07788 196 GSSTAPLPKPPKPG--GIVILTSGTTGTPKGAPRPEPSPLAPLAGLL---SRVPFRAGETTLLP----APMF-------- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 360 ycHGgrVGFFQGDIRLlsddmkALRPTIfpVVPRLL---NRMYDKIFHQAD------TSLKRwLLEFAAKRKQA-EVRSg 429
Cdd:PRK07788 259 --HA--TGWAHLTLAM------ALGSTV--VLRRRFdpeATLEDIAKHKATalvvvpVMLSR-ILDLGPEVLAKyDTSS- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 430 iirnnsiwdelffnkiqaslgghVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECtAGCTFTTPGDWT--SGHVGA 507
Cdd:PRK07788 325 -----------------------LKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEV-AFATIATPEDLAeaPGTVGR 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 508 PLPCNHIKLVDAE--ELNywtcKGE-GEICVKGPNVFKGYLkdEDRTKEALdsDGWLHTGDIGKWLPEGTLKIIDRKKHI 584
Cdd:PRK07788 381 PPKGVTVKILDENgnEVP----RGVvGRIFVGNGFPFEGYT--DGRDKQII--DGLLSSGDVGYFDEDGLLFVDGRDDDM 452
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 75992911 585 FkLAQGEYVAPEKIENIYIRSEPVAQIYVHGdslkaflvgivVPDPE 631
Cdd:PRK07788 453 I-VSGGENVFPAEVEDLLAGHPDVVEAAVIG-----------VDDEE 487
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
144-624 |
3.56e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 73.84 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 144 QWLSYQEVAKRAEFLGSGLLqhDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGS-ISYIINTADICT 222
Cdd:PRK12316 2027 QHLSYAELDSRANRLAHRLR--ARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPL-DPNYPAErLAYMLEDSGAAL 2103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 223 VIVDKPHKATLLLehverketPGLKLVILMEPfEDALRERgkkcgvdiksmqaiedcgrENHHAPVPPRPDDLSIVCFTS 302
Cdd:PRK12316 2104 LLTQRHLLERLPL--------PAGVARLPLDR-DAEWADY-------------------PDTAPAVQLAGENLAYVIYTS 2155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 303 GTTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPLAhmFERVIQSVVY--CHGGRVgffqgdirLLSDDM 380
Cdd:PRK12316 2156 GSTGLPKGVAVSHGALVA----HCQAAGERYELSPADCELQFMSFS--FDGAHEQWFHplLNGARV--------LIRDDE 2221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 381 KalrptifpvvpRLLNRMYDKIFHQADTslkrwLLEFAAKRKQAEVRSGIIRNNSIwdelffnkiqaslggHVRMIVTGA 460
Cdd:PRK12316 2222 L-----------WDPEQLYDEMERHGVT-----ILDFPPVYLQQLAEHAERDGRPP---------------AVRVYCFGG 2270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 461 APASPTVLGFLRAALGCQ-VYEGYGQTEctagcTFTTPGDWTSGH----------VGAPLPCNHIKLVDAeELNYWTCKG 529
Cdd:PRK12316 2271 EAVPAASLRLAWEALRPVyLFNGYGPTE-----AVVTPLLWKCRPqdpcgaayvpIGRALGNRRAYILDA-DLNLLAPGM 2344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 530 EGEICVKGPNVFKGYLKDEDRTKEALDSDGWLH-------TGDIGKWLPEGTLKIIDRKKHI-----FKLAQGEYVApEK 597
Cdd:PRK12316 2345 AGELYLGGEGLARGYLNRPGLTAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQvkirgFRIELGEIEA-RL 2423
|
490 500
....*....|....*....|....*...
gi 75992911 598 IENIYIRSEPV-AQIYVHGDSLKAFLVG 624
Cdd:PRK12316 2424 QAHPAVREAVVvAQDGASGKQLVAYVVP 2451
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
286-649 |
5.66e-13 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 71.85 E-value: 5.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 286 APVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkvteKVIFP-RQDDVLISFLPLAHMFERV--IQSVVych 362
Cdd:PRK09274 167 PMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEAL-----REDYGiEPGEIDLPTFPLFALFGPAlgMTSVI--- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 363 ggrvgffqgdirllsDDMKALRP-TIFPvvprllnrmyDKIFHQAD----TSLkrwlleFAA-----KRKQAEVRSGIIR 432
Cdd:PRK09274 239 ---------------PDMDPTRPaTVDP----------AKLFAAIErygvTNL------FGSpalleRLGRYGEANGIKL 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 433 NNsiwdelffnkiqaslgghVRMIVTGAAPASPTVLGFLRAAL--GCQVYEGYGQTECTAGCT-------FTTPGDWTSG 503
Cdd:PRK09274 288 PS------------------LRRVISAGAPVPIAVIERFRAMLppDAEILTPYGATEALPISSiesreilFATRAATDNG 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 504 H---VGAPLPCNHIKLV--DAEELNYWT-----CKGE-GEICVKGPNVFKGYLKDEDRTKEA--LDSDG--WLHTGDIGk 568
Cdd:PRK09274 350 AgicVGRPVDGVEVRIIaiSDAPIPEWDdalrlATGEiGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLG- 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 569 WL-PEGTLKIIDRKKHIFKLAQGEYVapekieniyirSEPVAQIY-VHGDSLKAFLVGIVVPD---P----EVMPSWAQK 639
Cdd:PRK09274 429 YLdAQGRLWFCGRKAHRVETAGGTLY-----------TIPCERIFnTHPGVKRSALVGVGVPGaqrPvlcvELEPGVACS 497
|
410
....*....|
gi 75992911 640 KgiEGTYQEL 649
Cdd:PRK09274 498 K--SALYQEL 505
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
296-711 |
7.50e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 71.66 E-value: 7.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 296 SIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVgFFQG---D 372
Cdd:PRK07008 179 SSLCYTSGTTGNPKGALYSHRSTV--LHAYGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPLTGAKL-VLPGpdlD 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 373 IRLLSDDMKALRPTIFPVVPR----LLNRMydkifhqadtslkrwllefaakrKQAEVRSGIIRnnsiwdelffnkiqas 448
Cdd:PRK07008 256 GKSLYELIEAERVTFSAGVPTvwlgLLNHM-----------------------REAGLRFSTLR---------------- 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 449 lgghvRMIVTGAApASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPgdwTSGHVGAPLPCNH--------------I 514
Cdd:PRK07008 297 -----RTVIGGSA-CPPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLCKL---KWKHSQLPLDEQRkllekqgrviygvdM 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 515 KLVDAE--ELNyWTCKGEGEICVKGPNVFKGYLKDEDrtkEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEY 592
Cdd:PRK07008 368 KIVGDDgrELP-WDGKAFGDLQVRGPWVIDRYFRGDA---SPLV-DGWFPTGDVATIDADGFMQITDRSKDVIK-SGGEW 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 593 VAPEKIENIYIRSEPVAQIYVhgdslkaflvgIVVPDPEvmpsW--------AQKKGIEGTYQELCMKKELKKA---ILD 661
Cdd:PRK07008 442 ISSIDIENVAVAHPAVAEAAC-----------IACAHPK----WderpllvvVKRPGAEVTREELLAFYEGKVAkwwIPD 506
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 75992911 662 DMVMlgkesglhsfeqVKAIyihcdmfsvqngLLTPTLKAKRPELREYFK 711
Cdd:PRK07008 507 DVVF------------VDAI------------PHTATGKLQKLKLREQFR 532
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
111-664 |
8.68e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 72.30 E-value: 8.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 111 YDDARTMYQVFRRGLSISGNGPCLGFRKpeqpyQWLSYQEVAKRAEFLGSGLLQHDckVGTEQFVGVFAQNRPEWIIAEL 190
Cdd:PRK12316 3053 YPLERGVHRLFEEQVERTPDAVALAFGE-----QRLSYAELNRRANRLAHRLIERG--VGPDVLVGVAVERSLEMVVGLL 3125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 191 ACYTYSMVVVPLYDTLGPGSISYIINTADIcTVIVDKPHkatLLLEHVERKEtpglklVILMEPFEDALRErgkkcgvdi 270
Cdd:PRK12316 3126 AILKAGGAYVPLDPEYPEERLAYMLEDSGA-QLLLSQSH---LRLPLAQGVQ------VLDLDRGDENYAE--------- 3186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 271 ksmqaiedcgrenHHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNvvadFSGFLKVTEKVIFPRQDDVLISFLPLAHM 350
Cdd:PRK12316 3187 -------------ANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSA----LSNHLCWMQQAYGLGVGDRVLQFTTFSFD 3249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 351 FERVIQSVVYCHGGRVgfFQGDIRLLSDdmkalrptifpvvPRLLNRMYDKifHQADTSLKRWllefaakrkqaevrsgi 430
Cdd:PRK12316 3250 VFVEELFWPLMSGARV--VLAGPEDWRD-------------PALLVELINS--EGVDVLHAYP----------------- 3295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 431 irnnSIWDELFFNKIQASLGGHVRMIVTGAAPASPtvlGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGH--VGAP 508
Cdd:PRK12316 3296 ----SMLQAFLEEEDAHRCTSLKRIVCGGEALPAD---LQQQVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRP 3368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 509 LPCNHIKLVDAeELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGW------LHTGDIGKWLPEGTLKIIDRKK 582
Cdd:PRK12316 3369 IANRACYILDG-SLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVD 3447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 583 HIFKLaQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAfLVGIVVPDPEvmpswaqkkgiEGTYQELcMKKELKKAILDD 662
Cdd:PRK12316 3448 HQVKI-RGFRIELGEIEARLLEHPWVREAVVLAVDGRQ-LVAYVVPEDE-----------AGDLREA-LKAHLKASLPEY 3513
|
..
gi 75992911 663 MV 664
Cdd:PRK12316 3514 MV 3515
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
146-630 |
1.06e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 71.07 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 225
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGPGDH--VGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 DK---PHKATLLlehverKETPGLKLVILMEpfeDALRERGKKCGVDIKSMQAIEDCGREnhhaPVPPRPDDLSIVCfTS 302
Cdd:PRK07798 107 ERefaPRVAEVL------PRLPKLRTLVVVE---DGSGNDLLPGAVDYEDALAAGSPERD----FGERSPDDLYLLY-TG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 303 GTTGNPKGAMLTHGNV-VADFSGFLKVTEKVIfprQDDVLIS----------FLPLAHMFERVIQSVVYchggrVGFFQG 371
Cdd:PRK07798 173 GTTGMPKGVMWRQEDIfRVLLGGRDFATGEPI---EDEEELAkraaagpgmrRFPAPPLMHGAGQWAAF-----AALFSG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 372 DIRLLSDDMKalrptifpVVPRLLNRMYDKifHQAdTSL-------KRWLLEFAAKRKQAEVRSgiirnnsiwdelffnk 444
Cdd:PRK07798 245 QTVVLLPDVR--------FDADEVWRTIER--EKV-NVItivgdamARPLLDALEARGPYDLSS---------------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 445 iqaslgghVRMIVTGAAPASPTV-LGFLRAALGCQVYEGYGQTECTAGCTFTTPGDwtSGHVGAPL--PCNHIKLVDaEE 521
Cdd:PRK07798 298 --------LFAIASGGALFSPSVkEALLELLPNVVLTDSIGSSETGFGGSGTVAKG--AVHTGGPRftIGPRTVVLD-ED 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 522 LNYWTcKGEGEICV--KGPNVFKGYLKDEDRTKEALDS-DG--WLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPE 596
Cdd:PRK07798 367 GNPVE-PGSGEIGWiaRRGHIPLGYYKDPEKTAETFPTiDGvrYAIPGDRARVEADGTITLLGRGSVCINTG-GEKVFPE 444
|
490 500 510
....*....|....*....|....*....|....
gi 75992911 597 KIENIyIRSepvaqiyvHGDSLKAFLVGivVPDP 630
Cdd:PRK07798 445 EVEEA-LKA--------HPDVADALVVG--VPDE 467
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
146-631 |
1.52e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 70.49 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 225
Cdd:PRK13391 25 VTYRELDERSNRLAHLFRSLGLKRGDH--VAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALIT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 DKPHK--ATLLLEHVerketPGLKLVILMEPFEDalRERgkkcgvdiksMQAIEDCGRENHHAPVP--PRPDDLsivCFT 301
Cdd:PRK13391 103 SAAKLdvARALLKQC-----PGVRHRLVLDGDGE--LEG----------FVGYAEAVAGLPATPIAdeSLGTDM---LYS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 302 SGTTGNPKG--AMLTHGNVVaDFSGFLKVTEKVIFPRQDDVLISFLPLAH----MFERVIQSVvychGGRV----GFfqg 371
Cdd:PRK13391 163 SGTTGRPKGikRPLPEQPPD-TPLPLTAFLQRLWGFRSDMVYLSPAPLYHsapqRAVMLVIRL----GGTVivmeHF--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 372 dirllsDDMKAL------RPTIFPVVPRLLNRMydkifhqadtsLKrwLLEfaAKRKQAEVRSgiirnnsiwdelffnki 445
Cdd:PRK13391 235 ------DAEQYLalieeyGVTHTQLVPTMFSRM-----------LK--LPE--EVRDKYDLSS----------------- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 446 qaslgghVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCN-HIKLVDAEEL 522
Cdd:PRK13391 277 -------LEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATE-GLGFTACDSEEWLAhpGTVGRAMFGDlHILDDDGAEL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 523 NywtcKGE-GEICVKGPNVFKgYLKDEDRTKEALDSDG-WLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIEN 600
Cdd:PRK13391 349 P----PGEpGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMI-ISGGVNIYPQEAEN 422
|
490 500 510
....*....|....*....|....*....|.
gi 75992911 601 IYIRSEPVAQIYVHGdslkaflvgivVPDPE 631
Cdd:PRK13391 423 LLITHPKVADAAVFG-----------VPNED 442
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
175-632 |
1.72e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 70.48 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 175 VGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIVDKPHKATL--LLEHVERKETPGLKLVILM 252
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLdgLDPGVRVINVDSPAWADEL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 253 EPFEDALRErgkkcgvdiksmqaiedcgrenhhaPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVTEKV 332
Cdd:PRK07867 137 AAHRDAEPP-------------------------FRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVA--SAGVMLAQRFG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 333 IFPrqDDVLISFLPLAHMfERVIQ--SVVYCHGGRV---------GFFqgdirllsDDMKALRPTIFPVVPRLLN----- 396
Cdd:PRK07867 190 LGP--DDVCYVSMPLFHS-NAVMAgwAVALAAGASIalrrkfsasGFL--------PDVRRYGATYANYVGKPLSyvlat 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 397 --RMYDkifhqADTSLKrwllefaakrkqaevrsgiirnnsiwdelffnkiqaslgghvrmIVTGAAPASPTVLGFlRAA 474
Cdd:PRK07867 259 peRPDD-----ADNPLR--------------------------------------------IVYGNEGAPGDIARF-ARR 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 475 LGCQVYEGYGQTEctAGCTFTTPGDWTSGHVGaPLPCNhIKLVDAE--------------ELNYWTCKGEgEICVKGPNV 540
Cdd:PRK07867 289 FGCVVVDGFGSTE--GGVAITRTPDTPPGALG-PLPPG-VAIVDPDtgtecppaedadgrLLNADEAIGE-LVNTAGPGG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 541 FKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYVHGdslka 620
Cdd:PRK07867 364 FEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPIERILLRYPDATEVAVYA----- 436
|
490
....*....|..
gi 75992911 621 flvgivVPDPEV 632
Cdd:PRK07867 437 ------VPDPVV 442
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
452-623 |
2.07e-12 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 70.19 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 452 HVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDaEELNYWTCKGEG 531
Cdd:cd05928 292 SLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIID-DNGNVLPPGTEG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 532 EICVK-GPN----VFKGYLKDEDRTKEALDSDGWLhTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSE 606
Cdd:cd05928 371 DIGIRvKPIrpfgLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYRIGPFEVESALIEHP 448
|
170 180
....*....|....*....|....
gi 75992911 607 PVAQIYV-------HGDSLKAFLV 623
Cdd:cd05928 449 AVVESAVvsspdpiRGEVVKAFVV 472
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
286-623 |
2.36e-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: 69.87 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 286 APVPPRPDDLSIVCFTSGTTGNPKGAMLTHGN--VVADFSGflkvtEKVIFPRQDDVLIS--------------FLPLA- 348
Cdd:TIGR02262 154 KPAATQADDPAFWLYSSGSTGMPKGVVHTHSNpyWTAELYA-----RNTLGIREDDVCFSaaklffayglgnalTFPMSv 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 349 -----HMFERVIQSVVYchggrvgffqgdirllsDDMKALRPTIFPVVPRLLNRMYdkifhqADTSLKrwllefaaKRKQ 423
Cdd:TIGR02262 229 gattvLMGERPTPDAVF-----------------DRLRRHQPTIFYGVPTLYAAML------ADPNLP--------SEDQ 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 424 AEVRsgiirnnsiwdelffnkiqaslgghvrmIVTGAAPASPTVLGF-LRAALGCQVYEGYGQTEctAGCTFTT--PGDW 500
Cdd:TIGR02262 278 VRLR----------------------------LCTSAGEALPAEVGQrWQARFGVDIVDGIGSTE--MLHIFLSnlPGDV 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 501 TSGHVGAPLPCNHIKLVDaeELNYWTCKGE-GEICVKGPNVFKGYLKDEDRTKEALDSdGWLHTGDigKWL--PEGTLKI 577
Cdd:TIGR02262 328 RYGTSGKPVPGYRLRLVG--DGGQDVADGEpGELLISGPSSATMYWNNRAKSRDTFQG-EWTRSGD--KYVrnDDGSYTY 402
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 75992911 578 IDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQIYVHG----DSL---KAFLV 623
Cdd:TIGR02262 403 AGRTDDMLKVS-GIYVSPFEIESALIQHPAVLEAAVVGvadeDGLikpKAFVV 454
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
299-615 |
3.35e-12 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 69.40 E-value: 3.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 299 CFTSGTTGNPKGAMLTHgnvvadfsgflkvtekvifpRQDdvlisflplahmferVIQSVVYCHGGRVGFFQGDirllsd 378
Cdd:PRK06018 183 CYTSGTTGDPKGVLYSH--------------------RSN---------------VLHALMANNGDALGTSAAD------ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 379 dmkalrpTIFPVVPrllnrmydkIFHqADTslkrWLLEFAAKRKQAE-VRSGI-IRNNSIWDELFFNKIQASLG------ 450
Cdd:PRK06018 222 -------TMLPVVP---------LFH-ANS----WGIAFSAPSMGTKlVMPGAkLDGASVYELLDTEKVTFTAGvptvwl 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 451 -------------GHVRMIVTGAApASPTvlGFLRA--ALGCQVYEGYGQTECTAGCTFTT--------PGDWTSGHV-- 505
Cdd:PRK06018 281 mllqymekeglklPHLKMVVCGGS-AMPR--SMIKAfeDMGVEVRHAWGMTEMSPLGTLAAlkppfsklPGDARLDVLqk 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 506 -GAPLPCNHIKLVD--AEELNyWTCKGEGEICVKGPNVFKGYLKDEDrtkEALDSDGWLHTGDIGKWLPEGTLKIIDRKK 582
Cdd:PRK06018 358 qGYPPFGVEMKITDdaGKELP-WDGKTFGRLKVRGPAVAAAYYRVDG---EILDDDGFFDTGDVATIDAYGYMRITDRSK 433
|
330 340 350
....*....|....*....|....*....|...
gi 75992911 583 HIFKlAQGEYVAPEKIENIYIRSEPVAQIYVHG 615
Cdd:PRK06018 434 DVIK-SGGEWISSIDLENLAVGHPKVAEAAVIG 465
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
446-584 |
3.56e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 69.59 E-value: 3.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 446 QASLGGHVRMIVTGAAPAsPTVLGFLRAAlGCQVYEGYGQTEcTAG----CTFTtpGDWTS----------GHVGAPLPC 511
Cdd:PRK08162 292 RAGIDHPVHAMVAGAAPP-AAVIAKMEEI-GFDLTHVYGLTE-TYGpatvCAWQ--PEWDAlplderaqlkARQGVRYPL 366
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75992911 512 -NHIKLVDAEELNYWTCKGE--GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHI 584
Cdd:PRK08162 367 qEGVTVLDPDTMQPVPADGEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDI 441
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
292-635 |
1.49e-11 |
|
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: 67.07 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVTEKVIFPRQDDVLISFLPLAhmFERVIQS--VVYCHGGRVgff 369
Cdd:cd17644 105 PENLAYVIYTSGSTGKPKGVMIEHQSLV----NLSHGLIKEYGITSSDRVLQFASIA--FDVAAEEiyVTLLSGATL--- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 370 qgdirllsddmkALRPT-IFPVVPRllnrMYDKIfhqadtslkrwllefaaKRKQAEVRSgiiRNNSIWDELFFNKIQAS 448
Cdd:cd17644 176 ------------VLRPEeMRSSLED----FVQYI-----------------QQWQLTVLS---LPPAYWHLLVLELLLST 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 449 LGG--HVRMIVTGAAPASPTVLGFLRAALG--CQVYEGYGQTECTAGCTFTTPGDWTSGH-----VGAPLPCNHIKLVDa 519
Cdd:cd17644 220 IDLpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIANTQVYILD- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 520 EELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLH--------TGDIGKWLPEGTLKIIDRKKHIFKLaQGE 591
Cdd:cd17644 299 ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKI-RGF 377
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 75992911 592 YVAPEKIENIYIRSEPVAQ--IYVHGDSL-KAFLVGIVVPDPEVMPS 635
Cdd:cd17644 378 RIELGEIEAVLSQHNDVKTavVIVREDQPgNKRLVAYIVPHYEESPS 424
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
146-582 |
1.97e-11 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 67.34 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGS-ISYI------INTA 218
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALGLKPGDR--VALIAETDGDFVEAFFACQYAGLVPVPLPLPMGFGGrESYIaqlrgmLASA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 219 DICTVIVDKphkatLLLEHVErKETPGLKLVILMEPFEDALRERGkkcGVDIKsmqaiedcgrenhhapvPPRPDDLSIV 298
Cdd:PRK09192 128 QPAAIITPD-----ELLPWVN-EATHGNPLLHVLSHAWFKALPEA---DVALP-----------------RPTPDDIAYL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 299 CFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifpRQDDVLISFLPLAH-MferviqsvvychgGRVGFF------Qg 371
Cdd:PRK09192 182 QYSSGSTRFPRGVIITHRALMANLRAISHDGLKV---RPGDRCVSWLPFYHdM-------------GLVGFLltpvatQ- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 372 dirlLSDDMkaLRPTIFPVVP----RLLNR-----MYDKIFHqadtslkrwlLEFAAKRkqAEVRSGIIRNNSIWdelff 442
Cdd:PRK09192 245 ----LSVDY--LPTRDFARRPlqwlDLISRnrgtiSYSPPFG----------YELCARR--VNSKDLAELDLSCW----- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 443 nkiqaslgghvRMIVTGAAPASPTVL----------GF-LRAALGCqvyegYGQTECTAGCTFTTPG----------DWT 501
Cdd:PRK09192 302 -----------RVAGIGADMIRPDVLhqfaeafapaGFdDKAFMPS-----YGLAEATLAVSFSPLGsgivveevdrDRL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 502 SGH------------------VGAPLPCNHIKLVDA--EELNYwtcKGEGEICVKGPNVFKGYLKDEDRTKeALDSDGWL 561
Cdd:PRK09192 366 EYQgkavapgaetrrvrtfvnCGKALPGHEIEIRNEagMPLPE---RVVGHICVRGPSLMSGYFRDEESQD-VLAADGWL 441
|
490 500
....*....|....*....|.
gi 75992911 562 HTGDIGkWLPEGTLKIIDRKK 582
Cdd:PRK09192 442 DTGDLG-YLLDGYLYITGRAK 461
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
146-638 |
5.22e-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: 65.35 E-value: 5.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLLqhDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGS-ISYIINTADictvi 224
Cdd:cd17652 13 LTYAELNARANRLARLLA--ARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPL-DPAYPAErIAYMLADAR----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 225 vdkphkATLLLEHverketpglklvilmepfedalrergkkcgvdiksmqaiedcgrenhhapvpprPDDLSIVCFTSGT 304
Cdd:cd17652 85 ------PALLLTT------------------------------------------------------PDNLAYVIYTSGS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 305 TGNPKGAMLTH---GNVVADFSGFLKVTEkvifprqDDVLISFLPLAhmFERVIQSVV--YCHGGRVGFFQGDIRL---- 375
Cdd:cd17652 105 TGRPKGVVVTHrglANLAAAQIAAFDVGP-------GSRVLQFASPS--FDASVWELLmaLLAGATLVLAPAEELLpgep 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 376 LSDDMKALRPTIFPVVPRLLNRMYDkifhqadtslkrwllefaakrkqaevrsgiirnnsiwDELffnkiqasLGGHVrM 455
Cdd:cd17652 176 LADLLREHRITHVTLPPAALAALPP-------------------------------------DDL--------PDLRT-L 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 456 IVTGAAPASPTVLgflRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLVDAeELNYWTCKGEGEIC 534
Cdd:cd17652 210 VVAGEACPAELVD---RWAPGRRMINAYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYVLDA-RLRPVPPGVPGELY 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 535 VKGPNVFKGYLKDEDRTKEALDSD------GWLH-TGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEP 607
Cdd:cd17652 286 IAGAGLARGYLNRPGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKI-RGFRIELGEVEAALTEHPG 364
|
490 500 510
....*....|....*....|....*....|....
gi 75992911 608 VAQ--IYVHGDSL-KAFLVGIVVPDPEVMPSWAQ 638
Cdd:cd17652 365 VAEavVVVRDDRPgDKRLVAYVVPAPGAAPTAAE 398
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
146-635 |
5.34e-11 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 65.49 E-value: 5.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLLQHDCKVGteQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 225
Cdd:PRK12406 12 RSFDELAQRAARAAGGLAALGVRPG--DCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 dkpHkaTLLLEHVERKETPGLKLVILMEPFE--------DALRErGKKCGVDIKSMQAiedcGRENHHAPVPPRPDDLsi 297
Cdd:PRK12406 90 ---H--ADLLHGLASALPAGVTVLSVPTPPEiaaayrisPALLT-PPAGAIDWEGWLA----QQEPYDGPPVPQPQSM-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 298 vCFTSGTTGNPKGAMLTHGNVvadfsGFLKVTEKVI-----FPRQDDVLISFlPLAHmferviqSVVYCHGGRVGFFQGD 372
Cdd:PRK12406 158 -IYTSGTTGHPKGVRRAAPTP-----EQAAAAEQMRaliygLKPGIRALLTG-PLYH-------SAPNAYGLRAGRLGGV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 373 IRLLS----DDMKAL----RPTIFPVVPRLLNRmydkifhqadtslkrwLLEFAAKRKQAEVRSgiirnnsiwdelffnk 444
Cdd:PRK12406 224 LVLQPrfdpEELLQLierhRITHMHMVPTMFIR----------------LLKLPEEVRAKYDVS---------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 445 iqaSLgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCNHIKLVDAE-- 520
Cdd:PRK12406 272 ---SL----RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE-SGAVTFATSEDALShpGTVGKAAPGAELRFVDEDgr 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 521 ELNywtcKGE-GEICVKGPNV--FKGYLKDEDRTkeALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEK 597
Cdd:PRK12406 344 PLP----QGEiGEIYSRIAGNpdFTYHNKPEKRA--EIDRGGFITSGDVGYLDADGYLFLCDRKRDMV-ISGGVNIYPAE 416
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 75992911 598 IENIYIRSEPVAQIYVHGDSLKAF---LVGIVVPDPEVMPS 635
Cdd:PRK12406 417 IEAVLHAVPGVHDCAVFGIPDAEFgeaLMAVVEPQPGATLD 457
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
144-638 |
7.42e-11 |
|
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: 65.08 E-value: 7.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 144 QWLSYQEVAKRAEFLGSGLLQHdcKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIIntadictv 223
Cdd:cd17649 11 QSLSYAELDARANRLAHRLRAL--GVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 224 ivdkphkatlllehverkETPGLKLVIlmepfedalrergkkcgvdiksmqaiedcgreNHHapvpprPDDLSIVCFTSG 303
Cdd:cd17649 81 ------------------EDSGAGLLL--------------------------------THH------PRQLAYVIYTSG 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 304 TTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPL----AHmfERVIQSVVycHGGRVgffqgdirllsdd 379
Cdd:cd17649 105 STGTPKGVAVSHGPLAA----HCQATAERYGLTPGDRELQFASFnfdgAH--EQLLPPLI--CGACV------------- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 380 mkALRPTIFPVVPRLLNRMYDK----IFHQADTSLKRWLLEFAAKrkqaevrsgiirnnsiwdelffnkiQASLGGHVRM 455
Cdd:cd17649 164 --VLRPDELWASADELAEMVRElgvtVLDLPPAYLQQLAEEADRT-------------------------GDGRPPSLRL 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 456 IVTGAAPASPTvlgFLRAALGCQVY--EGYGQTECTAGCT-FTTPGD----WTSGHVGAPLPCNHIKLVDAeELNYWTCK 528
Cdd:cd17649 217 YIFGGEALSPE---LLRRWLKAPVRlfNAYGPTEATVTPLvWKCEAGaaraGASMPIGRPLGGRSAYILDA-DLNPVPVG 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 529 GEGEICVKGPNVFKGYLKDEDRTKEAL--DSDG-----WLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENI 601
Cdd:cd17649 293 VTGELYIGGEGLARGYLGRPELTAERFvpDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-RGFRIELGEIEAA 371
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 75992911 602 YIRSEPVAQIYV---HGDSLKAfLVGIVVP-DPEVMPSWAQ 638
Cdd:cd17649 372 LLEHPGVREAAVvalDGAGGKQ-LVAYVVLrAAAAQPELRA 411
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
134-632 |
9.11e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 65.05 E-value: 9.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 134 LGFRKPEQPYQWLSY-QEVAKRAEFLgSGLLQHDCKVgteqFVGVFAQNRPEWII----AELACYTysmvVVPLYDTLGP 208
Cdd:PRK13388 18 IAVRYGDRTWTWREVlAEAAARAAAL-IALADPDRPL----HVGVLLGNTPEMLFwlaaAALGGYV----LVGLNTTRRG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 209 GSISYIINTADICTVIVDKPHKAtlLLEHVErkeTPGLKLVILMEPfedALRERgkkcgvdiksmqaIEDCGRENHHAPV 288
Cdd:PRK13388 89 AALAADIRRADCQLLVTDAEHRP--LLDGLD---LPGVRVLDVDTP---AYAEL-------------VAAAGALTPHREV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 289 PPrpDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLkVTEKVIFPRqDDVLISFLPLAH----MferVIQSVVYCHGG 364
Cdd:PRK13388 148 DA--MDPFMLIFTSGTTGAPKAVRCSHGRLA--FAGRA-LTERFGLTR-DDVCYVSMPLFHsnavM---AGWAPAVASGA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 365 RVgffqgdirllsddmkALRPTifpvvprllnrmydkifhqadtslkrwlleFAAKRKQAEVRSgiirnnsiWDELFFNK 444
Cdd:PRK13388 219 AV---------------ALPAK------------------------------FSASGFLDDVRR--------YGATYFNY 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 445 IQASLGghvRMIVTGAAP---ASPTVLGFLRAA-----------LGCQVYEGYGQTEctAGCTFTTPGDWTSGHVGAPLP 510
Cdd:PRK13388 246 VGKPLA---YILATPERPddaDNPLRVAFGNEAsprdiaefsrrFGCQVEDGYGSSE--GAVIVVREPGTPPGSIGRGAP 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 511 cnHIKLVDAEELNywTC---------------KGEGEICVK-GPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGT 574
Cdd:PRK13388 321 --GVAIYNPETLT--ECavarfdahgallnadEAIGELVNTaGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGW 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 75992911 575 LKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYVHGdslkaflvgivVPDPEV 632
Cdd:PRK13388 396 IYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYA-----------VPDERV 441
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
460-631 |
1.57e-10 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 63.94 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 460 AAPASPTVLGFLRAALGCQVYEGYGQTECTaGCTFTTPGDWTS--GHVGAPLPCN-HIKLVDAEELNYWTckgEGEICVK 536
Cdd:cd05929 253 AAPCPPWVKEQWIDWGGPIIWEYYGGTEGQ-GLTIINGEEWLThpGSVGRAVLGKvHILDEDGNEVPPGE---IGEVYFA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 537 GPNVFKgYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRsepvaqiyvHGD 616
Cdd:cd05929 329 NGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIA---------HPK 397
|
170
....*....|....*
gi 75992911 617 SLKAFLVGivVPDPE 631
Cdd:cd05929 398 VLDAAVVG--VPDEE 410
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
111-638 |
2.26e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 64.59 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 111 YDDARTMYQVFRRGLSISGNGPCLGFRKpeqpyQWLSYQEVAKRAEFLGSGLLQhdCKVGTEQFVGVFAQNRPEWIIAEL 190
Cdd:PRK12316 507 YPLQRGVHRLFEEQVERTPEAPALAFGE-----ETLDYAELNRRANRLAHALIE--RGVGPDVLVGVAMERSIEMVVALL 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 191 ACYTYSMVVVPLYDTLGPGSISYIINTADIctvivdkphkATLLLEHVERKETP---GLKLVILMEP--FEDALRERGKK 265
Cdd:PRK12316 580 AILKAGGAYVPLDPEYPAERLAYMLEDSGV----------QLLLSQSHLGRKLPlaaGVQVLDLDRPaaWLEGYSEENPG 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 266 CGVDiksmqaiedcgrenhhapvpprPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLK---------VTEKVIFPR 336
Cdd:PRK12316 650 TELN----------------------PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQayglgvgdtVLQKTPFSF 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 337 QDDVLISFLPLAhmferviqsvvycHGGR-VGFFQGDIRllsdDMKALrptifpvvPRLLNRmydkifHQADTslkrwlL 415
Cdd:PRK12316 708 DVSVWEFFWPLM-------------SGARlVVAAPGDHR----DPAKL--------VELINR------EGVDT------L 750
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 416 EFAAKRKQAEVRSGIIrnnsiwdelffnkiqASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFT 495
Cdd:PRK12316 751 HFVPSMLQAFLQDEDV---------------ASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHW 815
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 496 TPGDWTSGHV--GAPLPCNHIKLVDAeELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEAL------DSDGWLHTGDIG 567
Cdd:PRK12316 816 TCVEEGGDSVpiGRPIANLACYILDA-NLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFvpspfvAGERMYRTGDLA 894
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75992911 568 KWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAfLVGIVVPD------PEVMPSWAQ 638
Cdd:PRK12316 895 RYRADGVIEYAGRIDHQVKL-RGLRIELGEIEARLLEHPWVREAAVLAVDGKQ-LVGYVVLEseggdwREALKAHLA 969
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
293-617 |
3.15e-10 |
|
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: 63.26 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 293 DDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVT-EKVIFPRQDDVLiSFLPLAhmFERVIQSVV--YCHGGRvgff 369
Cdd:cd17656 128 DDLLYIIYTSGTTGKPKGVQLEHKNMV----NLLHFErEKTNINFSDKVL-QFATCS--FDVCYQEIFstLLSGGT---- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 370 qgdIRLLSDDMKALRPTIFPVVPRllnrmydkifHQADT-SLKRWLLEFAAKRKQAEVRsgiirnnsiwdelFFNKIQAS 448
Cdd:cd17656 197 ---LYIIREETKRDVEQLFDLVKR----------HNIEVvFLPVAFLKFIFSEREFINR-------------FPTCVKHI 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 449 LGGHVRMIVTgaapaSPTVLGFLRAalGCQVYEGYG--QTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDaEELNYW 525
Cdd:cd17656 251 ITAGEQLVIT-----NEFKEMLHEH--NVHLHNHYGpsETHVVTTYTINPEAEIPElPPIGKPISNTWIYILD-QEQQLQ 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 526 TCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGW------LHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIE 599
Cdd:cd17656 323 PQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-RGYRIELGEIE 401
|
330 340
....*....|....*....|
gi 75992911 600 NIYIRSEPVAQ--IYVHGDS 617
Cdd:cd17656 402 AQLLNHPGVSEavVLDKADD 421
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
453-623 |
3.19e-10 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 63.32 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 453 VRMIVTGAAPaSPTVLgFLRAALGCQVYEGYGQTEcTAG----CTFTTPGDWTSGHVGAPLPCNH---------IKLVDA 519
Cdd:PLN02479 313 VHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSE-TYGpstvCAWKPEWDSLPPEEQARLNARQgvryiglegLDVVDT 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 520 EELNYWTCKGE--GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEK 597
Cdd:PLN02479 390 KTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGGENISSLE 467
|
170 180
....*....|....*....|....*.
gi 75992911 598 IENIyirsepvaqIYVHGDSLKAFLV 623
Cdd:PLN02479 468 VENV---------VYTHPAVLEASVV 484
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
146-631 |
4.37e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 62.61 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLLQHDCKVGteQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 225
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREG--DVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 DKPHKATL--LLEHVERketpGLKLVILM-------EPFEDALrergkkcgvDIKSMQAIEDcgrenhhapVPPRPDDLs 296
Cdd:PRK08276 90 SAALADTAaeLAAELPA----GVPLLLVVagpvpgfRSYEEAL---------AAQPDTPIAD---------ETAGADML- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 297 ivcFTSGTTGNPKGAM--LTHGNVVADFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRV----GFfq 370
Cdd:PRK08276 147 ---YSSGTTGRPKGIKrpLPGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAPLRFGMSALALGGTVvvmeKF-- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 371 gdirllsDDMKAL------RPTIFPVVPRLLNRMydkifhqadtsLKrwLLEfaakrkqaEVRSGiirnnsiWDelffnk 444
Cdd:PRK08276 222 -------DAEEALalieryRVTHSQLVPTMFVRM-----------LK--LPE--------EVRAR-------YD------ 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 445 iQASLgghvRMIVTGAAPASPTVLgflRAAL---GCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCN-HIKLVD 518
Cdd:PRK08276 261 -VSSL----RVAIHAAAPCPVEVK---RAMIdwwGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGEvRILDED 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 519 AEELNywtcKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGkWLPE-GTLKIIDRKKHIFkLAQGEYVAPE 596
Cdd:PRK08276 332 GNELP----PGEiGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVG-YLDEdGYLYLTDRKSDMI-ISGGVNIYPQ 405
|
490 500 510
....*....|....*....|....*....|....*
gi 75992911 597 KIENIYIRSEPVAQIYVHGdslkaflvgivVPDPE 631
Cdd:PRK08276 406 EIENLLVTHPKVADVAVFG-----------VPDEE 429
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
146-660 |
7.59e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 62.22 E-value: 7.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLLQHDCKVGTEQFVgvFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADiCTVIV 225
Cdd:PRK04319 74 YTYKELKELSNKFANVLKELGVEKGDRVFI--FMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSE-AKVLI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 DKPhkatLLLEHVERKETPGLKLVILMepfeDALRERGKKCgVDIKSM--QAIEDCgrenhhAPVPPRPDDLSIVCFTSG 303
Cdd:PRK04319 151 TTP----ALLERKPADDLPSLKHVLLV----GEDVEEGPGT-LDFNALmeQASDEF------DIEWTDREDGAILHYTSG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 304 TTGNPKGAMLTHGNVVADFsgflkVTEKVIFP-RQDDVL---------------IsFLPLAHMfervIQSVVYchGGRvg 367
Cdd:PRK04319 216 STGKPKGVLHVHNAMLQHY-----QTGKYVLDlHEDDVYwctadpgwvtgtsygI-FAPWLNG----ATNVID--GGR-- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 368 fFQGD--IRLLSDdmkaLRPTIF---PVVPRLLNRMYDKIFHQADTSlkrwllefaakrkqaevrsgiirnnsiwdelff 442
Cdd:PRK04319 282 -FSPErwYRILED----YKVTVWytaPTAIRMLMGAGDDLVKKYDLS--------------------------------- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 443 nkiqaslggHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPCNHIKLVDAEE 521
Cdd:PRK04319 324 ---------SLRHILSVGEPLNPEVVRWGMKVFGLPIHDNWWMTETGGIMIANYPAmDIKPGSMGKPLPGIEAAIVDDQG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 522 lNYWTCKGEGEICVKG--PNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIE 599
Cdd:PRK04319 395 -NELPPNRMGNLAIKKgwPSMMRGIWNNPEKYESYF-AGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTS-GERVGPFEVE 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75992911 600 NIYIRSEPVAQIYVhgdslkaflvgIVVPDP---EVMPSW-AQKKGIEGTyqelcmkKELKKAIL 660
Cdd:PRK04319 472 SKLMEHPAVAEAGV-----------IGKPDPvrgEIIKAFvALRPGYEPS-------EELKEEIR 518
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
300-615 |
1.22e-09 |
|
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: 60.50 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 300 FTSGTTGNPKGAMLTHGNVVADFsgflKVTEKVIFPRQDDVLISFLPLAH-MFERVIQSVVYCHGGRVGFFQGDIRLLSD 378
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESF----VCNEDLFNISGEDAILAPGPLSHsLFLYGAISALYLGGTFIGQRKFNPKSWIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 379 DMKALRPTIFPVVPRLLnrmydkifhqadtslkrwllefaakrkQAEVRSGIIRNnsiwdelffnkiqaslggHVRMIVT 458
Cdd:cd17633 83 KINQYNATVIYLVPTML---------------------------QALARTLEPES------------------KIKSIFS 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 459 GAAPASPTVLGFLRAAL-GCQVYEGYGQTEcTAGCTFTTPGD-WTSGHVGAPLPCNHIKLVDAEElnywtcKGEGEICVK 536
Cdd:cd17633 118 SGQKLFESTKKKLKNIFpKANLIEFYGTSE-LSFITYNFNQEsRPPNSVGRPFPNVEIEIRNADG------GEIGKIFVK 190
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75992911 537 GPNVFKGYLKDEDRTKealdsDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYVHG 615
Cdd:cd17633 191 SEMVFSGYVRGGFSNP-----DGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIEEAIVVG 263
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
146-610 |
2.16e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 61.34 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLlQHDCKVGtEQFVGVFAQNrPEWIIAELACYTYSMVVVPLYDtlgPGSisyiintadictviv 225
Cdd:PRK05691 41 LSYRDLDLRARTIAAAL-QARASFG-DRAVLLFPSG-PDYVAAFFGCLYAGVIAVPAYP---PES--------------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 DKPHKATLLLEHVERKETpglKLVILMEPFEDALRERGKKCGVDIKSMQAI---EDCGRENHHAPVPPrPDDLSIVCFTS 302
Cdd:PRK05691 100 ARRHHQERLLSIIADAEP---RLLLTVADLRDSLLQMEELAAANAPELLCVdtlDPALAEAWQEPALQ-PDDIAFLQYTS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 303 GTTGNPKGAMLTHGNVVADFS----GFlkvtekVIFPRQDDVLISFLPLAHMFERV------IQSVVYCHGGRVGFFQG- 371
Cdd:PRK05691 176 GSTALPKGVQVSHGNLVANEQlirhGF------GIDLNPDDVIVSWLPLYHDMGLIggllqpIFSGVPCVLMSPAYFLEr 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 372 DIRLLsDDMKALRPTI-----FPVvpRLLN-RMYDKIFHQADtsLKRWLLEFAAkrkqaevrSGIIRNNSIwdELFFNKI 445
Cdd:PRK05691 250 PLRWL-EAISEYGGTIsggpdFAY--RLCSeRVSESALERLD--LSRWRVAYSG--------SEPIRQDSL--ERFAEKF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 446 Q----------ASLG-GHVRMIVTGAAPA-SPTVLGFLRAALGCQVYEGyGQTECTAGCTFTTPGdwtsghvgaplpcNH 513
Cdd:PRK05691 315 AacgfdpdsffASYGlAEATLFVSGGRRGqGIPALELDAEALARNRAEP-GTGSVLMSCGRSQPG-------------HA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 514 IKLVDAEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEA---LDSDGWLHTGDIGkWLPEGTLKIIDRKKHIFkLAQG 590
Cdd:PRK05691 381 VLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfveHDGRTWLRTGDLG-FLRDGELFVTGRLKDML-IVRG 458
|
490 500
....*....|....*....|
gi 75992911 591 EYVAPEKIENIYIRSEPVAQ 610
Cdd:PRK05691 459 HNLYPQDIEKTVEREVEVVR 478
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
476-639 |
2.25e-09 |
|
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: 60.26 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 476 GCQVYEGYGQTECTAGCT-FTTPGDWTSGHVGAPLPCNHIKLVDaEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEA 554
Cdd:cd17645 234 GYKLVNNYGPTENTVVATsFEIDKPYANIPIGKPIDNTRVYILD-EALQLQPIGVAGELCIAGEGLARGYLNRPELTAEK 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 555 LDSDGWL------HTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPV---AQIYVHGDSLKAFLVGI 625
Cdd:cd17645 313 FIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIEPFLMNHPLIelaAVLAKEDADGRKYLVAY 391
|
170
....*....|....*...
gi 75992911 626 VVP----DPEVMPSWAQK 639
Cdd:cd17645 392 VTApeeiPHEELREWLKN 409
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
146-632 |
2.37e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 60.41 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLlqHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIv 225
Cdd:PRK13390 25 VSYRQLDDDSAALARVL--YDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLV- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 dkphkATLLLEHVERKETPGLKLVILM-------EPFEDALRERGKKCgvdiksmqAIEDCGrenhhapvpprpddlSIV 298
Cdd:PRK13390 102 -----ASAALDGLAAKVGADLPLRLSFggeidgfGSFEAALAGAGPRL--------TEQPCG---------------AVM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 299 CFTSGTTGNPKG--------AMLTHGN-VVADFSGFLKVTEKvifprqdDVLISFLPLAHMFERVIQSVVYCHGGRVGFF 369
Cdd:PRK13390 154 LYSSGTTGFPKGiqpdlpgrDVDAPGDpIVAIARAFYDISES-------DIYYSSAPIYHAAPLRWCSMVHALGGTVVLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 370 QG-DIRLLSDDMKALRPTIFPVVPRLLNRMYdkifhqadtslkrwllefaakRKQAEVRSGiirnnsiWDelffnkiQAS 448
Cdd:PRK13390 227 KRfDAQATLGHVERYRITVTQMVPTMFVRLL---------------------KLDADVRTR-------YD-------VSS 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 449 LgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVG-APLPCNHIKLVDAEELNyw 525
Cdd:PRK13390 272 L----RAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGrSVLGDLHICDDDGNELP-- 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 526 tcKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDG--WLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIY 602
Cdd:PRK13390 345 --AGRiGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQETENAL 421
|
490 500 510
....*....|....*....|....*....|
gi 75992911 603 IRSEPVAQIYVHGdslkaflvgivVPDPEV 632
Cdd:PRK13390 422 TMHPAVHDVAVIG-----------VPDPEM 440
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
292-634 |
5.64e-09 |
|
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: 58.95 E-value: 5.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSG--FLKVTEkvifprqDDVLISFLplAHMFE-RVIQSVVYCHGGR 365
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVnlrTSLSEryFGRDNG-------DEAVLFFS--NYVFDfFVEQMTLALLNGQ 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 366 vgffqgDIRLLSDDMKALRPTIFPVV-----------PRLLnRMYDkiFHQAdTSLKRWLL---EFAAKRkqaevrsgii 431
Cdd:cd17648 164 ------KLVVPPDEMRFDPDRFYAYInrekvtylsgtPSVL-QQYD--LARL-PHLKRVDAageEFTAPV---------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 432 rnnsiwdelfFNKIQASLGGhvrmivtgaapasptvlgflraalgcQVYEGYGQTEC--TAGCTFTTPGDWTSGHVGAPL 509
Cdd:cd17648 224 ----------FEKLRSRFAG--------------------------LIINAYGPTETtvTNHKRFFPGDQRFDKSLGRPV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 510 PCNHIKLVDAEeLNYWTCKGEGEICVKGPNVFKGYLKDEDRTKE-------------ALDSDGWLH-TGDIGKWLPEGTL 575
Cdd:cd17648 268 RNTKCYVLNDA-MKRVPVGAVGELYLGGDGVARGYLNRPELTAErflpnpfqteqerARGRNARLYkTGDLVRWLPSGEL 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75992911 576 KIIDRKKHIFKLaQGEYVAPEKIENIY-----IRSEPVAQIYVHGDSLKA---FLVGIVVPDPEVMP 634
Cdd:cd17648 347 EYLGRNDFQVKI-RGQRIEPGEVEAALasypgVRECAVVAKEDASQAQSRiqkYLVGYYLPEPGHVP 412
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
146-639 |
6.21e-09 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 59.25 E-value: 6.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIV 225
Cdd:PRK05857 42 LRYRELVAEVGGLAADLRAQSVSRGSR--VLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 DKPHKatlllehVERKETPGLKLVILMEPFEDALRERGKKCGVDIKSMQAIEDCGrenhhapvpprPDDLSIVCFTSGTT 305
Cdd:PRK05857 120 APGSK-------MASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNADQG-----------SEDPLAMIFTSGTT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 306 GNPKGAMLTHGNVVA--DF---SGFLKVTEKVifprqDDVLISFLPLAHMFErvIQSVVYC--HGGR--VGFFQGD--IR 374
Cdd:PRK05857 182 GEPKAVLLANRTFFAvpDIlqkEGLNWVTWVV-----GETTYSPLPATHIGG--LWWILTClmHGGLcvTGGENTTslLE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 375 LLSDDMKALRPtifpVVPRLLNRMYDKIfhqadtslkrwllefaakrkqaevrsgiirnnsiwdelffnKIQASLGGHVR 454
Cdd:PRK05857 255 ILTTNAVATTC----LVPTLLSKLVSEL-----------------------------------------KSANATVPSLR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 455 MIVTGAAPASPTVLGFLRAA--LGCQVYeGYGQTECTAGCTFTTPGDWT---SGHVGAPLPCNHIKLVDAEELNYWTCKG 529
Cdd:PRK05857 290 LVGYGGSRAIAADVRFIEATgvRTAQVY-GLSETGCTALCLPTDDGSIVkieAGAVGRPYPGVDVYLAATDGIGPTAPGA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 530 E-----GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIyir 604
Cdd:PRK05857 369 GpsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGGVNIAPDEVDRI--- 443
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 75992911 605 SEPVAQI-----YVHGDSLKAFLVGI-VVPDPEVMPSWAQK 639
Cdd:PRK05857 444 AEGVSGVreaacYEIPDEEFGALVGLaVVASAELDESAARA 484
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
146-349 |
2.86e-08 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 57.19 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAE-----FLGSGLLQHDCkvgteqfVGVFAQNRPEWIIAELACyTYSMVVVPLYDT-LGPGSISYIINTAD 219
Cdd:PRK08279 63 ISYAELNARANryahwAAARGVGKGDV-------VALLMENRPEYLAAWLGL-AKLGAVVALLNTqQRGAVLAHSLNLVD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 220 ICTVIVDKPhkatlLLEHVErkETPGLKLVILMEPFEDalRERGKKCGVDIKSMQAIEDCGRENHHAPVPPRPDDLSIVC 299
Cdd:PRK08279 135 AKHLIVGEE-----LVEAFE--EARADLARPPRLWVAG--GDTLDDPEGYEDLAAAAAGAPTTNPASRSGVTAKDTAFYI 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 75992911 300 FTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAH 349
Cdd:PRK08279 206 YTSGTTGLPKAAVMSHMRWLKAMGGFGGLLR----LTPDDVLYCCLPLYH 251
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
280-601 |
3.66e-08 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 56.70 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 280 GRENHHAPVPPRPD-DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkVTEKVIFPRQDDVLISFLPLAH-Mferviqs 357
Cdd:PRK05851 138 AHTNRSASLTPPDSgGPAVLQGTAGSTGTPRTAILSPGAVLSNLRG---LNARVGLDAATDVGCSWLPLYHdM------- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 358 vvychggrvgffqGDIRLLSDDMKA----LRPT-IFPVVP-RLLNrmydkifhqadtslkrWLLEFAAKRKQA-EVRSGI 430
Cdd:PRK05851 208 -------------GLAFLLTAALAGaplwLAPTtAFSASPfRWLS----------------WLSDSRATLTAApNFAYNL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 431 IRNNSiwdelffNKIQASLGGHVRMIVTGAAP----------ASPTVLGFLRAALGcqvyEGYGQTECTAGCTFTTPG-- 498
Cdd:PRK05851 259 IGKYA-------RRVSDVDLGALRVALNGGEPvdcdgferfaTAMAPFGFDAGAAA----PSYGLAESTCAVTVPVPGig 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 499 ---------DWTSGH----VGAPLPCNHIKLVDAEELNYWTCKGEGEICVKGPNVFKGYLKDEdrtkeALDSDGWLHTGD 565
Cdd:PRK05851 328 lrvdevttdDGSGARrhavLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQA-----PIDPDDWFPTGD 402
|
330 340 350
....*....|....*....|....*....|....*.
gi 75992911 566 IGkWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENI 601
Cdd:PRK05851 403 LG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERV 436
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
454-630 |
1.97e-07 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 54.23 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 454 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT---------FTT------PGD--WTSGHVGAPLPCNHIkl 516
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAEGLVNYTrlddsderiFTTqgrpmsPDDevWVADADGNPLPQGEV-- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 517 vdaeelnywtckgeGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHifklaQ----GEY 592
Cdd:PRK10946 381 --------------GRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGEK 441
|
170 180 190
....*....|....*....|....*....|....*...
gi 75992911 593 VAPEKIENIYIRsepvaqiyvHGDSLKAFLVGIvvPDP 630
Cdd:PRK10946 442 IAAEEIENLLLR---------HPAVIHAALVSM--EDE 468
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
294-631 |
2.01e-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: 53.90 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 294 DLSIVCFTSGTTGNPKGAMLTH-----GNVVADFSGFLKvtekvifprQDDVLISFLPLAHmferviqsvvyCHGGRVGF 368
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHrrawrGGAFFAGSGGAL---------PSDVLYTCLPLYH-----------STALIVGW 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 369 FQGdirLLS----------------DDMKALRPTIFPVVPRLLnrmydkifhqadtslkRWLLefAAKRKQAEVRsgiir 432
Cdd:cd05940 142 SAC---LASgatlvirkkfsasnfwDDIRKYQATIFQYIGELC----------------RYLL--NQPPKPTERK----- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 433 nnsiwdelffNKIQASLGGHVRmivtgaapasPTVLGFLRAALGC-QVYEGYGQTECTAGCT--FTTPGdwTSGHVGAPL 509
Cdd:cd05940 196 ----------HKVRMIFGNGLR----------PDIWEEFKERFGVpRIAEFYAATEGNSGFInfFGKPG--AIGRNPSLL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 510 PCNH-IKLV--DAEELNYWT-----C----KGE-----GEICVKGPnvFKGYLKDEDRTKEAL-----DSDGWLHTGDIG 567
Cdd:cd05940 254 RKVApLALVkyDLESGEPIRdaegrCikvpRGEpglliSRINPLEP--FDGYTDPAATEKKILrdvfkKGDAWFNTGDLM 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75992911 568 KWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYVHGDSL-----KAFLVGIVVPDPE 631
Cdd:cd05940 332 RLDGEGFWYFVDRLGDTFRW-KGENVSTTEVAAVLGAFPGVEEANVYGVQVpgtdgRAGMAAIVLQPNE 399
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
454-638 |
3.51e-07 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 53.46 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 454 RMIVTGAAPASPTVLGF-----LRAALGcqvyegYGQTEcTAG--CTFTtPGDWTSG--HVGAPLPCNHIKLvdaeelny 524
Cdd:PRK07445 233 RTILLGGAPAWPSLLEQarqlqLRLAPT------YGMTE-TASqiATLK-PDDFLAGnnSSGQVLPHAQITI-------- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 525 wTCKGEGEICVKGPNVFKGYLkdedrtKEALDSDGWLHTGDIGKWLPEGTLKIIDR--KKHIfklAQGEYVAPEKIENIY 602
Cdd:PRK07445 297 -PANQTGNITIQAQSLALGYY------PQILDSQGIFETDDLGYLDAQGYLHILGRnsQKII---TGGENVYPAEVEAAI 366
|
170 180 190
....*....|....*....|....*....|....*.
gi 75992911 603 IRSEPVAQIYVHGdslkaflvgivVPDPEvmpsWAQ 638
Cdd:PRK07445 367 LATGLVQDVCVLG-----------LPDPH----WGE 387
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
453-623 |
5.16e-07 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 53.11 E-value: 5.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 453 VRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTEctAGCTFT--TPGDWTSGHVGAPLPCNHIKLVdAEELNYWTCKG 529
Cdd:PRK06060 262 LRCVVSAGEALELGLAERLMEFFGgIPILDGIGSTE--VGQTFVsnRVDEWRLGTLGRVLPPYEIRVV-APDGTTAGPGV 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 530 EGEICVKGPNVFKGYLkdeDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIfKLAQGEYVAPEKIENIYIRSEPVA 609
Cdd:PRK06060 339 EGDLWVRGPAIAKGYW---NRPDSPVANEGWLDTRDRVCIDSDGWVTYRCRADDT-EVIGGVNVDPREVERLIIEDEAVA 414
|
170 180
....*....|....*....|.
gi 75992911 610 QIYVHG-------DSLKAFLV 623
Cdd:PRK06060 415 EAAVVAvrestgaSTLQAFLV 435
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
286-349 |
1.24e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 51.87 E-value: 1.24e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75992911 286 APVPPRPDDLSIVCF---TSGTTGNPKGAMLTHGNVVADF----SGFLKVTEKVifPRQDDVLISFLPLAH 349
Cdd:PRK05850 150 RGSDARPRDLPSTAYlqyTSGSTRTPAGVMVSHRNVIANFeqlmSDYFGDTGGV--PPPDTTVVSWLPFYH 218
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
293-638 |
2.32e-06 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 50.43 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 293 DDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkVTEKVIFPRQddVLISfLPLAHM--FERVIQSVVychGGRV---- 366
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTASADA---THDRLGGPGQ--WLLA-LPAHHIagLQVLVRSVI---AGSEpvel 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 367 ----GFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKifhQADTSLKrwllEFAAkrkqaevrsgiirnnsiwdelff 442
Cdd:PRK07824 106 dvsaGFDPTALPRAVAELGGGRRYTSLVPMQLAKALDDP---AATAALA----ELDA----------------------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 443 nkiqaslgghvrmIVTGAAPASPTVlgfLRAA--LGCQVYEGYGQTECTAGCTFTtpgdwtsghvGAPLPCNHIKLVDae 520
Cdd:PRK07824 156 -------------VLVGGGPAPAPV---LDAAaaAGINVVRTYGMSETSGGCVYD----------GVPLDGVRVRVED-- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 521 elnywtckgeGEICVKGPNVFKGYLKDEDrtKEALDSDGWLHTGDIGKwLPEGTLKIIDRKKHIFKLAqGEYVAPEKIEN 600
Cdd:PRK07824 208 ----------GRIALGGPTLAKGYRNPVD--PDPFAEPGWFRTDDLGA-LDDGVLTVLGRADDAISTG-GLTVLPQVVEA 273
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 75992911 601 IYIRSEPVAQIYVHG---DSLKAFLVGIVVPDPEVMPSWAQ 638
Cdd:PRK07824 274 ALATHPAVADCAVFGlpdDRLGQRVVAAVVGDGGPAPTLEA 314
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
442-630 |
2.40e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 50.55 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 442 FNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPGDWTSGHVGAPLPCNHIKLVDAEE 521
Cdd:PRK07638 245 LYKENRVIENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSF-VTALVDEESERRPNSVGRPFHNVQVRICNE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 522 LNYWTCKGE-GEICVKGPNVFKGYLKDEDRTKEaLDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIEN 600
Cdd:PRK07638 324 AGEEVQKGEiGTVYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIES 401
|
170 180 190
....*....|....*....|....*....|
gi 75992911 601 IYIRSEPVAQIYVHGdslkaflvgivVPDP 630
Cdd:PRK07638 402 VLHEHPAVDEIVVIG-----------VPDS 420
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
258-350 |
4.77e-06 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 49.98 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 258 ALRERGKKCGVDIKSM--QAIEDCGRENHHAPVPPRPDDLS---------IVCFTSGTTGNPKGAMLTHGNVVAdFSGFL 326
Cdd:cd05938 98 ALRADGVSVWYLSHTSntEGVISLLDKVDAASDEPVPASLRahvtikspaLYIYTSGTTGLPKAARISHLRVLQ-CSGFL 176
|
90 100
....*....|....*....|....
gi 75992911 327 KVTeKVifpRQDDVLISFLPLAHM 350
Cdd:cd05938 177 SLC-GV---TADDVIYITLPLYHS 196
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
292-615 |
5.71e-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: 49.35 E-value: 5.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 292 PDDLSIVCFTSGTTGNPKGAMLTHG-NVVADfsgflKVTEKVIFPRQDDVLISFLPLAHMFERVIqSVVYC--HGGRVGF 368
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISWRrTLVTS-----NLLSHDLNLKNGDRTYTCMPLYHGTAAFL-GACNClmSGGTLAL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 369 ---FQgdIRLLSDDMKALRPTIFPVVPRLLnrmydkifhqadtslkRWLLEFAAkrkqaevrsgiirnnSIWDELffNKI 445
Cdd:cd05937 160 srkFS--ASQFWKDVRDSGATIIQYVGELC----------------RYLLSTPP---------------SPYDRD--HKV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 446 QASLGGHVRmivtgaapasPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKL-------- 516
Cdd:cd05937 205 RVAWGNGLR----------PDIWERFRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKFenqvvlvk 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 517 VDAEELNYWT------CK----GE-GEICVKGPNV----FKGYLKDEDRTKEAL------DSDGWLHTGDIGKWLPEGTL 575
Cdd:cd05937 275 MDPETDDPIRdpktgfCVrapvGEpGEMLGRVPFKnreaFQGYLHNEDATESKLvrdvfrKGDIYFRTGDLLRQDADGRW 354
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 75992911 576 KIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYVHG 615
Cdd:cd05937 355 YFLDRLGDTFRW-KSENVSTTEVADVLGAHPDIAEANVYG 393
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
147-635 |
1.03e-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: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 147 SYQEVAKRAEFLGSGLLQHDCKVGTEqfVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSI-SYIINTADICTVIV 225
Cdd:cd17634 86 SYRELHREVCRFAGTLLDLGVKKGDR--VAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVaGRIIDSSSRLLITA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 DkphkatlllEHVERKETPGLKLVIlmepfEDALRERG---------KKCGVDIKSMQA--------IEDCGREnhHAPV 288
Cdd:cd17634 164 D---------GGVRAGRSVPLKKNV-----DDALNPNVtsvehvivlKRTGSDIDWQEGrdlwwrdlIAKASPE--HQPE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 289 PPRPDDLSIVCFTSGTTGNPKGAMLTHGnvvadfsGFLkvtekvIFPRQDdvlisflpLAHMFERVIQSVVYChGGRVGF 368
Cdd:cd17634 228 AMNAEDPLFILYTSGTTGKPKGVLHTTG-------GYL------VYAATT--------MKYVFDYGPGDIYWC-TADVGW 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 369 FQGDIRLLSDDMkALRPTIF-----PVVPRlLNRMYDKIFHQADTSLkrWLLEFAAKRKQAEVRSGIIRNNsiwdelffn 443
Cdd:cd17634 286 VTGHSYLLYGPL-ACGATTLlyegvPNWPT-PARMWQVVDKHGVNIL--YTAPTAIRALMAAGDDAIEGTD--------- 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 444 kiQASLgghvRMIVTGAAPASPTVLGFLRAALG---CQVYEGYGQTECTAGCTFTTPG--DWTSGHVGAPLPCNHIKLVD 518
Cdd:cd17634 353 --RSSL----RILGSVGEPINPEAYEWYWKKIGkekCPVVDTWWQTETGGFMITPLPGaiELKAGSATRPVFGVQPAVVD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 519 AEElNYWTCKGEGEICVKG--PNVFKGYLKDEDRTKEALDS--DGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVA 594
Cdd:cd17634 427 NEG-HPQPGGTEGNLVITDpwPGQTRTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVA-GHRLG 504
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 75992911 595 PEKIENIYIRSEPVAQIYVHG--DSLKA-FLVGIVVPDPEVMPS 635
Cdd:cd17634 505 TAEIESVLVAHPKVAEAAVVGipHAIKGqAPYAYVVLNHGVEPS 548
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
508-575 |
1.16e-05 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 48.35 E-value: 1.16e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75992911 508 PLPCNHIK-----LVDAEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEAL-DSDGW--LHTGDIGKwLPEGTL 575
Cdd:PRK04813 317 RLPIGYAKpdsplLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGY-LEDGLL 391
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
443-668 |
3.57e-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: 47.04 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 443 NKIQASLGGHVRMIVTGAAPASPTV----LGFLRA--ALGCQVYEGYGqTECTAGCTFTTPGDWTSGHVGAPLPCNHI-K 515
Cdd:cd05915 263 ESTGHRLKTLRRLVVGGSAAPRSLIarfeRMGVEVrqGYGLTETSPVV-VQNFVKSHLESLSEEEKLTLKAKTGLPIPlV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 516 LVDAEELNYWTCKGEGE----ICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGE 591
Cdd:cd05915 342 RLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG-GE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 592 YVAPEKIENIyirsepvaqIYVHGDSLKAFLVGivVPDP---EVMPSWAQKKGIEGTYQELCmkkELKKAILDDMVMLGK 668
Cdd:cd05915 421 WISSVDLENA---------LMGHPKVKEAAVVA--IPHPkwqERPLAVVVPRGEKPTPEELN---EHLLKAGFAKWQLPD 486
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
290-639 |
4.61e-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: 46.22 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 290 PRPDDLSIVCfTSGTTGNPKGAMLTHGNV------VADFSGFLKVTEKVIFPRQ-DDVLISFLPLAHMFerviqsvvycH 362
Cdd:cd05924 1 RSADDLYILY-TGGTTGMPKGVMWRQEDIfrmlmgGADFGTGEFTPSEDAHKAAaAAAGTVMFPAPPLM----------H 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 363 G-----GRVGFFQGDIRLLSDDMkalrptifpVVPRLLNRMYDKifHQADT------SLKRWLLEfaakrkqaEVRSGII 431
Cdd:cd05924 70 GtgswtAFGGLLGGQTVVLPDDR---------FDPEEVWRTIEK--HKVTSmtivgdAMARPLID--------ALRDAGP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 432 RNNSiwdelffnkiqaSLgghvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFTTPGdwtSGHVGAPL- 509
Cdd:cd05924 131 YDLS------------SL----FAISSGGALLSPEVKqGLLELVPNITLVDAFGSSETGFTGSGHSAG---SGPETGPFt 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 510 PCNHIKLVDAEELNYWTCK--GEGEICVKGpNVFKGYLKDEDRTKEA---LDSDGWLHTGDIGKWLPEGTLKIIDRKKHI 584
Cdd:cd05924 192 RANPDTVVLDDDGRVVPPGsgGVGWIARRG-HIPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGRGSVC 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 75992911 585 FKLAqGEYVAPEKIEniyirsepvAQIYVHGDSLKAFLVGivVPDPEvmpsWAQK 639
Cdd:cd05924 271 INTG-GEKVFPEEVE---------EALKSHPAVYDVLVVG--RPDER----WGQE 309
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
292-623 |
7.35e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 46.31 E-value: 7.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 292 PDDLSIVCFTSGTTGNPKGAMLT-HGNVVADFSG--FLKVTEKVIFPRQ-----DDVLISFLPlAHMFerviqsvvychG 363
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEqRGMLNNQLSKvpYLALSEADVIAQTasqsfDISVWQFLA-APLF-----------G 3935
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 364 GRVGFFQGDI----RLLSDDMKALRPTIFPVVPRLLNRMYDKIfHQADTSLkRWllefaakrkqaevrsgiirnnsiwde 439
Cdd:PRK05691 3936 ARVEIVPNAIahdpQGLLAHVQAQGITVLESVPSLIQGMLAED-RQALDGL-RW-------------------------- 3987
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 440 lffnkiqaslgghvrMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF------TTPGDWTSghVGAPLPCNH 513
Cdd:PRK05691 3988 ---------------MLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFfrvdlaSTRGSYLP--IGSPTDNNR 4050
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 514 IKLVDaEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEAL-------DSDGWLHTGDIGKWLPEGTLKIIDRKKHI-- 584
Cdd:PRK05691 4051 LYLLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFvphpfgaPGERLYRTGDLARRRSDGVLEYVGRIDHQvk 4129
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 75992911 585 ---FKLAQGEYVApEKIENIYIRSEPVA-QIYVHGDSLKAFLV 623
Cdd:PRK05691 4130 irgYRIELGEIEA-RLHEQAEVREAAVAvQEGVNGKHLVGYLV 4171
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
289-632 |
1.29e-04 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 45.13 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 289 PPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTekvifP-RQDDVLISFLPLAHMFerviqsvvychggrvG 367
Cdd:PRK13382 192 EPTGRKGRVILLTSGTTGTPKGARRSGPGGIGTLKAILDRT-----PwRAEEPTVIVAPMFHAW---------------G 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 368 FFQGDIRLL------------SDDMKAL----RPTIFPVVPRLLNRMYDKIfhqadtslkrwllefaakrkqAEVRSgii 431
Cdd:PRK13382 252 FSQLVLAASlactivtrrrfdPEATLDLidrhRATGLAVVPVMFDRIMDLP---------------------AEVRN--- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 432 rnnsiwdelffnkiqASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFT-TPGDWTSG--HVGAP 508
Cdd:PRK13382 308 ---------------RYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATE--AGMIATaTPADLRAApdTAGRP 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 509 LPCNHIKLVDAE--ELNywtcKGE-GEICVKGPNVFKGYlkDEDRTKEAldSDGWLHTGDIGKWLPEGTLKIIDRKKHIF 585
Cdd:PRK13382 371 AEGTEIRILDQDfrEVP----TGEvGTIFVRNDTQFDGY--TSGSTKDF--HDGFMASGDVGYLDENGRLFVVGRDDEMI 442
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 75992911 586 kLAQGEYVAPEKIENIYIRSEPVAQIYV-------HGDSLKAFlvgiVVPDPEV 632
Cdd:PRK13382 443 -VSGGENVYPIEVEKTLATHPDVAEAAVigvddeqYGQRLAAF----VVLKPGA 491
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
146-624 |
1.34e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 45.54 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 146 LSYQEVAKRAEFLGSGLlqHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTAdictviv 225
Cdd:PRK05691 1157 LDYAELHAQANRLAHYL--RDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADS------- 1227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 226 dkphKATLLLEHVERKEtpglklvilmepfedALRERGKKCGVDIKSMQAiedcgrENH--HAP-VPPRPDDLSIVCFTS 302
Cdd:PRK05691 1228 ----GVELLLTQSHLLE---------------RLPQAEGVSAIALDSLHL------DSWpsQAPgLHLHGDNLAYVIYTS 1282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 303 GTTGNPKGAMLTHGnVVADFSGFLKVTEKVifpRQDDVLISFLPLAhmFErviQSVVYCH-----GGRVGFF----QGDI 373
Cdd:PRK05691 1283 GSTGQPKGVGNTHA-ALAERLQWMQATYAL---DDSDVLMQKAPIS--FD---VSVWECFwplitGCRLVLAgpgeHRDP 1353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 374 RLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTSLKRWlleFAAkrkqAEVRSGIIRNNsiwdelffnkiqaslgghv 453
Cdd:PRK05691 1354 QRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRL---FSG----GEALPAELRNR------------------- 1407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 454 rmivtgaapasptVLGFLRAAlgcQVYEGYGQTECTAGCTF--TTPGDWTSGHVGAPLPCNHIKLVDAEeLNYWTCKGEG 531
Cdd:PRK05691 1408 -------------VLQRLPQV---QLHNRYGPTETAINVTHwqCQAEDGERSPIGRPLGNVLCRVLDAE-LNLLPPGVAG 1470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992911 532 EICVKGPNVFKGYLKDEDRTKE-----ALDSDG--WLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIR 604
Cdd:PRK05691 1471 ELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL-RGFRVEPEEIQARLLA 1549
|
490 500
....*....|....*....|..
gi 75992911 605 SEPVAQ--IYVHGDSLKAFLVG 624
Cdd:PRK05691 1550 QPGVAQaaVLVREGAAGAQLVG 1571
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
288-319 |
7.73e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 43.11 E-value: 7.73e-04
10 20 30
....*....|....*....|....*....|..
gi 75992911 288 VPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVV 319
Cdd:PRK10252 593 QLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIV 624
|
|
| |
