|
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 ... |
141-707 |
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: 878.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 141 QPYQWLSYQEVADRAEFLGSGLLQHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADI 220
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 221 STVIVDKpqkavlllehverketpGLKlIILMDPFEEalKERGQKCGVVIKSMQAVEHFLLSGlwprespGSCGNPKGAM 300
Cdd:cd05927 81 SIVFCDA-----------------GVK-VYSLEEFEK--LGKKNKVPPPPPKPEDLATICYTS-------GTTGNPKGVM 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 301 LTHGNVVADFSGFLKVTESQWAPTCADVHISYLPLAHMFERMVQSVVYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVP 380
Cdd:cd05927 134 LTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDIKALKPTVFPGVP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 381 RLLNRMYDKIFS--QANTPLKRWLLEFAAKRKQAEVRSGIIRNDSIWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGF 458
Cdd:cd05927 214 RVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLTGSAPLSPEVLEF 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 459 LRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWA--CKGEGEICVRGPNVFKGYLKDP 536
Cdd:cd05927 294 LRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAkdPNPRGEVCIRGPNVFSGYYKDP 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 537 DRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGIVVP 616
Cdd:cd05927 374 EKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGDSLKSFLVAIVVP 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 617 DPEVMPSWA-QKRGIEGTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELR 695
Cdd:cd05927 454 DPDVLKEWAaSKGGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLLTPTFKLKRPQLK 533
|
570
....*....|..
gi 2230395409 696 EYFKKQIEELYS 707
Cdd:cd05927 534 KYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
97-707 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 659.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 97 RSViGSGPQLLTHY--YDDARTMYQVFRRGLSISGNGPCLGFRKPKQ----PYQWLSYQEVADRAEFLGSGLLQHNCK-- 168
Cdd:PLN02736 25 RSA-RSPLKLVSRFpdHPEIGTLHDNFVYAVETFRDYKYLGTRIRVDgtvgEYKWMTYGEAGTARTAIGSGLVQHGIPkg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 169 ACtdqfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVdKPQKAVLLLEHVerKETPGLKL 248
Cdd:PLN02736 104 AC----VGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCL--SEIPSVRL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 249 IILMDPFEEALKERGQKCGVVIKSMQAVEHFLLSGLWPRESP------------GSCGNPKGAMLTHGNVVADFSGFLKV 316
Cdd:PLN02736 177 IVVVGGADEPLPSLPSGTGVEIVTYSKLLAQGRSSPQPFRPPkpedvaticytsGTTGTPKGVVLTHGNLIANVAGSSLS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 317 TESqwAPtcADVHISYLPLAHMFERMVQSVVYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QA 394
Cdd:PLN02736 257 TKF--YP--SDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNavKE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 395 NTPLKRWLLEFAAKRKQAEVRSGiiRNDS-IWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQ 473
Cdd:PLN02736 333 SGGLKERLFNAAYNAKKQALENG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGM 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 474 TECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKG---EGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH 550
Cdd:PLN02736 411 TETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLH 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 551 TGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGI 630
Cdd:PLN02736 491 TGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGI 570
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2230395409 631 E-GTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 707
Cdd:PLN02736 571 KyEDLKQLCNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYA 648
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
111-707 |
5.56e-165 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 487.69 E-value: 5.56e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 111 YDDARTMYQVFRRGLSISGNGPCLGFRKPKQpYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVEL 190
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVALREKEDGI-WQSLTWAEFAERVRALAAGLLALGVKP--GDRVAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 191 ACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAVLLLEHveRKETPGLKLIILMDPFE----------EALK 260
Cdd:COG1022 84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEV--RDELPSLRHIVVLDPRGlrddprllslDELL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 261 ERGQKcgvvIKSMQAVEHfllsgLWPRESP----------GSCGNPKGAMLTHGNVVADFSGFLKVtesqWAPTCADVHI 330
Cdd:COG1022 162 ALGRE----VADPAELEA-----RRAAVKPddlatiiytsGTTGRPKGVMLTHRNLLSNARALLER----LPLGPGDRTL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 331 SYLPLAHMFERMVQSVVYCHGGRVGFfQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQAN--TPLKRWLLEFA-- 406
Cdd:COG1022 229 SFLPLAHVFERTVSYYALAAGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEeaGGLKRKLFRWAla 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 407 -AKRKQAEVRSGiiRNDSIW--------DELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECT 477
Cdd:COG1022 308 vGRRYARARLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 478 AGCTFTTPGDWTSGHVGAPLPCNHIKLVDveelnywackgEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKW 557
Cdd:COG1022 385 PVITVNRPGDNRIGTVGPPLPGVEVKIAE-----------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGEL 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 558 LPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKaFLVGIVVPDPEVMPSWAQKRGIE-GTYAD 636
Cdd:COG1022 454 DEDGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDGRP-FLAALIVPDFEALGEWAEENGLPyTSYAE 532
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2230395409 637 LCTNKDLKKAILEDMVRLGKesGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 707
Cdd:COG1022 533 LAQDPEVRALIQEEVDRANA--GLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYA 601
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
141-694 |
7.42e-154 |
|
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: 453.59 E-value: 7.42e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 141 QPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADI 220
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEP--GDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 221 STVIVDKPQkavlllehverketpGLKLIILmdpfeealkergqkcgvviksmqavehfllsglwpreSPGSCGNPKGAM 300
Cdd:cd05907 79 KALFVEDPD---------------DLATIIY-------------------------------------TSGTTGRPKGVM 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 301 LTHGNVVADFSGFLKVtesqWAPTCADVHISYLPLAHMFE-RMVQSVVYCHGGRVGFFQgDIRLLSDDMKALCPTIFPVV 379
Cdd:cd05907 107 LSHRNILSNALALAER----LPATEGDRHLSFLPLAHVFErRAGLYVPLLAGARIYFAS-SAETLLDDLSEVRPTVFLAV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 380 PRLLNRMYDKIFSQANTPLKRWLLEFAAkrkqaevrsgiirndsiwdelffnkiqaslGGCVRMIVTGAAPASPTVLGFL 459
Cdd:cd05907 182 PRVWEKVYAAIKVKAVPGLKRKLFDLAV------------------------------GGRLRFAASGGAPLPAELLHFF 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 460 RAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDveelnywackgEGEICVRGPNVFKGYLKDPDRT 539
Cdd:cd05907 232 RA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPNVMLGYYKNPEAT 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 540 KEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKaFLVGIVVPDPE 619
Cdd:cd05907 300 AEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDGRP-FLVALIVPDPE 378
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2230395409 620 VMPSWAQKRGIEG-TYADLCTNKDLKKAILEDMVRLGKEsgLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPEL 694
Cdd:cd05907 379 ALEAWAEEHGIAYtDVAELAANPAVRAEIEAAVEAANAR--LSRYEQIKKFLLLPEPFTIENGELTPTLKLKRPVI 452
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
142-691 |
5.69e-147 |
|
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: 438.19 E-value: 5.69e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 142 PYQWLSYQEVADRAEFLGSGL----LQHNCKactdqfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINT 217
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLvelgLKPGDK------VAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 218 ADISTVIVDKpqkavlllehverketpglkliilmDPFEEALkergqkcgVVIKSmqavehfllsglwprespGSCGNPK 297
Cdd:cd17639 76 TECSAIFTDG-------------------------KPDDLAC--------IMYTS------------------GSTGNPK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 298 GAMLTHGNVVADFSGFLKVTESQWAPTcaDVHISYLPLAHMFERMVQSVVYCHGGRVGFfqGDIRLLSDDMKALC----- 372
Cdd:cd17639 105 GVMLTHGNLVAGIAGLGDRVPELLGPD--DRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDKSKRGCkgdlt 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 373 ---PTIFPVVPRLLNRMYDKIFSQANTP--LKRWLLEFAAKRKQAEVRSGIirnDS-IWDELFFNKIQASLGGCVRMIVT 446
Cdd:cd17639 181 efkPTLMVGVPAIWDTIRKGVLAKLNPMggLKRTLFWTAYQSKLKALKEGP---GTpLLDELVFKKVRAALGGRLRYMLS 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 447 GAAPASPTVLGFLrAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKGE--GEICVR 524
Cdd:cd17639 258 GGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDKPPprGEILIR 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 525 GPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGD 604
Cdd:cd17639 337 GPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVNNICVYAD 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 605 SLKAFLVGIVVPDPEVMPSWAQKRG-IEGTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLL 683
Cdd:cd17639 417 PDKSYPVAIVVPNEKHLTKLAEKHGvINSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEWTPENGLV 496
|
....*...
gi 2230395409 684 TPTLKAKR 691
Cdd:cd17639 497 TAAQKLKR 504
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
83-706 |
6.27e-144 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 435.99 E-value: 6.27e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 83 LMQSEEVEDSGGARRSVigsGPQLLTHYYDDA--------RTMYQVFRRGLSISGNGPCLGFR-----KPKQpYQWLSYQ 149
Cdd:PLN02614 8 IFQVEEGKEGSDGRPSV---GPVYRSIFAKDGfpnpiegmDSCWDVFRMSVEKYPNNPMLGRReivdgKPGK-YVWQTYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 150 EVADRAEFLGSGLlqHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDkpQ 229
Cdd:PLN02614 84 EVYDIVIKLGNSL--RSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVE--E 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 230 KAVLLLEHVERKETPGLKLIILMDPFEEALKERGQKCGVVIKSMqavEHFLLSGL-----WPRESP----------GSCG 294
Cdd:PLN02614 160 KKISELFKTCPNSTEYMKTVVSFGGVSREQKEEAETFGLVIYAW---DEFLKLGEgkqydLPIKKKsdictimytsGTTG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 295 NPKGAMLTHGNVVADFSGFLKVTES-QWAPTCADVHISYLPLAHMFERMVQSVVYCHGGRVGFFQGDIRLLSDDMKALCP 373
Cdd:PLN02614 237 DPKGVMISNESIVTLIAGVIRLLKSaNAALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 374 TIFPVVPRLLNRMYDKIFSQANTP--LKRWLLEFAAKRKQAEVRSGI--IRNDSIWDELFFNKIQASLGGCVRMIVTGAA 449
Cdd:PLN02614 317 TIFCAVPRVLDRVYSGLQKKLSDGgfLKKFVFDSAFSYKFGNMKKGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 450 PASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDVEELNY--WACKGEGEICVRGP 526
Cdd:PLN02614 397 PLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELDMlGTVGPPVPNVDIRLESVPEMEYdaLASTPRGEICIRGK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 527 NVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSL 606
Cdd:PLN02614 477 TLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 607 KAFLVGIVVPDPEVMPSWAQKRGIEGTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPT 686
Cdd:PLN02614 556 ESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPT 635
|
650 660
....*....|....*....|
gi 2230395409 687 LKAKRPELREYFKKQIEELY 706
Cdd:PLN02614 636 FKKKRPQLLKYYQSVIDEMY 655
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
142-707 |
6.34e-140 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 425.41 E-value: 6.34e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 142 PYQWLSYQEVADRAEFLGSGLLQ------HNCkactdqfiGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYII 215
Cdd:PLN02861 74 PYVWLTYKEVYDAAIRIGSAIRSrgvnpgDRC--------GIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFII 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 216 NTADISTVIVDKPQKAVLLleHVERKETPGLKLIILMDPFEEALKERGQKCGVvikSMQAVEHFLLSGLWPRESP----- 290
Cdd:PLN02861 146 NHAEVSIAFVQESKISSIL--SCLPKCSSNLKTIVSFGDVSSEQKEEAEELGV---SCFSWEEFSLMGSLDCELPpkqkt 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 291 ---------GSCGNPKGAMLTHGNVVADF---SGFLKVTESqwAPTCADVHISYLPLAHMFERMVQSVVYCHGGRVGFFQ 358
Cdd:PLN02861 221 dictimytsGTTGEPKGVILTNRAIIAEVlstDHLLKVTDR--VATEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 359 GDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWLLEFAAKRKQAEVRSGIIRNDS--IWDELFFNKIQ 434
Cdd:PLN02861 299 GDIRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQkiSSGGMLRKKLFDFAYNYKLGNLRKGLKQEEAspRLDRLVFDKIK 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 435 ASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCtFTTPGDWTS--GHVGAPLPCNHIKLVDVEELNY 512
Cdd:PLN02861 379 EGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGC-FTSIANVFSmvGTVGVPMTTIEARLESVPEMGY 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 513 WACKG--EGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIY 590
Cdd:PLN02861 458 DALSDvpRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTY 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 591 IRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGIEGTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIH 670
Cdd:PLN02861 537 SRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIH 616
|
570 580 590
....*....|....*....|....*....|....*..
gi 2230395409 671 IHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 707
Cdd:PLN02861 617 LEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYS 653
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
113-706 |
1.98e-138 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 421.53 E-value: 1.98e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 113 DARTMYQVFRRGLSISGNGPCLGFRKPKQ----PYQWLSYQEVADRAEFLGSGLLQHNCKACTDqfIGVFAQNRPEWIIV 188
Cdd:PLN02430 40 DITTAWDIFSKSVEKYPDNKMLGWRRIVDgkvgPYMWKTYKEVYEEVLQIGSALRASGAEPGSR--VGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 189 ELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV-DKPQKAVLlleHVERKETPGLKLIILMDPFEEALKERGQKCG 267
Cdd:PLN02430 118 MEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVqDKKIKELL---EPDCKSAKRLKAIVSFTSVTEEESDKASQIG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 268 VVIKSMqavEHFLLSGlwpRESP------------------GSCGNPKGAMLTHGNVVADFSG---FLKVTESQWapTCA 326
Cdd:PLN02430 195 VKTYSW---IDFLHMG---KENPsetnppkpldictimytsGTSGDPKGVVLTHEAVATFVRGvdlFMEQFEDKM--THD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 327 DVHISYLPLAHMFERMVQSVVYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWLLE 404
Cdd:PLN02430 267 DVYLSFLPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFN 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 405 FAAKRKQAEVRSGIIRNDS--IWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF 482
Cdd:PLN02430 347 ALYKYKLAWMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTL 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 483 TTPGDWTS-GHVGAPLPCNHIKLVDVEELNY--WACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLP 559
Cdd:PLN02430 427 GFPDEMCMlGTVGAPAVYNELRLEEVPEMGYdpLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILP 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 560 AGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGIEGTYADLCT 639
Cdd:PLN02430 506 NGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCS 585
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2230395409 640 NKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 706
Cdd:PLN02430 586 LPELKEHILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMY 652
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
104-707 |
4.16e-119 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 372.53 E-value: 4.16e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 104 PQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRK--PKQ----------------PYQWLSYQEVADRAEFLGSGLLQ- 164
Cdd:PLN02387 47 PELVETPWEGATTLAALFEQSCKKYSDKRLLGTRKliSREfetssdgrkfeklhlgEYEWITYGQVFERVCNFASGLVAl 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 165 -HNckacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQ--KAVLLLEHVERk 241
Cdd:PLN02387 127 gHN----KEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQlkKLIDISSQLET- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 242 etpgLKLIILM-DPFEEALKERGQKCGVVIKSMQAVEHFllsglwPRESP------------------GSCGNPKGAMLT 302
Cdd:PLN02387 202 ----VKRVIYMdDEGVDSDSSLSGSSNWTVSSFSEVEKL------GKENPvdpdlpspndiavimytsGSTGLPKGVMMT 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 303 HGNVVADFSGFLKVTesqwaPTCA--DVHISYLPLAHMFERMVQSVVYCHGGRVGFfqGDIRLLSD-----------DMK 369
Cdd:PLN02387 272 HGNIVATVAGVMTVV-----PKLGknDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDtsnkikkgtkgDAS 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 370 ALCPTIFPVVPRLLNRMYDKIFSQANTP--LKRWLLEFAAKRKQAEVR------SGIIRndSIWDELFFNKIQASLGGCV 441
Cdd:PLN02387 345 ALKPTLMTAVPAILDRVRDGVRKKVDAKggLAKKLFDIAYKRRLAAIEgswfgaWGLEK--LLWDALVFKKIRAVLGGRI 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 442 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKG---E 518
Cdd:PLN02387 423 RFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLISDKpmpR 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 519 GEICVRGPNVFKGYLKDPDRTKEA--LDSDG--WLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQ 594
Cdd:PLN02387 503 GEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSP 582
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 595 PVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGIE-GTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHS 673
Cdd:PLN02387 583 YVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPAKIKLLP 662
|
650 660 670
....*....|....*....|....*....|....
gi 2230395409 674 DMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 707
Cdd:PLN02387 663 EPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
142-576 |
8.15e-113 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 346.61 E-value: 8.15e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 142 PYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADIS 221
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRALGVGK--GDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 222 TVIVDKPQKAVLLLEHVERKETPGLKLIILMDPF--EEALKERGQKCGVVIKSMQAVehfllsglwPRESP-------GS 292
Cdd:pfam00501 96 VLITDDALKLEELLEALGKLEVVKLVLVLDRDPVlkEEPLPEEAKPADVPPPPPPPP---------DPDDLayiiytsGT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 293 CGNPKGAMLTHGNVVADFSGFLKVTESQWAPTCADVHISYLPLAHMFER-MVQSVVYCHGGRVGFFQGDIRL----LSDD 367
Cdd:pfam00501 167 TGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALdpaaLLEL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 368 MKALCPTIFPVVPRLLNRMydkifsqantplkrwlleFAAKRKQAEVRSGiirndsiwdelffnkiqaslggcVRMIVTG 447
Cdd:pfam00501 247 IERYKVTVLYGVPTLLNML------------------LEAGAPKRALLSS-----------------------LRLVLSG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 448 AAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDW---TSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVR 524
Cdd:pfam00501 286 GAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVR 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2230395409 525 GPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLA 576
Cdd:pfam00501 366 GPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
88-706 |
1.02e-87 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 289.95 E-value: 1.02e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 88 EVEDSGGARRSVIGSGPQL--LTHYYDDARTMYQVFRRGLSISGNGPCLGFRKPK--------------QPY-------- 143
Cdd:PTZ00216 40 ETENASAIYRIAGVTDEEHerLRNEWYYGPNFLQRLERICKERGDRRALAYRPVErvekevvkdadgkeRTMevthfnet 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 144 QWLSYQEVADRAEFLGSGL----LQHNCKactdqfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTAD 219
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLaelgLTKGSN------VAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 220 iSTVIVDKPQKAVLLLEHVERKETPGLKLIILmDPFEEALKERGQKC----GVVIKSMQAVEHFLLSGlwpresPGSC-- 293
Cdd:PTZ00216 194 -CKAIVCNGKNVPNLLRLMKSGGMPNTTIIYL-DSLPASVDTEGCRLvawtDVVAKGHSAGSHHPLNI------PENNdd 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 294 -----------GNPKGAMLTHGNVVADFSGF-LKVTESQWAPTCADVHISYLPLAHMFERMVQSVVYCHGGRVGFfqGDI 361
Cdd:PTZ00216 266 lalimytsgttGDPKGVMHTHGSLTAGILALeDRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSP 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 362 RLLSD-------DMKALCPTIFPVVPRLLNRMydKIFSQANTP----LKRWLLEFAAKRKQAEVRSGiiRNDSIWDELFF 430
Cdd:PTZ00216 344 RTLTDtfarphgDLTEFRPVFLIGVPRIFDTI--KKAVEAKLPpvgsLKRRVFDHAYQSRLRALKEG--KDTPYWNEKVF 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 431 NKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCqVYEGYGQTE--CTAGCTFTtpGDWTSGHVGAPLPCNHIKLVDVE 508
Cdd:PTZ00216 420 SAPRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTEtvCCGGIQRT--GDLEPNAVGQLLKGVEMKLLDTE 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 509 ELNYwACKGE--GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKI 586
Cdd:PTZ00216 497 EYKH-TDTPEprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEAL 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 587 ENIYIRSQPVAQ----IYVHGDslKAFLVGIVVPDPEVMPSWAQKRGIEGTYADLCTNKDLKKAILEDMVRLGKESGLHS 662
Cdd:PTZ00216 576 EALYGQNELVVPngvcVLVHPA--RSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKS 653
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 2230395409 663 FEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 706
Cdd:PTZ00216 654 FEIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
141-692 |
6.83e-72 |
|
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: 241.11 E-value: 6.83e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 141 QPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADI 220
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKA--GEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 221 STVIVDKPQKavlllehverketpGLKLIILmdpfeealkergqkcgvviksmqavehfllsglwpreSPGSCGNPKGAM 300
Cdd:cd17640 79 VALVVENDSD--------------DLATIIY-------------------------------------TSGTTGNPKGVM 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 301 LTHGNVVADFSGFLKVTEsqwaPTCADVHISYLPLAHMFERMVQSVVYCHGGRVGFfqGDIRLLSDDMKALCPTIFPVVP 380
Cdd:cd17640 108 LTHANLLHQIRSLSDIVP----PQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDDLKRVKPHYIVSVP 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 381 RLLNRMYDKIFSQ--ANTPLKRWLLEFAAkrkqaevrsgiirndsiwdelffnkiqasLGGCVRMIVTGAAPASPTVLGF 458
Cdd:cd17640 182 RLWESLYSGIQKQvsKSSPIKQFLFLFFL-----------------------------SGGIFKFGISGGGALPPHVDTF 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 459 LRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDR 538
Cdd:cd17640 233 FEA-IGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEA 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 539 TKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKaFLVGIVVPDP 618
Cdd:cd17640 312 TSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQK-RLGALIVPNF 390
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2230395409 619 EVMPSWAQKRGI---EGTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFsVQNGLLTPTLKAKRP 692
Cdd:cd17640 391 EELEKWAKESGVklaNDRSQLLASKKVLKLYKNEIKDEISNRPGFKSFEQIAPFALLEEPF-IENGEMTQTMKIKRN 466
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
143-691 |
6.75e-70 |
|
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: 236.98 E-value: 6.75e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 143 YQWLSYQEVADRAEFLGSGLLQHNCKACTDqfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADIST 222
Cdd:cd05932 4 VVEFTWGEVADKARRLAAALRALGLEPGSK--IALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 223 VIVDKpqkavllLEHVERKE--TPGLKLIILMDPFEEAlkergqKCGVVIKSMQAvEHFLLSGLWPRE---------SPG 291
Cdd:cd05932 82 LFVGK-------LDDWKAMApgVPEGLISISLPPPSAA------NCQYQWDDLIA-QHPPLEERPTRFpeqlatliyTSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 292 SCGNPKGAMLTHGNVVADFSGF---LKVTESqwaptcaDVHISYLPLAHMFERMVQSVVYCHGGRVGFFQGDIRLLSDDM 368
Cdd:cd05932 148 TTGQPKGVMLTFGSFAWAAQAGiehIGTEEN-------DRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTFVEDV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 369 KALCPTIFPVVPRLL----NRMYDKIFSQAntpLKRWLlefaakrkQAEVRSGIIRndsiwdelffNKIQASLG-GCVRM 443
Cdd:cd05932 221 QRARPTLFFSVPRLWtkfqQGVQDKIPQQK---LNLLL--------KIPVVNSLVK----------RKVLKGLGlDQCRL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 444 IVTGAAPASPTVLGFLRaALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDveelnywackgEGEICV 523
Cdd:cd05932 280 AGCGSAPVPPALLEWYR-SLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEILV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 524 RGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHG 603
Cdd:cd05932 348 RSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 604 DSLKAfLVGIVVPDPEVMPSwaqkrgiegtyADLCTNKDLKKAILEDMVRLGKEsgLHSFEQVKAIHIHSDMFSVQNGLL 683
Cdd:cd05932 428 SGLPA-PLALVVLSEEARLR-----------ADAFARAELEASLRAHLARVNST--LDSHEQLAGIVVVKDPWSIDNGIL 493
|
....*...
gi 2230395409 684 TPTLKAKR 691
Cdd:cd05932 494 TPTLKIKR 501
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
138-706 |
3.72e-65 |
|
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: 226.47 E-value: 3.72e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 138 KPKQPYQWLSYQEVADRAE-----FLGSGLLQHNCkactdqfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIR 212
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRqaakaFLKLGLERFHG-------VGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 213 YIINTADISTVIVDKPQKAVLLLEhvERKETPGLKLII-LMDPFEEALK-----ERGQKCGVVIKSMQavEHFLLSGLWP 286
Cdd:cd05933 74 YVAETSEANILVVENQKQLQKILQ--IQDKLPHLKAIIqYKEPLKEKEPnlyswDEFMELGRSIPDEQ--LDAIISSQKP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 287 RE------SPGSCGNPKGAMLTHGNVVADFSGFLKVTESQWAPTCADVHISYLPLAHMFERMVQS-VVYCHGGRVGFFQG 359
Cdd:cd05933 150 NQcctliyTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIwLPIKVGGQVYFAQP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 360 DIR--LLSDDMKALCPTIFPVVPRLLNRMYDKI---FSQAnTPLKRWLLEFAaKRKQAEV-------RSGIIRNDSIWDE 427
Cdd:cd05933 230 DALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkavGAKS-GTLKRKIASWA-KGVGLETnlklmggESPSPLFYRLAKK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 428 LFFNKIQASLG--GCVRMIvTGAAPASPTVLGFLrAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLV 505
Cdd:cd05933 308 LVFKKVRKALGldRCQKFF-TGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIH 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 506 DVEelnywaCKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEK 585
Cdd:cd05933 386 NPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVP 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 586 IENIYIRSQP-VAQIYVHGDSLKaFLVGIVV------PD---------PEVMpSWAQKRGIEGTY-ADLCTNKDLK--KA 646
Cdd:cd05933 460 IEDAVKKELPiISNAMLIGDKRK-FLSMLLTlkcevnPEtgepldeltEEAI-EFCRKLGSQATRvSEIAGGKDPKvyEA 537
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 647 ILEDMVRLGKESGLHSFEQVKAIHIHSDmFSVQNGLLTPTLKAKRPELREYFKKQIEELY 706
Cdd:cd05933 538 IEEGIKRVNKKAISNAQKIQKWVILEKD-FSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
117-618 |
3.22e-60 |
|
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: 209.28 E-value: 3.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 117 MYQVFRRGLSISGNGPCLGFRkpkqpYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYS 196
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG-----GRRLTYAELDARARRLAAALRALGVGP--GDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 197 MVVVPLYDTLGPGAIRYIINTADISTVIVdkpqkAVLLLehverkeTpglkliilmdpfeealkergqkcgvviksmqav 276
Cdd:COG0318 74 AVVVPLNPRLTAEELAYILEDSGARALVT-----ALILY-------T--------------------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 277 ehfllsglwpreSpGSCGNPKGAMLTHGNVVADFSGFLKVtesqWAPTCADVHISYLPLAHMFErMVQSVVYC--HGGRV 354
Cdd:COG0318 109 ------------S-GTTGRPKGVMLTHRNLLANAAAIAAA----LGLTPGDVVLVALPLFHVFG-LTVGLLAPllAGATL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 355 ----GFfqgDIRLLSDDMKALCPTIFPVVPRLLNRMYDkifsqantplkrwllefAAKRKQAEVRSgiirndsiwdelff 430
Cdd:COG0318 171 vllpRF---DPERVLELIERERVTVLFGVPTMLARLLR-----------------HPEFARYDLSS-------------- 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 431 nkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPCNHIKLVDVE 508
Cdd:COG0318 217 ----------LRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGRPLPGVEVRIVDED 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 509 --ELnywACKGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKI 586
Cdd:COG0318 287 grEL---PPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-DGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEV 361
|
490 500 510
....*....|....*....|....*....|....*....
gi 2230395409 587 ENIYIRSQPVAQIYV-------HGDSLKAFlvgiVVPDP 618
Cdd:COG0318 362 EEVLAAHPGVAEAAVvgvpdekWGERVVAF----VVLRP 396
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
146-684 |
2.37e-59 |
|
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: 210.39 E-value: 2.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 146 LSYQEVADRAEFLGSgllQHNCKACTD--QFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTV 223
Cdd:cd17632 68 ITYAELWERVGAVAA---AHDPEQPVRpgDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 224 IVDKPQKAV---LLLEHverketPGLKLIILMDPFEEALKER-----------GQKCGVVIKSMQAVEHFLLSGLWPRES 289
Cdd:cd17632 145 AVSAEHLDLaveAVLEG------GTPPRLVVFDHRPEVDAHRaalesarerlaAVGIPVTTLTLIAVRGRDLPPAPLFRP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 290 P-------------GSCGNPKGAMLTHgNVVADFsgFLKVTESQWAPTCADVHISYLPLAHMFERMVQSVVYCHGGrVGF 356
Cdd:cd17632 219 EpdddplalliytsGSTGTPKGAMYTE-RLVATF--WLKVSSIQDIRPPASITLNFMPMSHIAGRISLYGTLARGG-TAY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 357 FQG--DIRLLSDDMKALCPTIFPVVPRLlnrmYDKIFSQANTPLKRWL-----LEFAAKRKQAEVRsgiirndsiwdelf 429
Cdd:cd17632 295 FAAasDMSTLFDDLALVRPTELFLVPRV----CDMLFQRYQAELDRRSvagadAETLAERVKAELR-------------- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 430 fnkiQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTtpgdwtSGHVGAPlPCNHIKLVDVEE 509
Cdd:cd17632 357 ----ERVLGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE--AGAVIL------DGVIVRP-PVLDYKLVDVPE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 510 LNYWACKG---EGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKI 586
Cdd:cd17632 424 LGYFRTDRphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARL 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 587 ENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMpswaqkrgiegtyaDLCTNKDLKKAILEDMVRLGKESGLHSFEQV 666
Cdd:cd17632 504 EAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDAL--------------AGEDTARLRAALAESLQRIAREAGLQSYEIP 569
|
570
....*....|....*...
gi 2230395409 667 KAIHIHSDMFSVQNGLLT 684
Cdd:cd17632 570 RDFLIETEPFTIANGLLS 587
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
143-657 |
2.86e-56 |
|
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: 201.50 E-value: 2.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 143 YQWLSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADIST 222
Cdd:cd17641 9 WQEFTWADYADRVRAFALGLLALGVG--RGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 223 VIVDKPQKAVLLLEHveRKETPGLKLIILMDP------------FEEALKERGQKC-----GVVIKSMQAVEHFLLSGLW 285
Cdd:cd17641 87 VIAEDEEQVDKLLEI--ADRIPSVRYVIYCDPrgmrkyddprliSFEDVVALGRALdrrdpGLYEREVAAGKGEDVAVLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 286 PreSPGSCGNPKGAMLTHGNVVADFSGFLKVTESqwAPTcaDVHISYLPLAHMFERM---VQSVVycHGGRVGFFQgDIR 362
Cdd:cd17641 165 T--TSGTTGKPKLAMLSHGNFLGHCAAYLAADPL--GPG--DEYVSVLPLPWIGEQMysvGQALV--CGFIVNFPE-EPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 363 LLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWL--------LEFAAKRKQAEVRSGIIRNDS-IWDELFFN 431
Cdd:cd17641 236 TMMEDLREIGPTFVLLPPRVWEGIAADVRArmMDATPFKRFMfelgmklgLRALDRGKRGRPVSLWLRLASwLADALLFR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 432 KIQASLG-GCVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTEcTAGCTFTTP-GDWTSGHVGAPLPCNHIKLVDVee 509
Cdd:cd17641 316 PLRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTE-LAGAYTVHRdGDVDPDTVGVPFPGTEVRIDEV-- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 510 lnywackgeGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENI 589
Cdd:cd17641 392 ---------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENK 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2230395409 590 YIRSQPVAQIYVHGDSlKAFLVGIVVPDPEVMPSWAQKRGIE-GTYADLCTNKDLKKAILEDMVRLGKE 657
Cdd:cd17641 463 LKFSPYIAEAVVLGAG-RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKVNAS 530
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
146-691 |
9.96e-56 |
|
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: 197.28 E-value: 9.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 146 LSYQEVADRAEFLgSGLLQHNCKACTDQfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd05914 8 LTYKDLADNIAKF-ALLLKINGVGTGDR-VALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 226 DKPQKAVLLLEhverketpglkliilmdpfeealkergqkcgvviksmqavehfllsglwpreSPGSCGNPKGAMLTHGN 305
Cdd:cd05914 86 SDEDDVALINY----------------------------------------------------TSGTTGNSKGVMLTYRN 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 306 VVADFSG---FLKVTESqwaptcaDVHISYLPLAHMFERMVQSVVYCHGGRVGFFQGDI---RLLSDDMKALCPTIfpVV 379
Cdd:cd05914 114 IVSNVDGvkeVVLLGKG-------DKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIpsaKIIALAFAQVTPTL--GV 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 380 PRLLNRMYDKIFSQANTPLKRWLLEFAAKrkqaevrsgIIRNDSIWdELFFNKIQASLGGCVRMIVTGAAPASPTVLGFL 459
Cdd:cd05914 185 PVPLVIEKIFKMDIIPKLTLKKFKFKLAK---------KINNRKIR-KLAFKKVHEAFGGNIKEFVIGGAKINPDVEEFL 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 460 RAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPlpcnhIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRT 539
Cdd:cd05914 255 RT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKV-----IDGVEVRIDSPDPATGEGEIIVRGPNVMKGYYKNPEAT 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 540 KEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVA--QIYVHGDSLKAflvgIVVPD 617
Cdd:cd05914 329 AEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLesLVVVQEKKLVA----LAYID 404
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2230395409 618 PEVMPSWAQKrgiegtyadlctNKDLKKAILEDmVRLGKESGLHSFEQVKAIHIHSDMFSVqngllTPTLKAKR 691
Cdd:cd05914 405 PDFLDVKALK------------QRNIIDAIKWE-VRDKVNQKVPNYKKISKVKIVKEEFEK-----TPKGKIKR 460
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
291-619 |
3.66e-49 |
|
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: 175.55 E-value: 3.66e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 291 GSCGNPKGAMLTHGNVVADFSGFLKVtesqWAPTCADVHISYLPLAHMFerMVQSVVYC--HGGRVGFFQG-DIRLLSDD 367
Cdd:cd04433 10 GTTGKPKGVVLSHRNLLAAAAALAAS----GGLTEGDVFLSTLPLFHIG--GLFGLLGAllAGGTVVLLPKfDPEAALEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 368 MKALCPTIFPVVPRLLNRMydkifsqantplkrwllefaakRKQAEVRSgiiRNDSiwdelffnkiqaslggCVRMIVTG 447
Cdd:cd04433 84 IEREKVTILLGVPTLLARL----------------------LKAPESAG---YDLS----------------SLRALVSG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 448 AAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT--SGHVGAPLPCNHIKLVDVEElNYWACKGEGEICVRG 525
Cdd:cd04433 123 GAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDPDG-GELPPGEIGELVVRG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 526 PNVFKGYLKDPDRTkEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYVHGds 605
Cdd:cd04433 202 PSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPGVAEAAVVG-- 277
|
330
....*....|....
gi 2230395409 606 lkaflvgivVPDPE 619
Cdd:cd04433 278 ---------VPDPE 282
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
118-611 |
3.88e-49 |
|
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: 179.30 E-value: 3.88e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 118 YQVFRRGLSISGNGPCLGFRKpkqpyQWLSYQEVADRAEFLGSGLLQHNCKaCTDQfIGVFAQNRPEWIIVELACYTYSM 197
Cdd:cd05936 2 ADLLEEAARRFPDKTALIFMG-----RKLTYRELDALAEAFAAGLQNLGVQ-PGDR-VALMLPNCPQFPIAYFGALKAGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 198 VVVPLYDTLGPGAIRYIINTADISTVIVDkpqkavlllehverketpglkliilmDPFEEALKERGQKCGVVIKSMQAVE 277
Cdd:cd05936 75 VVVPLNPLYTPRELEHILNDSGAKALIVA--------------------------VSFTDLLAAGAPLGERVALTPEDVA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 278 HFLLSGlwprespGSCGNPKGAMLTHGNVVADFSGFLKVTESQWAPTcaDVHISYLPLAHMFErmvQSVVYCHGGRVGFF 357
Cdd:cd05936 129 VLQYTS-------GTTGVPKGAMLTHRNLVANALQIKAWLEDLLEGD--DVVLAALPLFHVFG---LTVALLLPLALGAT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 358 Q------GDIRLLsDDMKALCPTIFPVVPRLLNRmydkifsqantplkrwLLEFAAKRKqaEVRSGIirndsiwdelffn 431
Cdd:cd05936 197 IvliprfRPIGVL-KEIRKHRVTIFPGVPTMYIA----------------LLNAPEFKK--RDFSSL------------- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 432 kiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT-SGHVGAPLPCNHIKLVDvEEL 510
Cdd:cd05936 245 ----------RLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRkPGSIGIPLPGTEVKIVD-DDG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 511 NYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIY 590
Cdd:cd05936 314 EELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGGFNVYPREVEEVL 391
|
490 500
....*....|....*....|....*...
gi 2230395409 591 IRSQPVAQIYV-------HGDSLKAFLV 611
Cdd:cd05936 392 YEHPAVAEAAVvgvpdpySGEAVKAFVV 419
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
146-628 |
2.63e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 175.09 E-value: 2.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 146 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGK-GDR-VAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 226 -------DKPQKAVL-LLEHVERKETP-GLKLIILMDPFEEALK--ERGQKCGVVIKSMQAVEHFllsglwpreSPGSCG 294
Cdd:PRK07656 109 lglflgvDYSATTRLpALEHVVICETEeDDPHTEKMKTFTDFLAagDPAERAPEVDPDDVADILF---------TSGTTG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 295 NPKGAMLTHGNV---VADFSGFLKVTESqwaptcaDVHISYLPLAHMFERMVqSVVYC--HGGRVgffqgdIRLLS---D 366
Cdd:PRK07656 180 RPKGAMLTHRQLlsnAADWAEYLGLTEG-------DRYLAANPFFHVFGYKA-GVNAPlmRGATI------LPLPVfdpD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 367 DMKALC----PTIFPVVPRLLNRMYDkifsqantplkrwllefAAKRKQAEVRSgiirndsiwdelffnkiqaslggcVR 442
Cdd:PRK07656 246 EVFRLIeterITVLPGPPTMYNSLLQ-----------------HPDRSAEDLSS------------------------LR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 443 MIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGCTFTTPGD---WTSGHVGAPLPCNHIKLVDveELNYWACKGE 518
Cdd:PRK07656 285 LAVTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIAGVENKIVN--ELGEEVPVGE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 519 -GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVA 597
Cdd:PRK07656 363 vGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IVGGFNVYPAEVEEVLYEHPAVA 441
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2230395409 598 QIYV-------HGDSLKAFLV---GIVVPDPEVMpSWAQKR 628
Cdd:PRK07656 442 EAAVigvpderLGEVGKAYVVlkpGAELTEEELI-AYCREH 481
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
146-611 |
4.84e-45 |
|
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: 168.16 E-value: 4.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 146 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLK--KGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 226 DKPQKAVLLLehVERKETPGLKlIILMDPFEEALKERGQ----KCGVVIKSMQAVEH-------FLLSglwpreSPGSCG 294
Cdd:cd05911 89 DPDGLEKVKE--AAKELGPKDK-IIVLDDKPDGVLSIEDllspTLGEEDEDLPPPLKdgkddtaAILY------SSGTTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 295 NPKGAMLTHGNVVADFS---GFLKVTESQwaptcADVHISYLPLAHMF--ERMVQSVVYchGGRV----GFFqgdirllS 365
Cdd:cd05911 160 LPKGVCLSHRNLIANLSqvqTFLYGNDGS-----NDVILGFLPLYHIYglFTTLASLLN--GATViimpKFD-------S 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 366 DDMKALCP----TIFPVVPRLLNRMydkifsqANTPLkrwllefaakrkqaevrsgiirndsiwdelfFNKIQASlggCV 441
Cdd:cd05911 226 ELFLDLIEkykiTFLYLVPPIAAAL-------AKSPL-------------------------------LDKYDLS---SL 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 442 RMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGE 520
Cdd:cd05911 265 RVILSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 521 ICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIyIRSQP----- 595
Cdd:cd05911 345 ICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAV-LLEHPgvada 422
|
490
....*....|....*....
gi 2230395409 596 -VAQIY--VHGDSLKAFLV 611
Cdd:cd05911 423 aVIGIPdeVSGELPRAYVV 441
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
241-707 |
3.63e-37 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 148.71 E-value: 3.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 241 KETPGLKLIILMDPFE---------EALKERGQKCGVVI--------------KSMQAVEHFLLSGLWpreSPGSCGNPK 297
Cdd:PTZ00342 244 NDLSNELEDISLGPLEydkeklekiKDLKEKAKKLGISIilfddmtknkttnyKIQNEDPDFITSIVY---TSGTSGKPK 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 298 GAMLTHGNV------VADFSGFLKvtesqWAPtcaDVHISYLPLAHMFERMVQSVVYCHGGRVGFFQGDIRLLSDDMKAL 371
Cdd:PTZ00342 321 GVMLSNKNLyntvvpLCKHSIFKK-----YNP---KTHLSYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNS 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 372 CPTIFPVVPRLLNRMYDKIFSQAN--TPLKRWLlefaAKRKQAEVRSGIIRNDSIWDELFFN---KIQASLGGCVRMIVT 446
Cdd:PTZ00342 393 KGNILAGVPKVFNRIYTNIMTEINnlPPLKRFL----VKKILSLRKSNNNGGFSKFLEGITHissKIKDKVNPNLEVILN 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 447 GAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPG-DWTSGHVGAPL-PCNHIKLVDVEELNYWACKGEGEICVR 524
Cdd:PTZ00342 469 GGGKLSPKIAEELSVLLNVNYYQGYGLTE-TTGPIFVQHAdDNNTESIGGPIsPNTKYKVRTWETYKATDTLPKGELLIK 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 525 GPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHG- 603
Cdd:PTZ00342 548 SDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGd 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 604 DSLKAFLvGIVVPDPEVM------PSWAQKRGI-EGTYADLCTNKDLKKAILEDMVR-----LGKESGLHSFEQVKAIHI 671
Cdd:PTZ00342 628 DSMDGPL-AIISVDKYLLfkclkdDNMLESTGInEKNYLEKLTDETINNNIYVDYVKgkmleVYKKTNLNRYNIINDIYL 706
|
490 500 510
....*....|....*....|....*....|....*....
gi 2230395409 672 HSDMFSVQNgLLTPTLKAKRPEL-REY--FKKQIEELYS 707
Cdd:PTZ00342 707 TSKVWDTNN-YLTPTFKVKRFYVfKDYafFIDQVKKIYK 744
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
111-618 |
4.77e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 145.71 E-value: 4.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 111 YDDARTMYQVFRRGLSISGNGPCLGFRKPKqpyqwLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVEL 190
Cdd:PRK06187 2 QDYPLTIGRILRHGARKHPDKEAVYFDGRR-----TTYAELDERVNRLANALRALGVKK--GDRVAVFDWNSHEYLEAYF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 191 ACytySM---VVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlLLEHVE--RKETPGLKLIILMDP----------- 254
Cdd:PRK06187 75 AV---PKigaVLHPINIRLKPEEIAYILNDAEDRVVLVDSE-----FVPLLAaiLPQLPTVRTVIVEGDgpaaplapevg 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 255 -FEEALKER-GQKCGVVIKSMQAVEHFLLSGlwprespgSCGNPKGAMLTHGNVvadFSGFLKVTES-QWapTCADVHIS 331
Cdd:PRK06187 147 eYEELLAAAsDTFDFPDIDENDAAAMLYTSG--------TTGHPKGVVLSHRNL---FLHSLAVCAWlKL--SRDDVYLV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 332 YLPLAHMFERMVqsvvychgGRVGFFQG---------DIRLLSDDMKALCPTIFPVVPRLLNRMydkifSQANTPLKRWL 402
Cdd:PRK06187 214 IVPMFHVHAWGL--------PYLALMAGakqviprrfDPENLLDLIETERVTFFFAVPTIWQML-----LKAPRAYFVDF 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 403 lefaakrkqaevrSGIirndsiwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF 482
Cdd:PRK06187 281 -------------SSL-----------------------RLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSV 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 483 TTPGDWTSGH------VGAPLPCNHIKLVDvEELNYWACKGE--GEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDI 554
Cdd:PRK06187 325 LPPEDQLPGQwtkrrsAGRPLPGVEARIVD-DDGDELPPDGGevGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDV 402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2230395409 555 GKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDP 618
Cdd:PRK06187 403 GYIDEDGYLYITDRIKDVIISG-GENIYPRELEDA---------LYGHPAVAEVAVIG--VPDE 454
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
146-622 |
3.47e-35 |
|
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: 138.96 E-value: 3.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 146 LSYQEVADRAEFLgSGLLQHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADIStviv 225
Cdd:cd05941 12 ITYADLVARAARL-ANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPS---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 226 dkpqkavlllehverketpglkliILMDPfeeALkergqkcgVVIKSmqavehfllsglwprespGSCGNPKGAMLTHGN 305
Cdd:cd05941 87 ------------------------LVLDP---AL--------ILYTS------------------GTTGRPKGVVLTHAN 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 306 VVADfsgfLKVTESQWAPTCADVHISYLPLAHmfermVQSVV-------YChGGRV---GFFQGDIRLLSDDMKALcpTI 375
Cdd:cd05941 114 LAAN----VRALVDAWRWTEDDVLLHVLPLHH-----VHGLVnallcplFA-GASVeflPKFDPKEVAISRLMPSI--TV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 376 FPVVPRllnrMYDKIFS--QANTPLKRWLLEFAAKRkqaevrsgiirndsiwdelffnkiqaslggcVRMIVTGAAPASP 453
Cdd:cd05941 182 FMGVPT----IYTRLLQyyEAHFTDPQFARAAAAER-------------------------------LRLMVSGSAALPV 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 454 TVLGFLRAALGCQVYEGYGQTEctAGCTFTTP--GDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKG 531
Cdd:cd05941 227 PTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKE 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 532 YLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKK-HIFKlAQGEYVAPEKIENIyIRSQP-VAQIYVHGDSLKAF 609
Cdd:cd05941 305 YWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEIERV-LLAHPgVSECAVIGVPDPDW 382
|
490
....*....|....*.
gi 2230395409 610 ---LVGIVVPDPEVMP 622
Cdd:cd05941 383 gerVVAVVVLRAGAAA 398
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
289-589 |
1.01e-32 |
|
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: 132.74 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 289 SPGSCGNPKGAMLTHGNVVADFSGFLKVTESQWAPTcaDVHISYLPLAHMFermvqsvvychgGRVGFFQGDIRL----- 363
Cdd:cd05904 166 SSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSE--DVFLCVLPMFHIY------------GLSSFALGLLRLgatvv 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 364 ------LSDDMKALCP---TIFPVVPrllnrmydkifsqantPLkrwlleFAAKRKQAEVRSGIIRndsiwdelffnkiq 434
Cdd:cd05904 232 vmprfdLEELLAAIERykvTHLPVVP----------------PI------VLALVKSPIVDKYDLS-------------- 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 435 aSLggcvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFTTP---GDWTSGHVGAPLPCNHIKLVDVEEL 510
Cdd:cd05904 276 -SL----RQIMSGAAPLGKELIeAFRAKFPNVDLGQGYGMTESTGVVAMCFApekDRAKYGSVGRLVPNVEAKIVDPETG 350
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2230395409 511 NYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENI 589
Cdd:cd05904 351 ESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEAL 428
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
121-618 |
1.12e-32 |
|
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: 131.58 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 121 FRRGLSISGNGPCLGFRKpkqpyQWLSYQEVADRAEFLGSGLlQHNCKACTDQfIGVFAQNRPEWIIVELACYTYSMVVV 200
Cdd:cd17631 1 LRRRARRHPDRTALVFGG-----RSLTYAELDERVNRLAHAL-RALGVAKGDR-VAVLSKNSPEFLELLFAAARLGAVFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 201 PLYDTLGPGAIRYIINTADiSTVIVDKPqkavlllehverketpglklIILMdpfeealkergqkcgvviksmqavehfl 280
Cdd:cd17631 74 PLNFRLTPPEVAYILADSG-AKVLFDDL--------------------ALLM---------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 281 lsglwprESPGSCGNPKGAMLTHGNVVADFSGFLkvteSQWAPTCADVHISYLPLAHMFE-RMVQSVVYCHGGRV----G 355
Cdd:cd17631 105 -------YTSGTTGRPKGAMLTHRNLLWNAVNAL----AALDLGPDDVLLVVAPLFHIGGlGVFTLPTLLRGGTVvilrK 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 356 FFQGDIRLLSDDMKAlcpTIFPVVPRLLNRMydkifsqANTPLkrwllefaakrkqaevrsgiirndsiWDELFFnkiqA 435
Cdd:cd17631 174 FDPETVLDLIERHRV---TSFFLVPTMIQAL-------LQHPR--------------------------FATTDL----S 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 436 SLggcvRMIVTGAAPASPTVLGFLRAAlGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPCNHIKLVDvEELNYW 513
Cdd:cd17631 214 SL----RAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHRRklGSAGRPVFFVEVRIVD-PDGREV 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 514 ACKGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENIyirs 593
Cdd:cd17631 288 PPGEVGEIVVRGPHVMAGYWNRPEATAAAFR-DGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDV---- 361
|
490 500
....*....|....*....|....*
gi 2230395409 594 qpvaqIYVHGDSLKAFLVGivVPDP 618
Cdd:cd17631 362 -----LYEHPAVAEVAVIG--VPDE 379
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
146-589 |
4.74e-32 |
|
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: 130.53 E-value: 4.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 146 LSYQEVADRAEFLGSgLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd05909 8 LTYRKLLTGAIALAR-KLAKMTKE--GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 226 DKPQKAVLLLEHVERKETPgLKLIILmdpfeEALKER---GQKCGVVIKSMQAVEHFLL-SGLWPRE---------SPGS 292
Cdd:cd05909 85 SKQFIEKLKLHHLFDVEYD-ARIVYL-----EDLRAKiskADKCKAFLAGKFPPKWLLRiFGVAPVQpddpavilfTSGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 293 CGNPKGAMLTHGNVVADFSGFLKVTEsqwaPTCADVHISYLPLAHMFermvqsvvychggrvGFFQGDIRLLSDDMKALC 372
Cdd:cd05909 159 EGLPKGVVLSHKNLLANVEQITAIFD----PNPEDVVFGALPFFHSF---------------GLTGCLWLPLLSGIKVVF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 373 ---PTIFPVVPRLLnrmYDK----IFSqanTPLkrwLLEFAAKRKQAEVRSGIirndsiwdelffnkiqaslggcvRMIV 445
Cdd:cd05909 220 hpnPLDYKKIPELI---YDKkatiLLG---TPT---FLRGYARAAHPEDFSSL-----------------------RLVV 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 446 TGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVR 524
Cdd:cd05909 268 AGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVR 347
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2230395409 525 GPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENI 589
Cdd:cd05909 348 GPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDI 410
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
114-707 |
4.57e-30 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 127.66 E-value: 4.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 114 ARTMYQVFRRGLSISGNGPCLGFRKPKQPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACY 193
Cdd:PTZ00297 426 VRSLGEMWERSVTRHSTFRCLGQTSESGESEWLTYGTVDARARELGSGLLALGVRP--GDVIGVDCEASRNIVILEVACA 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 194 TYSMVVVPLydtLGPG-AIRYIINTADISTVIVDKPQKAVLL------LEHV--------ERKETPGLKLIILMDPFEEa 258
Cdd:PTZ00297 504 LYGFTTLPL---VGKGsTMRTLIDEHKIKVVFADRNSVAAILtcrsrkLETVvythsfydEDDHAVARDLNITLIPYEF- 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 259 LKERGQKCGVVIKSMQAVEHFLLSGLWPRESpGSCGNPKGAMLTHGNVVADFSGFLKvteSQWAPTCADVH--ISYLPLA 336
Cdd:PTZ00297 580 VEQKGRLCPVPLKEHVTTDTVFTYVVDNTTS-ASGDGLAVVRVTHADVLRDISTLVM---TGVLPSSFKKHlmVHFTPFA 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 337 HMFERMVQSVVYCHGGRVGffQGDIRLLSDDMKALCPTIFPVVPRLlnrmydkiFSQANTPLKR----------WLLEfa 406
Cdd:PTZ00297 656 MLFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSL--------FSTSRLQLSRanerysavysWLFE-- 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 407 akrKQAEVRSGII----RNDSIWDELFFNKIQASLGGCVRMIVTGAAPASPTV-----LGFLRAALGCQVYegygQTECT 477
Cdd:PTZ00297 724 ---RAFQLRSRLInihrRDSSLLRFIFFRATQELLGGCVEKIVLCVSEESTSFsllehISVCYVPCLREVF----FLPSE 796
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 478 AGCTFTtpgdwtsghvGAPLPCNHIKLVDVEELNYWACKGEGEICVRGpnvfkgylkDPDRTKEAldsdgwlhtgdIGKW 557
Cdd:PTZ00297 797 GVFCVD----------GTPAPSLQVDLEPFDEPSDGAGIGQLVLAKKG---------EPRRTLPI-----------AAQW 846
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 558 LPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAfLVGIVVPDPEVMP-SWAQKRGIE--GTY 634
Cdd:PTZ00297 847 KRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEfEWRQSHCMGegGGP 925
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2230395409 635 ADLCTNKDLKK----AILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 707
Cdd:PTZ00297 926 ARQLGWTELVAyassLLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIERFYS 1002
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
441-612 |
2.61e-28 |
|
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: 116.45 E-value: 2.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 441 VRMIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGcTFTTPGD---WTSGHVGAPLPCNHIKLVDveelnywack 516
Cdd:cd17638 117 LRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVA-TMCRPGDdaeTVATTCGRACPGFEVRIAD---------- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 517 gEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPV 596
Cdd:cd17638 186 -DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGALAEHPGV 263
|
170 180
....*....|....*....|...
gi 2230395409 597 AQIYV-------HGDSLKAFLVG 612
Cdd:cd17638 264 AQVAVigvpderMGEVGKAFVVA 286
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
291-611 |
4.34e-28 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 119.39 E-value: 4.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 291 GSCGNPKGAMLTHGNVVADfsgflkVTESQWA--PTCADVH---ISYLPLAHMFERMVQSVVYCHGGrvgffqGDIRLLS 365
Cdd:PRK08974 216 GTTGVAKGAMLTHRNMLAN------LEQAKAAygPLLHPGKelvVTALPLYHIFALTVNCLLFIELG------GQNLLIT 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 366 DdmkalcPTIFPVVPRLLNRMYDKIFSQANTPLKRWLlefaakrkqaevrsgiirNDSIWDELFFNKIQASLGGcvrmiv 445
Cdd:PRK08974 284 N------PRDIPGFVKELKKYPFTAITGVNTLFNALL------------------NNEEFQELDFSSLKLSVGG------ 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 446 tgAAPASPTVLGFLRAALGCQVYEGYGQTECT---AGCTFTTPGdwTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEIC 522
Cdd:PRK08974 334 --GMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVNPYDLDY--YSGSIGLPVPSTEIKLVD-DDGNEVPPGEPGELW 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 523 VRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIY-- 600
Cdd:PRK08974 409 VKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMI-LVSGFNVYPNEIEDVVMLHPKVLEVAav 486
|
330
....*....|....*.
gi 2230395409 601 -----VHGDSLKAFLV 611
Cdd:PRK08974 487 gvpseVSGEAVKIFVV 502
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
291-617 |
1.57e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 117.79 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 291 GSCGNPKGAMLTHGNVVADfsgflkVTESQ-WAPTCAD---VHISYLPLAHMFE-RMVQSV-VYCHGGRVGFFQGDIRLL 364
Cdd:PRK05605 229 GTTGKPKGAQLTHRNLFAN------AAQGKaWVPGLGDgpeRVLAALPMFHAYGlTLCLTLaVSIGGELVLLPAPDIDLI 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 365 SDDMKALCPTIFPVVPRLlnrmYDKIfsqantplkrwlLEFAAKRkqaevrsGIirndsiwdelffnkiqaSLGGcVRMI 444
Cdd:PRK05605 303 LDAMKKHPPTWLPGVPPL----YEKI------------AEAAEER-------GV-----------------DLSG-VRNA 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 445 VTGAAPASPTVLGFLRAALGCQVYEGYGQTECT---AGCTFTTpgDWTSGHVGAPLPCNHIKLVDVEELNYWACKGE-GE 520
Cdd:PRK05605 342 FSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpiiVGNPMSD--DRRPGYVGVPFPDTEVRIVDPEDPDETMPDGEeGE 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 521 ICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIyirsqpVAQiy 600
Cdd:PRK05605 420 LLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELI-ITGGFNVYPAEVEEV------LRE-- 489
|
330
....*....|....*..
gi 2230395409 601 vHGDSLKAFLVGIVVPD 617
Cdd:PRK05605 490 -HPGVEDAAVVGLPRED 505
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
291-611 |
2.35e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 117.17 E-value: 2.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 291 GSCGNPKGAMLTHGNVVADFSGFLKVTESQWAPTCaDVHISYLPLAHM----FERMVQSVVYCHGgrvgffqgdiRLLSD 366
Cdd:PRK05677 217 GTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEGC-EILIAPLPLYHIyaftFHCMAMMLIGNHN----------ILISN 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 367 dmkalcPTIFPVVPRLLNRMYDKIFSQANTPlkrwlleFAAkrkqaevrsgiIRNDSIWDELFFNKIQASLGGcvRMIVT 446
Cdd:PRK05677 286 ------PRDLPAMVKELGKWKFSGFVGLNTL-------FVA-----------LCNNEAFRKLDFSALKLTLSG--GMALQ 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 447 GAAPASptvlgfLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGP 526
Cdd:PRK05677 340 LATAER------WKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVID-DDGNELPLGEVGELCVKGP 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 527 NVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIyIRSQP----VAQIYV- 601
Cdd:PRK05677 413 QVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVSGFNVYPNELEDV-LAALPgvlqCAAIGVp 490
|
330
....*....|...
gi 2230395409 602 ---HGDSLKAFLV 611
Cdd:PRK05677 491 dekSGEAIKVFVV 503
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
291-618 |
3.57e-27 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 116.51 E-value: 3.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 291 GSCGNPKGAMLTHGNVVADFSgflkvTESQWAPTCA------DVHISYLPLAHMFERMVQSVVYCHGGrvgffqGDIRLL 364
Cdd:PRK08751 218 GTTGVAKGAMLTHRNLVANMQ-----QAHQWLAGTGkleegcEVVITALPLYHIFALTANGLVFMKIG------GCNHLI 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 365 SDdmkalcPTIFPVVPRLLNRMYDKIFSQANTPLKRWLlefaakrkqaevrsgiirNDSIWDELFFNKIQASLGGcvRMI 444
Cdd:PRK08751 287 SN------PRDMPGFVKELKKTRFTAFTGVNTLFNGLL------------------NTPGFDQIDFSSLKMTLGG--GMA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 445 VTGAapasptVLGFLRAALGCQVYEGYGQTECT-AGCTFTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICV 523
Cdd:PRK08751 341 VQRS------VAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDACIKD-DAGTVLAIGEIGELCI 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 524 RGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYVHG 603
Cdd:PRK08751 414 KGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-LVSGFNVYPNEIEDVIAMMPGVLEVAAVG 492
|
330
....*....|....*....
gi 2230395409 604 ----DSLKAFLVGIVVPDP 618
Cdd:PRK08751 493 vpdeKSGEIVKVVIVKKDP 511
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
175-656 |
4.73e-27 |
|
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: 114.85 E-value: 4.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 175 IGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlllehVERKETPGLKLIILMDP 254
Cdd:TIGR01923 27 VALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL---------LEEKDFQADSLDRIEAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 255 FEEALKergqkcgvviksmqavehflLSGLWPRESP-------GSCGNPKGAMLTHGNVVADFSGF---LKVTESqwapt 324
Cdd:TIGR01923 98 GRYETS--------------------LSASFNMDQIatlmftsGTTGKPKAVPHTFRNHYASAVGSkenLGFTED----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 325 caDVHISYLPLAHMFErmvQSVVY---CHGGRVGFFQGDIRLLsDDMKALCPTIFPVVPRLLNRMYDKifSQANTPLKRW 401
Cdd:TIGR01923 153 --DNWLLSLPLYHISG---LSILFrwlIEGATLRIVDKFNQLL-EMIANERVTHISLVPTQLNRLLDE--GGHNENLRKI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 402 LLefaakrkqaevrsgiirndsiwdelffnkiqaslGGcvrmivtGAAPASptvlgFLRAAL--GCQVYEGYGQTE-CTA 478
Cdd:TIGR01923 225 LL----------------------------------GG-------SAIPAP-----LIEEAQqyGLPIYLSYGMTEtCSQ 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 479 GCTFTTPGDWTSGHVGAPLPCNHIKL-VDVEElnywackGEGEICVRGPNVFKGYLkDPDRTKEALDSDGWLHTGDIGKW 557
Cdd:TIGR01923 259 VTTATPEMLHARPDVGRPLAGREIKIkVDNKE-------GHGEIMVKGANLMKGYL-YQGELTPAFEQQGWFNTGDIGEL 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 558 LPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQiyvhgdslkAFLVGivVPDPEvmpsWAQKrgiegTYADL 637
Cdd:TIGR01923 331 DGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQE---------AVVVP--KPDAE----WGQV-----PVAYI 389
|
490 500
....*....|....*....|.
gi 2230395409 638 CTNKDLKKAILEDMV--RLGK 656
Cdd:TIGR01923 390 VSESDISQAKLIAYLteKLAK 410
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
146-603 |
1.03e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 115.26 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVV---PLYDT------LGPGAIRYII- 215
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQP--GDRVGIWAPNCAEWLLTQFATARIGAILVninPAYRAseleyaLGQSGVRWVIc 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 216 ----NTADISTVIVD-KPQKAVLLLEHVERKETPGLKLIILMDPFE-------EALKERGQkcGVVIKSMQAVEHFLlsg 283
Cdd:PRK12583 124 adafKTSDYHAMLQElLPGLAEGQPGALACERLPELRGVVSLAPAPppgflawHELQARGE--TVSREALAERQASL--- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 284 lwPRESP-------GSCGNPKGAMLTHGNVV--ADFSG-FLKVTESqwaptcaDVHISYLPLAHMFErMVQSVVYC--HG 351
Cdd:PRK12583 199 --DRDDPiniqytsGTTGFPKGATLSHHNILnnGYFVAeSLGLTEH-------DRLCVPVPLYHCFG-MVLANLGCmtVG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 352 GRVGF----FQGDIRLLSDDMKAlCPTIFPVvPRLLnrmydkiFSQANTPlKRWLLEFAAkrkqaeVRSGIIrndsiwde 427
Cdd:PRK12583 269 ACLVYpneaFDPLATLQAVEEER-CTALYGV-PTMF-------IAELDHP-QRGNFDLSS------LRTGIM-------- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 428 lffnkiqaslggcvrmivtGAAPASPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGD-----WTSghVGAPLPCNH 501
Cdd:PRK12583 325 -------------------AGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSLQTTAADdlerrVET--VGRTQPHLE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 502 IKLVDVEELNywACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEY 580
Cdd:PRK12583 384 VKVVDPDGAT--VPRGEiGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMI-IRGGEN 460
|
490 500
....*....|....*....|...
gi 2230395409 581 VAPEKIENIYIRSQPVAQIYVHG 603
Cdd:PRK12583 461 IYPREIEEFLFTHPAVADVQVFG 483
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
147-619 |
1.88e-26 |
|
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: 114.16 E-value: 1.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 147 SYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLgpgAIRYIINTADIST-VIV 225
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLK--QNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIY---NERELDHSLNISKpTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 226 DKPQKAVLLLEHVERKeTPGLKLIILMDPFEEAlkeRGQKCGVVIKSMQAVEHFLLSGLWPRE------------SPGSC 293
Cdd:cd17642 121 FCSKKGLQKVLNVQKK-LKIIKTIIILDSKEDY---KGYQCLYTFITQNLPPGFNEYDFKPPSfdrdeqvalimnSSGST 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 294 GNPKGAMLTHGNVVADFSGFLKVT-ESQWAPTCAdvHISYLPLAHMFERMVQSVVYCHGGRVGF---FQGD--IRLLSD- 366
Cdd:cd17642 197 GLPKGVQLTHKNIVARFSHARDPIfGNQIIPDTA--ILTVIPFHHGFGMFTTLGYLICGFRVVLmykFEEElfLRSLQDy 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 367 --DMKALCPTIFPVVPR--LLNRmYD----KIFSQANTPLKRWLLEFAAKRkqaevrsgiirndsiwdelfFNkiqaslg 438
Cdd:cd17642 275 kvQSALLVPTLFAFFAKstLVDK-YDlsnlHEIASGGAPLSKEVGEAVAKR--------------------FK------- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 439 gcvrmivtgaapasptvLGFLRaalgcqvyEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKGE 518
Cdd:cd17642 327 -----------------LPGIR--------QGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNER 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 519 GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRsqpvaq 598
Cdd:cd17642 382 GELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQ------ 454
|
490 500
....*....|....*....|.
gi 2230395409 599 iyvHGDSLKAFLVGIvvPDPE 619
Cdd:cd17642 455 ---HPKIFDAGVAGI--PDED 470
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
144-619 |
2.16e-25 |
|
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: 109.30 E-value: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 144 QWlSYQEVADRAEFLGSGLLQHNCKACTdqFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTV 223
Cdd:cd05934 3 RW-TYAELLRESARIAAALAALGIRPGD--RVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 224 IVDkpqkavlllehverketpglkliilmdPFEealkergqkcgVVIKSmqavehfllsglwprespGSCGNPKGAMLTH 303
Cdd:cd05934 80 VVD---------------------------PAS-----------ILYTS------------------GTTGPPKGVVITH 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 304 GNVVadFSGflKVTESQWAPTCADVHISYLPLAHM---FERMVQSVVycHGGRV--------GFFQGDIRllsdDMKALC 372
Cdd:cd05934 104 ANLT--FAG--YYSARRFGLGEDDVYLTVLPLFHInaqAVSVLAALS--VGATLvllprfsaSRFWSDVR----RYGATV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 373 PTIFPVVPRLLnrmydkiFSQANTPlkrwllefaaKRKQAEVRsgiirndsiwdelffnkiqaslggcvrmiVTGAAPAS 452
Cdd:cd05934 174 TNYLGAMLSYL-------LAQPPSP----------DDRAHRLR-----------------------------AAYGAPNP 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 453 PTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEelNYWACKGE-GEICVR---GPNV 528
Cdd:cd05934 208 PELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDD--GQELPAGEpGELVIRglrGWGF 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 529 FKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYVHG----- 603
Cdd:cd05934 286 FKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVERAILRHPAVREAAVVAvpdev 363
|
490
....*....|....*...
gi 2230395409 604 --DSLKAFlvgIVVPDPE 619
Cdd:cd05934 364 geDEVKAV---VVLRPGE 378
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
291-603 |
3.68e-25 |
|
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: 107.36 E-value: 3.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 291 GSCGNPKGAMLTHGNVV--ADFSGF-LKVTESqwaptcaDVHISYLPLAHMFErMVQSVVYC--HGGRVGFFQgdirlLS 365
Cdd:cd05917 12 GTTGSPKGATLTHHNIVnnGYFIGErLGLTEQ-------DRLCIPVPLFHCFG-SVLGVLACltHGATMVFPS-----PS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 366 DDMKAL--------C------PTIFPvvpRLLNRMydkifSQANTPLKRwllefaakrkqaeVRSGIIrndsiwdelffn 431
Cdd:cd05917 79 FDPLAVleaiekekCtalhgvPTMFI---AELEHP-----DFDKFDLSS-------------LRTGIM------------ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 432 kiqaslggcvrmivtGAAPASPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGDWTS---GHVGAPLPCNHIKLVDv 507
Cdd:cd05917 126 ---------------AGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDSIEkrvNTVGRIMPHTEAKIVD- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 508 EELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKI 586
Cdd:cd05917 190 PEGGIVPPVGVpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGENIYPREI 268
|
330
....*....|....*..
gi 2230395409 587 ENIYIRSQPVAQIYVHG 603
Cdd:cd05917 269 EEFLHTHPKVSDVQVVG 285
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
291-620 |
4.48e-25 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 110.11 E-value: 4.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 291 GSCGNPKGAMLTHGNVVADF--------SGFLKVTE-SQWAPTCAdvhisyLPLAHMFERMVQSVVYCHGGRVGFF---Q 358
Cdd:PRK07059 214 GTTGVSKGATLLHRNIVANVlqmeawlqPAFEKKPRpDQLNFVCA------LPLYHIFALTVCGLLGMRTGGRNILipnP 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 359 GDIRLLSDDMKALCPTIFPVVPRLLNRMYdkifsqaNTPlkrwllEFaakrkqaevrsgiirndsiwDELFFNKIQASLG 438
Cdd:PRK07059 288 RDIPGFIKELKKYQVHIFPAVNTLYNALL-------NNP------DF--------------------DKLDFSKLIVANG 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 439 GcvrmivtGAAPASPTVLGFLRAAlGCQVYEGYG--QTECTAGCTFTTPGDWTsGHVGAPLPCNHIKLVDvEELNYWACK 516
Cdd:PRK07059 335 G-------GMAVQRPVAERWLEMT-GCPITEGYGlsETSPVATCNPVDATEFS-GTIGLPLPSTEVSIRD-DDGNDLPLG 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 517 GEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIyIRSQP- 595
Cdd:PRK07059 405 EPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMI-LVSGFNVYPNEIEEV-VASHPg 482
|
330 340 350
....*....|....*....|....*....|..
gi 2230395409 596 ---VAQIYVH----GDSLKAFlvgIVVPDPEV 620
Cdd:PRK07059 483 vleVAAVGVPdehsGEAVKLF---VVKKDPAL 511
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
289-626 |
5.35e-25 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 109.93 E-value: 5.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 289 SPGSCGNPKGAMLTHGNVVADFSGFLKVTESQWA-PTCADVHISYLPLAHMFermvqsvvychgGRVGFFQGDIRL---- 363
Cdd:PLN02574 206 SSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEyPGSDNVYLAALPMFHIY------------GLSLFVVGLLSLgsti 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 364 -------LSDDMKAL---CPTIFPVVPRLLNRMYDKIFSQANTPLKrwllefaakrkqaevrsgiirndsiwdelffnki 433
Cdd:PLN02574 274 vvmrrfdASDMVKVIdrfKVTHFPVVPPILMALTKKAKGVCGEVLK---------------------------------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 434 qaslggCVRMIVTGAAPAS-PTVLGFLRAALGCQVYEGYGQTECTAGCT--FTTPGDWTSGHVGAPLPCNHIKLVDVEEL 510
Cdd:PLN02574 320 ------SLKQVSCGAAPLSgKFIQDFVQTLPHVDFIQGYGMTESTAVGTrgFNTEKLSKYSSVGLLAPNMQAKVVDWSTG 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 511 NYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIY 590
Cdd:PLN02574 394 CLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQIAPADLEAVL 472
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2230395409 591 IrSQP----VAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQ 626
Cdd:PLN02574 473 I-SHPeiidAAVTAVPDKECGEIPVAFVVRRQGSTLSQEA 511
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
145-696 |
1.19e-24 |
|
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: 108.17 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 145 WLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVI 224
Cdd:cd05926 14 ALTYADLAELVDDLARQLAALGIKK--GDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 225 VDKpqkaVLLLEHVERKETPGLkliilmdpfeeALKERGQKCGVVIKSMQAVE----HFLLSGLWPRESP---------- 290
Cdd:cd05926 92 TPK----GELGPASRAASKLGL-----------AILELALDVGVLIRAPSAESlsnlLADKKNAKSEGVPlpddlalilh 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 291 --GSCGNPKGAMLTHGNVVADFSGFLKVtesqWAPTCADVHISYLPLAHMFERMVQ--SVVYChGGRV----GFfqgDIR 362
Cdd:cd05926 157 tsGTTGRPKGVPLTHRNLAASATNITNT----YKLTPDDRTLVVMPLFHVHGLVASllSTLAA-GGSVvlppRF---SAS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 363 LLSDDMKALCPTIFPVVPRLLnrmydKIfsqantplkrwLLEFAAKRKQAEvrsgiirndsiwdelfFNKIqaslggcvR 442
Cdd:cd05926 229 TFWPDVRDYNATWYTAVPTIH-----QI-----------LLNRPEPNPESP----------------PPKL--------R 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 443 MIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTP---GDWTSGHVGAPlpcNHIKLVDVEElnywacKGE- 518
Cdd:cd05926 269 FIRSCSASLPPAVLEALEATFGAPVLEAYGMTE-AAHQMTSNPlppGPRKPGSVGKP---VGVEVRILDE------DGEi 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 519 ------GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIR 592
Cdd:cd05926 339 lppgvvGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVLLS 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 593 SQPVAQIYVHGdslkaflvgivVPDP---EVMPSWAQKRgiEGTYADlctnkdlKKAILEDMvrlgkESGLHSFEQVKAI 669
Cdd:cd05926 418 HPAVLEAVAFG-----------VPDEkygEEVAAAVVLR--EGASVT-------EEELRAFC-----RKHLAAFKVPKKV 472
|
570 580
....*....|....*....|....*..
gi 2230395409 670 HIhsdmfsVQNGLLTPTLKAKRPELRE 696
Cdd:cd05926 473 YF------VDELPKTATGKIQRRKVAE 493
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
146-626 |
1.40e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 108.15 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 146 LSYQEVADRAE-----FLGSGLLQHNCkactdqfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADI 220
Cdd:PRK06188 38 LTYGQLADRISryiqaFEALGLGTGDA-------VALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 221 STVIVDK---PQKAVLLLEHVerketPGLKLIILMDPFEEalkerGQKCGVVIKSMQAVEhfLLSGLWPRE------SPG 291
Cdd:PRK06188 111 STLIVDPapfVERALALLARV-----PSLKHVLTLGPVPD-----GVDLLAAAAKFGPAP--LVAAALPPDiaglayTGG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 292 SCGNPKGAMLTHGNVVADFSGFLkvTESQWAPtcadvHISYL---PLAHMFERMVQSVVYchggRVGFFqgdIRLLSDDM 368
Cdd:PRK06188 179 TTGKPKGVMGTHRSIATMAQIQL--AEWEWPA-----DPRFLmctPLSHAGGAFFLPTLL----RGGTV---IVLAKFDP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 369 KALCPTI--------FpVVPRLLNRmydkifsqantplkrwLLEFAAKRKqaevrsgiiRNDSiwdelffnkiqaSLggc 440
Cdd:PRK06188 245 AEVLRAIeeqritatF-LVPTMIYA----------------LLDHPDLRT---------RDLS------------SL--- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 441 vRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHV------GAPLPCNHIKLVDvEELNYWA 514
Cdd:PRK06188 284 -ETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLRVALLD-EDGREVA 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 515 cKGE-GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRS 593
Cdd:PRK06188 362 -QGEvGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMI-VTGGFNVFPREVEDVLAEH 438
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2230395409 594 QPVAQIYV-------HGDSLKAflvgIVVPDPEVMPSWAQ 626
Cdd:PRK06188 439 PAVAQVAVigvpdekWGEAVTA----VVVLRPGAAVDAAE 474
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
175-619 |
1.90e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 107.59 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 175 IGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADiSTVIV--DKPQKAVLLLEHVERketpglkLIILM 252
Cdd:PRK09088 50 LAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAE-PRLLLgdDAVAAGRTDVEDLAA-------FIASA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 253 DPFEEALKERGqkcgvviksmqavehfllsglwPRESP-------GSCGNPKGAMLTHGN---VVADFSGFLKVtesqwa 322
Cdd:PRK09088 122 DALEPADTPSI----------------------PPERVslilftsGTSGQPKGVMLSERNlqqTAHNFGVLGRV------ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 323 ptcaDVHISYLPLAHMFE--RMVQSV--VYCHGGRV----GFFQG-DIRLLSDdmKALCPTIFPVVPRLLNRmydkifsq 393
Cdd:PRK09088 174 ----DAHSSFLCDAPMFHiiGLITSVrpVLAVGGSIlvsnGFEPKrTLGRLGD--PALGITHYFCVPQMAQA-------- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 394 antplkrwllefaakrkqaevrsgiIRNDSIWDELFFNKIQAslggcvrmIVTGAAP-ASPTVLGFLraALGCQVYEGYG 472
Cdd:PRK09088 240 -------------------------FRAQPGFDAAALRHLTA--------LFTGGAPhAAEDILGWL--DDGIPMVDGFG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 473 QTEctAGCTFTTPGDWT-----SGHVGAPLPCNHIKLVDVEELNYWAckGE-GEICVRGPNVFKGYLKDPDRTKEALDSD 546
Cdd:PRK09088 285 MSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVVDDQGNDCPA--GVpGELLLRGPNLSPGYWRRPQATARAFTGD 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2230395409 547 GWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIEniyirsqpvAQIYVHGDSLKAFLVGivVPDPE 619
Cdd:PRK09088 361 GWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIE---------AVLADHPGIRECAVVG--MADAQ 421
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
146-628 |
3.31e-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: 106.02 E-value: 3.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 146 LSYQEVADRAEFLGSGLlqHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd05935 2 LTYLELLEVVKKLASFL--SNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 226 DKPQKAVLLLehverketpglkliilmdPFeealkergqkcgvviksmqavehfllsglwpreSPGSCGNPKGAMLTHGN 305
Cdd:cd05935 80 GSELDDLALI------------------PY---------------------------------TSGTTGLPKGCMHTHFS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 306 VVADFSGflkvtESQWAP-TCADVHISYLPLAHM--FERMVQSVVYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRL 382
Cdd:cd05935 109 AAANALQ-----SAVWTGlTPSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTM 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 383 LNRMydkifsqANTPlkrwllefaakrkqaevrsgiirndsiwdelffnKIQASLGGCVRMIVTGAAPASPTVLGFLRAA 462
Cdd:cd05935 184 LVDL-------LATP----------------------------------EFKTRDLSSLKVLTGGGAPMPPAVAEKLLKL 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 463 LGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEA 542
Cdd:cd05935 223 TGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEES 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 543 LDSDG---WLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLVg 612
Cdd:cd05935 303 FIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVisvpderVGEEVKAFIV- 380
|
490 500
....*....|....*....|..
gi 2230395409 613 iVVP------DPEVMPSWAQKR 628
Cdd:cd05935 381 -LRPeyrgkvTEEDIIEWAREQ 401
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
142-570 |
1.04e-23 |
|
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: 105.83 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 142 PYQWLSYQEVADRAEFLGSGLLQHNCKAcTDQFIGVFAQNRpEWIIVELACYTYSMVVVPLydtlGPGAIRYIINTA--- 218
Cdd:cd05906 36 SEEFQSYQDLLEDARRLAAGLRQLGLRP-GDSVILQFDDNE-DFIPAFWACVLAGFVPAPL----TVPPTYDEPNARlrk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 219 --DISTvIVDKPqkAVL----LLEHVERKETPGLKLIILMDPFEEALKERGQKCGVVIKSMQAVEHFLLSGlwprespgS 292
Cdd:cd05906 110 lrHIWQ-LLGSP--VVLtdaeLVAEFAGLETLSGLPGIRVLSIEELLDTAADHDLPQSRPDDLALLMLTSG--------S 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 293 CGNPKGAMLTHGNVVADFSGflKVTESQWAPtcADVHISYLPLAHmfermVQSVVYCHggrvgffQGDIRLLSDDMKALC 372
Cdd:cd05906 179 TGFPKAVPLTHRNILARSAG--KIQHNGLTP--QDVFLNWVPLDH-----VGGLVELH-------LRAVYLGCQQVHVPT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 373 PTIFPVVPRLLNRMyDKiFSQANTplkrWLLEFA-AK-RKQAEVRSgiirnDSIWDelffnkiqasLGGCVRMIVTGAAP 450
Cdd:cd05906 243 EEILADPLRWLDLI-DR-YRVTIT----WAPNFAfALlNDLLEEIE-----DGTWD----------LSSLRYLVNAGEAV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 451 ASPTVLGFLRAALGCQVYE-----GYGQTECTAGCTFTTP---GDWTSGH----VGAPLPCNHIKLVDVEElnywACKGE 518
Cdd:cd05906 302 VAKTIRRLLRLLEPYGLPPdairpAFGMTETCSGVIYSRSfptYDHSQALefvsLGRPIPGVSMRIVDDEG----QLLPE 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2230395409 519 GEIC---VRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkWLPAGTLKIIDRKK 570
Cdd:cd05906 378 GEVGrlqVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
146-601 |
1.30e-23 |
|
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: 104.38 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTAdistviv 225
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGP--GDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRA------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 226 dkpQKAVLLLEHVERKetpglkliilMDPFEEAlkerGQKCGVVIKSmqavehfllsglwprespGSCGNPKGAMLTHGN 305
Cdd:cd05903 73 ---KAKVFVVPERFRQ----------FDPAAMP----DAVALLLFTS------------------GTTGEPKGVMHSHNT 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 306 VVADFSGFLKvtesQWAPTCADVHISYLPLAHmfermvqsvvycHGGRVGFFqgdirllsddmkaLCPTIFPVvPRLLNR 385
Cdd:cd05903 118 LSASIRQYAE----RLGLGPGDVFLVASPMAH------------QTGFVYGF-------------TLPLLLGA-PVVLQD 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 386 MYDK------------IFSQANTPLKRWLLEfaAKRKQAEVRSGIirndsiwdelffnkiqaslggcvRMIVTGAAPASP 453
Cdd:cd05903 168 IWDPdkalalmrehgvTFMMGATPFLTDLLN--AVEEAGEPLSRL-----------------------RTFVCGGATVPR 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 454 TVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGD----WTSGhvGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVF 529
Cdd:cd05903 223 SLARRAAELLGAKVCSAYGSTECPGAVTSITPAPedrrLYTD--GRPLPGVEIKVVD-DTGATLAPGVEGELLSRGPSVF 299
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2230395409 530 KGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYV 601
Cdd:cd05903 300 LGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAV 369
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
294-619 |
1.35e-23 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 102.35 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 294 GNPKGAMLTHGNVVA---DFSGFLKVTEsqwaptcADVHISYLPLAHMFERMVQSVVYCHGGR---VGFFQGDIRL-LSD 366
Cdd:cd17637 13 GRPRGAVLSHGNLIAanlQLIHAMGLTE-------ADVYLNMLPLFHIAGLNLALATFHAGGAnvvMEKFDPAEALeLIE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 367 DMKAlcpTIFPVVPRLLNRMYDkifsqantplkrwllefAAKRKQAEVRSgiIRNdsiwdelffnkiqaslggcvrmiVT 446
Cdd:cd17637 86 EEKV---TLMGSFPPILSNLLD-----------------AAEKSGVDLSS--LRH-----------------------VL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 447 GAApaSPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDveELNYWACKGE-GEICVRG 525
Cdd:cd17637 121 GLD--APETIQRFEETTGATFWSLYGQTE-TSGLVTLSPYRERPGSAGRPGPLVRVRIVD--DNDRPVPAGEtGEIVVRG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 526 PNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRK--KHIFKlAQGEYVAPEKIENIyIRSQP-VAQIYVH 602
Cdd:cd17637 196 PLVFQGYWNLPELTAYTFR-NGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKV-ILEHPaIAEVCVI 272
|
330
....*....|....*..
gi 2230395409 603 GdslkaflvgivVPDPE 619
Cdd:cd17637 273 G-----------VPDPK 278
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
208-611 |
1.57e-23 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 105.29 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 208 PGAIRYIINTadistvIVDKPQKAVlllehverketPGLKLIILMdPFEEALKE-RGQKCGVVIKSMQAVEHFLLSGlwp 286
Cdd:PRK12492 158 PAAKGWLVNT------VVDKVKKMV-----------PAYHLPQAV-PFKQALRQgRGLSLKPVPVGLDDIAVLQYTG--- 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 287 respGSCGNPKGAMLTHGNVVADFSGFLKVTeSQWAP-------TCADVHISYLPLAHMFERMVQSVVYCHGGRVGFFQG 359
Cdd:PRK12492 217 ----GTTGLAKGAMLTHGNLVANMLQVRACL-SQLGPdgqplmkEGQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLIT 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 360 DIRLLSDDMKALCPTIFPVVPRLlnrmydkifsqaNTplkrwllEFAAKRKQAEVRSgiirndsiwdeLFFNKIQASLGG 439
Cdd:PRK12492 292 NPRDIPGFIKELGKWRFSALLGL------------NT-------LFVALMDHPGFKD-----------LDFSALKLTNSG 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 440 cvrmivtGAAPASPTVLGFlRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDvEELNYWACKGE 518
Cdd:PRK12492 342 -------GTALVKATAERW-EQLTGCTIVEGYGLTETSPVASTNPYGELARlGTVGIPVPGTALKVID-DDGNELPLGER 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 519 GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQ 598
Cdd:PRK12492 413 GELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLI-IVSGFNVYPNEIEDVVMAHPKVAN 491
|
410 420
....*....|....*....|
gi 2230395409 599 IYV-------HGDSLKAFLV 611
Cdd:PRK12492 492 CAAigvpderSGEAVKLFVV 511
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
289-601 |
5.00e-23 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 103.52 E-value: 5.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 289 SPGSCGNPKGAMLTHGNVVADFSGFLKVTESQWAPTCADVHIsyLPLAHMF--ERMVQSVVYCHGGRVGFFQGDIRLLSD 366
Cdd:PLN02330 192 SSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMIGQVVTLGL--IPFFHIYgiTGICCATLRNKGKVVVMSRFELRTFLN 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 367 DMKALCPTIFPVVPrllnrmydkifsqantPLKRWLLEfaakrkqaevrsgiirnDSIWDELFFNKIQaslggcVRMIVT 446
Cdd:PLN02330 270 ALITQEVSFAPIVP----------------PIILNLVK-----------------NPIVEEFDLSKLK------LQAIMT 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 447 GAAPASPTVL-GFLRAALGCQVYEGYGQTECTagCTFTTPGDWTSGH-------VGAPLPCNHIKLVDVEELNYWACKGE 518
Cdd:PLN02330 311 AAAPLAPELLtAFEAKFPGVQVQEAYGLTEHS--CITLTHGDPEKGHgiakknsVGFILPNLEVKFIDPDTGRSLPKNTP 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 519 GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQ 598
Cdd:PLN02330 389 GELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAILLTHPSVED 467
|
...
gi 2230395409 599 IYV 601
Cdd:PLN02330 468 AAV 470
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
198-623 |
5.27e-23 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 102.90 E-value: 5.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 198 VVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlLLEHVErketpgLKLIILMDPFEEALKERGQKCGvviKSMQAVE 277
Cdd:cd05922 48 VFVPLNPTLKESVLRYLVADAGGRIVLADAG-----AADRLR------DALPASPDPGTVLDADGIRAAR---ASAPAHE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 278 --HFLLSGLWPreSPGSCGNPKGAMLTHGNVVADFSG---FLKVTESQWAPTCADVHISY-LPLAHMFERMVQSVVYCHG 351
Cdd:cd05922 114 vsHEDLALLLY--TSGSTGSPKLVRLSHQNLLANARSiaeYLGITADDRALTVLPLSYDYgLSVLNTHLLRGATLVLTND 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 352 GRVGffqgdiRLLSDDMKALCPTIFPVVP---RLLNRMydkIFSQANTPLKRWLLEFAAKRKQAEVRSgiirndsiwdel 428
Cdd:cd05922 192 GVLD------DAFWEDLREHGATGLAGVPstyAMLTRL---GFDPAKLPSLRYLTQAGGRLPQETIAR------------ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 429 ffnkiqaslggcvrmivtgaapasptvlgfLRAAL-GCQVYEGYGQTECTAGCTFTTPG--DWTSGHVGAPLPCNHIklv 505
Cdd:cd05922 251 ------------------------------LRELLpGAQVYVMYGQTEATRRMTYLPPEriLEKPGSIGLAIPGGEF--- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 506 DVEELNYWACK-GE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkWLPA-GTLKIIDRKKHIFKLAqGEYVA 582
Cdd:cd05922 298 EILDDDGTPTPpGEpGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLA-RRDEdGFLFIVGRRDRMIKLF-GNRIS 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2230395409 583 PEKIENIyIRSQP---VAQIYVHGDSLKAFLVGIVVPDPEVMPS 623
Cdd:cd05922 376 PTEIEAA-ARSIGliiEAAAVGLPDPLGEKLALFVTAPDKIDPK 418
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
118-557 |
7.63e-23 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 103.27 E-value: 7.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 118 YQVFRRGLSISGNGPCLGFRKPKQPYQWLSYQEVADRAEFLGSGLLQHnckactdqfiGV--------FAQNRPEWIIVE 189
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRAL----------GVkkgdrvaiYLPNIPEAVIAM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 190 LACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVD----KPQKAVLLLEHVE--RKETPGLKLIILMD---------- 253
Cdd:COG0365 82 LACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITAdgglRGGKVIDLKEKVDeaLEELPSLEHVIVVGrtgadvpmeg 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 254 --PFEEALKERGQKCGVVikSMQAvEH--FLL--SGlwprespgSCGNPKGAMLTHGNVVADFSGFLK----VTESQ--W 321
Cdd:COG0365 162 dlDWDELLAAASAEFEPE--PTDA-DDplFILytSG--------TTGKPKGVVHTHGGYLVHAATTAKyvldLKPGDvfW 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 322 APtcADV----HISYL---PLAH-----MFERmvqSVVYCHGGRvgFFQgdirlLSDDMKalcPTIFPVVPRLLnRMydk 389
Cdd:COG0365 231 CT--ADIgwatGHSYIvygPLLNgatvvLYEG---RPDFPDPGR--LWE-----LIEKYG---VTVFFTAPTAI-RA--- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 390 ifsqantpLKRWLLEFAAKRKQAevrsgiirndsiwdelffnkiqaSLggcvRMIVTGAAPASPTVLGFLRAALGCQVYE 469
Cdd:COG0365 292 --------LMKAGDEPLKKYDLS-----------------------SL----RLLGSAGEPLNPEVWEWWYEAVGVPIVD 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 470 GYGQTECtaGCTFTTPGDWTS---GHVGAPLPCNHIKLVDvEELNywACKG--EGEICVRG--PNVFKGYLKDPDRTKEA 542
Cdd:COG0365 337 GWGQTET--GGIFISNLPGLPvkpGSMGKPVPGYDVAVVD-EDGN--PVPPgeEGELVIKGpwPGMFRGYWNDPERYRET 411
|
490
....*....|....*..
gi 2230395409 543 L--DSDGWLHTGDIGKW 557
Cdd:COG0365 412 YfgRFPGWYRTGDGARR 428
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
441-626 |
1.46e-22 |
|
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: 100.88 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 441 VRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTE-CTAGCTFTtPGDWTS--GHVGAPLPCNHIKLVDVEELNYwackG 517
Cdd:cd05912 191 LRCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTEtCSQIVTLS-PEDALNkiGSAGKPLFPVELKIEDDGQPPY----E 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 518 EGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVA 597
Cdd:cd05912 265 VGEILLKGPNVTKGYLNRPDATEESFE-NGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPAIK 342
|
170 180
....*....|....*....|....*....
gi 2230395409 598 QIYVhgdslkaflVGIvvPDPEvmpsWAQ 626
Cdd:cd05912 343 EAGV---------VGI--PDDK----WGQ 356
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
442-623 |
1.52e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 101.60 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 442 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGE--G 519
Cdd:PRK07787 244 RLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVD-EDGGPVPHDGEtvG 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 520 EICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDR------KKHIFKLAQGEyvapekIENIYIRS 593
Cdd:PRK07787 323 ELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGGYRIGAGE------IETALLGH 396
|
170 180 190
....*....|....*....|....*....|...
gi 2230395409 594 QPVAQIYVHG---DSLKAFLVGIVVPDPEVMPS 623
Cdd:PRK07787 397 PGVREAAVVGvpdDDLGQRIVAYVVGADDVAAD 429
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
289-591 |
1.89e-22 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 101.60 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 289 SPGSCGNPKGAMLTHGNVVADFSGFLKVTESQWAPTCADVHISYLPLAHMFErmVQSVVYChGGRVG--------FfqgD 360
Cdd:PLN02246 187 SSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYFHSDDVILCVLPMFHIYS--LNSVLLC-GLRVGaailimpkF---E 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 361 IRLLSDDMKALCPTIFPVVPrllnrmydkifsqantPLkrwLLEFAakrKQAEVRSgiirndsiwDELffnkiqASlggc 440
Cdd:PLN02246 261 IGALLELIQRHKVTIAPFVP----------------PI---VLAIA---KSPVVEK---------YDL------SS---- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 441 VRMIVTGAAPASPTVLGFLRAALGCQVY-EGYGQTE-------CTAgctFT-TPGDWTSGHVGAPLPCNHIKLVDVE--- 508
Cdd:PLN02246 300 IRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMTEagpvlamCLA---FAkEPFPVKSGSCGTVVRNAELKIVDPEtga 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 509 ELNYWACkgeGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIEN 588
Cdd:PLN02246 377 SLPRNQP---GEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAELEA 452
|
...
gi 2230395409 589 IYI 591
Cdd:PLN02246 453 LLI 455
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
146-623 |
4.06e-22 |
|
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: 99.91 E-value: 4.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACY----TYsmvvVPLYDTLGPGAIRYIINTADIS 221
Cdd:cd05930 13 LTYAELDARANRLARYLRERGVGP--GDLVAVLLERSLEMVVAILAVLkagaAY----VPLDPSYPAERLAYILEDSGAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 222 TVIVDKPQKAVLLLehverkeTpglkliilmdpfeealkergqkcgvviksmqavehfllsglwpreSpGSCGNPKGAML 301
Cdd:cd05930 87 LVLTDPDDLAYVIY-------T---------------------------------------------S-GSTGKPKGVMV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 302 THGNVV---ADFSGFLKVTES----QWAPTCADVHIS--YLPLAHmfermvqsvvychGGRVGFFQGDIRLLSDDMKALC 372
Cdd:cd05930 114 EHRGLVnllLWMQEAYPLTPGdrvlQFTSFSFDVSVWeiFGALLA-------------GATLVVLPEEVRKDPEALADLL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 373 ----PTIFPVVPRLLNRMYDKIFSQANTPLkrwllefaakrkqaevrsgiirndsiwdelffnkiqaslggcvRMIVTGA 448
Cdd:cd05930 181 aeegITVLHLTPSLLRLLLQELELAALPSL-------------------------------------------RLVLVGG 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 449 APASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFT--TPGDWTSGHV--GAPLPCNHIKLVDvEELNYWACKGEGEICV 523
Cdd:cd05930 218 EALPPDLVrRWRELLPGARLVNLYGPTEATVDATYYrvPPDDEEDGRVpiGRPIPNTRVYVLD-ENLRPVPPGVPGELYI 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 524 RGPNVFKGYLKDPDRTKEA-----LDSDGWLH-TGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVA 597
Cdd:cd05930 297 GGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIELGEIEAALLAHPGVR 375
|
490 500
....*....|....*....|....*....
gi 2230395409 598 QIYV---HGDSLKAFLVGIVVPDPEVMPS 623
Cdd:cd05930 376 EAAVvarEDGDGEKRLVAYVVPDEGGELD 404
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
147-589 |
7.85e-22 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 99.82 E-value: 7.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 147 SYQEVADRAEFLGSGLLQHNCKACTdqfigVFAQNRPEW---IIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTV 223
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGD-----RVAFQLPGWcefTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 224 IVDKPQKAV--LLLEHVERKETPGLKLIILMDPFEEALKERGQKcgVVIKSMQAVEHF----------LLSglwpreSPG 291
Cdd:PRK06087 126 FAPTLFKQTrpVDLILPLQNQLPQLQQIVGVDKLAPATSSLSLS--QIIADYEPLTTAitthgdelaaVLF------TSG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 292 SCGNPKGAMLTHGNVVADFSGFLKVTESQWAptcaDVHISYLPLAHmfermvqSVVYCHGGRVGFFQGDIRLLSDDMKAl 371
Cdd:PRK06087 198 TEGLPKGVMLTHNNILASERAYCARLNLTWQ----DVFMMPAPLGH-------ATGFLHGVTAPFLIGARSVLLDIFTP- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 372 cptifPVVPRLLNRmyDKI-FSQANTPLkrwllefaakrkqaevrsgiirndsIWDELFFNKIQASLGGCVRMIVTGAAP 450
Cdd:PRK06087 266 -----DACLALLEQ--QRCtCMLGATPF-------------------------IYDLLNLLEKQPADLSALRFFLCGGTT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 451 ASPTVLgflRAAL--GCQVYEGYGQTECTAGcTFTTPGD---WTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRG 525
Cdd:PRK06087 314 IPKKVA---RECQqrGIKLLSVYGSTESSPH-AVVNLDDplsRFMHTDGYAAAGVEIKVVD-EARKTLPPGCEGEEASRG 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2230395409 526 PNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENI 589
Cdd:PRK06087 389 PNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDI 451
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
144-628 |
6.46e-21 |
|
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: 96.59 E-value: 6.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 144 QWLSYQEVADRAEFLGSGLLQHNckACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLyDTLGPGA-IRYIINTADIST 222
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARG--VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPL-DPDYPADrLRYILEDAEPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 223 VIVDkpqkavlllehverketpglkliilmdpfeEALKERGQKCGVVIKSMQAVEHFLLSGLWPRESP----------GS 292
Cdd:cd12116 88 VLTD------------------------------DALPDRLPAGLPVLLLALAAAAAAPAAPRTPVSPddlayviytsGS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 293 CGNPKGAMLTHGNVVADFSGF------------LKVTesqwaPTCADvhIS----YLPLahmfermvqsvvyCHGGRVGF 356
Cdd:cd12116 138 TGRPKGVVVSHRNLVNFLHSMrerlglgpgdrlLAVT-----TYAFD--ISllelLLPL-------------LAGARVVI 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 357 FQGDI----RLLSDDMKALCPTIFpvvprllnrmydkifsQAnTP-LKRWLLefaakrkqaevrsgiirnDSIWDELffn 431
Cdd:cd12116 198 APRETqrdpEALARLIEAHSITVM----------------QA-TPaTWRMLL------------------DAGWQGR--- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 432 kiqASLggcvRMIVTGAApaSPTVLGFLRAALGCQVYEGYGQTECT--AGCTFTTPGDwTSGHVGAPLPCNHIKLVDvEE 509
Cdd:cd12116 240 ---AGL----TALCGGEA--LPPDLAARLLSRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLD-AA 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 510 LNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH-------TGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVA 582
Cdd:cd12116 309 LRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQVKI-RGHRIE 387
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2230395409 583 PEKIENIYIRSQPVAQ--IYVHGDSLKAFLVGIVVPDPEVMPSWAQKR 628
Cdd:cd12116 388 LGEIEAALAAHPGVAQaaVVVREDGGDRRLVAYVVLKAGAAPDAAALR 435
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
291-611 |
1.35e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 96.26 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 291 GSCGNPKGAMLTHGNVVADfsgflKVTESQWAPTCAD---VHISYLPLAHMF-ERMVQSVVYCHGGRVGFF-QGDIRLLS 365
Cdd:PRK06710 216 GTTGFPKGVMLTHKNLVSN-----TLMGVQWLYNCKEgeeVVLGVLPFFHVYgMTAVMNLSIMQGYKMVLIpKFDMKMVF 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 366 DDMKALCPTIFPVVPRLLnrmydkiFSQANTPLkrwllefaakRKQAEVRSgiirndsiwdelffnkiqaslggcVRMIV 445
Cdd:PRK06710 291 EAIKKHKVTLFPGAPTIY-------IALLNSPL----------LKEYDISS------------------------IRACI 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 446 TGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgctfTTPGDW-----TSGHVGAPLPCNHIKLVDVEELNYWACKGEGE 520
Cdd:PRK06710 330 SGSAPLPVEVQEKFETVTGGKLVEGYGLTESSP----VTHSNFlwekrVPGSIGVPWPDTEAMIMSLETGEALPPGEIGE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 521 ICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIY 600
Cdd:PRK06710 406 IVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREVEEVLYEHEKVQEVV 483
|
330
....*....|....*...
gi 2230395409 601 V-------HGDSLKAFLV 611
Cdd:PRK06710 484 TigvpdpyRGETVKAFVV 501
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
114-570 |
1.97e-20 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 95.79 E-value: 1.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 114 ARTMYQVFRRGLSISGNGPCLgfrkpkqpyqwlSYQEVADR---------AEFLG-----SGLLqHNCKACTDQFIGVFA 179
Cdd:PRK07529 24 PASTYELLSRAAARHPDAPAL------------SFLLDADPldrpetwtyAELLAdvtrtANLL-HSLGVGPGDVVAFLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 180 QNRPEWIIVELACYTYSmVVVPLYDTLGPGAIRYIINTADISTVIVDKP-------QKAVLLLEHVerketPGLKLIILM 252
Cdd:PRK07529 91 PNLPETHFALWGGEAAG-IANPINPLLEPEQIAELLRAAGAKVLVTLGPfpgtdiwQKVAEVLAAL-----PELRTVVEV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 253 D-------PFEEALKERGQKCGVVIKSM------QAVEHfLLSGLWPRESP--------GSCGNPKGAMLTHGNVVADfs 311
Cdd:PRK07529 165 DlarylpgPKRLAVPLIRRKAHARILDFdaelarQPGDR-LFSGRPIGPDDvaayfhtgGTTGMPKLAQHTHGNEVAN-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 312 GFLKVTESQWAPTcaDVHISYLPLAHMFERMVQSVVYCHGGR---VGFFQG--DIRLLSDDMK---ALCPTIFPVVPRLL 383
Cdd:PRK07529 242 AWLGALLLGLGPG--DTVFCGLPLFHVNALLVTGLAPLARGAhvvLATPQGyrGPGVIANFWKiveRYRINFLSGVPTVY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 384 NRMydkifsqANTPlkrwllefaakrkqaevrsgiirndsiwdelffnkIQASLGGCVRMIVTGAAPASPTVLGFLRAAL 463
Cdd:PRK07529 320 AAL-------LQVP-----------------------------------VDGHDISSLRYALCGAAPLPVEVFRRFEAAT 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 464 GCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLVDVEEL-NYW--ACKGE-GEICVRGPNVFKGYLkDPDR 538
Cdd:PRK07529 358 GVRIVEGYGLTEATCVSSVNPPdGERRIGSVGLRLPYQRVRVVILDDAgRYLrdCAVDEvGVLCIAGPNVFSGYL-EAAH 436
|
490 500 510
....*....|....*....|....*....|..
gi 2230395409 539 TKEALDSDGWLHTGDIGKWLPAGTLKIIDRKK 570
Cdd:PRK07529 437 NKGLWLEDGWLNTGDLGRIDADGYFWLTGRAK 468
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
146-603 |
5.29e-20 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 93.87 E-value: 5.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 146 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLAALGVK--KGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLIT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 226 DkpqkavlllEHVERKETPGLKLIilmdpFEEALKERGQKcgVVIKSMqavehfllsglWPRES-------PGSCGNPKG 298
Cdd:PRK03640 106 D---------DDFEAKLIPGISVK-----FAELMNGPKEE--AEIQEE-----------FDLDEvatimytSGTTGKPKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 299 AMLTHGNVVADFSGF---LKVTESQ-WapTCAdvhisyLPLAHM--FERMVQSVVYchGGRV----GFFQGDI-RLLSDD 367
Cdd:PRK03640 159 VIQTYGNHWWSAVGSalnLGLTEDDcW--LAA------VPIFHIsgLSILMRSVIY--GMRVvlveKFDAEKInKLLQTG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 368 MKalcpTIFPVVPRLLNRMYDKIfSQANTPlkrwllefaakrkqaevrsgiirnDSiwdelffnkiqaslggcVRMIVTG 447
Cdd:PRK03640 229 GV----TIISVVSTMLQRLLERL-GEGTYP------------------------SS-----------------FRCMLLG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 448 AAPASPTVLGFLRAAlGCQVYEGYGQTEcTAGCTFTTPGDWTS---GHVGAPL-PCNhIKLVDveELNYWACKGEGEICV 523
Cdd:PRK03640 263 GGPAPKPLLEQCKEK-GIPVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLfPCE-LKIEK--DGVVVPPFEEGEIVV 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 524 RGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYVHG 603
Cdd:PRK03640 338 KGPNVTKGYLNREDATRETFQ-DGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPGVAEAGVVG 415
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
181-611 |
7.84e-20 |
|
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: 92.79 E-value: 7.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 181 NRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAVLllehverketpglkliilmdpfeealk 260
Cdd:cd05972 34 RVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDAEDPALI--------------------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 261 ergqkcgvviksmqaveHFllsglwpreSPGSCGNPKGAMLTHGnvvadfsgflkvtesqwaptcadvhisyLPLAHMfe 340
Cdd:cd05972 87 -----------------YF---------TSGTTGLPKGVLHTHS----------------------------YPLGHI-- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 341 rmvQSVVYCHGGRvgffQGDIRLLSDD----MKALCPTIFPV---VPRLLN--------RMYDKI-------FSQANTPL 398
Cdd:cd05972 111 ---PTAAYWLGLR----PDDIHWNIADpgwaKGAWSSFFGPWllgATVFVYegprfdaeRILELLerygvtsFCGPPTAY 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 399 KRWLLEFAAKRKQAEVRSgiirndsiwdelffnkiqaslggcvrmIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTA 478
Cdd:cd05972 184 RMLIKQDLSSYKFSHLRL---------------------------VVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGL 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 479 GCTFTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNV--FKGYLKDPDRTKEALdSDGWLHTGDIGK 556
Cdd:cd05972 237 TVGNFPDMPVKPGSMGRPTPGYDVAIID-DDGRELPPGEEGDIAIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDRAY 314
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2230395409 557 WLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLV 611
Cdd:cd05972 315 RDEDGYFWFVGRADDIIK-SSGYRIGPFEVESALLEHPAVAEAAVvgspdpvRGEVVKAFVV 375
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
137-582 |
8.85e-20 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 93.79 E-value: 8.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 137 RKPKQPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPL---YDTLG--PGAI 211
Cdd:PRK08180 61 RGADGGWRRLTYAEALERVRAIAQALLDRGLSA--ERPLMILSGNSIEHALLALAAMYAGVPYAPVspaYSLVSqdFGKL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 212 RYIINTADISTVIVDKPQK-----AVLLLEHVE----RKETPGLKLIilmdPFEEALKERGQkcGVVIKSMQAVEH---- 278
Cdd:PRK08180 139 RHVLELLTPGLVFADDGAAfaralAAVVPADVEvvavRGAVPGRAAT----PFAALLATPPT--AAVDAAHAAVGPdtia 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 279 -FLLSGlwprespGSCGNPKGAMLTHGNVVA------DFSGFLKVTESqwaptcadVHISYLPLAHMF--ERMVQSVVYc 349
Cdd:PRK08180 213 kFLFTS-------GSTGLPKAVINTHRMLCAnqqmlaQTFPFLAEEPP--------VLVDWLPWNHTFggNHNLGIVLY- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 350 HGGR---------VGFFQGDIRLLsddmKALCPTIFPVVPRLlnrmydkifsqantplkrWLLEFAAKRKQAEVRsgiir 420
Cdd:PRK08180 277 NGGTlyiddgkptPGGFDETLRNL----REISPTVYFNVPKG------------------WEMLVPALERDAALR----- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 421 ndsiwdELFFNKiqaslggcVRMIVTGAAPASPTVLGFL----RAALGCQVY--EGYGQTECTAGCTFTTPGDWTSGHVG 494
Cdd:PRK08180 330 ------RRFFSR--------LKLLFYAGAALSQDVWDRLdrvaEATCGERIRmmTGLGMTETAPSATFTTGPLSRAGNIG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 495 APLPCNHIKLVDVEelnywackGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWL----PAGTLKIIDRKK 570
Cdd:PRK08180 396 LPAPGCEVKLVPVG--------GKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVdpadPERGLMFDGRIA 467
|
490
....*....|..
gi 2230395409 571 HIFKLAQGEYVA 582
Cdd:PRK08180 468 EDFKLSSGTWVS 479
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
144-628 |
1.03e-19 |
|
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: 94.54 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 144 QWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELA------CYtysmvvVPLyDTLGPGA-IRYIIN 216
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALGVGP--GDLVGVCLERSLEMVVALLAvlkagaAY------VPL-DPAYPAErLAYMLE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 217 TADISTVIVDKPQKAVLLLEHVErketpglklIILMDPFEEAlkergqkcgvviksmQAVEHFLLSGLWPrESP------ 290
Cdd:COG1020 571 DAGARLVLTQSALAARLPELGVP---------VLALDALALA---------------AEPATNPPVPVTP-DDLayviyt 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 291 -GSCGNPKGAMLTHGNVV---ADFSGFLKVTES----QWAPTCADVHIS--YLPLahmfermvqsvvyCHGGRVGFFQGD 360
Cdd:COG1020 626 sGSTGRPKGVMVEHRALVnllAWMQRRYGLGPGdrvlQFASLSFDASVWeiFGAL-------------LSGATLVLAPPE 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 361 IRLLSDDMKALC----PTIFPVVPRLLNRMYDkifsqantplkrwllefAAKRKQAEVRsgiirndsiwdelffnkiqas 436
Cdd:COG1020 693 ARRDPAALAELLarhrVTVLNLTPSLLRALLD-----------------AAPEALPSLR--------------------- 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 437 lggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF--TTPGDWTSGHV--GAPLPCNHIKLVDvEELN- 511
Cdd:COG1020 735 -----LVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYyeVTPPDADGGSVpiGRPIANTRVYVLD-AHLQp 808
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 512 --YWACkgeGEICVRGPNVFKGYLKDPDRTKEA-----LDSDG--WLHTGDIGKWLPAGTLKIIDRKKHifklaQ----- 577
Cdd:COG1020 809 vpVGVP---GELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNLEFLGRADD-----Qvkirg 880
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 578 -----GEyvapekIENIyIRSQP-VAQIYV--HGDSL-KAFLVGIVVPDPEVMPSWAQKR 628
Cdd:COG1020 881 frielGE------IEAA-LLQHPgVREAVVvaREDAPgDKRLVAYVVPEAGAAAAAALLR 933
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
147-595 |
1.21e-19 |
|
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: 91.94 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 147 SYQEVADRAEFLGSGLLQHnCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLyDTLGPGA-IRYIINTADISTVIV 225
Cdd:TIGR01733 1 TYRELDERANRLARHLRAA-GGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPL-DPAYPAErLAFILEDAGARLLLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 226 DKPqkavllleHVERKETPGLKLIILMDPFEEALkergqkcgvviksMQAVEHFLLSGLWPRESP-------GSCGNPKG 298
Cdd:TIGR01733 79 DSA--------LASRLAGLVLPVILLDPLELAAL-------------DDAPAPPPPDAPSGPDDLayviytsGSTGRPKG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 299 AMLTHGNVVAdfsgFLKVTESQWAPTCADVHISYLPLAH------MFermvqsVVYCHGGRVgffqgdiRLLSDDMKAlc 372
Cdd:TIGR01733 138 VVVTHRSLVN----LLAWLARRYGLDPDDRVLQFASLSFdasveeIF------GALLAGATL-------VVPPEDEER-- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 373 pTIFPVVPRLLNRMYDKIFSQANTPLKRWLLEfaakrkqaevrsgiirndsiwdelffnkiQASLGGCVRMIVTGAAPAS 452
Cdd:TIGR01733 199 -DDAALLAALIAEHPVTVLNLTPSLLALLAAA-----------------------------LPPALASLRLVILGGEALT 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 453 PTVLGFLRAALG-CQVYEGYGQTECTAGCT-FTTPGDWTSGHV----GAPLPCNHIKLVDvEELNYWACKGEGEICVRGP 526
Cdd:TIGR01733 249 PALVDRWRARGPgARLINLYGPTETTVWSTaTLVDPDDAPRESpvpiGRPLANTRLYVLD-DDLRPVPVGVVGELYIGGP 327
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2230395409 527 NVFKGYLKDPDRTKEA-LDSDGWL-------HTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIyIRSQP 595
Cdd:TIGR01733 328 GVARGYLNRPELTAERfVPDPFAGgdgarlyRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAA-LLRHP 402
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
441-617 |
1.40e-19 |
|
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: 91.99 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 441 VRMIVTGAAPASPTVLGflRAALGCQVYEGYGQTECTAGCTFT--TPGDWTsgHVGAPLPCNHIKLVDvEELNYWACKGE 518
Cdd:cd17653 211 LKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTelLPGQPV--TIGKPIPNSTCYILD-ADLQPVPEGVV 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 519 GEICVRGPNVFKGYLKDPDRTKEALDSDGWLH------TGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIR 592
Cdd:cd17653 286 GEICISGVQVARGYLGNPALTASKFVPDPFWPgsrmyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEIEEVVLQ 364
|
170 180
....*....|....*....|....*...
gi 2230395409 593 SQPVAQ---IYVHGDSLKAFlvgiVVPD 617
Cdd:cd17653 365 SQPEVTqaaAIVVNGRLVAF----VTPE 388
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
291-618 |
2.61e-19 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 91.86 E-value: 2.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 291 GSCGNPKGAMLTHGNVVADfsgfLKVTESQWAPTCADVHISYLPLAHMFERMVQS-VVYCHGGRVGFFQgdiRLLSDDMK 369
Cdd:PRK07514 166 GTTGRSKGAMLSHGNLLSN----ALTLVDYWRFTPDDVLIHALPIFHTHGLFVATnVALLAGASMIFLP---KFDPDAVL 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 370 ALCP--TIFPVVPRLLNRMYdkifsqANTPLKRwllEFAAKrkqaevrsgiirndsiwdelffnkiqaslggcVRMIVTG 447
Cdd:PRK07514 239 ALMPraTVMMGVPTFYTRLL------QEPRLTR---EAAAH--------------------------------MRLFISG 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 448 AAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTfTTP--GDWTSGHVGAPLPCNHIKLVDVE---ELNywacKGE-GEI 521
Cdd:PRK07514 278 SAPLLAETHREFQERTGHAILERYGMTE-TNMNT-SNPydGERRAGTVGFPLPGVSLRVTDPEtgaELP----PGEiGMI 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 522 CVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIfkLAQGEY-VAPEKIENiYIRSQP-VAQI 599
Cdd:PRK07514 352 EVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDL--IISGGYnVYPKEVEG-EIDELPgVVES 428
|
330 340
....*....|....*....|..
gi 2230395409 600 YVHGDSLKAF---LVGIVVPDP 618
Cdd:PRK07514 429 AVIGVPHPDFgegVTAVVVPKP 450
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
441-618 |
3.44e-19 |
|
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: 91.54 E-value: 3.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 441 VRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPgdwTSGHV--------------GAPLPCNHIKLVD 506
Cdd:cd12119 282 LRRVVIGGSAVPRSLIEAFEE-RGVRVIHAWGMTETSPLGTVARP---PSEHSnlsedeqlalrakqGRPVPGVELRIVD 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 507 VE--ELNyWACKGEGEICVRGPNVFKGYLKDPDRTkEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPE 584
Cdd:cd12119 358 DDgrELP-WDGKAVGELQVRGPWVTKSYYKNDEES-EALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSG-GEWISSV 434
|
170 180 190
....*....|....*....|....*....|....
gi 2230395409 585 KIENIYIRSQPVAQIYVhgdslkaflvgIVVPDP 618
Cdd:cd12119 435 ELENAIMAHPAVAEAAV-----------IGVPHP 457
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
146-619 |
5.10e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 91.17 E-value: 5.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 146 LSYQEVADRAEFLgSGLLQHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK08314 36 ISYRELLEEAERL-AGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 226 -----DKPQKAV--LLLEHV-------ERKETPGLKLIILMD--PFEEALKERGqkcgvVIKSMQAVEHFLLSG------ 283
Cdd:PRK08314 115 gselaPKVAPAVgnLRLRHVivaqysdYLPAEPEIAVPAWLRaePPLQALAPGG-----VVAWKEALAAGLAPPphtagp 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 284 ----LWPRESpGSCGNPKGAMLTHGNVVADFSGFlkvteSQWAP-TCADVHISYLPLAHM--FERMVQSVVYChGGRVgf 356
Cdd:PRK08314 190 ddlaVLPYTS-GTTGVPKGCMHTHRTVMANAVGS-----VLWSNsTPESVVLAVLPLFHVtgMVHSMNAPIYA-GATV-- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 357 fqgdirllsddmkalcpTIFP-----VVPRLLNRMydKIFSQANTPLKrwLLEFAAKRKQAEvrsgiiRNDSiwdelffn 431
Cdd:PRK08314 261 -----------------VLMPrwdreAAARLIERY--RVTHWTNIPTM--VVDFLASPGLAE------RDLS-------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 432 kiqaSLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWT-SGHVGAPLPCNHIKLVDVEEL 510
Cdd:PRK08314 306 ----SL----RYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTE-TMAQTHSNPPDRPkLQCLGIPTFGVDARVIDPETL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 511 NYWACKGEGEICVRGPNVFKGYLKDPDRTKEA---LDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKIE 587
Cdd:PRK08314 377 EELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMIN-ASGFKVWPAEVE 455
|
490 500 510
....*....|....*....|....*....|....*....
gi 2230395409 588 NIYIRSQPVAQIYV-------HGDSLKAFlvgiVVPDPE 619
Cdd:PRK08314 456 NLLYKHPAIQEACViatpdprRGETVKAV----VVLRPE 490
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
187-587 |
5.57e-19 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 91.91 E-value: 5.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 187 IVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKpqkavlllEHVERKETPGLKLIILMDP---FEEALKER- 262
Cdd:PRK08633 680 LANLALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVITSR--------KFLEKLKNKGFDLELPENVkviYLEDLKAKi 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 263 --GQKCGVVIKSMQAVEHFLLSGLWPRESP----------GSCGNPKGAMLTHGNVVAD---FSGFLKVTESqwaptcaD 327
Cdd:PRK08633 752 skVDKLTALLAARLLPARLLKRLYGPTFKPddtatiifssGSEGEPKGVMLSHHNILSNieqISDVFNLRND-------D 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 328 VHISYLPLAHMFERMVQ---------SVVYcH-----GGRVGffqgdirLLSDDMKA--LC--PTIFpvvprllnRMYdk 389
Cdd:PRK08633 825 VILSSLPFFHSFGLTVTlwlpllegiKVVY-HpdptdALGIA-------KLVAKHRAtiLLgtPTFL--------RLY-- 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 390 ifsqantplkrwllefaakrkqaevrsgiIRNDSIWDELFfnkiqASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYE 469
Cdd:PRK08633 887 -----------------------------LRNKKLHPLMF-----ASL----RLVVAGAEKLKPEVADAFEEKFGIRILE 928
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 470 GYGQTECTAGCTFTTP-----GDWT-----SGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRT 539
Cdd:PRK08633 929 GYGATETSPVASVNLPdvlaaDFKRqtgskEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKT 1008
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2230395409 540 KEAL---DSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIE 587
Cdd:PRK08633 1009 AEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIG-GEMVPLGAVE 1058
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
144-619 |
5.84e-19 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 90.69 E-value: 5.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 144 QWLSYQEVADRAEFLgSGLLQHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTV 223
Cdd:PRK06839 26 EEMTYKQLHEYVSKV-AAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 224 IVDKP-QKAVLLLEHVERKETPglklIILMDPFEEALKERGqkcGVVIKSMQAveHFLLSglwprESPGSCGNPKGAMLT 302
Cdd:PRK06839 105 FVEKTfQNMALSMQKVSYVQRV----ISITSLKEIEDRKID---NFVEKNESA--SFIIC-----YTSGTTGKPKGAVLT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 303 HGNVvadfsgFLKVTESQWAP--TCADVHISYLPLAHMfermvqsvvychgGRVGFFQgdirllsddmkalCPTIFP--- 377
Cdd:PRK06839 171 QENM------FWNALNNTFAIdlTMHDRSIVLLPLFHI-------------GGIGLFA-------------FPTLFAggv 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 378 -VVPRLLNRmyDKIFSQANTplKRWLLEFAAKRKQAEVRSGIIRNDSIWDElffnkiqaslggcVRMIVTGAAPAS-PTV 455
Cdd:PRK06839 219 iIVPRKFEP--TKALSMIEK--HKVTVVMGVPTIHQALINCSKFETTNLQS-------------VRWFYNGGAPCPeELM 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 456 LGFLRAalGCQVYEGYGQTEcTAGCTFTTPGD---WTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGY 532
Cdd:PRK06839 282 REFIDR--GFLFGQGFGMTE-TSPTVFMLSEEdarRKVGSIGKPVLFCDYELID-ENKNKVEVGEVGELLIRGPNVMKEY 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 533 LKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVG 612
Cdd:PRK06839 358 WNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQV---------INKLSDVYEVAVVG 426
|
....*..
gi 2230395409 613 ivVPDPE 619
Cdd:PRK06839 427 --RQHVK 431
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
460-619 |
7.86e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 90.49 E-value: 7.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 460 RAALGCQVYEG-YGQTECTAGCTFTTpGDWTSGH--------VGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFK 530
Cdd:PRK06178 348 RALTGSVLAEAaWGMTETHTCDTFTA-GFQDDDFdllsqpvfVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLK 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 531 GYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRsqpvaqiyvHGDSLKAFL 610
Cdd:PRK06178 427 GYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV-NGMSVFPSEVEALLGQ---------HPAVLGSAV 495
|
....*....
gi 2230395409 611 VGivVPDPE 619
Cdd:PRK06178 496 VG--RPDPD 502
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
145-555 |
8.94e-19 |
|
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: 90.38 E-value: 8.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 145 WLSYQEVADRAEFLGSGLLQHNckACTDQFIGVFAQNrPEWIIVELACYTYSMVVVPLYDTLGPGA---IRYIINTADIS 221
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAVG--KPGDRVLLLAPPG-LDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 222 TVIVDKPQKAvLLLEHVERKETPGLKLIILMDPFEEALKERGQKCGVVIKSMqaveHFLL--SGlwprespgSCGNPKGA 299
Cdd:cd05931 101 VVLTTAAALA-AVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDI----AYLQytSG--------STGTPKGV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 300 MLTHGNVVADFSGFLKvtesQWAPTCADVHISYLPLAH-MfermvqsvvychgGRVG------FFQGDIRLLSddmkalc 372
Cdd:cd05931 168 VVTHRNLLANVRQIRR----AYGLDPGDVVVSWLPLYHdM-------------GLIGglltplYSGGPSVLMS------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 373 PTIFpvvprlLNRmydkifsqantPLkRWL-----------------LEFAAKRKQAEVRSGIirndsiwdELffnkiqa 435
Cdd:cd05931 224 PAAF------LRR-----------PL-RWLrlisryratisaapnfaYDLCVRRVRDEDLEGL--------DL------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 436 slgGCVRMIVTGAAPASPTVL----------GFLRAAlgcqVYEGYGQTECTAGCTFTTPG----------DWTSGHV-- 493
Cdd:cd05931 271 ---SSWRVALNGAEPVRPATLrrfaeafapfGFRPEA----FRPSYGLAEATLFVSGGPPGtgpvvlrvdrDALAGRAva 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 494 --------------GAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKE------ALDSDGWLHTGD 553
Cdd:cd05931 344 vaaddpaarelvscGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaATDEGGWLRTGD 423
|
..
gi 2230395409 554 IG 555
Cdd:cd05931 424 LG 425
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
181-611 |
1.41e-18 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 89.74 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 181 NRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDkpQKAVLLLEHVERKETPGLKLIILMDPFEEALK 260
Cdd:PRK08008 71 NCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTS--AQFYPMYRQIQQEDATPLRHICLTRVALPADD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 261 ergqkcGVV----IKSMQAVE---HFLLSGLWPRE---SPGSCGNPKGAMLTHGNVVadFSGFLkvTESQWAPTCADVHI 330
Cdd:PRK08008 149 ------GVSsftqLKAQQPATlcyAPPLSTDDTAEilfTSGTTSRPKGVVITHYNLR--FAGYY--SAWQCALRDDDVYL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 331 SYLPLAHMFermvqsvvychggrvgfFQgdirllsddmkalCPTIFPVvprllnrmydkiFSQANTPLkrwLLE-FAAKR 409
Cdd:PRK08008 219 TVMPAFHID-----------------CQ-------------CTAAMAA------------FSAGATFV---LLEkYSARA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 410 KQAEVRsgiirndsiwdelffnKIQASLGGCVRMIVTG--AAPASPT--------VLGFLRAA----------LGCQVYE 469
Cdd:PRK08008 254 FWGQVC----------------KYRATITECIPMMIRTlmVQPPSANdrqhclreVMFYLNLSdqekdafeerFGVRLLT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 470 GYGQTECTAGCTFTTPGD---WTSghVGAPLPCNHIKLVDveELNYWACKGE-GEICVRG---PNVFKGYLKDPDRTKEA 542
Cdd:PRK08008 318 SYGMTETIVGIIGDRPGDkrrWPS--IGRPGFCYEAEIRD--DHNRPLPAGEiGEICIKGvpgKTIFKEYYLDPKATAKV 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2230395409 543 LDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIyIRSQP-VAQIYVHG--DSL-----KAFLV 611
Cdd:PRK08008 394 LEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVELENI-IATHPkIQDIVVVGikDSIrdeaiKAFVV 468
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
132-618 |
2.99e-18 |
|
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: 88.64 E-value: 2.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 132 PCLGFRKPKQPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTY---SMVVVPLYDTLGp 208
Cdd:cd05921 12 TWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGLSA--ERPLLILSGNSIEHALMALAAMYAgvpAAPVSPAYSLMS- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 209 gairyiintADISTvivdkpqkavllLEHVERKETPGLKLIILMDPFEEALKE-----------RGQKCGVVIKSMQAVE 277
Cdd:cd05921 89 ---------QDLAK------------LKHLFELLKPGLVFAQDAAPFARALAAifplgtplvvsRNAVAGRGAISFAELA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 278 HFLLSG----LWPRESP----------GSCGNPKGAMLTHGNVVADFSGFLkvtesQWAPTCAD---VHISYLPLAHMF- 339
Cdd:cd05921 148 ATPPTAavdaAFAAVGPdtvakflftsGSTGLPKAVINTQRMLCANQAMLE-----QTYPFFGEeppVLVDWLPWNHTFg 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 340 -ERMVQSVVYcHGGRV---------GFFQGDIRLLSDDMkalcPTIFPVVPrllnrmydkifsqantplKRWllefaakr 409
Cdd:cd05921 223 gNHNFNLVLY-NGGTLyiddgkpmpGGFEETLRNLREIS----PTVYFNVP------------------AGW-------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 410 kqaEVRSGIIRNDSIWDELFFNKiqaslggcVRMIVTGAAPASPTVLGFLRA----ALGCQV--YEGYGQTECTAGCTFT 483
Cdd:cd05921 272 ---EMLVAALEKDEALRRRFFKR--------LKLMFYAGAGLSQDVWDRLQAlavaTVGERIpmMAGLGATETAPTATFT 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 484 TPGDWTSGHVGAPLPCNHIKLVdveelnywACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWL----P 559
Cdd:cd05921 341 HWPTERSGLIGLPAPGTELKLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpddP 412
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2230395409 560 AGTLKIIDRKKHIFKLAQGEYVA--PekieniyIRSQPVAQI--YVHgDSL-----KAFLVGIVVPDP 618
Cdd:cd05921 413 AKGLVFDGRVAEDFKLASGTWVSvgP-------LRARAVAACapLVH-DAVvagedRAEVGALVFPDL 472
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
181-589 |
3.03e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 88.68 E-value: 3.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 181 NRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADiSTVIVDKPQKAVLLLEhvERKETPGLKLIILMDP------ 254
Cdd:PRK07786 76 NRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCG-AHVVVTEAALAPVATA--VRDIVPLLSTVVVAGGssddsv 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 255 --FEEALKERGQKCGVV-IksmqavehfllsglwPRESP-------GSCGNPKGAMLTHGNVVADFSGFLKVTEsqwAPT 324
Cdd:PRK07786 153 lgYEDLLAEAGPAHAPVdI---------------PNDSPalimytsGTTGRPKGAVLTHANLTGQAMTCLRTNG---ADI 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 325 CADVHISYLPLAHMfeRMVQSVVychggrVGFFQGdirllsddmkalCPT-IFPVVPRLLNRMYDkifsqantplkrwLL 403
Cdd:PRK07786 215 NSDVGFVGVPLFHI--AGIGSML------PGLLLG------------APTvIYPLGAFDPGQLLD-------------VL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 404 EfaakrkqAEVRSGIIRNDSIWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAgCTF 482
Cdd:PRK07786 262 E-------AEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEMSP-VTC 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 483 TTPGD---WTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSdGWLHTGDIGKWLP 559
Cdd:PRK07786 334 MLLGEdaiRKLGSVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDE 411
|
410 420 430
....*....|....*....|....*....|
gi 2230395409 560 AGTLKIIDRKKHIFkLAQGEYVAPEKIENI 589
Cdd:PRK07786 412 EGYVWVVDRKKDMI-ISGGENIYCAEVENV 440
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
291-619 |
4.24e-18 |
|
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: 87.98 E-value: 4.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 291 GSCGNPKGAMLTHGNVVadfsgflkvtesqwapTCADVHISYLPL----------AHMFERMVQSVVY--CHGG------ 352
Cdd:cd05918 116 GSTGKPKGVVIEHRALS----------------TSALAHGRALGLtsesrvlqfaSYTFDVSILEIFTtlAAGGclcips 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 353 ---RVGFFQGDIRllsdDMKALCPTIFPVVPRLLNRmydkifsqANTPlkrwllefaakrkqaevrsgiirndsiwdelf 429
Cdd:cd05918 180 eedRLNDLAGFIN----RLRVTWAFLTPSVARLLDP--------EDVP-------------------------------- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 430 fnkiqaslggCVRMIVTGAAPASPTVLGflRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPC--------N 500
Cdd:cd05918 216 ----------SLRTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRPLGAtcwvvdpdN 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 501 HIKLVDVeelnywackGE-GEICVRGPNVFKGYLKDPDRTKEA-LDSDGWLH------------TGDIGKWLPAGTLKII 566
Cdd:cd05918 284 HDRLVPI---------GAvGELLIEGPILARGYLNDPEKTAAAfIEDPAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYV 354
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 567 DRKKHIFKLaQGEYVAPEKIENiYIRSQP------VAQIYVH-GDSLKAFLVGIVVPDPE 619
Cdd:cd05918 355 GRKDTQVKI-RGQRVELGEIEH-HLRQSLpgakevVVEVVKPkDGSSSPQLVAFVVLDGS 412
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
459-620 |
5.63e-18 |
|
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: 87.30 E-value: 5.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 459 LRAAL-GCQVYEGYGQTECTAGCTFT--TP---GDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGY 532
Cdd:cd05945 234 LQQRFpDARIYNTYGPTEATVAVTYIevTPevlDGYDRLPIGYAKPGAKLVILD-EDGRPVPPGEKGELVISGPSVSKGY 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 533 LKDPDRTKEALDSD---GWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYV----HGDS 605
Cdd:cd05945 313 LNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIELEEIEAALRQVPGVKEAVVvpkyKGEK 391
|
170
....*....|....*
gi 2230395409 606 lKAFLVGIVVPDPEV 620
Cdd:cd05945 392 -VTELIAFVVPKPGA 405
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
291-628 |
7.33e-18 |
|
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: 86.00 E-value: 7.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 291 GSCGNPKGAMLTHGNVVADfsGFLKVTESQWAPTcaDVHISYLPLAHMFERMVQsvvychgGRVGFFQGDIRLLSDDMKA 370
Cdd:cd05944 12 GTTGTPKLAQHTHSNEVYN--AWMLALNSLFDPD--DVLLCGLPLFHVNGSVVT-------LLTPLASGAHVVLAGPAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 371 LCPTIFPVVPRLLNRMYDKIFSQANTPLkrwllefaAKRKQAEVRSGIirndsiwdelffnkiqaslgGCVRMIVTGAAP 450
Cdd:cd05944 81 RNPGLFDNFWKLVERYRITSLSTVPTVY--------AALLQVPVNADI--------------------SSLRFAMSGAAP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 451 ASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLV--DVEELNYWACKGE--GEICVRG 525
Cdd:cd05944 133 LPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKvlDGVGRLLRDCAPDevGEICVAG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 526 PNVFKGYLKDpDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYVHG-- 603
Cdd:cd05944 213 PGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLRHPAVAFAGAVGqp 290
|
330 340 350
....*....|....*....|....*....|..
gi 2230395409 604 DSLKAFL-VGIV--VPDPEVMP----SWAQKR 628
Cdd:cd05944 291 DAHAGELpVAYVqlKPGAVVEEeellAWARDH 322
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
434-618 |
1.18e-17 |
|
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: 86.58 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 434 QASLGGCVRMIVTGAAPaSPTVLgFLRAALGCQVYEGYGQTEcTAG----CTFTTPGDWTSGHVGAPLPC----NHIKL- 504
Cdd:cd12118 243 ARPLPHRVHVMTAGAPP-PAAVL-AKMEELGFDVTHVYGLTE-TYGpatvCAWKPEWDELPTEERARLKArqgvRYVGLe 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 505 -VDVEELNY-----WACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQG 578
Cdd:cd12118 320 eVDVLDPETmkpvpRDGKTIGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGG 397
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2230395409 579 EYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDP 618
Cdd:cd12118 398 ENISSVEVEGV---------LYKHPAVLEAAVVA--RPDE 426
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
470-621 |
1.75e-17 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 86.40 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 470 GYGQTECTAGCTFTTPGD------WTsghVGAPLPCNHIKLVDVEelnywacKGE-------GEICVRGPNVFKGYLKDP 536
Cdd:PRK08315 347 AYGMTETSPVSTQTRTDDplekrvTT---VGRALPHLEVKIVDPE-------TGEtvprgeqGELCTRGYSVMKGYWNDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 537 DRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivVP 616
Cdd:PRK08315 417 EKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEF---------LYTHPKIQDVQVVG--VP 484
|
....*....
gi 2230395409 617 DP----EVM 621
Cdd:PRK08315 485 DEkygeEVC 493
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
442-618 |
2.65e-17 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 85.88 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 442 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPGD---WTSGHVGAPLPCNHIKLVDvEELNYWACKGE 518
Cdd:PRK13295 315 RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA-VTLTKLDDpdeRASTTDGCPLPGVEVRVVD-ADGAPLPAGQI 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 519 GEICVRGPNVFKGYLKDPDRTkeALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQ 598
Cdd:PRK13295 393 GRLQVRGCSNFGGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEALLYRHPAIAQ 469
|
170 180
....*....|....*....|.
gi 2230395409 599 iyvhgdslkaflVGIV-VPDP 618
Cdd:PRK13295 470 ------------VAIVaYPDE 478
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
291-698 |
3.58e-17 |
|
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: 83.15 E-value: 3.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 291 GSCGNPKGAMLTHGNVVADFSGflkvTESQWAPTCADVHISYLPLAHM--FERMVQSVVycHGGRVGFFQGDiRLLSDDM 368
Cdd:cd17630 10 GSTGTPKAVVHTAANLLASAAG----LHSRLGFGGGDSWLLSLPLYHVggLAILVRSLL--AGAELVLLERN-QALAEDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 369 KALCPTIFPVVPRLLNRMYDKifSQANTPLKRwllefaakrkqaevrsgiirndsiwdelffnkiqaslggcVRMIVTGA 448
Cdd:cd17630 83 APPGVTHVSLVPTQLQRLLDS--GQGPAALKS----------------------------------------LRAVLLGG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 449 APASPTVLGflRAA-LGCQVYEGYGQTEcTAGCTFT-TPGDWTSGHVGAPLPCNHIKLVDveelnywackgEGEICVRGP 526
Cdd:cd17630 121 APIPPELLE--RAAdRGIPLYTTYGMTE-TASQVATkRPDGFGRGGVGVLLPGRELRIVE-----------DGEIWVGGA 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 527 NVFKGYLKDPdrTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIyIRSQP-VAQIYVHGds 605
Cdd:cd17630 187 SLAMGYLRGQ--LVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAA-LAAHPaVRDAFVVG-- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 606 lkaflvgivVPDPEvmpsWAQKrgiegTYADLCTNKDLKKAILEDMVRlgkeSGLHSFEQVKAIHIhsdmfsVQNGLLTP 685
Cdd:cd17630 261 ---------VPDEE----LGQR-----PVAVIVGRGPADPAELRAWLK----DKLARFKLPKRIYP------VPELPRTG 312
|
410
....*....|...
gi 2230395409 686 TLKAKRPELREYF 698
Cdd:cd17630 313 GGKVDRRALRAWL 325
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
146-619 |
8.15e-17 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 84.04 E-value: 8.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 146 LSYQEVADRAEFLGSGLLQHNCKActdqfiG--VFAQ--NRPEWIIVELACYtySMVVVPLYdTLgPG----AIRYIINT 217
Cdd:COG1021 51 LSYAELDRRADRLAAGLLALGLRP------GdrVVVQlpNVAEFVIVFFALF--RAGAIPVF-AL-PAhrraEISHFAEQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 218 ADISTVIVDKpqkAVLLLEHVE-----RKETPGLKLIILMD------PFEEALKERGQKCGVVIkSMQAVEHFLLSGlwp 286
Cdd:COG1021 121 SEAVAYIIPD---RHRGFDYRAlarelQAEVPSLRHVLVVGdageftSLDALLAAPADLSEPRP-DPDDVAFFQLSG--- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 287 respGSCGNPKGAMLTHgnvvADFsgFLKVTESqwAPTCA----DVHISYLPLAHMFErM----VQSVVYcHGGRVgffq 358
Cdd:COG1021 194 ----GTTGLPKLIPRTH----DDY--LYSVRAS--AEICGldadTVYLAALPAAHNFP-LsspgVLGVLY-AGGTV---- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 359 gdirLLSDDMKALcpTIFP-----------VVPRLLNRMydkifsqantplkrwlLEFAAKRKQAevrsgiirndsiwde 427
Cdd:COG1021 256 ----VLAPDPSPD--TAFPlierervtvtaLVPPLALLW----------------LDAAERSRYD--------------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 428 LffnkiqASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctaG-CTFTTPGD--WTSGH-VGAPL-PCNHI 502
Cdd:COG1021 299 L------SSL----RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---GlVNYTRLDDpeEVILTtQGRPIsPDDEV 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 503 KLVD-----VEElnywackGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKK-HIFKl 575
Cdd:COG1021 366 RIVDedgnpVPP-------GEvGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKdQINR- 437
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2230395409 576 aQGEYVAPEKIENiyirsqpvaQIYVHGDSLKAFLVGivVPDPE 619
Cdd:COG1021 438 -GGEKIAAEEVEN---------LLLAHPAVHDAAVVA--MPDEY 469
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
444-636 |
1.44e-16 |
|
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: 82.89 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 444 IVTGAAPASPTVLG-FLRAALGCQVYEGYGQTEctAGCTFTT--PGDWTSGHVGAPLPCNHIKLVDveELNYWACKGE-G 519
Cdd:cd05919 212 LCVSAGEALPRGLGeRWMEHFGGPILDGIGATE--VGHIFLSnrPGAWRLGSTGRPVPGYEIRLVD--EEGHTIPPGEeG 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 520 EICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQI 599
Cdd:cd05919 288 DLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVESLIIQHPAVAEA 365
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2230395409 600 YV----HGDSL---KAFlvgiVVPDPEVMPSWAQKRGIEGTYAD 636
Cdd:cd05919 366 AVvavpESTGLsrlTAF----VVLKSPAAPQESLARDIHRHLLE 405
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
245-587 |
2.68e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 82.35 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 245 GLKLIILMDPFEEA---LKERGqkcgvviksmqaVEHFLLSGLWPRESP-----------------GSCGNPKGAMLTHG 304
Cdd:PRK07768 108 GAKAVVVGEPFLAAapvLEEKG------------IRVLTVADLLAADPIdpvetgeddlalmqltsGSTGSPKAVQITHG 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 305 NVVADFSGFlkVTESQWAPTcADVHISYLPLAH-MfermvqsvvychgGRVGFfqgdirlLSDDMKALC------PTIFP 377
Cdd:PRK07768 176 NLYANAEAM--FVAAEFDVE-TDVMVSWLPLFHdM-------------GMVGF-------LTVPMYFGAelvkvtPMDFL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 378 VVPRLLNRMYDKiFSQANTPLKRWLLEFAAKR--KQAEvrsgiirnDSIWDElffnkiqaslgGCVRMIVTGAAPASPTV 455
Cdd:PRK07768 233 RDPLLWAELISK-YRGTMTAAPNFAYALLARRlrRQAK--------PGAFDL-----------SSLRFALNGAEPIDPAD 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 456 L----------GFLRAALGCqvyeGYGQTECTAGCTFTTPGD--------------------WTSGHV------GAPLPC 499
Cdd:PRK07768 293 VedlldagarfGLRPEAILP----AYGMAEATLAVSFSPCGAglvvdevdadllaalrravpATKGNTrrlatlGPPLPG 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 500 NHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLkDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGE 579
Cdd:PRK07768 369 LEVRVVD-EDGQVLPPRGVGVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GR 445
|
....*...
gi 2230395409 580 YVAPEKIE 587
Cdd:PRK07768 446 NIYPTDIE 453
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
146-618 |
3.49e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 81.90 E-value: 3.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 146 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK08316 37 WTYAELDAAVNRVAAALLDLGLKK-GDR-VAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 226 DkpqkaVLLLEHVErketPGLKLIiLMDPFEEALKERGQkcgVVIKSMQAVEHFLLSGLWPRESP--------------G 291
Cdd:PRK08316 115 D-----PALAPTAE----AALALL-PVDTLILSLVLGGR---EAPGGWLDFADWAEAGSVAEPDVeladddlaqilytsG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 292 SCGNPKGAMLTHGNVVADFSGflKVTESQWAPTcaDVHISYLPLAHMFERMVqsvvychggrvgFFQGDIRLLSDDMKAL 371
Cdd:PRK08316 182 TESLPKGAMLTHRALIAEYVS--CIVAGDMSAD--DIPLHALPLYHCAQLDV------------FLGPYLYVGATNVILD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 372 CPTIfpvvprllNRMYDKIFSQANTPLkrwlleFAAKrkqaevrsgiirndSIWDELF----FNKIQASlggCVRMIVTG 447
Cdd:PRK08316 246 APDP--------ELILRTIEAERITSF------FAPP--------------TVWISLLrhpdFDTRDLS---SLRKGYYG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 448 AAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFTTPGDwtsgHVGAP----LPCNHI--KLVDvEELNYWAcKGE-G 519
Cdd:PRK08316 295 ASIMPVEVLKELRERLpGLRFYNCYGQTEIAPLATVLGPEE----HLRRPgsagRPVLNVetRVVD-DDGNDVA-PGEvG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 520 EICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIyirsqpvaqI 599
Cdd:PRK08316 369 EIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEA---------L 437
|
490
....*....|....*....
gi 2230395409 600 YVHGDSLKAFLVGivVPDP 618
Cdd:PRK08316 438 YTHPAVAEVAVIG--LPDP 454
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
441-618 |
5.60e-16 |
|
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: 81.39 E-value: 5.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 441 VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPG-DWTSGHVGAPLPCNHIKLVDVEELnywACKG-- 517
Cdd:cd05970 303 LRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTL-TIATFPWmEPKPGSMGKPAPGYEIDLIDREGR---SCEAge 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 518 EGEICVRGPN-----VFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIR 592
Cdd:cd05970 379 EGEIVIRTSKgkpvgLFGGYYKDAEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVESALIQ 456
|
170 180
....*....|....*....|....*.
gi 2230395409 593 SQPVAQIYVHGdslkaflvgivVPDP 618
Cdd:cd05970 457 HPAVLECAVTG-----------VPDP 471
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
146-622 |
9.23e-16 |
|
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: 80.44 E-value: 9.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 146 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVG--PESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 226 DKPQKAVLLLehverketpglkliilmdpfeealkergqkcgvviksmqavehfllsglwpreSPGSCGNPKGAMLTHGN 305
Cdd:cd12115 103 DPDDLAYVIY-----------------------------------------------------TSGSTGRPKGVAIEHRN 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 306 VVA------------DFSGFLKVTesqwaPTCADVHI--SYLPLahmfermvqsvvyCHGGRVGFFQGDIRLLsdDMKAL 371
Cdd:cd12115 130 AAAflqwaaaafsaeELAGVLAST-----SICFDLSVfeLFGPL-------------ATGGKVVLADNVLALP--DLPAA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 372 CP-TIFPVVPRLLnrmydkifsqantplkRWLLEFaakrkqaevrsgiirndsiwdelffNKIQASlggcVRMIVTGAAP 450
Cdd:cd12115 190 AEvTLINTVPSAA----------------AELLRH-------------------------DALPAS----VRVVNLAGEP 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 451 ASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFT--TPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPN 527
Cdd:cd12115 225 LPRDLVQRLYARLqVERVVNLYGPSEDTTYSTVApvPPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVPGELYIGGAG 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 528 VFKGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIyIRSQP-VAQ-- 598
Cdd:cd12115 304 VARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAA-LRSIPgVREav 381
|
490 500
....*....|....*....|....*
gi 2230395409 599 IYVHGDSL-KAFLVGIVVPDPEVMP 622
Cdd:cd12115 382 VVAIGDAAgERRLVAYIVAEPGAAG 406
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
470-626 |
9.54e-16 |
|
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: 9.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 470 GYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVE--ELNywacKGE-GEICVRGPNVFKGYLKDPDRTKEALdSD 546
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDgrEVP----DGEvGEIVARGPTVMAGYWNRPEVNARRT-RG 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 547 GWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqgeyvapekIENIY-------IRSQP-VAQIYVhgdslkaflvgIVVPDp 618
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSG---------AENIYpaevercLRQHPaVADAAV-----------IGVPD- 275
|
....*...
gi 2230395409 619 evmPSWAQ 626
Cdd:cd17636 276 ---PRWAQ 280
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
434-618 |
1.04e-15 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 80.83 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 434 QASLGGCVRMIVTGAAPasPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGD-WTSghvgapLPCN------------ 500
Cdd:PLN03102 296 LSPRSGPVHVLTGGSPP--PAALVKKVQRLGFQVMHAYGLTEATGPVLFCEWQDeWNR------LPENqqmelkarqgvs 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 501 HIKLVDVEELNYWAC-------KGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIF 573
Cdd:PLN03102 368 ILGLADVDVKNKETQesvprdgKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII 446
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2230395409 574 kLAQGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGIvvPDP 618
Cdd:PLN03102 447 -ISGGENISSVEVENV---------LYKYPKVLETAVVAM--PHP 479
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
458-618 |
1.06e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 80.32 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 458 FLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKD 535
Cdd:PRK06145 284 FTRVFTRARYIDAYGLTETCSGDTLMEAGREIEkiGSTGRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKD 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 536 PDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIEN-IYIRSQ--PVAQIYVHGDSLKAFLVG 612
Cdd:PRK06145 363 PEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERvIYELPEvaEAAVIGVHDDRWGERITA 440
|
....*.
gi 2230395409 613 IVVPDP 618
Cdd:PRK06145 441 VVVLNP 446
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
442-631 |
2.84e-15 |
|
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: 78.63 E-value: 2.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 442 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEC---TAGCTFTTPGDwtSGHVGAPLPCNHIKLVDvEELNYWACKGE 518
Cdd:cd05971 210 RAIATGGESLGEELLGWAREQFGVEVNEFYGQTECnlvIGNCSALFPIK--PGSMGKPIPGHRVAIVD-DNGTPLPPGEV 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 519 GEICVRGPN--VFKGYLKDPDRTKEALDSDgWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSQPV 596
Cdd:cd05971 287 GEIAVELPDpvAFLGYWNNPSATEKKMAGD-WLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAEIEECLLKHPAV 364
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2230395409 597 AQIYV-------HGDSLKAFlvgiVVPDPEVMPSWAQKRGIE 631
Cdd:cd05971 365 LMAAVvgipdpiRGEIVKAF----VVLNPGETPSDALAREIQ 402
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
146-589 |
3.41e-15 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 80.01 E-value: 3.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 146 LSYQEVADRAEFLGsGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK06814 659 LTYRKLLTGAFVLG-RKLKKNTPP--GENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 226 DKP--QKA--------------VLLLEHVERKETPGLKLIILMDPF--EEALKER-GQKCGVVIksmqavehFllsglwp 286
Cdd:PRK06814 736 SRAfiEKArlgpliealefgirIIYLEDVRAQIGLADKIKGLLAGRfpLVYFCNRdPDDPAVIL--------F------- 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 287 reSPGSCGNPKGAMLTHGNVVA---------DFSGflkvtesqwaptcADVHISYLPLAHMFermvqsvvychggrvGFF 357
Cdd:PRK06814 801 --TSGSEGTPKGVVLSHRNLLAnraqvaariDFSP-------------EDKVFNALPVFHSF---------------GLT 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 358 QGDIRLLSDDMKAL---CPTIFPVVPRLLnrmYDK----IFSqANTPLkrwllefaakrkqaevrSGIIRNDSIWDelFF 430
Cdd:PRK06814 851 GGLVLPLLSGVKVFlypSPLHYRIIPELI---YDTnatiLFG-TDTFL-----------------NGYARYAHPYD--FR 907
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 431 NkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEEL 510
Cdd:PRK06814 908 S---------LRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGI 978
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 511 NywacKGeGEICVRGPNVFKGYLK-DPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENI 589
Cdd:PRK06814 979 D----EG-GRLFVRGPNVMLGYLRaENPGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAVEEL 1051
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
291-623 |
6.08e-15 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 78.39 E-value: 6.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 291 GSCGNPKGAMLTHGNVVADFSGFlkVTESQWAPtcADVHISYLPLAH---MFERMVQSVVycHGGRV-----GFFQGdiR 362
Cdd:PRK05852 186 GTTGLPKMVPWTHANIASSVRAI--ITGYRLSP--RDATVAVMPLYHghgLIAALLATLA--SGGAVllparGRFSA--H 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 363 LLSDDMKALCPTIFPVVPrllnrmydkifsqantPLKRWLLEFAAKRKQAEVRSGIirndsiwdelffnkiqaslggcvR 442
Cdd:PRK05852 258 TFWDDIKAVGATWYTAVP----------------TIHQILLERAATEPSGRKPAAL-----------------------R 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 443 MIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTfTTPGDWtSGHVGAPLPCN---------HIKLV--DVEELN 511
Cdd:PRK05852 299 FIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVT-TTQIEG-IGQTENPVVSTglvgrstgaQIRIVgsDGLPLP 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 512 YWACkgeGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYI 591
Cdd:PRK05852 377 AGAV---GEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLA 451
|
330 340 350
....*....|....*....|....*....|....*
gi 2230395409 592 RSQPVAQIYVHGDSLKAF---LVGIVVPDPEVMPS 623
Cdd:PRK05852 452 SHPNVMEAAVFGVPDQLYgeaVAAVIVPRESAPPT 486
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
279-619 |
3.71e-14 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 75.44 E-value: 3.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 279 FLLSGlwprespGSCGNPKGAMLTHgnvvADFSGFLKVTesqwAPTCA----DVHISYLPLAHMFERM---VQSVVYChG 351
Cdd:cd05920 144 FLLSG-------GTTGTPKLIPRTH----NDYAYNVRAS----AEVCGldqdTVYLAVLPAAHNFPLAcpgVLGTLLA-G 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 352 GRVgffqgdirLLSDDmkALCPTIFPVVPRllnrmyDKIFSQANTP--LKRWLlEFAAKRKQAEvrsgiirndsiwdelf 429
Cdd:cd05920 208 GRV--------VLAPD--PSPDAAFPLIER------EGVTVTALVPalVSLWL-DAAASRRADL---------------- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 430 fnkiqASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHVGAPL-PCNHIKLVDv 507
Cdd:cd05920 255 -----SSL----RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTrLDDPDEVIIHTQGRPMsPDDEIRVVD- 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 508 EELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIE 587
Cdd:cd05920 325 EEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVE 403
|
330 340 350
....*....|....*....|....*....|..
gi 2230395409 588 NiyirsqpvaQIYVHGDSLKAFLVGivVPDPE 619
Cdd:cd05920 404 N---------LLLRHPAVHDAAVVA--MPDEL 424
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
433-601 |
8.33e-14 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 74.14 E-value: 8.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 433 IQASLGGC---VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTfTTPGD-WTSGHVGAPLPCNHIKLVDVE 508
Cdd:cd05974 191 IQQDLASFdvkLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVG-NSPGQpVKAGSMGRPLPGYRVALLDPD 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 509 ElnywACKGEGEICV-----RGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAP 583
Cdd:cd05974 270 G----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SSDYRISP 343
|
170
....*....|....*...
gi 2230395409 584 EKIENIYIRSQPVAQIYV 601
Cdd:cd05974 344 FELESVLIEHPAVAEAAV 361
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
144-628 |
1.09e-13 |
|
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: 73.90 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 144 QWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLyDTLGPGA-IRYIINTADIST 222
Cdd:cd17655 21 QTLTYRELNERANQLARTLREKGVGP--DTIVGIMAERSLEMIVGILGILKAGGAYLPI-DPDYPEErIQYILEDSGADI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 223 VIVDKPQKAVLLlehverketpGLKLIILMDpfEEALKER-GQKCGVVIKSMQAVEHFLLSGlwprespgSCGNPKGAML 301
Cdd:cd17655 98 LLTQSHLQPPIA----------FIGLIDLLD--EDTIYHEeSENLEPVSKSDDLAYVIYTSG--------STGKPKGVMI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 302 THGNVVadfsgflkvtesqwaptcadvhisylplaHMFERMVQSVVYCHGGRVGFFQGdirlLSDDMkalcpTIFPVVPR 381
Cdd:cd17655 158 EHRGVV-----------------------------NLVEWANKVIYQGEHLRVALFAS----ISFDA-----SVTEIFAS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 382 LL--NRMYdkIFSQANTPLKRWLLEFAAKRkqaevRSGIIR-NDSIWDELffNKIQASLGGCVRMIVTGAAPASPTVLGF 458
Cdd:cd17655 200 LLsgNTLY--IVRKETVLDGQALTQYIRQN-----RITIIDlTPAHLKLL--DAADDSEGLSLKHLIVGGEALSTELAKK 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 459 L--RAALGCQVYEGYGQTECTAGCTF--TTPGDWTSGHV--GAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGY 532
Cdd:cd17655 271 IieLFGTNPTITNAYGPTETTVDASIyqYEPETDQQVSVpiGKPLGNTRIYILD-QYGRPQPVGVAGELYIGGEGVARGY 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 533 LKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQ---IYVHG 603
Cdd:cd17655 350 LNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-RGYRIELGEIEARLLQHPDIKEavvIARKD 428
|
490 500
....*....|....*....|....*
gi 2230395409 604 DSLKAFLVGIVVPDPEVMPSWAQKR 628
Cdd:cd17655 429 EQGQNYLCAYIVSEKELPVAQLREF 453
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
132-581 |
2.26e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 73.54 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 132 PCLGFRKPKQ-PYQWLSYQEVADRAEFLGSGLLqhNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVP--------- 201
Cdd:PRK12582 66 PWLAQREPGHgQWRKVTYGEAKRAVDALAQALL--DLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPvspayslms 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 202 --------LYDTLGPGAI-----------RYIINTADISTVIVDKPQKAVLLLEHVERKETPglkliiLMDPFEEALKER 262
Cdd:PRK12582 144 hdhaklkhLFDLVKPRVVfaqsgapfaraLAALDLLDVTVVHVTGPGEGIASIAFADLAATP------PTAAVAAAIAAI 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 263 GqkCGVVIKSMqavehFllsglwpreSPGSCGNPKGAMLTHGNVVADFSGFLKVT-ESQWAPTcaDVHISYLPLAHMFer 341
Cdd:PRK12582 218 T--PDTVAKYL-----F---------TSGSTGMPKAVINTQRMMCANIAMQEQLRpREPDPPP--PVSLDWMPWNHTM-- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 342 mvqsvvychGGRVGFfQGDIR----LLSDDMKALcPTIFPVVPRLLNRMYDKIFsqANTPLKRWLLEFAAKRKQAEVRSg 417
Cdd:PRK12582 278 ---------GGNANF-NGLLWgggtLYIDDGKPL-PGMFEETIRNLREISPTVY--GNVPAGYAMLAEAMEKDDALRRS- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 418 iirndsiwdelFFNKIqaslggcvRMIVTGAAPASPTVLGFLRA----ALGCQV--YEGYGQTEcTAGCTFTTpgDWTS- 490
Cdd:PRK12582 344 -----------FFKNL--------RLMAYGGATLSDDLYERMQAlavrTTGHRIpfYTGYGATE-TAPTTTGT--HWDTe 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 491 --GHVGAPLPCNHIKLVDVEElNYwackgegEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWL----PAGTLK 564
Cdd:PRK12582 402 rvGLIGLPLPGVELKLAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdpddPEKGLI 473
|
490
....*....|....*..
gi 2230395409 565 IIDRKKHIFKLAQGEYV 581
Cdd:PRK12582 474 FDGRVAEDFKLSTGTWV 490
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
445-611 |
3.55e-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: 72.50 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 445 VTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVR 524
Cdd:cd05928 297 VTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIID-DNGNVLPPGTEGDIGIR 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 525 -GPN----VFKGYLKDPDRTKEALDSDGWLhTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQI 599
Cdd:cd05928 376 vKPIrpfgLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYRIGPFEVESALIEHPAVVES 453
|
170
....*....|....*....
gi 2230395409 600 YV-------HGDSLKAFLV 611
Cdd:cd05928 454 AVvsspdpiRGEVVKAFVV 472
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
517-572 |
5.48e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 71.90 E-value: 5.48e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2230395409 517 GE--GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHI 572
Cdd:PRK08162 385 GEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDI 441
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
289-596 |
8.98e-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: 71.37 E-value: 8.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 289 SPGSCGNPKGAMLTHGNVVADFSGFLKVTESqwapTCADVHISYLPLAHmfermvqsvvychggRVGFFQGDIRLLSDDM 368
Cdd:cd05908 114 SSGSTGDPKGVMLTHENLVHNMFAILNSTEW----KTKDRILSWMPLTH---------------DMGLIAFHLAPLIAGM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 369 KA-LCPT-IFPVVPRLLNRMYDK----IFSQANTPLKrWLLEFAAKRKQAEvrsgiirndsiWDElffnkiqaslgGCVR 442
Cdd:cd05908 175 NQyLMPTrLFIRRPILWLKKASEhkatIVSSPNFGYK-YFLKTLKPEKAND-----------WDL-----------SSIR 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 443 MIVTGAAPASP----------TVLGFLRAAlgcqVYEGYGQTECTAGCTF----------------------------TT 484
Cdd:cd05908 232 MILNGAEPIDYelchefldhmSKYGLKRNA----ILPVYGLAEASVGASLpkaqspfktitlgrrhvthgepepevdkKD 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 485 PGDWTSGHVGAPLPCNHIKLVDveELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkWLPAGTL 563
Cdd:cd05908 308 SECLTFVEVGKPIDETDIRICD--EDNKILPDGYiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIRNGRL 384
|
330 340 350
....*....|....*....|....*....|...
gi 2230395409 564 KIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPV 596
Cdd:cd05908 385 VITGREKDII-FVNGQNVYPHDIERIAEELEGV 416
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
291-629 |
1.76e-12 |
|
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: 70.07 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 291 GSCGNPKGAMLTHGNVV-------ADFSGFLKVTESQWAPTCADVhisylplahmferMVQSV--VYCHGGRVGFFQGDI 361
Cdd:cd17651 146 GSTGRPKGVVMPHRSLAnlvawqaRASSLGPGARTLQFAGLGFDV-------------SVQEIfsTLCAGATLVLPPEEV 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 362 RLLSDDMKALCPTifpvvpRLLNRMYdkifsqANTPLKRWLLEfAAKRKQAEvrsgiirndsiwdelffnkiqaslGGCV 441
Cdd:cd17651 213 RTDPPALAAWLDE------QRISRVF------LPTVALRALAE-HGRPLGVR------------------------LAAL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 442 RMIVTG--AAPASPTVLGFLRAALGCQVYEGYGQTE---CTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDvEELNYWAC 515
Cdd:cd17651 256 RYLLTGgeQLVLTEDLREFCAGLPGLRLHNHYGPTEthvVTALSLPGDPAAWPApPPIGRPIDNTRVYVLD-AALRPVPP 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 516 KGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENI 589
Cdd:cd17651 335 GVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGFRIELGEIEAA 413
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2230395409 590 YIRSQPVAQIYV------HGDslkAFLVGIVVPDPEVMPSWAQKRG 629
Cdd:cd17651 414 LARHPGVREAVVlaredrPGE---KRLVAYVVGDPEAPVDAAELRA 456
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
291-628 |
5.48e-12 |
|
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: 68.65 E-value: 5.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 291 GSCGNPKGAMLTHGNVVADFSGFLKvtesqwaptcaDVHISYLPLAHMfermvqsvvychggRVGFFQGDIrLLSDDMKA 370
Cdd:cd17650 103 GTTGKPKGVMVEHRNVAHAAHAWRR-----------EYELDSFPVRLL--------------QMASFSFDV-FAGDFARS 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 371 LCP--TIFPVVPRLL---NRMYDKIFSQ-----ANTP-LKRWLLEFAAKRKQ--AEVRSGIIRNDSIWDElFFNKIQASL 437
Cdd:cd17650 157 LLNggTLVICPDEVKldpAALYDLILKSritlmESTPaLIRPVMAYVYRNGLdlSAMRLLIVGSDGCKAQ-DFKTLAARF 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 438 GGCVRMIvtgaapaspTVLGFLRAALGCQVYEGYGQTECTAGctfTTPgdwtsghVGAPLPCNHIKLVDvEELNYWACKG 517
Cdd:cd17650 236 GQGMRII---------NSYGVTEATIDSTYYEEGRDPLGDSA---NVP-------IGRPLPNTAMYVLD-ERLQPQPVGV 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 518 EGEICVRGPNVFKGYLKDPDRTKEALDSDGW------LHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYI 591
Cdd:cd17650 296 AGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI-RGFRIELGEIESQLA 374
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2230395409 592 RSQPVAQIYV---HGDSLKAFLVGIVVPDPEvmPSWAQKR 628
Cdd:cd17650 375 RHPAIDEAVVavrEDKGGEARLCAYVVAAAT--LNTAELR 412
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
435-620 |
8.41e-12 |
|
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: 68.00 E-value: 8.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 435 ASLGGcVRMIVTGAAPASPT-VLGFLRAALGCQVYEGYGQTECTagcTFTT-----PGDWTSGHV--GAPLPCNHIKLVD 506
Cdd:cd12117 246 ECFAG-LRELLTGGEVVSPPhVRRVLAACPGLRLVNGYGPTENT---TFTTshvvtELDEVAGSIpiGRPIANTRVYVLD 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 507 veELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKIIDRKKHIFKLaQGE 579
Cdd:cd12117 322 --EDGRPVPPGVpGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI-RGF 398
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2230395409 580 YVAPEKIENIyIRSQP-VAQIYV---HGDSLKAFLVGIVVPDPEV 620
Cdd:cd12117 399 RIELGEIEAA-LRAHPgVREAVVvvrEDAGGDKRLVAYVVAEGAL 442
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
441-611 |
8.62e-12 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 68.33 E-value: 8.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 441 VRMIVTGAAPaSPTVLgFLRAALGCQVYEGYGQTEcTAG----CTFTTPGDWTSGHVGAPLPCNH---------IKLVDV 507
Cdd:PLN02479 313 VHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSE-TYGpstvCAWKPEWDSLPPEEQARLNARQgvryiglegLDVVDT 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 508 EELNYWACKGE--GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEK 585
Cdd:PLN02479 390 KTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGGENISSLE 467
|
170 180
....*....|....*....|....*.
gi 2230395409 586 IENIyirsqpvaqIYVHGDSLKAFLV 611
Cdd:PLN02479 468 VENV---------VYTHPAVLEASVV 484
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
289-589 |
1.00e-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: 66.90 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 289 SPGSCGNPKGAMLTHGNVVADFSGFLKvteSQWAPTCADVHISYLPLAHMFE--RMVQSVVYcHGGRVGFfqGDIRLLSD 366
Cdd:cd17635 9 TSGTTGEPKAVLLANKTFFAVPDILQK---EGLNWVVGDVTYLPLPATHIGGlwWILTCLIH-GGLCVTG--GENTTYKS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 367 DMKAL---CPTIFPVVPRLLNRMYDKIFSQANTPLKRWLLEFAAKRkqaevrsgIIRNDSIWDELFFNkiqaslggcvrm 443
Cdd:cd17635 83 LFKILttnAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSR--------AIAADVRFIEATGL------------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 444 ivtgaapasptvlgflraalgCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDVEELNYWAcKGEGEIC 522
Cdd:cd17635 143 ---------------------TNTAQVYGLSETGTALCLPTDDDSIEiNAVGRPYPGVDVYLAATDGIAGPS-ASFGTIW 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2230395409 523 VRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENI 589
Cdd:cd17635 201 IKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERI 265
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
440-695 |
1.15e-11 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 67.90 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 440 CVRMIVTGAAPASP-----TVLGFLRAALgcqvYEGYGQTECTAGCTFTTPGDWT-----------------SGH----- 492
Cdd:PLN02860 289 SVRKILNGGGSLSSrllpdAKKLFPNAKL----FSAYGMTEACSSLTFMTLHDPTlespkqtlqtvnqtkssSVHqpqgv 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 493 -VGAPLPcnHIKLvdveELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKH 571
Cdd:PLN02860 365 cVGKPAP--HVEL----KIGLDESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSND 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 572 IFKlAQGEYVAPEKIENIYIRSQPVAQIYVHGdSLKAFLVGIVVPDPEVMPSWaqkRGIEGTYADLCTNKDLKKAILEDM 651
Cdd:PLN02860 439 RIK-TGGENVYPEEVEAVLSQHPGVASVVVVG-VPDSRLTEMVVACVRLRDGW---IWSDNEKENAKKNLTLSSETLRHH 513
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2230395409 652 VRlgkESGLHSFEQVKAIHIHSDMFSvqnglLTPTLKAKRPELR 695
Cdd:PLN02860 514 CR---EKNLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEVR 549
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
448-619 |
1.51e-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: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 448 AAPASPTVLGFLRAALGCQVYEGYGQTECTaGCTFTTPGDWTS--GHVGAPLPcNHIKLVDvEELNYWACKGEGEICVRG 525
Cdd:cd05929 253 AAPCPPWVKEQWIDWGGPIIWEYYGGTEGQ-GLTIINGEEWLThpGSVGRAVL-GKVHILD-EDGNEVPPGEIGEVYFAN 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 526 PNVFKgYLKDPDRTKEALDSDGWLHTGDIGkWLPA-GTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRsqpvaqiyvHGD 604
Cdd:cd05929 330 GPGFE-YTNDPEKTAAARNEGGWSTLGDVG-YLDEdGYLYLTDRRSDMI-ISGGVNIYPQEIENALIA---------HPK 397
|
170
....*....|....*
gi 2230395409 605 SLKAFLVGivVPDPE 619
Cdd:cd05929 398 VLDAAVVG--VPDEE 410
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
460-618 |
1.59e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 67.37 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 460 RAALGCQVYEGYGQTECTAGCTFTTP-----GDWTSGHVGaplPCNH--------IKLVDVEELNywacKGE-GEICVRG 525
Cdd:PRK07470 301 LAKLGKVLVQYFGLGEVTGNITVLPPalhdaEDGPDARIG---TCGFertgmevqIQDDEGRELP----PGEtGEICVIG 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 526 PNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENiyirsqpvaQIYVHGDS 605
Cdd:PRK07470 374 PAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPREIEE---------KLLTHPAV 442
|
170
....*....|...
gi 2230395409 606 LKAFLVGivVPDP 618
Cdd:PRK07470 443 SEVAVLG--VPDP 453
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
146-603 |
2.67e-11 |
|
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: 66.38 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVI- 224
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRP--GQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVi 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 225 -VDKP--QKAVLLLEHVER-KETPGLK-LIILMDPFEEALKERGQKCGVviksmqavehFLLSGlwprespgSCGNPKGA 299
Cdd:cd05923 107 aVDAQvmDAIFQSGVRVLAlSDLVGLGePESAGPLIEDPPREPEQPAFV----------FYTSG--------TTGLPKGA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 300 MLTHgNVVADFSGFLkVTESQWAPTCADVHISYLPLAHMfermvqsvvychggrVGFFQgdirLLSDDMkALCPTIFPVv 379
Cdd:cd05923 169 VIPQ-RAAESRVLFM-STQAGLRHGRHNVVLGLMPLYHV---------------IGFFA----VLVAAL-ALDGTYVVV- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 380 prllnrmydKIFSQANtplkrwllefAAKRKQAEVRSGIIRNDSIWDELFFNKIQASLG-GCVRMIVTGAAPASPTVLGF 458
Cdd:cd05923 226 ---------EEFDPAD----------ALKLIEQERVTSLFATPTHLDALAAAAEFAGLKlSSLRHVTFAGATMPDAVLER 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 459 LRAALGCQVYEGYGQTECTagcTFTTPGDWTSGHVGAPLPCNHIKLVDV-EELNYWACKG-EGEICVR--GPNVFKGYLK 534
Cdd:cd05923 287 VNQHLPGEKVNIYGTTEAM---NSLYMRDARTGTEMRPGFFSEVRIVRIgGSPDEALANGeEGELIVAaaADAAFTGYLN 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2230395409 535 DPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYVHG 603
Cdd:cd05923 364 QPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIG 430
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
453-601 |
3.43e-11 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 66.05 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 453 PTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTSGhVGAPLPCNHIKLVDveelnywackgeGEICVRGPNVFKGY 532
Cdd:PRK09029 253 PVELTEQAEQQGIRCWCGYGLTE-MASTVCAKRADGLAG-VGSPLPGREVKLVD------------GEIWLRGASLALGY 318
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2230395409 533 LKDpDRTKEALDSDGWLHTGDIGKWLpAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYV 601
Cdd:PRK09029 319 WRQ-GQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQVFV 384
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
519-622 |
5.31e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 65.53 E-value: 5.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 519 GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQ 598
Cdd:PRK06164 378 GEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNPAEIEHALEALPGVAA 456
|
90 100
....*....|....*....|....*.
gi 2230395409 599 IYVHGDSL--KAFLVGIVVPDPEVMP 622
Cdd:PRK06164 457 AQVVGATRdgKTVPVAFVIPTDGASP 482
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
442-623 |
5.34e-11 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 65.49 E-value: 5.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 442 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCNHIKLVDvEELNYWACKGEG 519
Cdd:PRK12406 274 RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE-SGAVTFATSEDALShpGTVGKAAPGAELRFVD-EDGRPLPQGEIG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 520 EICVRGPNV--FKgYLKDPDRTKEaLDSDGWLHTGDIGkWLPA-GTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPV 596
Cdd:PRK12406 352 EIYSRIAGNpdFT-YHNKPEKRAE-IDRGGFITSGDVG-YLDAdGYLFLCDRKRDMV-ISGGVNIYPAEIEAVLHAVPGV 427
|
170 180 190
....*....|....*....|....*....|
gi 2230395409 597 AQIYVHGDSLKAF---LVGIVVPDPEVMPS 623
Cdd:PRK12406 428 HDCAVFGIPDAEFgeaLMAVVEPQPGATLD 457
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
291-619 |
5.45e-11 |
|
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: 65.41 E-value: 5.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 291 GSCGNPKGAMLTHGNVVADFSGflkvTESQWAPTCADVHISYLPLAHMFermvqSV-----VYCHGGRVGFFQGDIRLLS 365
Cdd:cd17643 103 GSTGRPKGVVVSHANVLALFAA----TQRWFGFNEDDVWTLFHSYAFDF-----SVweiwgALLHGGRLVVVPYEVARSP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 366 DDMkalcptifpvvPRLLNRMYDKIFSQanTPLkrwllefAAKRKQAEVRSGIIRNDSIwdelffnkiqaslggcvRMIV 445
Cdd:cd17643 174 EDF-----------ARLLRDEGVTVLNQ--TPS-------AFYQLVEAADRDGRDPLAL-----------------RYVI 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 446 TGAAPASPTVLGFLRAALGC---QVYEGYGQTECTAGCTFT--TPGDW---TSGHVGAPLPCNHIKLVDvEELNYWACKG 517
Cdd:cd17643 217 FGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFRplDAADLpaaAASPIGRPLPGLRVYVLD-ADGRPVPPGV 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 518 EGEICVRGPNVFKGYLKDPDRTKE-------ALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIY 590
Cdd:cd17643 296 VGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI-RGFRIELGEIEAAL 374
|
330 340 350
....*....|....*....|....*....|..
gi 2230395409 591 IRSQPVAQIYV---HGDSLKAFLVGIVVPDPE 619
Cdd:cd17643 375 ATHPSVRDAAVivrEDEPGDTRLVAYVVADDG 406
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
441-607 |
5.57e-11 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 65.89 E-value: 5.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 441 VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNywacKGeGE 520
Cdd:PRK08043 481 LRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIE----QG-GR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 521 ICVRGPNVFKGYLK--DPDRTK-------EALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYI 591
Cdd:PRK08043 556 LQLKGPNIMNGYLRveKPGVLEvptaenaRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIA-GEMVSLEMVEQLAL 634
|
170
....*....|....*.
gi 2230395409 592 RSQPVAQiyvHGDSLK 607
Cdd:PRK08043 635 GVSPDKQ---HATAIK 647
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
441-630 |
7.47e-11 |
|
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: 65.08 E-value: 7.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 441 VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTF--TTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGE 518
Cdd:cd05959 282 LRLCVSAGEALPAEVGERWKARFGLDILDGIGSTE--MLHIFlsNRPGRVRYGTTGKPVPGYEVELRD-EDGGDVADGEP 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 519 GEICVRGPNVFKGYLKDPDRTKEALDSdGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQ 598
Cdd:cd05959 359 GELYVRGPSSATMYWNNRDKTRDTFQG-EWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSPFEVESALVQHPAVLE 436
|
170 180 190
....*....|....*....|....*....|....*....
gi 2230395409 599 IYVHG-------DSLKAFlvgiVVPDPEVMPSWAQKRGI 630
Cdd:cd05959 437 AAVVGvededglTKPKAF----VVLRPGYEDSEALEEEL 471
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
146-627 |
3.04e-10 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 63.26 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 146 LSYQEVADRAEFLGSGLlQHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK05620 39 TTFAAIGARAAALAHAL-HDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 226 D---KPQKAVLLlehverKETPGLKLIILMDPFEEALKERGQKCGVVIKSMQAvehfLLSGL-----WPRE--------- 288
Cdd:PRK05620 118 DprlAEQLGEIL------KECPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEA----LLDGRstvydWPELdettaaaic 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 289 -SPGSCGNPKGAMLTHGNVVADfSGFLKVTESqWAPTCADVHISYLPLAHMFERMVQSVVYCHGGrvgffqgdirllsdd 367
Cdd:PRK05620 188 ySTGTTGAPKGVVYSHRSLYLQ-SLSLRTTDS-LAVTHGESFLCCVPIYHVLSWGVPLAAFMSGT--------------- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 368 mkalcPTIFP----VVPRLLnrmydKIFSqanTPLKRwllefaakrkqaeVRSGIirnDSIWDELFFNKIQ-----ASLg 438
Cdd:PRK05620 251 -----PLVFPgpdlSAPTLA-----KIIA---TAMPR-------------VAHGV---PTLWIQLMVHYLKnpperMSL- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 439 gcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGA---------PLPCNHiKLVDVEE 509
Cdd:PRK05620 301 ---QEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEARWayrvsqgrfPASLEY-RIVNDGQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 510 LNYWACKGEGEICVRGPNVFKGYLKDP----------------DRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIF 573
Cdd:PRK05620 377 VMESTDRNEGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVI 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2230395409 574 KlAQGEYVAPEKIENIYIRSQPVaqiyvhgdsLKAFLVGIvvPDPEvmpsWAQK 627
Cdd:PRK05620 457 R-SGGEWIYSAQLENYIMAAPEV---------VECAVIGY--PDDK----WGER 494
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
146-622 |
3.87e-10 |
|
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: 62.67 E-value: 3.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 146 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVR--PGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 226 DKPQkaVLLLEHVERKETPGLKLIILMDPFEEALKERGQKCGVVIKSmqavehfllsglwprespGSCGNPKGAMLTHG- 304
Cdd:cd12114 91 DGPD--AQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTS------------------GSTGTPKGVMISHRa 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 305 --NVVADfsgflkvTESQWAPTCADVHISYLPLAHMFermvqSV-----VYCHGGRVgffqgdirllsddmkalcptifp 377
Cdd:cd12114 151 alNTILD-------INRRFAVGPDDRVLALSSLSFDL-----SVydifgALSAGATL----------------------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 378 VVPRLlnrmydkifSQANTPlKRWllefaakrKQAEVRSGIirndSIWdelffNKIQASLGgcvrMIVTgAAPASPTVLG 457
Cdd:cd12114 196 VLPDE---------ARRRDP-AHW--------AELIERHGV----TLW-----NSVPALLE----MLLD-VLEAAQALLP 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 458 FLRAAL-------------------GCQVYEGYGQTECTAGCTF----TTPGDWTSGHVGAPLPCNHIKLVDV--EELNY 512
Cdd:cd12114 244 SLRLVLlsgdwipldlparlralapDARLISLGGATEASIWSIYhpidEVPPDWRSIPYGRPLANQRYRVLDPrgRDCPD 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 513 WackGEGEICVRGPNVFKGYLKDPDRTKEAL--DSDG--WLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIEN 588
Cdd:cd12114 324 W---VPGELWIGGRGVALGYLGDPELTAARFvtHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKV-RGYRIELGEIEA 399
|
490 500 510
....*....|....*....|....*....|....*.
gi 2230395409 589 IYIRSQPVAQ--IYVHGDSLKAFLVGIVVPDPEVMP 622
Cdd:cd12114 400 ALQAHPGVARavVVVLGDPGGKRLAAFVVPDNDGTP 435
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
95-601 |
4.23e-10 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 62.85 E-value: 4.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 95 ARRSVIGSGPQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRKpkqpyQWLSYQEVADRAEFLGSGLLQHNCKAcTDQf 174
Cdd:PRK06155 1 GEPLGAGLAARAVDPLPPSERTLPAMLARQAERYPDRPLLVFGG-----TRWTYAEAARAAAAAAHALAAAGVKR-GDR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 175 IGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlLLEHVERKETPGLKL--IILM 252
Cdd:PRK06155 74 VALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAA-----LLAALEAADPGDLPLpaVWLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 253 DPFEEALKERGQKCGVVIKSMQAVEhflLSGLWPRE------SPGSCGNPKGAMLTHG-------NVVADfsgfLKVTES 319
Cdd:PRK06155 149 DAPASVSVPAGWSTAPLPPLDAPAP---AAAVQPGDtaailyTSGTTGPSKGVCCPHAqfywwgrNSAED----LEIGAD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 320 qwaptcaDVHISYLPLAH------MFERMVQSVVYCHGGRV---GFFqgdirllsDDMKALCPTIFpvvpRLLNRMYDKI 390
Cdd:PRK06155 222 -------DVLYTTLPLFHtnalnaFFQALLAGATYVLEPRFsasGFW--------PAVRRHGATVT----YLLGAMVSIL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 391 FSQANTPLKRwllefaakrkqaevrsgiirndsiwdelffnkiqaslGGCVRMIVTGAAPASptVLGFLRAALGCQVYEG 470
Cdd:PRK06155 283 LSQPARESDR-------------------------------------AHRVRVALGPGVPAA--LHAAFRERFGVDLLDG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 471 YGQTECTAGCtFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWAckGE-GEICVRG--PNVF-KGYLKDPDRTKEALdSD 546
Cdd:PRK06155 324 YGSTETNFVI-AVTHGSQRPGSMGRLAPGFEARVVDEHDQELPD--GEpGELLLRAdePFAFaTGYFGMPEKTVEAW-RN 399
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2230395409 547 GWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENIyIRSQP-VAQIYV 601
Cdd:PRK06155 400 LWFHTGDRVVRDADGWFRFVDRIKDAIR-RRGENISSFEVEQV-LLSHPaVAAAAV 453
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
441-580 |
6.00e-10 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 62.22 E-value: 6.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 441 VRMIVTGAAPASPTVLGFLRAAL--GCQVYEGYGQTECTAGCT-------FTTPGDWTSGH---VGAPLPCNHIKLVDV- 507
Cdd:PRK09274 290 LRRVISAGAPVPIAVIERFRAMLppDAEILTPYGATEALPISSiesreilFATRAATDNGAgicVGRPVDGVEVRIIAIs 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 508 -EELNYWA-----CKGE-GEICVRGPNVFKGYLKDPDRTKEA--LDSDG--WLHTGDIGkWL-PAGTLKIIDRKKHIFKL 575
Cdd:PRK09274 370 dAPIPEWDdalrlATGEiGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLG-YLdAQGRLWFCGRKAHRVET 448
|
....*
gi 2230395409 576 AQGEY 580
Cdd:PRK09274 449 AGGTL 453
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
451-620 |
6.02e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 62.39 E-value: 6.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 451 ASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTTPGDWTSGHVGaPLPCNhIKLVDVE--------------ELNYWACK 516
Cdd:PRK07867 277 GAPGDIARFARRFGCVVVDGFGSTE--GGVAITRTPDTPPGALG-PLPPG-VAIVDPDtgtecppaedadgrLLNADEAI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 517 GEgEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPV 596
Cdd:PRK07867 353 GE-LVNTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPIERILLRYPDA 429
|
170 180
....*....|....*....|....
gi 2230395409 597 AQIYVHGdslkaflvgivVPDPEV 620
Cdd:PRK07867 430 TEVAVYA-----------VPDPVV 442
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
441-619 |
1.43e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 61.07 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 441 VRMIVTGAAPASPTVLgflRAAL---GCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCNhIKLVDvEELNYWAC 515
Cdd:PRK08276 264 LRVAIHAAAPCPVEVK---RAMIdwwGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGE-VRILD-EDGNELPP 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 516 KGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkWLPA-GTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQ 594
Cdd:PRK08276 338 GEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVG-YLDEdGYLYLTDRKSDMI-ISGGVNIYPQEIENLLVTHP 415
|
170 180
....*....|....*....|....*
gi 2230395409 595 PVAQIYVHGdslkaflvgivVPDPE 619
Cdd:PRK08276 416 KVADVAVFG-----------VPDEE 429
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
296-591 |
1.63e-09 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 60.99 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 296 PKGAMLTHGNVVADFSGFLKVtesqWAPTCADVHISYLPLAHMFermvqsvvychggrvGFFqgdirllsddmkalCPTI 375
Cdd:PRK06334 198 PKGVPLTHANLLANQRACLKF----FSPKEDDVMMSFLPPFHAY---------------GFN--------------SCTL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 376 FPVVPRLlnrmyDKIFSQanTPLK-RWLLEFAAKRKQAEVRSGIIRNDSIwdeLFFNKIQASLGGCVRMIVTGAAPASPT 454
Cdd:PRK06334 245 FPLLSGV-----PVVFAY--NPLYpKKIVEMIDEAKVTFLGSTPVFFDYI---LKTAKKQESCLPSLRFVVIGGDAFKDS 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 455 VL-GFLRAALGCQVYEGYGQTECTAGCTFTT---PGDwtSGHVGAPLPCNHIKLVDvEELNYWACKGE-GEICVRGPNVF 529
Cdd:PRK06334 315 LYqEALKTFPHIQLRQGYGTTECSPVITINTvnsPKH--ESCVGMPIRGMDVLIVS-EETKVPVSSGEtGLVLTRGTSLF 391
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2230395409 530 KGYL-KDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYI 591
Cdd:PRK06334 392 SGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSLEALESILM 453
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
464-627 |
2.11e-09 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 60.26 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 464 GCQVYEGYGQTECTAGCT-FTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEA 542
Cdd:cd17645 234 GYKLVNNYGPTENTVVATsFEIDKPYANIPIGKPIDNTRVYILD-EALQLQPIGVAGELCIAGEGLARGYLNRPELTAEK 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 543 LDSDGWL------HTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENI---YIRSQPVAQIYVHGDSLKAFLVGI 613
Cdd:cd17645 313 FIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIEPFlmnHPLIELAAVLAKEDADGRKYLVAY 391
|
170
....*....|....*...
gi 2230395409 614 VVP----DPEVMPSWAQK 627
Cdd:cd17645 392 VTApeeiPHEELREWLKN 409
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
442-597 |
3.31e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 60.11 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 442 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPgdwTSGHVGAPLPCNH--------------IKLVDV 507
Cdd:PRK07008 296 RRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLCKL---KWKHSQLPLDEQRkllekqgrviygvdMKIVGD 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 508 E--ELNyWACKGEGEICVRGPNVFKGYLKdpdRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEK 585
Cdd:PRK07008 373 DgrELP-WDGKAFGDLQVRGPWVIDRYFR---GDASPLV-DGWFPTGDVATIDADGFMQITDRSKDVIK-SGGEWISSID 446
|
170
....*....|..
gi 2230395409 586 IENIYIRSQPVA 597
Cdd:PRK07008 447 IENVAVAHPAVA 458
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
441-616 |
3.96e-09 |
|
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: 59.40 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 441 VRMIVTGAAPASPTVLGFLRAAL--GCQVYEGYGQTECTAGCT------FTTPGDWTSGH----VGAPLPCNHIKLV--D 506
Cdd:cd05910 201 LRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrelLATTTAATSGGagtcVGRPIPGVRVRIIeiD 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 507 VEELNYWACKGE------GEICVRGPNVFKGYLKDPDRTKEALDSDG----WLHTGDIGKWLPAGTLKIIDRKKHIFKLA 576
Cdd:cd05910 281 DEPIAEWDDTLElprgeiGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITT 360
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2230395409 577 QGEYVapekieniyirSQPVAQIY-VHGDSLKAFLVGIVVP 616
Cdd:cd05910 361 GGTLY-----------TEPVERVFnTHPGVRRSALVGVGKP 390
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
434-619 |
4.07e-09 |
|
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: 59.60 E-value: 4.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 434 QASLGGC--VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHV--GAPLPCNHIKLVDvE 508
Cdd:cd17646 246 EPAAGSCasLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVThWPVRGPAETPSVpiGRPVPNTRLYVLD-D 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 509 ELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH------TGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVA 582
Cdd:cd17646 325 ALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKI-RGFRVE 403
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2230395409 583 PEKIENIyIRSQP-VAQIYV---HGDSLKAFLVGIVVPDPE 619
Cdd:cd17646 404 PGEIEAA-LAAHPaVTHAVVvarAAPAGAARLVGYVVPAAG 443
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
444-628 |
6.00e-09 |
|
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: 58.80 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 444 IVTGAAPASPTVLgflRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEIC 522
Cdd:cd17652 210 VVAGEACPAELVD---RWAPGRRMINAYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYVLD-ARLRPVPPGVPGELY 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 523 VRGPNVFKGYLKDPDRTKEALDSD------GWLH-TGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQP 595
Cdd:cd17652 286 IAGAGLARGYLNRPGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKI-RGFRIELGEVEAALTEHPG 364
|
170 180 190
....*....|....*....|....*....|....*.
gi 2230395409 596 VAQ--IYVHGDSL-KAFLVGIVVPDPEVMPSWAQKR 628
Cdd:cd17652 365 VAEavVVVRDDRPgDKRLVAYVVPAPGAAPTAAELR 400
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
442-618 |
6.94e-09 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 58.85 E-value: 6.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 442 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT---------FTT------PGD--WTSGHVGAPLPCNHIkl 504
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAEGLVNYTrlddsderiFTTqgrpmsPDDevWVADADGNPLPQGEV-- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 505 vdveelnywackgeGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHifklaQ----GEY 580
Cdd:PRK10946 381 --------------GRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGEK 441
|
170 180 190
....*....|....*....|....*....|....*...
gi 2230395409 581 VAPEKIENIYIRsqpvaqiyvHGDSLKAFLVGIvvPDP 618
Cdd:PRK10946 442 IAAEEIENLLLR---------HPAVIHAALVSM--EDE 468
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
146-620 |
1.70e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 57.71 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 146 LSYQEVADRAEFLGSGLlqHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIv 225
Cdd:PRK13390 25 VSYRQLDDDSAALARVL--YDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLV- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 226 dkpqkAVLLLEHVERKETPGLKLIILMD-------PFEEALKERG-----QKCGVVIksmqavehfllsgLWpreSPGSC 293
Cdd:PRK13390 102 -----ASAALDGLAAKVGADLPLRLSFGgeidgfgSFEAALAGAGprlteQPCGAVM-------------LY---SSGTT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 294 GNPKG--------AMLTHGN-VVADFSGFLKVTESqwaptcaDVHISYLPLAHMFERMVQSVVYCHGGRVGFFQG-DIRL 363
Cdd:PRK13390 161 GFPKGiqpdlpgrDVDAPGDpIVAIARAFYDISES-------DIYYSSAPIYHAAPLRWCSMVHALGGTVVLAKRfDAQA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 364 LSDDMKALCPTIFPVVPRLLNRMYdkifsqantplkrwllefaakRKQAEVRSgiiRNDSiwdelffnkiqASLggcvRM 443
Cdd:PRK13390 234 TLGHVERYRITVTQMVPTMFVRLL---------------------KLDADVRT---RYDV-----------SSL----RA 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 444 IVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVG-APLPCNHIKLVDVEELNywackgEGE 520
Cdd:PRK13390 275 VIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGrSVLGDLHICDDDGNELP------AGR 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 521 IcvrGPNVFK------GYLKDPDRTKEALDSDG--WLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIR 592
Cdd:PRK13390 348 I---GTVYFErdrlpfRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQETENALTM 423
|
490 500
....*....|....*....|....*...
gi 2230395409 593 SQPVAQIYVHGdslkaflvgivVPDPEV 620
Cdd:PRK13390 424 HPAVHDVAVIG-----------VPDPEM 440
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
442-603 |
2.29e-08 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 57.07 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 442 RMIVTGAApASPTvlGFLRA--ALGCQVYEGYGQTECTAGCTFTT--------PGDWTSGHV---GAPLPCNHIKLVDVE 508
Cdd:PRK06018 297 KMVVCGGS-AMPR--SMIKAfeDMGVEVRHAWGMTEMSPLGTLAAlkppfsklPGDARLDVLqkqGYPPFGVEMKITDDA 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 509 --ELNyWACKGEGEICVRGPNVFKGYLKDPDrtkEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKI 586
Cdd:PRK06018 374 gkELP-WDGKTFGRLKVRGPAVAAAYYRVDG---EILDDDGFFDTGDVATIDAYGYMRITDRSKDVIK-SGGEWISSIDL 448
|
170
....*....|....*..
gi 2230395409 587 ENIYIRSQPVAQIYVHG 603
Cdd:PRK06018 449 ENLAVGHPKVAEAAVIG 465
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
437-623 |
2.65e-08 |
|
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: 56.72 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 437 LGGCVRMIVTgAAPASPTVLGFL-RAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDveELNYWAC 515
Cdd:cd05958 211 DLSSLRKCVS-AGEALPAALHRAwKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD--DEGNPVP 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 516 KGE-GEICVRGPNVFKgYLKDPDRTKEAldSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSQ 594
Cdd:cd05958 288 DGTiGRLAVRGPTGCR-YLADKRQRTYV--QGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQHP 363
|
170 180 190
....*....|....*....|....*....|..
gi 2230395409 595 PVAQIYVHGDSLKAFLV---GIVVPDPEVMPS 623
Cdd:cd05958 364 AVAECAVVGHPDESRGVvvkAFVVLRPGVIPG 395
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
144-612 |
3.90e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 57.27 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 144 QWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLyDTLGPGA-IRYIINTADIST 222
Cdd:PRK12316 2027 QHLSYAELDSRANRLAHRLRARGVGP--EVRVAIAAERSFELVVALLAVLKAGGAYVPL-DPNYPAErLAYMLEDSGAAL 2103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 223 VIVDKPQKAVLLLehverkeTPGLKLIILMDPfeEALKERGQKCGVVIKSMQAVEHFLLSGlwprespGSCGNPKGAMLT 302
Cdd:PRK12316 2104 LLTQRHLLERLPL-------PAGVARLPLDRD--AEWADYPDTAPAVQLAGENLAYVIYTS-------GSTGLPKGVAVS 2167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 303 HGNVVAdfsgFLKVTESQWAPTCADVHISYLPLAhmFERMVQSVVY--CHGGRVgffqgdirLLSDDMKalcptifpvvp 380
Cdd:PRK12316 2168 HGALVA----HCQAAGERYELSPADCELQFMSFS--FDGAHEQWFHplLNGARV--------LIRDDEL----------- 2222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 381 RLLNRMYDKIFSQANTplkrwLLEFAAKRKQAEVRsgiirndsiwdelffnkiQASLGGC---VRMIVTGAAPASPTVLG 457
Cdd:PRK12316 2223 WDPEQLYDEMERHGVT-----ILDFPPVYLQQLAE------------------HAERDGRppaVRVYCFGGEAVPAASLR 2279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 458 FLRAALGCQ-VYEGYGQTEctagcTFTTPGDWTSGH----------VGAPLPCNHIKLVDvEELNYWACKGEGEICVRGP 526
Cdd:PRK12316 2280 LAWEALRPVyLFNGYGPTE-----AVVTPLLWKCRPqdpcgaayvpIGRALGNRRAYILD-ADLNLLAPGMAGELYLGGE 2353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 527 NVFKGYLKDPDRTKEALDSDGWLH-------TGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENiYIRSQP---- 595
Cdd:PRK12316 2354 GLARGYLNRPGLTAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKI-RGFRIELGEIEA-RLQAHPavre 2431
|
490 500
....*....|....*....|
gi 2230395409 596 ---VAQIYVHGDSLKAFLVG 612
Cdd:PRK12316 2432 avvVAQDGASGKQLVAYVVP 2451
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
441-634 |
6.48e-08 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 55.78 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 441 VRMIVTGAAPASPTVLGFLRAA--LGCQVYeGYGQTECTAGCTFTTPGDWT---SGHVGAPLPCNHIKLVDVEELNYWAC 515
Cdd:PRK05857 288 LRLVGYGGSRAIAADVRFIEATgvRTAQVY-GLSETGCTALCLPTDDGSIVkieAGAVGRPYPGVDVYLAATDGIGPTAP 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 516 KGE-----GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIY 590
Cdd:PRK05857 367 GAGpsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGGVNIAPDEVDRIA 444
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2230395409 591 IRSQPV--AQIYVHGDSLKAFLVGI-VVPDPEVMPSWAQ--KRGIEGTY 634
Cdd:PRK05857 445 EGVSGVreAACYEIPDEEFGALVGLaVVASAELDESAARalKHTIAARF 493
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
494-570 |
7.15e-08 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 55.78 E-value: 7.15e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2230395409 494 GAPLPCNHIKLVDV--EELNYwacKGEGEICVRGPNVFKGYLKDPDRTKeALDSDGWLHTGDIGkWLPAGTLKIIDRKK 570
Cdd:PRK09192 388 GKALPGHEIEIRNEagMPLPE---RVVGHICVRGPSLMSGYFRDEESQD-VLAADGWLDTGDLG-YLLDGYLYITGRAK 461
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
441-626 |
1.57e-07 |
|
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: 54.30 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 441 VRMIVTGAAPASPTvlgFLRAALGCQVY--EGYGQTECTAGCT-FTTPGD----WTSGHVGAPLPCNHIKLVDvEELNYW 513
Cdd:cd17649 214 LRLYIFGGEALSPE---LLRRWLKAPVRlfNAYGPTEATVTPLvWKCEAGaaraGASMPIGRPLGGRSAYILD-ADLNPV 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 514 ACKGEGEICVRGPNVFKGYLKDPDRTKEAL--DSDG-----WLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKI 586
Cdd:cd17649 290 PVGVTGELYIGGEGLARGYLGRPELTAERFvpDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-RGFRIELGEI 368
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2230395409 587 ENiYIRSQP----VAQIYVHGDSLKAfLVGIVVP-DPEVMPSWAQ 626
Cdd:cd17649 369 EA-ALLEHPgvreAAVVALDGAGGKQ-LVAYVVLrAAAAQPELRA 411
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
435-619 |
1.89e-07 |
|
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: 54.06 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 435 ASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEC-TAGCTFTTPGDWT-SGHVGAPLPCNHIKLVDvEELNY 512
Cdd:cd05973 201 ARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELgMVLANHHALEHPVhAGSAGRAMPGWRVAVLD-DDGDE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 513 WACKGEGEICV---RGPNV-FKGYLKDPDRTKealdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIEN 588
Cdd:cd05973 280 LGPGEPGRLAIdiaNSPLMwFRGYQLPDTPAI----DGGYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFDVES 354
|
170 180 190
....*....|....*....|....*....|.
gi 2230395409 589 IYIRSQPVAQIYVhgdslkaflvgIVVPDPE 619
Cdd:cd05973 355 ALIEHPAVAEAAV-----------IGVPDPE 374
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
429-611 |
2.12e-07 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 54.27 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 429 FFNKIqasLGGC-------VRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTEctAGCTFT--TPGDWTSGHVGAPLP 498
Cdd:PRK06060 246 FFARV---IDSCspdsfrsLRCVVSAGEALELGLAERLMEFFGgIPILDGIGSTE--VGQTFVsnRVDEWRLGTLGRVLP 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 499 CNHIKLVDVEELNYwACKGEGEICVRGPNVFKGYLKDPDrtkEALDSDGWLHTGDIGK-----WLPAGTlkiidrKKHIF 573
Cdd:PRK06060 321 PYEIRVVAPDGTTA-GPGVEGDLWVRGPAIAKGYWNRPD---SPVANEGWLDTRDRVCidsdgWVTYRC------RADDT 390
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2230395409 574 KLAQGEYVAPEKIENIYIRSQPVAQIYVHG-------DSLKAFLV 611
Cdd:PRK06060 391 EVIGGVNVDPREVERLIIEDEAVAEAAVVAvrestgaSTLQAFLV 435
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
291-628 |
2.99e-07 |
|
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: 53.59 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 291 GSCGNPKGAMLTHGNVVADFSGFLKV---TES----QWAPTCADVHISYLplahmfermvqSVVYCHGGRVGFFQGDIRL 363
Cdd:cd17644 116 GSTGKPKGVMIEHQSLVNLSHGLIKEygiTSSdrvlQFASIAFDVAAEEI-----------YVTLLSGATLVLRPEEMRS 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 364 LSDDMKALCP----TIFPVVPrllnrmydkifsqantplkrwllefaakrkqaevrsgiirndSIWDELFFNKIQASLGG 439
Cdd:cd17644 185 SLEDFVQYIQqwqlTVLSLPP------------------------------------------AYWHLLVLELLLSTIDL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 440 --CVRMIVTGAAPASPTVLGFLRAALG--CQVYEGYGQTECTAGCTFTTPGDWTSGH-----VGAPLPCNHIKLVDvEEL 510
Cdd:cd17644 223 psSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIANTQVYILD-ENL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 511 NYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH--------TGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVA 582
Cdd:cd17644 302 QPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKI-RGFRIE 380
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2230395409 583 PEKIENIYIRSQPVAQ--IYVHGDSL-KAFLVGIVVPDPEVMPSWAQKR 628
Cdd:cd17644 381 LGEIEAVLSQHNDVKTavVIVREDQPgNKRLVAYIVPHYEESPSTVELR 429
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
471-589 |
3.05e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 53.62 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 471 YGQTECTAGCTFTTPG-----------DWTSGH----VGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKD 535
Cdd:PRK05851 310 YGLAESTCAVTVPVPGiglrvdevttdDGSGARrhavLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQ 389
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2230395409 536 PdrtkeALDSDGWLHTGDIGkWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENI 589
Cdd:PRK05851 390 A-----PIDPDDWFPTGDLG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERV 436
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
464-620 |
6.63e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 52.72 E-value: 6.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 464 GCQVYEGYGQTEctAGCTFTTPGDWTSGHVGAPLPcnHIKLVDVEE---------------LNywACKGEGEICVR-GPN 527
Cdd:PRK13388 288 GCQVEDGYGSSE--GAVIVVREPGTPPGSIGRGAP--GVAIYNPETltecavarfdahgalLN--ADEAIGELVNTaGAG 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 528 VFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYVHGdslk 607
Cdd:PRK13388 362 FFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYA---- 435
|
170
....*....|...
gi 2230395409 608 aflvgivVPDPEV 620
Cdd:PRK13388 436 -------VPDERV 441
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
442-622 |
2.47e-06 |
|
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: 50.48 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 442 RMIVTGAAPASPtVLGFLRAALGCQVYEGYGQTEC--TAGCTFTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEG 519
Cdd:cd17648 211 RVDAAGEEFTAP-VFEKLRSRFAGLIINAYGPTETtvTNHKRFFPGDQRFDKSLGRPVRNTKCYVLN-DAMKRVPVGAVG 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 520 EICVRGPNVFKGYLKDPDRTKE-------------ALDSDGWLH-TGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEK 585
Cdd:cd17648 289 ELYLGGDGVARGYLNRPELTAErflpnpfqteqerARGRNARLYkTGDLVRWLPSGELEYLGRNDFQVKI-RGQRIEPGE 367
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2230395409 586 IENIY-----IRSQPVAQIYVHGDSLKA---FLVGIVVPDPEVMP 622
Cdd:cd17648 368 VEAALasypgVRECAVVAKEDASQAQSRiqkYLVGYYLPEPGHVP 412
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
496-556 |
2.47e-06 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 50.66 E-value: 2.47e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2230395409 496 PLPCNHIK-----LVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL-DSDGW--LHTGDIGK 556
Cdd:PRK04813 317 RLPIGYAKpdsplLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGY 385
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
464-587 |
4.84e-06 |
|
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: 49.78 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 464 GCQVYEGYG--QTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTK 540
Cdd:cd17656 271 NVHLHNHYGpsETHVVTTYTINPEAEIPElPPIGKPISNTWIYILD-QEQQLQPQGIVGELYISGASVARGYLNRQELTA 349
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2230395409 541 EALDSDGW------LHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIE 587
Cdd:cd17656 350 EKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-RGYRIELGEIE 401
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
441-588 |
5.62e-06 |
|
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: 48.94 E-value: 5.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 441 VRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTEcTAGCTFTTPGD-WTSGHVGAPLPCNHIKLVDVEElnywacKGE 518
Cdd:cd17633 112 IKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSE-LSFITYNFNQEsRPPNSVGRPFPNVEIEIRNADG------GEI 184
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 519 GEICVRGPNVFKGYLKDPDRTKealdsDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIEN 588
Cdd:cd17633 185 GKIFVKSEMVFSGYVRGGFSNP-----DGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIES 248
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
441-619 |
1.03e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 48.77 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 441 VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECtAGCTFTTPGDWT--SGHVGAPLPCNHIKLVD-----VEElnyw 513
Cdd:PRK07788 325 LKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEV-AFATIATPEDLAeaPGTVGRPPKGVTVKILDengneVPR---- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 514 ackGE-GEICVRGPNVFKGYlKDPdRTKEALdsDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIyir 592
Cdd:PRK07788 400 ---GVvGRIFVGNGFPFEGY-TDG-RDKQII--DGLLSSGDVGYFDEDGLLFVDGRDDDMI-VSGGENVFPAEVEDL--- 468
|
170 180
....*....|....*....|....*..
gi 2230395409 593 sqpvaqIYVHGDSLKAFLVGivVPDPE 619
Cdd:PRK07788 469 ------LAGHPDVVEAAVIG--VDDEE 487
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
444-628 |
1.54e-05 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 47.73 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 444 IVTGAAPASPTVLgflRAA--LGCQVYEGYGQTECTAGCTFTtpgdwtsghvGAPLPCNHIKLVDveelnywackgeGEI 521
Cdd:PRK07824 156 VLVGGGPAPAPVL---DAAaaAGINVVRTYGMSETSGGCVYD----------GVPLDGVRVRVED------------GRI 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 522 CVRGPNVFKGY--LKDPDrtkeALDSDGWLHTGDIGKwLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQI 599
Cdd:PRK07824 211 ALGGPTLAKGYrnPVDPD----PFAEPGWFRTDDLGA-LDDGVLTVLGRADDAISTG-GLTVLPQVVEAALATHPAVADC 284
|
170 180 190
....*....|....*....|....*....|..
gi 2230395409 600 YVHG---DSLKAFLVGIVVPDPEVMPSWAQKR 628
Cdd:PRK07824 285 AVFGlpdDRLGQRVVAAVVGDGGPAPTLEALR 316
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
146-618 |
1.83e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 47.96 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGP--GDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 226 DK---PQKAVLLlehverKETPGLKLIILMD------------PFEEALKERGQKCGVVIKSmqAVEHFLL-SGlwpres 289
Cdd:PRK07798 107 ERefaPRVAEVL------PRLPKLRTLVVVEdgsgndllpgavDYEDALAAGSPERDFGERS--PDDLYLLyTG------ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 290 pGSCGNPKGAMLTHGNV-VADFSGFLKVT-------ESQWAPTCADVHISYLPLAHMFERMVQSVVYchggrVGFFQGDI 361
Cdd:PRK07798 173 -GTTGMPKGVMWRQEDIfRVLLGGRDFATgepiedeEELAKRAAAGPGMRRFPAPPLMHGAGQWAAF-----AALFSGQT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 362 RLLSDDMKalcptifpvvprllnrmydkiFSQANtplkrwLLEFAAKRKqaeVRSGIIRNDS----IWDELffnkiqASL 437
Cdd:PRK07798 247 VVLLPDVR---------------------FDADE------VWRTIEREK---VNVITIVGDAmarpLLDAL------EAR 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 438 GG----CVRMIVTGAAPASPTV-LGFLRAALGCQVYEGYGQTECTAGCTFTTPGDwtSGHVGAPL--PCNHIKLVDvEEL 510
Cdd:PRK07798 291 GPydlsSLFAIASGGALFSPSVkEALLELLPNVVLTDSIGSSETGFGGSGTVAKG--AVHTGGPRftIGPRTVVLD-EDG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 511 NYWAcKGEGEICV--RGPNVFKGYLKDPDRTKEALDS-DG--WLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEK 585
Cdd:PRK07798 368 NPVE-PGSGEIGWiaRRGHIPLGYYKDPEKTAETFPTiDGvrYAIPGDRARVEADGTITLLGRGSVCINTG-GEKVFPEE 445
|
490 500 510
....*....|....*....|....*....|...
gi 2230395409 586 IENIyIRSQPvaqiyvhgDSLKAFLVGivVPDP 618
Cdd:PRK07798 446 VEEA-LKAHP--------DVADALVVG--VPDE 467
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
459-632 |
2.04e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 48.41 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 459 LRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSG----HVGAPLPCNHIKLVDVEeLNYWACKGEGEICVRGPNVFKGYL 533
Cdd:PRK12316 4830 WRALKPVYLFNGYGPTETTVTVLlWKARDGDACGaaymPIGTPLGNRSGYVLDGQ-LNPLPVGVAGELYLGGEGVARGYL 4908
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 534 KDPDRTKEALDSD------GWLH-TGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIEnIYIRSQP-------VAQI 599
Cdd:PRK12316 4909 ERPALTAERFVPDpfgapgGRLYrTGDLARYRADGVIDYLGRVDHQVKI-RGFRIELGEIE-ARLREHPavreavvIAQE 4986
|
170 180 190
....*....|....*....|....*....|....
gi 2230395409 600 YVHGdslkAFLVGIVVP-DPEVMPSWAQKRGIEG 632
Cdd:PRK12316 4987 GAVG----KQLVGYVVPqDPALADADEAQAELRD 5016
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
442-627 |
6.86e-05 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 45.84 E-value: 6.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 442 RMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFTTPGdwtSGHVGAPL-PCNHIKLVDVEELNYWACK--G 517
Cdd:cd05924 137 FAISSGGALLSPEVKqGLLELVPNITLVDAFGSSETGFTGSGHSAG---SGPETGPFtRANPDTVVLDDDGRVVPPGsgG 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 518 EGEICVRGpNVFKGYLKDPDRTKEA---LDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIyIRSQ 594
Cdd:cd05924 214 VGWIARRG-HIPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTG-GEKVFPEEVEEA-LKSH 290
|
170 180 190
....*....|....*....|....*....|....
gi 2230395409 595 P-VAQIYVHGdslkaflvgivVPDPEvmpsWAQK 627
Cdd:cd05924 291 PaVYDVLVVG-----------RPDER----WGQE 309
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
438-620 |
8.81e-05 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 45.90 E-value: 8.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 438 GGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFT-TPGDWTSG--HVGAPLPCNHIKLVDVE--ELNy 512
Cdd:PRK13382 311 GRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATE--AGMIATaTPADLRAApdTAGRPAEGTEIRILDQDfrEVP- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 513 wacKGE-GEICVRGPNVFKGYlkDPDRTKEAldSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIyI 591
Cdd:PRK13382 388 ---TGEvGTIFVRNDTQFDGY--TSGSTKDF--HDGFMASGDVGYLDENGRLFVVGRDDEMI-VSGGENVYPIEVEKT-L 458
|
170 180 190
....*....|....*....|....*....|....*..
gi 2230395409 592 RSQP-VAQIYV-------HGDSLKAFlvgiVVPDPEV 620
Cdd:PRK13382 459 ATHPdVAEAAVigvddeqYGQRLAAF----VVLKPGA 491
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
430-708 |
1.09e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 45.54 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 430 FNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPGDWTSGHVGAPLPCNHIKLVDVEE 509
Cdd:PRK07638 245 LYKENRVIENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSF-VTALVDEESERRPNSVGRPFHNVQVRICNE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 510 LNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEaLDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIEN 588
Cdd:PRK07638 324 AGEEVQKGEiGTVYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIES 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 589 IYIRSQPVAQIYVHGdslkaflvgivVPDpevmPSWAQKRG--IEGTyadlCTNKDLKKAILEDmvrlgkesgLHSFEQV 666
Cdd:PRK07638 402 VLHEHPAVDEIVVIG-----------VPD----SYWGEKPVaiIKGS----ATKQQLKSFCLQR---------LSSFKIP 453
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2230395409 667 KAIHIhsdmfsVQNGLLTPTLKAKRPELreyfKKQIEELYSI 708
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 ... |
431-595 |
1.13e-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: 45.50 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 431 NKIQASLGGCVRMIVTGAAPASPTV----LGFLRA--ALGCQVYEGYGqTECTAGCTFTTPGDWTSGHVGAPLPCNHI-K 503
Cdd:cd05915 263 ESTGHRLKTLRRLVVGGSAAPRSLIarfeRMGVEVrqGYGLTETSPVV-VQNFVKSHLESLSEEEKLTLKAKTGLPIPlV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 504 LVDVEELNYWACKGEGE----ICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGE 579
Cdd:cd05915 342 RLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG-GE 420
|
170
....*....|....*.
gi 2230395409 580 YVAPEKIENIyIRSQP 595
Cdd:cd05915 421 WISSVDLENA-LMGHP 435
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
440-611 |
2.76e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 44.22 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 440 CVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGcTFTTPG---DWTSGhVGAPLPCNHIKLVDVEELNYwACK 516
Cdd:PRK13383 293 QLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIG-ALATPAdlrDAPET-VGKPVAGCPVRILDRNNRPV-GPR 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 517 GEGEICVRGPNVFKGYlkdPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPV 596
Cdd:PRK13383 370 VTGRIFVGGELAGTRY---TDGGGKAV-VDGMTSTGDMGYLDNAGRLFIVGREDDMI-ISGGENVYPRAVENALAAHPAV 444
|
170 180
....*....|....*....|..
gi 2230395409 597 AQIYV-------HGDSLKAFLV 611
Cdd:PRK13383 445 ADNAVigvpderFGHRLAAFVV 466
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
434-611 |
1.14e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.46 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 434 QASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF------TTPGDWTSghVGAPLPCNHIKLVDv 507
Cdd:PRK05691 3979 RQALDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFfrvdlaSTRGSYLP--IGSPTDNNRLYLLD- 4055
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 508 EELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL-------DSDGWLHTGDIGKWLPAGTLKIIDRKKHI-----FKL 575
Cdd:PRK05691 4056 EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFvphpfgaPGERLYRTGDLARRRSDGVLEYVGRIDHQvkirgYRI 4135
|
170 180 190
....*....|....*....|....*....|....*..
gi 2230395409 576 AQGEYVApEKIENIYIRSQPVA-QIYVHGDSLKAFLV 611
Cdd:PRK05691 4136 ELGEIEA-RLHEQAEVREAAVAvQEGVNGKHLVGYLV 4171
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
427-612 |
1.16e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.46 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 427 ELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTF--TTPGDWTSGHVGAPLPCNHIK 503
Cdd:PRK05691 1376 QLFIDEPLAAACTSLRRLFSGGEALPAELRNRVLQRLpQVQLHNRYGPTETAINVTHwqCQAEDGERSPIGRPLGNVLCR 1455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 504 LVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKE-----ALDSDG--WLHTGDIGKWLPAGTLKIIDRKKHIFKLa 576
Cdd:PRK05691 1456 VLD-AELNLLPPGVAGELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL- 1533
|
170 180 190
....*....|....*....|....*....|....*...
gi 2230395409 577 QGEYVAPEKIENIYIRSQPVAQ--IYVHGDSLKAFLVG 612
Cdd:PRK05691 1534 RGFRVEPEEIQARLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
466-619 |
2.15e-03 |
|
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: 41.19 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 466 QVYEGYGQTECTAGCT--FTTPGdwTSGHVGAPLPCNH-IKLV--DVEELNYW---------ACKGE-----GEICVRGP 526
Cdd:cd05940 222 RIAEFYAATEGNSGFInfFGKPG--AIGRNPSLLRKVApLALVkyDLESGEPIrdaegrcikVPRGEpglliSRINPLEP 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 527 nvFKGYLKDPDRTKEAL-----DSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYV 601
Cdd:cd05940 300 --FDGYTDPAATEKKILrdvfkKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRW-KGENVSTTEVAAVLGAFPGVEEANV 376
|
170 180
....*....|....*....|...
gi 2230395409 602 HGDSL-----KAFLVGIVVPDPE 619
Cdd:cd05940 377 YGVQVpgtdgRAGMAAIVLQPNE 399
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
530-618 |
2.36e-03 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 41.57 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 530 KGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIyIRSQP-VAQIYVH 602
Cdd:PRK10252 814 QGYLGRPDLTASRFIADPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKI-RGQRIELGEIDRA-MQALPdVEQAVTH 891
|
90 100
....*....|....*....|....*..
gi 2230395409 603 -----------GDSLKafLVGIVVPDP 618
Cdd:PRK10252 892 acvinqaaatgGDARQ--LVGYLVSQS 916
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
494-598 |
2.52e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 41.31 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 494 GAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEA---LDSDGWLHTGDIGkWLPAGTLKIIDRKK 570
Cdd:PRK05691 373 GRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfveHDGRTWLRTGDLG-FLRDGELFVTGRLK 451
|
90 100
....*....|....*....|....*...
gi 2230395409 571 HIFkLAQGEYVAPEKIENIYIRSQPVAQ 598
Cdd:PRK05691 452 DML-IVRGHNLYPQDIEKTVEREVEVVR 478
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
467-603 |
2.56e-03 |
|
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: 40.88 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 467 VYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKL--------VDVEELNYW----------ACKGE-GEICVRGPN 527
Cdd:cd05937 229 IGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKFenqvvlvkMDPETDDPIrdpktgfcvrAPVGEpGEMLGRVPF 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230395409 528 V----FKGYLKDPDRTKEAL------DSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVA 597
Cdd:cd05937 309 KnreaFQGYLHNEDATESKLvrdvfrKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRW-KSENVSTTEVADVLGAHPDIA 387
|
....*.
gi 2230395409 598 QIYVHG 603
Cdd:cd05937 388 EANVYG 393
|
|
| |
