|
Name |
Accession |
Description |
Interval |
E-value |
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
141-693 |
0e+00 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 870.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 141 QPYQWLSYQEVADRAEFLGSGLLQHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADI 220
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 221 STVIVDKpqkavlllehverketpglkliilmdpfeealkergqkcGVVIKSMQAVEDCGQENHHAPVPPQPDDLSIVCF 300
Cdd:cd05927 81 SIVFCDA---------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 301 TSGTTGNPKGAMLTHGNVVADFSGFLK--------------------------VTESVVYCHGGRVGFFQGDIRLLSDDM 354
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKileilnkinptdvyisylplahiferVVEALFLYHGAKIGFYSGDIRLLLDDI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 355 KALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWLLEFAAKRKQAEVRSGIIRNDSIWDELFFNKIQASLGGCVRMIVT 432
Cdd:cd05927 202 KALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 433 GAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWA--CKGEGEICVR 510
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAkdPNPRGEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 511 GPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGD 590
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 591 SLKAFLVGIVVPDPEVMPSWA-QKRGIEGTYADLCTSKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLL 669
Cdd:cd05927 442 SLKSFLVAIVVPDPDVLKEWAaSKGGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLL 521
|
570 580
....*....|....*....|....
gi 1622946790 670 TPTLKAKRPELREYFKKQIEELYS 693
Cdd:cd05927 522 TPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
97-693 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 659.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 97 RSViGSGPQLLTHY--YDDARTMYQVFRRGLSISGNGPCLGFRKPNQ----PYQWLSYQEVADRAEFLGSGLLQHNCK-- 168
Cdd:PLN02736 25 RSA-RSPLKLVSRFpdHPEIGTLHDNFVYAVETFRDYKYLGTRIRVDgtvgEYKWMTYGEAGTARTAIGSGLVQHGIPkg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 169 ACtdqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVdKPQKAVLLLEHVerKETPGLKL 248
Cdd:PLN02736 104 AC----VGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCL--SEIPSVRL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 249 IILMDPFEEALKERGQKCGVVIKSMQAVEDCGQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKV 328
Cdd:PLN02736 177 IVVVGGADEPLPSLPSGTGVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 329 TE---SVVYC-------------------HGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QANTPL 384
Cdd:PLN02736 257 TKfypSDVHIsylplahiyervnqivmlhYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNavKESGGL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 385 KRWLLEFAAKRKQAEVRSGiiRNDS-IWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECT 463
Cdd:PLN02736 337 KERLFNAAYNAKKQALENG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETS 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 464 AGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKG---EGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDI 540
Cdd:PLN02736 415 CVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDI 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 541 GKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGIE-GT 619
Cdd:PLN02736 495 GLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyED 574
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622946790 620 YADLCTSKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 693
Cdd:PLN02736 575 LKQLCNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYA 648
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
111-693 |
1.23e-163 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 483.83 E-value: 1.23e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 111 YDDARTMYQVFRRGLSISGNGPCLGfRKPNQPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAEL 190
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVALR-EKEDGIWQSLTWAEFAERVRALAAGLLALGVKP--GDRVAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 191 ACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAVLLLEHveRKETPGLKLIILMDPfeealkeRGQKCGVVI 270
Cdd:COG1022 84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEV--RDELPSLRHIVVLDP-------RGLRDDPRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 271 KSMQAVEDCGQENHH------APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTESVVY------C 335
Cdd:COG1022 155 LSLDELLALGREVADpaeleaRRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARAlleRLPLGPGDRTlsflplA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 336 H-------------GGRVGFfQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQAN--TPLKRWLLEFA---AKRKQ 397
Cdd:COG1022 235 HvfertvsyyalaaGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEeaGGLKRKLFRWAlavGRRYA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 398 AEVRSGiiRNDSIW--------DELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFT 469
Cdd:COG1022 314 RARLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPVITVN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 470 TPGDWTSGHVGAPLPCNHIKLVDveelnywackgEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTL 549
Cdd:COG1022 391 RPGDNRIGTVGPPLPGVEVKIAE-----------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 550 KVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKaFLVGIVVPDPEVMPSWAQKRGIE-GTYADLCTSKD 628
Cdd:COG1022 460 RITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDGRP-FLAALIVPDFEALGEWAEENGLPyTSYAELAQDPE 538
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622946790 629 LKKAILEDMVRLGKesGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 693
Cdd:COG1022 539 VRALIQEEVDRANA--GLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYA 601
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
141-680 |
2.49e-145 |
|
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: 431.25 E-value: 2.49e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 141 QPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADI 220
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEP--GDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 221 STVIVDKPqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhhapvppqpDDLSIVCF 300
Cdd:cd05907 79 KALFVEDP----------------------------------------------------------------DDLATIIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 301 TSGTTGNPKGAMLTHGNVVADFSGFLKVT-----------------------ESVVYCHGGRVGFFQgDIRLLSDDMKAL 357
Cdd:cd05907 95 TSGTTGRPKGVMLSHRNILSNALALAERLpategdrhlsflplahvferragLYVPLLAGARIYFAS-SAETLLDDLSEV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 358 CPTIFPVVPRLLNRMYDKIFSQANTPLKRWLLEFAAkrkqaevrsgiirndsiwdelffnkiqaslGGCVRMIVTGAAPA 437
Cdd:cd05907 174 RPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV------------------------------GGRLRFAASGGAPL 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 438 SPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDveelnywackgEGEICVRGPNVFKG 517
Cdd:cd05907 224 PAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPNVMLG 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 518 YLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKaFLV 597
Cdd:cd05907 292 YYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDGRP-FLV 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 598 GIVVPDPEVMPSWAQKRGIEG-TYADLCTSKDLKKAILEDMVRLGKEsgLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAK 676
Cdd:cd05907 371 ALIVPDPEALEAWAEEHGIAYtDVAELAANPAVRAEIEAAVEAANAR--LSRYEQIKKFLLLPEPFTIENGELTPTLKLK 448
|
....
gi 1622946790 677 RPEL 680
Cdd:cd05907 449 RPVI 452
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
142-677 |
1.15e-140 |
|
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: 421.24 E-value: 1.15e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 142 PYQWLSYQEVADRAEFLGSGL----LQHNCKactdqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINT 217
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLvelgLKPGDK------VAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 218 ADISTVIVDkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhhapvpPQPDDLSI 297
Cdd:cd17639 76 TECSAIFTD---------------------------------------------------------------GKPDDLAC 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 298 VCFTSGTTGNPKGAMLTHGNVVADFSGFLK------------------------VTESVVYCHGGRVGFfqGDIRLLSDD 353
Cdd:cd17639 93 IMYTSGSTGNPKGVMLTHGNLVAGIAGLGDrvpellgpddrylaylplahifelAAENVCLYRGGTIGY--GSPRTLTDK 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 354 MKALC--------PTIFPVVPRLLNRMYDKIFSQANTP--LKRWLLEFAAKRKQAEVRSGIirnDS-IWDELFFNKIQAS 422
Cdd:cd17639 171 SKRGCkgdltefkPTLMVGVPAIWDTIRKGVLAKLNPMggLKRTLFWTAYQSKLKALKEGP---GTpLLDELVFKKVRAA 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 423 LGGCVRMIVTGAAPASPTVLGFLrAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACK 502
Cdd:cd17639 248 LGGRLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDK 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 503 GE--GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQ 580
Cdd:cd17639 327 PPprGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNP 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 581 PVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRG-IEGTYADLCTSKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHS 659
Cdd:cd17639 407 LVNNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGvINSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLD 486
|
570
....*....|....*...
gi 1622946790 660 DMFSVQNGLLTPTLKAKR 677
Cdd:cd17639 487 EEWTPENGLVTAAQKLKR 504
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
113-692 |
1.06e-138 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 421.53 E-value: 1.06e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 113 DARTMYQVFRRGLSISGNGPCLGFRKPNQ----PYQWLSYQEVADRAEFLGSGLLQHNCKACTDqfIGVFAQNRPEWIIA 188
Cdd:PLN02430 40 DITTAWDIFSKSVEKYPDNKMLGWRRIVDgkvgPYMWKTYKEVYEEVLQIGSALRASGAEPGSR--VGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 189 ELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV-DKPQKAVLlleHVERKETPGLKLIILMDPFEEALKERGQKCG 267
Cdd:PLN02430 118 MEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVqDKKIKELL---EPDCKSAKRLKAIVSFTSVTEEESDKASQIG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 268 VVIKSMQAVEDCGQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FL-----KVTESVVY----- 334
Cdd:PLN02430 195 VKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGvdlFMeqfedKMTHDDVYlsflp 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 335 -CH-------------GGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWLLEFAAKRKQA 398
Cdd:PLN02430 275 lAHildrmieeyffrkGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYKYKLA 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 399 EVRSGIIRNDS--IWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS 476
Cdd:PLN02430 355 WMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMCM 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 477 -GHVGAPLPCNHIKLVDVEELNY--WACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVID 553
Cdd:PLN02430 435 lGTVGAPAVYNELRLEEVPEMGYdpLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIID 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 554 RKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGIEGTYADLCTSKDLKKAI 633
Cdd:PLN02430 514 RKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKEHI 593
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622946790 634 LEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 692
Cdd:PLN02430 594 LSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMY 652
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
142-693 |
1.16e-138 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 421.56 E-value: 1.16e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 142 PYQWLSYQEVADRAEFLGSGLLQ------HNCkactdqfiGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYII 215
Cdd:PLN02861 74 PYVWLTYKEVYDAAIRIGSAIRSrgvnpgDRC--------GIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFII 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 216 NTADISTVIVDKPQKAVLLleHVERKETPGLKLIILMDPFEEALKERGQKCGVVIKSMQAVEDCGQENHHAPvPPQPDDL 295
Cdd:PLN02861 146 NHAEVSIAFVQESKISSIL--SCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLDCELP-PKQKTDI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 296 SIVCFTSGTTGNPKGAMLTHGNVVADF---SGFLKVTESVV----------------------YC--HGGRVGFFQGDIR 348
Cdd:PLN02861 223 CTIMYTSGTTGEPKGVILTNRAIIAEVlstDHLLKVTDRVAteedsyfsylplahvydqvietYCisKGASIGFWQGDIR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 349 LLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWLLEFAAKRKQAEVRSGIIRNDS--IWDELFFNKIQASLG 424
Cdd:PLN02861 303 YLMEDVQALKPTIFCGVPRVYDRIYTGIMQkiSSGGMLRKKLFDFAYNYKLGNLRKGLKQEEAspRLDRLVFDKIKEGLG 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 425 GCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCtFTTPGDWTS--GHVGAPLPCNHIKLVDVEELNYWACK 502
Cdd:PLN02861 383 GRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGC-FTSIANVFSmvGTVGVPMTTIEARLESVPEMGYDALS 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 503 G--EGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQ 580
Cdd:PLN02861 462 DvpRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCP 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 581 PVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGIEGTYADLCTSKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSD 660
Cdd:PLN02861 541 LIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPN 620
|
570 580 590
....*....|....*....|....*....|...
gi 1622946790 661 MFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 693
Cdd:PLN02861 621 PFDIERDLITPTFKLKRPQLLKYYKDCIDQLYS 653
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
83-692 |
5.66e-138 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 420.20 E-value: 5.66e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 83 LMQSEEVEDSGGARRSVigsGPQLLTHYYDDA--------RTMYQVFRRGLSISGNGPCLGFR-----KPNQpYQWLSYQ 149
Cdd:PLN02614 8 IFQVEEGKEGSDGRPSV---GPVYRSIFAKDGfpnpiegmDSCWDVFRMSVEKYPNNPMLGRReivdgKPGK-YVWQTYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 150 EVADRAEFLGSGLlqHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDkpQ 229
Cdd:PLN02614 84 EVYDIVIKLGNSL--RSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVE--E 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 230 KAVLLLEHVERKETPGLKLIILMDPFEEALKERGQKCGVVIKSMQAVEDCGQENHHAPVPPQPDDLSIVCFTSGTTGNPK 309
Cdd:PLN02614 160 KKISELFKTCPNSTEYMKTVVSFGGVSREQKEEAETFGLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 310 GAMLTHGNVVADFSG---------------------------FLKVTESVVYCHGGRVGFFQGDIRLLSDDMKALCPTIF 362
Cdd:PLN02614 240 GVMISNESIVTLIAGvirllksanaaltvkdvylsylplahiFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 363 PVVPRLLNRMYDKIFSQANTP--LKRWLLEFAAKRKQAEVRSGI--IRNDSIWDELFFNKIQASLGGCVRMIVTGAAPAS 438
Cdd:PLN02614 320 CAVPRVLDRVYSGLQKKLSDGgfLKKFVFDSAFSYKFGNMKKGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 439 PTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDVEELNY--WACKGEGEICVRGPNVF 515
Cdd:PLN02614 400 SHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELDMlGTVGPPVPNVDIRLESVPEMEYdaLASTPRGEICIRGKTLF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 516 KGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAF 595
Cdd:PLN02614 480 SGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESF 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 596 LVGIVVPDPEVMPSWAQKRGIEGTYADLCTSKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKA 675
Cdd:PLN02614 559 LVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKK 638
|
650
....*....|....*..
gi 1622946790 676 KRPELREYFKKQIEELY 692
Cdd:PLN02614 639 KRPQLLKYYQSVIDEMY 655
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
104-693 |
1.61e-122 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 381.00 E-value: 1.61e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 104 PQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRKPNQ------------------PYQWLSYQEVADRAEFLGSGLLQ- 164
Cdd:PLN02387 47 PELVETPWEGATTLAALFEQSCKKYSDKRLLGTRKLISrefetssdgrkfeklhlgEYEWITYGQVFERVCNFASGLVAl 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 165 -HNckacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQ--KAVLLLEHVERk 241
Cdd:PLN02387 127 gHN----KEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQlkKLIDISSQLET- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 242 etpgLKLIILM-DPFEEALKERGQKCGVVIKSMQAVEDCGQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVA 320
Cdd:PLN02387 202 ----VKRVIYMdDEGVDSDSSLSGSSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 321 DFSGFLKV-----------------------TESVVYCHGGRVGFfqGDIRLLSD-----------DMKALCPTIFPVVP 366
Cdd:PLN02387 278 TVAGVMTVvpklgkndvylaylplahilelaAESVMAAVGAAIGY--GSPLTLTDtsnkikkgtkgDASALKPTLMTAVP 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 367 RLLNRMYDKIFSQANTP--LKRWLLEFAAKRKQAEVR------SGIIRndSIWDELFFNKIQASLGGCVRMIVTGAAPAS 438
Cdd:PLN02387 356 AILDRVRDGVRKKVDAKggLAKKLFDIAYKRRLAAIEgswfgaWGLEK--LLWDALVFKKIRAVLGGRIRFMLSGGAPLS 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 439 PTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKG---EGEICVRGPNVF 515
Cdd:PLN02387 434 GDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLISDKpmpRGEIVIGGPSVT 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 516 KGYLKDPDRTKEA--LDSDG--WLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDS 591
Cdd:PLN02387 514 LGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIMVHADP 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 592 LKAFLVGIVVPDPEVMPSWAQKRGIE-GTYADLCTSKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLT 670
Cdd:PLN02387 594 FHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPAKIKLLPEPWTPESGLVT 673
|
650 660
....*....|....*....|...
gi 1622946790 671 PTLKAKRPELREYFKKQIEELYS 693
Cdd:PLN02387 674 AALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
142-562 |
1.65e-115 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 353.16 E-value: 1.65e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 142 PYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADIS 221
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRALGVGK--GDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 222 TVIVDKPQKAVLLLEHVERKETPGLKLIILMDPFEEALKergqkcgvviksMQAVEDCGQENHHAPVPPQPDDLSIVCFT 301
Cdd:pfam00501 96 VLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEP------------LPEEAKPADVPPPPPPPPDPDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 302 SGTTGNPKGAMLTHGNVVADFSGFLKVTESV---------------------------VYCHGGRVGFFQGDIRL----L 350
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNLVANVLSIKRVRPRGfglgpddrvlstlplfhdfglslgllgPLLAGATVVLPPGFPALdpaaL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 351 SDDMKALCPTIFPVVPRLLNRMydkifsqantplkrwlleFAAKRKQAEVRSGiirndsiwdelffnkiqaslggcVRMI 430
Cdd:pfam00501 244 LELIERYKVTVLYGVPTLLNML------------------LEAGAPKRALLSS-----------------------LRLV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 431 VTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDW---TSGHVGAPLPCNHIKLVDVEELNYWACKGEGEI 507
Cdd:pfam00501 283 LSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGEL 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1622946790 508 CVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLA 562
Cdd:pfam00501 363 CVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
88-692 |
3.64e-87 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 288.03 E-value: 3.64e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 88 EVEDSGGARRSVIGSGPQL--LTHYYDDARTMYQVFRRGLSISGNGPCLGFRKPN--------------QPY-------- 143
Cdd:PTZ00216 40 ETENASAIYRIAGVTDEEHerLRNEWYYGPNFLQRLERICKERGDRRALAYRPVErvekevvkdadgkeRTMevthfnet 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 144 QWLSYQEVADRAEFLGSGL----LQHNCKactdqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTAD 219
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLaelgLTKGSN------VAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 220 iSTVIVDKPQKAVLLLEHVERKETPGLKLIILmdpfeEALKERGQKCGVVIKSMQAVEDCG---QENHHAPVPPQPDDLS 296
Cdd:PTZ00216 194 -CKAIVCNGKNVPNLLRLMKSGGMPNTTIIYL-----DSLPASVDTEGCRLVAWTDVVAKGhsaGSHHPLNIPENNDDLA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 297 IVCFTSGTTGNPKGAMLTHGNVVADFSG--------FLKVTESVVYC------H-------------GGRVGFfqGDIRL 349
Cdd:PTZ00216 268 LIMYTSGTTGDPKGVMHTHGSLTAGILAledrlndlIGPPEEDETYCsylplaHimefgvtniflarGALIGF--GSPRT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 350 LSD-------DMKALCPTIFPVVPRLLNRMydKIFSQANTP----LKRWLLEFAAKRKQAEVRSGiiRNDSIWDELFFNK 418
Cdd:PTZ00216 346 LTDtfarphgDLTEFRPVFLIGVPRIFDTI--KKAVEAKLPpvgsLKRRVFDHAYQSRLRALKEG--KDTPYWNEKVFSA 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 419 IQASLGGCVRMIVTGAAPASPTVLGFLRAALGCqVYEGYGQTE--CTAGCTFTtpGDWTSGHVGAPLPCNHIKLVDVEEL 496
Cdd:PTZ00216 422 PRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTEtvCCGGIQRT--GDLEPNAVGQLLKGVEMKLLDTEEY 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 497 NYwACKGE--GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIEN 574
Cdd:PTZ00216 499 KH-TDTPEprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEA 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 575 IYIRSQPVAQ----IYVHGDslKAFLVGIVVPDPEVMPSWAQKRGIEGTYADLCTSKDLKKAILEDMVRLGKESGLHSFE 650
Cdd:PTZ00216 578 LYGQNELVVPngvcVLVHPA--RSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFE 655
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1622946790 651 QVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 692
Cdd:PTZ00216 656 IVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
141-678 |
2.05e-69 |
|
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: 234.18 E-value: 2.05e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 141 QPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADI 220
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKA--GEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 221 STVIVdkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqENHhapvppqPDDLSIVCF 300
Cdd:cd17640 79 VALVV--------------------------------------------------------END-------SDDLATIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 301 TSGTTGNPKGAMLTHGNV---VADFSGFL-------------------KVTESVVYCHGGRVGFfqGDIRLLSDDMKALC 358
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLlhqIRSLSDIVppqpgdrflsilpiwhsyeRSAEYFIFACGCSQAY--TSIRTLKDDLKRVK 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 359 PTIFPVVPRLLNRMYDKIFSQ--ANTPLKRWLLEFAAkrkqaevrsgiirndsiwdelffnkiqasLGGCVRMIVTGAAP 436
Cdd:cd17640 174 PHYIVSVPRLWESLYSGIQKQvsKSSPIKQFLFLFFL-----------------------------SGGIFKFGISGGGA 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 437 ASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFK 516
Cdd:cd17640 225 LPPHVDTFFEA-IGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMK 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 517 GYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKaFL 596
Cdd:cd17640 304 GYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQK-RL 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 597 VGIVVPDPEVMPSWAQKRGI---EGTYADLCTSKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFsVQNGLLTPTL 673
Cdd:cd17640 383 GALIVPNFEELEKWAKESGVklaNDRSQLLASKKVLKLYKNEIKDEISNRPGFKSFEQIAPFALLEEPF-IENGEMTQTM 461
|
....*
gi 1622946790 674 KAKRP 678
Cdd:cd17640 462 KIKRN 466
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
143-677 |
7.68e-69 |
|
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: 233.90 E-value: 7.68e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 143 YQWLSYQEVADRAEFLGSGLLQHNCKACTDqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADIST 222
Cdd:cd05932 4 VVEFTWGEVADKARRLAAALRALGLEPGSK--IALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 223 VIVDKpqkavllLEHVERKE--TPGLKLIILMDPFEEALKERGqkcgvviksMQAVEDCGQENHHAPvPPQPDDLSIVCF 300
Cdd:cd05932 82 LFVGK-------LDDWKAMApgVPEGLISISLPPPSAANCQYQ---------WDDLIAQHPPLEERP-TRFPEQLATLIY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 301 TSGTTGNPKGAMLTHGN-------VVADFS--------GFL---KVTESVVYCHG----GRVGFFQGDIRLLSDDMKALC 358
Cdd:cd05932 145 TSGTTGQPKGVMLTFGSfawaaqaGIEHIGteendrmlSYLplaHVTERVFVEGGslygGVLVAFAESLDTFVEDVQRAR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 359 PTIFPVVPRLL----NRMYDKIFSQAntpLKRWLlefaakrkQAEVRSGIIRndsiwdelffNKIQASLG-GCVRMIVTG 433
Cdd:cd05932 225 PTLFFSVPRLWtkfqQGVQDKIPQQK---LNLLL--------KIPVVNSLVK----------RKVLKGLGlDQCRLAGCG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 434 AAPASPTVLGFLRaALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDveelnywackgEGEICVRGPN 513
Cdd:cd05932 284 SAPVPPALLEWYR-SLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEILVRSPA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 514 VFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLK 593
Cdd:cd05932 352 LMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSGLP 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 594 AfLVGIVVPDPEvmpswAQKRGIEGTYADLCTSkdlKKAILEDMvrlgkESGLHSFEQVKAIHIHSDMFSVQNGLLTPTL 673
Cdd:cd05932 432 A-PLALVVLSEE-----ARLRADAFARAELEAS---LRAHLARV-----NSTLDSHEQLAGIVVVKDPWSIDNGILTPTL 497
|
....
gi 1622946790 674 KAKR 677
Cdd:cd05932 498 KIKR 501
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
138-692 |
1.92e-64 |
|
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: 224.16 E-value: 1.92e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 138 KPNQPYQWLSYQEVADRAE-----FLGSGLLQHNCkactdqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIR 212
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRqaakaFLKLGLERFHG-------VGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 213 YIINTADISTVIVDKPQKAVLLLEhvERKETPGLKLII-LMDPFEEalKERGQKcgvvikSMQAVEDCG----QENHHAP 287
Cdd:cd05933 74 YVAETSEANILVVENQKQLQKILQ--IQDKLPHLKAIIqYKEPLKE--KEPNLY------SWDEFMELGrsipDEQLDAI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 288 VPPQ-PDDLSIVCFTSGTTGNPKGAMLTHGNVV---------ADFSGFLKVTESVV-Y---CH--------------GGR 339
Cdd:cd05933 144 ISSQkPNQCCTLIYTSGTTGMPKGVMLSHDNITwtakaasqhMDLRPATVGQESVVsYlplSHiaaqildiwlpikvGGQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 340 VGFFQGDIR--LLSDDMKALCPTIFPVVPRLLNRMYDKI---FSQAnTPLKRWLLEFAaKRKQAEV-------RSGIIRN 407
Cdd:cd05933 224 VYFAQPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkavGAKS-GTLKRKIASWA-KGVGLETnlklmggESPSPLF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 408 DSIWDELFFNKIQASLG--GCVRMIvTGAAPASPTVLGFLrAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPC 485
Cdd:cd05933 302 YRLAKKLVFKKVRKALGldRCQKFF-TGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 486 NHIKLVDVEelnywaCKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGE 565
Cdd:cd05933 380 CKTKIHNPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGE 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 566 YVAPEKIENIYIRSQP-VAQIYVHGDSLKaFLVGIVV------PD---------PEVMpSWAQKRGIEGTY-ADLCTSKD 628
Cdd:cd05933 454 NVPPVPIEDAVKKELPiISNAMLIGDKRK-FLSMLLTlkcevnPEtgepldeltEEAI-EFCRKLGSQATRvSEIAGGKD 531
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622946790 629 LK--KAILEDMVRLGKESGLHSFEQVKAIHIHSDmFSVQNGLLTPTLKAKRPELREYFKKQIEELY 692
Cdd:cd05933 532 PKvyEAIEEGIKRVNKKAISNAQKIQKWVILEKD-FSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
117-690 |
6.33e-62 |
|
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: 213.52 E-value: 6.33e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 117 MYQVFRRGLSISGNGPCLGFRkpnqpYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYS 196
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG-----GRRLTYAELDARARRLAAALRALGVGP--GDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 197 MVVVPLYDTLGPGAIRYIINTADISTVIVdkpqkAVLLlehverketpglkliilmdpfeealkergqkcgvviksmqav 276
Cdd:COG0318 74 AVVVPLNPRLTAEELAYILEDSGARALVT-----ALIL------------------------------------------ 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 277 edcgqenhhapvppqpddlsivcFTSGTTGNPKGAMLTHGNVVA---DFSGFLKVTESVVYCH--------GGRVGFFQG 345
Cdd:COG0318 107 -----------------------YTSGTTGRPKGVMLTHRNLLAnaaAIAAALGLTPGDVVLValplfhvfGLTVGLLAP 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 346 -------------DIRLLSDDMKALCPTIFPVVPRLLNRMYDkifsqantplkrwllefAAKRKQAEVRSgiirndsiwd 412
Cdd:COG0318 164 llagatlvllprfDPERVLELIERERVTVLFGVPTMLARLLR-----------------HPEFARYDLSS---------- 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 413 elffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPCNHIKL 490
Cdd:COG0318 217 --------------LRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGRPLPGVEVRI 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 491 VDVE--ELnywACKGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVA 568
Cdd:COG0318 283 VDEDgrEL---PPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-DGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVY 357
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 569 PEKIENIYIRSQPVAQIYV-------HGDSLKAFlvgiVVPDPEvmpswaqkrgiegtyADLcTSKDLKKAILEdmvRLG 641
Cdd:COG0318 358 PAEVEEVLAAHPGVAEAAVvgvpdekWGERVVAF----VVLRPG---------------AEL-DAEELRAFLRE---RLA 414
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1622946790 642 KesglhsFEQVKAIHIHSDMfsvqngLLTPTLKAKRPELREYFKKQIEE 690
Cdd:COG0318 415 R------YKVPRRVEFVDEL------PRTASGKIDRRALRERYAAGALE 451
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
143-643 |
1.19e-59 |
|
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: 210.74 E-value: 1.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 143 YQWLSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADIST 222
Cdd:cd17641 9 WQEFTWADYADRVRAFALGLLALGVG--RGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 223 VIVDKPQKAVLLLEHveRKETPGLKLIILMDPfeeaLKERGQKCGVVIKSMQAVEDcGQEnHHAPVPP---------QPD 293
Cdd:cd17641 87 VIAEDEEQVDKLLEI--ADRIPSVRYVIYCDP----RGMRKYDDPRLISFEDVVAL-GRA-LDRRDPGlyerevaagKGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 294 DLSIVCFTSGTTGNPKGAMLTHGNVV---------------ADFSGFLK---VTESVVYCHGGRV-GF---FQGDIRLLS 351
Cdd:cd17641 159 DVAVLCTTSGTTGKPKLAMLSHGNFLghcaaylaadplgpgDEYVSVLPlpwIGEQMYSVGQALVcGFivnFPEEPETMM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 352 DDMKALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWL--------LEFAAKRKQAEVRSGIIRNDS-IWDELFFNKIQ 420
Cdd:cd17641 239 EDLREIGPTFVLLPPRVWEGIAADVRArmMDATPFKRFMfelgmklgLRALDRGKRGRPVSLWLRLASwLADALLFRPLR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 421 ASLG-GCVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTEcTAGCTFTTP-GDWTSGHVGAPLPCNHIKLVDVeelny 498
Cdd:cd17641 319 DRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTE-LAGAYTVHRdGDVDPDTVGVPFPGTEVRIDEV----- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 499 wackgeGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIR 578
Cdd:cd17641 392 ------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKF 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622946790 579 SQPVAQIYVHGDSlKAFLVGIVVPDPEVMPSWAQKRGIE-GTYADLCTSKDLKKAILEDMVRLGKE 643
Cdd:cd17641 466 SPYIAEAVVLGAG-RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKVNAS 530
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
146-670 |
5.15e-57 |
|
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: 203.84 E-value: 5.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGSgllQHNCKACTD--QFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTV 223
Cdd:cd17632 68 ITYAELWERVGAVAA---AHDPEQPVRpgDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 224 IVDKPQKAV---LLLEHverketPGLKLIILMDPFEEALKER-----------GQKCGVVIKSMQAVEDCGQENHHAPVP 289
Cdd:cd17632 145 AVSAEHLDLaveAVLEG------GTPPRLVVFDHRPEVDAHRaalesarerlaAVGIPVTTLTLIAVRGRDLPPAPLFRP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 290 PQPDD-LSIVCFTSGTTGNPKGAMLTHGNVVA---DFSGFLKVTESVV--------------------YCHGGrVGFFQG 345
Cdd:cd17632 219 EPDDDpLALLIYTSGSTGTPKGAMYTERLVATfwlKVSSIQDIRPPASitlnfmpmshiagrislygtLARGG-TAYFAA 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 346 --DIRLLSDDMKALCPTIFPVVPRLlnrmYDKIFSQANTPLKRWL-----LEFAAKRKQAEVRsgiirndsiwdelffnk 418
Cdd:cd17632 298 asDMSTLFDDLALVRPTELFLVPRV----CDMLFQRYQAELDRRSvagadAETLAERVKAELR----------------- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 419 iQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTtpgdwtSGHVGAPlPCNHIKLVDVEELNY 498
Cdd:cd17632 357 -ERVLGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE--AGAVIL------DGVIVRP-PVLDYKLVDVPELGY 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 499 WACKG---EGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENI 575
Cdd:cd17632 427 FRTDRphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAV 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 576 YIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMpswaqkrgiegtyaDLCTSKDLKKAILEDMVRLGKESGLHSFEQVKAI 655
Cdd:cd17632 507 FAASPLVRQIFVYGNSERAYLLAVVVPTQDAL--------------AGEDTARLRAALAESLQRIAREAGLQSYEIPRDF 572
|
570
....*....|....*
gi 1622946790 656 HIHSDMFSVQNGLLT 670
Cdd:cd17632 573 LIETEPFTIANGLLS 587
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
146-614 |
5.72e-56 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 198.97 E-value: 5.72e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGK-GDR-VAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 226 -------DKPQKAVL-LLEHVERKETP-GLKLIILMDPFEEALkERGQkcgvviksmqavedcgQENHHAPVppQPDDLS 296
Cdd:PRK07656 109 lglflgvDYSATTRLpALEHVVICETEeDDPHTEKMKTFTDFL-AAGD----------------PAERAPEV--DPDDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 297 IVCFTSGTTGNPKGAMLTHGNV---VADFSGFLKVTESVVYC------H--GGRVGF---------------FQGD--IR 348
Cdd:PRK07656 170 DILFTSGTTGRPKGAMLTHRQLlsnAADWAEYLGLTEGDRYLaanpffHvfGYKAGVnaplmrgatilplpvFDPDevFR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 349 LLSDDMkalcPTIFPVVPRLLNRMYDkifsqantplkrwllefAAKRKQAEVRSgiirndsiwdelffnkiqaslggcVR 428
Cdd:PRK07656 250 LIETER----ITVLPGPPTMYNSLLQ-----------------HPDRSAEDLSS------------------------LR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 429 MIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGCTFTTPGD---WTSGHVGAPLPCNHIKLVDveELNYWACKGE 504
Cdd:PRK07656 285 LAVTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIAGVENKIVN--ELGEEVPVGE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 505 -GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVA 583
Cdd:PRK07656 363 vGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IVGGFNVYPAEVEEVLYEHPAVA 441
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1622946790 584 QIYV-------HGDSLKAFLV---GIVVPDPEVMpSWAQKR 614
Cdd:PRK07656 442 EAAVigvpderLGEVGKAYVVlkpGAELTEEELI-AYCREH 481
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
146-677 |
3.52e-53 |
|
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: 190.35 E-value: 3.52e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLgSGLLQHNCKACTDQfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd05914 8 LTYKDLADNIAKF-ALLLKINGVGTGDR-VALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 226 DKPqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhhapvppqpDDLSIVCFTSGTT 305
Cdd:cd05914 86 SDE----------------------------------------------------------------DDVALINYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 306 GNPKGAMLTHGNVVADFSG---FLKVTE----------SVVY--CHGGRVGFFQGDIRLLSDDM---KALCPTIFPV--- 364
Cdd:cd05914 102 GNSKGVMLTYRNIVSNVDGvkeVVLLGKgdkilsilplHHIYplTFTLLLPLLNGAHVVFLDKIpsaKIIALAFAQVtpt 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 365 --VPRLLNRMYDKIFSQANTPLKRWLLEFAAKrkqaevrsgIIRNDSIWdELFFNKIQASLGGCVRMIVTGAAPASPTVL 442
Cdd:cd05914 182 lgVPVPLVIEKIFKMDIIPKLTLKKFKFKLAK---------KINNRKIR-KLAFKKVHEAFGGNIKEFVIGGAKINPDVE 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 443 GFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPlpcnhIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDP 522
Cdd:cd05914 252 EFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKV-----IDGVEVRIDSPDPATGEGEIIVRGPNVMKGYYKNP 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 523 DRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVA--QIYVHGDSLKAflvgIV 600
Cdd:cd05914 326 EATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLesLVVVQEKKLVA----LA 401
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622946790 601 VPDPEVMPSWAQKRgiegtyadlctsKDLKKAILEDmVRLGKESGLHSFEQVKAIHIHSDMFSVqngllTPTLKAKR 677
Cdd:cd05914 402 YIDPDFLDVKALKQ------------RNIIDAIKWE-VRDKVNQKVPNYKKISKVKIVKEEFEK-----TPKGKIKR 460
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
118-597 |
1.54e-52 |
|
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: 188.54 E-value: 1.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 118 YQVFRRGLSISGNGPCLGFRKpnqpyQWLSYQEVADRAEFLGSGLLQHNCKaCTDQfIGVFAQNRPEWIIAELACYTYSM 197
Cdd:cd05936 2 ADLLEEAARRFPDKTALIFMG-----RKLTYRELDALAEAFAAGLQNLGVQ-PGDR-VALMLPNCPQFPIAYFGALKAGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 198 VVVPLYDTLGPGAIRYIINTADISTVIVDkpqkavlllehverketpglkliilmDPFEEALKergqkcgvviksmqave 277
Cdd:cd05936 75 VVVPLNPLYTPRELEHILNDSGAKALIVA--------------------------VSFTDLLA----------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 278 dcGQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFS------GFLKVTESVVYC-----H------GGRV 340
Cdd:cd05936 112 --AGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALqikawlEDLLEGDDVVLAalplfHvfgltvALLL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 341 GFFQG----------DIRLLsDDMKALCPTIFPVVPRLLNRmydkifsqantplkrwLLEFAAKRKqaEVRSGIirndsi 410
Cdd:cd05936 190 PLALGativliprfrPIGVL-KEIRKHRVTIFPGVPTMYIA----------------LLNAPEFKK--RDFSSL------ 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 411 wdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT-SGHVGAPLPCNHIK 489
Cdd:cd05936 245 -----------------RLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRkPGSIGIPLPGTEVK 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 490 LVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAP 569
Cdd:cd05936 308 IVD-DDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGGFNVYP 384
|
490 500 510
....*....|....*....|....*....|....*
gi 1622946790 570 EKIENIYIRSQPVAQIYV-------HGDSLKAFLV 597
Cdd:cd05936 385 REVEEVLYEHPAVAEAAVvgvpdpySGEAVKAFVV 419
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
294-605 |
9.36e-52 |
|
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: 182.48 E-value: 9.36e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 294 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVT----ESVVYC------------------HGGRVGFFQG-DIRLL 350
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGglteGDVFLStlplfhigglfgllgallAGGTVVLLPKfDPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 351 SDDMKALCPTIFPVVPRLLNRMydkifsqantplkrwllefaakRKQAEVRSgiiRNDSiwdelffnkiqaslggCVRMI 430
Cdd:cd04433 81 LELIEREKVTILLGVPTLLARL----------------------LKAPESAG---YDLS----------------SLRAL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 431 VTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT--SGHVGAPLPCNHIKLVDVEElNYWACKGEGEIC 508
Cdd:cd04433 120 VSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDPDG-GELPPGEIGELV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 509 VRGPNVFKGYLKDPDRTkEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYVH 588
Cdd:cd04433 199 VRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPGVAEAAVV 276
|
330
....*....|....*..
gi 1622946790 589 GdslkaflvgivVPDPE 605
Cdd:cd04433 277 G-----------VPDPE 282
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
146-597 |
1.43e-49 |
|
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: 180.87 E-value: 1.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLK--KGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 226 DKPQKAVLLLehVERKETPGLKlIILMDPFEEALKERGQkcgvvikSMQAVedCGQENHHAPVPPQ--PDDLSIVCFTSG 303
Cdd:cd05911 89 DPDGLEKVKE--AAKELGPKDK-IIVLDDKPDGVLSIED-------LLSPT--LGEEDEDLPPPLKdgKDDTAAILYSSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 304 TTGNPKGAMLTHGNVVADFS---GFLKVTES---VVYC-----HGgrVGFF-------QGDIRLL-----SDDMKALCP- 359
Cdd:cd05911 157 TTGLPKGVCLSHRNLIANLSqvqTFLYGNDGsndVILGflplyHI--YGLFttlasllNGATVIImpkfdSELFLDLIEk 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 360 ---TIFPVVPRLLNRMydkifsqANTPLkrwllefaakrkqaevrsgiirndsiwdelfFNKIQASlggCVRMIVTGAAP 436
Cdd:cd05911 235 ykiTFLYLVPPIAAAL-------AKSPL-------------------------------LDKYDLS---SLRVILSGGAP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 437 ASPTVLGFLRAALG-CQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVF 515
Cdd:cd05911 274 LSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVM 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 516 KGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIyIRSQP------VAQIY--V 587
Cdd:cd05911 354 KGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAV-LLEHPgvadaaVIGIPdeV 431
|
490
....*....|
gi 1622946790 588 HGDSLKAFLV 597
Cdd:cd05911 432 SGELPRAYVV 441
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
111-604 |
6.95e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 165.36 E-value: 6.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 111 YDDARTMYQVFRRGLSISGNGPCLGFRKPNqpyqwLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAEL 190
Cdd:PRK06187 2 QDYPLTIGRILRHGARKHPDKEAVYFDGRR-----TTYAELDERVNRLANALRALGVKK--GDRVAVFDWNSHEYLEAYF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 191 ACytySM---VVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlLLEHVE--RKETPGLKLIILMDP----------- 254
Cdd:PRK06187 75 AV---PKigaVLHPINIRLKPEEIAYILNDAEDRVVLVDSE-----FVPLLAaiLPQLPTVRTVIVEGDgpaaplapevg 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 255 -FEEALKergqkcgvviksmqavedcGQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD---FSGFLKVTE 330
Cdd:PRK06187 147 eYEELLA-------------------AASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHslaVCAWLKLSR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 331 SVVY--------CHG---GRVGFFQG---------DIRLLSDDMKALCPTIFPVVPRLLNRMydkifSQANTPLKRWLle 390
Cdd:PRK06187 208 DDVYlvivpmfhVHAwglPYLALMAGakqviprrfDPENLLDLIETERVTFFFAVPTIWQML-----LKAPRAYFVDF-- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 391 faakrkqaevrSGIirndsiwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTT 470
Cdd:PRK06187 281 -----------SSL-----------------------RLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVLP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 471 PGDWTSGH------VGAPLPCNHIKLVDvEELNYWACKGE--GEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGK 542
Cdd:PRK06187 327 PEDQLPGQwtkrrsAGRPLPGVEARIVD-DDGDELPPDGGevGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGY 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622946790 543 WLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDP 604
Cdd:PRK06187 405 IDEDGYLYITDRIKDVIISG-GENIYPRELEDA---------LYGHPAVAEVAVIG--VPDE 454
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
146-608 |
4.00e-36 |
|
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: 141.66 E-value: 4.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLgSGLLQHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIv 225
Cdd:cd05941 12 ITYADLVARAARL-ANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 226 dkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhhapvppqpdDLSIVCFTSGTT 305
Cdd:cd05941 90 --------------------------------------------------------------------DPALILYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 306 GNPKGAMLTHGNVVADFSGFLKV---TESVVYCH--------------------GGRV---GFFQGDIRLLSDDMKALcp 359
Cdd:cd05941 102 GRPKGVVLTHANLAANVRALVDAwrwTEDDVLLHvlplhhvhglvnallcplfaGASVeflPKFDPKEVAISRLMPSI-- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 360 TIFPVVPRllnrMYDKIFS--QANTPLKRWLLEFAAKRkqaevrsgiirndsiwdelffnkiqaslggcVRMIVTGAAPA 437
Cdd:cd05941 180 TVFMGVPT----IYTRLLQyyEAHFTDPQFARAAAAER-------------------------------LRLMVSGSAAL 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 438 SPTVLGFLRAALGCQVYEGYGQTEctAGCTFTTP--GDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVF 515
Cdd:cd05941 225 PVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVF 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 516 KGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKK-HIFKlAQGEYVAPEKIENIyIRSQP-VAQIYVHGDSLK 593
Cdd:cd05941 303 KEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEIERV-LLAHPgVSECAVIGVPDP 380
|
490
....*....|....*...
gi 1622946790 594 AF---LVGIVVPDPEVMP 608
Cdd:cd05941 381 DWgerVVAVVVLRAGAAA 398
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
121-604 |
6.99e-36 |
|
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: 140.82 E-value: 6.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 121 FRRGLSISGNGPCLGFrkPNQPyqwLSYQEVADRAEFLGSGLlQHNCKACTDQfIGVFAQNRPEWIIAELACYTYSMVVV 200
Cdd:cd17631 1 LRRRARRHPDRTALVF--GGRS---LTYAELDERVNRLAHAL-RALGVAKGDR-VAVLSKNSPEFLELLFAAARLGAVFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 201 PLYDTLGPGAIRYIINTADiSTVIVDkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcg 280
Cdd:cd17631 74 PLNFRLTPPEVAYILADSG-AKVLFD------------------------------------------------------ 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 281 qenhhapvppqpdDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTESVVY------CHGGRVGFFQ------- 344
Cdd:cd17631 99 -------------DLALLMYTSGTTGRPKGAMLTHRNLLWNAVNalaALDLGPDDVLlvvaplFHIGGLGVFTlptllrg 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 345 GDIRLLS--DDMKALC------PTIFPVVPRLLNRMydkifsqANTPLkrwllefaakrkqaevrsgiirndsiWDELFF 416
Cdd:cd17631 166 GTVVILRkfDPETVLDlierhrVTSFFLVPTMIQAL-------LQHPR--------------------------FATTDL 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 417 nkiqASLggcvRMIVTGAAPASPTVLGFLRAAlGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPCNHIKLVDvE 494
Cdd:cd17631 213 ----SSL----RAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHRRklGSAGRPVFFVEVRIVD-P 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 495 ELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAPEKIEN 574
Cdd:cd17631 283 DGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFR-DGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVED 360
|
490 500 510
....*....|....*....|....*....|
gi 1622946790 575 IyirsqpvaqIYVHGDSLKAFLVGivVPDP 604
Cdd:cd17631 361 V---------LYEHPAVAEVAVIG--VPDE 379
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
272-575 |
4.70e-35 |
|
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: 139.68 E-value: 4.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 272 SMQAVEDCGQENHHAPVPPQ--PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESV-----VY------CH-G 337
Cdd:cd05904 135 SLSFSDLLFEADEAEPPVVVikQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNsdsedVFlcvlpmFHiY 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 338 GRVGFFQGDIRL-----------LSDDMKALCP---TIFPVVPrllnrmydkifsqantPLkrwlleFAAKRKQAEVRSG 403
Cdd:cd05904 215 GLSSFALGLLRLgatvvvmprfdLEELLAAIERykvTHLPVVP----------------PI------VLALVKSPIVDKY 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 404 IIRndsiwdelffnkiqaSLggcvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFTTP---GDWTSGHV 479
Cdd:cd05904 273 DLS---------------SL----RQIMSGAAPLGKELIeAFRAKFPNVDLGQGYGMTESTGVVAMCFApekDRAKYGSV 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 480 GAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIF 559
Cdd:cd05904 334 GRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELI 413
|
330
....*....|....*.
gi 1622946790 560 KLaQGEYVAPEKIENI 575
Cdd:cd05904 414 KY-KGFQVAPAELEAL 428
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
146-575 |
4.96e-35 |
|
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: 139.39 E-value: 4.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGSgLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd05909 8 LTYRKLLTGAIALAR-KLAKMTKE--GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 226 DKPQKAVLLLEHVERKETPgLKLIILmdpfeEALKER---GQKCGVVIKSMQAVEDCGQENHHAPVppQPDDLSIVCFTS 302
Cdd:cd05909 85 SKQFIEKLKLHHLFDVEYD-ARIVYL-----EDLRAKiskADKCKAFLAGKFPPKWLLRIFGVAPV--QPDDPAVILFTS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 303 GTTGNPKGAMLTHGNVVADFSGFLKV----TESVVYC-----HGgrVGFFQGDIRLLSDDMKALC---PTIFPVVPRLLn 370
Cdd:cd05909 157 GSEGLPKGVVLSHKNLLANVEQITAIfdpnPEDVVFGalpffHS--FGLTGCLWLPLLSGIKVVFhpnPLDYKKIPELI- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 371 rmYDK----IFSqanTPLkrwLLEFAAKRKQAEVRSGIirndsiwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLR 446
Cdd:cd05909 234 --YDKkatiLLG---TPT---FLRGYARAAHPEDFSSL-----------------------RLVVAGAEKLKDTLRQEFQ 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 447 AALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRT 525
Cdd:cd05909 283 EKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELT 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1622946790 526 KEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENI 575
Cdd:cd05909 363 SFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDI 410
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
145-682 |
4.14e-33 |
|
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: 133.59 E-value: 4.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 145 WLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVI 224
Cdd:cd05926 14 ALTYADLAELVDDLARQLAALGIKK--GDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 225 VDKpqkaVLLLEHVERKETPGLkliilmdpfeeALKERGQKCGVVIKSMQAVEDCGQENHHAPV----PPQPDDLSIVCF 300
Cdd:cd05926 92 TPK----GELGPASRAASKLGL-----------AILELALDVGVLIRAPSAESLSNLLADKKNAksegVPLPDDLALILH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 301 TSGTTGNPKGAMLTHGNVVA---DFSGFLKVTES-VVYC-------------------HGGRV----GFfqgDIRLLSDD 353
Cdd:cd05926 157 TSGTTGRPKGVPLTHRNLAAsatNITNTYKLTPDdRTLVvmplfhvhglvasllstlaAGGSVvlppRF---SASTFWPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 354 MKALCPTIFPVVPRLLnrmydKIfsqantplkrwLLEFAAKRKQAEvrsgiirndsiwdelfFNKIqaslggcvRMIVTG 433
Cdd:cd05926 234 VRDYNATWYTAVPTIH-----QI-----------LLNRPEPNPESP----------------PPKL--------RFIRSC 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 434 AAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTP---GDWTSGHVGAPlpcNHIKLVDVEElnywacKGE------ 504
Cdd:cd05926 274 SASLPPAVLEALEATFGAPVLEAYGMTE-AAHQMTSNPlppGPRKPGSVGKP---VGVEVRILDE------DGEilppgv 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 505 -GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVA 583
Cdd:cd05926 344 vGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVLLSHPAVL 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 584 QIYVHGdslkaflvgivVPDP---EVMPSWAQKRgiEGTYADlctskdlKKAILEDMvrlgkESGLHSFEQVKAIHIhsd 660
Cdd:cd05926 423 EAVAFG-----------VPDEkygEEVAAAVVLR--EGASVT-------EEELRAFC-----RKHLAAFKVPKKVYF--- 474
|
570 580
....*....|....*....|..
gi 1622946790 661 mfsVQNGLLTPTLKAKRPELRE 682
Cdd:cd05926 475 ---VDELPKTATGKIQRRKVAE 493
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
241-693 |
5.17e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 132.53 E-value: 5.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 241 KETPGLKLIILMDPFE---------EALKERGQKCGV-------VIKSMQAVEDCGQENhhapvppqPDDLSIVCFTSGT 304
Cdd:PTZ00342 244 NDLSNELEDISLGPLEydkeklekiKDLKEKAKKLGIsiilfddMTKNKTTNYKIQNED--------PDFITSIVYTSGT 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 305 TGNPKGAMLTHGNV------VADFSGFLK--------------VTE-SVVYC---HGGRVGFFQGDIRLLSDDMKALCPT 360
Cdd:PTZ00342 316 SGKPKGVMLSNKNLyntvvpLCKHSIFKKynpkthlsylpishIYErVIAYLsfmLGGTINIWSKDINYFSKDIYNSKGN 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 361 IFPVVPRLLNRMYDKIFSQAN--TPLKRWLlefaAKRKQAEVRSGIIRNDSIWDELFFN---KIQASLGGCVRMIVTGAA 435
Cdd:PTZ00342 396 ILAGVPKVFNRIYTNIMTEINnlPPLKRFL----VKKILSLRKSNNNGGFSKFLEGITHissKIKDKVNPNLEVILNGGG 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 436 PASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPG-DWTSGHVGAPL-PCNHIKLVDVEELNYWACKGEGEICVRGPN 513
Cdd:PTZ00342 472 KLSPKIAEELSVLLNVNYYQGYGLTE-TTGPIFVQHAdDNNTESIGGPIsPNTKYKVRTWETYKATDTLPKGELLIKSDS 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 514 VFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHG-DSL 592
Cdd:PTZ00342 551 IFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGdDSM 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 593 KAFLvGIVVPDPEVM------PSWAQKRGI-EGTYADLCTSKDLKKAILEDMVR-----LGKESGLHSFEQVKAIHIHSD 660
Cdd:PTZ00342 631 DGPL-AIISVDKYLLfkclkdDNMLESTGInEKNYLEKLTDETINNNIYVDYVKgkmleVYKKTNLNRYNIINDIYLTSK 709
|
490 500 510
....*....|....*....|....*....|....*.
gi 1622946790 661 MFSVQNgLLTPTLKAKRPEL-REY--FKKQIEELYS 693
Cdd:PTZ00342 710 VWDTNN-YLTPTFKVKRFYVfKDYafFIDQVKKIYK 744
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
290-603 |
1.69e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 129.73 E-value: 1.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 290 PQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD-------FSGFLKVTESV-------------------VYCHGGRVGFF 343
Cdd:PRK05605 216 PTPDDVALILYTSGTTGKPKGAQLTHRNLFANaaqgkawVPGLGDGPERVlaalpmfhaygltlcltlaVSIGGELVLLP 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 344 QGDIRLLSDDMKALCPTIFPVVPRLlnrmYDKIfsqantplkrwlLEFAAKRkqaevrsGIirndsiwdelffnkiqaSL 423
Cdd:PRK05605 296 APDIDLILDAMKKHPPTWLPGVPPL----YEKI------------AEAAEER-------GV-----------------DL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 424 GGcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECT---AGCTFTTpgDWTSGHVGAPLPCNHIKLVDVEELNYWA 500
Cdd:PRK05605 336 SG-VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpiiVGNPMSD--DRRPGYVGVPFPDTEVRIVDPEDPDETM 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 501 CKGE-GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIyirs 579
Cdd:PRK05605 413 PDGEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELI-ITGGFNVYPAEVEEV---- 486
|
330 340
....*....|....*....|....
gi 1622946790 580 qpVAQiyvHGDSLKAFLVGIVVPD 603
Cdd:PRK05605 487 --LRE---HPGVEDAAVVGLPRED 505
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
294-598 |
1.39e-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: 122.99 E-value: 1.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 294 DLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTESVVYC------H--GGRVGFFQGDIRllsddmkalCPTIF 362
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLraaAAWADCADLTEDDRYLiinpffHtfGYKAGIVACLLT---------GATVV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 363 PV----VPRLLNRMYDKIFSQANTP--LKRWLLEFAAkRKQAEVRSgiirndsiwdelffnkiqaslggcVRMIVTGAAP 436
Cdd:cd17638 72 PVavfdVDAILEAIERERITVLPGPptLFQSLLDHPG-RKKFDLSS------------------------LRAAVTGAAT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 437 ASPTVLGFLRAALGCQ-VYEGYGQTECTAGcTFTTPGD---WTSGHVGAPLPCNHIKLVDveelnywackgEGEICVRGP 512
Cdd:cd17638 127 VPVELVRRMRSELGFEtVLTAYGLTEAGVA-TMCRPGDdaeTVATTCGRACPGFEVRIAD-----------DGEVLVRGY 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 513 NVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYV----- 587
Cdd:cd17638 195 NVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGALAEHPGVAQVAVigvpd 273
|
330
....*....|...
gi 1622946790 588 --HGDSLKAFLVG 598
Cdd:cd17638 274 erMGEVGKAFVVA 286
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
147-581 |
3.66e-30 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 123.53 E-value: 3.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 147 SYQEVADRAEFLGSGLLQHnCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGA-IRYIINTADISTVIV 225
Cdd:TIGR01733 1 TYRELDERANRLARHLRAA-GGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPL-DPAYPAErLAFILEDAGARLLLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 226 DKPqkavllleHVERKETPGLKLIILMDPFEEALkergqkcgvviksmqavEDCGQENHhAPVPPQPDDLSIVCFTSGTT 305
Cdd:TIGR01733 79 DSA--------LASRLAGLVLPVILLDPLELAAL-----------------DDAPAPPP-PDAPSGPDDLAYVIYTSGST 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 306 GNPKGAMLTHGNVVADFSGFlkvtesvvychGGRVGFFQGDIRL----LSDDMKALcpTIFP---------VVPRllnrm 372
Cdd:TIGR01733 133 GRPKGVVVTHRSLVNLLAWL-----------ARRYGLDPDDRVLqfasLSFDASVE--EIFGallagatlvVPPE----- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 373 ydkifsqanTPLKRWLLEFAAKRKQAEVrsgiirndSIWDEL--FFNKIQASLGGC---VRMIVTGAAPASPTVLGFLRA 447
Cdd:TIGR01733 195 ---------DEERDDAALLAALIAEHPV--------TVLNLTpsLLALLAAALPPAlasLRLVILGGEALTPALVDRWRA 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 448 ALG-CQVYEGYGQTECTAGCT-FTTPGDWTSGHV----GAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKD 521
Cdd:TIGR01733 258 RGPgARLINLYGPTETTVWSTaTLVDPDDAPRESpvpiGRPLANTRLYVLD-DDLRPVPVGVVGELYIGGPGVARGYLNR 336
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622946790 522 PDRTKEA-LDSDGWL-------HTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIyIRSQP 581
Cdd:TIGR01733 337 PELTAERfVPDPFAGgdgarlyRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAA-LLRHP 402
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
146-609 |
6.36e-30 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 123.41 E-value: 6.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACY----TYsmvvVPLYDTLGPGAIRYIINTADIS 221
Cdd:cd05930 13 LTYAELDARANRLARYLRERGVGP--GDLVAVLLERSLEMVVAILAVLkagaAY----VPLDPSYPAERLAYILEDSGAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 222 TVIVDkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhhapvppqPDDLSIVCFT 301
Cdd:cd05930 87 LVLTD-----------------------------------------------------------------PDDLAYVIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 302 SGTTGNPKGAMLTHGNVV---ADFSGFLKVTESVVYCHGGRVGFfqgDIRLLSddmkalcptIFP---------VVPRLL 369
Cdd:cd05930 102 SGSTGKPKGVMVEHRGLVnllLWMQEAYPLTPGDRVLQFTSFSF---DVSVWE---------IFGallagatlvVLPEEV 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 370 NRMYDKifsqantpLKRWLlefaakrkqaeVRSGIIRND---SIWDELFFNKIQASLGgCVRMIVTGAAPASPTVL-GFL 445
Cdd:cd05930 170 RKDPEA--------LADLL-----------AEEGITVLHltpSLLRLLLQELELAALP-SLRLVLVGGEALPPDLVrRWR 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 446 RAALGCQVYEGYGQTECTAGCTFT--TPGDWTSGHV--GAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKD 521
Cdd:cd05930 230 ELLPGARLVNLYGPTEATVDATYYrvPPDDEEDGRVpiGRPIPNTRVYVLD-ENLRPVPPGVPGELYIGGAGLARGYLNR 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 522 PDRTKEA-----LDSDGWLH-TGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYV---HGDSL 592
Cdd:cd05930 309 PELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIELGEIEAALLAHPGVREAAVvarEDGDG 387
|
490
....*....|....*..
gi 1622946790 593 KAFLVGIVVPDPEVMPS 609
Cdd:cd05930 388 EKRLVAYVVPDEGGELD 404
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
146-587 |
6.86e-30 |
|
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: 123.26 E-value: 6.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADIstviv 225
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGP--GDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 226 dkpqkavlllehverketpglKLIILMDPFeealkergqkcgvviksmqavedcGQENHHApvppQPDDLSIVCFTSGTT 305
Cdd:cd05903 75 ---------------------KVFVVPERF------------------------RQFDPAA----MPDAVALLLFTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 306 GNPKGAMLTHGNVVADFSGF---LKVTESVVYCHGGRVGFFQGDIRLLsddmkaLCPTIFPVvPRLLNRMYDK------- 375
Cdd:cd05903 106 GEPKGVMHSHNTLSASIRQYaerLGLGPGDVFLVASPMAHQTGFVYGF------TLPLLLGA-PVVLQDIWDPdkalalm 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 376 -----IFSQANTPLKRWLLEfaAKRKQAEVRSGIirndsiwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALG 450
Cdd:cd05903 179 rehgvTFMMGATPFLTDLLN--AVEEAGEPLSRL-----------------------RTFVCGGATVPRSLARRAAELLG 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 451 CQVYEGYGQTECTAGCTFTTPGD----WTSGhvGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTK 526
Cdd:cd05903 234 AKVCSAYGSTECPGAVTSITPAPedrrLYTD--GRPLPGVEIKVVD-DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTA 310
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622946790 527 EALDsDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYV 587
Cdd:cd05903 311 DAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAV 369
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
280-597 |
8.30e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 124.49 E-value: 8.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 280 GQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFsgfLKVTESVvychGGRVG------------------ 341
Cdd:PRK05677 194 GAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANM---LQCRALM----GSNLNegceiliaplplyhiyaf 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 342 FFQGDIRLLSDDMKALC--PTIFPVVPRLLNRMYDKIFSQANTplkrwllEFAAkrkqaevrsgiIRNDSIWDELFFNKI 419
Cdd:PRK05677 267 TFHCMAMMLIGNHNILIsnPRDLPAMVKELGKWKFSGFVGLNT-------LFVA-----------LCNNEAFRKLDFSAL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 420 QASLGGcvRMIVTGAAPASptvlgfLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDvEELNYW 499
Cdd:PRK05677 329 KLTLSG--GMALQLATAER------WKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVID-DDGNEL 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 500 ACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIyIRS 579
Cdd:PRK05677 400 PLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVSGFNVYPNELEDV-LAA 477
|
330 340
....*....|....*....|....*.
gi 1622946790 580 QP----VAQIYV----HGDSLKAFLV 597
Cdd:PRK05677 478 LPgvlqCAAIGVpdekSGEAIKVFVV 503
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
144-614 |
2.59e-29 |
|
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: 122.01 E-value: 2.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 144 QWLSYQEVADRAEFLGSGLLQHNckACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGA-IRYIINTADIST 222
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARG--VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPL-DPDYPADrLRYILEDAEPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 223 VIVDkpqkavlllehverketpglkliilmdpfeEALKERGQKCGVVIksMQAVEDCGQENHHAPVPPQPDDLSIVCFTS 302
Cdd:cd12116 88 VLTD------------------------------DALPDRLPAGLPVL--LLALAAAAAAPAAPRTPVSPDDLAYVIYTS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 303 GTTGNPKGAMLTHGNVVADFSGFlkvtesvvychGGRVGFFQGDiRLLsddmkALCPTIFPV-VPRLLnrmydkifsqan 381
Cdd:cd12116 136 GSTGRPKGVVVSHRNLVNFLHSM-----------RERLGLGPGD-RLL-----AVTTYAFDIsLLELL------------ 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 382 TPL---KRWLLEFAAKRKQAEVRSGIIRNDSI---------WDELFFNKIQASLGgcVRMIVTGAApaSPTVLGFLRAAL 449
Cdd:cd12116 187 LPLlagARVVIAPRETQRDPEALARLIEAHSItvmqatpatWRMLLDAGWQGRAG--LTALCGGEA--LPPDLAARLLSR 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 450 GCQVYEGYGQTECT--AGCTFTTPGDwTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKE 527
Cdd:cd12116 263 VGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLD-AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAE 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 528 ALDSDGWLH-------TGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQ--IYVHGDSLKAFLVG 598
Cdd:cd12116 341 RFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQVKI-RGHRIELGEIEAALAAHPGVAQaaVVVREDGGDRRLVA 419
|
490
....*....|....*.
gi 1622946790 599 IVVPDPEVMPSWAQKR 614
Cdd:cd12116 420 YVVLKAGAAPDAAALR 435
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
147-605 |
3.54e-29 |
|
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: 122.25 E-value: 3.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 147 SYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLgpgAIRYIINTADIST-VIV 225
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLK--QNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIY---NERELDHSLNISKpTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 226 DKPQKAVLLLEHVERKeTPGLKLIILMDPFEEAlkeRGQKCGVVIKSMQAVEDCGQENHHAPVPPQPDDLSIVCFTSGTT 305
Cdd:cd17642 121 FCSKKGLQKVLNVQKK-LKIIKTIIILDSKEDY---KGYQCLYTFITQNLPPGFNEYDFKPPSFDRDEQVALIMNSSGST 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 306 GNPKGAMLTHGNVVADFS-------GFLKVTESVVYChggRVGFFQGdIRLLSDDMKALCPtiFPVVprLLNRMYDKIFS 378
Cdd:cd17642 197 GLPKGVQLTHKNIVARFShardpifGNQIIPDTAILT---VIPFHHG-FGMFTTLGYLICG--FRVV--LMYKFEEELFL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 379 QA-------NTPLKRWLLEFAAKrkqaevrSGIIrndsiwdelffNKIQASlggCVRMIVTGAAPASPTVLGFLRAALGC 451
Cdd:cd17642 269 RSlqdykvqSALLVPTLFAFFAK-------STLV-----------DKYDLS---NLHEIASGGAPLSKEVGEAVAKRFKL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 452 Q-VYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALD 530
Cdd:cd17642 328 PgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALID 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622946790 531 SDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRsqpvaqiyvHGDSLKAFLVGIvvPDPE 605
Cdd:cd17642 408 KDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQ---------HPKIFDAGVAGI--PDED 470
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
146-612 |
8.50e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 121.25 E-value: 8.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAE-----FLGSGLLQHNCkactdqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADI 220
Cdd:PRK06188 38 LTYGQLADRISryiqaFEALGLGTGDA-------VALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 221 STVIVDK---PQKAVLLLEHVerketPGLKLIILMDPFEEalkerGQKCGVVIKSMQavedcgqenhHAPVPP--QPDDL 295
Cdd:PRK06188 111 STLIVDPapfVERALALLARV-----PSLKHVLTLGPVPD-----GVDLLAAAAKFG----------PAPLVAaaLPPDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 296 SIVCFTSGTTGNPKGAMLTHGNVV-------ADFS-----GFLKVTEsvvYCHGGRVGFFQ-----GDIRLLSD-DMKAL 357
Cdd:PRK06188 171 AGLAYTGGTTGKPKGVMGTHRSIAtmaqiqlAEWEwpadpRFLMCTP---LSHAGGAFFLPtllrgGTVIVLAKfDPAEV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 358 CPTI--------FpVVPRLLNRmydkifsqantplkrwLLEFAAKRKqaevrsgiiRNDSiwdelffnkiqaSLggcvRM 429
Cdd:PRK06188 248 LRAIeeqritatF-LVPTMIYA----------------LLDHPDLRT---------RDLS------------SL----ET 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 430 IVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHV------GAPLPCNHIKLVDvEELNYWAcKG 503
Cdd:PRK06188 286 VYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLRVALLD-EDGREVA-QG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 504 E-GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPV 582
Cdd:PRK06188 364 EvGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMI-VTGGFNVFPREVEDVLAEHPAV 441
|
490 500 510
....*....|....*....|....*....|....*..
gi 1622946790 583 AQIYV-------HGDSLKAflvgIVVPDPEVMPSWAQ 612
Cdd:PRK06188 442 AQVAVigvpdekWGEAVTA----VVVLRPGAAVDAAE 474
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
175-605 |
1.06e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 120.30 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 175 IGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAvlllehverketpglkliilmdp 254
Cdd:PRK09088 50 LAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDDAVAA----------------------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 255 feealkerGQKCGVVIKSMQAVEDCGQENHHAPVPPqpDDLSIVCFTSGTTGNPKGAMLTHGN---VVADFSGFLKVT-E 330
Cdd:PRK09088 107 --------GRTDVEDLAAFIASADALEPADTPSIPP--ERVSLILFTSGTSGQPKGVMLSERNlqqTAHNFGVLGRVDaH 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 331 SVVYC-------------------HGGRV----GFFQG-DIRLLSDdmKALCPTIFPVVPRLLNRmydkifsqantplkr 386
Cdd:PRK09088 177 SSFLCdapmfhiiglitsvrpvlaVGGSIlvsnGFEPKrTLGRLGD--PALGITHYFCVPQMAQA--------------- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 387 wllefaakrkqaevrsgiIRNDSIWDELFFNKIQAslggcvrmIVTGAAP-ASPTVLGFLraALGCQVYEGYGQTEctAG 465
Cdd:PRK09088 240 ------------------FRAQPGFDAAALRHLTA--------LFTGGAPhAAEDILGWL--DDGIPMVDGFGMSE--AG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 466 CTFTTPGDWT-----SGHVGAPLPCNHIKLVDVEELNYWAckGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGD 539
Cdd:PRK09088 290 TVFGMSVDCDvirakAGAAGIPTPTVQTRVVDDQGNDCPA--GVpGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGD 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622946790 540 IGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIEniyirsqpvAQIYVHGDSLKAFLVGivVPDPE 605
Cdd:PRK09088 368 IARRDADGFFWVVDRKKDMF-ISGGENVYPAEIE---------AVLADHPGIRECAVVG--MADAQ 421
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
175-614 |
1.10e-28 |
|
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: 119.48 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 175 IGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlllehVERKETPGLKLIILMDP 254
Cdd:TIGR01923 27 VALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL---------LEEKDFQADSLDRIEAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 255 FEEALKERGQKcgvviksmqavedcgqenhhapvppQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF---LKVTE- 330
Cdd:TIGR01923 98 GRYETSLSASF-------------------------NMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSkenLGFTEd 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 331 ---------------SVVY---CHGGRVGFFQGDIRLLsDDMKALCPTIFPVVPRLLNRMYDKifSQANTPLKRWLLefa 392
Cdd:TIGR01923 153 dnwllslplyhisglSILFrwlIEGATLRIVDKFNQLL-EMIANERVTHISLVPTQLNRLLDE--GGHNENLRKILL--- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 393 akrkqaevrsgiirndsiwdelffnkiqaslGGcvrmivtGAAPASptvlgFLRAAL--GCQVYEGYGQTE-CTAGCTFT 469
Cdd:TIGR01923 227 -------------------------------GG-------SAIPAP-----LIEEAQqyGLPIYLSYGMTEtCSQVTTAT 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 470 TPGDWTSGHVGAPLPCNHIKL-VDVEElnywackGEGEICVRGPNVFKGYLkDPDRTKEALDSDGWLHTGDIGKWLPAGT 548
Cdd:TIGR01923 264 PEMLHARPDVGRPLAGREIKIkVDNKE-------GHGEIMVKGANLMKGYL-YQGELTPAFEQQGWFNTGDIGELDGEGF 335
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622946790 549 LKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYV--HGDSL-----KAFLVGIVVPDPEVMPSWAQKR 614
Cdd:TIGR01923 336 LYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVVvpKPDAEwgqvpVAYIVSESDISQAKLIAYLTEK 407
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
142-556 |
1.18e-28 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 120.85 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 142 PYQWLSYQEVADRAEFLGSGLLQHNCKAcTDQFIGVFAQNRpEWIIAELACYTYSMVVVPLydtlGPGAIRyiintadis 221
Cdd:cd05906 36 SEEFQSYQDLLEDARRLAAGLRQLGLRP-GDSVILQFDDNE-DFIPAFWACVLAGFVPAPL----TVPPTY--------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 222 tvivDKPQKAVLLLEHVerKETPGLKLII----LMDPFEEALKERGQkCGVVIKSMQAVEDCGqENHHAPvPPQPDDLSI 297
Cdd:cd05906 101 ----DEPNARLRKLRHI--WQLLGSPVVLtdaeLVAEFAGLETLSGL-PGIRVLSIEELLDTA-ADHDLP-QSRPDDLAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 298 VCFTSGTTGNPKGAMLTHGNVVADFSG------------FLK------VTeSVVYCHggrvgffQGDIRLLSDDMKALCP 359
Cdd:cd05906 172 LMLTSGSTGFPKAVPLTHRNILARSAGkiqhngltpqdvFLNwvpldhVG-GLVELH-------LRAVYLGCQQVHVPTE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 360 TIFPVVPRLLNRMyDKiFSQANTplkrWLLEFA-AK-RKQAEVRSgiirnDSIWDelffnkiqasLGGCVRMIVTGAAPA 437
Cdd:cd05906 244 EILADPLRWLDLI-DR-YRVTIT----WAPNFAfALlNDLLEEIE-----DGTWD----------LSSLRYLVNAGEAVV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 438 SPTVLGFLRAALGCQVYE-----GYGQTECTAGCTFTTP---GDWTSGH----VGAPLPCNHIKLVDVEElnywACKGEG 505
Cdd:cd05906 303 AKTIRRLLRLLEPYGLPPdairpAFGMTETCSGVIYSRSfptYDHSQALefvsLGRPIPGVSMRIVDDEG----QLLPEG 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1622946790 506 EIC---VRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkWLPAGTLKVIDRKK 556
Cdd:cd05906 379 EVGrlqVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
294-605 |
2.92e-28 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 118.16 E-value: 2.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 294 DLSIVCFTSGTTGNPKGAMLTHGNvvadfsgflkvtesvvYCHGGRVGFFQGDIRllSDDmkalcpTIFPVVP-----RL 368
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHAN----------------LTFAGYYSARRFGLG--EDD------VYLTVLPlfhinAQ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 369 LNRMYDKIFSQAN-TPLKRwlleFAAKRKQAEVRsgiiRNDSIWdelfFNkiqaSLGGCVRMI---------------VT 432
Cdd:cd05934 138 AVSVLAALSVGATlVLLPR----FSASRFWSDVR----RYGATV----TN----YLGAMLSYLlaqppspddrahrlrAA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 433 GAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEelNYWACKGE-GEICVR- 510
Cdd:cd05934 202 YGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDD--GQELPAGEpGELVIRg 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 511 --GPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYVH 588
Cdd:cd05934 280 lrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVERAILRHPAVREAAVV 357
|
330 340
....*....|....*....|....
gi 1622946790 589 G-------DSLKAFlvgIVVPDPE 605
Cdd:cd05934 358 AvpdevgeDEVKAV---VVLRPGE 378
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
280-597 |
3.07e-28 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 119.93 E-value: 3.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 280 GQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFsgflkvtESVVYCHGGRVGFFQGDIRLLSDDMKALCP 359
Cdd:PRK12492 194 GRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANM-------LQVRACLSQLGPDGQPLMKEGQEVMIAPLP 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 360 tIFPVVPRLLNRMYDKIFSQANT-------------PLKRWLLE--------FAAKRKQAEVRSgiirndsiwdeLFFNK 418
Cdd:PRK12492 267 -LYHIYAFTANCMCMMVSGNHNVlitnprdipgfikELGKWRFSallglntlFVALMDHPGFKD-----------LDFSA 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 419 IQASLGGcvrmivtGAAPASPTVLGFlRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDvEELN 497
Cdd:PRK12492 335 LKLTNSG-------GTALVKATAERW-EQLTGCTIVEGYGLTETSPVASTNPYGELARlGTVGIPVPGTALKVID-DDGN 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 498 YWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYI 577
Cdd:PRK12492 406 ELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLI-IVSGFNVYPNEIEDVVM 484
|
330 340
....*....|....*....|....*..
gi 1622946790 578 RSQPVAQIYV-------HGDSLKAFLV 597
Cdd:PRK12492 485 AHPKVANCAAigvpderSGEAVKLFVV 511
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
114-693 |
3.66e-28 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 121.50 E-value: 3.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 114 ARTMYQVFRRGLSISGNGPCLGFRKPNQPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACY 193
Cdd:PTZ00297 426 VRSLGEMWERSVTRHSTFRCLGQTSESGESEWLTYGTVDARARELGSGLLALGVRP--GDVIGVDCEASRNIVILEVACA 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 194 TYSMVVVPLydtLGPG-AIRYIINTADISTVIVDKPQKAVLLLEHVERKETpglklIILMDPFEEALKERGQK-CGVVIK 271
Cdd:PTZ00297 504 LYGFTTLPL---VGKGsTMRTLIDEHKIKVVFADRNSVAAILTCRSRKLET-----VVYTHSFYDEDDHAVARdLNITLI 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 272 SMQAVEdcgQENHHAPVPPQP--DDLSIVCFTSGTTGNPKGAML-----THGNVVADFSGFLKVT--------ESVVY-- 334
Cdd:PTZ00297 576 PYEFVE---QKGRLCPVPLKEhvTTDTVFTYVVDNTTSASGDGLavvrvTHADVLRDISTLVMTGvlpssfkkHLMVHft 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 335 ---------------CHGGRVGffQGDIRLLSDDMKALCPTIFPVVPRLlnrmydkiFSQANTPLKR----------WLL 389
Cdd:PTZ00297 653 pfamlfnrvfvlglfAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSL--------FSTSRLQLSRanerysavysWLF 722
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 390 EfaakrKQAEVRSGII----RNDSIWDELFFNKIQASLGGCVRMIVTGAAPASPTV-----LGFLRAALGCQVYegygQT 460
Cdd:PTZ00297 723 E-----RAFQLRSRLInihrRDSSLLRFIFFRATQELLGGCVEKIVLCVSEESTSFsllehISVCYVPCLREVF----FL 793
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 461 ECTAGCTFTtpgdwtsghvGAPLPCNHIKLVDVEELNYWACKGEGEICVRGpnvfkgylkDPDRTKEAldsdgwlhtgdI 540
Cdd:PTZ00297 794 PSEGVFCVD----------GTPAPSLQVDLEPFDEPSDGAGIGQLVLAKKG---------EPRRTLPI-----------A 843
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 541 GKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAfLVGIVVPDPEVMP-SWAQKRGIE-- 617
Cdd:PTZ00297 844 AQWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEfEWRQSHCMGeg 922
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 618 GTYADLCTSKDLKK----AILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 693
Cdd:PTZ00297 923 GGPARQLGWTELVAyassLLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIERFYS 1002
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
118-543 |
4.46e-28 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 119.45 E-value: 4.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 118 YQVFRRGLSISGNGPCLGFRKPNQPYQWLSYQEVADRAEFLGSGLLQHnckactdqfiGV--------FAQNRPEWIIAE 189
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRAL----------GVkkgdrvaiYLPNIPEAVIAM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 190 LACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVD----KPQKAVLLLEHVE--RKETPGLKLIILMD---------- 253
Cdd:COG0365 82 LACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITAdgglRGGKVIDLKEKVDeaLEELPSLEHVIVVGrtgadvpmeg 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 254 --PFEEALKERGQKCgvviksmqavedcgqenhhAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVV------------ 319
Cdd:COG0365 162 dlDWDELLAAASAEF-------------------EPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLvhaattakyvld 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 320 ----------ADFsGFLKVTESVVY---CHG-------GRVGFFQGDiRLLS--DDMKalcPTIFPVVPRLLnRMydkif 377
Cdd:COG0365 223 lkpgdvfwctADI-GWATGHSYIVYgplLNGatvvlyeGRPDFPDPG-RLWEliEKYG---VTVFFTAPTAI-RA----- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 378 sqantpLKRWLLEFAAKRKQAevrsgiirndsiwdelffnkiqaSLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGY 457
Cdd:COG0365 292 ------LMKAGDEPLKKYDLS-----------------------SL----RLLGSAGEPLNPEVWEWWYEAVGVPIVDGW 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 458 GQTECtaGCTFTTPGDWTS---GHVGAPLPCNHIKLVDvEELNywACKG--EGEICVRG--PNVFKGYLKDPDRTKEAL- 529
Cdd:COG0365 339 GQTET--GGIFISNLPGLPvkpGSMGKPVPGYDVAVVD-EDGN--PVPPgeEGELVIKGpwPGMFRGYWNDPERYRETYf 413
|
490
....*....|....*
gi 1622946790 530 -DSDGWLHTGDIGKW 543
Cdd:COG0365 414 gRFPGWYRTGDGARR 428
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
292-589 |
4.70e-28 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 115.84 E-value: 4.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSGF-LKVTESVVYC--------------------HGGRVGFFQgdir 348
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVnnGYFIGErLGLTEQDRLCipvplfhcfgsvlgvlacltHGATMVFPS---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 349 lLSDDMKAL--------C------PTIFPvvpRLLNRMydkifSQANTPLKRwllefaakrkqaeVRSGIIrndsiwdel 414
Cdd:cd05917 77 -PSFDPLAVleaiekekCtalhgvPTMFI---AELEHP-----DFDKFDLSS-------------LRTGIM--------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 415 ffnkiqaslggcvrmivtGAAPASPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGDWTS---GHVGAPLPCNHIKL 490
Cdd:cd05917 126 ------------------AGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDSIEkrvNTVGRIMPHTEAKI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 491 VDvEELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAP 569
Cdd:cd05917 188 VD-PEGGIVPPVGVpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGENIYP 265
|
330 340
....*....|....*....|
gi 1622946790 570 EKIENIYIRSQPVAQIYVHG 589
Cdd:cd05917 266 REIEEFLHTHPKVSDVQVVG 285
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
181-597 |
2.52e-27 |
|
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: 115.51 E-value: 2.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 181 NRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKpqkavlllehverketpglkliilmdpfeealk 260
Cdd:cd05972 34 RVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA--------------------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 261 ergqkcgvviksmqavedcgqenhhapvppqpDDLSIVCFTSGTTGNPKGAMLTHgnvvadfSGFLKVTESVVYCHGGRv 340
Cdd:cd05972 81 --------------------------------EDPALIYFTSGTTGLPKGVLHTH-------SYPLGHIPTAAYWLGLR- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 341 gffQGDIRLLSDD----MKALCPTIFPV---VPRLLN--------RMYDKI-------FSQANTPLKRWLLEFAAKRKQA 398
Cdd:cd05972 121 ---PDDIHWNIADpgwaKGAWSSFFGPWllgATVFVYegprfdaeRILELLerygvtsFCGPPTAYRMLIKQDLSSYKFS 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 399 EVRSgiirndsiwdelffnkiqaslggcvrmIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGH 478
Cdd:cd05972 198 HLRL---------------------------VVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGS 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 479 VGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNV--FKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKK 556
Cdd:cd05972 251 MGRPTPGYDVAIID-DDGRELPPGEEGDIAIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRAD 328
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1622946790 557 HIFKlAQGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLV 597
Cdd:cd05972 329 DIIK-SSGYRIGPFEVESALLEHPAVAEAAVvgspdpvRGEVVKAFVV 375
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
137-605 |
2.67e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 116.60 E-value: 2.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 137 RKPNQPYQW-----LSYQEVADRAEFLgSGLLQHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAI 211
Cdd:PRK08314 22 RYPDKTAIVfygraISYRELLEEAERL-AGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 212 RYIINTADISTVIV-----DKPQKAV--LLLEHV-------ERKETPGLKLIILMDpfEEALKERGQKCGVViksmqAVE 277
Cdd:PRK08314 101 AHYVTDSGARVAIVgselaPKVAPAVgnLRLRHVivaqysdYLPAEPEIAVPAWLR--AEPPLQALAPGGVV-----AWK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 278 DCGQENHHA-PVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgflkvteSVVychggrvgffqGDIRLLSDDMKA 356
Cdd:PRK08314 174 EALAAGLAPpPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMA----------NAV-----------GSVLWSNSTPES 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 357 LCPTIFPV--VPRLLNRMYDKIFSQANTPL-KRWLLEFAAkrkQAEVRSGIirndSIWD-------ELFFN-KIQASLGG 425
Cdd:PRK08314 233 VVLAVLPLfhVTGMVHSMNAPIYAGATVVLmPRWDREAAA---RLIERYRV----THWTniptmvvDFLASpGLAERDLS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 426 CVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWT-SGHVGAPLPCNHIKLVDVEELNYWACKGE 504
Cdd:PRK08314 306 SLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTE-TMAQTHSNPPDRPkLQCLGIPTFGVDARVIDPETLEELPPGEV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 505 GEICVRGPNVFKGYLKDPDRTKEA---LDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAPEKIENIYIRSQP 581
Cdd:PRK08314 385 GEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMIN-ASGFKVWPAEVENLLYKHPA 463
|
490 500 510
....*....|....*....|....*....|.
gi 1622946790 582 VAQIYV-------HGDSLKAFlvgiVVPDPE 605
Cdd:PRK08314 464 IQEACViatpdprRGETVKAV----VVLRPE 490
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
146-589 |
3.06e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 116.80 E-value: 3.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVV---PLYDT------LGPGAIRYII- 215
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQP--GDRVGIWAPNCAEWLLTQFATARIGAILVninPAYRAseleyaLGQSGVRWVIc 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 216 ----NTADISTVIVD-KPQKAVLLLEHVERKETPGLKLIILMDPFE-------EALKERGQkcGVVIKSMQAVEdcGQEN 283
Cdd:PRK12583 124 adafKTSDYHAMLQElLPGLAEGQPGALACERLPELRGVVSLAPAPppgflawHELQARGE--TVSREALAERQ--ASLD 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 284 HHAPVPPQpddlsivcFTSGTTGNPKGAMLTHGNVV--ADFSG-FLKVTESVVYChgGRVGFFQGDIRLLSDdmkALCPT 360
Cdd:PRK12583 200 RDDPINIQ--------YTSGTTGFPKGATLSHHNILnnGYFVAeSLGLTEHDRLC--VPVPLYHCFGMVLAN---LGCMT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 361 -----IFPvvprllNRMYD------KIFSQANTPLKRWLLEFAAKRKQAEvrsgiirndsiwdelFFNKIQASLggcvRM 429
Cdd:PRK12583 267 vgaclVYP------NEAFDplatlqAVEEERCTALYGVPTMFIAELDHPQ---------------RGNFDLSSL----RT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 430 IVTGAAPASPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGD-----WTSghVGAPLPCNHIKLVDVEELNywACKG 503
Cdd:PRK12583 322 GIMAGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSLQTTAADdlerrVET--VGRTQPHLEVKVVDPDGAT--VPRG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 504 E-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPV 582
Cdd:PRK12583 398 EiGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMI-IRGGENIYPREIEEFLFTHPAV 476
|
....*..
gi 1622946790 583 AQIYVHG 589
Cdd:PRK12583 477 ADVQVFG 483
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
273-587 |
3.53e-27 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 116.62 E-value: 3.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 273 MQAVEDCGQENHHAPVppQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADF-SGFLKVTESVV--YCHGGRVGFFQgdirl 349
Cdd:PLN02330 166 LEAADRAGDTSDNEEI--LQTDLCALPFSSGTTGISKGVMLTHRNLVANLcSSLFSVGPEMIgqVVTLGLIPFFH----- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 350 LSDDMKALCPTIfpvvprllnRMYDKIFSQANTPLKRWLLEFAAKRKQ-AEVRSGIIRN---DSIWDELFFNKIQaslgg 425
Cdd:PLN02330 239 IYGITGICCATL---------RNKGKVVVMSRFELRTFLNALITQEVSfAPIVPPIILNlvkNPIVEEFDLSKLK----- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 426 cVRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTagCTFTTPGDWTSGH-------VGAPLPCNHIKLVDVEELN 497
Cdd:PLN02330 305 -LQAIMTAAAPLAPELLtAFEAKFPGVQVQEAYGLTEHS--CITLTHGDPEKGHgiakknsVGFILPNLEVKFIDPDTGR 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 498 YWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYI 577
Cdd:PLN02330 382 SLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAILL 460
|
330
....*....|
gi 1622946790 578 RSQPVAQIYV 587
Cdd:PLN02330 461 THPSVEDAAV 470
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
288-597 |
4.41e-27 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 116.31 E-value: 4.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 288 VPPQ--PDDLSIVCFTSGTTGNPKGAMLTHGNVVAD-------FSGFLKV-TESVV-----Y--------CHggrvgFFq 344
Cdd:PRK08974 199 VKPElvPEDLAFLQYTGGTTGVAKGAMLTHRNMLANleqakaaYGPLLHPgKELVVtalplYhifaltvnCL-----LF- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 345 gdIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTPLKRWLlefaakrkqaevrsgiirNDSIWDELFFNKIQASLG 424
Cdd:PRK08974 273 --IELGGQNLLITNPRDIPGFVKELKKYPFTAITGVNTLFNALL------------------NNEEFQELDFSSLKLSVG 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 425 GcvrmivtgAAPASPTVLGFLRAALGCQVYEGYGQTECT---AGCTFTTPGdwTSGHVGAPLPCNHIKLVDvEELNYWAC 501
Cdd:PRK08974 333 G--------GMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVNPYDLDY--YSGSIGLPVPSTEIKLVD-DDGNEVPP 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 502 KGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQP 581
Cdd:PRK08974 402 GEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMI-LVSGFNVYPNEIEDVVMLHPK 479
|
330 340
....*....|....*....|...
gi 1622946790 582 VAQIY-------VHGDSLKAFLV 597
Cdd:PRK08974 480 VLEVAavgvpseVSGEAVKIFVV 502
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
286-606 |
5.79e-27 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 115.89 E-value: 5.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 286 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD-----------FSGFLKVTESVVYC-----H------GGRVGFF 343
Cdd:PRK07059 197 KPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANvlqmeawlqpaFEKKPRPDQLNFVCalplyHifaltvCGLLGMR 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 344 QG----------DIRLLSDDMKALCPTIFPVVPRLLNRMYdkifsqaNTPlkrwllEFaakrkqaevrsgiirndsiwDE 413
Cdd:PRK07059 277 TGgrnilipnprDIPGFIKELKKYQVHIFPAVNTLYNALL-------NNP------DF--------------------DK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 414 LFFNKIQASLGGcvrmivtGAAPASPTVLGFLRAAlGCQVYEGYG--QTECTAGCTFTTPGDWTsGHVGAPLPCNHIKLV 491
Cdd:PRK07059 324 LDFSKLIVANGG-------GMAVQRPVAERWLEMT-GCPITEGYGlsETSPVATCNPVDATEFS-GTIGLPLPSTEVSIR 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 492 DvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEK 571
Cdd:PRK07059 395 D-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMI-LVSGFNVYPNE 472
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1622946790 572 IENIyIRSQP----VAQIYVH----GDSLKAFlvgIVVPDPEV 606
Cdd:PRK07059 473 IEEV-VASHPgvleVAAVGVPdehsGEAVKLF---VVKKDPAL 511
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
138-575 |
6.04e-27 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 115.62 E-value: 6.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 138 KPNQPYQWlSYQEVADRAEFLGSGLLQHNCKACTdqfigVFAQNRPEW---IIAELACYTYSMVVVPLYDTLGPGAIRYI 214
Cdd:PRK06087 43 VDNHGASY-TYSALDHAASRLANWLLAKGIEPGD-----RVAFQLPGWcefTIIYLACLKVGAVSVPLLPSWREAELVWV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 215 INTADISTVIVDKPQKAV--LLLEHVERKETPGLKLIILMDPFEEALKErgqkcgvvIKSMQAVEDcgQENHHAPVPPQP 292
Cdd:PRK06087 117 LNKCQAKMFFAPTLFKQTrpVDLILPLQNQLPQLQQIVGVDKLAPATSS--------LSLSQIIAD--YEPLTTAITTHG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 293 DDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTE----SVVYCH---GGRVGFFQGDIRLLSDDMKALCPTIFPVV 365
Cdd:PRK06087 187 DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNltwqDVFMMPaplGHATGFLHGVTAPFLIGARSVLLDIFTPD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 366 P--RLLNRmyDKI-FSQANTPLkrwllefaakrkqaevrsgiirndsIWDELFFNKIQASLGGCVRMIVTGAAPASPTVL 442
Cdd:PRK06087 267 AclALLEQ--QRCtCMLGATPF-------------------------IYDLLNLLEKQPADLSALRFFLCGGTTIPKKVA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 443 gflRAAL--GCQVYEGYGQTECTAGcTFTTPGD---WTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKG 517
Cdd:PRK06087 320 ---RECQqrGIKLLSVYGSTESSPH-AVVNLDDplsRFMHTDGYAAAGVEIKVVD-EARKTLPPGCEGEEASRGPNVFMG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622946790 518 YLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENI 575
Cdd:PRK06087 395 YLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDI 451
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
198-609 |
8.27e-27 |
|
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: 114.07 E-value: 8.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 198 VVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlLLEHVErketpgLKLIILMDPfeealkergqkcGVVIKsmqaVE 277
Cdd:cd05922 48 VFVPLNPTLKESVLRYLVADAGGRIVLADAG-----AADRLR------DALPASPDP------------GTVLD----AD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 278 DCGQENHHAP-VPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTE--------SVVYCHGGRV---GF 342
Cdd:cd05922 101 GIRAARASAPaHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSiaeYLGITAddraltvlPLSYDYGLSVlntHL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 343 FQGDIRLLS----------DDMKALCPTIFPVVP---RLLNRMydkIFSQANTPLKRWLLEFAAKRKQAEVRSgiirnds 409
Cdd:cd05922 181 LRGATLVLTndgvlddafwEDLREHGATGLAGVPstyAMLTRL---GFDPAKLPSLRYLTQAGGRLPQETIAR------- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 410 iwdelffnkiqaslggcvrmivtgaapasptvlgfLRAAL-GCQVYEGYGQTECTAGCTFTTPG--DWTSGHVGAPLPCN 486
Cdd:cd05922 251 -----------------------------------LRELLpGAQVYVMYGQTEATRRMTYLPPEriLEKPGSIGLAIPGG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 487 HIklvDVEELNYWACK-GE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkWLPA-GTLKVIDRKKHIFKLAq 563
Cdd:cd05922 296 EF---EILDDDGTPTPpGEpGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLA-RRDEdGFLFIVGRRDRMIKLF- 370
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1622946790 564 GEYVAPEKIENIyIRSQP---VAQIYVHGDSLKAFLVGIVVPDPEVMPS 609
Cdd:cd05922 371 GNRISPTEIEAA-ARSIGliiEAAAVGLPDPLGEKLALFVTAPDKIDPK 418
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
280-604 |
1.47e-26 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 114.59 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 280 GQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADF---------SGFLKVTESVVY------------CHGG 338
Cdd:PRK08751 195 GRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMqqahqwlagTGKLEEGCEVVItalplyhifaltANGL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 339 RVGFFQGDIRLLSDdmkalcPTIFPVVPRLLNRMYDKIFSQANTPLKRWLlefaakrkqaevrsgiirNDSIWDELFFNK 418
Cdd:PRK08751 275 VFMKIGGCNHLISN------PRDMPGFVKELKKTRFTAFTGVNTLFNGLL------------------NTPGFDQIDFSS 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 419 IQASLGGcvRMIVTGAapasptVLGFLRAALGCQVYEGYGQTECT-AGCTFTTPGDWTSGHVGAPLPCNHIKLVDvEELN 497
Cdd:PRK08751 331 LKMTLGG--GMAVQRS------VAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDACIKD-DAGT 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 498 YWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYI 577
Cdd:PRK08751 402 VLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-LVSGFNVYPNEIEDVIA 480
|
330 340 350
....*....|....*....|....*....|.
gi 1622946790 578 RSQPVAQIYVHG----DSLKAFLVGIVVPDP 604
Cdd:PRK08751 481 MMPGVLEVAAVGvpdeKSGEIVKVVIVKKDP 511
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
144-614 |
2.78e-26 |
|
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: 115.34 E-value: 2.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 144 QWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELA------CYtysmvvVPLyDTLGPGA-IRYIIN 216
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALGVGP--GDLVGVCLERSLEMVVALLAvlkagaAY------VPL-DPAYPAErLAYMLE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 217 TADISTVIVDkpqkavlllehverketpglkliilmdpfeEALKERGQKCGVVIKSMQAVEDCGQENHHAPVPPQPDDLS 296
Cdd:COG1020 571 DAGARLVLTQ------------------------------SALAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLA 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 297 IVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTESVVY-------------------CHGGRVGFFQGDIRLLSDDM 354
Cdd:COG1020 621 YVIYTSGSTGRPKGVMVEHRALVnllAWMQRRYGLGPGDRVlqfaslsfdasvweifgalLSGATLVLAPPEARRDPAAL 700
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 355 KALC----PTIFPVVPRLLNRMYDkifsqantplkrwllefAAKRKQAEVRsgiirndsiwdelffnkiqaslggcvRMI 430
Cdd:COG1020 701 AELLarhrVTVLNLTPSLLRALLD-----------------AAPEALPSLR--------------------------LVL 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 431 VTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF--TTPGDWTSGHV--GAPLPCNHIKLVDvEELN---YWACkg 503
Cdd:COG1020 738 VGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYyeVTPPDADGGSVpiGRPIANTRVYVLD-AHLQpvpVGVP-- 814
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 504 eGEICVRGPNVFKGYLKDPDRTKEA-----LDSDG--WLHTGDIGKWLPAGTLKVIDRKKHifklaQ----------GEy 566
Cdd:COG1020 815 -GELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNLEFLGRADD-----QvkirgfrielGE- 887
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1622946790 567 vapekIENIyIRSQP-VAQIYV--HGDSL-KAFLVGIVVPDPEVMPSWAQKR 614
Cdd:COG1020 888 -----IEAA-LLQHPgVREAVVvaREDAPgDKRLVAYVVPEAGAAAAAALLR 933
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
147-604 |
1.08e-25 |
|
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: 111.57 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 147 SYQEVADRAEFLGSGLlqHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVD 226
Cdd:cd12119 27 TYAEVAERARRLANAL--RRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 227 K---PQKAVLL--LEHVERketpglklIILMDPFEEALKERGQKcgvVIKSMQAVEDcgqenhHAPVPPQPD----DLSI 297
Cdd:cd12119 105 RdflPLLEAIAprLPTVEH--------VVVMTDDAAMPEPAGVG---VLAYEELLAA------ESPEYDWPDfdenTAAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 298 VCFTSGTTGNPKGAMLTHGNVVadfsgflkvTESVVYCHGGRVGFFQGDirllsddmkalcpTIFPVVPrllnrMYdkif 377
Cdd:cd12119 168 ICYTSGTTGNPKGVVYSHRSLV---------LHAMAALLTDGLGLSESD-------------VVLPVVP-----MF---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 378 sQANTplkrWLLEFAA-----------KRKQAEVRSGIIRND---------SIWDELF--FNKIQASLGGCVRMIVTGAA 435
Cdd:cd12119 217 -HVNA----WGLPYAAamvgaklvlpgPYLDPASLAELIEREgvtfaagvpTVWQGLLdhLEANGRDLSSLRRVVIGGSA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 436 PASPTVLGFlrAALGCQVYEGYGQTECTAGCTFTTPgdwTSGHV--------------GAPLPCNHIKLVDVE--ELNyW 499
Cdd:cd12119 292 VPRSLIEAF--EERGVRVIHAWGMTETSPLGTVARP---PSEHSnlsedeqlalrakqGRPVPGVELRIVDDDgrELP-W 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 500 ACKGEGEICVRGPNVFKGYLKDPDRTkEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRS 579
Cdd:cd12119 366 DGKAVGELQVRGPWVTKSYYKNDEES-EALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSG-GEWISSVELENAIMAH 443
|
490 500
....*....|....*....|....*
gi 1622946790 580 QPVAQIYVhgdslkaflvgIVVPDP 604
Cdd:cd12119 444 PAVAEAAV-----------IGVPHP 457
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
245-577 |
1.18e-25 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 111.61 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 245 GLKLIILMDPFEEALKERGQKCGVVIKSM-QAVEDC--------GQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTH 315
Cdd:PLN02246 122 GAKLIITQSCYVDKLKGLAEDDGVTVVTIdDPPEGClhfseltqADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTH 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 316 GNVVADFSG---------FLKVtESVVYC-----H----------GGRVG--------FfqgDIRLLSDDMKALCPTIFP 363
Cdd:PLN02246 202 KGLVTSVAQqvdgenpnlYFHS-DDVILCvlpmfHiyslnsvllcGLRVGaailimpkF---EIGALLELIQRHKVTIAP 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 364 VVPrllnrmydkifsqantPLkrwLLEFAakrKQAEVRSgiirndsiwDELffnkiqASlggcVRMIVTGAAPASPTVLG 443
Cdd:PLN02246 278 FVP----------------PI---VLAIA---KSPVVEK---------YDL------SS----IRMVLSGAAPLGKELED 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 444 FLRAALGCQVY-EGYGQTE-------CTAgctFT-TPGDWTSGHVGAPLPCNHIKLVDVE---ELNYWACkgeGEICVRG 511
Cdd:PLN02246 317 AFRAKLPNAVLgQGYGMTEagpvlamCLA---FAkEPFPVKSGSCGTVVRNAELKIVDPEtgaSLPRNQP---GEICIRG 390
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622946790 512 PNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYI 577
Cdd:PLN02246 391 PQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAELEALLI 455
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
290-612 |
1.19e-25 |
|
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: 110.13 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 290 PQPDDLSIVCFTSGTTGNPKGAMLTHGN----------------------VVADF--SGFLKVTESVVYchGGRVGFFQG 345
Cdd:cd05912 74 VKLDDIATIMYTSGTTGKPKGVQQTFGNhwwsaigsalnlglteddnwlcALPLFhiSGLSILMRSVIY--GMTVYLVDK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 346 -DIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTPLKRWLLefaakrkqaevrsgiirndsiwdelffnkiqaslg 424
Cdd:cd05912 152 fDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRCILL----------------------------------- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 425 gcvrmivtGAAPASPTVLGFLRAaLGCQVYEGYGQTE-CTAGCTFTtPGDWTS--GHVGAPLPCNHIKLVDVEELNYwac 501
Cdd:cd05912 197 --------GGGPAPKPLLEQCKE-KGIPVYQSYGMTEtCSQIVTLS-PEDALNkiGSAGKPLFPVELKIEDDGQPPY--- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 502 kGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQP 581
Cdd:cd05912 264 -EVGEILLKGPNVTKGYLNRPDATEESFE-NGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPA 340
|
330 340 350
....*....|....*....|....*....|.
gi 1622946790 582 VAQIYVhgdslkaflVGIvvPDPEvmpsWAQ 612
Cdd:cd05912 341 IKEAGV---------VGI--PDDK----WGQ 356
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
114-556 |
1.25e-25 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 112.36 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 114 ARTMYQVFRRGLSISGNGPCLgfrkpnqpyqwlSYQEVADR---------AEFLG-----SGLLqHNCKACTDQFIGVFA 179
Cdd:PRK07529 24 PASTYELLSRAAARHPDAPAL------------SFLLDADPldrpetwtyAELLAdvtrtANLL-HSLGVGPGDVVAFLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 180 QNRPEWIIAELACYTYSmVVVPLYDTLGPGAIRYIINTADISTVIVDKP-------QKAVLLLEHVerketPGLKLIILM 252
Cdd:PRK07529 91 PNLPETHFALWGGEAAG-IANPINPLLEPEQIAELLRAAGAKVLVTLGPfpgtdiwQKVAEVLAAL-----PELRTVVEV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 253 D-------PFEEALKERGQKCGVVIKSMQAVEDCGQENHH-APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsG 324
Cdd:PRK07529 165 DlarylpgPKRLAVPLIRRKAHARILDFDAELARQPGDRLfSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVAN--A 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 325 FLkvtesvvychGGRVGFFQ-GDIRLlsddmkalCPT----IFPVVPRLLnrmydkifsqanTPLKRwllefaakrkQAE 399
Cdd:PRK07529 243 WL----------GALLLGLGpGDTVF--------CGLplfhVNALLVTGL------------APLAR----------GAH 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 400 VRSGII---RNDSIWDEL----------FFN--------KIQASLGG----CVRMIVTGAAPASPTVLGFLRAALGCQVY 454
Cdd:PRK07529 283 VVLATPqgyRGPGVIANFwkiveryrinFLSgvptvyaaLLQVPVDGhdisSLRYALCGAAPLPVEVFRRFEAATGVRIV 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 455 EGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLVDVEEL-NYW--ACKGE-GEICVRGPNVFKGYLkDPDRTKEAL 529
Cdd:PRK07529 363 EGYGLTEATCVSSVNPPdGERRIGSVGLRLPYQRVRVVILDDAgRYLrdCAVDEvGVLCIAGPNVFSGYL-EAAHNKGLW 441
|
490 500
....*....|....*....|....*..
gi 1622946790 530 DSDGWLHTGDIGKWLPAGTLKVIDRKK 556
Cdd:PRK07529 442 LEDGWLNTGDLGRIDADGYFWLTGRAK 468
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
181-575 |
4.46e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 109.87 E-value: 4.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 181 NRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADiSTVIVDKPQKAVLLLEhvERKETPGLKLIILMDP------ 254
Cdd:PRK07786 76 NRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCG-AHVVVTEAALAPVATA--VRDIVPLLSTVVVAGGssddsv 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 255 --FEEALKERGQKcgvviksmqavedcgqenhHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD-----FSGFLK 327
Cdd:PRK07786 153 lgYEDLLAEAGPA-------------------HAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANLTGQamtclRTNGAD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 328 VTESVVYChggRVGFFQ--GDIRLLSDDMKALCPTIFPVVPRLLNRMYDkifsqantplkrwLLEfaakrkqAEVRSGII 405
Cdd:PRK07786 214 INSDVGFV---GVPLFHiaGIGSMLPGLLLGAPTVIYPLGAFDPGQLLD-------------VLE-------AEKVTGIF 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 406 RNDSIWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAgCTFTTPGD---WTSGHVGA 481
Cdd:PRK07786 271 LVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEMSP-VTCMLLGEdaiRKLGSVGK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 482 PLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSdGWLHTGDIGKWLPAGTLKVIDRKKHIFkL 561
Cdd:PRK07786 350 VIPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMI-I 426
|
410
....*....|....
gi 1622946790 562 AQGEYVAPEKIENI 575
Cdd:PRK07786 427 SGGENIYCAEVENV 440
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
146-606 |
4.69e-25 |
|
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: 108.87 E-value: 4.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGA-IRYIINTADISTVI 224
Cdd:cd05945 17 LTYRELKERADALAAALASLGLDA--GDPVVVYGHKSPDAIAAFLAALKAGHAYVPL-DASSPAErIREILDAAKPALLI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 225 VDkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhhapvppqPDDLSIVCFTSGT 304
Cdd:cd05945 94 AD-----------------------------------------------------------------GDDNAYIIFTSGS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 305 TGNPKGAMLTHGNVVADFSG----FLKVTESVVYCHGGrvgfFQGDIRLLSddmkalcptIFP---------VVPRLLNR 371
Cdd:cd05945 109 TGRPKGVQISHDNLVSFTNWmlsdFPLGPGDVFLNQAP----FSFDLSVMD---------LYPalasgatlvPVPRDATA 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 372 MYDKIFSQ-ANTPLKRWLlefaakrkqaevrsgiiRNDSIWDELF----FNkiQASLGGCVRMIVTGAAPASPTVLGFLR 446
Cdd:cd05945 176 DPKQLFRFlAEHGITVWV-----------------STPSFAAMCLlsptFT--PESLPSLRHFLFCGEVLPHKTARALQQ 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 447 AALGCQVYEGYGQTECTAGCTFT--TP---GDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKD 521
Cdd:cd05945 237 RFPDARIYNTYGPTEATVAVTYIevTPevlDGYDRLPIGYAKPGAKLVILD-EDGRPVPPGEKGELVISGPSVSKGYLNN 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 522 PDRTKEALDSD---GWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYV----HGDSlKA 594
Cdd:cd05945 316 PEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIELEEIEAALRQVPGVKEAVVvpkyKGEK-VT 393
|
490
....*....|..
gi 1622946790 595 FLVGIVVPDPEV 606
Cdd:cd05945 394 ELIAFVVPKPGA 405
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
183-604 |
4.97e-25 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 109.58 E-value: 4.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 183 PEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDkPQKAVLLLEHVERKETPGLkliilmdpfeEALKER 262
Cdd:PRK07514 64 PEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCD-PANFAWLSKIAAAAGAPHV----------ETLDAD 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 263 GQkcGVViksMQAVEDCGQEnhHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGN------VVADFSGF----------- 325
Cdd:PRK07514 133 GT--GSL---LEAAAAAPDD--FETVPRGADDLAAILYTSGTTGRSKGAMLSHGNllsnalTLVDYWRFtpddvlihalp 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 326 ------LKVTESVVYCHGGRVGFFQgdiRLLSDDMKALCP--TIFPVVPRLLNRMYdkifsqANTPLKRwllEFAAKrkq 397
Cdd:PRK07514 206 ifhthgLFVATNVALLAGASMIFLP---KFDPDAVLALMPraTVMMGVPTFYTRLL------QEPRLTR---EAAAH--- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 398 aevrsgiirndsiwdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTfTTP--GDWT 475
Cdd:PRK07514 271 -----------------------------MRLFISGSAPLLAETHREFQERTGHAILERYGMTE-TNMNT-SNPydGERR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 476 SGHVGAPLPCNHIKLVDVE---ELNywacKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKV 551
Cdd:PRK07514 320 AGTVGFPLPGVSLRVTDPEtgaELP----PGEiGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHI 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622946790 552 IDRKKHIfkLAQGEY-VAPEKIENiYIRSQP-VAQIYVHGDSLKAF---LVGIVVPDP 604
Cdd:PRK07514 396 VGRGKDL--IISGGYnVYPKEVEG-EIDELPgVVESAVIGVPHPDFgegVTAVVVPKP 450
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
146-589 |
5.10e-25 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 109.28 E-value: 5.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLAALGVK--KGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLIT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 226 DkpqkavlllehverketpglkliilmDPFEEALKERGQkcgVVIKSMQAvedcGQENHHAPVPPQP-DDLSIVCFTSGT 304
Cdd:PRK03640 106 D--------------------------DDFEAKLIPGIS---VKFAELMN----GPKEEAEIQEEFDlDEVATIMYTSGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 305 TGNPKGAMLTHGN----------------------VVADF--SGFLKVTESVVYchGGRV----GFFQGDI-RLLSDDMK 355
Cdd:PRK03640 153 TGKPKGVIQTYGNhwwsavgsalnlglteddcwlaAVPIFhiSGLSILMRSVIY--GMRVvlveKFDAEKInKLLQTGGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 356 alcpTIFPVVPRLLNRMYDKIfSQANTPlkrwllefaakrkqaevrsgiirnDSiwdelffnkiqaslggcVRMIVTGAA 435
Cdd:PRK03640 231 ----TIISVVSTMLQRLLERL-GEGTYP------------------------SS-----------------FRCMLLGGG 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 436 PASPTVLGFLRAAlGCQVYEGYGQTEcTAGCTFTTPGDWTS---GHVGAPL-PCNhIKLVDveELNYWACKGEGEICVRG 511
Cdd:PRK03640 265 PAPKPLLEQCKEK-GIPVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLfPCE-LKIEK--DGVVVPPFEEGEIVVKG 339
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622946790 512 PNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYVHG 589
Cdd:PRK03640 340 PNVTKGYLNREDATRETFQ-DGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPGVAEAGVVG 415
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
289-603 |
8.85e-25 |
|
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: 107.78 E-value: 8.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 289 PPQPDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSGF-LKVTES-------------------VVYCHGGRVgFFQGD 346
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLnyVSQPPArLDVGPGsrvaqvlsiafdacigeifSTLCNGGTL-VLADP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 347 IRLLSDDMKALcpTIFPVVPRLLNRMYDKIFSQantplkrwllefaakrkqaevrsgiirndsiwdelffnkiqaslggc 426
Cdd:cd17653 180 SDPFAHVARTV--DALMSTPSILSTLSPQDFPN----------------------------------------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 427 VRMIVTGAAPASPTVLGflRAALGCQVYEGYGQTECTAGCTFT--TPGDWTsgHVGAPLPCNHIKLVDvEELNYWACKGE 504
Cdd:cd17653 211 LKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTelLPGQPV--TIGKPIPNSTCYILD-ADLQPVPEGVV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 505 GEICVRGPNVFKGYLKDPDRTKEALDSDGWLH------TGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIR 578
Cdd:cd17653 286 GEICISGVQVARGYLGNPALTASKFVPDPFWPgsrmyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEIEEVVLQ 364
|
330 340
....*....|....*....|....*...
gi 1622946790 579 SQPVAQ---IYVHGDSLKAFlvgiVVPD 603
Cdd:cd17653 365 SQPEVTqaaAIVVNGRLVAF----VTPE 388
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
146-614 |
1.56e-24 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 106.79 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGSGLlqHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd05935 2 LTYLELLEVVKKLASFL--SNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 226 DKPQkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhhapvppqpDDLSIVCFTSGTT 305
Cdd:cd05935 80 GSEL---------------------------------------------------------------DDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 306 GNPKGAMLTHGNVVADfsgflkVTESVVYCHGGRvgffqgdirllSDDMKALCPTIFpvVPRLLNRMYDKIFSQANTPL- 384
Cdd:cd05935 97 GLPKGCMHTHFSAAAN------ALQSAVWTGLTP-----------SDVILACLPLFH--VTGFVGSLNTAVYVGGTYVLm 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 385 KRWLLEFAakRKQAEVRSGIIRNDS---IWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTE 461
Cdd:cd05935 158 ARWDRETA--LELIEKYKVTFWTNIptmLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTE 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 462 CTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDG---WLHTG 538
Cdd:cd05935 236 TMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 539 DIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLVgiVVP------DPE 605
Cdd:cd05935 316 DLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVisvpderVGEEVKAFIV--LRPeyrgkvTEE 392
|
....*....
gi 1622946790 606 VMPSWAQKR 614
Cdd:cd05935 393 DIIEWAREQ 401
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
136-614 |
2.73e-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: 2.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 136 FRKPNQPY-----QWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGA 210
Cdd:cd17655 8 EKTPDHTAvvfedQTLTYRELNERANQLARTLREKGVGP--DTIVGIMAERSLEMIVGILGILKAGGAYLPI-DPDYPEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 211 -IRYIINTADISTVIVDKPQKAVLLlehverketpGLKLIILMDpfEEALKERGQkcgvviksmqavedcgqENHHAPVp 289
Cdd:cd17655 85 rIQYILEDSGADILLTQSHLQPPIA----------FIGLIDLLD--EDTIYHEES-----------------ENLEPVS- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 290 pQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkvTESVVYCHGGRVGFFQGdirlLSDDMkalcpTIFPVVPRLL 369
Cdd:cd17655 135 -KSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWA---NKVIYQGEHLRVALFAS----ISFDA-----SVTEIFASLL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 370 --NRMYdkIFSQANTPLKRWLLEFAAKRkqaevRSGIIR-NDSIWDELffNKIQASLGGCVRMIVTGAAPASPTVLGFL- 445
Cdd:cd17655 202 sgNTLY--IVRKETVLDGQALTQYIRQN-----RITIIDlTPAHLKLL--DAADDSEGLSLKHLIVGGEALSTELAKKIi 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 446 -RAALGCQVYEGYGQTECTAGCTF--TTPGDWTSGHV--GAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLK 520
Cdd:cd17655 273 eLFGTNPTITNAYGPTETTVDASIyqYEPETDQQVSVpiGKPLGNTRIYILD-QYGRPQPVGVAGELYIGGEGVARGYLN 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 521 DPDRTKEALDSDGWL------HTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQ---IYVHGDS 591
Cdd:cd17655 352 RPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-RGYRIELGEIEARLLQHPDIKEavvIARKDEQ 430
|
490 500
....*....|....*....|...
gi 1622946790 592 LKAFLVGIVVPDPEVMPSWAQKR 614
Cdd:cd17655 431 GQNYLCAYIVSEKELPVAQLREF 453
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
137-568 |
3.74e-24 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 107.66 E-value: 3.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 137 RKPNQPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPL---YDTLG--PGAI 211
Cdd:PRK08180 61 RGADGGWRRLTYAEALERVRAIAQALLDRGLSA--ERPLMILSGNSIEHALLALAAMYAGVPYAPVspaYSLVSqdFGKL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 212 RYIINTADISTVIVDKPQK-----AVLLLEHVE----RKETPGLKLIilmdPFEEALKERGQKcgvviksmqAVEDcgqe 282
Cdd:PRK08180 139 RHVLELLTPGLVFADDGAAfaralAAVVPADVEvvavRGAVPGRAAT----PFAALLATPPTA---------AVDA---- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 283 nHHAPVppQPDDLSIVCFTSGTTGNPKGAMLTHGNVVA------DFSGFLKVTESV-------------------VYCHG 337
Cdd:PRK08180 202 -AHAAV--GPDTIAKFLFTSGSTGLPKAVINTHRMLCAnqqmlaQTFPFLAEEPPVlvdwlpwnhtfggnhnlgiVLYNG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 338 GR---------VGFFQGDIRLLsddmKALCPTIFPVVPRLlnrmydkifsqantplkrWLLEFAAKRKQAEVRsgiirnd 408
Cdd:PRK08180 279 GTlyiddgkptPGGFDETLRNL----REISPTVYFNVPKG------------------WEMLVPALERDAALR------- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 409 siwdELFFNKiqaslggcVRMIVTGAAPASPTVLGFL----RAALGCQVY--EGYGQTECTAGCTFTTPGDWTSGHVGAP 482
Cdd:PRK08180 330 ----RRFFSR--------LKLLFYAGAALSQDVWDRLdrvaEATCGERIRmmTGLGMTETAPSATFTTGPLSRAGNIGLP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 483 LPCNHIKLVDVEelnywackGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWL----PAGTLKVIDRKKHI 558
Cdd:PRK08180 398 APGCEVKLVPVG--------GKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVdpadPERGLMFDGRIAED 469
|
490
....*....|
gi 1622946790 559 FKLAQGEYVA 568
Cdd:PRK08180 470 FKLSSGTWVS 479
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
181-597 |
4.13e-24 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 106.69 E-value: 4.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 181 NRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDkpQKAVLLLEHVERKETPGLKLIILMDPFEEALK 260
Cdd:PRK08008 71 NCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTS--AQFYPMYRQIQQEDATPLRHICLTRVALPADD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 261 ergqkcGVV----IKSMQAVEDCgqenhHAPvPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLkvtesvvych 336
Cdd:PRK08008 149 ------GVSsftqLKAQQPATLC-----YAP-PLSTDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYY---------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 337 ggrvGFFQGDIRllSDDMKALCPTIFPVVPRLLNRMydKIFSQANTPLkrwLLE-FAAKRKQAEVRsgiirndsiwdelf 415
Cdd:PRK08008 205 ----SAWQCALR--DDDVYLTVMPAFHIDCQCTAAM--AAFSAGATFV---LLEkYSARAFWGQVC-------------- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 416 fnKIQASLGGCVRMIVTG--AAPASPT--------VLGFLRAA----------LGCQVYEGYGQTECTAGCTFTTPGD-- 473
Cdd:PRK08008 260 --KYRATITECIPMMIRTlmVQPPSANdrqhclreVMFYLNLSdqekdafeerFGVRLLTSYGMTETIVGIIGDRPGDkr 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 474 -WTSghVGAPLPCNHIKLVDveELNYWACKGE-GEICVRG---PNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGT 548
Cdd:PRK08008 338 rWPS--IGRPGFCYEAEIRD--DHNRPLPAGEiGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGF 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622946790 549 LKVIDRKKHIFKLAqGEYVAPEKIENIyIRSQP-VAQIYVHG--DSL-----KAFLV 597
Cdd:PRK08008 414 FYFVDRRCNMIKRG-GENVSCVELENI-IATHPkIQDIVVVGikDSIrdeaiKAFVV 468
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
290-604 |
9.42e-24 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 105.91 E-value: 9.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 290 PQPDDLSIVCFTSGTTGNPKGAMLTHGNVvadFSGFLKVTEsvvychggRVGFFQGDIRLLSDDMKALCPTIFPV-VPRL 368
Cdd:PRK13295 194 PGPDDVTQLIYTSGTTGEPKGVMHTANTL---MANIVPYAE--------RLGLGADDVILMASPMAHQTGFMYGLmMPVM 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 369 LN------------RMYDKI------FSQANTPlkrWLLEFAakRKQAEVRSGIirndsiwdelffnkiqASLggcvRMI 430
Cdd:PRK13295 263 LGatavlqdiwdpaRAAELIrtegvtFTMASTP---FLTDLT--RAVKESGRPV----------------SSL----RTF 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 431 VTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPGD---WTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEI 507
Cdd:PRK13295 318 LCAGAPIPGALVERARAALGAKIVSAWGMTENGA-VTLTKLDDpdeRASTTDGCPLPGVEVRVVD-ADGAPLPAGQIGRL 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 508 CVRGPNVFKGYLKDPDRTkeALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQiyv 587
Cdd:PRK13295 396 QVRGCSNFGGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEALLYRHPAIAQ--- 469
|
330
....*....|....*...
gi 1622946790 588 hgdslkaflVGIV-VPDP 604
Cdd:PRK13295 470 ---------VAIVaYPDE 478
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
144-605 |
3.48e-23 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 103.79 E-value: 3.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 144 QWLSYQEVADRAEFLgSGLLQHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTV 223
Cdd:PRK06839 26 EEMTYKQLHEYVSKV-AAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 224 IVDKP-QKAVLLLEHVERKETPglkliilmdpfeealkergqkcgVVIKSMQAVEDCGQENHhapVPPQPDDLSIVCFTS 302
Cdd:PRK06839 105 FVEKTfQNMALSMQKVSYVQRV-----------------------ISITSLKEIEDRKIDNF---VEKNESASFIICYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 303 GTTGNPKGAMLTHGNVVAD-----FSGFLKVTE-SVVYC---HGGRVGFFQgdirllsddmkalCPTIFP----VVPRLL 369
Cdd:PRK06839 159 GTTGKPKGAVLTQENMFWNalnntFAIDLTMHDrSIVLLplfHIGGIGLFA-------------FPTLFAggviIVPRKF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 370 NRmyDKIFSQANTplKRWLLEFAAKRKQAEVRSGIIRNDSIWDElffnkiqaslggcVRMIVTGAAPAS-PTVLGFLRAa 448
Cdd:PRK06839 226 EP--TKALSMIEK--HKVTVVMGVPTIHQALINCSKFETTNLQS-------------VRWFYNGGAPCPeELMREFIDR- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 449 lGCQVYEGYGQTEcTAGCTFTTPGD---WTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRT 525
Cdd:PRK06839 288 -GFLFGQGFGMTE-TSPTVFMLSEEdarRKVGSIGKPVLFCDYELID-ENKNKVEVGEVGELLIRGPNVMKEYWNRPDAT 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 526 KEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDPE 605
Cdd:PRK06839 365 EETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQV---------INKLSDVYEVAVVG--RQHVK 431
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
291-605 |
3.63e-23 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 103.39 E-value: 3.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 291 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVadfsgflkvteSVVYCHGGRVGFfQGDIRLLsddmkALCPTIFPVvprlln 370
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALS-----------TSALAHGRALGL-TSESRVL-----QFASYTFDV------ 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 371 rmydkifSQANTplkrwlleFAAkrkqaeVRSG----IIRNDSIWDEL--FFNKIQASLGG---------------CVRM 429
Cdd:cd05918 161 -------SILEI--------FTT------LAAGgclcIPSEEDRLNDLagFINRLRVTWAFltpsvarlldpedvpSLRT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 430 IVTGAAPASPTVLGflRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPC--------NHIKLVDVeelnywa 500
Cdd:cd05918 220 LVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRPLGAtcwvvdpdNHDRLVPI------- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 501 ckGE-GEICVRGPNVFKGYLKDPDRTKEA-LDSDGWLH------------TGDIGKWLPAGTLKVIDRKKHIFKLaQGEY 566
Cdd:cd05918 291 --GAvGELLIEGPILARGYLNDPEKTAAAfIEDPAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKI-RGQR 367
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1622946790 567 VAPEKIENiYIRSQP------VAQIYVH-GDSLKAFLVGIVVPDPE 605
Cdd:cd05918 368 VELGEIEH-HLRQSLpgakevVVEVVKPkDGSSSPQLVAFVVLDGS 412
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
286-612 |
4.25e-23 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 103.77 E-value: 4.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 286 APVPPQpDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESV--------VY------CH-GGRVGFFQGDIRL- 349
Cdd:PLN02574 192 KPVIKQ-DDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQyeypgsdnVYlaalpmFHiYGLSLFVVGLLSLg 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 350 ----------LSDDMKAL---CPTIFPVVPRLLNRMYDKIFSQANTPLKrwllefaakrkqaevrsgiirndsiwdelff 416
Cdd:PLN02574 271 stivvmrrfdASDMVKVIdrfKVTHFPVVPPILMALTKKAKGVCGEVLK------------------------------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 417 nkiqaslggCVRMIVTGAAPAS-PTVLGFLRAALGCQVYEGYGQTECTAGCT--FTTPGDWTSGHVGAPLPCNHIKLVDV 493
Cdd:PLN02574 320 ---------SLKQVSCGAAPLSgKFIQDFVQTLPHVDFIQGYGMTESTAVGTrgFNTEKLSKYSSVGLLAPNMQAKVVDW 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 494 EELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIE 573
Cdd:PLN02574 391 STGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQIAPADLE 469
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1622946790 574 NIYIrSQP----VAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQ 612
Cdd:PLN02574 470 AVLI-SHPeiidAAVTAVPDKECGEIPVAFVVRRQGSTLSQEA 511
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
145-541 |
5.34e-23 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 103.47 E-value: 5.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 145 WLSYQEVADRAEFLGSGLLQHNckACTDQFIGVFAQNrPEWIIAELACYTYSMVVVPLYDTLGPGA---IRYIINTADIS 221
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAVG--KPGDRVLLLAPPG-LDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 222 TVIVDKPQKAvLLLEHVERKETPGLKLIILMDPFEEALKERGQkcgvviksmqavedcgqenhhaPVPPQPDDLSIVCFT 301
Cdd:cd05931 101 VVLTTAAALA-AVRAFAASRPAAGTPRLLVVDLLPDTSAADWP----------------------PPSPDPDDIAYLQYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 302 SGTTGNPKGAMLTHGNVVADFSGflkvtesvvychGGRVGFFQGDIRLLS-----DDM---KALCPTIF---PVVprLLN 370
Cdd:cd05931 158 SGSTGTPKGVVVTHRNLLANVRQ------------IRRAYGLDPGDVVVSwlplyHDMgliGGLLTPLYsggPSV--LMS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 371 RMYdkiFSQAntPLkRWL-----------------LEFAAKRKQAEVRSGIirndsiwdELffnkiqaslgGCVRMIVTG 433
Cdd:cd05931 224 PAA---FLRR--PL-RWLrlisryratisaapnfaYDLCVRRVRDEDLEGL--------DL----------SSWRVALNG 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 434 AAPASPTVL----------GFLRAAlgcqVYEGYGQTECTAGCTFTTPG----------DWTSGHV-------------- 479
Cdd:cd05931 280 AEPVRPATLrrfaeafapfGFRPEA----FRPSYGLAEATLFVSGGPPGtgpvvlrvdrDALAGRAvavaaddpaarelv 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 480 --GAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKE------ALDSDGWLHTGDIG 541
Cdd:cd05931 356 scGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaATDEGGWLRTGDLG 425
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
285-609 |
6.74e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 102.38 E-value: 6.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 285 HAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKV---TESVVYCH--------------------GGRV- 340
Cdd:PRK07787 120 HRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAwqwTADDVLVHglplfhvhglvlgvlgplriGNRFv 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 341 --GFF--QGDIRLLSDDmkalcPTIFPVVPRllnrMYDKIfsqantplkrwllefAAKRKQAEVRSGiirndsiwdelff 416
Cdd:PRK07787 200 htGRPtpEAYAQALSEG-----GTLYFGVPT----VWSRI---------------AADPEAARALRG------------- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 417 nkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDvEEL 496
Cdd:PRK07787 243 ----------ARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVD-EDG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 497 NYWACKGE--GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDR------KKHIFKLAQGEyva 568
Cdd:PRK07787 312 GPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGGYRIGAGE--- 388
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1622946790 569 pekIENIYIRSQPVAQIYVHG---DSLKAFLVGIVVPDPEVMPS 609
Cdd:PRK07787 389 ---IETALLGHPGVREAAVVGvpdDDLGQRIVAYVVGADDVAAD 429
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
146-607 |
5.89e-22 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 100.27 E-value: 5.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIAELACYTYSMVVV---PLYDTlgpGAIRYIINTADIST 222
Cdd:PRK08315 44 WTYREFNEEVDALAKGLLALGIEK-GDR-VGIWAPNVPEWVLTQFATAKIGAILVtinPAYRL---SELEYALNQSGCKA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 223 -VIVDK--------------PQKAVLLLEHVERKETPGLKLIILMDpfeeALKERGqkcgvvIKSMQAVEDCGQENHHAP 287
Cdd:PRK08315 119 lIAADGfkdsdyvamlyelaPELATCEPGQLQSARLPELRRVIFLG----DEKHPG------MLNFDELLALGRAVDDAE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 288 VPP-----QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsGFLkVTESVVYCHGGR----VGFFQ--GDIrllsddMKA 356
Cdd:PRK08315 189 LAArqatlDPDDPINIQYTSGTTGFPKGATLTHRNILNN--GYF-IGEAMKLTEEDRlcipVPLYHcfGMV------LGN 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 357 L-CPT-----IFPVvprllnrmydkifsQANTPLKrwLLEFAAKRK-----------QAEVrsgiirndsiwDELFFNKI 419
Cdd:PRK08315 260 LaCVThgatmVYPG--------------EGFDPLA--TLAAVEEERctalygvptmfIAEL-----------DHPDFARF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 420 QASlggCVRmivTGAAPASPtvlgflraalgC------QVYE---------GYGQTECTAGCTFTTPGD------WTsgh 478
Cdd:PRK08315 313 DLS---SLR---TGIMAGSP-----------CpievmkRVIDkmhmsevtiAYGMTETSPVSTQTRTDDplekrvTT--- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 479 VGAPLPCNHIKLVDVEelnywacKGE-------GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkwlpagtlkV 551
Cdd:PRK08315 373 VGRALPHLEVKIVDPE-------TGEtvprgeqGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLA---------V 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622946790 552 IDrkkhifklAQGeYVapeKI------------ENIYIRsqpvaQI----YVHGDSLKAFLVGivVPDP----EVM 607
Cdd:PRK08315 437 MD--------EEG-YV---NIvgrikdmiirggENIYPR-----EIeeflYTHPKIQDVQVVG--VPDEkygeEVC 493
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
146-604 |
6.85e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 100.01 E-value: 6.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK08316 37 WTYAELDAAVNRVAAALLDLGLKK-GDR-VAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 226 DkpqkaVLLLEHVErketPGLKLIiLMDPFEEALKERGQkcgVVIKSMQAVEDC--GQENHHAPVPPQPDDLSIVCFTSG 303
Cdd:PRK08316 115 D-----PALAPTAE----AALALL-PVDTLILSLVLGGR---EAPGGWLDFADWaeAGSVAEPDVELADDDLAQILYTSG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 304 TTGNPKGAMLTHGNVVADFSGflkvteSVVYChggrvGFFQGDIRLL------SDDMKALCPTIF-----------PVVP 366
Cdd:PRK08316 182 TESLPKGAMLTHRALIAEYVS------CIVAG-----DMSADDIPLHalplyhCAQLDVFLGPYLyvgatnvildaPDPE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 367 RLLnrmyDKIFSQANTPLkrwlleFAAKrkqaevrsgiirndSIWDELF----FNKIQASlggCVRMIVTGAAPASPTVL 442
Cdd:PRK08316 251 LIL----RTIEAERITSF------FAPP--------------TVWISLLrhpdFDTRDLS---SLRKGYYGASIMPVEVL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 443 GFLRAAL-GCQVYEGYGQTECTAGCTFTTPGDwtsgHVGAP----LPCNHI--KLVDvEELNYWAcKGE-GEICVRGPNV 514
Cdd:PRK08316 304 KELRERLpGLRFYNCYGQTEIAPLATVLGPEE----HLRRPgsagRPVLNVetRVVD-DDGNDVA-PGEvGEIVHRSPQL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 515 FKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIyirsqpvaqIYVHGDSLKA 594
Cdd:PRK08316 378 MLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEA---------LYTHPAVAEV 446
|
490
....*....|
gi 1622946790 595 FLVGivVPDP 604
Cdd:PRK08316 447 AVIG--LPDP 454
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
146-605 |
1.07e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 99.73 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK06178 59 ITYAELDELSDRFAALLRQRGVGA-GDR-VAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 226 dkpQKAVL-LLEHVeRKETPgLKLII---LMD--------PFEEALKERGQKCGVVIKSMQAVEDCGQENhhAPVPPQPD 293
Cdd:PRK06178 137 ---LDQLApVVEQV-RAETS-LRHVIvtsLADvlpaeptlPLPDSLRAPRLAAAGAIDLLPALRACTAPV--PLPPPALD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 294 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVT-----ESVVychggrVGFFQgDIRLLSDDMKALCPTIF--PVVp 366
Cdd:PRK06178 210 ALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAvvggeDSVF------LSFLP-EFWIAGENFGLLFPLFSgaTLV- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 367 rLLNRmydkifsqantplkrW-LLEFAAKRKQAEVRSGIIRNDSIwDELF---------FNKIQASlgGCVRMIvtgaAP 436
Cdd:PRK06178 282 -LLAR---------------WdAVAFMAAVERYRVTRTVMLVDNA-VELMdhprfaeydLSSLRQV--RVVSFV----KK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 437 ASPTVLGFLRAALGCQVYEG-YGQTECTAGCTFTTpGDWTSGH--------VGAPLPCNHIKLVDVEELNYWACKGEGEI 507
Cdd:PRK06178 339 LNPDYRQRWRALTGSVLAEAaWGMTETHTCDTFTA-GFQDDDFdllsqpvfVGLPVPGTEFKICDFETGELLPLGAEGEI 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 508 CVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRsqpvaqiyv 587
Cdd:PRK06178 418 VVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV-NGMSVFPSEVEALLGQ--------- 486
|
490
....*....|....*...
gi 1622946790 588 HGDSLKAFLVGivVPDPE 605
Cdd:PRK06178 487 HPAVLGSAVVG--RPDPD 502
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
288-597 |
1.42e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 99.34 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 288 VPPQPD-DLSIVCFTSGTTGNPKGAMLTHGNVVAD-FSGF-----LKVTESVVYchgGRVGFF--------------QG- 345
Cdd:PRK06710 200 VPCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSNtLMGVqwlynCKEGEEVVL---GVLPFFhvygmtavmnlsimQGy 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 346 --------DIRLLSDDMKALCPTIFPVVPRLLnrmydkiFSQANTPLkrwllefaakRKQAEVRSgiirndsiwdelffn 417
Cdd:PRK06710 277 kmvlipkfDMKMVFEAIKKHKVTLFPGAPTIY-------IALLNSPL----------LKEYDISS--------------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 418 kiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgctfTTPGDW-----TSGHVGAPLPCNHIKLVD 492
Cdd:PRK06710 325 ---------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSP----VTHSNFlwekrVPGSIGVPWPDTEAMIMS 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 493 VEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKI 572
Cdd:PRK06710 392 LETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREV 469
|
330 340 350
....*....|....*....|....*....|..
gi 1622946790 573 ENIYIRSQPVAQIYV-------HGDSLKAFLV 597
Cdd:PRK06710 470 EEVLYEHEKVQEVVTigvpdpyRGETVKAFVV 501
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
294-609 |
1.46e-21 |
|
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: 96.25 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 294 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKvtesvvychggRVGFFQGDIRLLSddmkalcptiFPVVprllnrmy 373
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHS-----------RLGFGGGDSWLLS----------LPLY-------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 374 dKIFSQAntPLKRWLL---EFAAKRKQAEVRSGIIRND------------SIWDELFFNKIQASLggcvRMIVTGAAPAS 438
Cdd:cd17630 52 -HVGGLA--ILVRSLLagaELVLLERNQALAEDLAPPGvthvslvptqlqRLLDSGQGPAALKSL----RAVLLGGAPIP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 439 PtvlGFLRAA--LGCQVYEGYGQTEcTAGCTFT-TPGDWTSGHVGAPLPCNHIKLVDveelnywackgEGEICVRGPNVF 515
Cdd:cd17630 125 P---ELLERAadRGIPLYTTYGMTE-TASQVATkRPDGFGRGGVGVLLPGRELRIVE-----------DGEIWVGGASLA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 516 KGYLKDPdrTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIyIRSQP-VAQIYVHG---DS 591
Cdd:cd17630 190 MGYLRGQ--LVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAA-LAAHPaVRDAFVVGvpdEE 265
|
330
....*....|....*...
gi 1622946790 592 LKAFLVGIVVPDPEVMPS 609
Cdd:cd17630 266 LGQRPVAVIVGRGPADPA 283
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
146-606 |
1.60e-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: 98.43 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELA------CYtysmvvVPLYDTLGPGAIRYIINTAD 219
Cdd:cd12117 23 LTYAELNERANRLARRLRAAGVGP--GDVVGVLAERSPELVVALLAvlkagaAY------VPLDPELPAERLAFMLADAG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 220 ISTVIVDKPQKAVLLLehverketPGLKLIILMDPFEEALKErgqkcgvviksmqavedcgqenhhAPVPPQPDDLSIVC 299
Cdd:cd12117 95 AKVLLTDRSLAGRAGG--------LEVAVVIDEALDAGPAGN------------------------PAVPVSPDDLAYVM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 300 FTSGTTGNPKGAMLTHGNVVAdfsgflkvtesvvYCHGGRVGFFQGDIRLL-----SDDmkALCPTIFpvVPrLLN---- 370
Cdd:cd12117 143 YTSGSTGRPKGVAVTHRGVVR-------------LVKNTNYVTLGPDDRVLqtsplAFD--ASTFEIW--GA-LLNgarl 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 371 RMYDKifsqaNTPLKrwllefaAKRKQAEVRSGIIrnDSIWdeL---FFNKI----QASLGGcVRMIVTGAAPASPT-VL 442
Cdd:cd12117 205 VLAPK-----GTLLD-------PDALGALIAEEGV--TVLW--LtaaLFNQLadedPECFAG-LRELLTGGEVVSPPhVR 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 443 GFLRAALGCQVYEGYGQTECTagcTFTT-----PGDWTSGHV--GAPLPCNHIKLVDveELNYWACKGE-GEICVRGPNV 514
Cdd:cd12117 268 RVLAACPGLRLVNGYGPTENT---TFTTshvvtELDEVAGSIpiGRPIANTRVYVLD--EDGRPVPPGVpGELYVGGDGL 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 515 FKGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIyIRSQP-VAQIYV 587
Cdd:cd12117 343 ALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI-RGFRIELGEIEAA-LRAHPgVREAVV 420
|
490 500
....*....|....*....|..
gi 1622946790 588 ---HGDSLKAFLVGIVVPDPEV 606
Cdd:cd12117 421 vvrEDAGGDKRLVAYVVAEGAL 442
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
438-605 |
2.06e-21 |
|
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: 95.80 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 438 SPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDveELNYWACKGE-GEICVRGPNVFK 516
Cdd:cd17637 124 APETIQRFEETTGATFWSLYGQTE-TSGLVTLSPYRERPGSAGRPGPLVRVRIVD--DNDRPVPAGEtGEIVVRGPLVFQ 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 517 GYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKVIDRK--KHIFKlAQGEYVAPEKIENIyIRSQP-VAQIYVHGdslk 593
Cdd:cd17637 201 GYWNLPELTAYTFR-NGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKV-ILEHPaIAEVCVIG---- 273
|
170
....*....|..
gi 1622946790 594 aflvgivVPDPE 605
Cdd:cd17637 274 -------VPDPK 278
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
177-604 |
2.08e-21 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 98.34 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 177 VFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKavlLLEHVE--RKETPGL-KLIILMD 253
Cdd:cd05970 77 LTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDN---IPEEIEkaAPECPSKpKLVWVGD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 254 PFEEALKERGQKCgvviksMQAVEDCgqENHHAPVPPQPDDLSIVCFTSGTTGNPKgaMLTHgnvvaDFSGFLKVTESVV 333
Cdd:cd05970 154 PVPEGWIDFRKLI------KNASPDF--ERPTANSYPCGEDILLVYFSSGTTGMPK--MVEH-----DFTYPLGHIVTAK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 334 YCHGGRvgffQGDIRLLSDDM---KALCPTIF-------PVVprllnrMYD-KIFSQANtplkrwLLEFAAKRKQAE--- 399
Cdd:cd05970 219 YWQNVR----EGGLHLTVADTgwgKAVWGKIYgqwiagaAVF------VYDyDKFDPKA------LLEKLSKYGVTTfca 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 400 ---VRSGIIRND-SIWDelfFNKIqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPG-DW 474
Cdd:cd05970 283 pptIYRFLIREDlSRYD---LSSL--------RYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTL-TIATFPWmEP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 475 TSGHVGAPLPCNHIKLVDVEELnywACKG--EGEICVRGPN-----VFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAG 547
Cdd:cd05970 351 KPGSMGKPAPGYEIDLIDREGR---SCEAgeEGEIVIRTSKgkpvgLFGGYYKDAEKTAEVW-HDGYYHTGDAAWMDEDG 426
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622946790 548 TLKVIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYVHGdslkaflvgivVPDP 604
Cdd:cd05970 427 YLWFVGRTDDLIK-SSGYRIGPFEVESALIQHPAVLECAVTG-----------VPDP 471
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
132-692 |
2.69e-21 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 98.27 E-value: 2.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 132 PCLGFRKPNQPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTY---SMVVVPLYDTLGp 208
Cdd:cd05921 12 TWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGLSA--ERPLLILSGNSIEHALMALAAMYAgvpAAPVSPAYSLMS- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 209 gairyiintADISTvivdkpqkavllLEHVERKETPGLKLIILMDPFEEALKE-----------RGQKCG---VVIKSMQ 274
Cdd:cd05921 89 ---------QDLAK------------LKHLFELLKPGLVFAQDAAPFARALAAifplgtplvvsRNAVAGrgaISFAELA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 275 AVEDCGQ-ENHHAPVppQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLK-----------VTESVVYCH--GGRV 340
Cdd:cd05921 148 ATPPTAAvDAAFAAV--GPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQtypffgeeppvLVDWLPWNHtfGGNH 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 341 GF---------------------FQGDIRLLSDDMkalcPTIFPVVPrllnrmydkifsqantplKRWllefaakrkqaE 399
Cdd:cd05921 226 NFnlvlynggtlyiddgkpmpggFEETLRNLREIS----PTVYFNVP------------------AGW-----------E 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 400 VRSGIIRNDSIWDELFFNKiqaslggcVRMIVTGAAPASPTVLGFLRA----ALGCQV--YEGYGQTECTAGCTFTTPGD 473
Cdd:cd05921 273 MLVAALEKDEALRRRFFKR--------LKLMFYAGAGLSQDVWDRLQAlavaTVGERIpmMAGLGATETAPTATFTHWPT 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 474 WTSGHVGAPLPCNHIKLVdveelnywACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWL----PAGTL 549
Cdd:cd05921 345 ERSGLIGLPAPGTELKLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpddPAKGL 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 550 KVIDRKKHIFKLAQGEYVA--PekieniyIRSQPVAQI--YVHgDSL-----KAFLVGIVVPDPEVMPswAQKRGIEGTY 620
Cdd:cd05921 417 VFDGRVAEDFKLASGTWVSvgP-------LRARAVAACapLVH-DAVvagedRAEVGALVFPDLLACR--RLVGLQEASD 486
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622946790 621 ADLCTSKDLKKAILEDMVRLGKESGLHSFEQVKAIhIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 692
Cdd:cd05921 487 AEVLRHAKVRAAFRDRLAALNGEATGSSSRIARAL-LLDEPPSIDKGEITDKGYINQRAVLERRAALVERLY 557
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
187-573 |
1.03e-20 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 97.69 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 187 IAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKpqkavlllEHVERKETPGLKLIILMDP---FEEALKER- 262
Cdd:PRK08633 680 LANLALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVITSR--------KFLEKLKNKGFDLELPENVkviYLEDLKAKi 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 263 --GQKC--GVVIKSMQAVEDCGQENHhapvPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD---FSGFLKVTESVVYC 335
Cdd:PRK08633 752 skVDKLtaLLAARLLPARLLKRLYGP----TFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNieqISDVFNLRNDDVIL 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 336 hgGRVGFFQgdirllsddmkALCPTIFPVVPrLLNRMydKIFSQANtPLKRWLLEFAAKRKQAEVRSGI-------IRND 408
Cdd:PRK08633 828 --SSLPFFH-----------SFGLTVTLWLP-LLEGI--KVVYHPD-PTDALGIAKLVAKHRATILLGTptflrlyLRNK 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 409 SIWDELFfnkiqASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-----GDWT-----SGH 478
Cdd:PRK08633 891 KLHPLMF-----ASL----RLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNLPdvlaaDFKRqtgskEGS 961
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 479 VGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL---DSDGWLHTGDIGKWLPAGTLKVIDRK 555
Cdd:PRK08633 962 VGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRY 1041
|
410
....*....|....*...
gi 1622946790 556 KHIFKLAqGEYVAPEKIE 573
Cdd:PRK08633 1042 SRFAKIG-GEMVPLGAVE 1058
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
175-617 |
6.66e-20 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 92.88 E-value: 6.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 175 IGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDkpqkavlllehverketpglkliilmdp 254
Cdd:cd05971 34 VGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTD---------------------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 255 feealkergqkcgvviksmqavedcgqenhhapvppQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkvtesVVY 334
Cdd:cd05971 86 ------------------------------------GSDDPALIIYTSGTTGPPKGALHAHRVLLGHLPG-------VQF 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 335 CH-----GGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLLNRMydKIFS--QANTPLKRW------LLEFAAK--RKQAE 399
Cdd:cd05971 123 PFnlfprDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRM--TKFDpkAALDLMSRYgvttafLPPTALKmmRQQGE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 400 VRSGIIRNdsiwdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEC---TAGCTFTTPGDwtS 476
Cdd:cd05971 201 QLKHAQVK-------------------LRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECnlvIGNCSALFPIK--P 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 477 GHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPN--VFKGYLKDPDRTKEALDSDgWLHTGDIGKWLPAGTLKVIDR 554
Cdd:cd05971 260 GSMGKPIPGHRVAIVD-DNGTPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKMAGD-WLLTGDLGRKDSDGYFWYVGR 337
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 555 KKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFlvgiVVPDPEVMPSWAQKRGIE 617
Cdd:cd05971 338 DDDVITSS-GYRIGPAEIEECLLKHPAVLMAAVvgipdpiRGEIVKAF----VVLNPGETPSDALAREIQ 402
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
146-608 |
6.70e-20 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 93.49 E-value: 6.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVR--PGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 226 DKPQkavlllehvERKETPGLKLIILMDPFEEALKERgqkcgvviksmqavedcgqenhhAPVPPQPDDLSIVCFTSGTT 305
Cdd:cd12114 91 DGPD---------AQLDVAVFDVLILDLDALAAPAPP-----------------------PPVDVAPDDLAYVIFTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 306 GNPKGAMLTHG---NVVADFSGFLKVTEsvvychggrvgffqgDIRL-----LSDDMKAlcptifpvvprllnrmYDkIF 377
Cdd:cd12114 139 GTPKGVMISHRaalNTILDINRRFAVGP---------------DDRVlalssLSFDLSV----------------YD-IF 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 378 --------------SQANTPlKRWllefaakrKQAEVRSGIirndSIWdelffNKIQASLGgcvrMIVTgAAPASPTVLG 443
Cdd:cd12114 187 galsagatlvlpdeARRRDP-AHW--------AELIERHGV----TLW-----NSVPALLE----MLLD-VLEAAQALLP 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 444 FLRAAL-------------------GCQVYEGYGQTECTAGCTF----TTPGDWTSGHVGAPLPCNHIKLVD--VEELNY 498
Cdd:cd12114 244 SLRLVLlsgdwipldlparlralapDARLISLGGATEASIWSIYhpidEVPPDWRSIPYGRPLANQRYRVLDprGRDCPD 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 499 WackGEGEICVRGPNVFKGYLKDPDRTKEAL--DSDG--WLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIEN 574
Cdd:cd12114 324 W---VPGELWIGGRGVALGYLGDPELTAARFvtHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKV-RGYRIELGEIEA 399
|
490 500 510
....*....|....*....|....*....|....*.
gi 1622946790 575 IYIRSQPVAQ--IYVHGDSLKAFLVGIVVPDPEVMP 608
Cdd:cd12114 400 ALQAHPGVARavVVVLGDPGGKRLAAFVVPDNDGTP 435
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
245-573 |
7.20e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 93.91 E-value: 7.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 245 GLKLIILMDPFEEA---LKERGQKcgvviksMQAVEDCGQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD 321
Cdd:PRK07768 108 GAKAVVVGEPFLAAapvLEEKGIR-------VLTVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYAN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 322 FSG------FLKVTESVV----YCHG-GRVGFfqgdirlLSDDMKALC------PTIFPVVPRLLNRMYDKiFSQANTPL 384
Cdd:PRK07768 181 AEAmfvaaeFDVETDVMVswlpLFHDmGMVGF-------LTVPMYFGAelvkvtPMDFLRDPLLWAELISK-YRGTMTAA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 385 KRWLLEFAAKR--KQAEvrsgiirnDSIWDElffnkiqaslgGCVRMIVTGAAPASPTVL----------GFLRAALGCq 452
Cdd:PRK07768 253 PNFAYALLARRlrRQAK--------PGAFDL-----------SSLRFALNGAEPIDPADVedlldagarfGLRPEAILP- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 453 vyeGYGQTECTAGCTFTTPGD--------------------WTSGHV------GAPLPCNHIKLVDvEELNYWACKGEGE 506
Cdd:PRK07768 313 ---AYGMAEATLAVSFSPCGAglvvdevdadllaalrravpATKGNTrrlatlGPPLPGLEVRVVD-EDGQVLPPRGVGV 388
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622946790 507 ICVRGPNVFKGYLkDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIE 573
Cdd:PRK07768 389 IELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPTDIE 453
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
146-575 |
8.89e-20 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 94.65 E-value: 8.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGsGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK06814 659 LTYRKLLTGAFVLG-RKLKKNTPP--GENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 226 DKP--QKAVL--LLEHVERketpGLKLIILMDPFEE---ALKERGqkcgVVIKSMQAVEDCGqenhhapvpPQPDDLSIV 298
Cdd:PRK06814 736 SRAfiEKARLgpLIEALEF----GIRIIYLEDVRAQiglADKIKG----LLAGRFPLVYFCN---------RDPDDPAVI 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 299 CFTSGTTGNPKGAMLTHGNVVA---------DFSGFLKVTES--VVYCHGGRVGFFqgdIRLLSDDMKALCPTifP---- 363
Cdd:PRK06814 799 LFTSGSEGTPKGVVLSHRNLLAnraqvaariDFSPEDKVFNAlpVFHSFGLTGGLV---LPLLSGVKVFLYPS--Plhyr 873
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 364 VVPRLLnrmYDK----IFSqANTPLkrwllefaakrkqaevrSGIIRNDSIWDelFFNkiqaslggcVRMIVTGAAPASP 439
Cdd:PRK06814 874 IIPELI---YDTnatiLFG-TDTFL-----------------NGYARYAHPYD--FRS---------LRYVFAGAEKVKE 921
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 440 TVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNywacKGeGEICVRGPNVFKGYL 519
Cdd:PRK06814 922 ETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGID----EG-GRLFVRGPNVMLGYL 996
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622946790 520 K-DPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENI 575
Cdd:PRK06814 997 RaENPGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAVEEL 1051
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
292-614 |
9.88e-20 |
|
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: 91.39 E-value: 9.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgflkvtesvVYChGGRVGFFQGDIRLLsddmkalCPT----IFPVVPR 367
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYN-----------AWM-LALNSLFDPDDVLL-------CGLplfhVNGSVVT 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 368 LLNrmydKIFSQAN----TPL---------KRWLLefaAKRKQAEVRSGIirnDSIWDELFFNKIQASLGGcVRMIVTGA 434
Cdd:cd05944 62 LLT----PLASGAHvvlaGPAgyrnpglfdNFWKL---VERYRITSLSTV---PTVYAALLQVPVNADISS-LRFAMSGA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 435 APASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLV--DVEELNYWACKGE--GEICV 509
Cdd:cd05944 131 APLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKvlDGVGRLLRDCAPDevGEICV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 510 RGPNVFKGYLKDpDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYVHG 589
Cdd:cd05944 211 AGPGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLRHPAVAFAGAVG 288
|
330 340 350
....*....|....*....|....*....|....
gi 1622946790 590 --DSLKAFL-VGIV--VPDPEVMP----SWAQKR 614
Cdd:cd05944 289 qpDAHAGELpVAYVqlKPGAVVEEeellAWARDH 322
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
291-614 |
1.21e-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: 92.15 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 291 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESVVYCHGG-RVGFFQGDIrLLSDDMKALCP--TIFPVVPR 367
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLlQMASFSFDV-FAGDFARSLLNggTLVICPDE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 368 LL---NRMYDKIFSQ-----ANTP-LKRWLLEFAAKRKQ--AEVRSGIIRNDSIWDElFFNKIQASLGGCVRMIvtgaap 436
Cdd:cd17650 170 VKldpAALYDLILKSritlmESTPaLIRPVMAYVYRNGLdlSAMRLLIVGSDGCKAQ-DFKTLAARFGQGMRII------ 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 437 aspTVLGFLRAALGCQVYEGYGQTECTAGctfTTPgdwtsghVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFK 516
Cdd:cd17650 243 ---NSYGVTEATIDSTYYEEGRDPLGDSA---NVP-------IGRPLPNTAMYVLD-ERLQPQPVGVAGELYIGGAGVAR 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 517 GYLKDPDRTKEALDSDGW------LHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYV--- 587
Cdd:cd17650 309 GYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI-RGFRIELGEIESQLARHPAIDEAVVavr 387
|
330 340
....*....|....*....|....*..
gi 1622946790 588 HGDSLKAFLVGIVVPDPEvmPSWAQKR 614
Cdd:cd17650 388 EDKGGEARLCAYVVAAAT--LNTAELR 412
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
274-622 |
1.87e-19 |
|
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: 91.75 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 274 QAVEDCGQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSG--FLKVTES-VVYCH---------GGR 339
Cdd:cd05919 72 DDYAYIARDCEARLVVTSADDIAYLLYSSGTTGPPKGVMHAHRDPLlfADAMAreALGLTPGdRVFSSakmffgyglGNS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 340 VGF--FQGDIRLLSDD----------MKALCPTIFPVVPRllnrMYDKIFSQANTPlkrwllefaakrkQAEVRSgiIRn 407
Cdd:cd05919 152 LWFplAVGASAVLNPGwptaervlatLARFRPTVLYGVPT----FYANLLDSCAGS-------------PDALRS--LR- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 408 dsiwdelffnkiqaslggcvrmIVTGAAPASPTVLG-FLRAALGCQVYEGYGQTEctAGCTFTT--PGDWTSGHVGAPLP 484
Cdd:cd05919 212 ----------------------LCVSAGEALPRGLGeRWMEHFGGPILDGIGATE--VGHIFLSnrPGAWRLGSTGRPVP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 485 CNHIKLVDveELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAq 563
Cdd:cd05919 268 GYEIRLVD--EEGHTIPPGEeGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGRADDMLKVG- 343
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622946790 564 GEYVAPEKIENIYIRSQPVAQIYV----HGDSL---KAFlvgiVVPDPEVMPSWAQKRGIEGTYAD 622
Cdd:cd05919 344 GQWVSPVEVESLIIQHPAVAEAAVvavpESTGLsrlTAF----VVLKSPAAPQESLARDIHRHLLE 405
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
292-589 |
9.60e-19 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 90.24 E-value: 9.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVVAD------FSGFlkvTESVVY------CH-GG--------RVG--------F 342
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSALIVQslakiaIVGY---GEDDVYlhtaplCHiGGlssalamlMVGachvllpkF 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 343 fqgDIRLLSDDMKALCPTIFPVVPRLlnrMYDkifsqantplkrwLLEFAAKRKqaevrsgiirndsIWDElffnkiqas 422
Cdd:PLN02860 248 ---DAKAALQAIKQHNVTSMITVPAM---MAD-------------LISLTRKSM-------------TWKV--------- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 423 lGGCVRMIVTGAAPASP-----TVLGFLRAALgcqvYEGYGQTECTAGCTFTTPGDWT-----------------SGH-- 478
Cdd:PLN02860 287 -FPSVRKILNGGGSLSSrllpdAKKLFPNAKL----FSAYGMTEACSSLTFMTLHDPTlespkqtlqtvnqtkssSVHqp 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 479 ----VGAPLPcnHIKLvdveELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDR 554
Cdd:PLN02860 362 qgvcVGKPAP--HVEL----KIGLDESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGR 435
|
330 340 350
....*....|....*....|....*....|....*
gi 1622946790 555 KKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYVHG 589
Cdd:PLN02860 436 SNDRIK-TGGENVYPEEVEAVLSQHPGVASVVVVG 469
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
146-608 |
9.98e-19 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 89.30 E-value: 9.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVG--PESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 226 DkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhhapvppqPDDLSIVCFTSGTT 305
Cdd:cd12115 103 D-----------------------------------------------------------------PDDLAYVIYTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 306 GNPKGAMLTHGNVVA------------DFSGFLKVTeSVVY-----------CHGGRVGFFQGDIRLLsdDMKALCP-TI 361
Cdd:cd12115 118 GRPKGVAIEHRNAAAflqwaaaafsaeELAGVLAST-SICFdlsvfelfgplATGGKVVLADNVLALP--DLPAAAEvTL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 362 FPVVPRLLnrmydkifsqantplkRWLLEFaakrkqaevrsgiirndsiwdelffNKIQASlggcVRMIVTGAAPASPTV 441
Cdd:cd12115 195 INTVPSAA----------------AELLRH-------------------------DALPAS----VRVVNLAGEPLPRDL 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 442 LGFLRAAL-GCQVYEGYGQTECTAGCTFT--TPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGY 518
Cdd:cd12115 230 VQRLYARLqVERVVNLYGPSEDTTYSTVApvPPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVPGELYIGGAGVARGY 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 519 LKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIyIRSQP-VAQ--IYVHG 589
Cdd:cd12115 309 LGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAA-LRSIPgVREavVVAIG 386
|
490 500
....*....|....*....|
gi 1622946790 590 DSL-KAFLVGIVVPDPEVMP 608
Cdd:cd12115 387 DAAgERRLVAYIVAEPGAAG 406
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
175-609 |
2.30e-18 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 88.79 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 175 IGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKpqkavlLLEHVERKET-PGLKLIILMD 253
Cdd:PRK05852 71 VALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDA------DGPHDRAEPTtRWWPLTVNVG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 254 PfeealkERGQKCGVVIKSMqaveDCGQENHHAPVPPQ---PDDLSIVcFTSGTTGNPKGAMLTHGNVVADFSGFLK--- 327
Cdd:PRK05852 145 G------DSGPSGGTLSVHL----DAATEPTPATSTPEglrPDDAMIM-FTGGTTGLPKMVPWTHANIASSVRAIITgyr 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 328 -----VTESVV---YCHG------------GRV-----GFFQGdiRLLSDDMKALCPTIFPVVPrllnrmydkifsqant 382
Cdd:PRK05852 214 lsprdATVAVMplyHGHGliaallatlasgGAVllparGRFSA--HTFWDDIKAVGATWYTAVP---------------- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 383 PLKRWLLEFAAKRKQAEVRSGIirndsiwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEC 462
Cdd:PRK05852 276 TIHQILLERAATEPSGRKPAAL-----------------------RFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 463 TAGCTfTTPGDWtSGHVGAPLPCN---------HIKLV--DVEELNYWACkgeGEICVRGPNVFKGYLKDPDRTKEALdS 531
Cdd:PRK05852 333 THQVT-TTQIEG-IGQTENPVVSTglvgrstgaQIRIVgsDGLPLPAGAV---GEVWLRGTTVVRGYLGDPTITAANF-T 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 532 DGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAF---LVGIVVPDPEVMP 608
Cdd:PRK05852 407 DGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLASHPNVMEAAVFGVPDQLYgeaVAAVIVPRESAPP 485
|
.
gi 1622946790 609 S 609
Cdd:PRK05852 486 T 486
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
175-604 |
4.93e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 87.63 E-value: 4.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 175 IGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAVLLLEHverketpglKLIILMDP 254
Cdd:PRK06145 55 VALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDEEFDAIVALET---------PKIVIDAA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 255 FEEALKERGQKcgvviksmqavedcgqenhHAPVPPQ----PDDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLK 327
Cdd:PRK06145 126 AQADSRRLAQG-------------------GLEIPPQaavaPTDLVRLMYTSGTTDRPKGVMHSYGNLHwksIDHVIALG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 328 VTES--------------------VVYCHGGRVGF---FQGDIRLLSDDMKALCPTIFpvVPRLLNRMYdkifsQANTPL 384
Cdd:PRK06145 187 LTASerllvvgplyhvgafdlpgiAVLWVGGTLRIhreFDPEAVLAAIERHRLTCAWM--APVMLSRVL-----TVPDRD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 385 K------RWLLefAAKRKQAEVRsgiIRNdsiwdelffnkiqaslggcvrmivtgaapasptvlgFLRAALGCQVYEGYG 458
Cdd:PRK06145 260 RfdldslAWCI--GGGEKTPESR---IRD------------------------------------FTRVFTRARYIDAYG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 459 QTECTAGCTFTTPGDWTS--GHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLH 536
Cdd:PRK06145 299 LTETCSGDTLMEAGREIEkiGSTGRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFR 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622946790 537 TGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIEN-IYIRSQ--PVAQIYVHGDSLKAFLVGIVVPDP 604
Cdd:PRK06145 377 SGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERvIYELPEvaEAAVIGVHDDRWGERITAVVVLNP 446
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
145-604 |
6.90e-18 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 86.97 E-value: 6.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 145 WLSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVI 224
Cdd:cd12118 29 RYTWRQTYDRCRRLASALAALGIS--RGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 225 VDKPqkavlllehverketpglkliilmdpFE-EALKERGQKcgvviksmqavedcgqenHHAPVPPQPDDLSIVC-FTS 302
Cdd:cd12118 107 VDRE--------------------------FEyEDLLAEGDP------------------DFEWIPPADEWDPIALnYTS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 303 GTTGNPKGAMLTH--------GNVVA----DFSGFLkVTESVVYCHGGrvGFFQGdirllsddMKALCPTIfpVVPRLLN 370
Cdd:cd12118 143 GTTGRPKGVVYHHrgaylnalANILEwemkQHPVYL-WTLPMFHCNGW--CFPWT--------VAAVGGTN--VCLRKVD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 371 rmYDKIFsqantplkRWLLE-----FAAkrkqAEVRSGIIRNDSIWDelffnkiQASLGGCVRMIVTGAAPaSPTVLgFL 445
Cdd:cd12118 210 --AKAIY--------DLIEKhkvthFCG----APTVLNMLANAPPSD-------ARPLPHRVHVMTAGAPP-PAAVL-AK 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 446 RAALGCQVYEGYGQTEcTAG----CTFTTPGDWTSGHVGAPLPC----NHIKL--VDVEELNY-----WACKGEGEICVR 510
Cdd:cd12118 267 MEELGFDVTHVYGLTE-TYGpatvCAWKPEWDELPTEERARLKArqgvRYVGLeeVDVLDPETmkpvpRDGKTIGEIVFR 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 511 GPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIyirsqpvaqIYVHGD 590
Cdd:cd12118 346 GNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENISSVEVEGV---------LYKHPA 414
|
490
....*....|....
gi 1622946790 591 SLKAFLVGivVPDP 604
Cdd:cd12118 415 VLEAAVVA--RPDE 426
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
287-615 |
9.52e-18 |
|
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: 86.63 E-value: 9.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 287 PVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVV------------------ADFSGF---LKVTESVVY-CHGGRVGFFQ 344
Cdd:cd17651 130 DPALDADDLAYVIYTSGSTGRPKGVVMPHRSLAnlvawqarasslgpgartLQFAGLgfdVSVQEIFSTlCAGATLVLPP 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 345 GDIRLLSDDMKALCPTifpvvpRLLNRMYdkifsqANTPLKRWLLEfAAKRKQAEvrsgiirndsiwdelffnkiqaslG 424
Cdd:cd17651 210 EEVRTDPPALAAWLDE------QRISRVF------LPTVALRALAE-HGRPLGVR------------------------L 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 425 GCVRMIVTG--AAPASPTVLGFLRAALGCQVYEGYGQTE---CTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDvEELNY 498
Cdd:cd17651 253 AALRYLLTGgeQLVLTEDLREFCAGLPGLRLHNHYGPTEthvVTALSLPGDPAAWPApPPIGRPIDNTRVYVLD-AALRP 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 499 WACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKI 572
Cdd:cd17651 332 VPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGFRIELGEI 410
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1622946790 573 ENIYIRSQPVAQIYV------HGDslkAFLVGIVVPDPEVMPSWAQKRG 615
Cdd:cd17651 411 EAALARHPGVREAVVlaredrPGE---KRLVAYVVGDPEAPVDAAELRA 456
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
52-603 |
3.37e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 86.75 E-value: 3.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 52 ATTLVSMGALAAILAYW--FTHRPKAlQPPCNL----LMQSEEVedsggaRRSVIGSGPqllTHYYDDARTMYQVFRRGL 125
Cdd:PRK12467 453 ATDLFEATTIERLATHWrnLLEAIVA-EPRRRLgelpLLDAEER------ARELVRWNA---PATEYAPDCVHQLIEAQA 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 126 SISGNGPCLGFRKpnqpyQWLSYQEVADRAEFLGSGLLQHNckACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDT 205
Cdd:PRK12467 523 RQHPERPALVFGE-----QVLSYAELNRQANRLAHVLIAAG--VGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPE 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 206 LGPGAIRYIINTADISTVIVDKPQKAVLLLehverkeTPGLKLIILMDPfeealkergqkcgvviksmqAVEDCGQENHH 285
Cdd:PRK12467 596 YPQDRLAYMLDDSGVRLLLTQSHLLAQLPV-------PAGLRSLCLDEP--------------------ADLLCGYSGHN 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 286 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVadfsgflkvtesvvychgGRVGFFQGDIRLLSDDMKALCPT----- 360
Cdd:PRK12467 649 PEVALDPDNLAYVIYTSGSTGQPKGVAISHGALA------------------NYVCVIAERLQLAADDSMLMVSTfafdl 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 361 ----IFPVV---PRLLNRMYDKIFSQAntplkrwllEFAAkrKQAEVRSGIIR-NDSIWDELFFNKIQASLGGCVRMIVT 432
Cdd:PRK12467 711 gvteLFGALasgATLHLLPPDCARDAE---------AFAA--LMADQGVTVLKiVPSHLQALLQASRVALPRPQRALVCG 779
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 433 GAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTT----PGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEIC 508
Cdd:PRK12467 780 GEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYElsdeERDFGNVPIGQPLANLGLYILD-HYLNPVPVGVVGELY 858
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 509 VRGPNVFKGYLKDPDRTKEALDSD------GWLH-TGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIyIRSQP 581
Cdd:PRK12467 859 IGGAGLARGYHRRPALTAERFVPDpfgadgGRLYrTGDLARYRADGVIEYLGRMDHQVKI-RGFRIELGEIEAR-LLAQP 936
|
570 580
....*....|....*....|....*....
gi 1622946790 582 -------VAQIYVHGDSLKAFLVGIVVPD 603
Cdd:PRK12467 937 gvreavvLAQPGDAGLQLVAYLVPAAVAD 965
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
291-605 |
4.69e-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: 84.28 E-value: 4.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 291 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTESVV------YC-------------HGGRVGFFQGDIR 348
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAAtqrWFGFNEDDVwtlfhsYAfdfsvweiwgallHGGRLVVVPYEVA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 349 LLSDDMkalcptifpvvPRLLNRMYDKIFSQanTPLkrwllefAAKRKQAEVRSGIIRNDSIwdelffnkiqaslggcvR 428
Cdd:cd17643 171 RSPEDF-----------ARLLRDEGVTVLNQ--TPS-------AFYQLVEAADRDGRDPLAL-----------------R 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 429 MIVTGAAPASPTVLGFLRAALGC---QVYEGYGQTECTAGCTFT--TPGDW---TSGHVGAPLPCNHIKLVDvEELNYWA 500
Cdd:cd17643 214 YVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFRplDAADLpaaAASPIGRPLPGLRVYVLD-ADGRPVP 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 501 CKGEGEICVRGPNVFKGYLKDPDRTKE-------ALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIE 573
Cdd:cd17643 293 PGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI-RGFRIELGEIE 371
|
330 340 350
....*....|....*....|....*....|....*
gi 1622946790 574 NIYIRSQPVAQIYV---HGDSLKAFLVGIVVPDPE 605
Cdd:cd17643 372 AALATHPSVRDAAVivrEDEPGDTRLVAYVVADDG 406
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
95-587 |
2.90e-16 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 82.50 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 95 ARRSVIGSGPQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRKpnqpyQWLSYQEVADRAEFLGSGLLQHNCKAcTDQf 174
Cdd:PRK06155 1 GEPLGAGLAARAVDPLPPSERTLPAMLARQAERYPDRPLLVFGG-----TRWTYAEAARAAAAAAHALAAAGVKR-GDR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 175 IGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlLLEHVERKETPGLKL--IILM 252
Cdd:PRK06155 74 VALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAA-----LLAALEAADPGDLPLpaVWLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 253 DPFEEALKERGQKCGVVIKSMQAVedcgqenhhAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHG-------NVVADfsgf 325
Cdd:PRK06155 149 DAPASVSVPAGWSTAPLPPLDAPA---------PAAAVQPGDTAAILYTSGTTGPSKGVCCPHAqfywwgrNSAED---- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 326 LKVTESVVYChggrvgffqgdirllsddmkalcpTIFPvvprLLNRMYDKIFSQANTPLKRWLLE--FAAKRkqaevrsg 403
Cdd:PRK06155 216 LEIGADDVLY------------------------TTLP----LFHTNALNAFFQALLAGATYVLEprFSASG-------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 404 iirndsIWDELFFNKIQAS--LGGCVRMIVT--------------GAAPASPTVLGF-LRAALGCQVYEGYGQTECTAGC 466
Cdd:PRK06155 260 ------FWPAVRRHGATVTylLGAMVSILLSqparesdrahrvrvALGPGVPAALHAaFRERFGVDLLDGYGSTETNFVI 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 467 tFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWAckGE-GEICVRG--PNVF-KGYLKDPDRTKEALdSDGWLHTGDIGK 542
Cdd:PRK06155 334 -AVTHGSQRPGSMGRLAPGFEARVVDEHDQELPD--GEpGELLLRAdePFAFaTGYFGMPEKTVEAW-RNLWFHTGDRVV 409
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1622946790 543 WLPAGTLKVIDRKKHIFKlAQGEYVAPEKIENIyIRSQP-VAQIYV 587
Cdd:PRK06155 410 RDADGWFRFVDRIKDAIR-RRGENISSFEVEQV-LLSHPaVAAAAV 453
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
146-605 |
2.95e-16 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 81.94 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd17646 24 LTYRELDERANRLAHLLRARGVGP--EDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 226 DKPQKAVLllehverketPGLKLIILMDPfeealkergqkcgvviksmqavEDCGQENHHAP-VPPQPDDLSIVCFTSGT 304
Cdd:cd17646 102 TADLAARL----------PAGGDVALLGD----------------------EALAAPPATPPlVPPRPDNLAYVIYTSGS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 305 TGNPKGAMLTHGNVVadfsgflkvtesvvychgGRVGFFQGDIRLLSDD---MKAlcPTIFPV-VPRLLnrmydkifsqa 380
Cdd:cd17646 150 TGRPKGVMVTHAGIV------------------NRLLWMQDEYPLGPGDrvlQKT--PLSFDVsVWELF----------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 381 ntplkrWLLEFAAK--------RKQAEVRSGIIRNDSIWD--------ELFFNKIQASLGGCVRMIVTGAAPASPTVLGF 444
Cdd:cd17646 199 ------WPLVAGARlvvarpggHRDPAYLAALIREHGVTTchfvpsmlRVFLAEPAAGSCASLRRVFCSGEALPPELAAR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 445 LRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHV--GAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKD 521
Cdd:cd17646 273 FLALPGAELHNLYGPTEAAIDVThWPVRGPAETPSVpiGRPVPNTRLYVLD-DALRPVPVGVPGELYLGGVQLARGYLGR 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 522 PDRTKEALDSDGWLH------TGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIyIRSQP-VAQIYV---HGDS 591
Cdd:cd17646 352 PALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKI-RGFRVEPGEIEAA-LAAHPaVTHAVVvarAAPA 429
|
490
....*....|....
gi 1622946790 592 LKAFLVGIVVPDPE 605
Cdd:cd17646 430 GAARLVGYVVPAAG 443
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
146-608 |
3.10e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 82.10 E-value: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGSGLLQHNckACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQG--VRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 226 DKPQKAVLL---LEHVERKETPGLKLIILMDPFEEALKERGQKCGVviksmQAVEDCGQENHHAPVPPQ-PDDLSIVCFT 301
Cdd:PRK06164 114 WPGFKGIDFaaiLAAVPPDALPPLRAIAVVDDAADATPAPAPGARV-----QLFALPDPAPPAAAGERAaDPDAGALLFT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 302 -SGTTGNPK------GAMLTHGNVVADFSGFlkVTESVVYC---------HGGRVGFFQGDIRLLSDDMKALCPTIfpvv 365
Cdd:PRK06164 189 tSGTTSGPKlvlhrqATLLRHARAIARAYGY--DPGAVLLAalpfcgvfgFSTLLGALAGGAPLVCEPVFDAARTA---- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 366 pRLL-----------NRMYDKIFSQANTPLkrwllEFAAKRkqaevRSGIirndsiwdelffnkiqASLggcvrmivtga 434
Cdd:PRK06164 263 -RALrrhrvthtfgnDEMLRRILDTAGERA-----DFPSAR-----LFGF----------------ASF----------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 435 APASPTVLGFLRAAlGCQVYEGYGQTECTA---GCTFTTPgdWTSGHVGAPLPCN---HIKLVDVEELNYWACKGEGEIC 508
Cdd:PRK06164 305 APALGELAALARAR-GVPLTGLYGSSEVQAlvaLQPATDP--VSVRIEGGGRPASpeaRVRARDPQDGALLPDGESGEIE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 509 VRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVH 588
Cdd:PRK06164 382 IRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNPAEIEHALEALPGVAAAQVV 460
|
490 500
....*....|....*....|..
gi 1622946790 589 GDSL--KAFLVGIVVPDPEVMP 608
Cdd:PRK06164 461 GATRdgKTVPVAFVIPTDGASP 482
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
146-589 |
3.95e-16 |
|
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: 81.79 E-value: 3.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRP--GQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 226 dkpqkavllleHVERKETPGLKLIILMDPFEEALKERGQKC--GVVIKsmqavedcgqenhhaPVPPQPDDLSIVCFTSG 303
Cdd:cd05923 107 -----------AVDAQVMDAIFQSGVRVLALSDLVGLGEPEsaGPLIE---------------DPPREPEQPAFVFYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 304 TTGNPKGAMLTHgNVVADFSGFLKVTESVVYCHGGRV----------GFFQgdirLLSDDMkALCPTIFPVvprllnrmy 373
Cdd:cd05923 161 TTGLPKGAVIPQ-RAAESRVLFMSTQAGLRHGRHNVVlglmplyhviGFFA----VLVAAL-ALDGTYVVV--------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 374 dKIFSQANtplkrwllefAAKRKQAEVRSGIIRNDSIWDELFFNKIQASLG-GCVRMIVTGAAPASPTVLGFLRAALGCQ 452
Cdd:cd05923 226 -EEFDPAD----------ALKLIEQERVTSLFATPTHLDALAAAAEFAGLKlSSLRHVTFAGATMPDAVLERVNQHLPGE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 453 VYEGYGQTECTagcTFTTPGDWTSGHVGAPLPCNHIKLVDV-EELNYWACKG-EGEICVR--GPNVFKGYLKDPDRTKEA 528
Cdd:cd05923 295 KVNIYGTTEAM---NSLYMRDARTGTEMRPGFFSEVRIVRIgGSPDEALANGeEGELIVAaaADAAFTGYLNQPEATAKK 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622946790 529 LdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYVHG 589
Cdd:cd05923 372 L-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIG 430
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
146-635 |
4.80e-16 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 81.75 E-value: 4.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGSGLlQHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK05620 39 TTFAAIGARAAALAHAL-HDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 226 D---KPQKAVLLlehverKETPGLKLIILMDPFEEALKERGQKCGVVIKSMQAVEDcGQENHHaPVPPQP-DDLSIVCFT 301
Cdd:PRK05620 118 DprlAEQLGEIL------KECPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALLD-GRSTVY-DWPELDeTTAAAICYS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 302 SGTTGNPKGAMLTHGNVVADfSGFLKVTESVVYCHGgrVGFFqgdirllsddmkaLCPTIFPV----VPrLLNRMydkif 377
Cdd:PRK05620 190 TGTTGAPKGVVYSHRSLYLQ-SLSLRTTDSLAVTHG--ESFL-------------CCVPIYHVlswgVP-LAAFM----- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 378 sqANTPLKrwlleFAAKRKQAEVRSGIIRN---------DSIWDELFFNKIQ-----ASLggcvRMIVTGAAPASPTVLG 443
Cdd:PRK05620 248 --SGTPLV-----FPGPDLSAPTLAKIIATamprvahgvPTLWIQLMVHYLKnpperMSL----QEIYVGGSAVPPILIK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 444 FLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGA---------PLPCNHiKLVDVEELNYWACKGEGEICVRGPNV 514
Cdd:PRK05620 317 AWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEARWayrvsqgrfPASLEY-RIVNDGQVMESTDRNEGEIQVRGNWV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 515 FKGYLKDP----------------DRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAPEKIENIYIR 578
Cdd:PRK05620 396 TASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIR-SGGEWIYSAQLENYIMA 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622946790 579 SQPVaqiyvhgdsLKAFLVGIvvPDPEvmpsWAQK--------RGIEGTYAdlcTSKDLKKAILE 635
Cdd:PRK05620 475 APEV---------VECAVIGY--PDDK----WGERplavtvlaPGIEPTRE---TAERLRDQLRD 521
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
146-604 |
5.77e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 81.60 E-value: 5.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PLN03102 40 FTWPQTYDRCCRLAASLISLNIT--KNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 226 DKP-----QKAVLLLEHVERKETPGLKLIILMD----PFE-----EALKERGQKCGVVIKSMQAVEDcgqenHHAPVPpq 291
Cdd:PLN03102 118 DRSfeplaREVLHLLSSEDSNLNLPVIFIHEIDfpkrPSSeeldyECLIQRGEPTPSLVARMFRIQD-----EHDPIS-- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 292 pddlsiVCFTSGTTGNPKGAMLTH-GNVVADFS-------GFLKV---TESVVYCHGGRVGF---FQGDIRLLSDDMKAl 357
Cdd:PLN03102 191 ------LNYTSGTTADPKGVVISHrGAYLSTLSaiigwemGTCPVylwTLPMFHCNGWTFTWgtaARGGTSVCMRHVTA- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 358 cPTIFPVVprllnRMYDKIFSQANTPLKRWLLEfaAKRKQAEVRSGIIRndsiwdelffnkiqaslggcvrmIVTGAAPA 437
Cdd:PLN03102 264 -PEIYKNI-----EMHNVTHMCCVPTVFNILLK--GNSLDLSPRSGPVH-----------------------VLTGGSPP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 438 sPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGD-WTSghvgapLPCN------------HIKLVDVEELNYWAC--- 501
Cdd:PLN03102 313 -PAALVKKVQRLGFQVMHAYGLTEATGPVLFCEWQDeWNR------LPENqqmelkarqgvsILGLADVDVKNKETQesv 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 502 ----KGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIyi 577
Cdd:PLN03102 386 prdgKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVENV-- 461
|
490 500
....*....|....*....|....*..
gi 1622946790 578 rsqpvaqIYVHGDSLKAFLVGIvvPDP 604
Cdd:PLN03102 462 -------LYKYPKVLETAVVAM--PHP 479
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
456-612 |
1.16e-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: 78.88 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 456 GYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVE--ELNywacKGE-GEICVRGPNVFKGYLKDPDRTKEALdSD 532
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDgrEVP----DGEvGEIVARGPTVMAGYWNRPEVNARRT-RG 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 533 GWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqgeyvapekIENIY-------IRSQP-VAQIYVhgdslkaflvgIVVPDp 604
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSG---------AENIYpaevercLRQHPaVADAAV-----------IGVPD- 275
|
....*...
gi 1622946790 605 evmPSWAQ 612
Cdd:cd17636 276 ---PRWAQ 280
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
175-606 |
1.30e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 80.11 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 175 IGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAVL--LLEHVERKETPGLKLIILM 252
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLdgLDPGVRVINVDSPAWADEL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 253 DPFEEALKErgqkcgvviksmqavedcgqenhhaPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSG------FL 326
Cdd:PRK07867 137 AAHRDAEPP-------------------------FRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVA--SAGvmlaqrFG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 327 KVTESVVYC-----HGGRVgffqgdirllsddMKALCPTIFpvvprllnrmydkifSQANTPLKRwllEFAAKRKQAEVR 401
Cdd:PRK07867 190 LGPDDVCYVsmplfHSNAV-------------MAGWAVALA---------------AGASIALRR---KFSASGFLPDVR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 402 S-GIIrndsiwdelFFNKIqaslGGCVRMIVtgAAP-----------------ASPTVLGFLRAALGCQVYEGYGQTEct 463
Cdd:PRK07867 239 RyGAT---------YANYV----GKPLSYVL--ATPerpddadnplrivygneGAPGDIARFARRFGCVVVDGFGSTE-- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 464 AGCTFTTPGDWTSGHVGaPLPCNhIKLVDVE--------------ELNYWACKGEgEICVRGPNVFKGYLKDPDRTKEAL 529
Cdd:PRK07867 302 GGVAITRTPDTPPGALG-PLPPG-VAIVDPDtgtecppaedadgrLLNADEAIGE-LVNTAGPGGFEGYYNDPEADAERM 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622946790 530 dSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYVHGdslkaflvgivVPDPEV 606
Cdd:PRK07867 379 -RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPIERILLRYPDATEVAVYA-----------VPDPVV 442
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
284-593 |
1.39e-15 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 80.52 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 284 HHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTH----GNV-----VADFSGFLKVTESVVYCH--GGRVGFFQGdirLLSD 352
Cdd:PRK08043 356 RLAQVKQQPEDAALILFTSGSEGHPKGVVHSHksllANVeqiktIADFTPNDRFMSALPLFHsfGLTVGLFTP---LLTG 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 353 DMKALCPTI--FPVVPRLLnrmYDK----IFSQANtplkrWLLEFAakrkqaevrsgiiRNDSIWDelFFNkiqaslggc 426
Cdd:PRK08043 433 AEVFLYPSPlhYRIVPELV---YDRnctvLFGTST-----FLGNYA-------------RFANPYD--FAR--------- 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 427 VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNywacKGeGE 506
Cdd:PRK08043 481 LRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIE----QG-GR 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 507 ICVRGPNVFKGYLK--DPDRTK-------EALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYI 577
Cdd:PRK08043 556 LQLKGPNIMNGYLRveKPGVLEvptaenaRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIA-GEMVSLEMVEQLAL 634
|
330
....*....|....*.
gi 1622946790 578 RSQPVAQiyvHGDSLK 593
Cdd:PRK08043 635 GVSPDKQ---HATAIK 647
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
146-605 |
1.67e-15 |
|
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: 79.80 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGSGLLQHNCKActdqfiG--VFAQ--NRPEWIIAELACYtySMVVVPLYdTLgPG----AIRYIINT 217
Cdd:COG1021 51 LSYAELDRRADRLAAGLLALGLRP------GdrVVVQlpNVAEFVIVFFALF--RAGAIPVF-AL-PAhrraEISHFAEQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 218 ADISTVIVDKpqkAVLLLEHVE-----RKETPGLKLIILMDPFEEalkergqkcgvviksMQAVEDCGQENHHAPVP-PQ 291
Cdd:COG1021 121 SEAVAYIIPD---RHRGFDYRAlarelQAEVPSLRHVLVVGDAGE---------------FTSLDALLAAPADLSEPrPD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 292 PDDlsiVCF---TSGTTGNPKGAMLTHG----NVV--ADFSGFlkvTESVVY---------------------CHGGRVg 341
Cdd:COG1021 183 PDD---VAFfqlSGGTTGLPKLIPRTHDdylySVRasAEICGL---DADTVYlaalpaahnfplsspgvlgvlYAGGTV- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 342 ffqgdirLLSDDMKALcpTIFP-----------VVPRLLNRMydkifsqantplkrwlLEFAAKRKQAevrsgiirndsi 410
Cdd:COG1021 256 -------VLAPDPSPD--TAFPlierervtvtaLVPPLALLW----------------LDAAERSRYD------------ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 411 wdeLffnkiqASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctaG-CTFTTPGD--WTSGH-VGAPL-PC 485
Cdd:COG1021 299 ---L------SSL----RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---GlVNYTRLDDpeEVILTtQGRPIsPD 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 486 NHIKLVD-----VEElnywackGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKK-HI 558
Cdd:COG1021 363 DEVRIVDedgnpVPP-------GEvGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKdQI 435
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1622946790 559 FKlaQGEYVAPEKIENiyirsqpvaQIYVHGDSLKAFLVGivVPDPE 605
Cdd:COG1021 436 NR--GGEKIAAEEVEN---------LLLAHPAVHDAAVVA--MPDEY 469
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
146-616 |
6.12e-15 |
|
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: 78.18 E-value: 6.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGSGLLQhnckactdqfIGVFAQNR--------PEWIIAELACYTYSMVVVPLYDTLGPGAIRYIInt 217
Cdd:cd05959 30 LTYAELEAEARRVAGALRA----------LGVKREERvllimldtVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 218 ADI-STVIVDKPQKAVLLLEHVERKEtPGLKLIILMDPFEEALKErgqkcgvviksMQAVEDCGQENHH-APVPPQPDDL 295
Cdd:cd05959 98 EDSrARVVVVSGELAPVLAAALTKSE-HTLVVLIVSGGAGPEAGA-----------LLLAELVAAEAEQlKPAATHADDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 296 SIVCFTSGTTGNPKGAMLTHGN--VVADFSG--FLKVTESVV----------YCHGGRVGF---FQGDIRLLS------- 351
Cdd:cd05959 166 AFWLYSSGSTGRPKGVVHLHADiyWTAELYArnVLGIREDDVcfsaaklffaYGLGNSLTFplsVGATTVLMPerptpaa 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 352 --DDMKALCPTIFPVVPRLLNRMydkifsqantplkrwlleFAAKRKQAEVRSGIirndsiwdelffnkiqaslggcvRM 429
Cdd:cd05959 246 vfKRIRRYRPTVFFGVPTLYAAM------------------LAAPNLPSRDLSSL-----------------------RL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 430 IVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTF--TTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEI 507
Cdd:cd05959 285 CVSAGEALPAEVGERWKARFGLDILDGIGSTE--MLHIFlsNRPGRVRYGTTGKPVPGYEVELRD-EDGGDVADGEPGEL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 508 CVRGPNVFKGYLKDPDRTKEALDSdGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYV 587
Cdd:cd05959 362 YVRGPSSATMYWNNRDKTRDTFQG-EWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSPFEVESALVQHPAVLEAAV 439
|
490 500 510
....*....|....*....|....*....|....*.
gi 1622946790 588 HG-------DSLKAFlvgiVVPDPEVMPSWAQKRGI 616
Cdd:cd05959 440 VGvededglTKPKAF----VVLRPGYEDSEALEEEL 471
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
292-670 |
7.31e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 78.16 E-value: 7.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTE-------SVV-------YCHGGRVGFfQGDIR----LLSDD 353
Cdd:PRK12582 219 PDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPrepdpppPVSldwmpwnHTMGGNANF-NGLLWgggtLYIDD 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 354 MKALcPTIFPVVPRLLNRMYDKIFsqANTPLKRWLLEFAAKRKQAEVRSgiirndsiwdelFFNKIqaslggcvRMIVTG 433
Cdd:PRK12582 298 GKPL-PGMFEETIRNLREISPTVY--GNVPAGYAMLAEAMEKDDALRRS------------FFKNL--------RLMAYG 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 434 AAPASPTVLGFLRA----ALGCQV--YEGYGQTEcTAGCTFTTpgDWTS---GHVGAPLPCNHIKLVDVEElNYwackge 504
Cdd:PRK12582 355 GATLSDDLYERMQAlavrTTGHRIpfYTGYGATE-TAPTTTGT--HWDTervGLIGLPLPGVELKLAPVGD-KY------ 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 505 gEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWL----PAGTLKVIDRKKHIFKLAQGEYV--APEKIENIYIR 578
Cdd:PRK12582 425 -EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdpddPEKGLIFDGRVAEDFKLSTGTWVsvGTLRPDAVAAC 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 579 SQPVAQIYVHGDSlKAFLVGIVVPDPEVMPSWAQKRGieGTYADLCTSKDLKKAILEDMVRLGKESGLHSfEQVKAIHIH 658
Cdd:PRK12582 504 SPVIHDAVVAGQD-RAFIGLLAWPNPAACRQLAGDPD--AAPEDVVKHPAVLAILREGLSAHNAEAGGSS-SRIARALLM 579
|
410
....*....|..
gi 1622946790 659 SDMFSVQNGLLT 670
Cdd:PRK12582 580 TEPPSIDAGEIT 591
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
428-605 |
1.41e-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: 76.60 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 428 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHVGAPL-PCNHIKLVDvEELNYWACKGEG 505
Cdd:cd05920 258 RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTrLDDPDEVIIHTQGRPMsPDDEIRVVD-EEGNPVPPGEEG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 506 EICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENiyirsqpvaQI 585
Cdd:cd05920 337 ELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVEN---------LL 406
|
170 180
....*....|....*....|
gi 1622946790 586 YVHGDSLKAFLVGivVPDPE 605
Cdd:cd05920 407 LRHPAVHDAAVVA--MPDEL 424
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
146-605 |
1.44e-14 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 76.39 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGSGLLQHNCKACTDQFigVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYiintadistviv 225
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVF--VLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRD------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 226 dkpqkavlllehveRKETPGLKLIILmdpfEEALKERgqkcgvviksmqavedcgqenhhapvpPQPDDLSIVCFTSGTT 305
Cdd:cd05969 67 --------------RLENSEAKVLIT----TEELYER---------------------------TDPEDPTLLHYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 306 GNPKGAMLTHGNVVAD-FSG--FLKVTESVVYCHGGRVGFFQGdirllsddmkalcpTIFPVVPRLLNRMYDKIFSQANT 382
Cdd:cd05969 102 GTPKGVLHVHDAMIFYyFTGkyVLDLHPDDIYWCTADPGWVTG--------------TVYGIWAPWLNGVTNVVYEGRFD 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 383 PlKRWLlefaakrkqaevrsGIIRND--SIW--------------DELFFNKIQASLggcvRMIVTGAAPASPTVLGFLR 446
Cdd:cd05969 168 A-ESWY--------------GIIERVkvTVWytaptairmlmkegDELARKYDLSSL----RFIHSVGEPLNPEAIRWGM 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 447 AALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRG--PNVFKGYLKDPD 523
Cdd:cd05969 229 EVFGVPIHDTWWQTETGSIMIANYPCmPIKPGSMGKPLPGVKAAVVD-ENGNELPPGTKGILALKPgwPSMFRGIWNDEE 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 524 RTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVHGdslkaflvgivVPD 603
Cdd:cd05969 308 RYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHRVGPFEVESALMEHPAVAEAGVIG-----------KPD 374
|
..
gi 1622946790 604 PE 605
Cdd:cd05969 375 PL 376
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
282-587 |
1.62e-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: 76.45 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 282 ENHHApvppqpDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsGFLkvteSVVYChggrVGFFQGDIRL-LSDdmkalcpt 360
Cdd:cd05974 80 ENTHA------DDPMLLYFTSGTTSKPKLVEHTHRSYPV---GHL----STMYW----IGLKPGDVHWnISS-------- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 361 ifpvvPRLLNRMYDKIFSQANTPLKRWLL---EFAAKRKQAE-VRSGIIR---NDSIWdELFFNKIQASLGGCVRMIVTG 433
Cdd:cd05974 135 -----PGWAKHAWSCFFAPWNAGATVFLFnyaRFDAKRVLAAlVRYGVTTlcaPPTVW-RMLIQQDLASFDVKLREVVGA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 434 AAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTfTTPGD-WTSGHVGAPLPCNHIKLVDVEElnywACKGEGEICV--- 509
Cdd:cd05974 209 GEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVG-NSPGQpVKAGSMGRPLPGYRVALLDPDG----APATEGEVALdlg 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 510 --RGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYV 587
Cdd:cd05974 284 dtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SSDYRISPFELESVLIEHPAVAEAAV 361
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
286-566 |
2.70e-14 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 76.09 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 286 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSgflKVTESVVYCHGGR-------VGFFqgDIRLlsdDMKALC 358
Cdd:PRK09274 167 PMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIE---ALREDYGIEPGEIdlptfplFALF--GPAL---GMTSVI 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 359 PTIFPVVPRLLNRmyDKIFSQ----------ANTPLKRWLLEFAAKRKQaevrsgiirndsiwdelffnkiqaSLGGCVR 428
Cdd:PRK09274 239 PDMDPTRPATVDP--AKLFAAierygvtnlfGSPALLERLGRYGEANGI------------------------KLPSLRR 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 429 MIVTGAaPASPTVLGFLRAAL--GCQVYEGYGQTECTAGCT-------FTTPGDWTSGH---VGAPLPCNHIKLVDV--E 494
Cdd:PRK09274 293 VISAGA-PVPIAVIERFRAMLppDAEILTPYGATEALPISSiesreilFATRAATDNGAgicVGRPVDGVEVRIIAIsdA 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 495 ELNYWA-----CKGE-GEICVRGPNVFKGYLKDPDRTKEA--LDSDG--WLHTGDIGkWL-PAGTLKVIDRKKHIFKLAQ 563
Cdd:PRK09274 372 PIPEWDdalrlATGEiGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLG-YLdAQGRLWFCGRKAHRVETAG 450
|
...
gi 1622946790 564 GEY 566
Cdd:PRK09274 451 GTL 453
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
143-597 |
4.91e-14 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 75.27 E-value: 4.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 143 YQWLsyqEVADRAEFLGSGLLQHNCKA-CTdqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADIS 221
Cdd:PLN02479 46 YTWA---QTYQRCRRLASALAKRSIGPgST---VAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 222 TVIVDkpQKAVLLLEH----VERKETPGLK---LIILMDP------FEEALKeRGqkcgvVIKSMQAVEDCGQEnhHAPV 288
Cdd:PLN02479 120 VVMVD--QEFFTLAEEalkiLAEKKKSSFKpplLIVIGDPtcdpksLQYALG-KG-----AIEYEKFLETGDPE--FAWK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 289 PPQPDDLSIVC-FTSGTTGNPKGAMLTH-GNVVADFSGFL--KVTESVVY--------CHGGrvgffqgdirLLSDDMKA 356
Cdd:PLN02479 190 PPADEWQSIALgYTSGTTASPKGVVLHHrGAYLMALSNALiwGMNEGAVYlwtlpmfhCNGW----------CFTWTLAA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 357 LCPTIFPVVPRLLNRMYDKIFSQANTplkrwllEFAAkrkqAEVRSGIIRNDSIWDELFfnkiqaSLGGCVRMIVTGAAP 436
Cdd:PLN02479 260 LCGTNICLRQVTAKAIYSAIANYGVT-------HFCA----APVVLNTIVNAPKSETIL------PLPRVVHVMTAGAAP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 437 aSPTVLgFLRAALGCQVYEGYGQTEcTAG----CTFTTPGDWTSGHVGAPLPCNH---------IKLVDVEELNYWACKG 503
Cdd:PLN02479 323 -PPSVL-FAMSEKGFRVTHTYGLSE-TYGpstvCAWKPEWDSLPPEEQARLNARQgvryiglegLDVVDTKTMKPVPADG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 504 E--GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIyirsqp 581
Cdd:PLN02479 400 KtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGGENISSLEVENV------ 471
|
490
....*....|....*.
gi 1622946790 582 vaqIYVHGDSLKAFLV 597
Cdd:PLN02479 472 ---VYTHPAVLEASVV 484
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
177-604 |
7.64e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 74.69 E-value: 7.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 177 VFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV--DKPqkavlllEHVE--RKETPGLKLIILM 252
Cdd:PRK07470 62 VHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMIChaDFP-------EHAAavRAASPDLTHVVAI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 253 D--PFEEAlkergqkcgvviksmqaVEDCGQENHHAPVPPQP---DDLSIVCFTSGTTGNPKGAMLTHG-------NVVA 320
Cdd:PRK07470 135 GgaRAGLD-----------------YEALVARHLGARVANAAvdhDDPCWFFFTSGTTGRPKAAVLTHGqmafvitNHLA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 321 D-FSGFLKVTESVVYC---HGGrvGFFQ--------GDIRLLSDDMKAlcptifPVVPRLLNRMYDKIFSQANTPLKrWL 388
Cdd:PRK07470 198 DlMPGTTEQDASLVVAplsHGA--GIHQlcqvargaATVLLPSERFDP------AEVWALVERHRVTNLFTVPTILK-ML 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 389 LEFAAkrkqaevrsgIIRNDsiwdelffnkiQASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF 468
Cdd:PRK07470 269 VEHPA----------VDRYD-----------HSSL----RYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVTGNITV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 469 TTP-----GDWTSGHVGaplPCNH--------IKLVDVEELNywacKGE-GEICVRGPNVFKGYLKDPDRTKEALdSDGW 534
Cdd:PRK07470 324 LPPalhdaEDGPDARIG---TCGFertgmevqIQDDEGRELP----PGEtGEICVIGPAVFAGYYNNPEANAKAF-RDGW 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 535 LHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENiyirsqpvaQIYVHGDSLKAFLVGivVPDP 604
Cdd:PRK07470 396 FRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPREIEE---------KLLTHPAVSEVAVLG--VPDP 453
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
183-597 |
1.20e-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: 74.04 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 183 PEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlLLEHVER--KETPGLKLIILMDPfeealk 260
Cdd:cd05928 78 PEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDE-----LAPEVDSvaSECPSLKTKLLVSE------ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 261 ERGQKCGVVIKSMQAVEDcgqenHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGN----VVADFSGFLKVTESVVYCH 336
Cdd:cd05928 147 KSRDGWLNFKELLNEAST-----EHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSlglgLKVNGRYWLDLTASDIMWN 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 337 GGRVGFFQGDI-RLLSDDMKALCptifpVVPRLLNRMYDKIFSQANT--PLKRWLLEFAAKRKqaevrsgIIRNDsiwde 413
Cdd:cd05928 222 TSDTGWIKSAWsSLFEPWIQGAC-----VFVHHLPRFDPLVILKTLSsyPITTFCGAPTVYRM-------LVQQD----- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 414 lfFNKIQ-ASLGGCVrmivTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVD 492
Cdd:cd05928 285 --LSSYKfPSLQHCV----TGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIID 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 493 vEELNYWACKGEGEICVR-GPN----VFKGYLKDPDRTKEALDSDGWLhTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYV 567
Cdd:cd05928 359 -DNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYRI 435
|
410 420 430
....*....|....*....|....*....|....*..
gi 1622946790 568 APEKIENIYIRSQPVAQIYV-------HGDSLKAFLV 597
Cdd:cd05928 436 GPFEVESALIEHPAVVESAVvsspdpiRGEVVKAFVV 472
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
146-604 |
1.94e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 73.38 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGP--GDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 226 DK---PQKAVLLlehverKETPGLKLIILMD------------PFEEALKErgqkcgvviksmqavedcgQENHHAPVPP 290
Cdd:PRK07798 107 ERefaPRVAEVL------PRLPKLRTLVVVEdgsgndllpgavDYEDALAA-------------------GSPERDFGER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 291 QPDDLSIVCfTSGTTGNPKGAMLTHGNV-VADFSGFLKVTESVV---YCHGGRVGFFQGDIRLlsddmkALCPTI----- 361
Cdd:PRK07798 162 SPDDLYLLY-TGGTTGMPKGVMWRQEDIfRVLLGGRDFATGEPIedeEELAKRAAAGPGMRRF------PAPPLMhgagq 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 362 ----------FPVVprllnrMYDKI-FSQANtplkrwLLEFAAKRKqaeVRSGIIRNDS----IWDELffnkiqASLGG- 425
Cdd:PRK07798 235 waafaalfsgQTVV------LLPDVrFDADE------VWRTIEREK---VNVITIVGDAmarpLLDAL------EARGPy 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 426 ---CVRMIVTGAAPASPTV-LGFLRAALGCQVYEGYGQTECTAGCTFTTPGDwtSGHVGAPL--PCNHIKLVDvEELNYW 499
Cdd:PRK07798 294 dlsSLFAIASGGALFSPSVkEALLELLPNVVLTDSIGSSETGFGGSGTVAKG--AVHTGGPRftIGPRTVVLD-EDGNPV 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 500 AcKGEGEICV--RGPNVFKGYLKDPDRTKEALDS-DG--WLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIEN 574
Cdd:PRK07798 371 E-PGSGEIGWiaRRGHIPLGYYKDPEKTAETFPTiDGvrYAIPGDRARVEADGTITLLGRGSVCINTG-GEKVFPEEVEE 448
|
490 500 510
....*....|....*....|....*....|
gi 1622946790 575 IyIRSQPvaqiyvhgDSLKAFLVGivVPDP 604
Cdd:PRK07798 449 A-LKAHP--------DVADALVVG--VPDE 467
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
292-582 |
3.56e-13 |
|
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: 72.52 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTES---------VVYCHGgrVGFFQGDIRLLSDDMKA-LCPT- 360
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWktkdrilswMPLTHD--MGLIAFHLAPLIAGMNQyLMPTr 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 361 IFPVVPRLLNRMYDK----IFSQANTPLKrWLLEFAAKRKQAEvrsgiirndsiWDElffnkiqaslgGCVRMIVTGAAP 436
Cdd:cd05908 183 LFIRRPILWLKKASEhkatIVSSPNFGYK-YFLKTLKPEKAND-----------WDL-----------SSIRMILNGAEP 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 437 ASP----------TVLGFLRAAlgcqVYEGYGQTECTAGCTF----------------------------TTPGDWTSGH 478
Cdd:cd05908 240 IDYelchefldhmSKYGLKRNA----ILPVYGLAEASVGASLpkaqspfktitlgrrhvthgepepevdkKDSECLTFVE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 479 VGAPLPCNHIKLVDveELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkWLPAGTLKVIDRKKH 557
Cdd:cd05908 316 VGKPIDETDIRICD--EDNKILPDGYiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIRNGRLVITGREKD 392
|
330 340
....*....|....*....|....*
gi 1622946790 558 IFkLAQGEYVAPEKIENIYIRSQPV 582
Cdd:cd05908 393 II-FVNGQNVYPHDIERIAEELEGV 416
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
290-602 |
3.87e-13 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 72.11 E-value: 3.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 290 PQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGfLKVTESVVycHGGR-------VGFFQGDIRLLS--DDMKALCPT 360
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDA-LRQLYGIR--PGEVdlatfplFALFGPALGLTSviPDMDPTRPA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 361 ifPVVPRllnrmydKIFSqantPLKRWllefaakrkqaEVrSGIIRNDSIWDEL--FFNKIQASLGGcVRMIVTGAAPAS 438
Cdd:cd05910 159 --RADPQ-------KLVG----AIRQY-----------GV-SIVFGSPALLERVarYCAQHGITLPS-LRRVLSAGAPVP 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 439 PTVLGFLRAAL--GCQVYEGYGQTECTAGCT------FTTPGDWTSGH----VGAPLPCNHIKLV--DVEELNYWACKGE 504
Cdd:cd05910 213 IALAARLRKMLsdEAEILTPYGATEALPVSSigsrelLATTTAATSGGagtcVGRPIPGVRVRIIeiDDEPIAEWDDTLE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 505 ------GEICVRGPNVFKGYLKDPDRTKEALDSDG----WLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVapekien 574
Cdd:cd05910 293 lprgeiGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLY------- 365
|
330 340
....*....|....*....|....*....
gi 1622946790 575 iyirSQPVAQIY-VHGDSLKAFLVGIVVP 602
Cdd:cd05910 366 ----TEPVERVFnTHPGVRRSALVGVGKP 390
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
28-597 |
1.33e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 71.91 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 28 TQEILRILRLPELGDLGQFfrSLSATTLVSMGALAAILAYWFTHRPKAL-----QPPCNLLMQS--------EEVEDSGG 94
Cdd:PRK12316 2959 QLPGLHIESFAWDGAATQF--DLALDTWESAEGLGASLTYATDLFDARTverlaRHWQNLLRGMvenpqrsvDELAMLDA 3036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 95 ARRSVIGSGPQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRKpnqpyQWLSYQEVADRAEFLGSGLLQHNCKActDQF 174
Cdd:PRK12316 3037 EERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVALAFGE-----QRLSYAELNRRANRLAHRLIERGVGP--DVL 3109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 175 IGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGAiryiintaDISTVIVDKPQKAVLLLEHVERKETPGLKlIILMDP 254
Cdd:PRK12316 3110 VGVAVERSLEMVVGLLAILKAGGAYVPL-DPEYPEE--------RLAYMLEDSGAQLLLSQSHLRLPLAQGVQ-VLDLDR 3179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 255 FEEALKErgqkcgvviksmqavedcgqenHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGnvvadfsGFLKVTESVVY 334
Cdd:PRK12316 3180 GDENYAE----------------------ANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHS-------ALSNHLCWMQQ 3230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 335 CHGGRVGFFQGDIRLLSDDMKALcptifpvvprllnRMYDKIFSQANTPLKRWLLEFA-AKRKQAEVRSGIIRNDSIWDE 413
Cdd:PRK12316 3231 AYGLGVGDRVLQFTTFSFDVFVE-------------ELFWPLMSGARVVLAGPEDWRDpALLVELINSEGVDVLHAYPSM 3297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 414 L--FFNKIQASLGGCVRMIVTGAAPASPTVLGflRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGH--VGAPLPCNHIK 489
Cdd:PRK12316 3298 LqaFLEEEDAHRCTSLKRIVCGGEALPADLQQ--QVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACY 3375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 490 LVDVeELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGW------LHTGDIGKWLPAGTLKVIDRKKHIFKLaQ 563
Cdd:PRK12316 3376 ILDG-SLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQVKI-R 3453
|
570 580 590
....*....|....*....|....*....|....*..
gi 1622946790 564 GEYVAPEKIENIYIRSQPV---AQIYVHGDSLKAFLV 597
Cdd:PRK12316 3454 GFRIELGEIEARLLEHPWVreaVVLAVDGRQLVAYVV 3490
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
291-614 |
2.04e-12 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 69.59 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 291 QPDDLSIVCFTSGTTGNPKGAMLTH---GNVVADFSGFLKVTesvvycHGGRV------GFfqgDIRLLSDDMKALCPTI 361
Cdd:cd17652 91 TPDNLAYVIYTSGSTGRPKGVVVTHrglANLAAAQIAAFDVG------PGSRVlqfaspSF---DASVWELLMALLAGAT 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 362 FPVVPRLLnrmydkifSQANTPLKRWLlefaakrkQAEVRSGIIRNDSIWDELffnkIQASLGGCVRMIVTGAAPASPTV 441
Cdd:cd17652 162 LVLAPAEE--------LLPGEPLADLL--------REHRITHVTLPPAALAAL----PPDDLPDLRTLVVAGEACPAELV 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 442 LgflRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLK 520
Cdd:cd17652 222 D---RWAPGRRMINAYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYVLD-ARLRPVPPGVPGELYIAGAGLARGYLN 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 521 DPDRTKEALDSD------GWLH-TGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQ--IYVHGDS 591
Cdd:cd17652 298 RPGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKI-RGFRIELGEVEAALTEHPGVAEavVVVRDDR 376
|
330 340
....*....|....*....|....
gi 1622946790 592 L-KAFLVGIVVPDPEVMPSWAQKR 614
Cdd:cd17652 377 PgDKRLVAYVVPAPGAAPTAAELR 400
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
291-614 |
2.48e-12 |
|
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: 69.77 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 291 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKV---TESVvychggRVGFFQGdirlLSDDMKAlcPTIFPVVPR 367
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEygiTSSD------RVLQFAS----IAFDVAA--EEIYVTLLS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 368 --LLNRMYDKIFSQantplkrwLLEFAAK--RKQAEVRSgiiRNDSIWDELFFNKIQASLGG--CVRMIVTGAAPASPTV 441
Cdd:cd17644 172 gaTLVLRPEEMRSS--------LEDFVQYiqQWQLTVLS---LPPAYWHLLVLELLLSTIDLpsSLRLVIVGGEAVQPEL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 442 LGFLRAALG--CQVYEGYGQTECTAGCTFTTPGDWTSGH-----VGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNV 514
Cdd:cd17644 241 VRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIANTQVYILD-ENLQPVPVGVPGELHIGGVGL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 515 FKGYLKDPDRTKEALDSDGWLH--------TGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQ-- 584
Cdd:cd17644 320 ARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKI-RGFRIELGEIEAVLSQHNDVKTav 398
|
330 340 350
....*....|....*....|....*....|.
gi 1622946790 585 IYVHGDSL-KAFLVGIVVPDPEVMPSWAQKR 614
Cdd:cd17644 399 VIVREDQPgNKRLVAYIVPHYEESPSTVELR 429
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
503-558 |
2.87e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 69.59 E-value: 2.87e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622946790 503 GE--GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHI 558
Cdd:PRK08162 385 GEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDI 441
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
299-589 |
3.45e-12 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 69.40 E-value: 3.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 299 CFTSGTTGNPKGamlthgnvvadfsgflkvtesVVYCHggRVGFFQGDIRLLSDDMKALCP-TIFPVVPrllnrMYdkif 377
Cdd:PRK06018 183 CYTSGTTGDPKG---------------------VLYSH--RSNVLHALMANNGDALGTSAAdTMLPVVP-----LF---- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 378 sQANTplkrWLLEFAAKRKQAEVRSGIIRND--SIWDELFFNKIQASLG-------------------GCVRMIVTGAAp 436
Cdd:PRK06018 231 -HANS----WGIAFSAPSMGTKLVMPGAKLDgaSVYELLDTEKVTFTAGvptvwlmllqymekeglklPHLKMVVCGGS- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 437 ASPTvlGFLRA--ALGCQVYEGYGQTECTAGCTFTT--------PGDWTSGHV---GAPLPCNHIKLVDVE--ELNyWAC 501
Cdd:PRK06018 305 AMPR--SMIKAfeDMGVEVRHAWGMTEMSPLGTLAAlkppfsklPGDARLDVLqkqGYPPFGVEMKITDDAgkELP-WDG 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 502 KGEGEICVRGPNVFKGYLKDPDrtkEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAPEKIENIYIRSQP 581
Cdd:PRK06018 382 KTFGRLKVRGPAVAAAYYRVDG---EILDDDGFFDTGDVATIDAYGYMRITDRSKDVIK-SGGEWISSIDLENLAVGHPK 457
|
....*...
gi 1622946790 582 VAQIYVHG 589
Cdd:PRK06018 458 VAEAAVIG 465
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
293-609 |
3.97e-12 |
|
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: 68.66 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 293 DDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF----LKVTESVVYCHGGRV--GFFQGDIRLLSDDMKALCpTIFPvvP 366
Cdd:cd05958 97 DDICILAFTSGTTGAPKATMHFHRDPLASADRYavnvLRLREDDRFVGSPPLafTFGLGGVLLFPFGVGASG-VLLE--E 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 367 RLLNRMYDKIFSQANTplkrwLLEFAAKRKQAEVRSGiirndsiwdelffnKIQASLGGCVRMIVTgAAPASPTVLGFL- 445
Cdd:cd05958 174 ATPDLLLSAIARYKPT-----VLFTAPTAYRAMLAHP--------------DAAGPDLSSLRKCVS-AGEALPAALHRAw 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 446 RAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDveELNYWACKGE-GEICVRGPNVFKgYLKDPDR 524
Cdd:cd05958 234 KEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD--DEGNPVPDGTiGRLAVRGPTGCR-YLADKRQ 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 525 TKEAldSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLV---GIVV 601
Cdd:cd05958 311 RTYV--QGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVvvkAFVV 387
|
....*...
gi 1622946790 602 PDPEVMPS 609
Cdd:cd05958 388 LRPGVIPG 395
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
292-577 |
5.47e-12 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 68.69 E-value: 5.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKvtesvvychggrvgFFQGdirLLSDDMKALCP----------TI 361
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLK--------------FFSP---KEDDVMMSFLPpfhaygfnscTL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 362 FPVVPRLlnrmyDKIFSQanTPLK-RWLLEFAAKRKQAEVRSGIIRNDSIwdeLFFNKIQASLGGCVRMIVTGAAPASPT 440
Cdd:PRK06334 245 FPLLSGV-----PVVFAY--NPLYpKKIVEMIDEAKVTFLGSTPVFFDYI---LKTAKKQESCLPSLRFVVIGGDAFKDS 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 441 VL-GFLRAALGCQVYEGYGQTECTAGCTFTT---PGDwtSGHVGAPLPCNHIKLVDvEELNYWACKGE-GEICVRGPNVF 515
Cdd:PRK06334 315 LYqEALKTFPHIQLRQGYGTTECSPVITINTvnsPKH--ESCVGMPIRGMDVLIVS-EETKVPVSSGEtGLVLTRGTSLF 391
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622946790 516 KGYL-KDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYI 577
Cdd:PRK06334 392 SGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSLEALESILM 453
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
296-583 |
1.45e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 67.42 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 296 SIVCFTSGTTGNPKGAMLTHgnvvadfsgflkvTESVVYCHGGRvgffqgdirlLSDDMK-ALCPTIFPVVPRLLNRMYD 374
Cdd:PRK07008 179 SSLCYTSGTTGNPKGALYSH-------------RSTVLHAYGAA----------LPDAMGlSARDAVLPVVPMFHVNAWG 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 375 KIFSQANTPLKrwlLEFAAKRKQAEVRSGIIRND---------SIWDELFFNKIQASLG-GCVRMIVTGAAPASPTVLGF 444
Cdd:PRK07008 236 LPYSAPLTGAK---LVLPGPDLDGKSLYELIEAErvtfsagvpTVWLGLLNHMREAGLRfSTLRRTVIGGSACPPAMIRT 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 445 LRAALGCQVYEGYGQTECTAGCTFTTPgdwTSGHVGAPLPCNH--------------IKLVDVE--ELNyWACKGEGEIC 508
Cdd:PRK07008 313 FEDEYGVEVIHAWGMTEMSPLGTLCKL---KWKHSQLPLDEQRkllekqgrviygvdMKIVGDDgrELP-WDGKAFGDLQ 388
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622946790 509 VRGPNVFKGYLKdpdRTKEALDsDGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVA 583
Cdd:PRK07008 389 VRGPWVIDRYFR---GDASPLV-DGWFPTGDVATIDADGFMQITDRSKDVIK-SGGEWISSIDIENVAVAHPAVA 458
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
434-605 |
1.80e-11 |
|
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: 67.02 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 434 AAPASPTVLGFLRAALGCQVYEGYGQTECTaGCTFTTPGDWTS--GHVGAPLPcNHIKLVDvEELNYWACKGEGEICVRG 511
Cdd:cd05929 253 AAPCPPWVKEQWIDWGGPIIWEYYGGTEGQ-GLTIINGEEWLThpGSVGRAVL-GKVHILD-EDGNEVPPGEIGEVYFAN 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 512 PNVFKgYLKDPDRTKEALDSDGWLHTGDIGkWLPA-GTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRsqpvaqiyvHGD 590
Cdd:cd05929 330 GPGFE-YTNDPEKTAAARNEGGWSTLGDVG-YLDEdGYLYLTDRRSDMI-ISGGVNIYPQEIENALIA---------HPK 397
|
170
....*....|....*
gi 1622946790 591 SLKAFLVGivVPDPE 605
Cdd:cd05929 398 VLDAAVVG--VPDEE 410
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
144-598 |
1.92e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 68.06 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 144 QWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGA-IRYIINTADIST 222
Cdd:PRK12316 2027 QHLSYAELDSRANRLAHRLRARGVGP--EVRVAIAAERSFELVVALLAVLKAGGAYVPL-DPNYPAErLAYMLEDSGAAL 2103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 223 VIVDKPQKAVLLLehverkeTPGLKLIILMDPfeEALKERGQkcgvviksmqavedcgqenHHAPVPPQPDDLSIVCFTS 302
Cdd:PRK12316 2104 LLTQRHLLERLPL-------PAGVARLPLDRD--AEWADYPD-------------------TAPAVQLAGENLAYVIYTS 2155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 303 GTTGNPKGAMLTHGNVVAdfsgflkvtesvvYCH--GGRVGFFQGDIRLlsddmkalcptifpvvpRLLNRMYDKIFSQA 380
Cdd:PRK12316 2156 GSTGLPKGVAVSHGALVA-------------HCQaaGERYELSPADCEL-----------------QFMSFSFDGAHEQW 2205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 381 NTPLKrwllefaakrKQAEVrsgIIRNDSIWD-ELFFNKIQ--------------------ASLGGC---VRMIVTGAAP 436
Cdd:PRK12316 2206 FHPLL----------NGARV---LIRDDELWDpEQLYDEMErhgvtildfppvylqqlaehAERDGRppaVRVYCFGGEA 2272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 437 ASPTVLGFLRAALGCQ-VYEGYGQTEctagcTFTTPGDWTSGH----------VGAPLPCNHIKLVDvEELNYWACKGEG 505
Cdd:PRK12316 2273 VPAASLRLAWEALRPVyLFNGYGPTE-----AVVTPLLWKCRPqdpcgaayvpIGRALGNRRAYILD-ADLNLLAPGMAG 2346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 506 EICVRGPNVFKGYLKDPDRTKEALDSDGWLH-------TGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENiYIR 578
Cdd:PRK12316 2347 ELYLGGEGLARGYLNRPGLTAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKI-RGFRIELGEIEA-RLQ 2424
|
490 500
....*....|....*....|....*..
gi 1622946790 579 SQP-------VAQIYVHGDSLKAFLVG 598
Cdd:PRK12316 2425 AHPavreavvVAQDGASGKQLVAYVVP 2451
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
144-612 |
2.15e-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: 66.62 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 144 QWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTV 223
Cdd:cd17649 11 QSLSYAELDARANRLAHRLRALGVGP--EVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 224 IvdkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqeNHHapvppqPDDLSIVCFTSG 303
Cdd:cd17649 89 L----------------------------------------------------------THH------PRQLAYVIYTSG 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 304 TTGNPKGAMLTHGNVVA---DFSGFLKVTESVVYCHGGRVGFFQGDIRLLSDDMKALCptifpVVPRllnrmydkifsqa 380
Cdd:cd17649 105 STGTPKGVAVSHGPLAAhcqATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGAC-----VVLR------------- 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 381 ntPLKRWLlefAAKRKQAEVRSGIIRNDSI----WDELF--FNKIQASLGGCVRMIVTGAAPASPTvlgFLRAALGCQVY 454
Cdd:cd17649 167 --PDELWA---SADELAEMVRELGVTVLDLppayLQQLAeeADRTGDGRPPSLRLYIFGGEALSPE---LLRRWLKAPVR 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 455 --EGYGQTECTAGCT-FTTPGD----WTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKE 527
Cdd:cd17649 239 lfNAYGPTEATVTPLvWKCEAGaaraGASMPIGRPLGGRSAYILD-ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 528 AL--DSDG-----WLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENiYIRSQP----VAQIYVHGDSLKAfL 596
Cdd:cd17649 318 RFvpDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-RGFRIELGEIEA-ALLEHPgvreAAVVALDGAGGKQ-L 394
|
490
....*....|....*..
gi 1622946790 597 VGIVVP-DPEVMPSWAQ 612
Cdd:cd17649 395 VAYVVLrAAAAQPELRA 411
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
294-575 |
2.48e-11 |
|
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: 65.74 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 294 DLSIVCFTSGTTGNPKGAMLTHGNVVAD------------------------FSGFLKVTESVVYCHGGRVGFfqGDIRL 349
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVpdilqkeglnwvvgdvtylplpatHIGGLWWILTCLIHGGLCVTG--GENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 350 LSDDMKAL---CPTIFPVVPRLLNRMYDKIFSQANTPLKRWLLEFAAKRkqaevrsgIIRNDSIWDELFFNkiqaslggc 426
Cdd:cd17635 80 YKSLFKILttnAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSR--------AIAADVRFIEATGL--------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 427 vrmivtgaapasptvlgflraalgCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDVEELNYWAcKGEG 505
Cdd:cd17635 143 ------------------------TNTAQVYGLSETGTALCLPTDDDSIEiNAVGRPYPGVDVYLAATDGIAGPS-ASFG 197
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 506 EICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENI 575
Cdd:cd17635 198 TIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERI 265
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
291-613 |
4.28e-11 |
|
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: 65.65 E-value: 4.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 291 QPDDLSIVCFTSGTTGNPKGAMLTHGNVV------ADFSGFLKVTESVVYchgGRVGFFQGDIRLLSDDMKALCPTIFPV 364
Cdd:cd17645 102 NPDDLAYVIYTSGSTGLPKGVMIEHHNLVnlcewhRPYFGVTPADKSLVY---ASFSFDASAWEIFPHLTAGAALHVVPS 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 365 VPRL----LNRMYDK---IFSQANTPLKRWLLEfaakrkqaevrsgiIRNDSIwdelffnkiqaslggcvRMIVTGAapa 437
Cdd:cd17645 179 ERRLdldaLNDYFNQegiTISFLPTGAAEQFMQ--------------LDNQSL-----------------RVLLTGG--- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 438 spTVLGFLRAAlGCQVYEGYGQTECTAGCT-FTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFK 516
Cdd:cd17645 225 --DKLKKIERK-GYKLVNNYGPTENTVVATsFEIDKPYANIPIGKPIDNTRVYILD-EALQLQPIGVAGELCIAGEGLAR 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 517 GYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENI---YIRSQPVAQIYV 587
Cdd:cd17645 301 GYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIEPFlmnHPLIELAAVLAK 379
|
330 340 350
....*....|....*....|....*....|
gi 1622946790 588 HGDSLKAFLVGIVVP----DPEVMPSWAQK 613
Cdd:cd17645 380 EDADGRKYLVAYVTApeeiPHEELREWLKN 409
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
177-320 |
5.63e-11 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 65.69 E-value: 5.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 177 VFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADiSTVIVDKPQkavlLLEHVERKETPGLKLIILMDPFE 256
Cdd:PRK04319 103 IFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSE-AKVLITTPA----LLERKPADDLPSLKHVLLVGEDV 177
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622946790 257 EAlkerGQKCGVVIKSMQAVEDcgqenHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVA 320
Cdd:PRK04319 178 EE----GPGTLDFNALMEQASD-----EFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQ 232
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
111-638 |
5.90e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 66.34 E-value: 5.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 111 YDDARTMYQVFRRGLSISGNGPCLGFRKpnqpyQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAEL 190
Cdd:PRK12467 1570 YPLARLVHQLIEDQAAATPEAVALVFGE-----QELTYGELNRRANRLAHRLIALGVGP--EVLVGIAVERSLEMVVGLL 1642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 191 ACYTYSMVVVPLYDTLGPGAIRYIINTADIStvivdkpqkavLLLEHveRKETPGLKLIilmdpfeealkeRGQKCgVVI 270
Cdd:PRK12467 1643 AILKAGGAYVPLDPEYPRERLAYMIEDSGIE-----------LLLTQ--SHLQARLPLP------------DGLRS-LVL 1696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 271 KSMQAVEDcGQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVA---------DFSGFLKVTESVVYCHGGRV- 340
Cdd:PRK12467 1697 DQEDDWLE-GYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNrlcatqeayQLSAADVVLQFTSFAFDVSVw 1775
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 341 GFFQGdirLLSDDMKALCPtifPVVPRLLNRMYDKIFSQANTplkrwLLEFAAKRKQAevrsgiirndsiwdelfFNKIQ 420
Cdd:PRK12467 1776 ELFWP---LINGARLVIAP---PGAHRDPEQLIQLIERQQVT-----TLHFVPSMLQQ-----------------LLQMD 1827
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 421 ASLGGC--VRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAG-----CTFTTPGDWTSGHVGAPLPCNHIKLVD 492
Cdd:PRK12467 1828 EQVEHPlsLRRVVCGGEALEVEALRPWLERLPdTGLFNLYGPTETAVDvthwtCRRKDLEGRDSVPIGQPIANLSTYILD 1907
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 493 vEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL------DSDGWLH-TGDIGKWLPAGTLKVIDRKKHIFKLaQGE 565
Cdd:PRK12467 1908 -ASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgTVGSRLYrTGDLARYRADGVIEYLGRIDHQVKI-RGF 1985
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622946790 566 YVAPEKIENiYIRSQP----VAQIYVHGDSLKAfLVGIVVPDPEVMPSWAQKRgieGTYADlcTSKDLKKAILED-MV 638
Cdd:PRK12467 1986 RIELGEIEA-RLREQGgvreAVVIAQDGANGKQ-LVAYVVPTDPGLVDDDEAQ---VALRA--ILKNHLKASLPEyMV 2056
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
439-587 |
6.64e-11 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 64.89 E-value: 6.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 439 PTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTSGhVGAPLPCNHIKLVDveelnywackgeGEICVRGPNVFKGY 518
Cdd:PRK09029 253 PVELTEQAEQQGIRCWCGYGLTE-MASTVCAKRADGLAG-VGSPLPGREVKLVD------------GEIWLRGASLALGY 318
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622946790 519 LKDpDRTKEALDSDGWLHTGDIGKWLpAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYV 587
Cdd:PRK09029 319 WRQ-GQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQVFV 384
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
146-605 |
7.21e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 65.33 E-value: 7.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACytySMVvvplydtlgpGAIRYIINTAdistviV 225
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRA--GDGVAVLARNHRGFVLALYAA---GKV----------GARIILLNTG------F 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 226 DKPQkavlLLEHVERKetpGLKLIILMDPFEE---ALKERGQKCGVVIKSMQAVEDC------------GQENHHAPVPP 290
Cdd:PRK07788 134 SGPQ----LAEVAARE---GVKALVYDDEFTDllsALPPDLGRLRAWGGNPDDDEPSgstdetlddliaGSSTAPLPKPP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 291 QPDdlSIVCFTSGTTGNPKGAMLTHGNVVADFSGFL-----KVTESVVYC----HGgrVGFFQGDI-------------- 347
Cdd:PRK07788 207 KPG--GIVILTSGTTGTPKGAPRPEPSPLAPLAGLLsrvpfRAGETTLLPapmfHA--TGWAHLTLamalgstvvlrrrf 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 348 ---RLLSDDMKALCPTIFpVVPRLLNRMYDkifsqantplkrwLLEfaakrkqaEVRSgiirndsiwdelffnKIQASlg 424
Cdd:PRK07788 283 dpeATLEDIAKHKATALV-VVPVMLSRILD-------------LGP--------EVLA---------------KYDTS-- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 425 gCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECtAGCTFTTPGDWT--SGHVGAPLPCNHIKLVD-----VEEln 497
Cdd:PRK07788 324 -SLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEV-AFATIATPEDLAeaPGTVGRPPKGVTVKILDengneVPR-- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 498 ywackGE-GEICVRGPNVFKGYlKDPdRTKEALdsDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIy 576
Cdd:PRK07788 400 -----GVvGRIFVGNGFPFEGY-TDG-RDKQII--DGLLSSGDVGYFDEDGLLFVDGRDDDMI-VSGGENVFPAEVEDL- 468
|
490 500
....*....|....*....|....*....
gi 1622946790 577 irsqpvaqIYVHGDSLKAFLVGivVPDPE 605
Cdd:PRK07788 469 --------LAGHPDVVEAAVIG--VDDEE 487
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
280-609 |
7.53e-11 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 65.10 E-value: 7.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 280 GQENHHAPVPPQPDDLsivCFTSGTTGNPKG-----------------AMLTHG---NVVADFSGFLkvTESVVYCHGGR 339
Cdd:PRK12406 142 QQEPYDGPPVPQPQSM---IYTSGTTGHPKGvrraaptpeqaaaaeqmRALIYGlkpGIRALLTGPL--YHSAPNAYGLR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 340 VGFFQGDIRLLS----DDMKALCP-----TIFpVVPRLLNRmydkifsqantplkrwLLEFAAKRKQAEVRSgiirndsi 410
Cdd:PRK12406 217 AGRLGGVLVLQPrfdpEELLQLIErhritHMH-MVPTMFIR----------------LLKLPEEVRAKYDVS-------- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 411 wdelffnkiqaSLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCNHI 488
Cdd:PRK12406 272 -----------SL----RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE-SGAVTFATSEDALShpGTVGKAAPGAEL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 489 KLVDvEELNYWACKGEGEICVRGPNV--FKgYLKDPDRTKEaLDSDGWLHTGDIGkWLPA-GTLKVIDRKKHIFkLAQGE 565
Cdd:PRK12406 336 RFVD-EDGRPLPQGEIGEIYSRIAGNpdFT-YHNKPEKRAE-IDRGGFITSGDVG-YLDAdGYLFLCDRKRDMV-ISGGV 410
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1622946790 566 YVAPEKIENIYIRSQPVAQIYVHGDSLKAF---LVGIVVPDPEVMPS 609
Cdd:PRK12406 411 NIYPAEIEAVLHAVPGVHDCAVFGIPDAEFgeaLMAVVEPQPGATLD 457
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
175-606 |
2.66e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 63.51 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 175 IGVFAQNRPEWII----AELACYTysmvVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAvlLLEHVErkeTPGLKLII 250
Cdd:PRK13388 55 VGVLLGNTPEMLFwlaaAALGGYV----LVGLNTTRRGAALAADIRRADCQLLVTDAEHRP--LLDGLD---LPGVRVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 251 LMDPfeealkergqkcgvviKSMQAVEDCGQENHHAPVppQPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSG------ 324
Cdd:PRK13388 126 VDTP----------------AYAELVAAAGALTPHREV--DAMDPFMLIFTSGTTGAPKAVRCSHGRLA--FAGralter 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 325 FLKVTESVVYC-----HGGRVgffqgdirllsddMKALCPTIFpvvprllnrmydkifSQANTPLKRwllEFAAKRKQAE 399
Cdd:PRK13388 186 FGLTRDDVCYVsmplfHSNAV-------------MAGWAPAVA---------------SGAAVALPA---KFSASGFLDD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 400 VRSgiirndsiWDELFFNKIQASLGgcvRMIVTGAAP---ASPTVLGFLRAA-----------LGCQVYEGYGQTEctAG 465
Cdd:PRK13388 235 VRR--------YGATYFNYVGKPLA---YILATPERPddaDNPLRVAFGNEAsprdiaefsrrFGCQVEDGYGSSE--GA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 466 CTFTTPGDWTSGHVGAPLPcnHIKLVDVEE---------------LNywACKGEGEICVR-GPNVFKGYLKDPDRTKEAL 529
Cdd:PRK13388 302 VIVVREPGTPPGSIGRGAP--GVAIYNPETltecavarfdahgalLN--ADEAIGELVNTaGAGFFEGYYNNPEATAERM 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622946790 530 dSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYVHGdslkaflvgivVPDPEV 606
Cdd:PRK13388 378 -RHGMYWSGDLAYRDADGWIYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYA-----------VPDERV 441
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
293-573 |
6.65e-10 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 62.11 E-value: 6.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 293 DDLSIVCFTSGTTGNPKGAMLTHGNVV-----------ADFSG----FLKVTESVVYCHGGRVGFFQGDIRLLSDDMKAL 357
Cdd:cd17656 128 DDLLYIIYTSGTTGKPKGVQLEHKNMVnllhferektnINFSDkvlqFATCSFDVCYQEIFSTLLSGGTLYIIREETKRD 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 358 CPTIFPVVPRllNRMYDKIFSQAntplkrwLLEFAAKRKQaevrsgiirndsiwdelFFNkiqaSLGGCVRMIVTGAAP- 436
Cdd:cd17656 208 VEQLFDLVKR--HNIEVVFLPVA-------FLKFIFSERE-----------------FIN----RFPTCVKHIITAGEQl 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 437 -ASPTVLGFLRAAlGCQVYEGYG--QTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGP 512
Cdd:cd17656 258 vITNEFKEMLHEH-NVHLHNHYGpsETHVVTTYTINPEAEIPElPPIGKPISNTWIYILD-QEQQLQPQGIVGELYISGA 335
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622946790 513 NVFKGYLKDPDRTKEALDSDGW------LHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIE 573
Cdd:cd17656 336 SVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-RGYRIELGEIE 401
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
427-605 |
1.99e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 60.69 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 427 VRMIVTGAAPASPTVLgflRAAL---GCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCNhIKLVDvEELNYWAC 501
Cdd:PRK08276 264 LRVAIHAAAPCPVEVK---RAMIdwwGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGE-VRILD-EDGNELPP 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 502 KGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkWLPA-GTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQ 580
Cdd:PRK08276 338 GEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVG-YLDEdGYLYLTDRKSDMI-ISGGVNIYPQEIENLLVTHP 415
|
170 180
....*....|....*....|....*
gi 1622946790 581 PVAQIYVHGdslkaflvgivVPDPE 605
Cdd:PRK08276 416 KVADVAVFG-----------VPDEE 429
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
428-604 |
2.02e-09 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 60.39 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 428 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT---------FTT------PGD--WTSGHVGAPLPCNHIkl 490
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAEGLVNYTrlddsderiFTTqgrpmsPDDevWVADADGNPLPQGEV-- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 491 vdveelnywackgeGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHifklaQ----GEY 566
Cdd:PRK10946 381 --------------GRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGEK 441
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622946790 567 VAPEKIENIYIRsqpvaqiyvHGDSLKAFLVGIvvPDP 604
Cdd:PRK10946 442 IAAEEIENLLLR---------HPAVIHAALVSM--EDE 468
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
286-597 |
2.44e-09 |
|
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: 60.24 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 286 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGN--VVADFSG--FLKVTESVVYCHGGRVGFFQGdirlLSDDMkalcptI 361
Cdd:TIGR02262 154 KPAATQADDPAFWLYSSGSTGMPKGVVHTHSNpyWTAELYArnTLGIREDDVCFSAAKLFFAYG----LGNAL------T 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 362 FPVVPRLLNRMYdkifSQANTP---LKRWLlefaakRKQAEVRSGIirnDSIWDELFFNKIQASLGGCVRMIVTGAAPAS 438
Cdd:TIGR02262 224 FPMSVGATTVLM----GERPTPdavFDRLR------RHQPTIFYGV---PTLYAAMLADPNLPSEDQVRLRLCTSAGEAL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 439 PTVLGF-LRAALGCQVYEGYGQTEctAGCTFTT--PGDWTSGHVGAPLPCNHIKLVDveELNYWACKGE-GEICVRGPNV 514
Cdd:TIGR02262 291 PAEVGQrWQARFGVDIVDGIGSTE--MLHIFLSnlPGDVRYGTSGKPVPGYRLRLVG--DGGQDVADGEpGELLISGPSS 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 515 FKGYLKDPDRTKEALDSdGWLHTGDigKWL--PAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVHG--- 589
Cdd:TIGR02262 367 ATMYWNNRAKSRDTFQG-EWTRSGD--KYVrnDDGSYTYAGRTDDMLKVS-GIYVSPFEIESALIQHPAVLEAAVVGvad 442
|
330
....*....|..
gi 1622946790 590 -DSL---KAFLV 597
Cdd:TIGR02262 443 eDGLikpKAFVV 454
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
292-608 |
3.03e-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: 59.72 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgfLKVTESVVY---CHGG-RVGFF----------QGDIRLLSDDMKAL 357
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVN-----LRTSLSERYfgrDNGDeAVLFFsnyvfdffveQMTLALLNGQKLVV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 358 CPTIFPVVPrllNRMYDKIFSQANTPLkrwllefaakrkqaevrSGiirNDSIWDELFFnkiqASLGGCVRMIVTGAAPA 437
Cdd:cd17648 168 PPDEMRFDP---DRFYAYINREKVTYL-----------------SG---TPSVLQQYDL----ARLPHLKRVDAAGEEFT 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 438 SPtVLGFLRAALGCQVYEGYGQTEC--TAGCTFTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVF 515
Cdd:cd17648 221 AP-VFEKLRSRFAGLIINAYGPTETtvTNHKRFFPGDQRFDKSLGRPVRNTKCYVLN-DAMKRVPVGAVGELYLGGDGVA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 516 KGYLKDPDRTKE-------------ALDSDGWLH-TGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIY----- 576
Cdd:cd17648 299 RGYLNRPELTAErflpnpfqteqerARGRNARLYkTGDLVRWLPSGELEYLGRNDFQVKI-RGQRIEPGEVEAALasypg 377
|
330 340 350
....*....|....*....|....*....|....*
gi 1622946790 577 IRSQPVAQIYVHGDSLKA---FLVGIVVPDPEVMP 608
Cdd:cd17648 378 VRECAVVAKEDASQAQSRiqkYLVGYYLPEPGHVP 412
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
146-605 |
3.94e-09 |
|
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: 59.45 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGSGLLQHNCKAcTDQFIGVFAQNrPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGP-GDVVAGLLPRT-PELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 226 DKPQKAVLllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhhapvppqPDDLSIVCFTSGTT 305
Cdd:cd05973 79 DAANRHKL----------------------------------------------------------DSDPFVMMFTSGTT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 306 GNPKGAMLTHgNVVADFSGFLK----VTESVVYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQAN 381
Cdd:cd05973 101 GLPKGVPVPL-RALAAFGAYLRdavdLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGFSVESTWRVIERLGV 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 382 TplkrwllEFAAkrkqAEVRSGIIRNDSIwdelffnKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTE 461
Cdd:cd05973 180 T-------NLAG----SPTAYRLLMAAGA-------EVPARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTE 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 462 C-TAGCTFTTPGDWT-SGHVGAPLPCNHIKLVDvEELNYWACKGEGEICV---RGPNV-FKGYLKDPDRTKealdSDGWL 535
Cdd:cd05973 242 LgMVLANHHALEHPVhAGSAGRAMPGWRVAVLD-DDGDELGPGEPGRLAIdiaNSPLMwFRGYQLPDTPAI----DGGYY 316
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 536 HTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVhgdslkaflvgIVVPDPE 605
Cdd:cd05973 317 LTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFDVESALIEHPAVAEAAV-----------IGVPDPE 374
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
285-618 |
9.56e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 59.20 E-value: 9.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 285 HAP-VPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgFLKVTESvvychggrvgFFQgdirLLSDDmkalcptifp 363
Cdd:PRK12316 4685 HDPaVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVN----HLHATGE----------RYE----LTPDD---------- 4736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 364 vvpRLLNRM---YDKIFSQANTPLKRwllefaakrkQAEVrsgIIRNDSIWD-ELFFNKI---QASLGGCV----RMIVT 432
Cdd:PRK12316 4737 ---RVLQFMsfsFDGSHEGLYHPLIN----------GASV---VIRDDSLWDpERLYAEIhehRVTVLVFPpvylQQLAE 4800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 433 GAA----PASPTVLGF-------------LRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSG----HVGAPLPCNHIKL 490
Cdd:PRK12316 4801 HAErdgePPSLRVYCFggeavaqasydlaWRALKPVYLFNGYGPTETTVTVLlWKARDGDACGaaymPIGTPLGNRSGYV 4880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 491 VDVEeLNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSD------GWLH-TGDIGKWLPAGTLKVIDRKKHIFKLaQ 563
Cdd:PRK12316 4881 LDGQ-LNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDpfgapgGRLYrTGDLARYRADGVIDYLGRVDHQVKI-R 4958
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622946790 564 GEYVAPEKIEnIYIRSQP-------VAQIYVHGdslkAFLVGIVVP-DPEVMPSWAQKRGIEG 618
Cdd:PRK12316 4959 GFRIELGEIE-ARLREHPavreavvIAQEGAVG----KQLVGYVVPqDPALADADEAQAELRD 5016
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
111-614 |
2.47e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 57.66 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 111 YDDARTMYQVFRRGLSISGNGPCLGFRKpnqpyQWLSYQEVADRAEFLGSGLLQhnCKACTDQFIGVFAQNRPEWIIAEL 190
Cdd:PRK12316 507 YPLQRGVHRLFEEQVERTPEAPALAFGE-----ETLDYAELNRRANRLAHALIE--RGVGPDVLVGVAMERSIEMVVALL 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 191 ACYTYSMVVVPLYDTLGPGAIRYIINTADIstvivdkpqkAVLLLEHVERKETP---GLKLIILMDP--FEEALKERGQK 265
Cdd:PRK12316 580 AILKAGGAYVPLDPEYPAERLAYMLEDSGV----------QLLLSQSHLGRKLPlaaGVQVLDLDRPaaWLEGYSEENPG 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 266 CGVViksmqavedcgqenhhapvppqPDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgflkvtesvvychggRVGFFQG 345
Cdd:PRK12316 650 TELN----------------------PENLAYVIYTSGSTGKPKGAGNRHRALSN------------------RLCWMQQ 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 346 DIRL-LSDDMKALCPTIFPV------VPrLLN--RMYDKIFSQANTPLKRW---------LLEFAAKRKQAEVRSGIIrn 407
Cdd:PRK12316 690 AYGLgVGDTVLQKTPFSFDVsvweffWP-LMSgaRLVVAAPGDHRDPAKLVelinregvdTLHFVPSMLQAFLQDEDV-- 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 408 dsiwdelffnkiqASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHV--GAPLPC 485
Cdd:PRK12316 767 -------------ASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGGDSVpiGRPIAN 833
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 486 NHIKLVDVeELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL------DSDGWLHTGDIGKWLPAGTLKVIDRKKHIF 559
Cdd:PRK12316 834 LACYILDA-NLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFvpspfvAGERMYRTGDLARYRADGVIEYAGRIDHQV 912
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622946790 560 KLaQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAfLVGIVVPD------PEVMPSWAQKR 614
Cdd:PRK12316 913 KL-RGLRIELGEIEARLLEHPWVREAAVLAVDGKQ-LVGYVVLEseggdwREALKAHLAAS 971
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
226-597 |
3.46e-08 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 56.96 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 226 DKPQKAVLLLEHVERketpGLkLIILMDPF----EEALKERGQKCGVVIKS------------MQAVEDCGQENHHAPVP 289
Cdd:PRK06060 64 DSPDLVQLLLACLAR----GV-MAFLANPElhrdDHALAARNTEPALVVTSdalrdrfqpsrvAEAAELMSEAARVAPGG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 290 PQP---DDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgFLKVTesvvyCHGGrvgffqgdIRLLSDDMkALCPTIFPVVP 366
Cdd:PRK06060 139 YEPmggDALAYATYTSGTTGPPKAAIHRHADPLT----FVDAM-----CRKA--------LRLTPEDT-GLCSARMYFAY 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 367 RLLNRMYDKIFSQANT-----PLKRWLLEFAAKRKQAEVRSGIIRndsiwdelFFNKIqasLGGC-------VRMIVTGA 434
Cdd:PRK06060 201 GLGNSVWFPLATGGSAvinsaPVTPEAAAILSARFGPSVLYGVPN--------FFARV---IDSCspdsfrsLRCVVSAG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 435 APASPTVLGFLRAALG-CQVYEGYGQTEctAGCTFT--TPGDWTSGHVGAPLPCNHIKLVDVEELNYwACKGEGEICVRG 511
Cdd:PRK06060 270 EALELGLAERLMEFFGgIPILDGIGSTE--VGQTFVsnRVDEWRLGTLGRVLPPYEIRVVAPDGTTA-GPGVEGDLWVRG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 512 PNVFKGYLKDPDrtkEALDSDGWLHTGDIGK-----WLPAGTlkvidrKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIY 586
Cdd:PRK06060 347 PAIAKGYWNRPD---SPVANEGWLDTRDRVCidsdgWVTYRC------RADDTEVIGGVNVDPREVERLIIEDEAVAEAA 417
|
410
....*....|....*...
gi 1622946790 587 VHG-------DSLKAFLV 597
Cdd:PRK06060 418 VVAvrestgaSTLQAFLV 435
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
287-606 |
6.07e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 55.79 E-value: 6.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 287 PVPPQPDDlSIVCFTSGTTGNPKG--------AMLTHGN-VVADFSGFLKVTESVVYCHGGRVgFFQGDIRLLSDdMKAL 357
Cdd:PRK13390 143 RLTEQPCG-AVMLYSSGTTGFPKGiqpdlpgrDVDAPGDpIVAIARAFYDISESDIYYSSAPI-YHAAPLRWCSM-VHAL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 358 CPTIfpvvprllnrMYDKIFSQANTplKRWLLEFAAKRKQAeVRSGIIRNDSIWDELFFNKIQASLggcvRMIVTGAAPA 437
Cdd:PRK13390 220 GGTV----------VLAKRFDAQAT--LGHVERYRITVTQM-VPTMFVRLLKLDADVRTRYDVSSL----RAVIHAAAPC 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 438 SPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVG-APLPCNHIKLVDVEELNywackgEGEIcvrGPNV 514
Cdd:PRK13390 283 PVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGrSVLGDLHICDDDGNELP------AGRI---GTVY 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 515 FK------GYLKDPDRTKEALDSDG--WLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIY 586
Cdd:PRK13390 353 FErdrlpfRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQETENALTMHPAVHDVA 431
|
330 340
....*....|....*....|
gi 1622946790 587 VHGdslkaflvgivVPDPEV 606
Cdd:PRK13390 432 VIG-----------VPDPEM 440
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
480-556 |
1.11e-07 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 55.01 E-value: 1.11e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622946790 480 GAPLPCNHIKLVDV--EELNYwacKGEGEICVRGPNVFKGYLKDPDRTKeALDSDGWLHTGDIGkWLPAGTLKVIDRKK 556
Cdd:PRK09192 388 GKALPGHEIEIRNEagMPLPE---RVVGHICVRGPSLMSGYFRDEESQD-VLAADGWLDTGDLG-YLLDGYLYITGRAK 461
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
293-614 |
1.11e-07 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 54.28 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 293 DDLSIVCFTSGTTGNPKGAMLTHGNVVAD----------------------FSGFLKVTESVV---------YCHGGRVG 341
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTASadathdrlggpgqwllalpahhIAGLQVLVRSVIagsepveldVSAGFDPT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 342 FFQGDIRLLSDDMK--ALCPTifpvvpRLLNRMYDKIFSQAntplkrwLLEFAAkrkqaevrsgiirndsiwdelffnki 419
Cdd:PRK07824 115 ALPRAVAELGGGRRytSLVPM------QLAKALDDPAATAA-------LAELDA-------------------------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 420 qaslggcvrmIVTGAAPASPTVlgfLRAA--LGCQVYEGYGQTECTAGCTFTtpgdwtsghvGAPLPCNHIKLVDveeln 497
Cdd:PRK07824 156 ----------VLVGGGPAPAPV---LDAAaaAGINVVRTYGMSETSGGCVYD----------GVPLDGVRVRVED----- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 498 ywackgeGEICVRGPNVFKGY--LKDPDrtkeALDSDGWLHTGDIGKwLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENI 575
Cdd:PRK07824 208 -------GRIALGGPTLAKGYrnPVDPD----PFAEPGWFRTDDLGA-LDDGVLTVLGRADDAISTG-GLTVLPQVVEAA 274
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1622946790 576 YIRSQPVAQIYVHG---DSLKAFLVGIVVPDPEVMPSWAQKR 614
Cdd:PRK07824 275 LATHPAVADCAVFGlpdDRLGQRVVAAVVGDGGPAPTLEALR 316
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
427-620 |
1.46e-07 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 54.63 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 427 VRMIVTGAAPASPTVLGFLRAA--LGCQVYeGYGQTECTAGCTFTTPGDWT---SGHVGAPLPCNHIKLVDVEELNYWAC 501
Cdd:PRK05857 288 LRLVGYGGSRAIAADVRFIEATgvRTAQVY-GLSETGCTALCLPTDDGSIVkieAGAVGRPYPGVDVYLAATDGIGPTAP 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 502 KGE-----GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIY 576
Cdd:PRK05857 367 GAGpsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGGVNIAPDEVDRIA 444
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622946790 577 IRSQPV--AQIYVHGDSLKAFLVGI-VVPDPEVMPSWAQ--KRGIEGTY 620
Cdd:PRK05857 445 EGVSGVreAACYEIPDEEFGALVGLaVVASAELDESAARalKHTIAARF 493
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
290-613 |
1.72e-07 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 53.93 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 290 PQPDDLSIVCfTSGTTGNPKGAMLTHGNV-VADFSGFLKVTESvvychggrvgfFQGDIRLLSDDMKALCPTIFPVVP-- 366
Cdd:cd05924 1 RSADDLYILY-TGGTTGMPKGVMWRQEDIfRMLMGGADFGTGE-----------FTPSEDAHKAAAAAAGTVMFPAPPlm 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 367 ---RLLNRMYDKIFSQA-NTPLKRW----LLEFAAKRKqaeVRSGIIRNDSIWDELffnkIQASLGG------CVRMIVT 432
Cdd:cd05924 69 hgtGSWTAFGGLLGGQTvVLPDDRFdpeeVWRTIEKHK---VTSMTIVGDAMARPL----IDALRDAgpydlsSLFAISS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 433 GAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFTTPGdwtSGHVGAPL-PCNHIKLVDVEELNYWACK--GEGEIC 508
Cdd:cd05924 142 GGALLSPEVKqGLLELVPNITLVDAFGSSETGFTGSGHSAG---SGPETGPFtRANPDTVVLDDDGRVVPPGsgGVGWIA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 509 VRGpNVFKGYLKDPDRTKEA---LDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIyIRSQP-VAQ 584
Cdd:cd05924 219 RRG-HIPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTG-GEKVFPEEVEEA-LKSHPaVYD 295
|
330 340
....*....|....*....|....*....
gi 1622946790 585 IYVHGdslkaflvgivVPDPEvmpsWAQK 613
Cdd:cd05924 296 VLVVG-----------RPDER----WGQE 309
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
457-575 |
1.72e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 54.39 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 457 YGQTECTAGCTFTTPG-----------DWTSGH----VGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKD 521
Cdd:PRK05851 310 YGLAESTCAVTVPVPGiglrvdevttdDGSGARrhavLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQ 389
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1622946790 522 PdrtkeALDSDGWLHTGDIGkWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENI 575
Cdd:PRK05851 390 A-----PIDPDDWFPTGDLG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERV 436
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
147-609 |
8.42e-07 |
|
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: 52.19 E-value: 8.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 147 SYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIIntADISTVIVd 226
Cdd:cd17634 86 SYRELHREVCRFAGTLLDLGVKK--GDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRI--IDSSSRLL- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 227 kpqkaVLLLEHVERKETPGLKLIIlmdpfEEALKERGQKC-GVVIKSMQAVEDCGQEN--------------HHAPVPPQ 291
Cdd:cd17634 161 -----ITADGGVRAGRSVPLKKNV-----DDALNPNVTSVeHVIVLKRTGSDIDWQEGrdlwwrdliakaspEHQPEAMN 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 292 PDDLSIVCFTSGTTGNPKGAMLTHGnvvadfsGF-LKVTESVVYC---HGG-------RVGFFQGDIRLLSDDMkALCPT 360
Cdd:cd17634 231 AEDPLFILYTSGTTGKPKGVLHTTG-------GYlVYAATTMKYVfdyGPGdiywctaDVGWVTGHSYLLYGPL-ACGAT 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 361 IF-----PVVPRlLNRMYDKIFSQANTPLkrWLLEFAAKRKQAEVRSGIIRNDsiwdelffnkiQASLggcvRMIVTGAA 435
Cdd:cd17634 303 TLlyegvPNWPT-PARMWQVVDKHGVNIL--YTAPTAIRALMAAGDDAIEGTD-----------RSSL----RILGSVGE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 436 PASPTVLGFLRAALG---CQVYEGYGQTECTAGCTFTTPG--DWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVR 510
Cdd:cd17634 365 PINPEAYEWYWKKIGkekCPVVDTWWQTETGGFMITPLPGaiELKAGSATRPVFGVQPAVVD-NEGHPQPGGTEGNLVIT 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 511 G--PNVFKGYLKDPDRTKEALDS--DGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIY 586
Cdd:cd17634 444 DpwPGQTRTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVA-GHRLGTAEIESVLVAHPKVAEAA 522
|
490 500
....*....|....*....|....*.
gi 1622946790 587 VHG--DSLKA-FLVGIVVPDPEVMPS 609
Cdd:cd17634 523 VVGipHAIKGqAPYAYVVLNHGVEPS 548
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
146-584 |
1.02e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 52.48 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGSGLLQHncKACTDQFIGVFAQNrPEWIIAELACYTYSMVVVPLYDtlgPGAIR--------YIINT 217
Cdd:PRK05691 41 LSYRDLDLRARTIAAALQAR--ASFGDRAVLLFPSG-PDYVAAFFGCLYAGVIAVPAYP---PESARrhhqerllSIIAD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 218 ADISTVIVDKP-QKAVLLLEHVERKETPGLkliILMDPFEEALKERGQKCGVviksmqavedcgqenhhapvppQPDDLS 296
Cdd:PRK05691 115 AEPRLLLTVADlRDSLLQMEELAAANAPEL---LCVDTLDPALAEAWQEPAL----------------------QPDDIA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 297 IVCFTSGTTGNPKGAMLTHGNVVADfsgflkvtESVVYcHGGRVGFFQGDIRL----LSDDM---KALCPTIFPVVPRLL 369
Cdd:PRK05691 170 FLQYTSGSTALPKGVQVSHGNLVAN--------EQLIR-HGFGIDLNPDDVIVswlpLYHDMgliGGLLQPIFSGVPCVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 370 nrMYDKIFSQanTPLkRWLL-------------EFAAKRKQAEVR------------------SGIIRNDSIwdELFFNK 418
Cdd:PRK05691 241 --MSPAYFLE--RPL-RWLEaiseyggtisggpDFAYRLCSERVSesalerldlsrwrvaysgSEPIRQDSL--ERFAEK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 419 IQ----------ASLG-GCVRMIVTGAAPA-SPTVLGFLRAALGCQVYEGyGQTECTAGCTFTTPGdwtsghvgaplpcN 486
Cdd:PRK05691 314 FAacgfdpdsffASYGlAEATLFVSGGRRGqGIPALELDAEALARNRAEP-GTGSVLMSCGRSQPG-------------H 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 487 HIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEA---LDSDGWLHTGDIGkWLPAGTLKVIDRKKHIFkLAQ 563
Cdd:PRK05691 380 AVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfveHDGRTWLRTGDLG-FLRDGELFVTGRLKDML-IVR 457
|
490 500
....*....|....*....|.
gi 1622946790 564 GEYVAPEKIENIYIRSQPVAQ 584
Cdd:PRK05691 458 GHNLYPQDIEKTVEREVEVVR 478
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
482-542 |
2.41e-06 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 50.66 E-value: 2.41e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622946790 482 PLPCNHIK-----LVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL-DSDGW--LHTGDIGK 542
Cdd:PRK04813 317 RLPIGYAKpdsplLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGY 385
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
146-335 |
1.36e-05 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 48.33 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAE-----FLGSGLLQHNCkactdqfIGVFAQNRPEWIIAELACyTYSMVVVPLYDT-LGPGAIRYIINTAD 219
Cdd:PRK08279 63 ISYAELNARANryahwAAARGVGKGDV-------VALLMENRPEYLAAWLGL-AKLGAVVALLNTqQRGAVLAHSLNLVD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 220 ISTVIVDKPqkavlLLEHVE--RKETPGLKLIILMDPFEEALKERgqkcgvVIKSMQAVEDCGQENHHAPVPPQPDDLSI 297
Cdd:PRK08279 135 AKHLIVGEE-----LVEAFEeaRADLARPPRLWVAGGDTLDDPEG------YEDLAAAAAGAPTTNPASRSGVTAKDTAF 203
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622946790 298 VCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTES-VVYC 335
Cdd:PRK08279 204 YIYTSGTTGLPKAAVMSHMRWLkamGGFGGLLRLTPDdVLYC 245
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
427-574 |
1.49e-05 |
|
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: 47.40 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 427 VRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTEcTAGCTFTTPGD-WTSGHVGAPLPCNHIKLVDVEElnywacKGE 504
Cdd:cd17633 112 IKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSE-LSFITYNFNQEsRPPNSVGRPFPNVEIEIRNADG------GEI 184
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 505 GEICVRGPNVFKGYLKDPDRTKealdsDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIEN 574
Cdd:cd17633 185 GKIFVKSEMVFSGYVRGGFSNP-----DGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIES 248
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
146-597 |
2.27e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 47.68 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK13383 61 LSYRELQRATESLARRLTRDGVAP--GRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 226 DkpqkavlllehverketpglkliilmDPFEEALKERGQKCGVVIKSMQAVEDCGQENHHAPVPpqpddlSIVCFTSGTT 305
Cdd:PRK13383 139 D--------------------------NEFAERIAGADDAVAVIDPATAGAEESGGRPAVAAPG------RIVLLTSGTT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 306 GNPKGaMLTHGNVVADFSGFLKVTESVVYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVprLLNRMYDKIFSQANTPLK 385
Cdd:PRK13383 187 GKPKG-VPRAPQLRSAVGVWVTILDRTRLRTGSRISVAMPMFHGLGLGMLMLTIALGGTV--LTHRHFDAEAALAQASLH 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 386 RwllefaakrkqAEVRSGI-IRNDSIWDelFFNKIQA-SLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECT 463
Cdd:PRK13383 264 R-----------ADAFTAVpVVLARILE--LPPRVRArNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 464 AGcTFTTPG---DWTSGhVGAPLPCNHIKLVDVEELNYwACKGEGEICVRGPNVFKGYlkdPDRTKEALdSDGWLHTGDI 540
Cdd:PRK13383 331 IG-ALATPAdlrDAPET-VGKPVAGCPVRILDRNNRPV-GPRVTGRIFVGGELAGTRY---TDGGGKAV-VDGMTSTGDM 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622946790 541 GKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLV 597
Cdd:PRK13383 404 GYLDNAGRLFIVGREDDMI-ISGGENVYPRAVENALAAHPAVADNAVigvpderFGHRLAAFVV 466
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
292-597 |
2.36e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 47.86 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 292 PDDLSIVCFTSGTTGNPKGAMLT-HGNVVADFSG--FLKVTESVVYCH-------------------GGRVGFFQGDIrl 349
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEqRGMLNNQLSKvpYLALSEADVIAQtasqsfdisvwqflaaplfGARVEIVPNAI-- 3945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 350 lSDDMKALCP-------TIFPVVPRLLNRMydkifsqantplkrwllefaakrkqaevrsgiIRNDsiwdelffnkiQAS 422
Cdd:PRK05691 3946 -AHDPQGLLAhvqaqgiTVLESVPSLIQGM--------------------------------LAED-----------RQA 3981
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 423 LGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF------TTPGDWTSghVGAPLPCNHIKLVDvEEL 496
Cdd:PRK05691 3982 LDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFfrvdlaSTRGSYLP--IGSPTDNNRLYLLD-EAL 4058
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 497 NYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL-------DSDGWLHTGDIGKWLPAGTLKVIDRKKHI-----FKLAQG 564
Cdd:PRK05691 4059 ELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFvphpfgaPGERLYRTGDLARRRSDGVLEYVGRIDHQvkirgYRIELG 4138
|
330 340 350
....*....|....*....|....*....|....
gi 1622946790 565 EYVApEKIENIYIRSQPVA-QIYVHGDSLKAFLV 597
Cdd:PRK05691 4139 EIEA-RLHEQAEVREAAVAvQEGVNGKHLVGYLV 4171
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
424-606 |
4.42e-05 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 46.68 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 424 GGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFT-TPGDWTSG--HVGAPLPCNHIKLVDVE--ELNy 498
Cdd:PRK13382 311 GRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATE--AGMIATaTPADLRAApdTAGRPAEGTEIRILDQDfrEVP- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 499 wacKGE-GEICVRGPNVFKGYlkDPDRTKEAldSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIyI 577
Cdd:PRK13382 388 ---TGEvGTIFVRNDTQFDGY--TSGSTKDF--HDGFMASGDVGYLDENGRLFVVGRDDEMI-VSGGENVYPIEVEKT-L 458
|
170 180 190
....*....|....*....|....*....|....*..
gi 1622946790 578 RSQP-VAQIYV-------HGDSLKAFlvgiVVPDPEV 606
Cdd:PRK13382 459 ATHPdVAEAAVigvddeqYGQRLAAF----VVLKPGA 491
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
294-605 |
5.99e-05 |
|
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: 46.19 E-value: 5.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 294 DLSIVCFTSGTTGNPKGAMLTH-----GNVVADFSGFLKVTESVVYC----H--GGRVGFFQGdirLLS----------- 351
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHrrawrGGAFFAGSGGALPSDVLYTClplyHstALIVGWSAC---LASgatlvirkkfs 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 352 -----DDMKALCPTIFPVVPRLLnrmydkifsqantplkRWLLefAAKRKQAEVRsgiirndsiwdelffNKIQASLGGC 426
Cdd:cd05940 159 asnfwDDIRKYQATIFQYIGELC----------------RYLL--NQPPKPTERK---------------HKVRMIFGNG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 427 VRmivtgaapasPTVLGFLRAALGC-QVYEGYGQTECTAGCT--FTTPGdwTSGHVGAPLPCNH-IKLV--DVEELNYW- 499
Cdd:cd05940 206 LR----------PDIWEEFKERFGVpRIAEFYAATEGNSGFInfFGKPG--AIGRNPSLLRKVApLALVkyDLESGEPIr 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 500 --------ACKGE-----GEICVRGPnvFKGYLKDPDRTKEAL-----DSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKL 561
Cdd:cd05940 274 daegrcikVPRGEpglliSRINPLEP--FDGYTDPAATEKKILrdvfkKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRW 351
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1622946790 562 aQGEYVAPEKIENIYIRSQPVAQIYVHGDSL-----KAFLVGIVVPDPE 605
Cdd:cd05940 352 -KGENVSTTEVAAVLGAFPGVEEANVYGVQVpgtdgRAGMAAIVLQPNE 399
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
416-694 |
9.73e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 45.54 E-value: 9.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 416 FNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPGDWTSGHVGAPLPCNHIKLVDVEE 495
Cdd:PRK07638 245 LYKENRVIENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSF-VTALVDEESERRPNSVGRPFHNVQVRICNE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 496 LNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEaLDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIEN 574
Cdd:PRK07638 324 AGEEVQKGEiGTVYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIES 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 575 IYIRSQPVAQIYVHGdslkaflvgivVPDpevmPSWAQKRG--IEGTyadlCTSKDLKKAILEDmvrlgkesgLHSFEQV 652
Cdd:PRK07638 402 VLHEHPAVDEIVVIG-----------VPD----SYWGEKPVaiIKGS----ATKQQLKSFCLQR---------LSSFKIP 453
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1622946790 653 KAIHIhsdmfsVQNGLLTPTLKAKRPELreyfKKQIEELYSI 694
Cdd:PRK07638 454 KEWHF------VDEIPYTNSGKIARMEA----KSWIENQEKI 485
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
417-581 |
1.36e-04 |
|
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: 45.11 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 417 NKIQASLGGCVRMIVTGAAPASPTV----LGFLRA--ALGCQVYEGYGqTECTAGCTFTTPGDWTSGHVGAPLPCNHI-K 489
Cdd:cd05915 263 ESTGHRLKTLRRLVVGGSAAPRSLIarfeRMGVEVrqGYGLTETSPVV-VQNFVKSHLESLSEEEKLTLKAKTGLPIPlV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 490 LVDVEELNYWACKGEGE----ICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGE 565
Cdd:cd05915 342 RLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG-GE 420
|
170
....*....|....*.
gi 1622946790 566 YVAPEKIENIyIRSQP 581
Cdd:cd05915 421 WISSVDLENA-LMGHP 435
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
292-589 |
2.91e-04 |
|
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: 43.96 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 292 PDDLSIVCFTSGTTGNPKGAM------LTHGNVVADFSGfLKVTESVVYC----HGgrVGFFQGdirLLSDDMKALCPTI 361
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAiswrrtLVTSNLLSHDLN-LKNGDRTYTCmplyHG--TAAFLG---ACNCLMSGGTLAL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 362 FPVVPrlLNRMYDKIF-SQANT-----PLKRWLLEFAAkrkqaevrsgiirndSIWDELffNKIQASLGGCVRmivtgaa 435
Cdd:cd05937 160 SRKFS--ASQFWKDVRdSGATIiqyvgELCRYLLSTPP---------------SPYDRD--HKVRVAWGNGLR------- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 436 pasPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKL--------VDVEELNYW------- 499
Cdd:cd05937 214 ---PDIWERFRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKFenqvvlvkMDPETDDPIrdpktgf 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 500 ---ACKGE-GEICVRGPNV----FKGYLKDPDRTKEAL------DSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGE 565
Cdd:cd05937 291 cvrAPVGEpGEMLGRVPFKnreaFQGYLHNEDATESKLvrdvfrKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRW-KSE 369
|
330 340
....*....|....*....|....
gi 1622946790 566 YVAPEKIENIYIRSQPVAQIYVHG 589
Cdd:cd05937 370 NVSTTEVADVLGAHPDIAEANVYG 393
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
251-334 |
5.41e-04 |
|
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: 43.05 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 251 LMDPFEE---ALKERGQKCGVVIKSM--QAVEDCGQENHHAPVPPQPDDLS---------IVCFTSGTTGNPKGAMLTHG 316
Cdd:cd05938 88 LQEAVEEvlpALRADGVSVWYLSHTSntEGVISLLDKVDAASDEPVPASLRahvtikspaLYIYTSGTTGLPKAARISHL 167
|
90 100
....*....|....*....|..
gi 1622946790 317 NVVAdFSGFLKV----TESVVY 334
Cdd:cd05938 168 RVLQ-CSGFLSLcgvtADDVIY 188
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
288-319 |
5.66e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 43.49 E-value: 5.66e-04
10 20 30
....*....|....*....|....*....|..
gi 1622946790 288 VPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVV 319
Cdd:PRK10252 593 QLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIV 624
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
413-598 |
1.04e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.85 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 413 ELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTF--TTPGDWTSGHVGAPLPCNHIK 489
Cdd:PRK05691 1376 QLFIDEPLAAACTSLRRLFSGGEALPAELRNRVLQRLpQVQLHNRYGPTETAINVTHwqCQAEDGERSPIGRPLGNVLCR 1455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 490 LVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKE-----ALDSDG--WLHTGDIGKWLPAGTLKVIDRKKHIFKLa 562
Cdd:PRK05691 1456 VLD-AELNLLPPGVAGELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL- 1533
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622946790 563 QGEYVAPEKIENIYIRSQPVAQ--IYVHGDSLKAFLVG 598
Cdd:PRK05691 1534 RGFRVEPEEIQARLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
516-604 |
2.26e-03 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 41.57 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946790 516 KGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIyIRSQP-VAQIYVH 588
Cdd:PRK10252 814 QGYLGRPDLTASRFIADPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKI-RGQRIELGEIDRA-MQALPdVEQAVTH 891
|
90 100
....*....|....*....|....*..
gi 1622946790 589 -----------GDSLKafLVGIVVPDP 604
Cdd:PRK10252 892 acvinqaaatgGDARQ--LVGYLVSQS 916
|
|
| |
