|
Name |
Accession |
Description |
Interval |
E-value |
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
116-694 |
0e+00 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 905.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 116 QPYQWLSYQEVAKRAEFLGSGLLQHDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADI 195
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 196 CTVIVDKphkailllehverketpglklvilmepfddalrergkkcGVDIKSMQAIEDSGQENHRVPVPPRPDDLSIVCF 275
Cdd:cd05927 81 SIVFCDA---------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 276 TSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDM 355
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 356 KALRPTIFPVVPRLLNRMYDKIFH--QADTSLKRWLLEFAAKRKQAEVRSGIIRNNSIWDELFFNKIQASLGGHVRMIVT 433
Cdd:cd05927 202 KALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 434 GAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYW--TSKGEGEICVK 511
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDakDPNPRGEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 512 GPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGD 591
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 592 SLKAFLVGIVVPDPEVMPCWAQKK-GIEGNYQELCKSKELKKAILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLL 670
Cdd:cd05927 442 SLKSFLVAIVVPDPDVLKEWAASKgGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLL 521
|
570 580
....*....|....*....|....
gi 48256734 671 TPTLKAKRPELREYFKKQIEELYS 694
Cdd:cd05927 522 TPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
79-694 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 699.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 79 TQLLTHY--YDDARTMYQVFRRGLSISGNGPCLGFRKPEQ----PYQWLSYQEVAKRAEFLGSGLLQHDCKVGteQFIGV 152
Cdd:PLN02736 31 LKLVSRFpdHPEIGTLHDNFVYAVETFRDYKYLGTRIRVDgtvgEYKWMTYGEAGTARTAIGSGLVQHGIPKG--ACVGL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 153 FAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIVdKPHKAILLLEHVerKETPGLKLVILMEPFDD 232
Cdd:PLN02736 109 YFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCL--SEIPSVRLIVVVGGADE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 233 ALRERGKKCGVDIKSMQAIEDSGQENHRVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvIFPrq 312
Cdd:PLN02736 186 PLPSLPSGTGVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTK--FYP-- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 313 DDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTS--LKRWLL 390
Cdd:PLN02736 262 SDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESggLKERLF 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 391 EFAAKRKQAEVRSGiiRNNS-IWDELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF 469
Cdd:PLN02736 342 NAAYNAKKQALENG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 470 TTPGDWTSGHVGAPLPCNHIKLVDAEELNYwTSKGE----GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWL 545
Cdd:PLN02736 420 MDEGDNLSGHVGSPNPACEVKLVDVPEMNY-TSEDQpyprGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWL 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 546 PEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAFLVGIVVPDPEVMPCWAQKKGIE-GNYQEL 624
Cdd:PLN02736 499 PGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQL 578
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 625 CKSKELKKAILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 694
Cdd:PLN02736 579 CNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYA 648
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
86-694 |
3.20e-175 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 513.49 E-value: 3.20e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 86 YDDARTMYQVFRRGLSISGNGPCLGfRKPEQPYQWLSYQEVAKRAEFLGSGLLQHDCKVGteQFIGVFAQNRPEWIIAEL 165
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVALR-EKEDGIWQSLTWAEFAERVRALAAGLLALGVKPG--DRVAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 166 ACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIVDKPHKAILLLEHveRKETPGLKLVILMEPfddalreRGKKCGVDI 245
Cdd:COG1022 84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEV--RDELPSLRHIVVLDP-------RGLRDDPRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 246 KSMQAIEDSGQENH------RVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekvIFPRQDDVLISF 319
Cdd:COG1022 155 LSLDELLALGREVAdpaeleARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLER----LPLGPGDRTLSF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 320 LPLAHMFERVIQSVVYCHGGRVGFfQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTS--LKRWLLEFA---A 394
Cdd:COG1022 231 LPLAHVFERTVSYYALAAGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAggLKRKLFRWAlavG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 395 KRKQAEVRSGiiRNNSIW--------DELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAG 466
Cdd:COG1022 310 RRYARARLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 467 CTFTTPGDWTSGHVGAPLPCNHIKLvdAEElnywtskgeGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLP 546
Cdd:COG1022 387 ITVNRPGDNRIGTVGPPLPGVEVKI--AED---------GEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 547 EGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKaFLVGIVVPDPEVMPCWAQKKGIE-GNYQELC 625
Cdd:COG1022 456 DGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDGRP-FLAALIVPDFEALGEWAEENGLPyTSYAELA 534
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 48256734 626 KSKELKKAILDDMVMLGKesGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 694
Cdd:COG1022 535 QDPEVRALIQEEVDRANA--GLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYA 601
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
116-681 |
9.68e-161 |
|
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: 470.92 E-value: 9.68e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 116 QPYQWLSYQEVAKRAEFLGSGLLQHDCKVGteQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADI 195
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPG--DRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 196 CTVIVDKPhkailllehverketpglklvilmepfddalrergkkcgvdiksmqaiedsgqenhrvpvpprpDDLSIVCF 275
Cdd:cd05907 79 KALFVEDP----------------------------------------------------------------DDLATIIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 276 TSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAHMFERV-IQSVVYCHGGRVGFFQgDIRLLSDD 354
Cdd:cd05907 95 TSGTTGRPKGVMLSHRNILSNALALAERLP----ATEGDRHLSFLPLAHVFERRaGLYVPLLAGARIYFAS-SAETLLDD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 355 MKALRPTIFPVVPRLLNRMYDKIFHQADTSLKRWLLEFAAkrkqaevrsgiirnnsiwdelffnkiqaslGGHVRMIVTG 434
Cdd:cd05907 170 LSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV------------------------------GGRLRFAASG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 435 AAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDaeelnywtskgEGEICVKGPN 514
Cdd:cd05907 220 GAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPN 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 515 VFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLK 594
Cdd:cd05907 288 VMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDGRP 367
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 595 aFLVGIVVPDPEVMPCWAQKKGIEG-NYQELCKSKELKKAILDDMVMLGKEsgLHSFEQVKAIYIHCDMFSVQNGLLTPT 673
Cdd:cd05907 368 -FLVALIVPDPEALEAWAEEHGIAYtDVAELAANPAVRAEIEAAVEAANAR--LSRYEQIKKFLLLPEPFTIENGELTPT 444
|
....*...
gi 48256734 674 LKAKRPEL 681
Cdd:cd05907 445 LKLKRPVI 452
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
117-678 |
1.26e-153 |
|
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: 454.75 E-value: 1.26e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 117 PYQWLSYQEVAKRAEFLGSGLlqhdCKVG--TEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTAD 194
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGL----VELGlkPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 195 ICTVIVDkphkailllehverketpglklvilmepfddalrergkkcgvdiksmqaiedsgqenhrvpvpPRPDDLSIVC 274
Cdd:cd17639 78 CSAIFTD---------------------------------------------------------------GKPDDLACIM 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 275 FTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPrqDDVLISFLPLAHMFERVIQSVVYCHGGRVGFfqGDIRLLSD- 353
Cdd:cd17639 95 YTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGP--DDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDk 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 354 -------DMKALRPTIFPVVPRLLNRMYDKIFHQADTS--LKRWLLEFAAKRKQAEVRSGIirNNSIWDELFFNKIQASL 424
Cdd:cd17639 171 skrgckgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMggLKRTLFWTAYQSKLKALKEGP--GTPLLDELVFKKVRAAL 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 425 GGHVRMIVTGAAPASPTVLGFLrAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYWTSKG 504
Cdd:cd17639 249 GGRLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDKP 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 505 E--GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEP 582
Cdd:cd17639 328 PprGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPL 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 583 VAQIYVHGDSLKAFLVGIVVPDPEVMPCWAQKKG-IEGNYQELCKSKELKKAILDDMVMLGKESGLHSFEQVKAIYIHCD 661
Cdd:cd17639 408 VNNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGvINSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDE 487
|
570
....*....|....*..
gi 48256734 662 MFSVQNGLLTPTLKAKR 678
Cdd:cd17639 488 EWTPENGLVTAAQKLKR 504
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
117-694 |
2.12e-150 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 451.99 E-value: 2.12e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 117 PYQWLSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADIC 196
Cdd:PLN02861 74 PYVWLTYKEVYDAAIRIGSAIRSRGVNPGDR--CGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 197 TVIV-DKPHKAILlleHVERKETPGLKLVILMEPFDDALRERGKKCGVDIKSMQAIEDSGQENHRVPvPPRPDDLSIVCF 275
Cdd:PLN02861 152 IAFVqESKISSIL---SCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLDCELP-PKQKTDICTIMY 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 276 TSGTTGNPKGAMLTHGNVVADF---SGFLKVTEKVIfpRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLS 352
Cdd:PLN02861 228 TSGTTGEPKGVILTNRAIIAEVlstDHLLKVTDRVA--TEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQGDIRYLM 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 353 DDMKALRPTIFPVVPRLLNRMYDKIFH--QADTSLKRWLLEFAAKRKQAEVRSGIIRNNS--IWDELFFNKIQASLGGHV 428
Cdd:PLN02861 306 EDVQALKPTIFCGVPRVYDRIYTGIMQkiSSGGMLRKKLFDFAYNYKLGNLRKGLKQEEAspRLDRLVFDKIKEGLGGRV 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 429 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCtFTTPGDWTS--GHVGAPLPCNHIKLVDAEELNY--WTSKG 504
Cdd:PLN02861 386 RLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGC-FTSIANVFSmvGTVGVPMTTIEARLESVPEMGYdaLSDVP 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 505 EGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVA 584
Cdd:PLN02861 465 RGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIA 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 585 QIYVHGDSLKAFLVGIVVPDPEVMPCWAQKKGIEGNYQELCKSKELKKAILDDMVMLGKESGLHSFEQVKAIYIHCDMFS 664
Cdd:PLN02861 544 SIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFD 623
|
570 580 590
....*....|....*....|....*....|
gi 48256734 665 VQNGLLTPTLKAKRPELREYFKKQIEELYS 694
Cdd:PLN02861 624 IERDLITPTFKLKRPQLLKYYKDCIDQLYS 653
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
87-693 |
1.05e-148 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 447.93 E-value: 1.05e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 87 DDARTMYQVFRRGLSISGNGPCLGFR-----KPEQpYQWLSYQEVAKRAEFLGSGLlqHDCKVGTEQFIGVFAQNRPEWI 161
Cdd:PLN02614 42 EGMDSCWDVFRMSVEKYPNNPMLGRReivdgKPGK-YVWQTYQEVYDIVIKLGNSL--RSVGVKDEAKCGIYGANSPEWI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 162 IAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIVDKphKAILLLEHVERKETPGLKLVILMEPFDDALRERGKKC 241
Cdd:PLN02614 119 ISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEE--KKISELFKTCPNSTEYMKTVVSFGGVSREQKEEAETF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 242 GVDIKSMQAIEDSGQ-ENHRVPVPpRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTEKVIfpRQDDVLI 317
Cdd:PLN02614 197 GLVIYAWDEFLKLGEgKQYDLPIK-KKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGvirLLKSANAAL--TVKDVYL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 318 SFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTS--LKRWLLEFAAK 395
Cdd:PLN02614 274 SYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGgfLKKFVFDSAFS 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 396 RKQAEVRSGI--IRNNSIWDELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPG 473
Cdd:PLN02614 354 YKFGNMKKGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPD 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 474 DWTS-GHVGAPLPCNHIKLVDAEELNY--WTSKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTL 550
Cdd:PLN02614 434 ELDMlGTVGPPVPNVDIRLESVPEMEYdaLASTPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSM 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 551 KIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAFLVGIVVPDPEVMPCWAQKKGIEGNYQELCKSKEL 630
Cdd:PLN02614 513 KIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKA 592
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 48256734 631 KKAILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 693
Cdd:PLN02614 593 KEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMY 655
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
88-693 |
5.40e-147 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 443.10 E-value: 5.40e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 88 DARTMYQVFRRGLSISGNGPCLGFRKPEQ----PYQWLSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIA 163
Cdd:PLN02430 40 DITTAWDIFSKSVEKYPDNKMLGWRRIVDgkvgPYMWKTYKEVYEEVLQIGSALRASGAEPGSR--VGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 164 ELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV-DKPHKAILlleHVERKETPGLKLVILMEPFDDALRERGKKCG 242
Cdd:PLN02430 118 MEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVqDKKIKELL---EPDCKSAKRLKAIVSFTSVTEEESDKASQIG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 243 VDIKSMQAIEDSGQENHRVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTEKVIfpRQDDVLISF 319
Cdd:PLN02430 195 VKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGvdlFMEQFEDKM--THDDVYLSF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 320 LPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFH--QADTSLKRWLLEFAAKRK 397
Cdd:PLN02430 273 LPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYKYK 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 398 QAEVRSGIIRNNS--IWDELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDW 475
Cdd:PLN02430 353 LAWMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEM 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 476 TS-GHVGAPLPCNHIKLVDAEELNYwTSKGE---GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLK 551
Cdd:PLN02430 433 CMlGTVGAPAVYNELRLEEVPEMGY-DPLGEpprGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLK 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 552 IIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAFLVGIVVPDPEVMPCWAQKKGIEGNYQELCKSKELK 631
Cdd:PLN02430 511 IIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELK 590
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 48256734 632 KAILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 693
Cdd:PLN02430 591 EHILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMY 652
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
79-694 |
7.17e-135 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 412.97 E-value: 7.17e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 79 TQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRK---PEQ---------------PYQWLSYQEVAKRAEFLGSGLLQ- 139
Cdd:PLN02387 47 PELVETPWEGATTLAALFEQSCKKYSDKRLLGTRKlisREFetssdgrkfeklhlgEYEWITYGQVFERVCNFASGLVAl 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 140 -HDckvgTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIVD-KPHKAILLLEhvERKE 217
Cdd:PLN02387 127 gHN----KEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDsKQLKKLIDIS--SQLE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 218 TpgLKLVILME-PFDDALRERGKKCGVDIKSMQAIEDSGQENHRVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD 296
Cdd:PLN02387 201 T--VKRVIYMDdEGVDSDSSLSGSSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVAT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 297 FSGFLKVTEKVifpRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFfqGDIRLLSD-----------DMKALRPTIFPV 365
Cdd:PLN02387 279 VAGVMTVVPKL---GKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDtsnkikkgtkgDASALKPTLMTA 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 366 VPRLLNRMYDKIFHQADTS--LKRWLLEFAAKRKQAEVR------SGIIRnnSIWDELFFNKIQASLGGHVRMIVTGAAP 437
Cdd:PLN02387 354 VPAILDRVRDGVRKKVDAKggLAKKLFDIAYKRRLAAIEgswfgaWGLEK--LLWDALVFKKIRAVLGGRIRFMLSGGAP 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 438 ASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYWTSKG---EGEICVKGPN 514
Cdd:PLN02387 432 LSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLISDKpmpRGEIVIGGPS 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 515 VFKGYLKDEDRTKEA--LDSDG--WLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHG 590
Cdd:PLN02387 512 VTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIMVHA 591
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 591 DSLKAFLVGIVVPDPEVMPCWAQKKGIE-GNYQELCKSKELKKAILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGL 669
Cdd:PLN02387 592 DPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPAKIKLLPEPWTPESGL 671
|
650 660
....*....|....*....|....*
gi 48256734 670 LTPTLKAKRPELREYFKKQIEELYS 694
Cdd:PLN02387 672 VTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
117-563 |
5.38e-126 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 380.50 E-value: 5.38e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 117 PYQWLSYQEVAKRAEFLGSGLLQHDCKVGteQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADIC 196
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRALGVGKG--DRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 197 TVIVDKPHKAILLLEHVERKETPGLKLVILMEPFDDALRergkkcgvdiksMQAIEDSGQENHRVPVPPRPDDLSIVCFT 276
Cdd:pfam00501 96 VLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEP------------LPEEAKPADVPPPPPPPPDPDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 277 SGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERV-IQSVVYCHGGRVGFFQGDIRL----L 351
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSlGLLGPLLAGATVVLPPGFPALdpaaL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 352 SDDMKALRPTIFPVVPRLLNRmydkifhqadtslkrwllefaakrkqaevrsgIIRNNSIWDELFfnkiqaslgGHVRMI 431
Cdd:pfam00501 244 LELIERYKVTVLYGVPTLLNM--------------------------------LLEAGAPKRALL---------SSLRLV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 432 VTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDW---TSGHVGAPLPCNHIKLVDAEELNYWTSKGEGEI 508
Cdd:pfam00501 283 LSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGEL 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 48256734 509 CVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLA 563
Cdd:pfam00501 363 CVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
60-693 |
1.82e-102 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 328.47 E-value: 1.82e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 60 QSEEVEDSGGARRSVI--------GDCTQLLTHYYDdARTMYQVFRRGLSISGNGPCLGFRK--------------PEQP 117
Cdd:PTZ00216 32 QNVPVPGTETENASAIyriagvtdEEHERLRNEWYY-GPNFLQRLERICKERGDRRALAYRPvervekevvkdadgKERT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 118 Y--------QWLSYQEVAKRAEFLGSGL----LQHDCKVGteqfigVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGS 185
Cdd:PTZ00216 111 MevthfnetRYITYAELWERIVNFGRGLaelgLTKGSNVA------IYEETRWEWLASIYGIWSQSMVAATVYANLGEDA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 186 IRYIINTADiCTVIVDKPHKAILLLEHVERKETPGLKLVILmepfdDALRERGKKCGVDIKSMQAIEDSG---QENHRVP 262
Cdd:PTZ00216 185 LAYALRETE-CKAIVCNGKNVPNLLRLMKSGGMPNTTIIYL-----DSLPASVDTEGCRLVAWTDVVAKGhsaGSHHPLN 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 263 VPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF-LKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRV 341
Cdd:PTZ00216 259 IPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALeDRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLARGALI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 342 GFfqGDIRLLSD-------DMKALRPTIFPVVPRllnrmydkIFhqaDT-------------SLKRWLLEFAAKRKQAEV 401
Cdd:PTZ00216 339 GF--GSPRTLTDtfarphgDLTEFRPVFLIGVPR--------IF---DTikkaveaklppvgSLKRRVFDHAYQSRLRAL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 402 RSGiiRNNSIWDELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCqVYEGYGQTE--CTAGCTFTtpGDWTSGH 479
Cdd:PTZ00216 406 KEG--KDTPYWNEKVFSAPRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTEtvCCGGIQRT--GDLEPNA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 480 VGAPLPCNHIKLVDAEELNYwTSKGE--GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKK 557
Cdd:PTZ00216 481 VGQLLKGVEMKLLDTEEYKH-TDTPEprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVK 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 558 HIFKLAQGEYVAPEKIENIYIRSEPVAQ----IYVHGDslKAFLVGIVVPD-PEVMPcWAQKKGIEGNYQELCKSKELKK 632
Cdd:PTZ00216 560 ALAKNCLGEYIALEALEALYGQNELVVPngvcVLVHPA--RSYICALVLTDeAKAMA-FAKEHGIEGEYPAILKDPEFQK 636
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 48256734 633 AILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 693
Cdd:PTZ00216 637 KATESLQETARAAGRKSFEIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
118-678 |
4.83e-81 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 266.64 E-value: 4.83e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 118 YQWLSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICT 197
Cdd:cd05932 4 VVEFTWGEVADKARRLAAALRALGLEPGSK--IALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 198 VIVDKphkaillLEHVERKE--TPGLKLVILMEPFDDALRERGKKcgvDIKSMQAIEDSgqenhrvPVPPRPDDLSIVCF 275
Cdd:cd05932 82 LFVGK-------LDDWKAMApgVPEGLISISLPPPSAANCQYQWD---DLIAQHPPLEE-------RPTRFPEQLATLIY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 276 TSGTTGNPKGAMLTHGNvvadFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDM 355
Cdd:cd05932 145 TSGTTGQPKGVMLTFGS----FAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTFVEDV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 356 KALRPTIFPVVPRLL----NRMYDKIFHQadtSLKRWLlefaakrkQAEVRSGIIRNnsiwdelffnKIQASLG-GHVRM 430
Cdd:cd05932 221 QRARPTLFFSVPRLWtkfqQGVQDKIPQQ---KLNLLL--------KIPVVNSLVKR----------KVLKGLGlDQCRL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 431 IVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDaeelnywtskgEGEICV 510
Cdd:cd05932 280 AGCGSAPVPPALLEWYRS-LGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEILV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 511 KGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHG 590
Cdd:cd05932 348 RSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 591 DSLKAfLVGIVVPDPEvmpcwAQKKGIEGNYQELCKSkelKKAILDDMvmlgkESGLHSFEQVKAIYIHCDMFSVQNGLL 670
Cdd:cd05932 428 SGLPA-PLALVVLSEE-----ARLRADAFARAELEAS---LRAHLARV-----NSTLDSHEQLAGIVVVKDPWSIDNGIL 493
|
....*...
gi 48256734 671 TPTLKAKR 678
Cdd:cd05932 494 TPTLKIKR 501
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
116-679 |
9.83e-76 |
|
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: 251.12 E-value: 9.83e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 116 QPYQWLSYQEVAKRAEFLGSGLLqhDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADI 195
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLR--SLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 196 CTVIVdkphkailllehverketpglklvilmepfddalrergkkcgvdiksmqaiedsgqENHrvpvpprPDDLSIVCF 275
Cdd:cd17640 79 VALVV--------------------------------------------------------END-------SDDLATIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 276 TSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFfqGDIRLLSDDM 355
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLLHQIRSLSDIVP----PQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDDL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 356 KALRPTIFPVVPRLLNRMYDKIFHQadtslkrwllefaaKRKQAEVRSGIIrnnsiwdeLFFnkiqaSLGGHVRMIVTGA 435
Cdd:cd17640 170 KRVKPHYIVSVPRLWESLYSGIQKQ--------------VSKSSPIKQFLF--------LFF-----LSGGIFKFGISGG 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 436 APASPTVLGFLRaALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYWTSKGEGEICVKGPNV 515
Cdd:cd17640 223 GALPPHVDTFFE-AIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQV 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 516 FKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKa 595
Cdd:cd17640 302 MKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQK- 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 596 FLVGIVVPDPEVMPCWAQKKG--IEGNYQELCKSKELKKAILDD-MVMLGKESGLHSFEQVKAIYIHCDMFsVQNGLLTP 672
Cdd:cd17640 381 RLGALIVPNFEELEKWAKESGvkLANDRSQLLASKKVLKLYKNEiKDEISNRPGFKSFEQIAPFALLEEPF-IENGEMTQ 459
|
....*..
gi 48256734 673 TLKAKRP 679
Cdd:cd17640 460 TMKIKRN 466
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
92-605 |
4.92e-70 |
|
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: 235.48 E-value: 4.92e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 92 MYQVFRRGLSISGNGPCLGFRkpeqpYQWLSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELACYTYS 171
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG-----GRRLTYAELDARARRLAAALRALG--VGPGDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 172 MVVVPLYDTLGPGSIRYIINTADICTVIVdkphkailllehverketpglklvilmepfddalrergkkcgvdiksmqai 251
Cdd:COG0318 74 AVVVPLNPRLTAEELAYILEDSGARALVT--------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 252 edsgqenhrvpvpprpddlSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAHMF---ER 328
Cdd:COG0318 103 -------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALG----LTPGDVVLVALPLFHVFgltVG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 329 VIQSVVycHGGRV----GFfqgDIRLLSDDMKALRPTIFPVVPRLLNRMYDKI-FHQADTSlkrwllefaakrkqaevrs 403
Cdd:COG0318 160 LLAPLL--AGATLvllpRF---DPERVLELIERERVTVLFGVPTMLARLLRHPeFARYDLS------------------- 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 404 giirnnsiwdelffnkiqaslggHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVG 481
Cdd:COG0318 216 -----------------------SLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVG 272
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 482 APLPCNHIKLVDAE--ELnywtSKGE-GEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKH 558
Cdd:COG0318 273 RPLPGVEVRIVDEDgrEL----PPGEvGEIVVRGPNVMKGYWNDPEATAEAFR-DGWLRTGDLGRLDEDGYLYIVGRKKD 347
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 48256734 559 IFKLAqGEYVAPEKIENIYIRSEPVAQIYV-------HGDSLKAFlvgiVVPDP 605
Cdd:COG0318 348 MIISG-GENVYPAEVEEVLAAHPGVAEAAVvgvpdekWGERVVAF----VVLRP 396
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
119-693 |
3.67e-69 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 237.26 E-value: 3.67e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 119 QW--LSYQEVAKRAEFLGSGLLqhdcKVGTEQF--IGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINT-- 192
Cdd:cd05933 5 KWhtLTYKEYYEACRQAAKAFL----KLGLERFhgVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETse 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 193 ADICTVIVDKPHKAILLLEHverkETPGLKLVI-LMEPFDDalrergKKCGVdiKSMQAIEDSG------QENHRVPVPp 265
Cdd:cd05933 81 ANILVVENQKQLQKILQIQD----KLPHLKAIIqYKEPLKE------KEPNL--YSWDEFMELGrsipdeQLDAIISSQ- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 266 RPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQS-VVYCHGGRVGFF 344
Cdd:cd05933 148 KPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIwLPIKVGGQVYFA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 345 QGDIR--LLSDDMKALRPTIFPVVPRLLNRMYDKI---FHQAdTSLKRWLLEFAaKRKQAEV-------RSGIIRNNSIW 412
Cdd:cd05933 228 QPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkavGAKS-GTLKRKIASWA-KGVGLETnlklmggESPSPLFYRLA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 413 DELFFNKIQASLG-GHVRMIVTGAAPASPTVLGFLrAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKL 491
Cdd:cd05933 306 KKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 492 V--DAEelnywtskGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVA 569
Cdd:cd05933 385 HnpDAD--------GIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 570 PEKIENIYIRSEP-VAQIYVHGDSLKaFLVGIVV------PD---------PEVMPcWAQKKGIEGNY-QELCKSKELK- 631
Cdd:cd05933 457 PVPIEDAVKKELPiISNAMLIGDKRK-FLSMLLTlkcevnPEtgepldeltEEAIE-FCRKLGSQATRvSEIAGGKDPKv 534
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 48256734 632 -KAILDDMVMLGKESGLHSFEQVKAIYIHCDmFSVQNGLLTPTLKAKRPELREYFKKQIEELY 693
Cdd:cd05933 535 yEAIEEGIKRVNKKAISNAQKIQKWVILEKD-FSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
121-671 |
5.53e-67 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 231.19 E-value: 5.53e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSGLlQHDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:cd17632 68 ITYAELWERVGAVAAAH-DPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 201 DKPHKAiLLLEHVERKETPGLKLVILMEPFDDA-------LRERGKKCGVDIKSMQAIEDSGQE---NHRVPVPPRPDDL 270
Cdd:cd17632 147 SAEHLD-LAVEAVLEGGTPPRLVVFDHRPEVDAhraalesARERLAAVGIPVTTLTLIAVRGRDlppAPLFRPEPDDDPL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 271 SIVCFTSGTTGNPKGAMLTHgNVVADFsgFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGrVGFFQG--DI 348
Cdd:cd17632 226 ALLIYTSGSTGTPKGAMYTE-RLVATF--WLKVSSIQDIRPPASITLNFMPMSHIAGRISLYGTLARGG-TAYFAAasDM 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 349 RLLSDDMKALRPTIFPVVPRLLNRMYDKifHQADtsLKRWL-----LEFAAKRKQAEVRsgiirnnsiwdelffnkiQAS 423
Cdd:cd17632 302 STLFDDLALVRPTELFLVPRVCDMLFQR--YQAE--LDRRSvagadAETLAERVKAELR------------------ERV 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 424 LGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTtpgdwtSGHVGAPlPCNHIKLVDAEELNYWTSK 503
Cdd:cd17632 360 LGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE--AGAVIL------DGVIVRP-PVLDYKLVDVPELGYFRTD 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 504 G---EGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRS 580
Cdd:cd17632 431 RphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFAAS 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 581 EPVAQIYVHGDSLKAFLVGIVVPDPEVmpcwaqkkgiegnyQELCKSKELKKAILDDMVMLGKESGLHSFEQVKAIYIHC 660
Cdd:cd17632 511 PLVRQIFVYGNSERAYLLAVVVPTQDA--------------LAGEDTARLRAALAESLQRIAREAGLQSYEIPRDFLIET 576
|
570
....*....|.
gi 48256734 661 DMFSVQNGLLT 671
Cdd:cd17632 577 EPFTIANGLLS 587
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
118-644 |
7.22e-64 |
|
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: 222.30 E-value: 7.22e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 118 YQWLSYQEVAKRAEFLGSGLlqHDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICT 197
Cdd:cd17641 9 WQEFTWADYADRVRAFALGL--LALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 198 VIVDKPHKAILLLEHveRKETPGLKLVILMEP------FDDALRergkkcgvdikSMQAIEDSGQENHRVPvpP------ 265
Cdd:cd17641 87 VIAEDEEQVDKLLEI--ADRIPSVRYVIYCDPrgmrkyDDPRLI-----------SFEDVVALGRALDRRD--Pglyere 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 266 ----RPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKvifpRQDDVLISFLPLAHMFER---VIQSVVycHG 338
Cdd:cd17641 152 vaagKGEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPL----GPGDEYVSVLPLPWIGEQmysVGQALV--CG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 339 GRVGFFQgDIRLLSDDMKALRPTIFPVVPRLLN--------RMYDKifhqadTSLKRWL--------LEFAAKRKQAEVR 402
Cdd:cd17641 226 FIVNFPE-EPETMMEDLREIGPTFVLLPPRVWEgiaadvraRMMDA------TPFKRFMfelgmklgLRALDRGKRGRPV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 403 SGIIRNNS-IWDELFFNKIQASLG-GHVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTEcTAGCTFTTP-GDWTSGH 479
Cdd:cd17641 299 SLWLRLASwLADALLFRPLRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTE-LAGAYTVHRdGDVDPDT 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 480 VGAPLPCNHIKLVDaeelnywtskgEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHI 559
Cdd:cd17641 377 VGVPFPGTEVRIDE-----------VGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDV 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 560 FKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSlKAFLVGIVVPDPEVMPCWAQKKGIE-GNYQELCKSKELKKAILDDM 638
Cdd:cd17641 446 GTTSDGTRFSPQFIENKLKFSPYIAEAVVLGAG-RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEV 524
|
....*.
gi 48256734 639 VMLGKE 644
Cdd:cd17641 525 EKVNAS 530
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
121-606 |
2.99e-62 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 215.00 E-value: 2.99e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGsgLLQHDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:cd05914 8 LTYKDLADNIAKFA--LLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 201 DKPhkailllehverketpglklvilmepfddalrergkkcgvdiksmqaiedsgqenhrvpvpprpDDLSIVCFTSGTT 280
Cdd:cd05914 86 SDE----------------------------------------------------------------DDVALINYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 281 GNPKGAMLTHGNVVADFSGfLKVTEKVifpRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDI---RLLSDDMKA 357
Cdd:cd05914 102 GNSKGVMLTYRNIVSNVDG-VKEVVLL---GKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIpsaKIIALAFAQ 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 358 LRPTIfpVVPRLLNRMYDKIFHQADTSLKRWLLEFAAKrkqaevrsgIIRNNSIWdELFFNKIQASLGGHVRMIVTGAAP 437
Cdd:cd05914 178 VTPTL--GVPVPLVIEKIFKMDIIPKLTLKKFKFKLAK---------KINNRKIR-KLAFKKVHEAFGGNIKEFVIGGAK 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 438 ASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEElnywtSKGEGEICVKGPNVFK 517
Cdd:cd05914 246 INPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDP-----ATGEGEIIVRGPNVMK 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 518 GYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVA--QIYVHGDSLKA 595
Cdd:cd05914 320 GYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLesLVVVQEKKLVA 399
|
490
....*....|.
gi 48256734 596 flvgIVVPDPE 606
Cdd:cd05914 400 ----LAYIDPD 406
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
93-598 |
8.73e-62 |
|
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: 213.96 E-value: 8.73e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 93 YQVFRRGLSISGNGPCLGFRKpeqpyQWLSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSM 172
Cdd:cd05936 2 ADLLEEAARRFPDKTALIFMG-----RKLTYRELDALAEAFAAGLQNLGVQPGDR--VALMLPNCPQFPIAYFGALKAGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 173 VVVPLYDTLGPGSIRYIINTAdictvivdkphkailllehverketpGLKLVILMEPFDDALrergkkcgvdiksmqaie 252
Cdd:cd05936 75 VVVPLNPLYTPRELEHILNDS--------------------------GAKALIVAVSFTDLL------------------ 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 253 dSGQENHRVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIfpRQDDVLISFLPLAHMFErviQS 332
Cdd:cd05936 111 -AAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLL--EGDDVVLAALPLFHVFG---LT 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 333 VVYCHGGRVGFFQ------GDIRLLsDDMKALRPTIFPVVPRllnrMYDKIFHQADtslkrwllefaakrkqaevrsgii 406
Cdd:cd05936 185 VALLLPLALGATIvliprfRPIGVL-KEIRKHRVTIFPGVPT----MYIALLNAPE------------------------ 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 407 rnnsiwdelfFNKIQASlggHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT-SGHVGAPLP 485
Cdd:cd05936 236 ----------FKKRDFS---SLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRkPGSIGIPLP 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 486 CNHIKLVDAE--ELnywtSKGE-GEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFkL 562
Cdd:cd05936 303 GTEVKIVDDDgeEL----PPGEvGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMI-I 376
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 48256734 563 AQGEYVAPEKIENIYIRSEPVAQIYV-------HGDSLKAFLV 598
Cdd:cd05936 377 VGGFNVYPREVEEVLYEHPAVAEAAVvgvpdpySGEAVKAFVV 419
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
121-598 |
9.90e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 212.07 E-value: 9.90e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGKGDR--VAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 201 -------DKP-HKAILLLEHVERKETP-GLKLVILMEPFDDALRergkkcgvdiksmqaiedSGQENHRVPvPPRPDDLS 271
Cdd:PRK07656 109 lglflgvDYSaTTRLPALEHVVICETEeDDPHTEKMKTFTDFLA------------------AGDPAERAP-EVDPDDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 272 IVCFTSGTTGNPKGAMLTHGNV---VADFSGFLKVTEKvifprqDDVLISfLPLAHMFerviqsvvychGGRVGF----- 343
Cdd:PRK07656 170 DILFTSGTTGRPKGAMLTHRQLlsnAADWAEYLGLTEG------DRYLAA-NPFFHVF-----------GYKAGVnaplm 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 344 ----------FQGD--IRLLSDDmkalRPTIFPVVPRLLNRMYDkifhqadtslkrwllefAAKRKQAEVRSgiirnnsi 411
Cdd:PRK07656 232 rgatilplpvFDPDevFRLIETE----RITVLPGPPTMYNSLLQ-----------------HPDRSAEDLSS-------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 412 wdelffnkiqaslgghVRMIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGCTFTTPGD---WTSGHVGAPLPCN 487
Cdd:PRK07656 283 ----------------LRLAVTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIAGV 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 488 HIKLVDaeELNYWTSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGE 566
Cdd:PRK07656 347 ENKIVN--ELGEEVPVGEvGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IVGGF 423
|
490 500 510
....*....|....*....|....*....|....*....
gi 48256734 567 YVAPEKIENIYIRSEPVAQIYV-------HGDSLKAFLV 598
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 ... |
269-606 |
3.45e-60 |
|
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: 205.60 E-value: 3.45e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 269 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekvIFPRQDDVLISFLPLAHMFerVIQSVVYC--HGGRVGFFQG 346
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS----GGLTEGDVFLSTLPLFHIG--GLFGLLGAllAGGTVVLLPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 347 -DIRLLSDDMKALRPTIFPVVPRLLNRmydkifhqadtslkrwLLEFAAKRKQAevrsgiirnnsiwdelffnkiQASLg 425
Cdd:cd04433 75 fDPEAALELIEREKVTILLGVPTLLAR----------------LLKAPESAGYD---------------------LSSL- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 426 ghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT--SGHVGAPLPCNHIKLVDaEELNYWTSK 503
Cdd:cd04433 117 ---RALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVD-PDGGELPPG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 504 GEGEICVKGPNVFKGYLKDEDRTkEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSEPV 583
Cdd:cd04433 193 EIGELVVRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPGV 270
|
330 340
....*....|....*....|...
gi 48256734 584 AQIYVHGdslkaflvgivVPDPE 606
Cdd:cd04433 271 AEAAVVG-----------VPDPE 282
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
121-598 |
2.82e-53 |
|
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: 190.89 E-value: 2.82e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSGLLQHDCKVGteQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKG--DVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 201 DKPhkailLLEHVER--KETPGLKLVILMEPFDDALRergkkcgvDIKSMQAIEDSGQENHRVPVPPR-PDDLSIVCFTS 277
Cdd:cd05911 89 DPD-----GLEKVKEaaKELGPKDKIIVLDDKPDGVL--------SIEDLLSPTLGEEDEDLPPPLKDgKDDTAAILYSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 278 GTTGNPKGAMLTHGNVVADFSgFLKVTEKVIFPRqDDVLISFLPLAHMFErvIQSVVYC--HGGRV----GFFqgdirll 351
Cdd:cd05911 156 GTTGLPKGVCLSHRNLIANLS-QVQTFLYGNDGS-NDVILGFLPLYHIYG--LFTTLASllNGATViimpKFD------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 352 SDDMKAL----RPTIFPVVPRLLNRMydkifhqadtslkrwllefaakrkqaeVRSGIirnnsiwdelfFNKIQASlggH 427
Cdd:cd05911 225 SELFLDLiekyKITFLYLVPPIAAAL---------------------------AKSPL-----------LDKYDLS---S 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 428 VRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYWTSKGEG 506
Cdd:cd05911 264 LRVILSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEPG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 507 EICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIyIRSEP---- 582
Cdd:cd05911 344 EICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAV-LLEHPgvad 421
|
490 500
....*....|....*....|
gi 48256734 583 --VAQIY--VHGDSLKAFLV 598
Cdd:cd05911 422 aaVIGIPdeVSGELPRAYVV 441
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
86-605 |
8.36e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 182.31 E-value: 8.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 86 YDDARTMYQVFRRGLSISGNGPCLGFRKPEqpyqwLSYQEVAKRAEFLGSGLLqhDCKVGTEQFIGVFAQNRPEWIIAEL 165
Cdd:PRK06187 2 QDYPLTIGRILRHGARKHPDKEAVYFDGRR-----TTYAELDERVNRLANALR--ALGVKKGDRVAVFDWNSHEYLEAYF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 166 ACytySM---VVVPLYDTLGPGSIRYIINTADICTVIVDKPhkailLLEHVE--RKETPGLKLVILMEPFDDALrergkk 240
Cdd:PRK06187 75 AV---PKigaVLHPINIRLKPEEIAYILNDAEDRVVLVDSE-----FVPLLAaiLPQLPTVRTVIVEGDGPAAP------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 241 CGVDIKSMQAIEDsGQENHRVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVvadFSGFLKVTEKVIFpRQDDVLISFL 320
Cdd:PRK06187 141 LAPEVGEYEELLA-AASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNL---FLHSLAVCAWLKL-SRDDVYLVIV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 321 PLAHmferviqsvvyCHG---GRVGFFQG---------DIRLLSDDMKALRPTIFPVVPRLLNRMydkifHQADTSLKRW 388
Cdd:PRK06187 216 PMFH-----------VHAwglPYLALMAGakqviprrfDPENLLDLIETERVTFFFAVPTIWQML-----LKAPRAYFVD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 389 LlefaakrkqaevrsgiirnnsiwdelffnkiqaslgGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT 468
Cdd:PRK06187 280 F------------------------------------SSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVS 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 469 FTTPGDWTSGH------VGAPLPCNHIKLVDAEELNYWTSKGE-GEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDI 541
Cdd:PRK06187 324 VLPPEDQLPGQwtkrrsAGRPLPGVEARIVDDDGDELPPDGGEvGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDV 402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 48256734 542 GKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIyirsepvaqIYVHGDSLKAFLVGivVPDP 605
Cdd:PRK06187 403 GYIDEDGYLYITDRIKDVIISG-GENIYPRELEDA---------LYGHPAVAEVAVIG--VPDE 454
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
233-694 |
2.92e-43 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 166.82 E-value: 2.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 233 ALRERGKKCGVDIksMQAIEDSGQENHRVPVP-PRPDDLSIVCFTSGTTGNPKGAMLTHGNV------VADFSGFLKVTE 305
Cdd:PTZ00342 270 DLKEKAKKLGISI--ILFDDMTKNKTTNYKIQnEDPDFITSIVYTSGTSGKPKGVMLSNKNLyntvvpLCKHSIFKKYNP 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 306 KVIFprqddvliSFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQAD--T 383
Cdd:PTZ00342 348 KTHL--------SYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINnlP 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 384 SLKRWLLE--FAAKRkqaevrsgiiRNNSIWDELFF-------NKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQV 454
Cdd:PTZ00342 420 PLKRFLVKkiLSLRK----------SNNNGGFSKFLegithisSKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNY 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 455 YEGYGQTEcTAGCTFTTPG-DWTSGHVGAPL-PCNHIKLVDAEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEALDS 532
Cdd:PTZ00342 490 YQGYGLTE-TTGPIFVQHAdDNNTESIGGPIsPNTKYKVRTWETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTE 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 533 DGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHG-DSLKAFLVGIVVPDPEVMPCW 611
Cdd:PTZ00342 569 DGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGdDSMDGPLAIISVDKYLLFKCL 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 612 A-----QKKGI-EGNYQELCKSKELKKAILDDMV---MLG--KESGLHSFEQVKAIYIHCDMFSVQNgLLTPTLKAKRPE 680
Cdd:PTZ00342 649 KddnmlESTGInEKNYLEKLTDETINNNIYVDYVkgkMLEvyKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKRFY 727
|
490
....*....|....*..
gi 48256734 681 L-REY--FKKQIEELYS 694
Cdd:PTZ00342 728 VfKDYafFIDQVKKIYK 744
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
96-605 |
3.20e-41 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 155.85 E-value: 3.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 96 FRRGLSISGNGPCLGFRKPEqpyqwLSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVV 175
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRS-----LTYAELDERVNRLAHALRALGVAKGDR--VAVLSKNSPEFLELLFAAARLGAVFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 176 PLYDTLGPGSIRYIINTAdictvivdkphkailllehverketpGLKLVIlmepfddalrergkkcgvdiksmqaiedsg 255
Cdd:cd17631 74 PLNFRLTPPEVAYILADS--------------------------GAKVLF------------------------------ 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 256 qenhrvpvpprpDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekvIFPRQDDVLISFLPLAHMFE-RVIQSVV 334
Cdd:cd17631 98 ------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAA----LDLGPDDVLLVVAPLFHIGGlGVFTLPT 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 335 YCHGGRV----GFfqgDIRLLSDDMKALRPTIFPVVPRLLNRMYDK-IFHQADTSlkrwllefaakrkqaevrsgiirnn 409
Cdd:cd17631 162 LLRGGTVvilrKF---DPETVLDLIERHRVTSFFLVPTMIQALLQHpRFATTDLS------------------------- 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 410 siwdelffnkiqaSLgghvRMIVTGAAPASPTVLGFLRAAlGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPCN 487
Cdd:cd17631 214 -------------SL----RAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHRRklGSAGRPVFFV 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 488 HIKLVDAE--ELnywtSKGE-GEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQ 564
Cdd:cd17631 276 EVRIVDPDgrEV----PPGEvGEIVVRGPHVMAGYWNRPEATAAAFR-DGWFHTGDLGRLDEDGYLYIVDRKKDMII-SG 349
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 48256734 565 GEYVAPEKIENIyirsepvaqIYVHGDSLKAFLVGivVPDP 605
Cdd:cd17631 350 GENVYPAEVEDV---------LYEHPAVAEVAVIG--VPDE 379
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
121-576 |
4.36e-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: 157.01 E-value: 4.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSGLlqHDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTAdictviv 200
Cdd:cd05904 33 LTYAELERRVRRLAAGL--AKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDS------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 201 dKPHKAILLLEHVERKETPGLKLVILMEPFDDALRergkkcgvdIKSMQAIEDSGQenhrVPVPP-RPDDLSIVCFTSGT 279
Cdd:cd05904 104 -GAKLAFTTAELAEKLASLALPVVLLDSAEFDSLS---------FSDLLFEADEAE----PPVVViKQDDVAALLYSSGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 280 TGNPKGAMLTHGNVVADFSGFLKVTEKVifPRQDDVLISFLPLAHMFerviqsvvychgGRVGFFQGDIRL--------- 350
Cdd:cd05904 170 TGRSKGVMLTHRNLIAMVAQFVAGEGSN--SDSEDVFLCVLPMFHIY------------GLSSFALGLLRLgatvvvmpr 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 351 --LSDDMKAL---RPTIFPVVPRLLnrmydkifhqadtslkrwllefAAKRKQAEVRSGIIRnnsiwdelffnkiqaSLg 425
Cdd:cd05904 236 fdLEELLAAIeryKVTHLPVVPPIV----------------------LALVKSPIVDKYDLS---------------SL- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 426 ghvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFTTP---GDWTSGHVGAPLPCNHIKLVDAEELNYWT 501
Cdd:cd05904 278 ---RQIMSGAAPLGKELIeAFRAKFPNVDLGQGYGMTESTGVVAMCFApekDRAKYGSVGRLVPNVEAKIVDPETGESLP 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 48256734 502 SKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENI 576
Cdd:cd05904 355 PNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEAL 428
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
121-609 |
1.82e-40 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 153.98 E-value: 1.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLgSGLLQHDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIv 200
Cdd:cd05941 12 ITYADLVARAARL-ANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 201 dkphkailllehverketpglklvilmepfDDALrergkkcgvdiksmqaiedsgqenhrvpvpprpddlsiVCFTSGTT 280
Cdd:cd05941 90 ------------------------------DPAL--------------------------------------ILYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 281 GNPKGAMLTHGNVVADFSGFLKVTEKvifpRQDDVLISFLPLAHMFERV--IQSVVYChGGRV---GFFQGDIRLLSDDM 355
Cdd:cd05941 102 GRPKGVVLTHANLAANVRALVDAWRW----TEDDVLLHVLPLHHVHGLVnaLLCPLFA-GASVeflPKFDPKEVAISRLM 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 356 KALrpTIFPVVPRllnrMYDKIFHQADTSLKrwllEFAAKRKQAEvrsgiirnnsiwdelffnkiqaslgGHVRMIVTGA 435
Cdd:cd05941 177 PSI--TVFMGVPT----IYTRLLQYYEAHFT----DPQFARAAAA-------------------------ERLRLMVSGS 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 436 APASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTTP--GDWTSGHVGAPLPCNHIKLVDAEELNYWTSKGEGEICVKGP 513
Cdd:cd05941 222 AALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGP 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 514 NVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKK-HIFKlAQGEYVAPEKIENIYIRSEPVAQIYVHGDS 592
Cdd:cd05941 300 SVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEIERVLLAHPGVSECAVIGVP 378
|
490 500
....*....|....*....|
gi 48256734 593 LKAF---LVGIVVPDPEVMP 609
Cdd:cd05941 379 DPDWgerVVAVVVLRAGAAA 398
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
121-576 |
2.78e-40 |
|
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: 154.41 E-value: 2.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSgLLQHDCKVGteQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:cd05909 8 LTYRKLLTGAIALAR-KLAKMTKEG--ENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 201 DKPHKAILLLEHVERKETPgLKLVILmepfdDALRER---GKKCGVDIKSMQAIEDSGQENHRVPVppRPDDLSIVCFTS 277
Cdd:cd05909 85 SKQFIEKLKLHHLFDVEYD-ARIVYL-----EDLRAKiskADKCKAFLAGKFPPKWLLRIFGVAPV--QPDDPAVILFTS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 278 GTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAHMFerviqsvvychggrvGFFQGDIRLLSDDMKA 357
Cdd:cd05909 157 GSEGLPKGVVLSHKNLLANVEQITAIFD----PNPEDVVFGALPFFHSF---------------GLTGCLWLPLLSGIKV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 358 L---RPTIFPVVPRLLnrmYDK---IFHQADTSLKRWllefaAKRKQAEVRSGIirnnsiwdelffnkiqaslgghvRMI 431
Cdd:cd05909 218 VfhpNPLDYKKIPELI---YDKkatILLGTPTFLRGY-----ARAAHPEDFSSL-----------------------RLV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 432 VTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPCNHIKLVDAEELNYWTSKGEGEICV 510
Cdd:cd05909 267 VAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLV 346
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 48256734 511 KGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENI 576
Cdd:cd05909 347 RGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDI 410
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
120-683 |
7.48e-38 |
|
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: 147.46 E-value: 7.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 120 WLSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVI 199
Cdd:cd05926 14 ALTYADLAELVDDLARQLAALGIKKGDR--VAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 200 VDKPHkailLLEHVERKETPGLKLVILMepFDDALRERgkkcgVDIKSMQAIEDSGQENHRVPVPPRPDDLSIVCFTSGT 279
Cdd:cd05926 92 TPKGE----LGPASRAASKLGLAILELA--LDVGVLIR-----APSAESLSNLLADKKNAKSEGVPLPDDLALILHTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 280 TGNPKGAMLTHGNVVADFSGFLKVTEkvIFPrqDDVLISFLPLAHmferVIQSVVYC-----HGGRV----GFfqgDIRL 350
Cdd:cd05926 161 TGRPKGVPLTHRNLAASATNITNTYK--LTP--DDRTLVVMPLFH----VHGLVASLlstlaAGGSVvlppRF---SAST 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 351 LSDDMKALRPTIFPVVPRLlnrmydkifHQAdtslkrwLLEFAAKRKQAEVrsgiirnnsiwdelffnkiqaslgGHVRM 430
Cdd:cd05926 230 FWPDVRDYNATWYTAVPTI---------HQI-------LLNRPEPNPESPP------------------------PKLRF 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 431 IVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTP---GDWTSGHVGAPLPcNHIKLVDaEELNYWTSKGEGE 507
Cdd:cd05926 270 IRSCSASLPPAVLEALEATFGAPVLEAYGMTE-AAHQMTSNPlppGPRKPGSVGKPVG-VEVRILD-EDGEILPPGVVGE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 508 ICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQIY 587
Cdd:cd05926 347 ICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVLLSHPAVLEAV 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 588 VHGdslkaflvgivVPDP---EVMPCWAQKKGiegnyqelcKSKELKKAILDDMvmlgkESGLHSFEQVKAIYIhcdmfs 664
Cdd:cd05926 426 AFG-----------VPDEkygEEVAAAVVLRE---------GASVTEEELRAFC-----RKHLAAFKVPKKVYF------ 474
|
570
....*....|....*....
gi 48256734 665 VQNGLLTPTLKAKRPELRE 683
Cdd:cd05926 475 VDELPKTATGKIQRRKVAE 493
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
123-615 |
6.47e-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: 143.74 E-value: 6.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 123 YQEVAKRAEFLgsgllqHDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIVDK 202
Cdd:TIGR01923 6 DCEAAHLAKAL------KAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 203 PhkailllehverketpglklvilmepfddaLRERGkkcgVDIKSMQAIEDSGQENHRVPVPPRPDDLSIVCFTSGTTGN 282
Cdd:TIGR01923 80 L------------------------------LEEKD----FQADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 283 PKGAMLTHGNVVADFSGflkVTEKVIFPRQDDVLISfLPLAH------MFERVIQsvvychGGRVGFFQGDIRLLsDDMK 356
Cdd:TIGR01923 126 PKAVPHTFRNHYASAVG---SKENLGFTEDDNWLLS-LPLYHisglsiLFRWLIE------GATLRIVDKFNQLL-EMIA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 357 ALRPTIFPVVPRLLNRMYDKIFHqaDTSLKRWLLefaakrkqaevrsgiirnnsiwdelffnkiqaslGGhvrmivtGAA 436
Cdd:TIGR01923 195 NERVTHISLVPTQLNRLLDEGGH--NENLRKILL----------------------------------GG-------SAI 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 437 PASptvlgFLRAAL--GCQVYEGYGQTE-CTAGCTFTTPGDWTSGHVGAPLPCNHIKL-VDAEElnywtskGEGEICVKG 512
Cdd:TIGR01923 232 PAP-----LIEEAQqyGLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIkVDNKE-------GHGEIMVKG 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 513 PNVFKGYLKDEDRTkEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYV--HG 590
Cdd:TIGR01923 300 ANLMKGYLYQGELT-PAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVVvpKP 377
|
490 500 510
....*....|....*....|....*....|
gi 48256734 591 DSL-----KAFLVGIVVPDPEVMPCWAQKK 615
Cdd:TIGR01923 378 DAEwgqvpVAYIVSESDISQAKLIAYLTEK 407
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
255-604 |
1.85e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 144.76 E-value: 1.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 255 GQENHRVPVP-PRPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD-FSGFLKVTEkviFPRQDDVLISFLPLAHMF--ERVI 330
Cdd:PRK05605 205 GGDGSDVSHPrPTPDDVALILYTSGTTGKPKGAQLTHRNLFANaAQGKAWVPG---LGDGPERVLAALPMFHAYglTLCL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 331 QSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLlnrmYDKIfhqadtslkrwlLEFAAKRkqaevrsGIirnns 410
Cdd:PRK05605 282 TLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPL----YEKI------------AEAAEER-------GV----- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 411 iwdelffnkiqaSLGGhVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECT---AGCTFTTpgDWTSGHVGAPLPCN 487
Cdd:PRK05605 334 ------------DLSG-VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpiiVGNPMSD--DRRPGYVGVPFPDT 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 488 HIKLVDAEELNYWTSKGE-GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGE 566
Cdd:PRK05605 399 EVRIVDPEDPDETMPDGEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELI-ITGGF 476
|
330 340 350
....*....|....*....|....*....|....*...
gi 48256734 567 YVAPEKIEniyirsEPVAQiyvHGDSLKAFLVGIVVPD 604
Cdd:PRK05605 477 NVYPAEVE------EVLRE---HPGVEDAAVVGLPRED 505
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
137-606 |
1.11e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 135.32 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 137 LLQHDCKVGteQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADictvivdkphkailllehverk 216
Cdd:PRK09088 39 LRRRGCVDG--ERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAE---------------------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 217 etPGLKLvilmepfDDALRERGKKCGVDIKSMQAIEDSGQENHRVPVPPrpDDLSIVCFTSGTTGNPKGAMLTHGNVVAD 296
Cdd:PRK09088 95 --PRLLL-------GDDAVAAGRTDVEDLAAFIASADALEPADTPSIPP--ERVSLILFTSGTSGQPKGVMLSERNLQQT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 297 FSGFlKVTEKVifprqdDVLISFLPLAHMFERV--IQSV--VYCHGGRV----GFFQG-DIRLLSDdmKALRPTIFPVVP 367
Cdd:PRK09088 164 AHNF-GVLGRV------DAHSSFLCDAPMFHIIglITSVrpVLAVGGSIlvsnGFEPKrTLGRLGD--PALGITHYFCVP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 368 RllnrMYDKIFHQADtslkrwlleFAAkrkqaevrsgiirnnsiwdelffnkiqASLGgHVRMIVTGAAP-ASPTVLGFL 446
Cdd:PRK09088 235 Q----MAQAFRAQPG---------FDA---------------------------AALR-HLTALFTGGAPhAAEDILGWL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 447 raALGCQVYEGYGQTEctAGCTFTTPGDWT-----SGHVGAPLPCNHIKLVDAEELNywTSKGE-GEICVKGPNVFKGYL 520
Cdd:PRK09088 274 --DDGIPMVDGFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVVDDQGND--CPAGVpGELLLRGPNLSPGYW 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 521 KDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIEniyirsepvAQIYVHGDSLKAFLVGi 600
Cdd:PRK09088 348 RRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIE---------AVLADHPGIRECAVVG- 416
|
....*.
gi 48256734 601 vVPDPE 606
Cdd:PRK09088 417 -MADAQ 421
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
262-598 |
2.52e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 135.28 E-value: 2.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 262 PVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGfLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRV 341
Cdd:PRK05677 201 EANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQ-CRALMGSNLNEGCEILIAPLPLYHIYAFTFHCMAMMLIGNH 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 342 GFFQGDIRLLSDDMKALRPTIFPVVPRLlNRMydkifhqadtslkrwlleFAAkrkqaevrsgiIRNNSIWDELFFNKIQ 421
Cdd:PRK05677 280 NILISNPRDLPAMVKELGKWKFSGFVGL-NTL------------------FVA-----------LCNNEAFRKLDFSALK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 422 ASLGGHvrMIVTGAAPASptvlgfLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVD--AEELny 499
Cdd:PRK05677 330 LTLSGG--MALQLATAER------WKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDddGNEL-- 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 500 wtSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYI 578
Cdd:PRK05677 400 --PLGEvGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVSGFNVYPNELEDVLA 476
|
330 340
....*....|....*....|....*..
gi 48256734 579 RSEPVAQ---IYV----HGDSLKAFLV 598
Cdd:PRK05677 477 ALPGVLQcaaIGVpdekSGEAIKVFVV 503
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
122-588 |
6.92e-33 |
|
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: 131.23 E-value: 6.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 122 SYQEVAKRAEFLGSGLLQHdCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGS-IRYIINTADICTVIV 200
Cdd:TIGR01733 1 TYRELDERANRLARHLRAA-GGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPL-DPAYPAErLAFILEDAGARLLLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 201 DKPHkailllehveRKETPGLKLVILMEPFDDALrergkkcgvdiksmqAIEDSGQENHRvPVPPRPDDLSIVCFTSGTT 280
Cdd:TIGR01733 79 DSAL----------ASRLAGLVLPVILLDPLELA---------------ALDDAPAPPPP-DAPSGPDDLAYVIYTSGST 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 281 GNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPLAH------MFerviqsVVYCHGGRVGFFQGDIRLlsDD 354
Cdd:TIGR01733 133 GRPKGVVVTHRSLVN----LLAWLARRYGLDPDDRVLQFASLSFdasveeIF------GALLAGATLVVPPEDEER--DD 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 355 MKALRptifpvvpRLLNRMYDKIFHQADTSLKRWLLEfaakrkqaevrsgiirnnsiwdelffnkiQASLGGHVRMIVTG 434
Cdd:TIGR01733 201 AALLA--------ALIAEHPVTVLNLTPSLLALLAAA-----------------------------LPPALASLRLVILG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 435 AAPASPTVLGFLRAALG-CQVYEGYGQTECTAGCT-FTTPGDWTSGHV----GAPLPCNHIKLVDaEELNYWTSKGEGEI 508
Cdd:TIGR01733 244 GEALTPALVDRWRARGPgARLINLYGPTETTVWSTaTLVDPDDAPRESpvpiGRPLANTRLYVLD-DDLRPVPVGVVGEL 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 509 CVKGPNVFKGYLKDEDRTKEA-LDSDGWL-------HTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRS 580
Cdd:TIGR01733 323 YIGGPGVARGYLNRPELTAERfVPDPFAGgdgarlyRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAALLRH 401
|
....*...
gi 48256734 581 EPVAQIYV 588
Cdd:TIGR01733 402 PGVREAVV 409
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
259-605 |
6.98e-33 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 133.85 E-value: 6.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 259 HRVP-VPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADF---SGFLKVTEKVifPRQDDVLISFLPLAHMFERVIQSVV 334
Cdd:PRK08751 198 HSMPtLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMqqaHQWLAGTGKL--EEGCEVVITALPLYHIFALTANGLV 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 335 YCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLlNRMYDKIFhqadtslkrwllefaakrkqaevrsgiirNNSIWDE 414
Cdd:PRK08751 276 FMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGV-NTLFNGLL-----------------------------NTPGFDQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 415 LFFNKIQASLGGHvrMIVTGAapasptVLGFLRAALGCQVYEGYGQTECT-AGCTFTTPGDWTSGHVGAPLPCNHIKLVD 493
Cdd:PRK08751 326 IDFSSLKMTLGGG--MAVQRS------VAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDACIKD 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 494 aeELNYWTSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEK 572
Cdd:PRK08751 398 --DAGTVLAIGEiGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-LVSGFNVYPNE 474
|
330 340 350
....*....|....*....|....*....|....*..
gi 48256734 573 IENIYIRSEPVAQIYVHG----DSLKAFLVGIVVPDP 605
Cdd:PRK08751 475 IEDVIAMMPGVLEVAAVGvpdeKSGEIVKVVIVKKDP 511
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
267-598 |
1.01e-32 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 133.26 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPRQDDVLISfLPLAHMFERVIQSVVYCHGGRVGFF-- 344
Cdd:PRK08974 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGPLLHPGKELVVTA-LPLYHIFALTVNCLLFIELGGQNLLit 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 345 -QGDIRLLSDDMKALRPTIFPVVPRLLNRmydkifhqadtslkrWLlefaakrkqaevrsgiirNNSIWDELFFNKIQAS 423
Cdd:PRK08974 284 nPRDIPGFVKELKKYPFTAITGVNTLFNA---------------LL------------------NNEEFQELDFSSLKLS 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 424 LGGhvrmivtgAAPASPTVLGFLRAALGCQVYEGYGQTECT---AGCTFTTPGdwTSGHVGAPLPCNHIKLVDaEELNYW 500
Cdd:PRK08974 331 VGG--------GMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVNPYDLDY--YSGSIGLPVPSTEIKLVD-DDGNEV 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 501 TSKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRS 580
Cdd:PRK08974 400 PPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMI-LVSGFNVYPNEIEDVVMLH 477
|
330 340
....*....|....*....|....*
gi 48256734 581 EPVAQIY-------VHGDSLKAFLV 598
Cdd:PRK08974 478 PKVLEVAavgvpseVSGEAVKIFVV 502
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
93-636 |
1.33e-32 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 132.93 E-value: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 93 YQVFRRGLSISGNGPCLGFRKPEQPYQWLSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELACYTYSM 172
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRALG--VKKGDRVAIYLPNIPEAVIAMLACARIGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 173 VVVPLYDTLGPGSIRYIINTADICTVIVD----KPHKAILLLEHVE--RKETPGLKLVILMEPFDDALRERGkkcgvDIK 246
Cdd:COG0365 90 VHSPVFPGFGAEALADRIEDAEAKVLITAdgglRGGKVIDLKEKVDeaLEELPSLEHVIVVGRTGADVPMEG-----DLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 247 SMQAIEDSGQENHRVPVPPrpDDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVTEKVIF-PRQDDVL--------- 316
Cdd:COG0365 165 WDELLAAASAEFEPEPTDA--DDPLFILYTSGTTGKPKGVVHTHGGYL----VHAATTAKYVLdLKPGDVFwctadigwa 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 317 -----ISFLPLAH-----MFERVIqsvVYCHGGRVgffqgdIRLLSDdmkaLRPTIFPVVPRLLnRMydkifhqadtsLK 386
Cdd:COG0365 239 tghsyIVYGPLLNgatvvLYEGRP---DFPDPGRL------WELIEK----YGVTVFFTAPTAI-RA-----------LM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 387 RWLLEFAAKRKQAevrsgiirnnsiwdelffnkiqaslggHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECtaG 466
Cdd:COG0365 294 KAGDEPLKKYDLS---------------------------SLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTET--G 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 467 CTFTTPGDWTS---GHVGAPLPCNHIKLVDAE--ELnywTSKGEGEICVKG--PNVFKGYLKDEDRTKEAL--DSDGWLH 537
Cdd:COG0365 345 GIFISNLPGLPvkpGSMGKPVPGYDVAVVDEDgnPV---PPGEEGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYR 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 538 TGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQIYVhgdslkaflVGivVPDP---EVMPCWAQ- 613
Cdd:COG0365 422 TGDGARRDEDGYFWILGRSDDVINVS-GHRIGTAEIESALVSHPAVAEAAV---------VG--VPDEirgQVVKAFVVl 489
|
570 580
....*....|....*....|...
gi 48256734 614 KKGIEGnyqelckSKELKKAILD 636
Cdd:COG0365 490 KPGVEP-------SDELAKELQA 505
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
122-606 |
4.43e-32 |
|
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: 131.11 E-value: 4.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 122 SYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLgpgSIRYIINTADICT-VIV 200
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYG--LKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIY---NERELDHSLNISKpTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 201 DKPHKAILLLEHVERKeTPGLKLVILMEPFDDAlreRGKKCGVDIKSMQAIEDSGQENHRVPVPPRPDDLSIVCFTSGTT 280
Cdd:cd17642 121 FCSKKGLQKVLNVQKK-LKIIKTIIILDSKEDY---KGYQCLYTFITQNLPPGFNEYDFKPPSFDRDEQVALIMNSSGST 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 281 GNPKGAMLTHGNVVADFSGflkvTEKVIF---PRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGffqgdirllsddmka 357
Cdd:cd17642 197 GLPKGVQLTHKNIVARFSH----ARDPIFgnqIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVV--------------- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 358 lrptifpvvprLLNRMYDKIFHQA-------DTSLKRWLLEFAAKrkqaevrSGIIrnnsiwdelffNKIQASlggHVRM 430
Cdd:cd17642 258 -----------LMYKFEEELFLRSlqdykvqSALLVPTLFAFFAK-------STLV-----------DKYDLS---NLHE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 431 IVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYWTSKGEGEIC 509
Cdd:cd17642 306 IASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELC 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 510 VKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYVH 589
Cdd:cd17642 386 VKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQHPKIFDAGVA 464
|
490
....*....|....*..
gi 48256734 590 GdslkaflvgivVPDPE 606
Cdd:cd17642 465 G-----------IPDED 470
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-628 |
5.09e-32 |
|
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: 127.39 E-value: 5.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSGF-LKVTEkvifprqDDVLISFLPLAHMFERVIqSVVYC--HGGRV 341
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVnnGYFIGErLGLTE-------QDRLCIPVPLFHCFGSVL-GVLACltHGATM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 342 GF----FqgDIRLLSDDMKALRPTIFPVVPRllnrMYDKIFHQADtslkrwLLEFAAKRkqaeVRSGIIrnnsiwdelff 417
Cdd:cd05917 73 VFpspsF--DPLAVLEAIEKEKCTALHGVPT----MFIAELEHPD------FDKFDLSS----LRTGIM----------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 418 nkiqaslgghvrmivtGAAPASPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGDWTS---GHVGAPLPCNHIKLVD 493
Cdd:cd05917 126 ----------------AGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDSIEkrvNTVGRIMPHTEAKIVD 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 494 AEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKI 573
Cdd:cd05917 190 PEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGENIYPREI 268
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 48256734 574 ENIyirsepvaqIYVHGDSLKAFLVGivVPDP----EVMPCWAQKKG---IEGNYQELCKSK 628
Cdd:cd05917 269 EEF---------LHTHPKVSDVQVVG--VPDErygeEVCAWIRLKEGaelTEEDIKAYCKGK 319
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
89-694 |
8.07e-32 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 133.06 E-value: 8.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 89 ARTMYQVFRRGLSISGNGPCLGFRKPEQPYQWLSYQEVAKRAEFLGSGLLQHDCKVGteQFIGVFAQNRPEWIIAELACY 168
Cdd:PTZ00297 426 VRSLGEMWERSVTRHSTFRCLGQTSESGESEWLTYGTVDARARELGSGLLALGVRPG--DVIGVDCEASRNIVILEVACA 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 169 TYSMVVVPLydtLGPGS-IRYIINTADICTVIVDKPHKAILLLEHVERKETpglklVILMEPFDDALRER-GKKCGVDIK 246
Cdd:PTZ00297 504 LYGFTTLPL---VGKGStMRTLIDEHKIKVVFADRNSVAAILTCRSRKLET-----VVYTHSFYDEDDHAvARDLNITLI 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 247 SMQAIEDSGQENhrvPVPPRP--DDLSIVCFTSGTTGNPKGAML-----THGNVVADFSgFLKVTEKVIFPRQDDVLISF 319
Cdd:PTZ00297 576 PYEFVEQKGRLC---PVPLKEhvTTDTVFTYVVDNTTSASGDGLavvrvTHADVLRDIS-TLVMTGVLPSSFKKHLMVHF 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 320 LPLAHMFERVIQSVVYCHGGRVGffQGDIRLLSDDMKALRPTIFPVVPRLlnrmydkiFHQADTSLKR----------WL 389
Cdd:PTZ00297 652 TPFAMLFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSL--------FSTSRLQLSRanerysavysWL 721
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 390 LEfaakrKQAEVRSGII----RNNSIWDELFFNKIQASLGGHVRMIVTGAAPASPTV-----LGFLRAALGCQVYegygQ 460
Cdd:PTZ00297 722 FE-----RAFQLRSRLInihrRDSSLLRFIFFRATQELLGGCVEKIVLCVSEESTSFsllehISVCYVPCLREVF----F 792
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 461 TECTAGCTFTtpgdwtsghvGAPLPCNHIKLVDAEELNYWTSKGEGEICVKGpnvfkgylkDEDRTKEAldsdgwlhtgd 540
Cdd:PTZ00297 793 LPSEGVFCVD----------GTPAPSLQVDLEPFDEPSDGAGIGQLVLAKKG---------EPRRTLPI----------- 842
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 541 IGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAfLVGIVVPDPEVMPC-WAQKKGIEG 619
Cdd:PTZ00297 843 AAQWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEFeWRQSHCMGE 921
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 620 --------NYQELckSKELKKAILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEE 691
Cdd:PTZ00297 922 gggparqlGWTEL--VAYASSLLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIER 999
|
...
gi 48256734 692 LYS 694
Cdd:PTZ00297 1000 FYS 1002
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
121-590 |
1.72e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 129.89 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQPGDR--VGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVIC 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 201 DKPHK-----AILL-----LEHVERKET-----PGLKLVILMEPFD-------DALRERGKkcGVdikSMQAIEDSGQEN 258
Cdd:PRK12583 124 ADAFKtsdyhAMLQellpgLAEGQPGALacerlPELRGVVSLAPAPppgflawHELQARGE--TV---SREALAERQASL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 259 HRvpvpprpDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSG-FLKVTEKvifprqdDVLISFLPLAHMFERVIqSVVY 335
Cdd:PRK12583 199 DR-------DDPINIQYTSGTTGFPKGATLSHHNILnnGYFVAeSLGLTEH-------DRLCVPVPLYHCFGMVL-ANLG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 336 C--HGGRVGF----FQGDIRLLSddMKALRPTIFPVVPRL-LNRMYDKIFHQADTSlkrwllefaakrkqaEVRSGIIrn 408
Cdd:PRK12583 264 CmtVGACLVYpneaFDPLATLQA--VEEERCTALYGVPTMfIAELDHPQRGNFDLS---------------SLRTGIM-- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 409 nsiwdelffnkiqaslgghvrmivtGAAPASPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGD-----WTSghVGA 482
Cdd:PRK12583 325 -------------------------AGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSLQTTAADdlerrVET--VGR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 483 PLPCNHIKLVDAEELNywTSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFk 561
Cdd:PRK12583 378 TQPHLEVKVVDPDGAT--VPRGEiGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMI- 454
|
490 500
....*....|....*....|....*....
gi 48256734 562 LAQGEYVAPEKIENIYIRSEPVAQIYVHG 590
Cdd:PRK12583 455 IRGGENIYPREIEEFLFTHPAVADVQVFG 483
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
268-613 |
2.83e-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: 2.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 268 DDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF---LKVTEkvifprqDDVLISFLPLAHM--FERVIQSVVYchGGRVG 342
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSalnLGLTE-------DDNWLCALPLFHIsgLSILMRSVIY--GMTVY 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 343 FFQG-DIRLLSDDMKALRPTIFPVVPRLLNRMYdKIFHQADTSlkrwllefaakrkqaevrsgiirnnsiwdelffnkiq 421
Cdd:cd05912 148 LVDKfDAEQVLHLINSGKVTIISVVPTMLQRLL-EILGEGYPN------------------------------------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 422 aslggHVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTE-CTAGCTFTtPGDWTS--GHVGAPLPCNHIKLVDAEELN 498
Cdd:cd05912 190 -----NLRCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTEtCSQIVTLS-PEDALNkiGSAGKPLFPVELKIEDDGQPP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 499 YwtskGEGEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYI 578
Cdd:cd05912 263 Y----EVGEILLKGPNVTKGYLNRPDATEESFE-NGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLL 336
|
330 340 350
....*....|....*....|....*....|....*
gi 48256734 579 RSEPVAQIYVhgdslkaflVGIvvPDPEvmpcWAQ 613
Cdd:cd05912 337 SHPAIKEAGV---------VGI--PDDK----WGQ 356
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
119-615 |
2.83e-31 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 127.02 E-value: 2.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 119 QWlSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADiCTV 198
Cdd:cd05934 3 RW-TYAELLRESARIAAALAALGIRPGDR--VALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSG-AQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 199 IVdkphkailllehverketpglklvilmepfddalrergkkcgVDIKSMQaiedsgqenhrvpvpprpddlsivcFTSG 278
Cdd:cd05934 79 VV------------------------------------------VDPASIL-------------------------YTSG 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 279 TTGNPKGAMLTHGNVVadFSGFLKVTEKVIfpRQDDVLISFLPLAHM---FERVIQSVVycHGGRV--------GFFQGD 347
Cdd:cd05934 92 TTGPPKGVVITHANLT--FAGYYSARRFGL--GEDDVYLTVLPLFHInaqAVSVLAALS--VGATLvllprfsaSRFWSD 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 348 IRllsdDMKALRPTIFPVVPRLLNRmydkifhQADtslkrwllefAAKRKQAEVRsgiirnnsiwdelffnkiqaslggh 427
Cdd:cd05934 166 VR----RYGATVTNYLGAMLSYLLA-------QPP----------SPDDRAHRLR------------------------- 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 428 vrmiVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEelNYWTSKGE-G 506
Cdd:cd05934 200 ----AAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDD--GQELPAGEpG 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 507 EICVK---GPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSEPV 583
Cdd:cd05934 274 ELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVERAILRHPAV 351
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 48256734 584 AQIYVHG-------DSLKAFLVgiVVP----DPEVMPCWAQKK 615
Cdd:cd05934 352 REAAVVAvpdevgeDEVKAVVV--LRPgetlDPEELFAFCEGQ 392
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
121-606 |
6.42e-31 |
|
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: 126.10 E-value: 6.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELACY----TYsmvvVPLYDTLGPGSIRYIINTADIC 196
Cdd:cd05930 13 LTYAELDARANRLARYLRERG--VGPGDLVAVLLERSLEMVVAILAVLkagaAY----VPLDPSYPAERLAYILEDSGAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 197 TVIVDkphkailllehverketpglklvilmepfddalrergkkcgvdiksmqaiedsgqenhrvpvpprPDDLSIVCFT 276
Cdd:cd05930 87 LVLTD-----------------------------------------------------------------PDDLAYVIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 277 SGTTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPLAH------MFerviqsVVYCHGGRV----GFFQG 346
Cdd:cd05930 102 SGSTGKPKGVMVEHRGLVN----LLLWMQEAYPLTPGDRVLQFTSFSFdvsvweIF------GALLAGATLvvlpEEVRK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 347 DIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTSLkrwllefaakrkqaevrsgiirnnsiwdelffnkiqaslgg 426
Cdd:cd05930 172 DPEALADLLAEEGITVLHLTPSLLRLLLQELELAALPSL----------------------------------------- 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 427 hvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFT--TPGDWTSGHV--GAPLPCNHIKLVDaEELNYWT 501
Cdd:cd05930 211 --RLVLVGGEALPPDLVrRWRELLPGARLVNLYGPTEATVDATYYrvPPDDEEDGRVpiGRPIPNTRVYVLD-ENLRPVP 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 502 SKGEGEICVKGPNVFKGYLKDEDRTKEA-----LDSDGWLH-TGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIEN 575
Cdd:cd05930 288 PGVPGELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIELGEIEA 366
|
490 500 510
....*....|....*....|....*....|....
gi 48256734 576 IYIRSEPVAQIYV---HGDSLKAFLVGIVVPDPE 606
Cdd:cd05930 367 ALLAHPGVREAAVvarEDGDGEKRLVAYVVPDEG 400
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
269-599 |
1.57e-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: 1.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 269 DLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTEkvifprqDDVLISFLPLAHMFErviqsvvYCHGGRVGFFQ 345
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLraaAAWADCADLTE-------DDRYLIINPFFHTFG-------YKAGIVACLLT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 346 G---------DIRLLSDDMKALRPTIFPVVPRLlnrmYDKIFHQADtslkrwllefaakRKQAEVRSgiirnnsiwdelf 416
Cdd:cd17638 67 GatvvpvavfDVDAILEAIERERITVLPGPPTL----FQSLLDHPG-------------RKKFDLSS------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 417 fnkiqaslgghVRMIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGcTFTTPGD---WTSGHVGAPLPCNHIKLV 492
Cdd:cd17638 117 -----------LRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVA-TMCRPGDdaeTVATTCGRACPGFEVRIA 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 493 DAeelnywtskgeGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEK 572
Cdd:cd17638 185 DD-----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAE 252
|
330 340 350
....*....|....*....|....*....|....
gi 48256734 573 IENIYIRSEPVAQIYV-------HGDSLKAFLVG 599
Cdd:cd17638 253 VEGALAEHPGVAQVAVigvpderMGEVGKAFVVA 286
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
262-607 |
2.08e-30 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 126.29 E-value: 2.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 262 PVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADF--------SGFLKvtekvifPRQDDVLISF--LPLAHMFERVIQ 331
Cdd:PRK07059 198 PVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqmeawlqPAFEK-------KPRPDQLNFVcaLPLYHIFALTVC 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 332 SVVYCHGGRVGFF---QGDIRLLSDDMKALRPTIFPVVPRLLNRMYdkifhqadtslkrwllefaakrkqaevrsgiirN 408
Cdd:PRK07059 271 GLLGMRTGGRNILipnPRDIPGFIKELKKYQVHIFPAVNTLYNALL---------------------------------N 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 409 NSIWDELFFNKIQASLGGhvrmivtGAAPASPTVLGFLRAAlGCQVYEGYG--QTECTAGCTFTTPGDWTsGHVGAPLPC 486
Cdd:PRK07059 318 NPDFDKLDFSKLIVANGG-------GMAVQRPVAERWLEMT-GCPITEGYGlsETSPVATCNPVDATEFS-GTIGLPLPS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 487 NHIKLVDAE--ELnywtSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLA 563
Cdd:PRK07059 389 TEVSIRDDDgnDL----PLGEpGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMI-LV 463
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 48256734 564 QGEYVAPEKIENIyIRSEP----VAQIYVH----GDSLKAFlvgIVVPDPEV 607
Cdd:PRK07059 464 SGFNVYPNEIEEV-VASHPgvleVAAVGVPdehsGEAVKLF---VVKKDPAL 511
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
220-578 |
2.19e-30 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 126.25 E-value: 2.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 220 GLKLVILMEPFDDALRERGKKCGVDIKSMQAIED---------SGQENHRVPVPPRPDDLSIVCFTSGTTGNPKGAMLTH 290
Cdd:PLN02246 122 GAKLIITQSCYVDKLKGLAEDDGVTVVTIDDPPEgclhfseltQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTH 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 291 GNVVADfsgflkVTEKV------IFPRQDDVLISFLPLAHMFErvIQSVVYChGGRVG--------FfqgDIRLLSDDMK 356
Cdd:PLN02246 202 KGLVTS------VAQQVdgenpnLYFHSDDVILCVLPMFHIYS--LNSVLLC-GLRVGaailimpkF---EIGALLELIQ 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 357 ALRPTIFPVVPRLLnrmydkifhqadtslkrwlLEFAakrKQAEVRSgiirnnsiwDELffnkiqASlgghVRMIVTGAA 436
Cdd:PLN02246 270 RHKVTIAPFVPPIV-------------------LAIA---KSPVVEK---------YDL------SS----IRMVLSGAA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 437 PASPTVLGFLRAALGCQVY-EGYGQTE-------CTAgctFT-TPGDWTSGHVGAPLPCNHIKLVDAE---ELNYWTSkg 504
Cdd:PLN02246 309 PLGKELEDAFRAKLPNAVLgQGYGMTEagpvlamCLA---FAkEPFPVKSGSCGTVVRNAELKIVDPEtgaSLPRNQP-- 383
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 48256734 505 eGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYI 578
Cdd:PLN02246 384 -GEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAELEALLI 455
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
89-557 |
2.76e-30 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 126.61 E-value: 2.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 89 ARTMYQVFRRGLSISGNGPCLGF-------RKPEQpyqwLSYqevakrAEFLG-----SGLLqHDCKVGTEQFIGVFAQN 156
Cdd:PRK07529 24 PASTYELLSRAAARHPDAPALSFlldadplDRPET----WTY------AELLAdvtrtANLL-HSLGVGPGDVVAFLLPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 157 RPEWIIAELACYTYSmVVVPLYDTLGPGSIRYIINTADICTVIVDKP-------HKAILLLEHVerketPGLKLVI---- 225
Cdd:PRK07529 93 LPETHFALWGGEAAG-IANPINPLLEPEQIAELLRAAGAKVLVTLGPfpgtdiwQKVAEVLAAL-----PELRTVVevdl 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 226 ---LMEPFDDALRERGKKCGVDIKSMQAIEDSGQENHRV-PVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD-FSGF 300
Cdd:PRK07529 167 aryLPGPKRLAVPLIRRKAHARILDFDAELARQPGDRLFsGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANaWLGA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 301 LkvtekVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGR---VGFFQG--DIRLLSDDMK---ALRPTIFPVVPRLLNR 372
Cdd:PRK07529 247 L-----LLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAhvvLATPQGyrGPGVIANFWKiveRYRINFLSGVPTVYAA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 373 MYDKIFHQADTSLkrwlLEFAAkrkqaevrsgiirnnsiwdelffnkiqaslgghvrmivTGAAPASPTVLGFLRAALGC 452
Cdd:PRK07529 322 LLQVPVDGHDISS----LRYAL--------------------------------------CGAAPLPVEVFRRFEAATGV 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 453 QVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLVDAEEL-NYW--TSKGE-GEICVKGPNVFKGYLkDEDRTK 527
Cdd:PRK07529 360 RIVEGYGLTEATCVSSVNPPdGERRIGSVGLRLPYQRVRVVILDDAgRYLrdCAVDEvGVLCIAGPNVFSGYL-EAAHNK 438
|
490 500 510
....*....|....*....|....*....|
gi 48256734 528 EALDSDGWLHTGDIGKWLPEGTLKIIDRKK 557
Cdd:PRK07529 439 GLWLEDGWLNTGDLGRIDADGYFWLTGRAK 468
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
254-605 |
3.09e-30 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 125.37 E-value: 3.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 254 SGQENHRVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGN------VVADFSGFlkvtekvifpRQDDVLISFLPLAH--- 324
Cdd:PRK07514 142 AAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNllsnalTLVDYWRF----------TPDDVLIHALPIFHthg 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 325 MFerVIQSVVYCHGGRVGFFQG-DIRLLSDDMKalRPTIFPVVPRLLNRMYdkifhqADTSLKRwllEFAAkrkqaevrs 403
Cdd:PRK07514 212 LF--VATNVALLAGASMIFLPKfDPDAVLALMP--RATVMMGVPTFYTRLL------QEPRLTR---EAAA--------- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 404 giirnnsiwdelffnkiqaslggHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTfTTP--GDWTSGHVG 481
Cdd:PRK07514 270 -----------------------HMRLFISGSAPLLAETHREFQERTGHAILERYGMTE-TNMNT-SNPydGERRAGTVG 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 482 APLPCNHIKLVDAE---ELnywtSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKK 557
Cdd:PRK07514 325 FPLPGVSLRVTDPEtgaEL----PPGEiGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGK 400
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 48256734 558 HIfkLAQGEY-VAPEKIENiYIRSEP-VAQIYVHGDSLKAF---LVGIVVPDP 605
Cdd:PRK07514 401 DL--IISGGYnVYPKEVEG-EIDELPgVVESAVIGVPHPDFgegVTAVVVPKP 450
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
117-557 |
1.16e-29 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 123.93 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 117 PYQWLSYQEVAKRAEFLGSGLLQHDCKVGtEQFIGVFAQNRpEWIIAELACYTYSMVVVPLydtlGPGSIRYIINTAdic 196
Cdd:cd05906 36 SEEFQSYQDLLEDARRLAAGLRQLGLRPG-DSVILQFDDNE-DFIPAFWACVLAGFVPAPL----TVPPTYDEPNAR--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 197 tvivdkphkaILLLEHVerKETPGLKLVI----LMEPFDDALRERGKkCGVDIKSMQAIEDSGQENHRVPvpPRPDDLSI 272
Cdd:cd05906 107 ----------LRKLRHI--WQLLGSPVVLtdaeLVAEFAGLETLSGL-PGIRVLSIEELLDTAADHDLPQ--SRPDDLAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 273 VCFTSGTTGNPKGAMLTHGNVVADFSGflKVTEKVIFPrqDDVLISFLPLAHmfervIQSVVYCHggrvgffQGDIRLLS 352
Cdd:cd05906 172 LMLTSGSTGFPKAVPLTHRNILARSAG--KIQHNGLTP--QDVFLNWVPLDH-----VGGLVELH-------LRAVYLGC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 353 DDMKALRPTIFPVVPRLLNRMyDKifHQADTSlkrWLLEFA-AK-RKQAEVRSGiirnnSIWDelffnkiqasLGGHVRM 430
Cdd:cd05906 236 QQVHVPTEEILADPLRWLDLI-DR--YRVTIT---WAPNFAfALlNDLLEEIED-----GTWD----------LSSLRYL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 431 IVTGAAPASPTVLGFLRAALGCQVYE-----GYGQTECTAGCTFTTP---GDWTSGH----VGAPLPCNHIKLVDAEelN 498
Cdd:cd05906 295 VNAGEAVVAKTIRRLLRLLEPYGLPPdairpAFGMTETCSGVIYSRSfptYDHSQALefvsLGRPIPGVSMRIVDDE--G 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 499 YWTSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGkWLPEGTLKIIDRKK 557
Cdd:cd05906 373 QLLPEGEvGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
119-606 |
3.17e-29 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 122.28 E-value: 3.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 119 QWLSYQEVAKRAEFLgSGLLQHDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTV 198
Cdd:PRK06839 26 EEMTYKQLHEYVSKV-AAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 199 IVDKPHKAILLLehverketpgLKLVILMEPFddalrergkkcgVDIKSMQAIEDSGQENHrvpVPPRPDDLSIVCFTSG 278
Cdd:PRK06839 105 FVEKTFQNMALS----------MQKVSYVQRV------------ISITSLKEIEDRKIDNF---VEKNESASFIICYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 279 TTGNPKGAMLTHGNVvadfsgFLKVTEKV--IFPRQDDVLISFLPLAHMferviqsvvychgGRVGFFqgdirllsddmk 356
Cdd:PRK06839 160 TTGKPKGAVLTQENM------FWNALNNTfaIDLTMHDRSIVLLPLFHI-------------GGIGLF------------ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 357 ALrPTIFP----VVPRLLNRmyDKIFHQADTslKRWLLEFAAKRKQAEVRSGIIRNNSIWDelffnkiqaslggHVRMIV 432
Cdd:PRK06839 209 AF-PTLFAggviIVPRKFEP--TKALSMIEK--HKVTVVMGVPTIHQALINCSKFETTNLQ-------------SVRWFY 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 433 TGAAPAS-PTVLGFLRAalGCQVYEGYGQTEcTAGCTFTTPGD---WTSGHVGAPLPCNHIKLVDaEELNYWTSKGEGEI 508
Cdd:PRK06839 271 NGGAPCPeELMREFIDR--GFLFGQGFGMTE-TSPTVFMLSEEdarRKVGSIGKPVLFCDYELID-ENKNKVEVGEVGEL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 509 CVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIyirsepvaqIYV 588
Cdd:PRK06839 347 LIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQV---------INK 415
|
490
....*....|....*...
gi 48256734 589 HGDSLKAFLVGivVPDPE 606
Cdd:PRK06839 416 LSDVYEVAVVG--RQHVK 431
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
121-606 |
5.84e-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: 120.28 E-value: 5.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSGLlqHDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:cd05935 2 LTYLELLEVVKKLASFL--SNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 201 dkphkaillleHVERketpglklvilmepfddalrergkkcgvdiksmqaiedsgqenhrvpvpprpDDLSIVCFTSGTT 280
Cdd:cd05935 80 -----------GSEL----------------------------------------------------DDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 281 GNPKGAMLTHGNVVADFSGFLKVTEKVifprQDDVLISFLPLAHM--FERVIQSVVYCHGGRVGFFQGDIRLLSDDMKAL 358
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQSAVWTGLT----PSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMARWDRETALELIEKY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 359 RPTIFPVVPRLLNrmydkifhqadtslkrwllefaakrkqaevrsgiirnnsiwDELFFNKIQASLGGHVRMIVTGAAPA 438
Cdd:cd05935 173 KVTFWTNIPTMLV-----------------------------------------DLLATPEFKTRDLSSLKVLTGGGAPM 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 439 SPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYWTSKGEGEICVKGPNVFKG 518
Cdd:cd05935 212 PPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKG 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 519 YLKDEDRTKEALDSDG---WLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQIYV------- 588
Cdd:cd05935 292 YWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVisvpder 370
|
490
....*....|....*...
gi 48256734 589 HGDSLKAFlvgiVVPDPE 606
Cdd:cd05935 371 VGEEVKAF----IVLRPE 384
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
173-575 |
7.06e-29 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 120.62 E-value: 7.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 173 VVVPLYDTLGPGSIRYIINTADIctvivdkphkailllehverketpglKLVILMEPFDDALRERGKKCGVDIKSMQAIE 252
Cdd:cd05922 48 VFVPLNPTLKESVLRYLVADAGG--------------------------RIVLADAGAADRLRDALPASPDPGTVLDADG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 253 DSGQENHRVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTEkvifprqDDVLISFLPLAhmferv 329
Cdd:cd05922 102 IRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSiaeYLGITA-------DDRALTVLPLS------ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 330 iqsvvYCHGGRV---GFFQGDIRLLSDDMkalrptifpVVPRLLnrmYDKIFHQADTSLkrwllefaakrkqaevrSGII 406
Cdd:cd05922 169 -----YDYGLSVlntHLLRGATLVLTNDG---------VLDDAF---WEDLREHGATGL-----------------AGVP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 407 RNNSIWDELFFNKIQASlggHVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFTTPG--DWTSGHVGAP 483
Cdd:cd05922 215 STYAMLTRLGFDPAKLP---SLRYLTQAGGRLPQETIARLRELLpGAQVYVMYGQTEATRRMTYLPPEriLEKPGSIGLA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 484 LPCNHIKLVDAEELNywTSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKL 562
Cdd:cd05922 292 IPGGEFEILDDDGTP--TPPGEpGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKL 369
|
410
....*....|...
gi 48256734 563 AqGEYVAPEKIEN 575
Cdd:cd05922 370 F-GNRISPTEIEA 381
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
269-588 |
1.36e-28 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 120.85 E-value: 1.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 269 DLSIVCFTSGTTGNPKGAMLTHGNVVADF-SGFLKVTEKVIfprQDDVLISFLPLAHMF--ERVIQSVVYCHGGRVGFFQ 345
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTHRNLVANLcSSLFSVGPEMI---GQVVTLGLIPFFHIYgiTGICCATLRNKGKVVVMSR 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 346 GDIRLLSDDMKALRPTIFPVVPRLLNRMYdkifhqadtslkrwllefaakrkqaevrsgiirNNSIWDELFFNKIQaslg 425
Cdd:PLN02330 262 FELRTFLNALITQEVSFAPIVPPIILNLV---------------------------------KNPIVEEFDLSKLK---- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 426 ghVRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTagCTFTTPGDWTSGH-------VGAPLPCNHIKLVDAEEL 497
Cdd:PLN02330 305 --LQAIMTAAAPLAPELLtAFEAKFPGVQVQEAYGLTEHS--CITLTHGDPEKGHgiakknsVGFILPNLEVKFIDPDTG 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 498 NYWTSKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIY 577
Cdd:PLN02330 381 RSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAIL 459
|
330
....*....|.
gi 48256734 578 IRSEPVAQIYV 588
Cdd:PLN02330 460 LTHPSVEDAAV 470
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
262-598 |
1.39e-28 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 121.08 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 262 PVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKV------IFPRQDDVLISFLPLAHMFErviqsvvy 335
Cdd:PRK12492 201 PVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLgpdgqpLMKEGQEVMIAPLPLYHIYA-------- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 336 chggrvgfFQGDIRLLsddMKALRPTIFPVVPRLLNRMYDKifhqadtsLKRWLLefaakrkqaevrSGIIRNNSIWDEL 415
Cdd:PRK12492 273 --------FTANCMCM---MVSGNHNVLITNPRDIPGFIKE--------LGKWRF------------SALLGLNTLFVAL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 416 F----FNKIQASlggHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHIK 490
Cdd:PRK12492 322 MdhpgFKDLDFS---ALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELARlGTVGIPVPGTALK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 491 LVDAE--ELNYwtskGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEY 567
Cdd:PRK12492 399 VIDDDgnELPL----GErGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLI-IVSGFN 473
|
330 340 350
....*....|....*....|....*....|....*...
gi 48256734 568 VAPEKIENIYIRSEPVAQIYV-------HGDSLKAFLV 598
Cdd:PRK12492 474 VYPNEIEDVVMAHPKVANCAAigvpderSGEAVKLFVV 511
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
121-588 |
1.40e-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: 119.41 E-value: 1.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSGLLQhdCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADIctviv 200
Cdd:cd05903 2 LTYSELDTRADRLAAGLAA--LGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 201 dkphkailllehverketpglKLVILMEPFddalrergkkcgvdiksmqaiedsGQENHRvpvpPRPDDLSIVCFTSGTT 280
Cdd:cd05903 75 ---------------------KVFVVPERF------------------------RQFDPA----AMPDAVALLLFTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 281 GNPKGAMLTHGNVVADFSGFLkvtEKVIFPRQDDVLISfLPLAHMferviqsVVYCHGGRVGFFQGDIRLLSDDMKALRp 360
Cdd:cd05903 106 GEPKGVMHSHNTLSASIRQYA---ERLGLGPGDVFLVA-SPMAHQ-------TGFVYGFTLPLLLGAPVVLQDIWDPDK- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 361 tifpvVPRLLNRMYDKIFHQADTSLKRWL--LEFAAKRKQaevrsgiirnnsiwdelffnkiqaslggHVRMIVTGAAPA 438
Cdd:cd05903 174 -----ALALMREHGVTFMMGATPFLTDLLnaVEEAGEPLS----------------------------RLRTFVCGGATV 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 439 SPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGD----WTSGhvGAPLPCNHIKLVDAEELNYwTSKGEGEICVKGPN 514
Cdd:cd05903 221 PRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPedrrLYTD--GRPLPGVEIKVVDDTGATL-APGVEGELLSRGPS 297
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 48256734 515 VFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYV 588
Cdd:cd05903 298 VFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAV 369
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
112-606 |
4.23e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 119.29 E-value: 4.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 112 RKPEQPYQW-----LSYQEVAKRAEFLgSGLLQHDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSI 186
Cdd:PRK08314 22 RYPDKTAIVfygraISYRELLEEAERL-AGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 187 RYIINTADICTVIVD-------KPHKAILLLEHV-------ERKETPGLKLvilmePfdDALRERGKKCGVDIKSMQAIE 252
Cdd:PRK08314 101 AHYVTDSGARVAIVGselapkvAPAVGNLRLRHVivaqysdYLPAEPEIAV-----P--AWLRAEPPLQALAPGGVVAWK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 253 DSGQENHRV-PVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD-FSGFLKVTEKVifprqDDVLISFLPLAHM--FER 328
Cdd:PRK08314 174 EALAAGLAPpPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANaVGSVLWSNSTP-----ESVVLAVLPLFHVtgMVH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 329 VIQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLL-NRMYDKIFHQADTSlkrwllefaakrkqaevrsgiir 407
Cdd:PRK08314 249 SMNAPIYAGATVVLMPRWDREAAARLIERYRVTHWTNIPTMVvDFLASPGLAERDLS----------------------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 408 nnsiwdelffnkiqaSLgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWT-SGHVGAPLPC 486
Cdd:PRK08314 306 ---------------SL----RYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTE-TMAQTHSNPPDRPkLQCLGIPTFG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 487 NHIKLVDAEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEA---LDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlA 563
Cdd:PRK08314 366 VDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMIN-A 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 48256734 564 QGEYVAPEKIENIYIRSEPVAQIYV-------HGDSLKAFlvgiVVPDPE 606
Cdd:PRK08314 445 SGFKVWPAEVENLLYKHPAIQEACViatpdprRGETVKAV----VVLRPE 490
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
119-550 |
5.58e-28 |
|
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: 120.73 E-value: 5.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 119 QWLSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELA------CYtysmvvVPLYDTLGPGSIRYIINT 192
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALG--VGPGDLVGVCLERSLEMVVALLAvlkagaAY------VPLDPAYPAERLAYMLED 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 193 ADICTVIVDkphkailllehverketpglklvilmepfdDALRERGKKCGVDIKSMQAIEDSGQENHRVPVPPRPDDLSI 272
Cdd:COG1020 572 AGARLVLTQ------------------------------SALAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLAY 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 273 VCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTEkvifprQDDVL----ISF--------LPLahmferviqsvvyCH 337
Cdd:COG1020 622 VIYTSGSTGRPKGVMVEHRALVnllAWMQRRYGLGP------GDRVLqfasLSFdasvweifGAL-------------LS 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 338 GGRVGFFQGDIRL----LSDDMKALRPTIFPVVPRLLNRmydkifhqadtslkrwLLEFAAKRkqaevrsgiirnnsiwd 413
Cdd:COG1020 683 GATLVLAPPEARRdpaaLAELLARHRVTVLNLTPSLLRA----------------LLDAAPEA----------------- 729
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 414 elffnkiqaslGGHVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTF--TTPGDWTSGHV--GAPLPCNH 488
Cdd:COG1020 730 -----------LPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTVDSTYyeVTPPDADGGSVpiGRPIANTR 798
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 48256734 489 IKLVDAEelnywtskGE-------GEICVKGPNVFKGYLKDEDRTKEA-----LDSDG--WLHTGDIGKWLPEGTL 550
Cdd:COG1020 799 VYVLDAH--------LQpvpvgvpGELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNL 866
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
123-590 |
9.97e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 117.37 E-value: 9.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 123 YQEVAKRAEFLGSGLLQHDCKVGteqfigVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIVDk 202
Cdd:PRK03640 34 HEAVVSVAGKLAALGVKKGDRVA------LLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITD- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 203 phkailllehverketpglklvilmEPFDDALRErgkKCGVDIKSMQAiedsGQENHRVPVPPRP-DDLSIVCFTSGTTG 281
Cdd:PRK03640 107 -------------------------DDFEAKLIP---GISVKFAELMN----GPKEEAEIQEEFDlDEVATIMYTSGTTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 282 NPKGAMLTHGNVVADFSGF---LKVTEKvifprqDDVLISfLPLAHM--FERVIQSVVYchGGRVGFFQG-DIRLLSDDM 355
Cdd:PRK03640 155 KPKGVIQTYGNHWWSAVGSalnLGLTED------DCWLAA-VPIFHIsgLSILMRSVIY--GMRVVLVEKfDAEKINKLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 356 KALRPTIFPVVPRLLNRMYDKIFhqadtslkrwllefaakrkqaevrsgiirnnsiwdelffnkiQASLGGHVRMIVTGA 435
Cdd:PRK03640 226 QTGGVTIISVVSTMLQRLLERLG------------------------------------------EGTYPSSFRCMLLGG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 436 APASPTVLGFLRAAlGCQVYEGYGQTEcTAGCTFTTPGDWTS---GHVGAPL-PCNhIKLVDaeELNYWTSKGEGEICVK 511
Cdd:PRK03640 264 GPAPKPLLEQCKEK-GIPVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLfPCE-LKIEK--DGVVVPPFEEGEIVVK 338
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 48256734 512 GPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYVHG 590
Cdd:PRK03640 339 GPNVTKGYLNREDATRETFQ-DGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPGVAEAGVVG 415
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
119-604 |
2.25e-27 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 116.24 E-value: 2.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 119 QWLSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTAdictv 198
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARG--VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDA----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 199 ivdkphKAILLLEhverketpglklvilmepfDDALRERGKKCGVDIksMQAIEDSGQENHRVPVPPRPDDLSIVCFTSG 278
Cdd:cd12116 84 ------EPALVLT-------------------DDALPDRLPAGLPVL--LLALAAAAAAPAAPRTPVSPDDLAYVIYTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 279 TTGNPKGAMLTHGNVVADFSGFlkvTEKVIFPRQDDVL--------IS----FLPLahmferviqsvvyCHGGRVGFFQG 346
Cdd:cd12116 137 STGRPKGVVVSHRNLVNFLHSM---RERLGLGPGDRLLavttyafdISllelLLPL-------------LAGARVVIAPR 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 347 DI----RLLSDDMKALRPTIFpvvprllnrmydkifhQADTSLKRWLLEfaakrkqaevrSGiirnnsiWDELffnkiqa 422
Cdd:cd12116 201 ETqrdpEALARLIEAHSITVM----------------QATPATWRMLLD-----------AG-------WQGR------- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 423 slgGHVRMIVTGAApaSPTVLGFLRAALGCQVYEGYGQTECT--AGCTFTTPGDwTSGHVGAPLPCNHIKLVDAeelnYW 500
Cdd:cd12116 240 ---AGLTALCGGEA--LPPDLAARLLSRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLDA----AL 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 501 TS--KGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLH-------TGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAP 570
Cdd:cd12116 310 RPvpPGVpGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQVKI-RGHRIEL 388
|
490 500 510
....*....|....*....|....*....|....*.
gi 48256734 571 EKIENIYIRSEPVAQ--IYVHGDSLKAFLVGIVVPD 604
Cdd:cd12116 389 GEIEAALAAHPGVAQaaVVVREDGGDRRLVAYVVLK 424
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
121-609 |
4.15e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 115.85 E-value: 4.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAE-----FLGSGLLQHDCkvgteqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADI 195
Cdd:PRK06188 38 LTYGQLADRISryiqaFEALGLGTGDA-------VALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 196 CTVIVDK---PHKAILLLEHVerketPGLKLVILMEPFDDalrergkkcGVDIKSMQAIEDsgqenHRVPVPP-RPDDLS 271
Cdd:PRK06188 111 STLIVDPapfVERALALLARV-----PSLKHVLTLGPVPD---------GVDLLAAAAKFG-----PAPLVAAaLPPDIA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 272 IVCFTSGTTGNPKGAMLTHGNVV-------ADFSgflkvtekviFPRQddvlISFL---PLAH----MFERVIQsvvycH 337
Cdd:PRK06188 172 GLAYTGGTTGKPKGVMGTHRSIAtmaqiqlAEWE----------WPAD----PRFLmctPLSHaggaFFLPTLL-----R 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 338 GGRVGFFQG-DIRLLSDDMKALRPTIFPVVPRLLNRmydkifhqadtslkrwLLEFAAKRKqaevrsgiiRNNSiwdelf 416
Cdd:PRK06188 233 GGTVIVLAKfDPAEVLRAIEEQRITATFLVPTMIYA----------------LLDHPDLRT---------RDLS------ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 417 fnkiqaSLgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHV------GAPLPCNHIK 490
Cdd:PRK06188 282 ------SL----ETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLRVA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 491 LVDAEELNywTSKGE-GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVA 569
Cdd:PRK06188 352 LLDEDGRE--VAQGEvGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMI-VTGGFNVF 427
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 48256734 570 PEKIENIYIRSEPVAQIYV-------HGDSLKAflvgIVVPDPEVMP 609
Cdd:PRK06188 428 PREVEDVLAEHPAVAQVAVigvpdekWGEAVTA----VVVLRPGAAV 470
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
241-604 |
5.76e-27 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 114.33 E-value: 5.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 241 CGVDIKS----MQAIEDSGQENHRVPvPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVL 316
Cdd:cd17653 75 VPLDAKLpsarIQAILRTSGATLLLT-TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLN----YVSQPPARLDVGPGSRV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 317 ISFLPLAhmFERVIQSV--VYCHGGRVgFFQGDIRLLSDDMKALrpTIFPVVPRLLNrMYDkifhqaDTSLKRwllefaa 394
Cdd:cd17653 150 AQVLSIA--FDACIGEIfsTLCNGGTL-VLADPSDPFAHVARTV--DALMSTPSILS-TLS------PQDFPN------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 395 krkqaevrsgiirnnsiwdelffnkiqaslgghVRMIVTGAAPASPTVLGflRAALGCQVYEGYGQTECTAGCTFT--TP 472
Cdd:cd17653 211 ---------------------------------LKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTelLP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 473 GDWTsgHVGAPLPCNHIKLVDAEELNywTSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLH------TGDIGKWL 545
Cdd:cd17653 256 GQPV--TIGKPIPNSTCYILDADLQP--VPEGVvGEICISGVQVARGYLGNPALTASKFVPDPFWPgsrmyrTGDYGRWT 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 48256734 546 PEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQ---IYVHGDSLKAFlvgiVVPD 604
Cdd:cd17653 332 EDGGLEFLGREDNQVKV-RGFRINLEEIEEVVLQSQPEVTqaaAIVVNGRLVAF----VTPE 388
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
162-574 |
6.88e-27 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 117.33 E-value: 6.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 162 IAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIVDKPhkailLLEHVERK----ETPGLKLVILMEPFDDALRER 237
Cdd:PRK08633 680 LANLALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVITSRK-----FLEKLKNKgfdlELPENVKVIYLEDLKAKISKV 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 238 GKKC-GVDIKSMQA--IEDSGQENhrvpvpPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgfLKVTEKVIFPRQDD 314
Cdd:PRK08633 755 DKLTaLLAARLLPArlLKRLYGPT------FKPDDTATIIFSSGSEGEPKGVMLSHHNILSN----IEQISDVFNLRNDD 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 315 VLISFLPLAHMFE-RVIQSVVYCHGGRVGFFqgdirllSDDMKAL---------RPTIFPVVPRLLnRMYdkifhqadts 384
Cdd:PRK08633 825 VILSSLPFFHSFGlTVTLWLPLLEGIKVVYH-------PDPTDALgiaklvakhRATILLGTPTFL-RLY---------- 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 385 lkrwllefaakrkqaevrsgiIRNNSIWDELFfnkiqASLgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECT 464
Cdd:PRK08633 887 ---------------------LRNKKLHPLMF-----ASL----RLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETS 936
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 465 AGCTFTTP-----GDWT-----SGHVGAPLPCNHIKLVDAEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEAL---D 531
Cdd:PRK08633 937 PVASVNLPdvlaaDFKRqtgskEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiD 1016
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 48256734 532 SDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIE 574
Cdd:PRK08633 1017 GIGWYVTGDKGHLDEDGFLTITDRYSRFAKIG-GEMVPLGAVE 1058
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
112-605 |
7.04e-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: 115.04 E-value: 7.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 112 RKPEQPYQWLSYQEVAKRAEFLGSGLlqHDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIIN 191
Cdd:cd12119 17 RTHEGEVHRYTYAEVAERARRLANAL--RRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 192 TADICTVIVDKPHKAIL-----LLEHVERketpglklVILMEPFDDALRERGKKCG-----VDIKSMQAIEDSGQENhrv 261
Cdd:cd12119 95 HAEDRVVFVDRDFLPLLeaiapRLPTVEH--------VVVMTDDAAMPEPAGVGVLayeelLAAESPEYDWPDFDEN--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 262 pvpprpdDLSIVCFTSGTTGNPKGAMLTHGNVV--------ADFSGFlkvtekvifpRQDDVLISFLPLAHM------FE 327
Cdd:cd12119 164 -------TAAAICYTSGTTGNPKGVVYSHRSLVlhamaallTDGLGL----------SESDVVLPVVPMFHVnawglpYA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 328 RVIQSVVYCHGGRvgFFQGDirLLSDDMKALRPTIFPVVPRLlnrmydkifhqadtslkrWLLefaakrkqaeVRSGIIR 407
Cdd:cd12119 227 AAMVGAKLVLPGP--YLDPA--SLAELIEREGVTFAAGVPTV------------------WQG----------LLDHLEA 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 408 NNSiwdELFfnkiqaslggHVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPgdwTSGHV------- 480
Cdd:cd12119 275 NGR---DLS----------SLRRVVIGGSAVPRSLIEAFEE-RGVRVIHAWGMTETSPLGTVARP---PSEHSnlsedeq 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 481 -------GAPLPCNHIKLVDAE--ELNyWTSKGEGEICVKGPNVFKGYLKDeDRTKEALDSDGWLHTGDIGKWLPEGTLK 551
Cdd:cd12119 338 lalrakqGRPVPGVELRIVDDDgrELP-WDGKAVGELQVRGPWVTKSYYKN-DEESEALTEDGWLRTGDVATIDEDGYLT 415
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 48256734 552 IIDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQIYVhgdslkaflvgIVVPDP 605
Cdd:cd12119 416 ITDRSKDVIKSG-GEWISSVELENAIMAHPAVAEAAV-----------IGVPHP 457
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
114-608 |
8.61e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 115.29 E-value: 8.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 114 PEQPYQWlSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVV---PLYDTlgpGSIRYII 190
Cdd:PRK08315 38 RDQGLRW-TYREFNEEVDALAKGLLALGIEKGDR--VGIWAPNVPEWVLTQFATAKIGAILVtinPAYRL---SELEYAL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 191 NTADICTVIVDKPHK-----AILL-----LEHVER-----KETPGLKLVIL--------MEPFDDaLRERGKkcGVDIKS 247
Cdd:PRK08315 112 NQSGCKALIAADGFKdsdyvAMLYelapeLATCEPgqlqsARLPELRRVIFlgdekhpgMLNFDE-LLALGR--AVDDAE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 248 MQAIEDSGQenhrvpvpprPDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsGFLkVTEKVIFPRQDDVLISfLPLAHMFE 327
Cdd:PRK08315 189 LAARQATLD----------PDDPINIQYTSGTTGFPKGATLTHRNILNN--GYF-IGEAMKLTEEDRLCIP-VPLYHCFG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 328 RVIqSVVYC--HGGRV-----GFfqgdirllsDDMKALR-------------PTIFPVVprlLNrmyDKIFHQAD-TSLk 386
Cdd:PRK08315 255 MVL-GNLACvtHGATMvypgeGF---------DPLATLAaveeerctalygvPTMFIAE---LD---HPDFARFDlSSL- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 387 rwllefaakrkqaevRSGIirnnsiwdelffnkiqaslgghvrMivtgAAPASPT-----VLGFLRAAlgcQVYEGYGQT 461
Cdd:PRK08315 318 ---------------RTGI------------------------M----AGSPCPIevmkrVIDKMHMS---EVTIAYGMT 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 462 ECTAGCTFTTPGD------WTsghVGAPLPCNHIKLVDAEelnywtsKGE-------GEICVKGPNVFKGYLKDEDRTKE 528
Cdd:PRK08315 352 ETSPVSTQTRTDDplekrvTT---VGRALPHLEVKIVDPE-------TGEtvprgeqGELCTRGYSVMKGYWNDPEKTAE 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 529 ALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIyirsepvaqIYVHGDSLKAFLVGivVPDP--- 605
Cdd:PRK08315 422 AIDADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEF---------LYTHPKIQDVQVVG--VPDEkyg 489
|
....
gi 48256734 606 -EVM 608
Cdd:PRK08315 490 eEVC 493
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
261-578 |
1.38e-26 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 114.55 E-value: 1.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 261 VPVPP-RPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKV-TEKVIFPRQDDVLISFLPLAHMFerviqsvvychg 338
Cdd:PLN02574 190 VPKPViKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFeASQYEYPGSDNVYLAALPMFHIY------------ 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 339 GRVGFFQGDIRL-----------LSDDMKAL---RPTIFPVVPRLLnrmydkifhqadTSLKRwllefAAKRKQAEVRsg 404
Cdd:PLN02574 258 GLSLFVVGLLSLgstivvmrrfdASDMVKVIdrfKVTHFPVVPPIL------------MALTK-----KAKGVCGEVL-- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 405 iirnnsiwdelffnkiqaslgGHVRMIVTGAAPAS-PTVLGFLRAALGCQVYEGYGQTECTAGCT--FTTPGDWTSGHVG 481
Cdd:PLN02574 319 ---------------------KSLKQVSCGAAPLSgKFIQDFVQTLPHVDFIQGYGMTESTAVGTrgFNTEKLSKYSSVG 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 482 APLPCNHIKLVDAEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFK 561
Cdd:PLN02574 378 LLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIK 457
|
330
....*....|....*..
gi 48256734 562 LaQGEYVAPEKIENIYI 578
Cdd:PLN02574 458 Y-KGFQIAPADLEAVLI 473
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
122-576 |
2.07e-26 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 114.07 E-value: 2.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 122 SYQEVAKRAEFLGSGLLQHDCKVGTeqfigVFAQNRPEW---IIAELACYTYSMVVVPLYDTLGPGSIRYIIN----TAD 194
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGD-----RVAFQLPGWcefTIIYLACLKVGAVSVPLLPSWREAELVWVLNkcqaKMF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 195 ICTVIVDK--PHKAILLLehveRKETPGLKLVILMEPFDDALRergkkcgvDIKSMQAIEDSGQENHrvPVPPRPDDLSI 272
Cdd:PRK06087 126 FAPTLFKQtrPVDLILPL----QNQLPQLQQIVGVDKLAPATS--------SLSLSQIIADYEPLTT--AITTHGDELAA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 273 VCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifprQDDVLISFLPLAHmferviqSVVYCHGGRVGFFQGDIRLLS 352
Cdd:PRK06087 192 VLFTSGTEGLPKGVMLTHNNILASERAYCARLNLT----WQDVFMMPAPLGH-------ATGFLHGVTAPFLIGARSVLL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 353 DDMKALRPTifpvvpRLLNRmydkifhQADTslkrWLL---EFaakrkqaevrsgiirnnsIWDELffNKIQASlGGHV- 428
Cdd:PRK06087 261 DIFTPDACL------ALLEQ-------QRCT----CMLgatPF------------------IYDLL--NLLEKQ-PADLs 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 429 --RMIVTGAAPASPTVLgflRAAL--GCQVYEGYGQTECTAGcTFTTPGD---WTSGHVGAPLPCNHIKLVDaEELNYWT 501
Cdd:PRK06087 303 alRFFLCGGTTIPKKVA---RECQqrGIKLLSVYGSTESSPH-AVVNLDDplsRFMHTDGYAAAGVEIKVVD-EARKTLP 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 48256734 502 SKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENI 576
Cdd:PRK06087 378 PGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDI 451
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
156-598 |
5.70e-26 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 111.27 E-value: 5.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 156 NRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIVDKphkailllehverketpglklvilmepfddalr 235
Cdd:cd05972 34 RVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA--------------------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 236 ergkkcgvdiksmqaiedsgqenhrvpvpprpDDLSIVCFTSGTTGNPKGAMLTHG---NVVADFSGFLKVTEKVIFPRQ 312
Cdd:cd05972 81 --------------------------------EDPALIYFTSGTTGLPKGVLHTHSyplGHIPTAAYWLGLRPDDIHWNI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 313 DD------VLISFL-PLAHMFerviqSVVYCHGGRvgffqgdirllsddMKALRptifpvVPRLLNRMYDKIFHQADTSL 385
Cdd:cd05972 129 ADpgwakgAWSSFFgPWLLGA-----TVFVYEGPR--------------FDAER------ILELLERYGVTSFCGPPTAY 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 386 KRWLLEFAAKRKQaevrsgiirnnsiwdelffnkiqaslgGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTA 465
Cdd:cd05972 184 RMLIKQDLSSYKF---------------------------SHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGL 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 466 GCTFTTPGDWTSGHVGAPLPCNHIKLVDAE--ELNYWTskgEGEICVKGPNV--FKGYLKDEDRTKEALdSDGWLHTGDI 541
Cdd:cd05972 237 TVGNFPDMPVKPGSMGRPTPGYDVAIIDDDgrELPPGE---EGDIAIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDR 312
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 48256734 542 GKWLPEGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSEPVAQIYV-------HGDSLKAFLV 598
Cdd:cd05972 313 AYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVESALLEHPAVAEAAVvgspdpvRGEVVKAFVV 375
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
259-609 |
9.91e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 111.23 E-value: 9.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 259 HRVPVPPrPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifprQDDVLISFLPLAHMferviqsvvycHG 338
Cdd:PRK07787 120 HRYPEPD-PDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWT----ADDVLVHGLPLFHV-----------HG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 339 GRVGFFqGDIRLLSDDMKALRPTIFPVVPRLLNR---------MYDKIfhQADTSLKRwllefaakrkqaevrsgiirnn 409
Cdd:PRK07787 184 LVLGVL-GPLRIGNRFVHTGRPTPEAYAQALSEGgtlyfgvptVWSRI--AADPEAAR---------------------- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 410 siwdelffnkiqaSLGGhVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHI 489
Cdd:PRK07787 239 -------------ALRG-ARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVET 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 490 KLVDaEELNYWTSKGE--GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDR------KKHIFK 561
Cdd:PRK07787 305 RLVD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGGYR 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 48256734 562 LAQGEyvapekIENIYIRSEPVAQIYVHG---DSLKAFLVGIVVPDPEVMP 609
Cdd:PRK07787 384 IGAGE------IETALLGHPGVREAAVVGvpdDDLGQRIVAYVVGADDVAA 428
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
120-557 |
1.16e-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: 111.95 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 120 WLSYQEVAKRAEFLGSGLLQHdCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGS---IRYIINTADIC 196
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAV-GKPGDR--VLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 197 TVIVDKPHKAiLLLEHVERKETPGLKLVILMEPFDDALRERGkkcgvdiksmqaiedsgqenhrVPVPPRPDDLSIVCFT 276
Cdd:cd05931 101 VVLTTAAALA-AVRAFAASRPAAGTPRLLVVDLLPDTSAADW----------------------PPPSPDPDDIAYLQYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 277 SGTTGNPKGAMLTHGNVVADFSGFLkvteKVIFPRQDDVLISFLPLAH---MFERVIQSVVYchGGRVGFFQgdirllsd 353
Cdd:cd05931 158 SGSTGTPKGVVVTHRNLLANVRQIR----RAYGLDPGDVVVSWLPLYHdmgLIGGLLTPLYS--GGPSVLMS-------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 354 dmkalrPTIFpvvprlLNRMYdkifhqadtslkRWL-----------------LEFAAKRKQAEVRSGIirnnsiwdELf 416
Cdd:cd05931 224 ------PAAF------LRRPL------------RWLrlisryratisaapnfaYDLCVRRVRDEDLEGL--------DL- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 417 fnkiqaslgGHVRMIVTGAAPASPTVL----------GFLRAAlgcqVYEGYGQTECTAGCTFTTPG----------DWT 476
Cdd:cd05931 271 ---------SSWRVALNGAEPVRPATLrrfaeafapfGFRPEA----FRPSYGLAEATLFVSGGPPGtgpvvlrvdrDAL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 477 SGHV----------------GAPLPCNHIKLVDAEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKE------ALDSDG 534
Cdd:cd05931 338 AGRAvavaaddpaarelvscGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaATDEGG 417
|
490 500
....*....|....*....|...
gi 48256734 535 WLHTGDIGkWLPEGTLKIIDRKK 557
Cdd:cd05931 418 WLRTGDLG-FLHDGELYITGRLK 439
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
112-569 |
1.86e-25 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 111.51 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 112 RKPEQPYQWLSYQEVAKRAEFLGSGLLqhDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPL---YDTLG--PGSI 186
Cdd:PRK08180 61 RGADGGWRRLTYAEALERVRAIAQALL--DRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVspaYSLVSqdFGKL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 187 RYIINtadictvivdkphkailLLehverkeTPGLKLVILMEPFDDALRE-----------RGKKCGVDIKSMQAIEDSg 255
Cdd:PRK08180 139 RHVLE-----------------LL-------TPGLVFADDGAAFARALAAvvpadvevvavRGAVPGRAATPFAALLAT- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 256 qenhrvPVPP---------RPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekVIFPRQDD-VLISFLPLAHM 325
Cdd:PRK08180 194 ------PPTAavdaahaavGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQT---FPFLAEEPpVLVDWLPWNHT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 326 F-ERVIQSVVYCHGGR---------VGFFQGDIRLLsddmKALRPTIFPVVPRLlnrmydkifhqadtslkrWLLEFAAK 395
Cdd:PRK08180 265 FgGNHNLGIVLYNGGTlyiddgkptPGGFDETLRNL----REISPTVYFNVPKG------------------WEMLVPAL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 396 RKQAEVRsgiirnnsiwdELFFNKiqaslgghVRMIVTGAAPASPTVLGFL----RAALGCQVY--EGYGQTECTAGCTF 469
Cdd:PRK08180 323 ERDAALR-----------RRFFSR--------LKLLFYAGAALSQDVWDRLdrvaEATCGERIRmmTGLGMTETAPSATF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 470 TTPGDWTSGHVGAPLPCNHIKLVDAEelnywtskGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWL---- 545
Cdd:PRK08180 384 TTGPLSRAGNIGLPAPGCEVKLVPVG--------GKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVdpad 455
|
490 500
....*....|....*....|....
gi 48256734 546 PEGTLKIIDRKKHIFKLAQGEYVA 569
Cdd:PRK08180 456 PERGLMFDGRIAEDFKLSSGTWVS 479
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
111-588 |
2.60e-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: 2.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 111 FRKPEQPY-----QWLSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLydtlGPGS 185
Cdd:cd17655 8 EKTPDHTAvvfedQTLTYRELNERANQLARTLREKG--VGPDTIVGIMAERSLEMIVGILGILKAGGAYLPI----DPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 186 ----IRYIINTADIctvivdkphkAILLLEHVERKETPGLKLVILMEpfDDALRERGKkcgvdiksmqaiedsgqENhrV 261
Cdd:cd17655 82 peerIQYILEDSGA----------DILLTQSHLQPPIAFIGLIDLLD--EDTIYHEES-----------------EN--L 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 262 PVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkvtEKVIFPRQDDVLISFLPLAhmFERVIQSvvychggrv 341
Cdd:cd17655 131 EPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWA----NKVIYQGEHLRVALFASIS--FDASVTE--------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 342 gffqgdirllsddmkalrptIFPvvPRLL-NRMYdkIFHQADTSLKRWLLEFAAKRkqaevRSGIIR-NNSIWDELffNK 419
Cdd:cd17655 196 --------------------IFA--SLLSgNTLY--IVRKETVLDGQALTQYIRQN-----RITIIDlTPAHLKLL--DA 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 420 IQASLGGHVRMIVTGAAPASPTVLGFL--RAALGCQVYEGYGQTECTAGCTF--TTPGDWTSGHV--GAPLPCNHIKLVD 493
Cdd:cd17655 245 ADDSEGLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETTVDASIyqYEPETDQQVSVpiGKPLGNTRIYILD 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 494 AEElnYWTSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWL------HTGDIGKWLPEGTLKIIDRKKHIFKLaQGE 566
Cdd:cd17655 325 QYG--RPQPVGVaGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-RGY 401
|
490 500
....*....|....*....|..
gi 48256734 567 YVAPEKIENIYIRSEPVAQIYV 588
Cdd:cd17655 402 RIELGEIEARLLQHPDIKEAVV 423
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
220-574 |
4.63e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 106.62 E-value: 4.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 220 GLKLVILMEPFDDA---LRERGKKcgvdiksMQAIEDSGQENHRVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD 296
Cdd:PRK07768 108 GAKAVVVGEPFLAAapvLEEKGIR-------VLTVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYAN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 297 FSGflkVTEKVIFPRQDDVLISFLPLAH-MferviqsvvychgGRVGFfqgdirlLSDDMKA------LRPTIFPVVPRL 369
Cdd:PRK07768 181 AEA---MFVAAEFDVETDVMVSWLPLFHdM-------------GMVGF-------LTVPMYFgaelvkVTPMDFLRDPLL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 370 LNRMYDKifHQADT--------SLKRWLLEFAAKRKQAEVRSgiirnnsiwdelffnkiqaslgghVRMIVTGAAPASPT 441
Cdd:PRK07768 238 WAELISK--YRGTMtaapnfayALLARRLRRQAKPGAFDLSS------------------------LRFALNGAEPIDPA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 442 VL----------GFLRAALGCqvyeGYGQTECTAGCTFTTPGD--------------------WTSGHV------GAPLP 485
Cdd:PRK07768 292 DVedlldagarfGLRPEAILP----AYGMAEATLAVSFSPCGAglvvdevdadllaalrravpATKGNTrrlatlGPPLP 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 486 CNHIKLVDaEELNYWTSKGEGEICVKGPNVFKGYLkDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqG 565
Cdd:PRK07768 368 GLEVRVVD-EDGQVLPPRGVGVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-G 444
|
....*....
gi 48256734 566 EYVAPEKIE 574
Cdd:PRK07768 445 RNIYPTDIE 453
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
112-606 |
5.06e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 106.66 E-value: 5.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 112 RKPEQP----Y-QWLSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSI 186
Cdd:PRK06178 45 ERPQRPaiifYgHVITYAELDELSDRFAALLRQRG--VGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 187 RYIINTADICTVIV-D------KPHKAILLLEHVErkeTPGLKLVILMEP---FDDALRERGKKCGVDIKSMQAIEDSGQ 256
Cdd:PRK06178 123 SYELNDAGAEVLLAlDqlapvvEQVRAETSLRHVI---VTSLADVLPAEPtlpLPDSLRAPRLAAAGAIDLLPALRACTA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 257 enhRVPVP-PRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifpRQDDVLISFLPlahMFerviqsvvy 335
Cdd:PRK06178 200 ---PVPLPpPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVG---GEDSVFLSFLP---EF--------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 336 chggrvgFFQGDirllsdDMKALRPTIF--PVVprLLNRmYDkifhqADTSLKrwllefAAKRKQAEVRSGIIRNnsiWD 413
Cdd:PRK06178 262 -------WIAGE------NFGLLFPLFSgaTLV--LLAR-WD-----AVAFMA------AVERYRVTRTVMLVDN---AV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 414 ELF----FNKIQASLGGHVRmIVTGAAPASPTVLGFLRAALGCQVYEG-YGQTECTAGCTFTTpGDWTSGH--------V 480
Cdd:PRK06178 312 ELMdhprFAEYDLSSLRQVR-VVSFVKKLNPDYRQRWRALTGSVLAEAaWGMTETHTCDTFTA-GFQDDDFdllsqpvfV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 481 GAPLPCNHIKLVDAEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIF 560
Cdd:PRK06178 390 GLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEML 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 48256734 561 KLaQGEYVAPEKIENIYIRsepvaqiyvHGDSLKAFLVGivVPDPE 606
Cdd:PRK06178 469 KV-NGMSVFPSEVEALLGQ---------HPAVLGSAVVG--RPDPD 502
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
107-693 |
1.02e-23 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 105.98 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 107 PCLGFRKPEQPYQWLSYQEVAKRAEFLGSGLLQHDCKVgtEQFIGVFAQNRPEWIIAELACYTysmVVVPLydtlGPGSI 186
Cdd:cd05921 12 TWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGLSA--ERPLLILSGNSIEHALMALAAMY---AGVPA----APVSP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 187 RYIINTADIctvivDKphkaillLEHVERKETPGLKLVILMEPFDDALRE-----------RGKKCGVDIKSM------Q 249
Cdd:cd05921 83 AYSLMSQDL-----AK-------LKHLFELLKPGLVFAQDAAPFARALAAifplgtplvvsRNAVAGRGAISFaelaatP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 250 AIEDSGQENHRVpvppRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekviFPRQDD---VLISFLPLAHMF 326
Cdd:cd05921 151 PTAAVDAAFAAV----GPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQT-----YPFFGEeppVLVDWLPWNHTF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 327 --ERVIQSVVYcHGGRV---------GFFQGDIRLLSDDMkalrPTIFPVVPR----LLNRMYDkifhqaDTSLKRwllE 391
Cdd:cd05921 222 ggNHNFNLVLY-NGGTLyiddgkpmpGGFEETLRNLREIS----PTVYFNVPAgwemLVAALEK------DEALRR---R 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 392 FAAKRKQAEVrSGIIRNNSIWDELFFNKIQaSLGGHVRMivtgaapasptvlgflraalgcqvYEGYGQTECTAGCTFTT 471
Cdd:cd05921 288 FFKRLKLMFY-AGAGLSQDVWDRLQALAVA-TVGERIPM------------------------MAGLGATETAPTATFTH 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 472 PGDWTSGHVGAPLPCNHIKLVdaeelnywTSKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWL----PE 547
Cdd:cd05921 342 WPTERSGLIGLPAPGTELKLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpddPA 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 548 GTLKIIDRKKHIFKLAQGEYVA--PekieniyIRSEPVAQI--YVHgDSL-----KAFLVGIVVPDPevMPCWAQKKGIE 618
Cdd:cd05921 414 KGLVFDGRVAEDFKLASGTWVSvgP-------LRARAVAACapLVH-DAVvagedRAEVGALVFPDL--LACRRLVGLQE 483
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 48256734 619 GNYQELCKSKELKKAILDDMVMLGKESGlHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 693
Cdd:cd05921 484 ASDAEVLRHAKVRAAFRDRLAALNGEAT-GSSSRIARALLLDEPPSIDKGEITDKGYINQRAVLERRAALVERLY 557
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
269-685 |
1.23e-23 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 102.41 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 269 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkVTEKVIFPRQDDVLISfLPLAHM--FERVIQSVVycHGGRVGFFQG 346
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAG---LHSRLGFGGGDSWLLS-LPLYHVggLAILVRSLL--AGAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 347 DiRLLSDDMKALRPTIFPVVPRLLNRMYDKifHQADTSLKRwllefaakrkqaevrsgiirnnsiwdelffnkiqaslgg 426
Cdd:cd17630 75 N-QALAEDLAPPGVTHVSLVPTQLQRLLDS--GQGPAALKS--------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 427 hVRMIVTGAAPASPtvlGFLRAA--LGCQVYEGYGQTEcTAGCTFT-TPGDWTSGHVGAPLPCNHIKLVDaeelnywtsk 503
Cdd:cd17630 113 -LRAVLLGGAPIPP---ELLERAadRGIPLYTTYGMTE-TASQVATkRPDGFGRGGVGVLLPGRELRIVE---------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 504 gEGEICVKGPNVFKGYLKDedRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIEniyirsepv 583
Cdd:cd17630 178 -DGEIWVGGASLAMGYLRG--QLVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIE--------- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 584 AQIYVHGDSLKAFLVGivVPDPEvmpcWAQK---------KGIEGNYQELCKSKelkkailddmvmlgkesgLHSFEQVK 654
Cdd:cd17630 245 AALAAHPAVRDAFVVG--VPDEE----LGQRpvavivgrgPADPAELRAWLKDK------------------LARFKLPK 300
|
410 420 430
....*....|....*....|....*....|.
gi 48256734 655 AIYIhcdmfsVQNGLLTPTLKAKRPELREYF 685
Cdd:cd17630 301 RIYP------VPELPRTGGGKVDRRALRAWL 325
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
269-606 |
1.61e-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: 102.35 E-value: 1.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 269 DLSIVCFTSGTTGNPKGAMLTHGNVVA---DFSGFLKVTEkvifprqDDVLISFLPLAHMFERVIQSVVYCHGGR-VGFF 344
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAanlQLIHAMGLTE-------ADVYLNMLPLFHIAGLNLALATFHAGGAnVVME 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 345 QGDIRLLSDDMKALRPTIFPVVPRLLNRMYDkifhqadtslkrwllefAAKRKQAEVRSgiIRNnsiwdelffnkiqasl 424
Cdd:cd17637 74 KFDPAEALELIEEEKVTLMGSFPPILSNLLD-----------------AAEKSGVDLSS--LRH---------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 425 gghvrmiVTGAApaSPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDaeELNYWTSKG 504
Cdd:cd17637 119 -------VLGLD--APETIQRFEETTGATFWSLYGQTE-TSGLVTLSPYRERPGSAGRPGPLVRVRIVD--DNDRPVPAG 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 505 E-GEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRK--KHIFKlAQGEYVAPEKIENIYIRSE 581
Cdd:cd17637 187 EtGEIVVRGPLVFQGYWNLPELTAYTFR-NGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKVILEHP 264
|
330 340
....*....|....*....|....*
gi 48256734 582 PVAQIYVHGdslkaflvgivVPDPE 606
Cdd:cd17637 265 AIAEVCVIG-----------VPDPK 278
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
256-598 |
2.37e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 104.73 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 256 QENHRVPVPPRPD-DLSIVCFTSGTTGNPKGAMLTHGNVVADfsGFLKVTEKVIFPRQDDVLISFLPLAHMF-ERVIQSV 333
Cdd:PRK06710 193 EVNTGVEVPCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSN--TLMGVQWLYNCKEGEEVVLGVLPFFHVYgMTAVMNL 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 334 VYCHGGRVGFF-QGDIRLLSDDMKALRPTIFPVVPRLLNRMydkifhqadtsLKRWLLefaakrKQAEVRSgiirnnsiw 412
Cdd:PRK06710 271 SIMQGYKMVLIpKFDMKMVFEAIKKHKVTLFPGAPTIYIAL-----------LNSPLL------KEYDISS--------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 413 delffnkiqaslgghVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgctfTTPGDW-----TSGHVGAPLPCN 487
Cdd:PRK06710 325 ---------------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSP----VTHSNFlwekrVPGSIGVPWPDT 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 488 HIKLVDAEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEY 567
Cdd:PRK06710 386 EAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFN 463
|
330 340 350
....*....|....*....|....*....|....*...
gi 48256734 568 VAPEKIENIYIRSEPVAQIYV-------HGDSLKAFLV 598
Cdd:PRK06710 464 VYPREVEEVLYEHEKVQEVVTigvpdpyRGETVKAFVV 501
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
111-590 |
3.11e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 104.09 E-value: 3.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 111 FRKPEQPY-----QWLSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGS 185
Cdd:PRK07786 28 LMQPDAPAlrflgNTTTWRELDDRVAALAGALSRRG--VGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 186 IRYIINTADiCTVIVDKPHKAILLLEhvERKETPGLKLVILMEP--------FDDALRERGKKCG-VDIksmqaiedsgq 256
Cdd:PRK07786 106 IAFLVSDCG-AHVVVTEAALAPVATA--VRDIVPLLSTVVVAGGssddsvlgYEDLLAEAGPAHApVDI----------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 257 enhrvpvpprPDDL-SIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkviFPRQDDVLISFLPLAHMfeRVIQSVVy 335
Cdd:PRK07786 172 ----------PNDSpALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNG---ADINSDVGFVGVPLFHI--AGIGSML- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 336 chggrVGFFQGdirllsddmkalRPT-IFPVVPRLLNRMYDKIFHQADTSL----KRWLLEFAAKRKQAevrsgiiRNNS 410
Cdd:PRK07786 236 -----PGLLLG------------APTvIYPLGAFDPGQLLDVLEAEKVTGIflvpAQWQAVCAEQQARP-------RDLA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 411 IwdelffnkiqaslgghvRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAgCTFTTPGD---WTSGHVGAPLPC 486
Cdd:PRK07786 292 L-----------------RVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEMSP-VTCMLLGEdaiRKLGSVGKVIPT 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 487 NHIKLVDaEELNYwTSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSdGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQG 565
Cdd:PRK07786 354 VAARVVD-ENMND-VPVGEvGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGG 429
|
490 500
....*....|....*....|....*
gi 48256734 566 EYVAPEKIENIYIRSEPVAQIYVHG 590
Cdd:PRK07786 430 ENIYCAEVENVLASHPDIVEVAVIG 454
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
121-605 |
3.93e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 103.86 E-value: 3.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:PRK08316 37 WTYAELDAAVNRVAAALLDLGLKKGDR--VAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 201 DKPhkailLLEHVERketpglklVILMEPFDDALRERGKKCGVDIKSMQAIED--SGQENHRVPVPPRPDDLSIVCFTSG 278
Cdd:PRK08316 115 DPA-----LAPTAEA--------ALALLPVDTLILSLVLGGREAPGGWLDFADwaEAGSVAEPDVELADDDLAQILYTSG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 279 TTGNPKGAMLTHGNVVADFSGFLKVTEKvifpRQDDVLISFLPLAHMFER--VIQSVVYCHGGRVGFFQGDIRLLSDDMK 356
Cdd:PRK08316 182 TESLPKGAMLTHRALIAEYVSCIVAGDM----SADDIPLHALPLYHCAQLdvFLGPYLYVGATNVILDAPDPELILRTIE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 357 ALRPTIF---PVVPRLLNRMYDkiFHQADTSlkrwllefaakrkqaevrsgiirnnsiwdelffnkiqaSLgghvRMIVT 433
Cdd:PRK08316 258 AERITSFfapPTVWISLLRHPD--FDTRDLS--------------------------------------SL----RKGYY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 434 GAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFTTPGDwtsgHVGAP----LPCNHI--KLVDA--EELnywtSKG 504
Cdd:PRK08316 294 GASIMPVEVLKELRERLpGLRFYNCYGQTEIAPLATVLGPEE----HLRRPgsagRPVLNVetRVVDDdgNDV----APG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 505 E-GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIyirsepv 583
Cdd:PRK08316 366 EvGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEA------- 436
|
490 500
....*....|....*....|..
gi 48256734 584 aqIYVHGDSLKAFLVGivVPDP 605
Cdd:PRK08316 437 --LYTHPAVAEVAVIG--LPDP 454
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
121-605 |
4.08e-23 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 103.98 E-value: 4.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSGLLqhdcKVGTEQFIGVFAQ--NRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTV 198
Cdd:PRK13295 56 FTYRELAALVDRVAVGLA----RLGVGRGDVVSCQlpNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 199 IVDK-----PHKAIL--LlehveRKETPGLKLVILM-----EPFDDALRERGKKCGVDIksmQAIEDSgqenHRvpvpPR 266
Cdd:PRK13295 132 VVPKtfrgfDHAAMArrL-----RPELPALRHVVVVggdgaDSFEALLITPAWEQEPDA---PAILAR----LR----PG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVvadFSGFLKVTEKVIFpRQDDVLISFLPLAHMferviqsvvychggrVGFFQG 346
Cdd:PRK13295 196 PDDVTQLIYTSGTTGEPKGVMHTANTL---MANIVPYAERLGL-GADDVILMASPMAHQ---------------TGFMYG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 347 DIRLLSDDMKALRPTIFPVVprllnRMYDKI------FHQADTSlkrWLLEFAakRKQAEVRSGIirnnsiwdelffnki 420
Cdd:PRK13295 257 LMMPVMLGATAVLQDIWDPA-----RAAELIrtegvtFTMASTP---FLTDLT--RAVKESGRPV--------------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 421 qASLgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPGD---WTSGHVGAPLPCNHIKLVDAE-- 495
Cdd:PRK13295 312 -SSL----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA-VTLTKLDDpdeRASTTDGCPLPGVEVRVVDADga 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 496 ELnywtSKGE-GEICVKGPNVFKGYLKDEDRTkeALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIE 574
Cdd:PRK13295 386 PL----PAGQiGRLQVRGCSNFGGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIE 458
|
490 500 510
....*....|....*....|....*....|..
gi 48256734 575 NIYIRSEPVAQiyvhgdslkaflVGIV-VPDP 605
Cdd:PRK13295 459 ALLYRHPAIAQ------------VAIVaYPDE 478
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-584 |
4.30e-23 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 101.40 E-value: 4.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgfLKVTEKVIFPRQDDVLISFLPLAHMFERVIQsvvychgGRVGFFQG 346
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYN----AWMLALNSLFDPDDVLLCGLPLFHVNGSVVT-------LLTPLASG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 347 DIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTSLkrwllefaAKRKQAEVRSGIirnnsiwdelffnkiqaslgG 426
Cdd:cd05944 70 AHVVLAGPAGYRNPGLFDNFWKLVERYRITSLSTVPTVY--------AALLQVPVNADI--------------------S 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 427 HVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLV--DAEELNYWTSK 503
Cdd:cd05944 122 SLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKvlDGVGRLLRDCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 504 GE--GEICVKGPNVFKGYLKDEDRtKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSE 581
Cdd:cd05944 202 PDevGEICVAGPGVFGGYLYTEGN-KNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLRHP 279
|
...
gi 48256734 582 PVA 584
Cdd:cd05944 280 AVA 282
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
121-576 |
1.18e-22 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 103.89 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGsGLLQHDCKVGteQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:PRK06814 659 LTYRKLLTGAFVLG-RKLKKNTPPG--ENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 201 DKP--HKA--------------ILLLEHVERKETPGLKLVILMEPFddalRERGKKCGVDiksmqaiedsgqenhrvpvp 264
Cdd:PRK06814 736 SRAfiEKArlgpliealefgirIIYLEDVRAQIGLADKIKGLLAGR----FPLVYFCNRD-------------------- 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 265 prPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSgflKVTEKVIFPRQDDVLiSFLPLAHMFerviqsvvychggrvGFF 344
Cdd:PRK06814 792 --PDDPAVILFTSGSEGTPKGVVLSHRNLLANRA---QVAARIDFSPEDKVF-NALPVFHSF---------------GLT 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 345 QGDIRLLSDDMKAL---RPTIFPVVPRLLnrmYD---KIFHQADTSLkrwllefaakrkqaevrSGIIRNNSIWDelFFN 418
Cdd:PRK06814 851 GGLVLPLLSGVKVFlypSPLHYRIIPELI---YDtnaTILFGTDTFL-----------------NGYARYAHPYD--FRS 908
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 419 kiqaslgghVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELN 498
Cdd:PRK06814 909 ---------LRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGID 979
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 48256734 499 ywtsKGeGEICVKGPNVFKGYLKDED-RTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENI 576
Cdd:PRK06814 980 ----EG-GRLFVRGPNVMLGYLRAENpGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAVEEL 1051
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
266-606 |
1.99e-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: 101.08 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 266 RPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkviFPRQDDVL----ISF-LPLAHMFerviqsVVYCHGG- 339
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALG---LTSESRVLqfasYTFdVSILEIF------TTLAAGGc 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 340 --------RVGFFQGDIRllsdDMKA----LRPTifpvVPRLLNRmydkifhqadtslkrwllefaakrkqAEVRSgiir 407
Cdd:cd05918 175 lcipseedRLNDLAGFIN----RLRVtwafLTPS----VARLLDP--------------------------EDVPS---- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 408 nnsiwdelffnkiqaslgghVRMIVTGAAPASPTVLGflRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPC 486
Cdd:cd05918 217 --------------------LRTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRPLGA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 487 --------NHIKLVdaeelnywtSKGE-GEICVKGPNVFKGYLKDEDRTKEA-LDSDGWLH------------TGDIGKW 544
Cdd:cd05918 275 tcwvvdpdNHDRLV---------PIGAvGELLIEGPILARGYLNDPEKTAAAfIEDPAWLKqegsgrgrrlyrTGDLVRY 345
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 48256734 545 LPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEP-----VAQIYVH-GDSLKAFLVGIVVPDPE 606
Cdd:cd05918 346 NPDGSLEYVGRKDTQVKI-RGQRVELGEIEHHLRQSLPgakevVVEVVKPkDGSSSPQLVAFVVLDGS 412
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
156-598 |
6.21e-22 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 100.14 E-value: 6.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 156 NRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIVDKphKAILLLEHVERKETPGLKLVILMEPFDDALR 235
Cdd:PRK08008 71 NCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSA--QFYPMYRQIQQEDATPLRHICLTRVALPADD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 236 ERgkkcgVDIKSMQAiEDSGQENHRVPVppRPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVTEKVIfpRQDDV 315
Cdd:PRK08008 149 GV-----SSFTQLKA-QQPATLCYAPPL--STDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYYSAWQCAL--RDDDV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 316 LISFLPLAHMFerviqsvvychggrvgfFQgdirlLSDDMKAlrptiFPVVPRLLnrmydkifhqadtslkrwLLE-FAA 394
Cdd:PRK08008 217 YLTVMPAFHID-----------------CQ-----CTAAMAA-----FSAGATFV------------------LLEkYSA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 395 KRKQAEVRsgiirnnsiwdelffnKIQASLGGHVRMIVTG--AAPASPT--------VLGFLRAA----------LGCQV 454
Cdd:PRK08008 252 RAFWGQVC----------------KYRATITECIPMMIRTlmVQPPSANdrqhclreVMFYLNLSdqekdafeerFGVRL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 455 YEGYGQTECTAGCTFTTPGD---WTSghVGAPLPCNHIKLVDAEelNYWTSKGE-GEICVKG---PNVFKGYLKDEDRTK 527
Cdd:PRK08008 316 LTSYGMTETIVGIIGDRPGDkrrWPS--IGRPGFCYEAEIRDDH--NRPLPAGEiGEICIKGvpgKTIFKEYYLDPKATA 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 48256734 528 EALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIyIRSEP-VAQIYVHG--DSL-----KAFLV 598
Cdd:PRK08008 392 KVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVELENI-IATHPkIQDIVVVGikDSIrdeaiKAFVV 468
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
112-605 |
9.00e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 99.19 E-value: 9.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 112 RKPEQPY-----QWLSYQEVAKRAEfLGSGLLqHDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSI 186
Cdd:PRK06145 14 RTPDRAAlvyrdQEISYAEFHQRIL-QAAGML-HARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 187 RYIINTADICTVIVDKPHKAILLLEHverketpglklvilmepfddalrergKKCGVDIKSMQAIEDSGQENHRVP--VP 264
Cdd:PRK06145 92 AYILGDAGAKLLLVDEEFDAIVALET--------------------------PKIVIDAAAQADSRRLAQGGLEIPpqAA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 265 PRPDDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTekvifprQDDVLISFLPLAHMFERVIQSV-VYCHGGR 340
Cdd:PRK06145 146 VAPTDLVRLMYTSGTTDRPKGVMHSYGNLHwksIDHVIALGLT-------ASERLLVVGPLYHVGAFDLPGIaVLWVGGT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 341 VGF---FQGDIRLLSDDMKALRPTIFpvVPRLLNRMY---DKifHQADTSLKRWLLefAAKRKQAEVRsgiIRNnsiwde 414
Cdd:PRK06145 219 LRIhreFDPEAVLAAIERHRLTCAWM--APVMLSRVLtvpDR--DRFDLDSLAWCI--GGGEKTPESR---IRD------ 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 415 lffnkiqaslgghvrmivtgaapasptvlgFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPcnHIKLV 492
Cdd:PRK06145 284 ------------------------------FTRVFTRARYIDAYGLTETCSGDTLMEAGREIEkiGSTGRALA--HVEIR 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 493 DAEELNYWTSKG-EGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPE 571
Cdd:PRK06145 332 IADGAGRWLPPNmKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASS 409
|
490 500 510
....*....|....*....|....*....|....*..
gi 48256734 572 KIEN-IYIRSE--PVAQIYVHGDSLKAFLVGIVVPDP 605
Cdd:PRK06145 410 EVERvIYELPEvaEAAVIGVHDDRWGERITAVVVLNP 446
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
121-613 |
1.61e-21 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 98.81 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSGLLQHDCKVGteQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGLLPG--DRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 201 DKphkailllehverkETPGLKLVILMEPFDDALRERGKKCGVDIKSMQAIEDSGQENHRVPVPP--RPDDLSIVcFTSG 278
Cdd:PRK05852 122 DA--------------DGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTPATSTPEglRPDDAMIM-FTGG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 279 TTGNPKGAMLTHGNVVADFSGFlkVTEKVIFPRqdDVLISFLPLAH---MFERVIQSVVycHGGRV-----GFFQGdiRL 350
Cdd:PRK05852 187 TTGLPKMVPWTHANIASSVRAI--ITGYRLSPR--DATVAVMPLYHghgLIAALLATLA--SGGAVllparGRFSA--HT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 351 LSDDMKALRPTIFPVVPRLlnrmydkifHQAdtslkrwLLEFAAKRKQAEVRSGIirnnsiwdelffnkiqaslgghvRM 430
Cdd:PRK05852 259 FWDDIKAVGATWYTAVPTI---------HQI-------LLERAATEPSGRKPAAL-----------------------RF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 431 IVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTfTTPGDWtSGHVGAPLPCN---------HIKLV--DAEELny 499
Cdd:PRK05852 300 IRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVT-TTQIEG-IGQTENPVVSTglvgrstgaQIRIVgsDGLPL-- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 500 wTSKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIR 579
Cdd:PRK05852 376 -PAGAVGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLAS 452
|
490 500 510
....*....|....*....|....*....|....*.
gi 48256734 580 SEPVAQIYVHG--DSLKAFLVGIVVPDPEVMPCWAQ 613
Cdd:PRK05852 453 HPNVMEAAVFGvpDQLYGEAVAAVIVPRESAPPTAE 488
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
121-607 |
3.36e-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: 96.93 E-value: 3.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSGLlqHDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:cd05945 17 LTYRELKERADALAAAL--ASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPALLIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 201 DkphkailllehverketpglklvilmepfddalrergkkcgvdiksmqaiedsgqenhrvpvpprPDDLSIVCFTSGTT 280
Cdd:cd05945 95 D-----------------------------------------------------------------GDDNAYIIFTSGST 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 281 GNPKGAMLTHGNVVAdFS----GFLKVTEkvifprqDDVLISFLPLAhmFERVIQSVVYC--HGGrvgffqgdirllsdd 354
Cdd:cd05945 110 GRPKGVQISHDNLVS-FTnwmlSDFPLGP-------GDVFLNQAPFS--FDLSVMDLYPAlaSGA--------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 355 mkalrpTIFPVvPRLLNRMYdkifhqadtslkRWLLEFAAKRKQAEVRSgiirNNSIWDELF----FNkiQASLGGHVRM 430
Cdd:cd05945 165 ------TLVPV-PRDATADP------------KQLFRFLAEHGITVWVS----TPSFAAMCLlsptFT--PESLPSLRHF 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 431 IVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFT--TP---GDWTSGHVGAPLPCNHIKLVDAEELNywTSKGE 505
Cdd:cd05945 220 LFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIevTPevlDGYDRLPIGYAKPGAKLVILDEDGRP--VPPGE 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 506 -GEICVKGPNVFKGYLKDEDRTKEALDSD---GWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSE 581
Cdd:cd05945 298 kGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIELEEIEAALRQVP 376
|
490 500 510
....*....|....*....|....*....|
gi 48256734 582 PVAQIYV----HGDSlKAFLVGIVVPDPEV 607
Cdd:cd05945 377 GVKEAVVvpkyKGEK-VTELIAFVVPKPGA 405
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
121-609 |
7.81e-21 |
|
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: 96.19 E-value: 7.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSGLlqHDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:cd12114 13 LTYGELAERARRVAGAL--KAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 201 DKPHkailLLEHVERketpglklvilmepfDDALRERGkkcgvdiksmQAIEDSGQEnhrVPVPPRPDDLSIVCFTSGTT 280
Cdd:cd12114 91 DGPD----AQLDVAV---------------FDVLILDL----------DALAAPAPP---PPVDVAPDDLAYVIFTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 281 GNPKGAMLTHG---NVVADFSGFLKVTEkvifprqDDVLISFLPLAHMFerviqSV-----VYCHGGRVgffqgdirlls 352
Cdd:cd12114 139 GTPKGVMISHRaalNTILDINRRFAVGP-------DDRVLALSSLSFDL-----SVydifgALSAGATL----------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 353 ddmkalrptifpVVPRllnrmydkifHQADTSLKRWllefaakrKQAEVRSGIirnnSIWdelffNKIQASLGghvrMIV 432
Cdd:cd12114 196 ------------VLPD----------EARRRDPAHW--------AELIERHGV----TLW-----NSVPALLE----MLL 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 433 TgAAPASPTVLGFLRAAL-------------------GCQVYEGYGQTECTAGCTF----TTPGDWTSGHVGAPLPCNHI 489
Cdd:cd12114 233 D-VLEAAQALLPSLRLVLlsgdwipldlparlralapDARLISLGGATEASIWSIYhpidEVPPDWRSIPYGRPLANQRY 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 490 KLVDA--EELNYWTskgEGEICVKGPNVFKGYLKDEDRTKEAL--DSDG--WLHTGDIGKWLPEGTLKIIDRKKHIFKLa 563
Cdd:cd12114 312 RVLDPrgRDCPDWV---PGELWIGGRGVALGYLGDPELTAARFvtHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKV- 387
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 48256734 564 QGEYVAPEKIENIYIRSEPVAQ--IYVHGDSLKAFLVGIVVPDPEVMP 609
Cdd:cd12114 388 RGYRIELGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPDNDGTP 435
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
121-607 |
9.01e-21 |
|
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: 96.12 E-value: 9.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELA------CYtysmvvVPLYDTLGPGSIRYIINTAD 194
Cdd:cd12117 23 LTYAELNERANRLARRLRAAG--VGPGDVVGVLAERSPELVVALLAvlkagaAY------VPLDPELPAERLAFMLADAG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 195 ICTVIVDKPhkailllehverketpglklvilmepfddaLRERGKKCGVDIKSMQAIEDSGQENhrVPVPPRPDDLSIVC 274
Cdd:cd12117 95 AKVLLTDRS------------------------------LAGRAGGLEVAVVIDEALDAGPAGN--PAVPVSPDDLAYVM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 275 FTSGTTGNPKGAMLTHGNV---VADfSGFLKVTEkvifprqDDVLISFLPL---AHMFErviqsvVY---CHGGRVgffq 345
Cdd:cd12117 143 YTSGSTGRPKGVAVTHRGVvrlVKN-TNYVTLGP-------DDRVLQTSPLafdASTFE------IWgalLNGARL---- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 346 gdiRLLSDDmkalrptifpvVPRLLNRMYDKIFHQADTSLkrWLLefAAkrkqaevrsgiirnnsiwdelFFNKI----Q 421
Cdd:cd12117 205 ---VLAPKG-----------TLLDPDALGALIAEEGVTVL--WLT--AA---------------------LFNQLadedP 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 422 ASLGGhVRMIVTGAAPASPT-VLGFLRAALGCQVYEGYGQTECTagcTFTT-----PGDWTSGHV--GAPLPCNHIKLVD 493
Cdd:cd12117 246 ECFAG-LRELLTGGEVVSPPhVRRVLAACPGLRLVNGYGPTENT---TFTTshvvtELDEVAGSIpiGRPIANTRVYVLD 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 494 AeelnywtsKG-------EGEICVKGPNVFKGYLKDEDRTKEALDSDGWL------HTGDIGKWLPEGTLKIIDRKKHIF 560
Cdd:cd12117 322 E--------DGrpvppgvPGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQV 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 48256734 561 KLaQGEYVAPEKIENIYIRSEPVAQIYV---HGDSLKAFLVGIVVPDPEV 607
Cdd:cd12117 394 KI-RGFRIELGEIEAALRAHPGVREAVVvvrEDAGGDKRLVAYVVAEGAL 442
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
268-598 |
1.63e-20 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 94.84 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 268 DDLSIVCFTSGTTGNPKGAMLTHgnvvADFSGFLKVTEKVIFP-RQDDVLISflpLAHMFerviqsVVYCHGGRVGF--F 344
Cdd:cd05919 91 DDIAYLLYSSGTTGPPKGVMHAH----RDPLLFADAMAREALGlTPGDRVFS---SAKMF------FGYGLGNSLWFplA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 345 QGDIRLLSDD----------MKALRPTIFPVVPRllnrMYDKIFHQADTSlkrwllefaakrkQAEVRSgiIRnnsiwde 414
Cdd:cd05919 158 VGASAVLNPGwptaervlatLARFRPTVLYGVPT----FYANLLDSCAGS-------------PDALRS--LR------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 415 lffnkiqaslgghvrmIVTGAAPASPTVLG-FLRAALGCQVYEGYGQTEctAGCTFTT--PGDWTSGHVGAPLPCNHIKL 491
Cdd:cd05919 212 ----------------LCVSAGEALPRGLGeRWMEHFGGPILDGIGATE--VGHIFLSnrPGAWRLGSTGRPVPGYEIRL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 492 VDaEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPE 571
Cdd:cd05919 274 VD-EEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPV 350
|
330 340 350
....*....|....*....|....*....|....
gi 48256734 572 KIENIYIRSEPVAQIYV----HGDSL---KAFLV 598
Cdd:cd05919 351 EVESLIIQHPAVAEAAVvavpESTGLsrlTAFVV 384
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
260-635 |
1.68e-19 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 91.72 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 260 RVPVPPRPDDLSIVCFTSGTTGNPKGAMLTH----GNVVADFSGFlkvtekVIFPRQDDVLIS-------------FLP- 321
Cdd:cd05971 80 SALVTDGSDDPALIIYTSGTTGPPKGALHAHrvllGHLPGVQFPF------NLFPRDGDLYWTpadwawigglldvLLPs 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 322 -------LAHMFERviqsvvychggrvgfFQGD--IRLLSD---DMKALRPTIFpvvprllnrmydKIFHQADTSLKRWL 389
Cdd:cd05971 154 lyfgvpvLAHRMTK---------------FDPKaaLDLMSRygvTTAFLPPTAL------------KMMRQQGEQLKHAQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 390 LEfaakrkqaevrsgiirnnsiwdelffnkiqaslgghVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEC---TAG 466
Cdd:cd05971 207 VK------------------------------------LRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECnlvIGN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 467 CTFTTPGDwtSGHVGAPLPCNHIKLVDAEElNYWTSKGEGEICVKGPN--VFKGYLKDEDRTKEALDSDgWLHTGDIGKW 544
Cdd:cd05971 251 CSALFPIK--PGSMGKPIPGHRVAIVDDNG-TPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKMAGD-WLLTGDLGRK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 545 LPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRsepvaqiyvHGDSLKAFLVGIvvPDP---EVMPCWAQKKGIEGNY 621
Cdd:cd05971 327 DSDGYFWYVGRDDDVITSS-GYRIGPAEIEECLLK---------HPAVLMAAVVGI--PDPirgEIVKAFVVLNPGETPS 394
|
410
....*....|....*
gi 48256734 622 QELCKS-KELKKAIL 635
Cdd:cd05971 395 DALAREiQELVKTRL 409
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
120-610 |
3.60e-19 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 91.21 E-value: 3.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 120 WLSYQEVAKRAEFLGSGLLqhDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVI 199
Cdd:cd12118 29 RYTWRQTYDRCRRLASALA--ALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 200 VDKPHKailllehverketpglklvilmepFDDALrergkkcgvdiksmqAIEDSGQEnhrvPVPPRPDDLSIVC-FTSG 278
Cdd:cd12118 107 VDREFE------------------------YEDLL---------------AEGDPDFE----WIPPADEWDPIALnYTSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 279 TTGNPKGAMLTHGnvvadfSGFLKVTEKVIFPRQDD--VLISFLPLAHmferviqSVVYCHGGRVGFFQG--------DI 348
Cdd:cd12118 144 TTGRPKGVVYHHR------GAYLNALANILEWEMKQhpVYLWTLPMFH-------CNGWCFPWTVAAVGGtnvclrkvDA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 349 RLLSDDMKALRPTIFPVVPRLLNrmydkifhqadtslkrwllefaakrkqaevrsgIIRNNSIWDelffnkiQASLGGHV 428
Cdd:cd12118 211 KAIYDLIEKHKVTHFCGAPTVLN---------------------------------MLANAPPSD-------ARPLPHRV 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 429 RMIVTGAAPaSPTVLgFLRAALGCQVYEGYGQTEcTAG----CTF-----TTPGDWTS--------GHVGAplpcNHIKL 491
Cdd:cd12118 251 HVMTAGAPP-PAAVL-AKMEELGFDVTHVYGLTE-TYGpatvCAWkpewdELPTEERArlkarqgvRYVGL----EEVDV 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 492 VDAEELNYWTSKGE--GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVA 569
Cdd:cd12118 324 LDPETMKPVPRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENIS 401
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 48256734 570 PEKIENIyirsepvaqIYVHGDSLKAFLVGivVPDP---EVmPC 610
Cdd:cd12118 402 SVEVEGV---------LYKHPAVLEAAVVA--RPDEkwgEV-PC 433
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
118-605 |
3.68e-19 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 91.40 E-value: 3.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 118 YQWLSYQeVAKRAEFLGSgllqhdCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICT 197
Cdd:cd05970 50 FAELADY-SDKTANFFKA------MGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 198 VIVDKPHKailLLEHVE--RKETPGLKLVI-----LMEPFDDaLRERGKKCGVDIKSMQAiedsgqenhrvPVPPRPDDL 270
Cdd:cd05970 123 IVAIAEDN---IPEEIEkaAPECPSKPKLVwvgdpVPEGWID-FRKLIKNASPDFERPTA-----------NSYPCGEDI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 271 SIVCFTSGTTGNPKgaMLTHgnvvaDFSgflkvtekvifprqddvlisfLPLAHmfervIQSVVYCHGGRvgffQGDIRL 350
Cdd:cd05970 188 LLVYFSSGTTGMPK--MVEH-----DFT---------------------YPLGH-----IVTAKYWQNVR----EGGLHL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 351 LSDDM---KAlrptifpvvprllnrMYDKIFHQ-----------ADTSLKRWLLEFAAKRkqaEVRSgIIRNNSIWDELF 416
Cdd:cd05970 231 TVADTgwgKA---------------VWGKIYGQwiagaavfvydYDKFDPKALLEKLSKY---GVTT-FCAPPTIYRFLI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 417 FNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPG-DWTSGHVGAPLPCNHIKLVDAE 495
Cdd:cd05970 292 REDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTL-TIATFPWmEPKPGSMGKPAPGYEIDLIDRE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 496 ELNYWTSKgEGEICV---KGPNV--FKGYLKDEDRTKEALdSDGWLHTGDIGkWLPE-GTLKIIDRKKHIFKlAQGEYVA 569
Cdd:cd05970 371 GRSCEAGE-EGEIVIrtsKGKPVglFGGYYKDAEKTAEVW-HDGYYHTGDAA-WMDEdGYLWFVGRTDDLIK-SSGYRIG 446
|
490 500 510
....*....|....*....|....*....|....*.
gi 48256734 570 PEKIENIYIRSEPVAQIYVHGdslkaflvgivVPDP 605
Cdd:cd05970 447 PFEVESALIQHPAVLECAVTG-----------VPDP 471
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
267-682 |
4.64e-19 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 91.40 E-value: 4.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfSGFLKVTekVIFPRQDDVLISFLPLAHMFErvIQSVVY------CHggr 340
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSALIV--QSLAKIA--IVGYGEDDVYLHTAPLCHIGG--LSSALAmlmvgaCH--- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 341 VGFFQGDIRLLSDDMKALRPTIFPVVPRLLnrmydkifhqADtslkrwLLEFAAKRKQAEVRSGiirnnsiwdelffnki 420
Cdd:PLN02860 242 VLLPKFDAKAALQAIKQHNVTSMITVPAMM----------AD------LISLTRKSMTWKVFPS---------------- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 421 qaslgghVRMIVTGAAPASP-----TVLGFLRAALgcqvYEGYGQTECTAGCTFTTPGDWT-----------------SG 478
Cdd:PLN02860 290 -------VRKILNGGGSLSSrllpdAKKLFPNAKL----FSAYGMTEACSSLTFMTLHDPTlespkqtlqtvnqtkssSV 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 479 H------VGAPLPcnHIKL-VDAEElnywtSKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLK 551
Cdd:PLN02860 359 HqpqgvcVGKPAP--HVELkIGLDE-----SSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLW 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 552 IIDRKKHIFKlAQGEYVAPEKIENIYIRSEPVAQIYVHGdslkaflvgivVPDPE----VMPC--------WAQKkgieg 619
Cdd:PLN02860 432 LIGRSNDRIK-TGGENVYPEEVEAVLSQHPGVASVVVVG-----------VPDSRltemVVACvrlrdgwiWSDN----- 494
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 48256734 620 NYQELCKSKELKKAILDDMVmlgKESGLHSFEQVKAIYIHCDMFSvqnglLTPTLKAKRPELR 682
Cdd:PLN02860 495 EKENAKKNLTLSSETLRHHC---REKNLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEVR 549
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
267-604 |
6.41e-19 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 90.22 E-value: 6.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPRQDDVL--ISFLPLAHMFERVIqsvvyCHGGRVGFF 344
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQMasFSFDVFAGDFARSL-----LNGGTLVIC 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 345 QGDIRL----LSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTSLKRWLLEFAAKRKQAEvrsgiirnnsiWdelfFNKI 420
Cdd:cd17650 167 PDEVKLdpaaLYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQ-----------D----FKTL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 421 QASLGGHVRMIvtgaapaspTVLGFLRAALGCQVYEGYGQTECTAGctfTTPgdwtsghVGAPLPCNHIKLVDaEELNYW 500
Cdd:cd17650 232 AARFGQGMRII---------NSYGVTEATIDSTYYEEGRDPLGDSA---NVP-------IGRPLPNTAMYVLD-ERLQPQ 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 501 TSKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGW------LHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIE 574
Cdd:cd17650 292 PVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI-RGFRIELGEIE 370
|
330 340 350
....*....|....*....|....*....|...
gi 48256734 575 NIYIRSEPVAQIYV---HGDSLKAFLVGIVVPD 604
Cdd:cd17650 371 SQLARHPAIDEAVVavrEDKGGEARLCAYVVAA 403
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
121-609 |
4.06e-18 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 87.76 E-value: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAG--VGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 201 DkphkailllehverketpglklvilmepfddalrergkkcgvdiksmqaiedsgqenhrvpvpprPDDLSIVCFTSGTT 280
Cdd:cd12115 103 D-----------------------------------------------------------------PDDLAYVIYTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 281 GNPKGAMLTHGNVVA------------DFSGFLKVTEkVIFprqdDVLI--SFLPLahmferviqsvvyCHGGRVGFFQG 346
Cdd:cd12115 118 GRPKGVAIEHRNAAAflqwaaaafsaeELAGVLASTS-ICF----DLSVfeLFGPL-------------ATGGKVVLADN 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 347 DIRLLsDDMKALRPTIFPVVPrllnrmydkifhqadtSLKRWLLEFaakrkqaevrsgiirnnsiwdelffNKIQASlgg 426
Cdd:cd12115 180 VLALP-DLPAAAEVTLINTVP----------------SAAAELLRH-------------------------DALPAS--- 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 427 hVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFT--TPGDWTSGHVGAPLPCNHIKLVDaEELNYWTSK 503
Cdd:cd12115 215 -VRVVNLAGEPLPRDLVQRLYARLqVERVVNLYGPSEDTTYSTVApvPPGASGEVSIGRPLANTQAYVLD-RALQPVPLG 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 504 GEGEICVKGPNVFKGYLKDEDRTKEALDSDGWL------HTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIY 577
Cdd:cd12115 293 VPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAAL 371
|
490 500 510
....*....|....*....|....*....|....*
gi 48256734 578 IRSEPVAQ--IYVHGDSL-KAFLVGIVVPDPEVMP 609
Cdd:cd12115 372 RSIPGVREavVVAIGDAAgERRLVAYIVAEPGAAG 406
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
121-590 |
7.14e-18 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 87.18 E-value: 7.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSGLLQHDCKVGteQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRPG--QRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 201 dkphkaillleHVERKETPGLKLVILMEPFDDALRERGKKCgvdiKSMQAIEDSgqenhrvpvPPRPDDLSIVCFTSGTT 280
Cdd:cd05923 107 -----------AVDAQVMDAIFQSGVRVLALSDLVGLGEPE----SAGPLIEDP---------PREPEQPAFVFYTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 281 GNPKGAMLTHgNVVADFSGFLKVTEKVIFPRQDdVLISFLPLAHMferviqsvvychggrVGFFQgdirLLSDDMkALRP 360
Cdd:cd05923 163 GLPKGAVIPQ-RAAESRVLFMSTQAGLRHGRHN-VVLGLMPLYHV---------------IGFFA----VLVAAL-ALDG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 361 TIFPVvprllnrmydKIFHQADtslkrwllefAAKRKQAEVRSGIIRNNSIWDELFFNKIQASLG-GHVRMIVTGAAPAS 439
Cdd:cd05923 221 TYVVV----------EEFDPAD----------ALKLIEQERVTSLFATPTHLDALAAAAEFAGLKlSSLRHVTFAGATMP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 440 PTVLGFLRAALGCQVYEGYGQTECTagcTFTTPGDWTSGHVGAPLPCNHIKLVD-AEELNYWTSKG-EGEICVK--GPNV 515
Cdd:cd05923 281 DAVLERVNQHLPGEKVNIYGTTEAM---NSLYMRDARTGTEMRPGFFSEVRIVRiGGSPDEALANGeEGELIVAaaADAA 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 48256734 516 FKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYVHG 590
Cdd:cd05923 358 FTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIG 430
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
121-628 |
7.50e-18 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 87.04 E-value: 7.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSGLLQhdCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIIN--------- 191
Cdd:cd05959 30 LTYAELEAEARRVAGALRA--LGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEdsrarvvvv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 192 TADICTVIVDKPHKAILLLEHVERKE-TPGLKLVILMEPFDDALRERGKkcgvdiksmqaiedsgqenhrvPVPPRPDDL 270
Cdd:cd05959 108 SGELAPVLAAALTKSEHTLVVLIVSGgAGPEAGALLLAELVAAEAEQLK----------------------PAATHADDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 271 SIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKvteKVIFPRQDDVLIS--------------FLPLAH------MFERVI 330
Cdd:cd05959 166 AFWLYSSGSTGRPKGVVHLHADIYWTAELYAR---NVLGIREDDVCFSaaklffayglgnslTFPLSVgattvlMPERPT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 331 QSVVYchggrvgffqgdirllsDDMKALRPTIFPVVPRLLNRMydkifhqadtslkrwlleFAAKRKQAEVRSGIirnns 410
Cdd:cd05959 243 PAAVF-----------------KRIRRYRPTVFFGVPTLYAAM------------------LAAPNLPSRDLSSL----- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 411 iwdelffnkiqaslgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTF--TTPGDWTSGHVGAPLPCNH 488
Cdd:cd05959 283 ------------------RLCVSAGEALPAEVGERWKARFGLDILDGIGSTE--MLHIFlsNRPGRVRYGTTGKPVPGYE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 489 IKLVDaEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEALDSdGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYV 568
Cdd:cd05959 343 VELRD-EDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQG-EWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWV 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 48256734 569 APEKIENIYIRSEPVAQIYVHG-------DSLKAFlvgiVVPDPEVMPCWAQKKGIegnyQELCKSK 628
Cdd:cd05959 420 SPFEVESALVQHPAVLEAAVVGvededglTKPKAF----VVLRPGYEDSEALEEEL----KEFVKDR 478
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
259-594 |
1.08e-17 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 87.46 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 259 HRVPVPPRPDDLSIVCFTSGTTGNPKGAMLTH----GNV-----VADFSgflkvtekvifPRqdDVLISFLPLAHMFerv 329
Cdd:PRK08043 356 RLAQVKQQPEDAALILFTSGSEGHPKGVVHSHksllANVeqiktIADFT-----------PN--DRFMSALPLFHSF--- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 330 iqsvvychGGRVGffqgdirLLSDDMKALRPTIFP------VVPRLLnrmYDK----IFhqaDTSlkRWLLEFAakrkqa 399
Cdd:PRK08043 420 --------GLTVG-------LFTPLLTGAEVFLYPsplhyrIVPELV---YDRnctvLF---GTS--TFLGNYA------ 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 400 evrsgiiRNNSIWDelFFnkiqaslggHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGH 479
Cdd:PRK08043 471 -------RFANPYD--FA---------RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGT 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 480 VGAPLPCnhiklVDAEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTK-EALDSD--------GWLHTGDIGKWLPEGTL 550
Cdd:PRK08043 533 VGRILPG-----MDARLLSVPGIEQGGRLQLKGPNIMNGYLRVEKPGVlEVPTAEnargemerGWYDTGDIVRFDEQGFV 607
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 48256734 551 KIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQiyvHGDSLK 594
Cdd:PRK08043 608 QIQGRAKRFAKIA-GEMVSLEMVEQLALGVSPDKQ---HATAIK 647
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
121-606 |
1.19e-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: 86.56 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:cd17646 24 LTYRELDERANRLAHLLRARG--VGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 201 DkphkailllehverketpglklvilmepfdDALRERGKKcGVDIKSMQAIEDSGQENHRVPVPPRPDDLSIVCFTSGTT 280
Cdd:cd17646 102 T------------------------------ADLAARLPA-GGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGST 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 281 GNPKGAMLTHGNVVADFSGF-----LKVTEKVIF--PRQDDVLIS--FLPLAHMfERViqsVVYCHGGRvgffqGDIRLL 351
Cdd:cd17646 151 GRPKGVMVTHAGIVNRLLWMqdeypLGPGDRVLQktPLSFDVSVWelFWPLVAG-ARL---VVARPGGH-----RDPAYL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 352 SDDMKALRPTIFPVVPRLLnrmydkifhqadtslkrwllefaakrkqaevrsgiirnnsiwdELFFNKIQASLGGHVRMI 431
Cdd:cd17646 222 AALIREHGVTTCHFVPSML-------------------------------------------RVFLAEPAAGSCASLRRV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 432 VTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHV--GAPLPCNHIKLVDAEeLNYWTSKGEGEI 508
Cdd:cd17646 259 FCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVThWPVRGPAETPSVpiGRPVPNTRLYVLDDA-LRPVPVGVPGEL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 509 CVKGPNVFKGYLKDEDRTKEALDSDGWLH------TGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEP 582
Cdd:cd17646 338 YLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKI-RGFRVEPGEIEAALAAHPA 416
|
490 500
....*....|....*....|....*..
gi 48256734 583 VAQIYV---HGDSLKAFLVGIVVPDPE 606
Cdd:cd17646 417 VTHAVVvarAAPAGAARLVGYVVPAAG 443
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
269-576 |
1.28e-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: 84.62 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 269 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIfprQDDVLISFLPLAHMFERV-IQSVVYCHGGRVGFfqGD 347
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWV---VGDVTYLPLPATHIGGLWwILTCLIHGGLCVTG--GE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 348 IRLLSDDMKAL---RPTIFPVVPRLLNRMydkifhqadTSLKRWLLEFAAKrkqaevrsgiirnnsiwdelffnkiqasl 424
Cdd:cd17635 77 NTTYKSLFKILttnAVTTTCLVPTLLSKL---------VSELKSANATVPS----------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 425 gghVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDAEELNYwTSK 503
Cdd:cd17635 119 ---LRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLPTDDDSIEiNAVGRPYPGVDVYLAATDGIAG-PSA 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 48256734 504 GEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENI 576
Cdd:cd17635 195 SFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERI 265
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
266-606 |
1.59e-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: 85.82 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 266 RPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkvTEKVIFPRQDDVLISFLPLAHMFerviqSV-----VYCHGGR 340
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA----TQRWFGFNEDDVWTLFHSYAFDF-----SVweiwgALLHGGR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 341 VGFFQGDIRLLSDDMkalrptifpvvPRLLNRMYDKIFHQADTSLKRWLlefaakrkQAEVRsgiirnnsiwdelfFNKI 420
Cdd:cd17643 162 LVVVPYEVARSPEDF-----------ARLLRDEGVTVLNQTPSAFYQLV--------EAADR--------------DGRD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 421 QASLgghvRMIVTGAAPASPTVLGFLRAALGC---QVYEGYGQTECTAGCTFT--TPGDW---TSGHVGAPLPCNHIKLV 492
Cdd:cd17643 209 PLAL----RYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFRplDAADLpaaAASPIGRPLPGLRVYVL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 493 DAEeLNYWTSKGEGEICVKGPNVFKGYLKDEDRTKE-------ALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQG 565
Cdd:cd17643 285 DAD-GRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI-RG 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 48256734 566 EYVAPEKIENIYIRSEPVAQIYV---HGDSLKAFLVGIVVPDPE 606
Cdd:cd17643 363 FRIELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVADDG 406
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
27-604 |
1.61e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 87.52 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 27 ATTLVSMGALAAILAYW--LTHRPKAlQPPCNL----LMQSEEVEDSGGARRsvigdctqlLTHYYDDARTMYQVFRRGL 100
Cdd:PRK12467 453 ATDLFEATTIERLATHWrnLLEAIVA-EPRRRLgelpLLDAEERARELVRWN---------APATEYAPDCVHQLIEAQA 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 101 SISGNGPCLGFRKpeqpyQWLSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDT 180
Cdd:PRK12467 523 RQHPERPALVFGE-----QVLSYAELNRQANRLAHVLIAAG--VGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPE 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 181 LGPGSIRYIINTADICTVIVDkPHKAILLlehverkETP-GLKLVILMEPFDdalrergkkcgvdiksmqaiEDSGQENH 259
Cdd:PRK12467 596 YPQDRLAYMLDDSGVRLLLTQ-SHLLAQL-------PVPaGLRSLCLDEPAD--------------------LLCGYSGH 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 260 RVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVvadfSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGG 339
Cdd:PRK12467 648 NPEVALDPDNLAYVIYTSGSTGQPKGVAISHGAL----ANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGA 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 340 RVgffqgdirLLSDDMKALRPTIFpvvprllnrmYDKIFHQADTSLKrwllefaakrkqaevrsgiiRNNSIWDELFFNK 419
Cdd:PRK12467 724 TL--------HLLPPDCARDAEAF----------AALMADQGVTVLK--------------------IVPSHLQALLQAS 765
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 420 IQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTT----PGDWTSGHVGAPLPCNHIKLVDAe 495
Cdd:PRK12467 766 RVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYElsdeERDFGNVPIGQPLANLGLYILDH- 844
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 496 ELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEALDSD------GWLH-TGDIGKWLPEGTLKIIDRKKHIFKLaQGEYV 568
Cdd:PRK12467 845 YLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDpfgadgGRLYrTGDLARYRADGVIEYLGRMDHQVKI-RGFRI 923
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 48256734 569 APEKIENIYIRSEPVAQIYV------HGDSLKAFLVGIVVPD 604
Cdd:PRK12467 924 ELGEIEARLLAQPGVREAVVlaqpgdAGLQLVAYLVPAAVAD 965
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
267-583 |
2.23e-17 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 85.62 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKvifpRQDDVLISFLPLAHmferviqsvvychggRVGFFQG 346
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEW----KTKDRILSWMPLTH---------------DMGLIAF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 347 DIRLLSDDMKA-LRPT-IFPVVPRLlnrmydkifhqadtslkrWLLEfAAKRKQAEVRSGIIRNNSIWDELFFNKIQASL 424
Cdd:cd05908 166 HLAPLIAGMNQyLMPTrLFIRRPIL------------------WLKK-ASEHKATIVSSPNFGYKYFLKTLKPEKANDWD 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 425 GGHVRMIVTGAAPASP----------TVLGFLRAAlgcqVYEGYGQTECTAGCTF------------------------- 469
Cdd:cd05908 227 LSSIRMILNGAEPIDYelchefldhmSKYGLKRNA----ILPVYGLAEASVGASLpkaqspfktitlgrrhvthgepepe 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 470 ---TTPGDWTSGHVGAPLPCNHIKLVDaeELNYWTSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGkWL 545
Cdd:cd05908 303 vdkKDSECLTFVEVGKPIDETDIRICD--EDNKILPDGYiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FI 379
|
330 340 350
....*....|....*....|....*....|....*...
gi 48256734 546 PEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPV 583
Cdd:cd05908 380 RNGRLVITGREKDII-FVNGQNVYPHDIERIAEELEGV 416
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
121-606 |
2.69e-17 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 85.58 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfigVFAQ--NRPEWIIAELACYtySMVVVPLYdTLgPG----SIRYIINTAD 194
Cdd:COG1021 51 LSYAELDRRADRLAAGLLALGLRPGDR----VVVQlpNVAEFVIVFFALF--RAGAIPVF-AL-PAhrraEISHFAEQSE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 195 ICTVIVDKPHkaiLLLEHVE-----RKETPGLKLVILMEPFDDALrergkkcgvdikSMQAIEDSGQEnHRVPVPPrPDD 269
Cdd:COG1021 123 AVAYIIPDRH---RGFDYRAlarelQAEVPSLRHVLVVGDAGEFT------------SLDALLAAPAD-LSEPRPD-PDD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 270 lsiVCF---TSGTTGNPKGAMLTHG----NVV--ADFSGFlkvtekvifpRQDDVLISFLPLAHMF---ERVIQSVVYcH 337
Cdd:COG1021 186 ---VAFfqlSGGTTGLPKLIPRTHDdylySVRasAEICGL----------DADTVYLAALPAAHNFplsSPGVLGVLY-A 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 338 GGRVgffqgdirLLSDDMKALrpTIFPVVPRllnrmydkifHQAD-TSL-----KRWLlEFAAKRKQAevrsgiirnnsi 411
Cdd:COG1021 252 GGTV--------VLAPDPSPD--TAFPLIER----------ERVTvTALvpplaLLWL-DAAERSRYD------------ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 412 wdeLffnkiqASLgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctaG-CTFTTPGD--WTSGH-VGAPL-PC 486
Cdd:COG1021 299 ---L------SSL----RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---GlVNYTRLDDpeEVILTtQGRPIsPD 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 487 NHIKLVDAEELNywTSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKK-HIFKlaQ 564
Cdd:COG1021 363 DEVRIVDEDGNP--VPPGEvGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKdQINR--G 438
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 48256734 565 GEYVAPEKIENiyirsepvaQIYVHGDSLKAFLVGivVPDPE 606
Cdd:COG1021 439 GEKIAAEEVEN---------LLLAHPAVHDAAVVA--MPDEY 469
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
121-609 |
2.76e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 85.57 E-value: 2.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADiCTVIV 200
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQG--VRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGR-ARWLV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 201 DKPH-KAILL---LEHVERKETPGLKLVILMEPFDDALRERGKKCGVdiksmQAIEDSGQENHRV-PVPPRPDDLSIVCF 275
Cdd:PRK06164 113 VWPGfKGIDFaaiLAAVPPDALPPLRAIAVVDDAADATPAPAPGARV-----QLFALPDPAPPAAaGERAADPDAGALLF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 276 T-SGTTGNPK------GAMLTHGNVVADFSGFlkvtekvifpRQDDVLISFLPLahmferviqSVVYCHGGRVGFFQGDI 348
Cdd:PRK06164 188 TtSGTTSGPKlvlhrqATLLRHARAIARAYGY----------DPGAVLLAALPF---------CGVFGFSTLLGALAGGA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 349 RLLSDDmkalrptIF--PVVPRLL-----------NRMYDKIFHQADTSLkrwllEFAAKRkqaevRSGIIRNNSIWDEL 415
Cdd:PRK06164 249 PLVCEP-------VFdaARTARALrrhrvthtfgnDEMLRRILDTAGERA-----DFPSAR-----LFGFASFAPALGEL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 416 ffnkiqaslgghvrmivtgaaPASPTVLGFLRAALgcqvyegYGQTECTA---GCTFTTPgdWTSGHVGAPLPCN---HI 489
Cdd:PRK06164 312 ---------------------AALARARGVPLTGL-------YGSSEVQAlvaLQPATDP--VSVRIEGGGRPASpeaRV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 490 KLVDAEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVA 569
Cdd:PRK06164 362 RARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVN 440
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 48256734 570 PEKIENIYIRSEPVAQIYVHGDSL--KAFLVGIVVPDPEVMP 609
Cdd:PRK06164 441 PAEIEHALEALPGVAAAQVVGATRdgKTVPVAFVIPTDGASP 482
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
421-626 |
1.16e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 83.92 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 421 QASLGGHVRMIVTGAAPasPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGD-WTSghvgapLPCN------------ 487
Cdd:PLN03102 296 LSPRSGPVHVLTGGSPP--PAALVKKVQRLGFQVMHAYGLTEATGPVLFCEWQDeWNR------LPENqqmelkarqgvs 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 488 HIKLVDAEELNYWT-------SKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIF 560
Cdd:PLN03102 368 ILGLADVDVKNKETqesvprdGKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 48256734 561 kLAQGEYVAPEKIENIyirsepvaqIYVHGDSLKAFLVGIVVPDPEVMPCW--AQKKGIEGNYQELCK 626
Cdd:PLN03102 447 -ISGGENISSVEVENV---------LYKYPKVLETAVVAMPHPTWGETPCAfvVLEKGETTKEDRVDK 504
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
268-609 |
4.29e-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: 81.37 E-value: 4.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 268 DDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkvTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGR--VGFFQ 345
Cdd:cd05958 97 DDICILAFTSGTTGAPKATMHFHRDPLASADRY---AVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGAsgVLLEE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 346 GDIRLLSDDMKALRPTIFPVVPRllnrMYDKIFHQADTSlkrwllefaakrkqaevrsgiirnnsiwdelffnkiqASLG 425
Cdd:cd05958 174 ATPDLLLSAIARYKPTVLFTAPT----AYRAMLAHPDAA-------------------------------------GPDL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 426 GHVRMIVTgAAPASPTVLGFL-RAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNywTSKG 504
Cdd:cd05958 213 SSLRKCVS-AGEALPAALHRAwKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVDDEGNP--VPDG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 505 E-GEICVKGPNvfkGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPV 583
Cdd:cd05958 290 TiGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQHPAV 365
|
330 340
....*....|....*....|....*....
gi 48256734 584 AQIYVHGDSLKAFLV---GIVVPDPEVMP 609
Cdd:cd05958 366 AECAVVGHPDESRGVvvkAFVVLRPGVIP 394
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
265-603 |
4.58e-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: 81.35 E-value: 4.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 265 PRPDDLSIVCFTSGTTGNPKGAMLTHGNvvadFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERV--IQSVVychggrvg 342
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGT----FAAQIDALRQLYGIRPGEVDLATFPLFALFGPAlgLTSVI-------- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 343 ffqgdirllsDDMKALRPtifpvvprllnrmydkifhqADTSlKRWLLEFAAkrkQAEVrSGIIRNNSIWDEL--FFNKI 420
Cdd:cd05910 150 ----------PDMDPTRP--------------------ARAD-PQKLVGAIR---QYGV-SIVFGSPALLERVarYCAQH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 421 QASLGGhVRMIVTGAAPASPTVLGFLRAAL--GCQVYEGYGQTECTAGCT------FTTPGDWTSGH----VGAPLPCNH 488
Cdd:cd05910 195 GITLPS-LRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrelLATTTAATSGGagtcVGRPIPGVR 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 489 IKLV--DAEELNYWTSKGE------GEICVKGPNVFKGYLKDEDRTKEALDSDG----WLHTGDIGKWLPEGTLKIIDRK 556
Cdd:cd05910 274 VRIIeiDDEPIAEWDDTLElprgeiGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRK 353
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 48256734 557 KHIFKLAQGEYVapekieniyirSEPVAQIY-VHGDSLKAFLVGIVVP 603
Cdd:cd05910 354 AHRVITTGGTLY-----------TEPVERVFnTHPGVRRSALVGVGKP 390
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
94-614 |
6.71e-16 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 81.37 E-value: 6.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 94 QVFRRGLSISGNGPCLGFRKPEQpyQWLSYQEVAKRAEFLGSGLlqHD-CKVGTEQFIGVFAQNRPEWIIAELACYTYSM 172
Cdd:PRK05620 14 RILEYGSTVHGDTTVTTWGGAEQ--EQTTFAAIGARAAALAHAL--HDeLGITGDQRVGSMMYNCAEHLEVLFAVACMGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 173 VVVPLYDTLGPGSIRYIINTADIcTVIVDKPHKAILLLEHVerKETPGLKLVILMEPFDDALRERGKKCGVDIKSMQAIE 252
Cdd:PRK05620 90 VFNPLNKQLMNDQIVHIINHAED-EVIVADPRLAEQLGEIL--KECPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 253 DSGQENHRVPVPPRpDDLSIVCFTSGTTGNPKGAMLTHGNVVADfSGFLKVTEKviFPRQDDVliSFL---PLAHMFERV 329
Cdd:PRK05620 167 DGRSTVYDWPELDE-TTAAAICYSTGTTGAPKGVVYSHRSLYLQ-SLSLRTTDS--LAVTHGE--SFLccvPIYHVLSWG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 330 IQSVVYCHGGrvgffqgdirllsddmkalrPTIFP----VVPRLLnrmydkifHQADTSLKRwllefaakrkqaeVRSGI 405
Cdd:PRK05620 241 VPLAAFMSGT--------------------PLVFPgpdlSAPTLA--------KIIATAMPR-------------VAHGV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 406 irnNSIWDELFFNKIQ-----ASLgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHV 480
Cdd:PRK05620 280 ---PTLWIQLMVHYLKnpperMSL----QEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEA 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 481 GA---------PLPCNHiKLVDAEELNYWTSKGEGEICVKGPNVFKGYLKDE----------------DRTKEALDSDGW 535
Cdd:PRK05620 353 RWayrvsqgrfPASLEY-RIVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGW 431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 48256734 536 LHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSEPVaqiyvhgdsLKAFLVGIvvPDPEvmpcWAQK 614
Cdd:PRK05620 432 LRTGDVGSVTRDGFLTIHDRARDVIR-SGGEWIYSAQLENYIMAAPEV---------VECAVIGY--PDDK----WGER 494
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
88-588 |
8.48e-16 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 80.96 E-value: 8.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 88 DARTMYQVFRRGLSISGNGPCLGFRKpeqpyQWLSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELAC 167
Cdd:PRK06155 19 SERTLPAMLARQAERYPDRPLLVFGG-----TRWTYAEAARAAAAAAHALAAAGVKRGDR--VALMCGNRIEFLDVFLGC 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 168 YTYSMVVVPLYDTLGPGSIRYIINTADICTVIVDKPHKAilLLEHVERKETPGLKLVILmepfdDALRERGKKCGVDIKS 247
Cdd:PRK06155 92 AWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLA--ALEAADPGDLPLPAVWLL-----DAPASVSVPAGWSTAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 248 MQAIEDSGQenhrvPVPPRPDDLSIVCFTSGTTGNPKGAMLTHgnvvADFSGFLKVTEKVIFPRQDDVLISFLPLAH--- 324
Cdd:PRK06155 165 LPPLDAPAP-----AAAVQPGDTAAILYTSGTTGPSKGVCCPH----AQFYWWGRNSAEDLEIGADDVLYTTLPLFHtna 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 325 --MFervIQSVVycHGGRV---------GFFqgdirllsDDMKALRPTIF----PVVPRLLnrmydkifhqadtslkrwl 389
Cdd:PRK06155 236 lnAF---FQALL--AGATYvleprfsasGFW--------PAVRRHGATVTyllgAMVSILL------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 390 lefaAKRKQAEVRsgiirnnsiwdelffnkiqaslgGH-VRMIVTGAAPASptVLGFLRAALGCQVYEGYGQTECTAGCt 468
Cdd:PRK06155 284 ----SQPARESDR-----------------------AHrVRVALGPGVPAA--LHAAFRERFGVDLLDGYGSTETNFVI- 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 469 FTTPGDWTSGHVGAPLPCNHIKLVDAEELNywTSKGE-GEICVKG--PNVF-KGYLKDEDRTKEALdSDGWLHTGDIGKW 544
Cdd:PRK06155 334 AVTHGSQRPGSMGRLAPGFEARVVDEHDQE--LPDGEpGELLLRAdePFAFaTGYFGMPEKTVEAW-RNLWFHTGDRVVR 410
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 48256734 545 LPEGTLKIIDRKKHIFKlAQGEYVAPEKIENIyIRSEP-VAQIYV 588
Cdd:PRK06155 411 DADGWFRFVDRIKDAIR-RRGENISSFEVEQV-LLSHPaVAAAAV 453
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
107-568 |
1.07e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 80.86 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 107 PCLGFRKPEQ-PYQWLSYQEVAKRAEFLGSGLLqhDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLydtlgpgS 185
Cdd:PRK12582 66 PWLAQREPGHgQWRKVTYGEAKRAVDALAQALL--DLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPV-------S 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 186 IRYIINTADIctvivDKphkaillLEHVERKETPGLKLVILMEPFDDALRERGKKcGVDIKSMQAIEDSGQENH---RVP 262
Cdd:PRK12582 137 PAYSLMSHDH-----AK-------LKHLFDLVKPRVVFAQSGAPFARALAALDLL-DVTVVHVTGPGEGIASIAfadLAA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 263 VPPR-----------PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekviFPRQDD----VLISFLPLAHM-- 325
Cdd:PRK12582 204 TPPTaavaaaiaaitPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQL-----RPREPDppppVSLDWMPWNHTmg 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 326 ----FERVIQS--VVYCHGGR--VGFFQGDIRLLSDdmkaLRPTIFPVVPRLLNRMYDKIfhQADTSLKRWLLefaaKRK 397
Cdd:PRK12582 279 gnanFNGLLWGggTLYIDDGKplPGMFEETIRNLRE----ISPTVYGNVPAGYAMLAEAM--EKDDALRRSFF----KNL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 398 QAEVRSGIIRNNSIWDELFFNKIQASlgGHvrMIVtgaapasptvlgflraalgcqVYEGYGQTEcTAGCTFTTpgDWTS 477
Cdd:PRK12582 349 RLMAYGGATLSDDLYERMQALAVRTT--GH--RIP---------------------FYTGYGATE-TAPTTTGT--HWDT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 478 ---GHVGAPLPCNHIKLVDAEElNYwtskgegEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWL----PEGTL 550
Cdd:PRK12582 401 ervGLIGLPLPGVELKLAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdpddPEKGL 472
|
490
....*....|....*...
gi 48256734 551 KIIDRKKHIFKLAQGEYV 568
Cdd:PRK12582 473 IFDGRVAEDFKLSTGTWV 490
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
258-588 |
1.54e-15 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 79.53 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 258 NHRVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkVTEKVIFPRQDDVLISfLPLAHmferVI-QSVVY- 335
Cdd:PRK09029 125 EGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEG---VLSLMPFTAQDSWLLS-LPLFH----VSgQGIVWr 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 336 --CHGGRVGFfqGDIRLLSDDMK-----ALRPTifpVVPRLLNRmydkifHQADTSLKRWLLefaakrkqaevrsgiirn 408
Cdd:PRK09029 197 wlYAGATLVV--RDKQPLEQALAgcthaSLVPT---QLWRLLDN------RSEPLSLKAVLL------------------ 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 409 nsiwdelffnkiqaslGGhvRMIvtgaapasPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTSGhVGAPLPCNH 488
Cdd:PRK09029 248 ----------------GG--AAI--------PVELTEQAEQQGIRCWCGYGLTE-MASTVCAKRADGLAG-VGSPLPGRE 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 489 IKLVDaeelnywtskgeGEICVKGPNVFKGYLKDeDRTKEALDSDGWLHTGDIGKWLpEGTLKIIDRKKHIFkLAQGEYV 568
Cdd:PRK09029 300 VKLVD------------GEIWLRGASLALGYWRQ-GQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGI 364
|
330 340
....*....|....*....|
gi 48256734 569 APEKIENIYIRSEPVAQIYV 588
Cdd:PRK09029 365 QPEEIERVINQHPLVQQVFV 384
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
457-613 |
3.65e-15 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 77.34 E-value: 3.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 457 GYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAE--ELnywtSKGE-GEICVKGPNVFKGYLkDEDRTKEALDSD 533
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDgrEV----PDGEvGEIVARGPTVMAGYW-NRPEVNARRTRG 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 534 GWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqgeyvapekIENIY-------IRSEP-VAQIYVhgdslkaflvgIVVPDP 605
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSG---------AENIYpaevercLRQHPaVADAAV-----------IGVPDP 276
|
....*...
gi 48256734 606 EvmpcWAQ 613
Cdd:cd17636 277 R----WAQ 280
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
267-578 |
8.51e-15 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 77.55 E-value: 8.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAHMFerviqsvvychggrvGFfqG 346
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFS----PKEDDVMMSFLPPFHAY---------------GF--N 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 347 DIRLLSddMKALRPTIF---PVVPRLLNRMYDK---IFHQADTSLKRWLLEFAAKRKQA--EVRSGIIRNNSIWDELFfn 418
Cdd:PRK06334 241 SCTLFP--LLSGVPVVFaynPLYPKKIVEMIDEakvTFLGSTPVFFDYILKTAKKQESClpSLRFVVIGGDAFKDSLY-- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 419 kiqaslgghvrmivTGAAPASPTVlgflraalgcQVYEGYGQTECTAGCTFTT---PGDwtSGHVGAPLPCNHIKLVdAE 495
Cdd:PRK06334 317 --------------QEALKTFPHI----------QLRQGYGTTECSPVITINTvnsPKH--ESCVGMPIRGMDVLIV-SE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 496 ELNYWTSKGE-GEICVKGPNVFKGYL-KDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKI 573
Cdd:PRK06334 370 ETKVPVSSGEtGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSLEAL 448
|
....*
gi 48256734 574 ENIYI 578
Cdd:PRK06334 449 ESILM 453
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
276-606 |
1.86e-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: 76.21 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 276 TSGTTGNPKGAMLTHgnvvADFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERV---IQSVVYChGGRVgffqgdirLLS 352
Cdd:cd05920 147 SGGTTGTPKLIPRTH----NDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLAcpgVLGTLLA-GGRV--------VLA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 353 DDMKALrpTIFPVVPRllnrmyDKIFHqadTSL-----KRWLlEFAAKRkqaevrsgiirnnsiwdelffnkiQASLGGH 427
Cdd:cd05920 214 PDPSPD--AAFPLIER------EGVTV---TALvpalvSLWL-DAAASR------------------------RADLSSL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 428 vRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHVGAPL-PCNHIKLVDaEELNYWTSKGE 505
Cdd:cd05920 258 -RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTrLDDPDEVIIHTQGRPMsPDDEIRVVD-EEGNPVPPGEE 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 506 GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENiyirsepvaQ 585
Cdd:cd05920 336 GELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVEN---------L 405
|
330 340
....*....|....*....|.
gi 48256734 586 IYVHGDSLKAFLVGivVPDPE 606
Cdd:cd05920 406 LLRHPAVHDAAVVA--MPDEL 424
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
420-588 |
2.19e-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: 76.07 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 420 IQASLGG---HVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTfTTPGD-WTSGHVGAPLPCNHIKLVDAE 495
Cdd:cd05974 191 IQQDLASfdvKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVG-NSPGQpVKAGSMGRPLPGYRVALLDPD 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 496 ElnywTSKGEGEICV-----KGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAP 570
Cdd:cd05974 270 G----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SSDYRISP 343
|
170
....*....|....*...
gi 48256734 571 EKIENIYIRSEPVAQIYV 588
Cdd:cd05974 344 FELESVLIEHPAVAEAAV 361
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
262-609 |
4.04e-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: 75.46 E-value: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 262 PVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVTEKVIFPRQDDVLISFLPLAhmFERVIQSV--VYCHGG 339
Cdd:cd17651 130 DPALDADDLAYVIYTSGSTGRPKGVVMPHRSLA----NLVAWQARASSLGPGARTLQFAGLG--FDVSVQEIfsTLCAGA 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 340 RVGFFQGDIRLLSDDMKALrptifpvvprLLNRMYDKIFhqADTSLKRWLLEfAAKRKQAEvrsgiirnnsiwdelffnk 419
Cdd:cd17651 204 TLVLPPEEVRTDPPALAAW----------LDEQRISRVF--LPTVALRALAE-HGRPLGVR------------------- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 420 iqaslGGHVRMIVTG--AAPASPTVLGFLRAALGCQVYEGYGQTE---CTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVD 493
Cdd:cd17651 252 -----LAALRYLLTGgeQLVLTEDLREFCAGLPGLRLHNHYGPTEthvVTALSLPGDPAAWPApPPIGRPIDNTRVYVLD 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 494 AeelnywtsKGE-------GEICVKGPNVFKGYLKDEDRTKEALDSDGWL------HTGDIGKWLPEGTLKIIDRKKHIF 560
Cdd:cd17651 327 A--------ALRpvppgvpGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQV 398
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 48256734 561 KLaQGEYVAPEKIENIYIRSEPVAQIYV------HGDslkAFLVGIVVPDPEVMP 609
Cdd:cd17651 399 KI-RGFRIELGEIEAALARHPGVREAVVlaredrPGE---KRLVAYVVGDPEAPV 449
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
121-605 |
7.45e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 74.54 E-value: 7.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGPGDH--VGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 201 DKPhkailLLEHVE--RKETPGLKLVILMEPFDDALRERGkkcGVDIKSMQAIEDSGqenhRVPVPPRPDDLSIVCfTSG 278
Cdd:PRK07798 107 ERE-----FAPRVAevLPRLPKLRTLVVVEDGSGNDLLPG---AVDYEDALAAGSPE----RDFGERSPDDLYLLY-TGG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 279 TTGNPKGAMLTHGNV-VADFSGFLKVTEKVIfprQDDVLIS----------FLPLAHMFERVIQSVVYchggrVGFFQGD 347
Cdd:PRK07798 174 TTGMPKGVMWRQEDIfRVLLGGRDFATGEPI---EDEEELAkraaagpgmrRFPAPPLMHGAGQWAAF-----AALFSGQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 348 IRLLSDDMKalrptifpVVPRLLNRMYDKifHQAdTSL-------KRWLLEFAAKRKQAEVRSgiirnnsiwdelffnki 420
Cdd:PRK07798 246 TVVLLPDVR--------FDADEVWRTIER--EKV-NVItivgdamARPLLDALEARGPYDLSS----------------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 421 qaslgghVRMIVTGAAPASPTV-LGFLRAALGCQVYEGYGQTECTAGCTFTTPGDwtSGHVGAPL--PCNHIKLVDaEEL 497
Cdd:PRK07798 298 -------LFAIASGGALFSPSVkEALLELLPNVVLTDSIGSSETGFGGSGTVAKG--AVHTGGPRftIGPRTVVLD-EDG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 498 NYWTsKGEGEICV--KGPNVFKGYLKDEDRTKEALDS-DG--WLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEK 572
Cdd:PRK07798 368 NPVE-PGSGEIGWiaRRGHIPLGYYKDPEKTAETFPTiDGvrYAIPGDRARVEADGTITLLGRGSVCINTG-GEKVFPEE 445
|
490 500 510
....*....|....*....|....*....|...
gi 48256734 573 IENIyIRSepvaqiyvHGDSLKAFLVGivVPDP 605
Cdd:PRK07798 446 VEEA-LKA--------HPDVADALVVG--VPDE 467
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
255-606 |
8.79e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 74.58 E-value: 8.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 255 GQENHRVPVPPRPDdlSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLkvtEKVIFPRQDDVLISflplAHMFerviqsvv 334
Cdd:PRK07788 196 GSSTAPLPKPPKPG--GIVILTSGTTGTPKGAPRPEPSPLAPLAGLL---SRVPFRAGETTLLP----APMF-------- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 335 ycHGgrVGFFQGDIRLlsddmkALRPTIfpVVPRLL---NRMYDKIFHQAD------TSLKRwLLEFAAKRKQA-EVRSg 404
Cdd:PRK07788 259 --HA--TGWAHLTLAM------ALGSTV--VLRRRFdpeATLEDIAKHKATalvvvpVMLSR-ILDLGPEVLAKyDTSS- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 405 iirnnsiwdelffnkiqaslgghVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECtAGCTFTTPGDWT--SGHVGA 482
Cdd:PRK07788 325 -----------------------LKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEV-AFATIATPEDLAeaPGTVGR 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 483 PLPCNHIKLVDAE--ELnywtSKGE-GEICVKGPNVFKGYLkdEDRTKEALdsDGWLHTGDIGKWLPEGTLKIIDRKKHI 559
Cdd:PRK07788 381 PPKGVTVKILDENgnEV----PRGVvGRIFVGNGFPFEGYT--DGRDKQII--DGLLSSGDVGYFDEDGLLFVDGRDDDM 452
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 48256734 560 FkLAQGEYVAPEKIENIYIRSEPVAQIYVHGdslkaflvgivVPDPE 606
Cdd:PRK07788 453 I-VSGGENVFPAEVEDLLAGHPDVVEAAVIG-----------VDDEE 487
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
130-605 |
1.27e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 73.92 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 130 AEFLGSGLLQHDCkvgteqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV--DKPhkai 207
Cdd:PRK07470 47 AALAARGVRKGDR-------ILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMIChaDFP---- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 208 lllEHVE--RKETPGLKLVIlmePFDDALRERGKKCGVDIKSMQAIEDSGQENhrvpvpprpDDLSIVCFTSGTTGNPKG 285
Cdd:PRK07470 116 ---EHAAavRAASPDLTHVV---AIGGARAGLDYEALVARHLGARVANAAVDH---------DDPCWFFFTSGTTGRPKA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 286 AMLTHG-------NVVADfsgflkvtekvIFP--RQDDVLISFLPLAHMfERVIQSVVYCHGGRVGFFQGDiRLLSDDMK 356
Cdd:PRK07470 181 AVLTHGqmafvitNHLAD-----------LMPgtTEQDASLVVAPLSHG-AGIHQLCQVARGAATVLLPSE-RFDPAEVW 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 357 AL----RPTIFPVVPRLLNRMY-DKIFHQADTSlkrwllefaakrkqaevrsgiirnnsiwdelffnkiqaSLgghvRMI 431
Cdd:PRK07470 248 ALverhRVTNLFTVPTILKMLVeHPAVDRYDHS--------------------------------------SL----RYV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 432 VTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-----GDWTSGHVGaplPCNH------IKLVDAE--ELn 498
Cdd:PRK07470 286 IYAGAPMYRADQKRALAKLGKVLVQYFGLGEVTGNITVLPPalhdaEDGPDARIG---TCGFertgmeVQIQDDEgrEL- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 499 ywtSKGE-GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENiy 577
Cdd:PRK07470 362 ---PPGEtGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPREIEE-- 434
|
490 500
....*....|....*....|....*...
gi 48256734 578 irsepvaQIYVHGDSLKAFLVGivVPDP 605
Cdd:PRK07470 435 -------KLLTHPAVSEVAVLG--VPDP 453
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
262-603 |
1.94e-13 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 73.39 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 262 PVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkvteKVIFP-RQDDVLISFLPLAHMFERV--IQSVVychg 338
Cdd:PRK09274 168 MADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEAL-----REDYGiEPGEIDLPTFPLFALFGPAlgMTSVI---- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 339 grvgffqgdirllsDDMKALRP-TIFPvvprllnrmyDKIFHQAD----TSLkrwlleFAA-----KRKQAEVRSGIIRN 408
Cdd:PRK09274 239 --------------PDMDPTRPaTVDP----------AKLFAAIErygvTNL------FGSpalleRLGRYGEANGIKLP 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 409 NsiwdelffnkiqaslgghVRMIVTGAAPASPTVLGFLRAAL--GCQVYEGYGQTECTAGCT-------FTTPGDWTSGH 479
Cdd:PRK09274 289 S------------------LRRVISAGAPVPIAVIERFRAMLppDAEILTPYGATEALPISSiesreilFATRAATDNGA 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 480 ---VGAPLPCNHIKLV--DAEELNYWT-----SKGE-GEICVKGPNVFKGYLKDEDRTKEA--LDSDG--WLHTGDIGkW 544
Cdd:PRK09274 351 gicVGRPVDGVEVRIIaiSDAPIPEWDdalrlATGEiGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLG-Y 429
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 48256734 545 L-PEGTLKIIDRKKHIFKLAQGEYVapekieniyirSEPVAQIY-VHGDSLKAFLVGIVVP 603
Cdd:PRK09274 430 LdAQGRLWFCGRKAHRVETAGGTLY-----------TIPCERIFnTHPGVKRSALVGVGVP 479
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
271-584 |
4.27e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 72.43 E-value: 4.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 271 SIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVgFFQG---D 347
Cdd:PRK07008 179 SSLCYTSGTTGNPKGALYSHRSTV--LHAYGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPLTGAKL-VLPGpdlD 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 348 IRLLSDDMKALRPTIFPVVPR----LLNRMydkifhqadtslkrwllefaakrKQAEVRSGIIRnnsiwdelffnkiqas 423
Cdd:PRK07008 256 GKSLYELIEAERVTFSAGVPTvwlgLLNHM-----------------------REAGLRFSTLR---------------- 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 424 lgghvRMIVTGAApASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPgdwTSGHVGAPLPCNH--------------I 489
Cdd:PRK07008 297 -----RTVIGGSA-CPPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLCKL---KWKHSQLPLDEQRkllekqgrviygvdM 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 490 KLVDAE--ELNyWTSKGEGEICVKGPNVFKGYLKDEDrtkEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEY 567
Cdd:PRK07008 368 KIVGDDgrELP-WDGKAFGDLQVRGPWVIDRYFRGDA---SPLV-DGWFPTGDVATIDADGFMQITDRSKDVIK-SGGEW 441
|
330
....*....|....*..
gi 48256734 568 VAPEKIENIYIRSEPVA 584
Cdd:PRK07008 442 ISSIDIENVAVAHPAVA 458
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
421-610 |
4.70e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 72.29 E-value: 4.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 421 QASLGGHVRMIVTGAAPAsPTVLGFLRAAlGCQVYEGYGQTEcTAG----CTFTtpGDWTS----------GHVGAPLPC 486
Cdd:PRK08162 292 RAGIDHPVHAMVAGAAPP-AAVIAKMEEI-GFDLTHVYGLTE-TYGpatvCAWQ--PEWDAlplderaqlkARQGVRYPL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 487 -NHIKLVDAEELNYWTSKGE--GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLA 563
Cdd:PRK08162 367 qEGVTVLDPDTMQPVPADGEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDII-IS 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 48256734 564 QGEYVAPEKIENIyirsepvaqIYVHgdslKAFLVGIVV--PDP---EVmPC 610
Cdd:PRK08162 445 GGENISSIEVEDV---------LYRH----PAVLVAAVVakPDPkwgEV-PC 482
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
427-598 |
5.71e-13 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 71.73 E-value: 5.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 427 HVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDaEELNYWTSKGEG 506
Cdd:cd05928 292 SLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIID-DNGNVLPPGTEG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 507 EICVK-GPN----VFKGYLKDEDRTKEALDSDGWLhTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSE 581
Cdd:cd05928 371 DIGIRvKPIrpfgLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYRIGPFEVESALIEHP 448
|
170 180
....*....|....*....|....
gi 48256734 582 PVAQIYV-------HGDSLKAFLV 598
Cdd:cd05928 449 AVVESAVvsspdpiRGEVVKAFVV 472
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
119-599 |
5.80e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 73.07 E-value: 5.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 119 QWLSYQEVAKRAEFLGSGLLqhDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGS-IRYIINTADICT 197
Cdd:PRK12316 2027 QHLSYAELDSRANRLAHRLR--ARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPL-DPNYPAErLAYMLEDSGAAL 2103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 198 VIVDkphkailllEHVERKETPGLKLVILmePFDDALrergkkcgvdiksmqAIEDSGQENHRVPVPprPDDLSIVCFTS 277
Cdd:PRK12316 2104 LLTQ---------RHLLERLPLPAGVARL--PLDRDA---------------EWADYPDTAPAVQLA--GENLAYVIYTS 2155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 278 GTTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPLAhmFERVIQSVVY--CHGGRVgffqgdirLLSDDM 355
Cdd:PRK12316 2156 GSTGLPKGVAVSHGALVA----HCQAAGERYELSPADCELQFMSFS--FDGAHEQWFHplLNGARV--------LIRDDE 2221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 356 KalrptifpvvpRLLNRMYDKIFHQADTslkrwLLEFAAKRKQAEVRSGIIRNNSIwdelffnkiqaslggHVRMIVTGA 435
Cdd:PRK12316 2222 L-----------WDPEQLYDEMERHGVT-----ILDFPPVYLQQLAEHAERDGRPP---------------AVRVYCFGG 2270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 436 APASPTVLGFLRAALGCQ-VYEGYGQTEctagcTFTTPGDWTSGH----------VGAPLPCNHIKLVDAeELNYWTSKG 504
Cdd:PRK12316 2271 EAVPAASLRLAWEALRPVyLFNGYGPTE-----AVVTPLLWKCRPqdpcgaayvpIGRALGNRRAYILDA-DLNLLAPGM 2344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 505 EGEICVKGPNVFKGYLKDEDRTKEALDSDGWLH-------TGDIGKWLPEGTLKIIDRKKHI-----FKLAQGEYVApEK 572
Cdd:PRK12316 2345 AGELYLGGEGLARGYLNRPGLTAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQvkirgFRIELGEIEA-RL 2423
|
490 500
....*....|....*....|....*...
gi 48256734 573 IENIYIRSEPV-AQIYVHGDSLKAFLVG 599
Cdd:PRK12316 2424 QAHPAVREAVVvAQDGASGKQLVAYVVP 2451
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
121-606 |
1.16e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 70.88 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:PRK13391 25 VTYRELDERSNRLAHLFRSLGLKRGDH--VAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALIT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 201 DKPHKAI--LLLEHVerketPGLKLVILMEPFDDalrergkkcgvdiksMQAIEDSGQENHRVPVPPRPDDL--SIVCFT 276
Cdd:PRK13391 103 SAAKLDVarALLKQC-----PGVRHRLVLDGDGE---------------LEGFVGYAEAVAGLPATPIADESlgTDMLYS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 277 SGTTGNPKG--AMLTHGNVVaDFSGFLKVTEKVIFPRQDDVLISFLPLAH----MFERVIQSVvychGGRV----GFfqg 346
Cdd:PRK13391 163 SGTTGRPKGikRPLPEQPPD-TPLPLTAFLQRLWGFRSDMVYLSPAPLYHsapqRAVMLVIRL----GGTVivmeHF--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 347 dirllsDDMKAL------RPTIFPVVPRLLNRMydkifhqadtsLKrwLLEfaAKRKQAEVRSgiirnnsiwdelffnki 420
Cdd:PRK13391 235 ------DAEQYLalieeyGVTHTQLVPTMFSRM-----------LK--LPE--EVRDKYDLSS----------------- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 421 qaslgghVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCN-HIKLVDAEEL 497
Cdd:PRK13391 277 -------LEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATE-GLGFTACDSEEWLAhpGTVGRAMFGDlHILDDDGAEL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 498 nywtSKGE-GEICVKGPNVFKgYLKDEDRTKEALDSDG-WLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIEN 575
Cdd:PRK13391 349 ----PPGEpGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMI-ISGGVNIYPQEAEN 422
|
490 500 510
....*....|....*....|....*....|.
gi 48256734 576 IYIRSEPVAQIYVHGdslkaflvgivVPDPE 606
Cdd:PRK13391 423 LLITHPKVADAAVFG-----------VPNED 442
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
274-590 |
1.62e-12 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 70.55 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 274 CFTSGTTGNPKGAMLTHgnvvadfsgflkvtekvifpRQDdvlisflplahmferVIQSVVYCHGGRVGFFQGDirllsd 353
Cdd:PRK06018 183 CYTSGTTGDPKGVLYSH--------------------RSN---------------VLHALMANNGDALGTSAAD------ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 354 dmkalrpTIFPVVPrllnrmydkIFHqADTslkrWLLEFAAKRKQAE-VRSGI-IRNNSIWDELFFNKIQASLG------ 425
Cdd:PRK06018 222 -------TMLPVVP---------LFH-ANS----WGIAFSAPSMGTKlVMPGAkLDGASVYELLDTEKVTFTAGvptvwl 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 426 -------------GHVRMIVTGAApASPTvlGFLRA--ALGCQVYEGYGQTECTAGCTFTT--------PGDWTSGHV-- 480
Cdd:PRK06018 281 mllqymekeglklPHLKMVVCGGS-AMPR--SMIKAfeDMGVEVRHAWGMTEMSPLGTLAAlkppfsklPGDARLDVLqk 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 481 -GAPLPCNHIKLVD--AEELNyWTSKGEGEICVKGPNVFKGYLKDEDrtkEALDSDGWLHTGDIGKWLPEGTLKIIDRKK 557
Cdd:PRK06018 358 qGYPPFGVEMKITDdaGKELP-WDGKTFGRLKVRGPAVAAAYYRVDG---EILDDDGFFDTGDVATIDAYGYMRITDRSK 433
|
330 340 350
....*....|....*....|....*....|...
gi 48256734 558 HIFKlAQGEYVAPEKIENIYIRSEPVAQIYVHG 590
Cdd:PRK06018 434 DVIK-SGGEWISSIDLENLAVGHPKVAEAAVIG 465
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
86-598 |
1.96e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 71.14 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 86 YDDARTMYQVFRRGLSISGNGPCLGFRKpeqpyQWLSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAEL 165
Cdd:PRK12316 3053 YPLERGVHRLFEEQVERTPDAVALAFGE-----QRLSYAELNRRANRLAHRLIERG--VGPDVLVGVAVERSLEMVVGLL 3125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 166 ACYTYSMVVVPLYDTLGPGSIRYIINTADIcTVIVDKPHKAILLLEHVErketpglklVILMEPFDDALRErgkkcgvdi 245
Cdd:PRK12316 3126 AILKAGGAYVPLDPEYPEERLAYMLEDSGA-QLLLSQSHLRLPLAQGVQ---------VLDLDRGDENYAE--------- 3186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 246 ksmqaiedsgqenHRVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNvvadFSGFLKVTEKVIFPRQDDVLISFLPLAHM 325
Cdd:PRK12316 3187 -------------ANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSA----LSNHLCWMQQAYGLGVGDRVLQFTTFSFD 3249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 326 FERVIQSVVYCHGGRVgfFQGDIRLLSDdmkalrptifpvvPRLLNRMYDKifHQADTSLKRWllefaakrkqaevrsgi 405
Cdd:PRK12316 3250 VFVEELFWPLMSGARV--VLAGPEDWRD-------------PALLVELINS--EGVDVLHAYP----------------- 3295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 406 irnnSIWDELFFNKIQASLGGHVRMIVTGAAPASPtvlGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGH--VGAP 483
Cdd:PRK12316 3296 ----SMLQAFLEEEDAHRCTSLKRIVCGGEALPAD---LQQQVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRP 3368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 484 LPCNHIKLVDAeELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGW------LHTGDIGKWLPEGTLKIIDRKK 557
Cdd:PRK12316 3369 IANRACYILDG-SLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVD 3447
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 48256734 558 HIFKLaQGEYVAPEKIENIYIRSEPV---AQIYVHGDSLKAFLV 598
Cdd:PRK12316 3448 HQVKI-RGFRIELGEIEARLLEHPWVreaVVLAVDGRQLVAYVV 3490
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
150-607 |
2.13e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 70.09 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 150 IGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIVDKPHKAIL--LLEHVERKETPGLKLVILM 227
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLdgLDPGVRVINVDSPAWADEL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 228 EPFDDALRErgkkcgvdiksmqaiedsgqenhrvPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVTEKV 307
Cdd:PRK07867 137 AAHRDAEPP-------------------------FRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVA--SAGVMLAQRFG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 308 IFPrqDDVLISFLPLAHMfERVIQ--SVVYCHGGRV---------GFFqgdirllsDDMKALRPTIFPVVPRLLN----- 371
Cdd:PRK07867 190 LGP--DDVCYVSMPLFHS-NAVMAgwAVALAAGASIalrrkfsasGFL--------PDVRRYGATYANYVGKPLSyvlat 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 372 --RMYDkifhqADTSLKrwllefaakrkqaevrsgiirnnsiwdelffnkiqaslgghvrmIVTGAAPASPTVLGFlRAA 449
Cdd:PRK07867 259 peRPDD-----ADNPLR--------------------------------------------IVYGNEGAPGDIARF-ARR 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 450 LGCQVYEGYGQTEctAGCTFTTPGDWTSGHVGaPLPCNhIKLVDAE----------ELNYWTSKGE--GEIC-VKGPNVF 516
Cdd:PRK07867 289 FGCVVVDGFGSTE--GGVAITRTPDTPPGALG-PLPPG-VAIVDPDtgtecppaedADGRLLNADEaiGELVnTAGPGGF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 517 KGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYVHGdslkaf 596
Cdd:PRK07867 365 EGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPIERILLRYPDATEVAVYA------ 436
|
490
....*....|.
gi 48256734 597 lvgivVPDPEV 607
Cdd:PRK07867 437 -----VPDPVV 442
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
262-598 |
2.33e-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: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 262 PVPPRPDDLSIVCFTSGTTGNPKGAMLTHGN--VVADFSGflkvtEKVIFPRQDDVLIS--------------FLPLA-- 323
Cdd:TIGR02262 155 PAATQADDPAFWLYSSGSTGMPKGVVHTHSNpyWTAELYA-----RNTLGIREDDVCFSaaklffayglgnalTFPMSvg 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 324 ----HMFERVIQSVVYchggrvgffqgdirllsDDMKALRPTIFPVVPRLLNRMYdkifhqADTSLKrwllefaaKRKQA 399
Cdd:TIGR02262 230 attvLMGERPTPDAVF-----------------DRLRRHQPTIFYGVPTLYAAML------ADPNLP--------SEDQV 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 400 EVRsgiirnnsiwdelffnkiqaslgghvrmIVTGAAPASPTVLGF-LRAALGCQVYEGYGQTEctAGCTFTT--PGDWT 476
Cdd:TIGR02262 279 RLR----------------------------LCTSAGEALPAEVGQrWQARFGVDIVDGIGSTE--MLHIFLSnlPGDVR 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 477 SGHVGAPLPCNHIKLVDaeELNYWTSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSdGWLHTGDigKWL--PEGTLKII 553
Cdd:TIGR02262 329 YGTSGKPVPGYRLRLVG--DGGQDVADGEpGELLISGPSSATMYWNNRAKSRDTFQG-EWTRSGD--KYVrnDDGSYTYA 403
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 48256734 554 DRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQIYVHG----DSL---KAFLV 598
Cdd:TIGR02262 404 GRTDDMLKVS-GIYVSPFEIESALIQHPAVLEAAVVGvadeDGLikpKAFVV 454
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
86-639 |
1.13e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 68.65 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 86 YDDARTMYQVFRRGLSISGNGPCLGFRKpeqpyQWLSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAEL 165
Cdd:PRK12467 1570 YPLARLVHQLIEDQAAATPEAVALVFGE-----QELTYGELNRRANRLAHRLIALG--VGPEVLVGIAVERSLEMVVGLL 1642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 166 ACYTYSMVVVPLYDTLGPGSIRYIINTADIctvivdkphkAILLLEHVERKETP---GLKLVILmEPFDDALrergkkcg 242
Cdd:PRK12467 1643 AILKAGGAYVPLDPEYPRERLAYMIEDSGI----------ELLLTQSHLQARLPlpdGLRSLVL-DQEDDWL-------- 1703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 243 vdiksmqaiedSGQENHRVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFsgflKVTEKVIFPRQDDVLISFLPL 322
Cdd:PRK12467 1704 -----------EGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRL----CATQEAYQLSAADVVLQFTSF 1768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 323 AhmFERVIQSVVY--CHGGRVgffqgdirLLSDDMKALRPTIFpvvPRLLNRMYDKIFHQADTSLKRwLLEFAAkrKQAE 400
Cdd:PRK12467 1769 A--FDVSVWELFWplINGARL--------VIAPPGAHRDPEQL---IQLIERQQVTTLHFVPSMLQQ-LLQMDE--QVEH 1832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 401 VRSgiirnnsiwdelffnkiqaslgghVRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAG-----CTFTTPGD 474
Cdd:PRK12467 1833 PLS------------------------LRRVVCGGEALEVEALRPWLERLPdTGLFNLYGPTETAVDvthwtCRRKDLEG 1888
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 475 WTSGHVGAPLPCNHIKLVDAeELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEAL------DSDGWLH-TGDIGKWLPE 547
Cdd:PRK12467 1889 RDSVPIGQPIANLSTYILDA-SLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgTVGSRLYrTGDLARYRAD 1967
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 548 GTLKIIDRKKHIFKLaQGEYVAPEKIENiYIRSEP----VAQIYVHGDSLKAfLVGIVVPDPEVMPCWAQKKgieGNYQE 623
Cdd:PRK12467 1968 GVIEYLGRIDHQVKI-RGFRIELGEIEA-RLREQGgvreAVVIAQDGANGKQ-LVAYVVPTDPGLVDDDEAQ---VALRA 2041
|
570
....*....|....*.
gi 48256734 624 LCKsKELKKAILDDMV 639
Cdd:PRK12467 2042 ILK-NHLKASLPEYMV 2056
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
121-557 |
1.92e-11 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 66.95 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGS-------IRYIINTA 193
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALGLKPGDR--VALIAETDGDFVEAFFACQYAGLVPVPLPLPMGFGGresyiaqLRGMLASA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 194 DICTVIVDKphkaiLLLEHVErKETPGLKLVILMEPFDDALRERGkkcGVDIKsmqaiedsgqenhrvpvPPRPDDLSIV 273
Cdd:PRK09192 128 QPAAIITPD-----ELLPWVN-EATHGNPLLHVLSHAWFKALPEA---DVALP-----------------RPTPDDIAYL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 274 CFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifpRQDDVLISFLPLAH-MferviqsvvychgGRVGFF------Qg 346
Cdd:PRK09192 182 QYSSGSTRFPRGVIITHRALMANLRAISHDGLKV---RPGDRCVSWLPFYHdM-------------GLVGFLltpvatQ- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 347 dirlLSDDMkaLRPTIFPVVP----RLLNR-----MYDKIFHqadtslkrwlLEFAAKRkqAEVRSGIIRNNSIWdelff 417
Cdd:PRK09192 245 ----LSVDY--LPTRDFARRPlqwlDLISRnrgtiSYSPPFG----------YELCARR--VNSKDLAELDLSCW----- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 418 nkiqaslgghvRMIVTGAAPASPTVL----------GF-LRAALGCqvyegYGQTECTAGCTFTTPG----------DWT 476
Cdd:PRK09192 302 -----------RVAGIGADMIRPDVLhqfaeafapaGFdDKAFMPS-----YGLAEATLAVSFSPLGsgivveevdrDRL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 477 SGH------------------VGAPLPCNHIKLVDA--EELNywtSKGEGEICVKGPNVFKGYLKDEDRTKeALDSDGWL 536
Cdd:PRK09192 366 EYQgkavapgaetrrvrtfvnCGKALPGHEIEIRNEagMPLP---ERVVGHICVRGPSLMSGYFRDEESQD-VLAADGWL 441
|
490 500
....*....|....*....|.
gi 48256734 537 HTGDIGkWLPEGTLKIIDRKK 557
Cdd:PRK09192 442 DTGDLG-YLLDGYLYITGRAK 461
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
119-639 |
3.53e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 66.90 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 119 QWLSYQEVAKRAEFLGSGLLQHDckVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGS-IRYIINTAdict 197
Cdd:PRK12316 4575 EKLTYAELNRRANRLAHALIARG--VGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPL-DPEYPRErLAYMMEDS---- 4647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 198 vivdkphKAILLLEHveRKETPGLklvilmePFDDalrergkkcGVDIKSMQAIED-SGQENHRVPVPPRPDDLSIVCFT 276
Cdd:PRK12316 4648 -------GAALLLTQ--SHLLQRL-------PIPD---------GLASLALDRDEDwEGFPAHDPAVRLHPDNLAYVIYT 4702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 277 SGTTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPLAhmFERVIQSV--VYCHGGRVgffqgdirLLSDD 354
Cdd:PRK12316 4703 SGSTGRPKGVAVSHGSLVN----HLHATGERYELTPDDRVLQFMSFS--FDGSHEGLyhPLINGASV--------VIRDD 4768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 355 MKALRPTIFpvvpRLLNRMYDKIFHQADTSLKRWLLEFAAKRKQAEVRsgiirnnsiwdelffnkiQASLGGHvrmivtG 434
Cdd:PRK12316 4769 SLWDPERLY----AEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLR------------------VYCFGGE------A 4820
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 435 AAPASPTVLgfLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSG----HVGAPLPCNHIKLVDaEELNYWTSKGEGEIC 509
Cdd:PRK12316 4821 VAQASYDLA--WRALKPVYLFNGYGPTETTVTVLlWKARDGDACGaaymPIGTPLGNRSGYVLD-GQLNPLPVGVAGELY 4897
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 510 VKGPNVFKGYLKDEDRTKEALDSD------GWLH-TGDIGKWLPEGTLKIIDRKKHI-----FKLAQGEYVAPEKiENIY 577
Cdd:PRK12316 4898 LGGEGVARGYLERPALTAERFVPDpfgapgGRLYrTGDLARYRADGVIDYLGRVDHQvkirgFRIELGEIEARLR-EHPA 4976
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 48256734 578 IRSEPVaqIYVHGdSLKAFLVGIVVP-DPEVMPCWAQKKGIEGNYQELckskeLKKAILDDMV 639
Cdd:PRK12316 4977 VREAVV--IAQEG-AVGKQLVGYVVPqDPALADADEAQAELRDELKAA-----LRERLPEYMV 5031
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
119-613 |
3.55e-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: 65.85 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 119 QWLSYQEVAKRAEFLGSGLLQHdcKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIIntadictv 198
Cdd:cd17649 11 QSLSYAELDARANRLAHRLRAL--GVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 199 ivdkphkailllehverketpglklvilmepfddalrergkkcgvdiksmqaiEDSGqenHRVPVPPRPDDLSIVCFTSG 278
Cdd:cd17649 81 -----------------------------------------------------EDSG---AGLLLTHHPRQLAYVIYTSG 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 279 TTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPL----AHmfERVIQSVVycHGGRVgffqgdirllsdd 354
Cdd:cd17649 105 STGTPKGVAVSHGPLAA----HCQATAERYGLTPGDRELQFASFnfdgAH--EQLLPPLI--CGACV------------- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 355 mkALRPTIFPVVPRLLNRMYDK----IFHQADTSLKRWLLEFAAKrkqaevrsgiirnnsiwdelffnkiQASLGGHVRM 430
Cdd:cd17649 164 --VLRPDELWASADELAEMVRElgvtVLDLPPAYLQQLAEEADRT-------------------------GDGRPPSLRL 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 431 IVTGAAPASPTvlgFLRAALGCQVY--EGYGQTECTAGCT-FTTPGD----WTSGHVGAPLPCNHIKLVDAeELNYWTSK 503
Cdd:cd17649 217 YIFGGEALSPE---LLRRWLKAPVRlfNAYGPTEATVTPLvWKCEAGaaraGASMPIGRPLGGRSAYILDA-DLNPVPVG 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 504 GEGEICVKGPNVFKGYLKDEDRTKEAL--DSDG-----WLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENI 576
Cdd:cd17649 293 VTGELYIGGEGLARGYLGRPELTAERFvpDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-RGFRIELGEIEAA 371
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 48256734 577 YIRSEPVAQIYV---HGDSLKAfLVGIVVP-DPEVMPCWAQ 613
Cdd:cd17649 372 LLEHPGVREAAVvalDGAGGKQ-LVAYVVLrAAAAQPELRA 411
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
267-609 |
3.90e-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: 65.92 E-value: 3.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVTEKVIFPRQDDVLISFLPLAhmFERVIQS--VVYCHGGRVgff 344
Cdd:cd17644 105 PENLAYVIYTSGSTGKPKGVMIEHQSLV----NLSHGLIKEYGITSSDRVLQFASIA--FDVAAEEiyVTLLSGATL--- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 345 qgdirllsddmkALRPT-IFPVVPRllnrMYDKIfhqadtslkrwllefaaKRKQAEVRSgiiRNNSIWDELFFNKIQAS 423
Cdd:cd17644 176 ------------VLRPEeMRSSLED----FVQYI-----------------QQWQLTVLS---LPPAYWHLLVLELLLST 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 424 LGG--HVRMIVTGAAPASPTVLGFLRAALG--CQVYEGYGQTECTAGCTFTTPGDWTSGH-----VGAPLPCNHIKLVDa 494
Cdd:cd17644 220 IDLpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIANTQVYILD- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 495 EELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLH--------TGDIGKWLPEGTLKIIDRKKHIFKLaQGE 566
Cdd:cd17644 299 ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKI-RGF 377
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 48256734 567 YVAPEKIENIYIRSEPVAQ--IYVHGDSL-KAFLVGIVVPDPEVMP 609
Cdd:cd17644 378 RIELGEIEAVLSQHNDVKTavVIVREDQPgNKRLVAYIVPHYEESP 423
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
121-607 |
5.62e-11 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 65.49 E-value: 5.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSGLLQHDCKVGteQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINtadictviv 200
Cdd:PRK12406 12 RSFDELAQRAARAAGGLAALGVRPG--DCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILE--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 201 DKPHKAIL----LLEHVERKETPGLKLVILMEP--------FDDALRErGKKCGVDIKSMQAiedsGQENHRVPVPPRPD 268
Cdd:PRK12406 81 DSGARVLIahadLLHGLASALPAGVTVLSVPTPpeiaaayrISPALLT-PPAGAIDWEGWLA----QQEPYDGPPVPQPQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 269 DLsivCFTSGTTGNPKGAMLTHGNVvadfsGFLKVTEKVI-----FPRQDDVLISFlPLAHmferviqSVVYCHGGRVGF 343
Cdd:PRK12406 156 SM---IYTSGTTGHPKGVRRAAPTP-----EQAAAAEQMRaliygLKPGIRALLTG-PLYH-------SAPNAYGLRAGR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 344 FQGDIRLLS----DDMKAL----RPTIFPVVPRLLNRmydkifhqadtslkrwLLEFAAKRKQAEVRSgiirnnsiwdel 415
Cdd:PRK12406 220 LGGVLVLQPrfdpEELLQLierhRITHMHMVPTMFIR----------------LLKLPEEVRAKYDVS------------ 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 416 ffnkiqaSLgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCNHIKLVD 493
Cdd:PRK12406 272 -------SL----RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE-SGAVTFATSEDALShpGTVGKAAPGAELRFVD 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 494 AE--ELnywtSKGE-GEICVKGPNV--FKGYLKDEDRTkeALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYV 568
Cdd:PRK12406 340 EDgrPL----PQGEiGEIYSRIAGNpdFTYHNKPEKRA--EIDRGGFITSGDVGYLDADGYLFLCDRKRDMV-ISGGVNI 412
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 48256734 569 APEKIENIYIRSEPVAQIYVHGDSLKAF---LVGIVVPDPEV 607
Cdd:PRK12406 413 YPAEIEAVLHAVPGVHDCAVFGIPDAEFgeaLMAVVEPQPGA 454
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
121-635 |
8.48e-11 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 64.92 E-value: 8.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSGLLQHDCKVGTEQFIgvFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADiCTVIV 200
Cdd:PRK04319 74 YTYKELKELSNKFANVLKELGVEKGDRVFI--FMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSE-AKVLI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 201 DKPhkaiLLLEHVERKETPGLKLVILMepfdDALRERGKKCgVDIKSMQAiedsgQENHRVPVPP-RPDDLSIVCFTSGT 279
Cdd:PRK04319 151 TTP----ALLERKPADDLPSLKHVLLV----GEDVEEGPGT-LDFNALME-----QASDEFDIEWtDREDGAILHYTSGS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 280 TGNPKGAMLTHGNVVADFsgflkVTEKVIFP-RQDDVL---------------IsFLPLAHMfervIQSVVYchGGRvgf 343
Cdd:PRK04319 217 TGKPKGVLHVHNAMLQHY-----QTGKYVLDlHEDDVYwctadpgwvtgtsygI-FAPWLNG----ATNVID--GGR--- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 344 FQGD--IRLLSDdmkaLRPTIF---PVVPRLLNRMYDKIFHQADTSlkrwllefaakrkqaevrsgiirnnsiwdelffn 418
Cdd:PRK04319 282 FSPErwYRILED----YKVTVWytaPTAIRMLMGAGDDLVKKYDLS---------------------------------- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 419 kiqaslggHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPCNHIKLVDAEEl 497
Cdd:PRK04319 324 --------SLRHILSVGEPLNPEVVRWGMKVFGLPIHDNWWMTETGGIMIANYPAmDIKPGSMGKPLPGIEAAIVDDQG- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 498 NYWTSKGEGEICVKG--PNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIEN 575
Cdd:PRK04319 395 NELPPNRMGNLAIKKgwPSMMRGIWNNPEKYESYF-AGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTS-GERVGPFEVES 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 48256734 576 IYIRSEPVAQIYVhgdslkaflvgIVVPDP---EVMPCW-AQKKGIEGnyqelckSKELKKAIL 635
Cdd:PRK04319 473 KLMEHPAVAEAGV-----------IGKPDPvrgEIIKAFvALRPGYEP-------SEELKEEIR 518
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
435-606 |
1.00e-10 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 64.71 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 435 AAPASPTVLGFLRAALGCQVYEGYGQTECTaGCTFTTPGDWTS--GHVGAPLPCN-HIKLVDAEELnywtSKGE-GEICV 510
Cdd:cd05929 253 AAPCPPWVKEQWIDWGGPIIWEYYGGTEGQ-GLTIINGEEWLThpGSVGRAVLGKvHILDEDGNEV----PPGEiGEVYF 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 511 KGPNVFKgYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRsepvaqiyvHG 590
Cdd:cd05929 328 ANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIA---------HP 396
|
170
....*....|....*.
gi 48256734 591 DSLKAFLVGivVPDPE 606
Cdd:cd05929 397 KVLDAAVVG--VPDEE 410
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
121-606 |
1.43e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 64.15 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSGLLQHDCKVGteQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREG--DVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 201 dkpHKAILLLEHVERKETP-GLKLVILM-------EPFDDALrergkkcgvdiksmqaiedSGQENHRVPVPPRPDDLSi 272
Cdd:PRK08276 90 ---SAALADTAAELAAELPaGVPLLLVVagpvpgfRSYEEAL-------------------AAQPDTPIADETAGADML- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 273 vcFTSGTTGNPKGAM--LTHGNVVADFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRV----GFfqg 346
Cdd:PRK08276 147 --YSSGTTGRPKGIKrpLPGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAPLRFGMSALALGGTVvvmeKF--- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 347 dirllsDDMKAL------RPTIFPVVPRLLNRMydkifhqadtsLKrwLLEfaakrkqaEVRSGiirnnsiWDelffnki 420
Cdd:PRK08276 222 ------DAEEALalieryRVTHSQLVPTMFVRM-----------LK--LPE--------EVRAR-------YD------- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 421 QASLgghvRMIVTGAAPASPTVLgflRAAL---GCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCN-HIKLVDA 494
Cdd:PRK08276 261 VSSL----RVAIHAAAPCPVEVK---RAMIdwwGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGEvRILDEDG 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 495 EELnywtSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGkWLPE-GTLKIIDRKKHIFkLAQGEYVAPEK 572
Cdd:PRK08276 333 NEL----PPGEiGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVG-YLDEdGYLYLTDRKSDMI-ISGGVNIYPQE 406
|
490 500 510
....*....|....*....|....*....|....
gi 48256734 573 IENIYIRSEPVAQIYVHGdslkaflvgivVPDPE 606
Cdd:PRK08276 407 IENLLVTHPKVADVAVFG-----------VPDEE 429
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
428-598 |
1.80e-10 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 64.10 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 428 VRMIVTGAAPaSPTVLgFLRAALGCQVYEGYGQTEcTAG----CTFTTPGDWTSGHVGAPLPCNH-IKLVDAEELNYWTS 502
Cdd:PLN02479 313 VHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSE-TYGpstvCAWKPEWDSLPPEEQARLNARQgVRYIGLEGLDVVDT 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 503 KGE----------GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEK 572
Cdd:PLN02479 390 KTMkpvpadgktmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGGENISSLE 467
|
170 180
....*....|....*....|....*.
gi 48256734 573 IENIyirsepvaqIYVHGDSLKAFLV 598
Cdd:PLN02479 468 VENV---------VYTHPAVLEASVV 484
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
121-585 |
2.41e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 64.42 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSGLlQHDCKVGtEQFIGVFAQNrPEWIIAELACYTYSMVVVPLYDtlgPGSIRyiintadictviv 200
Cdd:PRK05691 41 LSYRDLDLRARTIAAAL-QARASFG-DRAVLLFPSG-PDYVAAFFGCLYAGVIAVPAYP---PESAR------------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 201 dkPHKAILLLEHVERKETpglKLVILMEPFDDALRERGKKCGVDIKSMQAIE--DSGQENHRVPVPPRPDDLSIVCFTSG 278
Cdd:PRK05691 102 --RHHQERLLSIIADAEP---RLLLTVADLRDSLLQMEELAAANAPELLCVDtlDPALAEAWQEPALQPDDIAFLQYTSG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 279 TTGNPKGAMLTHGNVVADFS----GFlkvtekVIFPRQDDVLISFLPLAHMFERV------IQSVVYCHGGRVGFFQG-D 347
Cdd:PRK05691 177 STALPKGVQVSHGNLVANEQlirhGF------GIDLNPDDVIVSWLPLYHDMGLIggllqpIFSGVPCVLMSPAYFLErP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 348 IRLLsDDMKALRPTI-----FPVvpRLLN-RMYDKIFHQADtsLKRWLLEFAAkrkqaevrSGIIRNNSIwdELFFNKIQ 421
Cdd:PRK05691 251 LRWL-EAISEYGGTIsggpdFAY--RLCSeRVSESALERLD--LSRWRVAYSG--------SEPIRQDSL--ERFAEKFA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 422 ----------ASLG-GHVRMIVTGAAPA-SPTVLGFLRAALGCQVYEGyGQTECTAGCTFTTPGdwtsghvgaplpcNHI 489
Cdd:PRK05691 316 acgfdpdsffASYGlAEATLFVSGGRRGqGIPALELDAEALARNRAEP-GTGSVLMSCGRSQPG-------------HAV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 490 KLVDAEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEA---LDSDGWLHTGDIGkWLPEGTLKIIDRKKHIFkLAQGE 566
Cdd:PRK05691 382 LIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfveHDGRTWLRTGDLG-FLRDGELFVTGRLKDML-IVRGH 459
|
490
....*....|....*....
gi 48256734 567 YVAPEKIENIYIRSEPVAQ 585
Cdd:PRK05691 460 NLYPQDIEKTVEREVEVVR 478
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
86-606 |
2.78e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 64.21 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 86 YDDARTMYQVFRRGLSISGNGPCLGFRKpeqpyQWLSYQEVAKRAEFLGSGLLQhdCKVGTEQFIGVFAQNRPEWIIAEL 165
Cdd:PRK12316 507 YPLQRGVHRLFEEQVERTPEAPALAFGE-----ETLDYAELNRRANRLAHALIE--RGVGPDVLVGVAMERSIEMVVALL 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 166 ACYTYSMVVVPLYDTLGPGSIRYIINTADIctvivdkphkAILLLEHVERKETP---GLKLVILMEPfddalrergkkcg 242
Cdd:PRK12316 580 AILKAGGAYVPLDPEYPAERLAYMLEDSGV----------QLLLSQSHLGRKLPlaaGVQVLDLDRP------------- 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 243 vdiksmqAIEDSGQENHRVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLK---------VTEKVIFPRQD 313
Cdd:PRK12316 637 -------AAWLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQayglgvgdtVLQKTPFSFDV 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 314 DVLISFLPLAhmferviqsvvycHGGR-VGFFQGDIRllsdDMKALrptifpvvPRLLNRmydkifHQADTslkrwlLEF 392
Cdd:PRK12316 710 SVWEFFWPLM-------------SGARlVVAAPGDHR----DPAKL--------VELINR------EGVDT------LHF 752
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 393 AAKRKQAEVRSGIIrnnsiwdelffnkiqASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP 472
Cdd:PRK12316 753 VPSMLQAFLQDEDV---------------ASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTC 817
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 473 GDWTSGHV--GAPLPCNHIKLVDAeELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEAL------DSDGWLHTGDIGKW 544
Cdd:PRK12316 818 VEEGGDSVpiGRPIANLACYILDA-NLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFvpspfvAGERMYRTGDLARY 896
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 48256734 545 LPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAfLVGIVVPDPE 606
Cdd:PRK12316 897 RADGVIEYAGRIDHQVKL-RGLRIELGEIEARLLEHPWVREAAVLAVDGKQ-LVGYVVLESE 956
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
121-609 |
4.04e-10 |
|
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: 62.66 E-value: 4.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSGLLqhDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGS-IRYIINTADictvi 199
Cdd:cd17652 13 LTYAELNARANRLARLLA--ARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPL-DPAYPAErIAYMLADAR----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 200 vdkphkAILLLEHverketpglklvilmepfddalrergkkcgvdiksmqaiedsgqenhrvpvpprPDDLSIVCFTSGT 279
Cdd:cd17652 85 ------PALLLTT------------------------------------------------------PDNLAYVIYTSGS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 280 TGNPKGAMLTH---GNVVADFSGFLKVTEkvifprqDDVLISFLPLAhmFERVIQSVV--YCHGGRVGFFQGDIRL---- 350
Cdd:cd17652 105 TGRPKGVVVTHrglANLAAAQIAAFDVGP-------GSRVLQFASPS--FDASVWELLmaLLAGATLVLAPAEELLpgep 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 351 LSDDMKALRPTIFPVVPRLLNRMYDkifhqadtslkrwllefaakrkqaevrsgiirnnsiwDELffnkiqasLGGHVrM 430
Cdd:cd17652 176 LADLLREHRITHVTLPPAALAALPP-------------------------------------DDL--------PDLRT-L 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 431 IVTGAAPASPTVLgflRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLVDAeELNYWTSKGEGEIC 509
Cdd:cd17652 210 VVAGEACPAELVD---RWAPGRRMINAYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYVLDA-RLRPVPPGVPGELY 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 510 VKGPNVFKGYLKDEDRTKEALDSD------GWLH-TGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEP 582
Cdd:cd17652 286 IAGAGLARGYLNRPGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKI-RGFRIELGEVEAALTEHPG 364
|
490 500 510
....*....|....*....|....*....|
gi 48256734 583 VAQ--IYVHGDSL-KAFLVGIVVPDPEVMP 609
Cdd:cd17652 365 VAEavVVVRDDRPgDKRLVAYVVPAPGAAP 394
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
275-590 |
1.06e-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: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 275 FTSGTTGNPKGAMLTHGNVVADFsgflKVTEKVIFPRQDDVLISFLPLAH-MFERVIQSVVYCHGGRVGFFQGDIRLLSD 353
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESF----VCNEDLFNISGEDAILAPGPLSHsLFLYGAISALYLGGTFIGQRKFNPKSWIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 354 DMKALRPTIFPVVPRLLnrmydkifhqadtslkrwllefaakrkQAEVRSGIIRNnsiwdelffnkiqaslggHVRMIVT 433
Cdd:cd17633 83 KINQYNATVIYLVPTML---------------------------QALARTLEPES------------------KIKSIFS 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 434 GAAPASPTVLGFLRAAL-GCQVYEGYGQTEcTAGCTFTTPGD-WTSGHVGAPLPCNHIKLVDAEelnywtSKGEGEICVK 511
Cdd:cd17633 118 SGQKLFESTKKKLKNIFpKANLIEFYGTSE-LSFITYNFNQEsRPPNSVGRPFPNVEIEIRNAD------GGEIGKIFVK 190
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 48256734 512 GPNVFKGYLKDEDRTKealdsDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYVHG 590
Cdd:cd17633 191 SEMVFSGYVRGGFSNP-----DGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIEEAIVVG 263
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
109-607 |
1.46e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 61.20 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 109 LGFRKPEQPYQWLSY-QEVAKRAEFLgSGLLQHDCKVgteqFIGVFAQNRPEWII----AELACYTysmvVVPLYDTLGP 183
Cdd:PRK13388 18 IAVRYGDRTWTWREVlAEAAARAAAL-IALADPDRPL----HVGVLLGNTPEMLFwlaaAALGGYV----LVGLNTTRRG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 184 GSIRYIINTADICTVIVDKPHKAilLLEHVErkeTPGLKLVILMEPfddALRERgkkcgvdiksmqaIEDSGQEN-HRvp 262
Cdd:PRK13388 89 AALAADIRRADCQLLVTDAEHRP--LLDGLD---LPGVRVLDVDTP---AYAEL-------------VAAAGALTpHR-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 263 vPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLkVTEKVIFPRqDDVLISFLPLAH----MferVIQSVVYCHG 338
Cdd:PRK13388 146 -EVDAMDPFMLIFTSGTTGAPKAVRCSHGRLA--FAGRA-LTERFGLTR-DDVCYVSMPLFHsnavM---AGWAPAVASG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 339 GRVgffqgdirllsddmkALRPTifpvvprllnrmydkifhqadtslkrwlleFAAKRKQAEVRSgiirnnsiWDELFFN 418
Cdd:PRK13388 218 AAV---------------ALPAK------------------------------FSASGFLDDVRR--------YGATYFN 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 419 KIQASLGghvRMIVTGAAP---ASPTVLGFLRAA-----------LGCQVYEGYGQTEctAGCTFTTPGDWTSGHVGAPL 484
Cdd:PRK13388 245 YVGKPLA---YILATPERPddaDNPLRVAFGNEAsprdiaefsrrFGCQVEDGYGSSE--GAVIVVREPGTPPGSIGRGA 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 485 P------------C------NHIKLVDAEElnywtskGEGEICVK-GPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWL 545
Cdd:PRK13388 320 PgvaiynpetlteCavarfdAHGALLNADE-------AIGELVNTaGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRD 391
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 48256734 546 PEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYVHGdslkaflvgivVPDPEV 607
Cdd:PRK13388 392 ADGWIYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYA-----------VPDERV 441
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
451-609 |
2.83e-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: 59.88 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 451 GCQVYEGYGQTECTAGCT-FTTPGDWTSGHVGAPLPCNHIKLVDaEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEA 529
Cdd:cd17645 234 GYKLVNNYGPTENTVVATsFEIDKPYANIPIGKPIDNTRVYILD-EALQLQPIGVAGELCIAGEGLARGYLNRPELTAEK 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 530 LDSDGWL------HTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPV---AQIYVHGDSLKAFLVGI 600
Cdd:cd17645 313 FIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIEPFLMNHPLIelaAVLAKEDADGRKYLVAY 391
|
....*....
gi 48256734 601 VVPDPEVMP 609
Cdd:cd17645 392 VTAPEEIPH 400
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
271-636 |
3.41e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 59.64 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 271 SIVCFTSGTTGNPKG--------AMLTHGN-VVADFSGFLKVTEKvifprqdDVLISFLPLAHMFERVIQSVVYCHGGRV 341
Cdd:PRK13390 151 AVMLYSSGTTGFPKGiqpdlpgrDVDAPGDpIVAIARAFYDISES-------DIYYSSAPIYHAAPLRWCSMVHALGGTV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 342 GFFQG-DIRLLSDDMKALRPTIFPVVPRLLNRMYdkifhqadtslkrwllefaakRKQAEVRSGiirnnsiWDelffnki 420
Cdd:PRK13390 224 VLAKRfDAQATLGHVERYRITVTQMVPTMFVRLL---------------------KLDADVRTR-------YD------- 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 421 QASLgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVG-APLPCNHIKLVDAEEL 497
Cdd:PRK13390 269 VSSL----RAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGrSVLGDLHICDDDGNEL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 498 nywtSKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDG--WLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIE 574
Cdd:PRK13390 344 ----PAGRiGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQETE 418
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 48256734 575 NIYIRSEPVAQIYVHGdslkaflvgivVPDPEVmpcWAQKKGIEGNYQELCKSKELKKAILD 636
Cdd:PRK13390 419 NALTMHPAVHDVAVIG-----------VPDPEM---GEQVKAVIQLVEGIRGSDELARELID 466
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
268-592 |
3.64e-09 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 59.80 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 268 DDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVT-EKVIFPRQDDVLiSFLPLAhmFERVIQSVV--YCHGGRvgff 344
Cdd:cd17656 128 DDLLYIIYTSGTTGKPKGVQLEHKNMV----NLLHFErEKTNINFSDKVL-QFATCS--FDVCYQEIFstLLSGGT---- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 345 qgdIRLLSDDMKALRPTIFPVVPRllnrmydkifHQADT-SLKRWLLEFAAKRKQAEVRsgiirnnsiwdelFFNKIQAS 423
Cdd:cd17656 197 ---LYIIREETKRDVEQLFDLVKR----------HNIEVvFLPVAFLKFIFSEREFINR-------------FPTCVKHI 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 424 LGGHVRMIVTgaapaSPTVLGFLRAalGCQVYEGYG--QTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDaEELNYW 500
Cdd:cd17656 251 ITAGEQLVIT-----NEFKEMLHEH--NVHLHNHYGpsETHVVTTYTINPEAEIPElPPIGKPISNTWIYILD-QEQQLQ 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 501 TSKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGW------LHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIE 574
Cdd:cd17656 323 PQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-RGYRIELGEIE 401
|
330 340
....*....|....*....|
gi 48256734 575 NIYIRSEPVAQ--IYVHGDS 592
Cdd:cd17656 402 AQLLNHPGVSEavVLDKADD 421
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
267-609 |
5.40e-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: 5.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSG--FLKVTEkvifprqDDVLISFLplAHMFE-RVIQSVVYCHGGR 340
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVnlrTSLSEryFGRDNG-------DEAVLFFS--NYVFDfFVEQMTLALLNGQ 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 341 vgffqgDIRLLSDDMKALRPTIFPVV-----------PRLLnRMYDkiFHQAdTSLKRWLL---EFAAKRkqaevrsgii 406
Cdd:cd17648 164 ------KLVVPPDEMRFDPDRFYAYInrekvtylsgtPSVL-QQYD--LARL-PHLKRVDAageEFTAPV---------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 407 rnnsiwdelfFNKIQASLGGhvrmivtgaapasptvlgflraalgcQVYEGYGQTEC--TAGCTFTTPGDWTSGHVGAPL 484
Cdd:cd17648 224 ----------FEKLRSRFAG--------------------------LIINAYGPTETtvTNHKRFFPGDQRFDKSLGRPV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 485 PCNHIKLVDAEeLNYWTSKGEGEICVKGPNVFKGYLKDEDRTKE-------------ALDSDGWLH-TGDIGKWLPEGTL 550
Cdd:cd17648 268 RNTKCYVLNDA-MKRVPVGAVGELYLGGDGVARGYLNRPELTAErflpnpfqteqerARGRNARLYkTGDLVRWLPSGEL 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 48256734 551 KIIDRKKHIFKLaQGEYVAPEKIENIY-----IRSEPVAQIYVHGDSLKA---FLVGIVVPDPEVMP 609
Cdd:cd17648 347 EYLGRNDFQVKI-RGQRIEPGEVEAALasypgVRECAVVAKEDASQAQSRiqkYLVGYYLPEPGHVP 412
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
121-607 |
5.60e-09 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 59.25 E-value: 5.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIV 200
Cdd:PRK05857 42 LRYRELVAEVGGLAADLRAQSVSRGSR--VLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 201 DKPHKailllehVERKETPGLKLVILMEPFDDALRERGKKCGVDIKSMQAIEDSGQenhrvpvpprpDDLSIVCFTSGTT 280
Cdd:PRK05857 120 APGSK-------MASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNADQGS-----------EDPLAMIFTSGTT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 281 GNPKGAMLTHGNVVA--DF---SGFLKVTEKVifprqDDVLISFLPLAHMFErvIQSVVYC--HGGR--VGFFQGD--IR 349
Cdd:PRK05857 182 GEPKAVLLANRTFFAvpDIlqkEGLNWVTWVV-----GETTYSPLPATHIGG--LWWILTClmHGGLcvTGGENTTslLE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 350 LLSDDMKALRPtifpVVPRLLNRMYDKIfhqadtslkrwllefaakrkqaevrsgiirnnsiwdelffnKIQASLGGHVR 429
Cdd:PRK05857 255 ILTTNAVATTC----LVPTLLSKLVSEL-----------------------------------------KSANATVPSLR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 430 MIVTGAAPASPTVLGFLRAA--LGCQVYeGYGQTECTAGCTFTTPGDWT---SGHVGAPLPCNHIKLVDAEELNYWTSKG 504
Cdd:PRK05857 290 LVGYGGSRAIAADVRFIEATgvRTAQVY-GLSETGCTALCLPTDDGSIVkieAGAVGRPYPGVDVYLAATDGIGPTAPGA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 505 E-----GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIyir 579
Cdd:PRK05857 369 GpsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGGVNIAPDEVDRI--- 443
|
490 500 510
....*....|....*....|....*....|....
gi 48256734 580 SEPVAQI-----YVHGDSLKAFLVGI-VVPDPEV 607
Cdd:PRK05857 444 AEGVSGVreaacYEIPDEEFGALVGLaVVASAEL 477
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
255-576 |
2.71e-08 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 57.08 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 255 GQENHRVPVPPRPD-DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkVTEKVIFPRQDDVLISFLPLAH-Mferviqs 332
Cdd:PRK05851 138 AHTNRSASLTPPDSgGPAVLQGTAGSTGTPRTAILSPGAVLSNLRG---LNARVGLDAATDVGCSWLPLYHdM------- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 333 vvychggrvgffqGDIRLLSDDMKA----LRPT-IFPVVP-RLLNrmydkifhqadtslkrWLLEFAAKRKQA-EVRSGI 405
Cdd:PRK05851 208 -------------GLAFLLTAALAGaplwLAPTtAFSASPfRWLS----------------WLSDSRATLTAApNFAYNL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 406 IRNNSiwdelffNKIQASLGGHVRMIVTGAAP----------ASPTVLGFLRAALGcqvyEGYGQTECTAGCTFTTPG-- 473
Cdd:PRK05851 259 IGKYA-------RRVSDVDLGALRVALNGGEPvdcdgferfaTAMAPFGFDAGAAA----PSYGLAESTCAVTVPVPGig 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 474 ---------DWTSGH----VGAPLPCNHIKLVDAEELNYWTSKGEGEICVKGPNVFKGYLKDedrtkEALDSDGWLHTGD 540
Cdd:PRK05851 328 lrvdevttdDGSGARrhavLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQ-----APIDPDDWFPTGD 402
|
330 340 350
....*....|....*....|....*....|....*.
gi 48256734 541 IGkWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENI 576
Cdd:PRK05851 403 LG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERV 436
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
422-606 |
3.48e-08 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 56.37 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 422 ASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEC-TAGCTFTTPGDWT-SGHVGAPLPCNHIKLVDaEELNy 499
Cdd:cd05973 201 ARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELgMVLANHHALEHPVhAGSAGRAMPGWRVAVLD-DDGD- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 500 wtSKGEGEICVKGPNV-------FKGYLKDEDRTKealdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEK 572
Cdd:cd05973 279 --ELGPGEPGRLAIDIansplmwFRGYQLPDTPAI----DGGYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFD 351
|
170 180 190
....*....|....*....|....*....|....
gi 48256734 573 IENIYIRSEPVAQIYVhgdslkaflvgIVVPDPE 606
Cdd:cd05973 352 VESALIEHPAVAEAAV-----------IGVPDPE 374
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
429-605 |
8.74e-08 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 55.38 E-value: 8.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 429 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctaGCTFTTPGDWTSGHV----GAPL-PCNHIKLVDAE--ELnywt 501
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAE---GLVNYTRLDDSDERIfttqGRPMsPDDEVWVADADgnPL---- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 502 SKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHifklaQ----GEYVAPEKIENI 576
Cdd:PRK10946 376 PQGEvGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGEKIAAEEIENL 450
|
170 180
....*....|....*....|....*....
gi 48256734 577 YIRsepvaqiyvHGDSLKAFLVGIvvPDP 605
Cdd:PRK10946 451 LLR---------HPAVIHAALVSM--EDE 468
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
428-598 |
1.16e-07 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 55.04 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 428 VRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTEctAGCTFT--TPGDWTSGHVGAPLPCNHIKLVdAEELNYWTSKG 504
Cdd:PRK06060 262 LRCVVSAGEALELGLAERLMEFFGgIPILDGIGSTE--VGQTFVsnRVDEWRLGTLGRVLPPYEIRVV-APDGTTAGPGV 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 505 EGEICVKGPNVFKGYLkdeDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIfKLAQGEYVAPEKIENIYIRSEPVA 584
Cdd:PRK06060 339 EGDLWVRGPAIAKGYW---NRPDSPVANEGWLDTRDRVCIDSDGWVTYRCRADDT-EVIGGVNVDPREVERLIIEDEAVA 414
|
170 180
....*....|....*....|.
gi 48256734 585 QIYVHG-------DSLKAFLV 598
Cdd:PRK06060 415 EAAVVAvrestgaSTLQAFLV 435
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
269-606 |
1.46e-07 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 54.28 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 269 DLSIVCFTSGTTGNPKGAMLTH-----GNVVADFSGFLKvtekvifprQDDVLISFLPLAHmferviqsvvyCHGGRVGF 343
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHrrawrGGAFFAGSGGAL---------PSDVLYTCLPLYH-----------STALIVGW 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 344 FQGdirLLS----------------DDMKALRPTIFPVVPRLLnrmydkifhqadtslkRWLLefAAKRKQAEVRsgiir 407
Cdd:cd05940 142 SAC---LASgatlvirkkfsasnfwDDIRKYQATIFQYIGELC----------------RYLL--NQPPKPTERK----- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 408 nnsiwdelffNKIQASLGGHVRmivtgaapasPTVLGFLRAALGC-QVYEGYGQTECTAGCT--FTTPGdwTSGHVGAPL 484
Cdd:cd05940 196 ----------HKVRMIFGNGLR----------PDIWEEFKERFGVpRIAEFYAATEGNSGFInfFGKPG--AIGRNPSLL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 485 PCNH-IKLV-----------DAEELNYWTSKGE-----GEICVKGPnvFKGYLKDEDRTKEAL-----DSDGWLHTGDIG 542
Cdd:cd05940 254 RKVApLALVkydlesgepirDAEGRCIKVPRGEpglliSRINPLEP--FDGYTDPAATEKKILrdvfkKGDAWFNTGDLM 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 48256734 543 KWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYVHGDSL-----KAFLVGIVVPDPE 606
Cdd:cd05940 332 RLDGEGFWYFVDRLGDTFRW-KGENVSTTEVAAVLGAFPGVEEANVYGVQVpgtdgRAGMAAIVLQPNE 399
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
429-613 |
4.12e-07 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 53.07 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 429 RMIVTGAAPASPTVLGF-----LRAALGcqvyegYGQTEcTAG--CTFTtPGDWTSG--HVGAPLPCNHIKLvdaeelny 499
Cdd:PRK07445 233 RTILLGGAPAWPSLLEQarqlqLRLAPT------YGMTE-TASqiATLK-PDDFLAGnnSSGQVLPHAQITI-------- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 500 wTSKGEGEICVKGPNVFKGYLkdedrtKEALDSDGWLHTGDIGKWLPEGTLKIIDR--KKHIfklAQGEYVAPEKIENIY 577
Cdd:PRK07445 297 -PANQTGNITIQAQSLALGYY------PQILDSQGIFETDDLGYLDAQGYLHILGRnsQKII---TGGENVYPAEVEAAI 366
|
170 180 190
....*....|....*....|....*....|....*.
gi 48256734 578 IRSEPVAQIYVHGdslkaflvgivVPDPEvmpcWAQ 613
Cdd:PRK07445 367 LATGLVQDVCVLG-----------LPDPH----WGE 387
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
121-324 |
4.75e-07 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 52.95 E-value: 4.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 121 LSYQEVAKRAE-----FLGSGLLQHDCkvgteqfIGVFAQNRPEWIIAELACyTYSMVVVPLYDT-LGPGSIRYIINTAD 194
Cdd:PRK08279 63 ISYAELNARANryahwAAARGVGKGDV-------VALLMENRPEYLAAWLGL-AKLGAVVALLNTqQRGAVLAHSLNLVD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 195 ICTVIVDKPhkailLLEHVErkETPGLKLVILMEPFDDalRERGKKCGVDIKSMQAIEDSGQENHRVPVPPRPDDLSIVC 274
Cdd:PRK08279 135 AKHLIVGEE-----LVEAFE--EARADLARPPRLWVAG--GDTLDDPEGYEDLAAAAAGAPTTNPASRSGVTAKDTAFYI 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 48256734 275 FTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAH 324
Cdd:PRK08279 206 YTSGTTGLPKAAVMSHMRWLKAMGGFGGLLR----LTPDDVLYCCLPLYH 251
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
417-605 |
1.08e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 51.70 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 417 FNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPGDWTSGHVGAPLPCNHIKLVDAEE 496
Cdd:PRK07638 245 LYKENRVIENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSF-VTALVDEESERRPNSVGRPFHNVQVRICNE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 497 LNYWTSKGE-GEICVKGPNVFKGYLKDEDRTKEaLDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIEN 575
Cdd:PRK07638 324 AGEEVQKGEiGTVYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIES 401
|
170 180 190
....*....|....*....|....*....|
gi 48256734 576 IYIRSEPVAQIYVHGdslkaflvgivVPDP 605
Cdd:PRK07638 402 VLHEHPAVDEIVVIG-----------VPDS 420
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
275-557 |
1.26e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 51.48 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 275 FTSGTTGNPKGAMLTHGNVVADF----SGFLKVTEKVifPRQDDVLISFLPLAHMFERVIQSVVYCHGGR-------VGF 343
Cdd:PRK05850 167 YTSGSTRTPAGVMVSHRNVIANFeqlmSDYFGDTGGV--PPPDTTVVSWLPFYHDMGLVLGVCAPILGGCpavltspVAF 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 344 FQGDIRLLSddMKALRPTIFPVVPrllnrmydkifhqadtslkRWLLEFAAKRKQAEVRSGIirnnsiwdELffnkiqas 423
Cdd:PRK05850 245 LQRPARWMQ--LLASNPHAFSAAP-------------------NFAFELAVRKTSDDDMAGL--------DL-------- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 424 lgGHVRMIVTGAAPASP-TVLGFLR--AALGCQ---VYEGYGQTECTAGCTFTTPGD-----------WTSGHV------ 480
Cdd:PRK05850 288 --GGVLGIISGSERVHPaTLKRFADrfAPFNLRetaIRPSYGLAEATVYVATREPGQppesvrfdyekLSAGHAkrcetg 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 481 -GAPLPCNH------IKLVDAEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEALD------SDG-----WLHTGDIG 542
Cdd:PRK05850 366 gGTPLVSYGsprsptVRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGatlvdpSPGtpegpWLRTGDLG 445
|
330
....*....|....*
gi 48256734 543 kWLPEGTLKIIDRKK 557
Cdd:PRK05850 446 -FISEGELFIVGRIK 459
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
267-590 |
2.50e-06 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 50.51 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 267 PDDLSIVCFTSGTTGNPKGAMLTHG-NVVADfsgflKVTEKVIFPRQDDVLISFLPLAHMFERVIqSVVYC--HGGRVGF 343
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISWRrTLVTS-----NLLSHDLNLKNGDRTYTCMPLYHGTAAFL-GACNClmSGGTLAL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 344 ---FQgdIRLLSDDMKALRPTIFPVVPRLLnrmydkifhqadtslkRWLLEFAAkrkqaevrsgiirnnSIWDELffNKI 420
Cdd:cd05937 160 srkFS--ASQFWKDVRDSGATIIQYVGELC----------------RYLLSTPP---------------SPYDRD--HKV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 421 QASLGGHVRmivtgaapasPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKL-------- 491
Cdd:cd05937 205 RVAWGNGLR----------PDIWERFRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKFenqvvlvk 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 492 VDAEELNYW--TSKG---------EGEICVKGPNV----FKGYLKDEDRTKEAL------DSDGWLHTGDIGKWLPEGTL 550
Cdd:cd05937 275 MDPETDDPIrdPKTGfcvrapvgePGEMLGRVPFKnreaFQGYLHNEDATESKLvrdvfrKGDIYFRTGDLLRQDADGRW 354
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 48256734 551 KIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYVHG 590
Cdd:cd05937 355 YFLDRLGDTFRW-KSENVSTTEVADVLGAHPDIAEANVYG 393
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
254-609 |
3.17e-06 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 50.04 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 254 SGQENHRVPVPPRP------------------DDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkVTEKVIFPRQddV 315
Cdd:PRK07824 3 AGRAPALLPVPAQDerraallrdalrvgepidDDVALVVATSGTTGTPKGAMLTAAALTASADA---THDRLGGPGQ--W 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 316 LISfLPLAHM--FERVIQSVVychGGRV--------GFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKifhQADTSL 385
Cdd:PRK07824 78 LLA-LPAHHIagLQVLVRSVI---AGSEpveldvsaGFDPTALPRAVAELGGGRRYTSLVPMQLAKALDDP---AATAAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 386 KrwllEFAAkrkqaevrsgiirnnsiwdelffnkiqaslgghvrmIVTGAAPASPTVlgfLRAA--LGCQVYEGYGQTEC 463
Cdd:PRK07824 151 A----ELDA------------------------------------VLVGGGPAPAPV---LDAAaaAGINVVRTYGMSET 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 464 TAGCTFTtpgdwtsghvGAPLPCNHIKLVDaeelnywtskgeGEICVKGPNVFKGYLKDEDrtKEALDSDGWLHTGDIGK 543
Cdd:PRK07824 188 SGGCVYD----------GVPLDGVRVRVED------------GRIALGGPTLAKGYRNPVD--PDPFAEPGWFRTDDLGA 243
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 48256734 544 wLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQIYVHG---DSLKAFLVGIVVPDPEVMP 609
Cdd:PRK07824 244 -LDDGVLTVLGRADDAISTG-GLTVLPQVVEAALATHPAVADCAVFGlpdDRLGQRVVAAVVGDGGPAP 310
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
233-325 |
3.42e-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: 50.37 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 233 ALRERGKKCGV--------DIKSMQAiEDSGQENHRVP----VPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVAdFSGF 300
Cdd:cd05938 98 ALRADGVSVWYlshtsnteGVISLLD-KVDAASDEPVPaslrAHVTIKSPALYIYTSGTTGLPKAARISHLRVLQ-CSGF 175
|
90 100
....*....|....*....|....*
gi 48256734 301 LKVTeKVifpRQDDVLISFLPLAHM 325
Cdd:cd05938 176 LSLC-GV---TADDVIYITLPLYHS 196
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
483-550 |
5.77e-06 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 49.51 E-value: 5.77e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 48256734 483 PLPCNHIK-----LVDAEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEAL-DSDGW--LHTGDIGKwLPEGTL 550
Cdd:PRK04813 317 RLPIGYAKpdsplLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGY-LEDGLL 391
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
265-614 |
1.13e-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: 48.15 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 265 PRPDDLSIVCfTSGTTGNPKGAMLTHGNV------VADFSGFLKVTEKVIFPRQ-DDVLISFLPLAHMFerviqsvvycH 337
Cdd:cd05924 1 RSADDLYILY-TGGTTGMPKGVMWRQEDIfrmlmgGADFGTGEFTPSEDAHKAAaAAAGTVMFPAPPLM----------H 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 338 G-----GRVGFFQGDIRLLSDDMkalrptifpVVPRLLNRMYDKifHQADT------SLKRWLLEfaakrkqaEVRSGII 406
Cdd:cd05924 70 GtgswtAFGGLLGGQTVVLPDDR---------FDPEEVWRTIEK--HKVTSmtivgdAMARPLID--------ALRDAGP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 407 RNNSiwdelffnkiqaSLgghvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFTTPGdwtSGHVGAPL- 484
Cdd:cd05924 131 YDLS------------SL----FAISSGGALLSPEVKqGLLELVPNITLVDAFGSSETGFTGSGHSAG---SGPETGPFt 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 485 PCNHIKLVDAEELNYWT--SKGEGEICVKGpNVFKGYLKDEDRTKEA---LDSDGWLHTGDIGKWLPEGTLKIIDRKKHI 559
Cdd:cd05924 192 RANPDTVVLDDDGRVVPpgSGGVGWIARRG-HIPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGRGSVC 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 48256734 560 FKLAqGEYVAPEKIEniyirsepvAQIYVHGDSLKAFLVGivVPDPEvmpcWAQK 614
Cdd:cd05924 271 INTG-GEKVFPEEVE---------EALKSHPAVYDVLVVG--RPDER----WGQE 309
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
122-609 |
2.75e-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: 47.19 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 122 SYQEVAKRAEFLGSGLLQHDCKVGTEqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPgsiryiintADICTVIVD 201
Cdd:cd17634 86 SYRELHREVCRFAGTLLDLGVKKGDR--VAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAP---------EAVAGRIID 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 202 -KPHKAILLLEHVERKETPGLKLVIlmepfDDALRERG---------KKCGVDIKSMQA--------IEDSGQENHrvPV 263
Cdd:cd17634 155 sSSRLLITADGGVRAGRSVPLKKNV-----DDALNPNVtsvehvivlKRTGSDIDWQEGrdlwwrdlIAKASPEHQ--PE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 264 PPRPDDLSIVCFTSGTTGNPKGAMLTHGnvvadfsGFLkvtekvIFPRQDdvlisflpLAHMFERVIQSVVYChGGRVGF 343
Cdd:cd17634 228 AMNAEDPLFILYTSGTTGKPKGVLHTTG-------GYL------VYAATT--------MKYVFDYGPGDIYWC-TADVGW 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 344 FQGDIRLLSDDMkALRPTIF-----PVVPRlLNRMYDKIFHQADTSLkrWLLEFAAKRKQAEVRSGIIRNNsiwdelffn 418
Cdd:cd17634 286 VTGHSYLLYGPL-ACGATTLlyegvPNWPT-PARMWQVVDKHGVNIL--YTAPTAIRALMAAGDDAIEGTD--------- 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 419 kiQASLgghvRMIVTGAAPASPTVLGFLRAALG---CQVYEGYGQTECTAGCTFTTPG--DWTSGHVGAPLPCNHIKLVD 493
Cdd:cd17634 353 --RSSL----RILGSVGEPINPEAYEWYWKKIGkekCPVVDTWWQTETGGFMITPLPGaiELKAGSATRPVFGVQPAVVD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 494 AEElNYWTSKGEGEICVKG--PNVFKGYLKDEDRTKEALDS--DGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVA 569
Cdd:cd17634 427 NEG-HPQPGGTEGNLVITDpwPGQTRTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVA-GHRLG 504
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 48256734 570 PEKIENIYIRSEPVAQIYVHG--DSLKA-FLVGIVVPDPEVMP 609
Cdd:cd17634 505 TAEIESVLVAHPKVAEAAVVGipHAIKGqAPYAYVVLNHGVEP 547
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
418-643 |
5.24e-05 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 46.27 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 418 NKIQASLGGHVRMIVTGAAPASPTV----LGFLRA--ALGCQVYEGYGqTECTAGCTFTTPGDWTSGHVGAPLPCNHI-K 490
Cdd:cd05915 263 ESTGHRLKTLRRLVVGGSAAPRSLIarfeRMGVEVrqGYGLTETSPVV-VQNFVKSHLESLSEEEKLTLKAKTGLPIPlV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 491 LVDAEELNYWTSKGEGE----ICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGE 566
Cdd:cd05915 342 RLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG-GE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 567 YVAPEKIENIyirsepvaqIYVHGDSLKAFLVGivVPDP---EVMPCWAQKKGIEGNYQELCkskELKKAILDDMVMLGK 643
Cdd:cd05915 421 WISSVDLENA---------LMGHPKVKEAAVVA--IPHPkwqERPLAVVVPRGEKPTPEELN---EHLLKAGFAKWQLPD 486
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
264-607 |
8.60e-05 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 45.90 E-value: 8.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 264 PPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTekvifP-RQDDVLISFLPLAHMFerviqsvvychggrvG 342
Cdd:PRK13382 192 EPTGRKGRVILLTSGTTGTPKGARRSGPGGIGTLKAILDRT-----PwRAEEPTVIVAPMFHAW---------------G 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 343 FFQGDIRLL------------SDDMKAL----RPTIFPVVPRLLNRMYDKIfhqadtslkrwllefaakrkqAEVRSgii 406
Cdd:PRK13382 252 FSQLVLAASlactivtrrrfdPEATLDLidrhRATGLAVVPVMFDRIMDLP---------------------AEVRN--- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 407 rnnsiwdelffnkiqASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFT-TPGDWTSG--HVGAP 483
Cdd:PRK13382 308 ---------------RYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATE--AGMIATaTPADLRAApdTAGRP 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 484 LPCNHIKLVDAE--ELnywtSKGE-GEICVKGPNVFKGYlkDEDRTKEAldSDGWLHTGDIGKWLPEGTLKIIDRKKHIF 560
Cdd:PRK13382 371 AEGTEIRILDQDfrEV----PTGEvGTIFVRNDTQFDGY--TSGSTKDF--HDGFMASGDVGYLDENGRLFVVGRDDEMI 442
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 48256734 561 kLAQGEYVAPEKIENIYIRSEPVAQIYV-------HGDSLKAFlvgiVVPDPEV 607
Cdd:PRK13382 443 -VSGGENVYPIEVEKTLATHPDVAEAAVigvddeqYGQRLAAF----VVLKPGA 491
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
268-599 |
2.16e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.77 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 268 DDLSIVCFTSGTTGNPKGAMLTHGnVVADFSGFLKVTEKVifpRQDDVLISFLPLAhmFErviQSVVYCH-----GGRVG 342
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNTHA-ALAERLQWMQATYAL---DDSDVLMQKAPIS--FD---VSVWECFwplitGCRLV 1343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 343 FF----QGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTSLKRWlleFAAkrkqAEVRSGIIRNNsiwdelffn 418
Cdd:PRK05691 1344 LAgpgeHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRL---FSG----GEALPAELRNR--------- 1407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 419 kiqaslgghvrmivtgaapasptVLGFLRAAlgcQVYEGYGQTECTAGCTF--TTPGDWTSGHVGAPLPCNHIKLVDAEe 496
Cdd:PRK05691 1408 -----------------------VLQRLPQV---QLHNRYGPTETAINVTHwqCQAEDGERSPIGRPLGNVLCRVLDAE- 1460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48256734 497 LNYWTSKGEGEICVKGPNVFKGYLKDEDRTKE-----ALDSDG--WLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVA 569
Cdd:PRK05691 1461 LNLLPPGVAGELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL-RGFRVE 1539
|
330 340 350
....*....|....*....|....*....|..
gi 48256734 570 PEKIENIYIRSEPVAQ--IYVHGDSLKAFLVG 599
Cdd:PRK05691 1540 PEEIQARLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
260-294 |
6.28e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 43.11 E-value: 6.28e-04
10 20 30
....*....|....*....|....*....|....*
gi 48256734 260 RVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVV 294
Cdd:PRK10252 590 APLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIV 624
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
244-294 |
5.68e-03 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 39.88 E-value: 5.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 48256734 244 DIKSMQAIEDSGQENHRVpvppRPDDLSIVCFTSGTTGNPKGAMLTHGNVV 294
Cdd:PRK04813 123 ELKDIFATGNPYDFDHAV----KGDDNYYIIFTSGTTGKPKGVQISHDNLV 169
|
|
| |
