|
Name |
Accession |
Description |
Interval |
E-value |
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
116-694 |
0e+00 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 928.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 116 QPYQWLSYQEVADRAEFLGSGLLQHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADI 195
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 196 STVIVDKpqkavlllehverketpglkliilmdpfeealkergqkcGVVIKSMQAVEDCGQENHQAPVPPQPDDLSIVCF 275
Cdd:cd05927 81 SIVFCDA---------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 276 TSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTCADVHISYLPLAHMFERMVQSVVYCHGGRVGFFQGDIRLLSDDM 355
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 356 KALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWLLEFAAKRKQAEVRSGIIRNDSIWDELFFNKIQASLGGCVRMIVT 433
Cdd:cd05927 202 KALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 434 GAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWA--CKGEGEICVR 511
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAkdPNPRGEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 512 GPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGD 591
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 592 SLKAFLVGIVVPDPEVMPSWA-QKRGIEGTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLL 670
Cdd:cd05927 442 SLKSFLVAIVVPDPDVLKEWAaSKGGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLL 521
|
570 580
....*....|....*....|....
gi 327412323 671 TPTLKAKRPELREYFKKQIEELYS 694
Cdd:cd05927 522 TPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
72-694 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 708.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 72 RSViGSGPQLLTHY--YDDARTMYQVFRRGLSISGNGPCLGFRKPKQ----PYQWLSYQEVADRAEFLGSGLLQHNCK-- 143
Cdd:PLN02736 25 RSA-RSPLKLVSRFpdHPEIGTLHDNFVYAVETFRDYKYLGTRIRVDgtvgEYKWMTYGEAGTARTAIGSGLVQHGIPkg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 144 ACtdqfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVdKPQKAVLLLEHVerKETPGLKL 223
Cdd:PLN02736 104 AC----VGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCL--SEIPSVRL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 224 IILMDPFEEALKERGQKCGVVIKSMQAVEDCGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKV 303
Cdd:PLN02736 177 IVVVGGADEPLPSLPSGTGVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 304 TESqwAPtcADVHISYLPLAHMFERMVQSVVYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QA 381
Cdd:PLN02736 257 TKF--YP--SDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNavKE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 382 NTPLKRWLLEFAAKRKQAEVRSGiiRNDS-IWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQ 460
Cdd:PLN02736 333 SGGLKERLFNAAYNAKKQALENG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGM 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 461 TECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKG---EGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH 537
Cdd:PLN02736 411 TETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLH 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 538 TGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGI 617
Cdd:PLN02736 491 TGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGI 570
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 327412323 618 E-GTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 694
Cdd:PLN02736 571 KyEDLKQLCNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYA 648
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
86-694 |
1.87e-178 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 521.58 E-value: 1.87e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 86 YDDARTMYQVFRRGLSISGNGPCLGFRKPKQpYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVEL 165
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVALREKEDGI-WQSLTWAEFAERVRALAAGLLALGVKP--GDRVAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 166 ACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAVLLLEHveRKETPGLKLIILMDPfeealkeRGQKCGVVI 245
Cdd:COG1022 84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEV--RDELPSLRHIVVLDP-------RGLRDDPRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 246 KSMQAVEDCGQE-NHQAPVP-----PQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWAPTCADVHISY 319
Cdd:COG1022 155 LSLDELLALGREvADPAELEarraaVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLER----LPLGPGDRTLSF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 320 LPLAHMFERMVQSVVYCHGGRVGFfQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQAN--TPLKRWLLEFA---A 394
Cdd:COG1022 231 LPLAHVFERTVSYYALAAGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEeaGGLKRKLFRWAlavG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 395 KRKQAEVRSGiiRNDSIW--------DELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAG 466
Cdd:COG1022 310 RRYARARLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 467 CTFTTPGDWTSGHVGAPLPCNHIKLVDveelnywackgEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLP 546
Cdd:COG1022 387 ITVNRPGDNRIGTVGPPLPGVEVKIAE-----------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 547 AGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKaFLVGIVVPDPEVMPSWAQKRGIE-GTYADLC 625
Cdd:COG1022 456 DGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDGRP-FLAALIVPDFEALGEWAEENGLPyTSYAELA 534
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 327412323 626 TNKDLKKAILEDMVRLGKesGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 694
Cdd:COG1022 535 QDPEVRALIQEEVDRANA--GLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYA 601
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
116-681 |
1.77e-162 |
|
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: 475.16 E-value: 1.77e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 116 QPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADI 195
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEP--GDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 196 STVIVDKPqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhqapvppqpDDLSIVCF 275
Cdd:cd05907 79 KALFVEDP----------------------------------------------------------------DDLATIIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 276 TSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWAPTCADVHISYLPLAHMFE-RMVQSVVYCHGGRVGFFQgDIRLLSDD 354
Cdd:cd05907 95 TSGTTGRPKGVMLSHRNILSNALALAER----LPATEGDRHLSFLPLAHVFErRAGLYVPLLAGARIYFAS-SAETLLDD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 355 MKALCPTIFPVVPRLLNRMYDKIFSQANTPLKRWLLEFAAkrkqaevrsgiirndsiwdelffnkiqaslGGCVRMIVTG 434
Cdd:cd05907 170 LSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV------------------------------GGRLRFAASG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 435 AAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDveelnywackgEGEICVRGPN 514
Cdd:cd05907 220 GAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPN 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 515 VFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLK 594
Cdd:cd05907 288 VMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDGRP 367
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 595 aFLVGIVVPDPEVMPSWAQKRGIEG-TYADLCTNKDLKKAILEDMVRLGKEsgLHSFEQVKAIHIHSDMFSVQNGLLTPT 673
Cdd:cd05907 368 -FLVALIVPDPEALEAWAEEHGIAYtDVAELAANPAVRAEIEAAVEAANAR--LSRYEQIKKFLLLPEPFTIENGELTPT 444
|
....*...
gi 327412323 674 LKAKRPEL 681
Cdd:cd05907 445 LKLKRPVI 452
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
117-678 |
1.54e-154 |
|
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: 457.06 E-value: 1.54e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 117 PYQWLSYQEVADRAEFLGSGL----LQHNCKactdqfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINT 192
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLvelgLKPGDK------VAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 193 ADISTVIVDkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhqapvpPQPDDLSI 272
Cdd:cd17639 76 TECSAIFTD---------------------------------------------------------------GKPDDLAC 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 273 VCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTcaDVHISYLPLAHMFERMVQSVVYCHGGRVGFfqGDIRLLS 352
Cdd:cd17639 93 IMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGPD--DRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLT 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 353 DDMKALC--------PTIFPVVPRLLNRMYDKIFSQANTP--LKRWLLEFAAKRKQAEVRSGIirnDS-IWDELFFNKIQ 421
Cdd:cd17639 169 DKSKRGCkgdltefkPTLMVGVPAIWDTIRKGVLAKLNPMggLKRTLFWTAYQSKLKALKEGP---GTpLLDELVFKKVR 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 422 ASLGGCVRMIVTGAAPASPTVLGFLrAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWA 501
Cdd:cd17639 246 AALGGRLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYST 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 502 CKGE--GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIR 579
Cdd:cd17639 325 DKPPprGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRS 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 580 SQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRG-IEGTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHI 658
Cdd:cd17639 405 NPLVNNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGvINSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVL 484
|
570 580
....*....|....*....|
gi 327412323 659 HSDMFSVQNGLLTPTLKAKR 678
Cdd:cd17639 485 LDEEWTPENGLVTAAQKLKR 504
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
58-693 |
1.04e-152 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 457.95 E-value: 1.04e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 58 LMQSEEVEDSGGARRSVigsGPQLLTHYYDDA--------RTMYQVFRRGLSISGNGPCLGFR-----KPKQpYQWLSYQ 124
Cdd:PLN02614 8 IFQVEEGKEGSDGRPSV---GPVYRSIFAKDGfpnpiegmDSCWDVFRMSVEKYPNNPMLGRReivdgKPGK-YVWQTYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 125 EVADRAEFLGSGLlqHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDkpQ 204
Cdd:PLN02614 84 EVYDIVIKLGNSL--RSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVE--E 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 205 KAVLLLEHVERKETPGLKLIILMDPFEEALKERGQKCGVVIKSMQAVEDCGqENHQAPVP-PQPDDLSIVCFTSGTTGNP 283
Cdd:PLN02614 160 KKISELFKTCPNSTEYMKTVVSFGGVSREQKEEAETFGLVIYAWDEFLKLG-EGKQYDLPiKKKSDICTIMYTSGTTGDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 284 KGAMLTHGNVVADFSGFLKVTES-QWAPTCADVHISYLPLAHMFERMVQSVVYCHGGRVGFFQGDIRLLSDDMKALCPTI 362
Cdd:PLN02614 239 KGVMISNESIVTLIAGVIRLLKSaNAALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 363 FPVVPRLLNRMYDKIFSQANTP--LKRWLLEFAAKRKQAEVRSGI--IRNDSIWDELFFNKIQASLGGCVRMIVTGAAPA 438
Cdd:PLN02614 319 FCAVPRVLDRVYSGLQKKLSDGgfLKKFVFDSAFSYKFGNMKKGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 439 SPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDVEELNY--WACKGEGEICVRGPNV 515
Cdd:PLN02614 399 ASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELDMlGTVGPPVPNVDIRLESVPEMEYdaLASTPRGEICIRGKTL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 516 FKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKA 595
Cdd:PLN02614 479 FSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFES 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 596 FLVGIVVPDPEVMPSWAQKRGIEGTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLK 675
Cdd:PLN02614 558 FLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFK 637
|
650
....*....|....*...
gi 327412323 676 AKRPELREYFKKQIEELY 693
Cdd:PLN02614 638 KKRPQLLKYYQSVIDEMY 655
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
88-693 |
6.83e-151 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 453.12 E-value: 6.83e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 88 DARTMYQVFRRGLSISGNGPCLGFRKPKQ----PYQWLSYQEVADRAEFLGSGLLQHNCKACTDqfIGVFAQNRPEWIIV 163
Cdd:PLN02430 40 DITTAWDIFSKSVEKYPDNKMLGWRRIVDgkvgPYMWKTYKEVYEEVLQIGSALRASGAEPGSR--VGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 164 ELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV-DKPQKAVLlleHVERKETPGLKLIILMDPFEEALKERGQKCG 242
Cdd:PLN02430 118 MEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVqDKKIKELL---EPDCKSAKRLKAIVSFTSVTEEESDKASQIG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 243 VVIKSMQAVEDCGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTESQWapTCADVHISY 319
Cdd:PLN02430 195 VKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGvdlFMEQFEDKM--THDDVYLSF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 320 LPLAHMFERMVQSVVYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWLLEFAAKRK 397
Cdd:PLN02430 273 LPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYKYK 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 398 QAEVRSGIIRNDS--IWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDW 475
Cdd:PLN02430 353 LAWMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEM 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 476 TS-GHVGAPLPCNHIKLVDVEELNY--WACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKI 552
Cdd:PLN02430 433 CMlGTVGAPAVYNELRLEEVPEMGYdpLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKI 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 553 IDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGIEGTYADLCTNKDLKK 632
Cdd:PLN02430 512 IDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKE 591
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 327412323 633 AILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 693
Cdd:PLN02430 592 HILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMY 652
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
117-694 |
4.91e-149 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 448.52 E-value: 4.91e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 117 PYQWLSYQEVADRAEFLGSGLLQ------HNCkactdqfiGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYII 190
Cdd:PLN02861 74 PYVWLTYKEVYDAAIRIGSAIRSrgvnpgDRC--------GIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFII 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 191 NTADISTVIVDKPQKAVLLleHVERKETPGLKLIILMDPFEEALKERGQKCGVVIKSMQAVEDCGQENHQAPvPPQPDDL 270
Cdd:PLN02861 146 NHAEVSIAFVQESKISSIL--SCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLDCELP-PKQKTDI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 271 SIVCFTSGTTGNPKGAMLTHGNVVADF---SGFLKVTESqwAPTCADVHISYLPLAHMFERMVQSVVYCHGGRVGFFQGD 347
Cdd:PLN02861 223 CTIMYTSGTTGEPKGVILTNRAIIAEVlstDHLLKVTDR--VATEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQGD 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 348 IRLLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWLLEFAAKRKQAEVRSGIIRNDS--IWDELFFNKIQAS 423
Cdd:PLN02861 301 IRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQkiSSGGMLRKKLFDFAYNYKLGNLRKGLKQEEAspRLDRLVFDKIKEG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 424 LGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCtFTTPGDWTS--GHVGAPLPCNHIKLVDVEELNYWA 501
Cdd:PLN02861 381 LGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGC-FTSIANVFSmvGTVGVPMTTIEARLESVPEMGYDA 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 502 CKG--EGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIR 579
Cdd:PLN02861 460 LSDvpRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSR 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 580 SQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGIEGTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIH 659
Cdd:PLN02861 539 CPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLE 618
|
570 580 590
....*....|....*....|....*....|....*
gi 327412323 660 SDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 694
Cdd:PLN02861 619 PNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYS 653
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
79-694 |
6.42e-133 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 407.97 E-value: 6.42e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 79 PQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRK--PKQ----------------PYQWLSYQEVADRAEFLGSGLLQ- 139
Cdd:PLN02387 47 PELVETPWEGATTLAALFEQSCKKYSDKRLLGTRKliSREfetssdgrkfeklhlgEYEWITYGQVFERVCNFASGLVAl 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 140 -HNckacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQ--KAVLLLEHVERk 216
Cdd:PLN02387 127 gHN----KEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQlkKLIDISSQLET- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 217 etpgLKLIILM-DPFEEALKERGQKCGVVIKSMQAVEDCGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVA 295
Cdd:PLN02387 202 ----VKRVIYMdDEGVDSDSSLSGSSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 296 DFSGFLKVTesqwaPTCA--DVHISYLPLAHMFERMVQSVVYCHGGRVGFfqGDIRLLSD-----------DMKALCPTI 362
Cdd:PLN02387 278 TVAGVMTVV-----PKLGknDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDtsnkikkgtkgDASALKPTL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 363 FPVVPRLLNRMYDKIFSQANTP--LKRWLLEFAAKRKQAEVR------SGIIRndSIWDELFFNKIQASLGGCVRMIVTG 434
Cdd:PLN02387 351 MTAVPAILDRVRDGVRKKVDAKggLAKKLFDIAYKRRLAAIEgswfgaWGLEK--LLWDALVFKKIRAVLGGRIRFMLSG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 435 AAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKG---EGEICVR 511
Cdd:PLN02387 429 GAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLISDKpmpRGEIVIG 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 512 GPNVFKGYLKDPDRTKEA--LDSDG--WLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIY 587
Cdd:PLN02387 509 GPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIM 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 588 VHGDSLKAFLVGIVVPDPEVMPSWAQKRGIE-GTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQ 666
Cdd:PLN02387 589 VHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPAKIKLLPEPWTPE 668
|
650 660
....*....|....*....|....*...
gi 327412323 667 NGLLTPTLKAKRPELREYFKKQIEELYS 694
Cdd:PLN02387 669 SGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
117-563 |
1.35e-126 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 382.05 E-value: 1.35e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 117 PYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADIS 196
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRALGVGK--GDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 197 TVIVDKPQKAVLLLEHVERKETPGLKLIILMDPFEEALKergqkcgvviksMQAVEDCGQENHQAPVPPQPDDLSIVCFT 276
Cdd:pfam00501 96 VLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEP------------LPEEAKPADVPPPPPPPPDPDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 277 SGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTCADVHISYLPLAHMFER-MVQSVVYCHGGRVGFFQGDIRL----L 351
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALdpaaL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 352 SDDMKALCPTIFPVVPRLLNRMydkifsqantplkrwlleFAAKRKQAEVRSGiirndsiwdelffnkiqaslggcVRMI 431
Cdd:pfam00501 244 LELIERYKVTVLYGVPTLLNML------------------LEAGAPKRALLSS-----------------------LRLV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 432 VTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDW---TSGHVGAPLPCNHIKLVDVEELNYWACKGEGEI 508
Cdd:pfam00501 283 LSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGEL 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 327412323 509 CVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLA 563
Cdd:pfam00501 363 CVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
63-693 |
1.24e-98 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 318.46 E-value: 1.24e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 63 EVEDSGGARRSVIGSGPQL--LTHYYDDARTMYQVFRRGLSISGNGPCLGFRKPK--------------QPY-------- 118
Cdd:PTZ00216 40 ETENASAIYRIAGVTDEEHerLRNEWYYGPNFLQRLERICKERGDRRALAYRPVErvekevvkdadgkeRTMevthfnet 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 119 QWLSYQEVADRAEFLGSGL----LQHNCKactdqfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTAD 194
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLaelgLTKGSN------VAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 195 iSTVIVDKPQKAVLLLEHVERKETPGLKLIILmdpfeEALKERGQKCGVVIKSMQAVEDCG---QENHQAPVPPQPDDLS 271
Cdd:PTZ00216 194 -CKAIVCNGKNVPNLLRLMKSGGMPNTTIIYL-----DSLPASVDTEGCRLVAWTDVVAKGhsaGSHHPLNIPENNDDLA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 272 IVCFTSGTTGNPKGAMLTHGNVVADFSGF-LKVTESQWAPTCADVHISYLPLAHMFERMVQSVVYCHGGRVGFfqGDIRL 350
Cdd:PTZ00216 268 LIMYTSGTTGDPKGVMHTHGSLTAGILALeDRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 351 LSD-------DMKALCPTIFPVVPRLLNRMydKIFSQANTP----LKRWLLEFAAKRKQAEVRSGiiRNDSIWDELFFNK 419
Cdd:PTZ00216 346 LTDtfarphgDLTEFRPVFLIGVPRIFDTI--KKAVEAKLPpvgsLKRRVFDHAYQSRLRALKEG--KDTPYWNEKVFSA 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 420 IQASLGGCVRMIVTGAAPASPTVLGFLRAALGCqVYEGYGQTE--CTAGCTFTtpGDWTSGHVGAPLPCNHIKLVDVEEL 497
Cdd:PTZ00216 422 PRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTEtvCCGGIQRT--GDLEPNAVGQLLKGVEMKLLDTEEY 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 498 NYwACKGE--GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIEN 575
Cdd:PTZ00216 499 KH-TDTPEprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEA 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 576 IYIRSQPVAQ----IYVHGDslKAFLVGIVVPDPEVMPSWAQKRGIEGTYADLCTNKDLKKAILEDMVRLGKESGLHSFE 651
Cdd:PTZ00216 578 LYGQNELVVPngvcVLVHPA--RSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFE 655
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 327412323 652 QVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 693
Cdd:PTZ00216 656 IVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
116-679 |
5.01e-79 |
|
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: 259.98 E-value: 5.01e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 116 QPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADI 195
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKA--GEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 196 STVIVdkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqENHqapvppqPDDLSIVCF 275
Cdd:cd17640 79 VALVV--------------------------------------------------------END-------SDDLATIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 276 TSGTTGNPKGAMLTHGNVVADFSGFLKVTEsqwaPTCADVHISYLPLAHMFERMVQSVVYCHGGRVGFfqGDIRLLSDDM 355
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLLHQIRSLSDIVP----PQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDDL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 356 KALCPTIFPVVPRLLNRMYDKIFSQ--ANTPLKRWLLEFAAkrkqaevrsgiirndsiwdelffnkiqasLGGCVRMIVT 433
Cdd:cd17640 170 KRVKPHYIVSVPRLWESLYSGIQKQvsKSSPIKQFLFLFFL-----------------------------SGGIFKFGIS 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 434 GAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGP 513
Cdd:cd17640 221 GGGALPPHVDTFFEA-IGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGP 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 514 NVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSL 593
Cdd:cd17640 300 QVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQ 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 594 KaFLVGIVVPDPEVMPSWAQKRGI---EGTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFsVQNGLL 670
Cdd:cd17640 380 K-RLGALIVPNFEELEKWAKESGVklaNDRSQLLASKKVLKLYKNEIKDEISNRPGFKSFEQIAPFALLEEPF-IENGEM 457
|
....*....
gi 327412323 671 TPTLKAKRP 679
Cdd:cd17640 458 TQTMKIKRN 466
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
118-678 |
5.55e-78 |
|
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: 258.55 E-value: 5.55e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 118 YQWLSYQEVADRAEFLGSGLLQHNCKACTDqfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADIST 197
Cdd:cd05932 4 VVEFTWGEVADKARRLAAALRALGLEPGSK--IALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 198 VIVDKpqkavllLEHVERKE--TPGLKLIILMDPFEEALKERGqkcgvviksMQAVEDCGQENHQAPvPPQPDDLSIVCF 275
Cdd:cd05932 82 LFVGK-------LDDWKAMApgVPEGLISISLPPPSAANCQYQ---------WDDLIAQHPPLEERP-TRFPEQLATLIY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 276 TSGTTGNPKGAMLTHGNVVADFSGF---LKVTESqwaptcaDVHISYLPLAHMFERMVQSVVYCHGGRVGFFQGDIRLLS 352
Cdd:cd05932 145 TSGTTGQPKGVMLTFGSFAWAAQAGiehIGTEEN-------DRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTFV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 353 DDMKALCPTIFPVVPRLL----NRMYDKIFSQAntpLKRWLlefaakrkQAEVRSGIIRndsiwdelffNKIQASLG-GC 427
Cdd:cd05932 218 EDVQRARPTLFFSVPRLWtkfqQGVQDKIPQQK---LNLLL--------KIPVVNSLVK----------RKVLKGLGlDQ 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 428 VRMIVTGAAPASPTVLGFLRaALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDveelnywackgEGE 507
Cdd:cd05932 277 CRLAGCGSAPVPPALLEWYR-SLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 508 ICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIY 587
Cdd:cd05932 345 ILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVC 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 588 VHGDSLKAfLVGIVVPDPEVMPSwaqkrgiegtyADLCTNKDLKKAILEDMVRLGKEsgLHSFEQVKAIHIHSDMFSVQN 667
Cdd:cd05932 425 VIGSGLPA-PLALVVLSEEARLR-----------ADAFARAELEASLRAHLARVNST--LDSHEQLAGIVVVKDPWSIDN 490
|
570
....*....|.
gi 327412323 668 GLLTPTLKAKR 678
Cdd:cd05932 491 GILTPTLKIKR 501
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
113-693 |
2.05e-70 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 240.72 E-value: 2.05e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 113 KPKQPYQWLSYQEVADRAE-----FLGSGLLQHNCkactdqfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIR 187
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRqaakaFLKLGLERFHG-------VGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 188 YIINTADISTVIVDKPQKAVLLLEhvERKETPGLKLII-LMDPFEEalKERGQKcgvvikSMQAVEDCG-----QENHQA 261
Cdd:cd05933 74 YVAETSEANILVVENQKQLQKILQ--IQDKLPHLKAIIqYKEPLKE--KEPNLY------SWDEFMELGrsipdEQLDAI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 262 PVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTCADVHISYLPLAHMFERMVQS-VVYCHGGR 340
Cdd:cd05933 144 ISSQKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIwLPIKVGGQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 341 VGFFQGDIR--LLSDDMKALCPTIFPVVPRLLNRMYDKI---FSQAnTPLKRWLLEFAaKRKQAEV-------RSGIIRN 408
Cdd:cd05933 224 VYFAQPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkavGAKS-GTLKRKIASWA-KGVGLETnlklmggESPSPLF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 409 DSIWDELFFNKIQASLG--GCVRMIvTGAAPASPTVLGFLrAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPC 486
Cdd:cd05933 302 YRLAKKLVFKKVRKALGldRCQKFF-TGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 487 NHIKLVDVEelnywaCKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGE 566
Cdd:cd05933 380 CKTKIHNPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGE 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 567 YVAPEKIENIYIRSQP-VAQIYVHGDSLKaFLVGIVV------PD---------PEVMpSWAQKRGIEGTY-ADLCTNKD 629
Cdd:cd05933 454 NVPPVPIEDAVKKELPiISNAMLIGDKRK-FLSMLLTlkcevnPEtgepldeltEEAI-EFCRKLGSQATRvSEIAGGKD 531
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 327412323 630 LK--KAILEDMVRLGKESGLHSFEQVKAIHIHSDmFSVQNGLLTPTLKAKRPELREYFKKQIEELY 693
Cdd:cd05933 532 PKvyEAIEEGIKRVNKKAISNAQKIQKWVILEKD-FSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
121-671 |
7.67e-67 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 230.81 E-value: 7.67e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLGSgllQHNCKACTD--QFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTV 198
Cdd:cd17632 68 ITYAELWERVGAVAA---AHDPEQPVRpgDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 199 IVDKPQKAV---LLLEHverketPGLKLIILMDPFEEALKER-----------GQKCGVVIKSMQAVEDCGQENHQAPVP 264
Cdd:cd17632 145 AVSAEHLDLaveAVLEG------GTPPRLVVFDHRPEVDAHRaalesarerlaAVGIPVTTLTLIAVRGRDLPPAPLFRP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 265 PQPDD-LSIVCFTSGTTGNPKGAMLTHgNVVADFsgFLKVTESQWAPTCADVHISYLPLAHMFERMVQSVVYCHGGrVGF 343
Cdd:cd17632 219 EPDDDpLALLIYTSGSTGTPKGAMYTE-RLVATF--WLKVSSIQDIRPPASITLNFMPMSHIAGRISLYGTLARGG-TAY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 344 FQG--DIRLLSDDMKALCPTIFPVVPRLlnrmYDKIFSQANTPLKRWL-----LEFAAKRKQAEVRsgiirndsiwdelf 416
Cdd:cd17632 295 FAAasDMSTLFDDLALVRPTELFLVPRV----CDMLFQRYQAELDRRSvagadAETLAERVKAELR-------------- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 417 fnkiQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTtpgdwtSGHVGAPlPCNHIKLVDVEE 496
Cdd:cd17632 357 ----ERVLGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE--AGAVIL------DGVIVRP-PVLDYKLVDVPE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 497 LNYWACKG---EGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKI 573
Cdd:cd17632 424 LGYFRTDRphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARL 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 574 ENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMpswaqkrgiegtyaDLCTNKDLKKAILEDMVRLGKESGLHSFEQV 653
Cdd:cd17632 504 EAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDAL--------------AGEDTARLRAALAESLQRIAREAGLQSYEIP 569
|
570
....*....|....*...
gi 327412323 654 KAIHIHSDMFSVQNGLLT 671
Cdd:cd17632 570 RDFLIETEPFTIANGLLS 587
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
92-605 |
6.52e-66 |
|
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: 224.30 E-value: 6.52e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 92 MYQVFRRGLSISGNGPCLGFRkpkqpYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYS 171
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG-----GRRLTYAELDARARRLAAALRALGVGP--GDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 172 MVVVPLYDTLGPGAIRYIINTADISTVIVdkpqkAVLLlehverketpglkliilmdpfeealkergqkcgvviksmqav 251
Cdd:COG0318 74 AVVVPLNPRLTAEELAYILEDSGARALVT-----ALIL------------------------------------------ 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 252 edcgqenhqapvppqpddlsivcFTSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWAPTCADVHISYLPLAHMFErMVQ 331
Cdd:COG0318 107 -----------------------YTSGTTGRPKGVMLTHRNLLANAAAIAAA----LGLTPGDVVLVALPLFHVFG-LTV 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 332 SVVYC--HGGRV----GFfqgDIRLLSDDMKALCPTIFPVVPRLLNRMYDkifsqantplkrwllefAAKRKQAEVRSgi 405
Cdd:COG0318 159 GLLAPllAGATLvllpRF---DPERVLELIERERVTVLFGVPTMLARLLR-----------------HPEFARYDLSS-- 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 406 irndsiwdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAP 483
Cdd:COG0318 217 ----------------------LRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGRP 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 484 LPCNHIKLVDVE--ELnywACKGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFK 561
Cdd:COG0318 275 LPGVEVRIVDEDgrEL---PPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-DGWLRTGDLGRLDEDGYLYIVGRKKDMII 350
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 327412323 562 LAqGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFlvgiVVPDP 605
Cdd:COG0318 351 SG-GENVYPAEVEEVLAAHPGVAEAAVvgvpdekWGERVVAF----VVLRP 396
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
118-644 |
2.10e-64 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 223.45 E-value: 2.10e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 118 YQWLSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADIST 197
Cdd:cd17641 9 WQEFTWADYADRVRAFALGLLALGVG--RGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 198 VIVDKPQKAVLLLEHveRKETPGLKLIILMDP------------FEEALKERGQkcgvvikSMQAVEDCGQENHQAPVpp 265
Cdd:cd17641 87 VIAEDEEQVDKLLEI--ADRIPSVRYVIYCDPrgmrkyddprliSFEDVVALGR-------ALDRRDPGLYEREVAAG-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 266 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESqwAPTcaDVHISYLPLAHMFERM---VQSVVycHGGRVG 342
Cdd:cd17641 156 KGEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPL--GPG--DEYVSVLPLPWIGEQMysvGQALV--CGFIVN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 343 FFQgDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWL--------LEFAAKRKQAEVRSGIIRNDS-I 411
Cdd:cd17641 230 FPE-EPETMMEDLREIGPTFVLLPPRVWEGIAADVRArmMDATPFKRFMfelgmklgLRALDRGKRGRPVSLWLRLASwL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 412 WDELFFNKIQASLG-GCVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTEcTAGCTFTTP-GDWTSGHVGAPLPCNHI 489
Cdd:cd17641 309 ADALLFRPLRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTE-LAGAYTVHRdGDVDPDTVGVPFPGTEV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 490 KLVDVeelnywackgeGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVA 569
Cdd:cd17641 387 RIDEV-----------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFS 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 327412323 570 PEKIENIYIRSQPVAQIYVHGDSlKAFLVGIVVPDPEVMPSWAQKRGIE-GTYADLCTNKDLKKAILEDMVRLGKE 644
Cdd:cd17641 456 PQFIENKLKFSPYIAEAVVLGAG-RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKVNAS 530
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
121-678 |
2.34e-60 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 209.99 E-value: 2.34e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLgSGLLQHNCKACTDQfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:cd05914 8 LTYKDLADNIAKF-ALLLKINGVGTGDR-VALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 201 DKPqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhqapvppqpDDLSIVCFTSGTT 280
Cdd:cd05914 86 SDE----------------------------------------------------------------DDVALINYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 281 GNPKGAMLTHGNVVADFSG---FLKVTESqwaptcaDVHISYLPLAHMFERMVQSVVYCHGGRVGFFQGDI---RLLSDD 354
Cdd:cd05914 102 GNSKGVMLTYRNIVSNVDGvkeVVLLGKG-------DKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIpsaKIIALA 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 355 MKALCPTIfpVVPRLLNRMYDKIFSQANTPLKRWLLEFAAKrkqaevrsgIIRNDSIWdELFFNKIQASLGGCVRMIVTG 434
Cdd:cd05914 175 FAQVTPTL--GVPVPLVIEKIFKMDIIPKLTLKKFKFKLAK---------KINNRKIR-KLAFKKVHEAFGGNIKEFVIG 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 435 AAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPlpcnhIKLVDVEELNYWACKGEGEICVRGPN 514
Cdd:cd05914 243 GAKINPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKV-----IDGVEVRIDSPDPATGEGEIIVRGPN 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 515 VFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVA--QIYVHGDS 592
Cdd:cd05914 317 VMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLesLVVVQEKK 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 593 LKAflvgIVVPDPEVMPSWAQKrgiegtyadlctNKDLKKAILEDmVRLGKESGLHSFEQVKAIHIHSDMFSVqngllTP 672
Cdd:cd05914 397 LVA----LAYIDPDFLDVKALK------------QRNIIDAIKWE-VRDKVNQKVPNYKKISKVKIVKEEFEK-----TP 454
|
....*.
gi 327412323 673 TLKAKR 678
Cdd:cd05914 455 KGKIKR 460
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
121-615 |
8.11e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 204.37 E-value: 8.11e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGK-GDR-VAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 201 -------DKPQKAVL-LLEHVERKETP-GLKLIILMDPFEEALKergqkcgvviksmqavedCGQENHQAPvPPQPDDLS 271
Cdd:PRK07656 109 lglflgvDYSATTRLpALEHVVICETEeDDPHTEKMKTFTDFLA------------------AGDPAERAP-EVDPDDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 272 IVCFTSGTTGNPKGAMLTHGNV---VADFSGFLKVTESqwaptcaDVHISYLPLAHMFERMVqSVVYC--HGGRVgffqg 346
Cdd:PRK07656 170 DILFTSGTTGRPKGAMLTHRQLlsnAADWAEYLGLTEG-------DRYLAANPFFHVFGYKA-GVNAPlmRGATI----- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 347 dIRLLS---DDMKALC----PTIFPVVPRLLNRMYDkifsqantplkrwllefAAKRKQAEVRSgiirndsiwdelffnk 419
Cdd:PRK07656 237 -LPLPVfdpDEVFRLIeterITVLPGPPTMYNSLLQ-----------------HPDRSAEDLSS---------------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 420 iqaslggcVRMIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGCTFTTPGD---WTSGHVGAPLPCNHIKLVDve 495
Cdd:PRK07656 283 --------LRLAVTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIAGVENKIVN-- 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 496 ELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIE 574
Cdd:PRK07656 353 ELGEEVPVGEvGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IVGGFNVYPAEVE 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 327412323 575 NIYIRSQPVAQIYV-------HGDSLKAFLV---GIVVPDPEVMpSWAQKR 615
Cdd:PRK07656 432 EVLYEHPAVAEAAVigvpderLGEVGKAYVVlkpGAELTEEELI-AYCREH 481
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
93-598 |
4.39e-57 |
|
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: 200.87 E-value: 4.39e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 93 YQVFRRGLSISGNGPCLGFRKpkqpyQWLSYQEVADRAEFLGSGLLQHNCKaCTDQfIGVFAQNRPEWIIVELACYTYSM 172
Cdd:cd05936 2 ADLLEEAARRFPDKTALIFMG-----RKLTYRELDALAEAFAAGLQNLGVQ-PGDR-VALMLPNCPQFPIAYFGALKAGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 173 VVVPLYDTLGPGAIRYIINTADISTVIVDkpqkavlllehverketpglkliilmDPFEEALKergqkcgvviksmqave 252
Cdd:cd05936 75 VVVPLNPLYTPRELEHILNDSGAKALIVA--------------------------VSFTDLLA----------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 253 dcGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTcaDVHISYLPLAHMFErmvQS 332
Cdd:cd05936 112 --AGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEGD--DVVLAALPLFHVFG---LT 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 333 VVYCHGGRVGFFQ------GDIRLLsDDMKALCPTIFPVVPRLLNRmydkifsqantplkrwLLEFAAKRKqaEVRSGIi 406
Cdd:cd05936 185 VALLLPLALGATIvliprfRPIGVL-KEIRKHRVTIFPGVPTMYIA----------------LLNAPEFKK--RDFSSL- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 407 rndsiwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT-SGHVGAPLP 485
Cdd:cd05936 245 ----------------------RLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRkPGSIGIPLP 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 486 CNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQG 565
Cdd:cd05936 303 GTEVKIVD-DDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGG 379
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 327412323 566 EYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLV 598
Cdd:cd05936 380 FNVYPREVEEVLYEHPAVAEAAVvgvpdpySGEAVKAFVV 419
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
269-606 |
1.62e-56 |
|
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: 195.58 E-value: 1.62e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 269 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWAPTCADVHISYLPLAHMFerMVQSVVYC--HGGRVGFFQG 346
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS----GGLTEGDVFLSTLPLFHIG--GLFGLLGAllAGGTVVLLPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 347 -DIRLLSDDMKALCPTIFPVVPRLLNRMydkifsqantplkrwllefaakRKQAEVRSgiiRNDSiwdelffnkiqaslg 425
Cdd:cd04433 75 fDPEAALELIEREKVTILLGVPTLLARL----------------------LKAPESAG---YDLS--------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 426 gCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT--SGHVGAPLPCNHIKLVDVEElNYWACK 503
Cdd:cd04433 115 -SLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDPDG-GELPPG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 504 GEGEICVRGPNVFKGYLKDPDRTkEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSQPV 583
Cdd:cd04433 193 EIGELVVRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPGV 270
|
330 340
....*....|....*....|...
gi 327412323 584 AQIYVHGdslkaflvgivVPDPE 606
Cdd:cd04433 271 AEAAVVG-----------VPDPE 282
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
121-598 |
1.42e-54 |
|
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: 194.74 E-value: 1.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLK--KGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 201 DKPQKAVLLLehVERKETPGLKlIILMDPFEEALKERGQkcgvviksMQAVEDCGQENHQAPVPPQ-PDDLSIVCFTSGT 279
Cdd:cd05911 89 DPDGLEKVKE--AAKELGPKDK-IIVLDDKPDGVLSIED--------LLSPTLGEEDEDLPPPLKDgKDDTAAILYSSGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 280 TGNPKGAMLTHGNVVADFS---GFLKVTESQwaptcADVHISYLPLAHMF--ERMVQSVVYchGGRV----GFFqgdirl 350
Cdd:cd05911 158 TGLPKGVCLSHRNLIANLSqvqTFLYGNDGS-----NDVILGFLPLYHIYglFTTLASLLN--GATViimpKFD------ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 351 lSDDMKALCP----TIFPVVPRLLNRMydkifsqANTPLkrwllefaakrkqaevrsgiirndsiwdelfFNKIQASlgg 426
Cdd:cd05911 225 -SELFLDLIEkykiTFLYLVPPIAAAL-------AKSPL-------------------------------LDKYDLS--- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 427 CVRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKGE 505
Cdd:cd05911 263 SLRVILSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEP 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 506 GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIyIRSQP--- 582
Cdd:cd05911 343 GEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAV-LLEHPgva 420
|
490 500
....*....|....*....|.
gi 327412323 583 ---VAQIY--VHGDSLKAFLV 598
Cdd:cd05911 421 daaVIGIPdeVSGELPRAYVV 441
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
86-605 |
1.64e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 173.06 E-value: 1.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 86 YDDARTMYQVFRRGLSISGNGPCLGFRKPKqpyqwLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVEL 165
Cdd:PRK06187 2 QDYPLTIGRILRHGARKHPDKEAVYFDGRR-----TTYAELDERVNRLANALRALGVKK--GDRVAVFDWNSHEYLEAYF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 166 ACytySM---VVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlLLEHVE--RKETPGLKLIILMDPFEEALkergqk 240
Cdd:PRK06187 75 AV---PKigaVLHPINIRLKPEEIAYILNDAEDRVVLVDSE-----FVPLLAaiLPQLPTVRTVIVEGDGPAAP------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 241 CGVVIKSMQAVEDCGQENHQAPvPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVvadFSGFLKVTES-QWapTCADVHISY 319
Cdd:PRK06187 141 LAPEVGEYEELLAAASDTFDFP-DIDENDAAAMLYTSGTTGHPKGVVLSHRNL---FLHSLAVCAWlKL--SRDDVYLVI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 320 LPLAHMFERMVqsvvychgGRVGFFQG---------DIRLLSDDMKALCPTIFPVVPRLLNRMydkifSQANTPLKRWLl 390
Cdd:PRK06187 215 VPMFHVHAWGL--------PYLALMAGakqviprrfDPENLLDLIETERVTFFFAVPTIWQML-----LKAPRAYFVDF- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 391 efaakrkqaevrSGIirndsiwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFT 470
Cdd:PRK06187 281 ------------SSL-----------------------RLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVL 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 471 TPGDWTSGH------VGAPLPCNHIKLVDvEELNYWACKGE--GEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIG 542
Cdd:PRK06187 326 PPEDQLPGQwtkrrsAGRPLPGVEARIVD-DDGDELPPDGGevGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVG 403
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 327412323 543 KWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDP 605
Cdd:PRK06187 404 YIDEDGYLYITDRIKDVIISG-GENIYPRELEDA---------LYGHPAVAEVAVIG--VPDE 454
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
216-694 |
3.80e-41 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 160.65 E-value: 3.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 216 KETPGLKLIILMDPFE---------EALKERGQKCGvvIKSMQAVEDCGQENHQAPVPPQ-PDDLSIVCFTSGTTGNPKG 285
Cdd:PTZ00342 244 NDLSNELEDISLGPLEydkeklekiKDLKEKAKKLG--ISIILFDDMTKNKTTNYKIQNEdPDFITSIVYTSGTSGKPKG 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 286 AMLTHGNV------VADFSGFLKvtesqWAPtcaDVHISYLPLAHMFERMVQSVVYCHGGRVGFFQGDIRLLSDDMKALC 359
Cdd:PTZ00342 322 VMLSNKNLyntvvpLCKHSIFKK-----YNP---KTHLSYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 360 PTIFPVVPRLLNRMYDKIFSQAN--TPLKRWLlefaAKRKQAEVRSGIIRNDSIWDELFFN---KIQASLGGCVRMIVTG 434
Cdd:PTZ00342 394 GNILAGVPKVFNRIYTNIMTEINnlPPLKRFL----VKKILSLRKSNNNGGFSKFLEGITHissKIKDKVNPNLEVILNG 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 435 AAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPG-DWTSGHVGAPL-PCNHIKLVDVEELNYWACKGEGEICVRG 512
Cdd:PTZ00342 470 GGKLSPKIAEELSVLLNVNYYQGYGLTE-TTGPIFVQHAdDNNTESIGGPIsPNTKYKVRTWETYKATDTLPKGELLIKS 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 513 PNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHG-D 591
Cdd:PTZ00342 549 DSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGdD 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 592 SLKAFLvGIVVPDPEVM------PSWAQKRGI-EGTYADLCTNKDLKKAILEDMVR-----LGKESGLHSFEQVKAIHIH 659
Cdd:PTZ00342 629 SMDGPL-AIISVDKYLLfkclkdDNMLESTGInEKNYLEKLTDETINNNIYVDYVKgkmleVYKKTNLNRYNIINDIYLT 707
|
490 500 510
....*....|....*....|....*....|....*...
gi 327412323 660 SDMFSVQNgLLTPTLKAKRPEL-REY--FKKQIEELYS 694
Cdd:PTZ00342 708 SKVWDTNN-YLTPTFKVKRFYVfKDYafFIDQVKKIYK 744
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
121-609 |
1.02e-40 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 154.76 E-value: 1.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLgSGLLQHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIv 200
Cdd:cd05941 12 ITYADLVARAARL-ANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 201 dkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhqapvppqpdDLSIVCFTSGTT 280
Cdd:cd05941 90 --------------------------------------------------------------------DPALILYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 281 GNPKGAMLTHGNVVADfsgfLKVTESQWAPTCADVHISYLPLAHmfermVQSVV-------YChGGRV---GFFQGDIRL 350
Cdd:cd05941 102 GRPKGVVLTHANLAAN----VRALVDAWRWTEDDVLLHVLPLHH-----VHGLVnallcplFA-GASVeflPKFDPKEVA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 351 LSDDMKALcpTIFPVVPRllnrMYDKIFS--QANTPLKRWLLEFAAKRkqaevrsgiirndsiwdelffnkiqaslggcV 428
Cdd:cd05941 172 ISRLMPSI--TVFMGVPT----IYTRLLQyyEAHFTDPQFARAAAAER-------------------------------L 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 429 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTTP--GDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEG 506
Cdd:cd05941 215 RLMVSGSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVDEETGEPLPRGEVG 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 507 EICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKK-HIFKlAQGEYVAPEKIENIyIRSQP-VA 584
Cdd:cd05941 293 EIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEIERV-LLAHPgVS 370
|
490 500
....*....|....*....|....*...
gi 327412323 585 QIYVHGDSLKAF---LVGIVVPDPEVMP 609
Cdd:cd05941 371 ECAVIGVPDPDWgerVVAVVVLRAGAAA 398
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
121-576 |
4.00e-40 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 154.03 E-value: 4.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLGSgLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:cd05909 8 LTYRKLLTGAIALAR-KLAKMTKE--GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 201 DKPQKAVLLLEHVERKETPgLKLIILmdpfeEALKER---GQKCGVVIKSMQAVEDCGQENHQAPVppQPDDLSIVCFTS 277
Cdd:cd05909 85 SKQFIEKLKLHHLFDVEYD-ARIVYL-----EDLRAKiskADKCKAFLAGKFPPKWLLRIFGVAPV--QPDDPAVILFTS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 278 GTTGNPKGAMLTHGNVVADFSGFLKVTEsqwaPTCADVHISYLPLAHMFermvqsvvychggrvGFFQGDIRLLSDDMKA 357
Cdd:cd05909 157 GSEGLPKGVVLSHKNLLANVEQITAIFD----PNPEDVVFGALPFFHSF---------------GLTGCLWLPLLSGIKV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 358 LC---PTIFPVVPRLLnrmYDK----IFSqanTPLkrwLLEFAAKRKQAEVRSGIirndsiwdelffnkiqaslggcvRM 430
Cdd:cd05909 218 VFhpnPLDYKKIPELI---YDKkatiLLG---TPT---FLRGYARAAHPEDFSSL-----------------------RL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 431 IVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEIC 509
Cdd:cd05909 266 VVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLL 345
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 327412323 510 VRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENI 576
Cdd:cd05909 346 VRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDI 410
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
96-605 |
1.24e-38 |
|
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: 148.53 E-value: 1.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 96 FRRGLSISGNGPCLGFRKpkqpyQWLSYQEVADRAEFLGSGLlQHNCKACTDQfIGVFAQNRPEWIIVELACYTYSMVVV 175
Cdd:cd17631 1 LRRRARRHPDRTALVFGG-----RSLTYAELDERVNRLAHAL-RALGVAKGDR-VAVLSKNSPEFLELLFAAARLGAVFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 176 PLYDTLGPGAIRYIINTADiSTVIVDkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcg 255
Cdd:cd17631 74 PLNFRLTPPEVAYILADSG-AKVLFD------------------------------------------------------ 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 256 qenhqapvppqpdDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLkvteSQWAPTCADVHISYLPLAHMFE-RMVQSVV 334
Cdd:cd17631 99 -------------DLALLMYTSGTTGRPKGAMLTHRNLLWNAVNAL----AALDLGPDDVLLVVAPLFHIGGlGVFTLPT 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 335 YCHGGRV----GFFQGDIRLLSDDMKAlcpTIFPVVPRLLNRMydkifsqANTPLkrwllefaakrkqaevrsgiirnds 410
Cdd:cd17631 162 LLRGGTVvilrKFDPETVLDLIERHRV---TSFFLVPTMIQAL-------LQHPR------------------------- 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 411 iWDELFFnkiqASLggcvRMIVTGAAPASPTVLGFLRAAlGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPCNH 488
Cdd:cd17631 207 -FATTDL----SSL----RAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHRRklGSAGRPVFFVE 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 489 IKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYV 568
Cdd:cd17631 277 VRIVD-PDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFR-DGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENV 353
|
490 500 510
....*....|....*....|....*....|....*..
gi 327412323 569 APEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDP 605
Cdd:cd17631 354 YPAEVEDV---------LYEHPAVAEVAVIG--VPDE 379
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
247-576 |
3.12e-38 |
|
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: 148.92 E-value: 3.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 247 SMQAVEDCGQENHQAPVPPQ--PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTcaDVHISYLPLAH 324
Cdd:cd05904 135 SLSFSDLLFEADEAEPPVVVikQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSE--DVFLCVLPMFH 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 325 MFermvqsvvychgGRVGFFQGDIRL-----------LSDDMKALCP---TIFPVVPrllnrmydkifsqantPLkrwll 390
Cdd:cd05904 213 IY------------GLSSFALGLLRLgatvvvmprfdLEELLAAIERykvTHLPVVP----------------PI----- 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 391 eFAAKRKQAEVRSGIIRndsiwdelffnkiqaSLggcvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTF 469
Cdd:cd05904 260 -VLALVKSPIVDKYDLS---------------SL----RQIMSGAAPLGKELIeAFRAKFPNVDLGQGYGMTESTGVVAM 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 470 TTP---GDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLP 546
Cdd:cd05904 320 CFApekDRAKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDE 399
|
330 340 350
....*....|....*....|....*....|
gi 327412323 547 AGTLKIIDRKKHIFKLaQGEYVAPEKIENI 576
Cdd:cd05904 400 DGYLFIVDRLKELIKY-KGFQVAPAELEAL 428
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
120-683 |
1.10e-34 |
|
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: 138.21 E-value: 1.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 120 WLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVI 199
Cdd:cd05926 14 ALTYADLAELVDDLARQLAALGIKK--GDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 200 VDKpqkaVLLLEHVERKETPGLkliilmdpfeeALKERGQKCGVVIKSMQAVE----DCGQENHQAPVPPQPDDLSIVCF 275
Cdd:cd05926 92 TPK----GELGPASRAASKLGL-----------AILELALDVGVLIRAPSAESlsnlLADKKNAKSEGVPLPDDLALILH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 276 TSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWAPTCADVHISYLPLAHMFERMVQ--SVVYChGGRV----GFfqgDIR 349
Cdd:cd05926 157 TSGTTGRPKGVPLTHRNLAASATNITNT----YKLTPDDRTLVVMPLFHVHGLVASllSTLAA-GGSVvlppRF---SAS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 350 LLSDDMKALCPTIFPVVPRLLnrmydKIfsqantplkrwLLEFAAKRKQAEvrsgiirndsiwdelfFNKIqaslggcvR 429
Cdd:cd05926 229 TFWPDVRDYNATWYTAVPTIH-----QI-----------LLNRPEPNPESP----------------PPKL--------R 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 430 MIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTP---GDWTSGHVGAPlpcNHIKLVDVEElnywacKGE- 505
Cdd:cd05926 269 FIRSCSASLPPAVLEALEATFGAPVLEAYGMTE-AAHQMTSNPlppGPRKPGSVGKP---VGVEVRILDE------DGEi 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 506 ------GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIR 579
Cdd:cd05926 339 lppgvvGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVLLS 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 580 SQPVAQIYVHGdslkaflvgivVPDP---EVMPSWAQKRgiEGTYADlctnkdlKKAILEDMvrlgkESGLHSFEQVKAI 656
Cdd:cd05926 418 HPAVLEAVAFG-----------VPDEkygEEVAAAVVLR--EGASVT-------EEELRAFC-----RKHLAAFKVPKKV 472
|
570 580
....*....|....*....|....*..
gi 327412323 657 HIhsdmfsVQNGLLTPTLKAKRPELRE 683
Cdd:cd05926 473 YF------VDELPKTATGKIQRRKVAE 493
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
255-604 |
1.46e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 138.98 E-value: 1.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 255 GQENHQAPVP-PQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgflkVTESQ-WAPTCAD---VHISYLPLAHMFE-R 328
Cdd:PRK05605 205 GGDGSDVSHPrPTPDDVALILYTSGTTGKPKGAQLTHRNLFAN------AAQGKaWVPGLGDgpeRVLAALPMFHAYGlT 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 329 MVQSV-VYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLlnrmYDKIfsqantplkrwlLEFAAKRkqaevrsGIir 407
Cdd:PRK05605 279 LCLTLaVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPL----YEKI------------AEAAEER-------GV-- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 408 ndsiwdelffnkiqaSLGGcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECT---AGCTFTTpgDWTSGHVGAPL 484
Cdd:PRK05605 334 ---------------DLSG-VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpiiVGNPMSD--DRRPGYVGVPF 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 485 PCNHIKLVDVEELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLA 563
Cdd:PRK05605 396 PDTEVRIVDPEDPDETMPDGEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELI-IT 473
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 327412323 564 QGEYVAPEKIENIyirsqpVAQiyvHGDSLKAFLVGIVVPD 604
Cdd:PRK05605 474 GGFNVYPAEVEEV------LRE---HPGVEDAAVVGLPRED 505
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
255-598 |
6.93e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 136.82 E-value: 6.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 255 GQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTCaDVHISYLPLAHM----FERMV 330
Cdd:PRK05677 194 GAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEGC-EILIAPLPLYHIyaftFHCMA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 331 QSVVYCHGgrvgffqgdiRLLSDdmkalcPTIFPVVPRLLNRMYDKIFSQANTplkrwllEFAAkrkqaevrsgiIRNDS 410
Cdd:PRK05677 273 MMLIGNHN----------ILISN------PRDLPAMVKELGKWKFSGFVGLNT-------LFVA-----------LCNNE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 411 IWDELFFNKIQASLGGcvRMIVTGAAPASptvlgfLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIK 490
Cdd:PRK05677 319 AFRKLDFSALKLTLSG--GMALQLATAER------WKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCK 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 491 LVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAP 570
Cdd:PRK05677 391 VID-DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVSGFNVYP 468
|
330 340 350
....*....|....*....|....*....|....*.
gi 327412323 571 EKIENIyIRSQP----VAQIYV----HGDSLKAFLV 598
Cdd:PRK05677 469 NELEDV-LAALPgvlqCAAIGVpdekSGEAIKVFVV 503
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
263-598 |
8.44e-33 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 133.64 E-value: 8.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 263 VPPQ--PDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgflkVTESQWA--PTCADVH---ISYLPLAHMFERMVQSVVY 335
Cdd:PRK08974 199 VKPElvPEDLAFLQYTGGTTGVAKGAMLTHRNMLAN------LEQAKAAygPLLHPGKelvVTALPLYHIFALTVNCLLF 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 336 CHGGrvgffqGDIRLLSDdmkalcPTIFPVVPRLLNRMYDKIFSQANTPLKRWLlefaakrkqaevrsgiirNDSIWDEL 415
Cdd:PRK08974 273 IELG------GQNLLITN------PRDIPGFVKELKKYPFTAITGVNTLFNALL------------------NNEEFQEL 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 416 FFNKIQASLGGcvrmivtgAAPASPTVLGFLRAALGCQVYEGYGQTECT---AGCTFTTPGdwTSGHVGAPLPCNHIKLV 492
Cdd:PRK08974 323 DFSSLKLSVGG--------GMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVNPYDLDY--YSGSIGLPVPSTEIKLV 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 493 DvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEK 572
Cdd:PRK08974 393 D-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMI-LVSGFNVYPNE 469
|
330 340 350
....*....|....*....|....*....|...
gi 327412323 573 IENIYIRSQPVAQIY-------VHGDSLKAFLV 598
Cdd:PRK08974 470 IEDVVMLHPKVLEVAavgvpseVSGEAVKIFVV 502
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
117-557 |
9.86e-33 |
|
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: 133.18 E-value: 9.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 117 PYQWLSYQEVADRAEFLGSGLLQHNCKAcTDQFIGVFAQNRpEWIIVELACYTYSMVVVPLydtlGPGAIRyiintadis 196
Cdd:cd05906 36 SEEFQSYQDLLEDARRLAAGLRQLGLRP-GDSVILQFDDNE-DFIPAFWACVLAGFVPAPL----TVPPTY--------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 197 tvivDKPQKAVLLLEHVerKETPGLKLII----LMDPFEEALKERGQkCGVVIKSMQAVEDCGqENHQAPvPPQPDDLSI 272
Cdd:cd05906 101 ----DEPNARLRKLRHI--WQLLGSPVVLtdaeLVAEFAGLETLSGL-PGIRVLSIEELLDTA-ADHDLP-QSRPDDLAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 273 VCFTSGTTGNPKGAMLTHGNVVADFSGflKVTESQWAPtcADVHISYLPLAHmfermVQSVVYCHggrvgffQGDIRLLS 352
Cdd:cd05906 172 LMLTSGSTGFPKAVPLTHRNILARSAG--KIQHNGLTP--QDVFLNWVPLDH-----VGGLVELH-------LRAVYLGC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 353 DDMKALCPTIFPVVPRLLNRMyDKiFSQANTplkrWLLEFA-AK-RKQAEVRSgiirnDSIWDelffnkiqasLGGCVRM 430
Cdd:cd05906 236 QQVHVPTEEILADPLRWLDLI-DR-YRVTIT----WAPNFAfALlNDLLEEIE-----DGTWD----------LSSLRYL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 431 IVTGAAPASPTVLGFLRAALGCQVYE-----GYGQTECTAGCTFTTP---GDWTSGH----VGAPLPCNHIKLVDVEEln 498
Cdd:cd05906 295 VNAGEAVVAKTIRRLLRLLEPYGLPPdairpAFGMTETCSGVIYSRSfptYDHSQALefvsLGRPIPGVSMRIVDDEG-- 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 327412323 499 ywACKGEGEIC---VRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkWLPAGTLKIIDRKK 557
Cdd:cd05906 373 --QLLPEGEVGrlqVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
255-605 |
1.42e-32 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 133.08 E-value: 1.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 255 GQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSgflkvTESQWAPTCA------DVHISYLPLAHMFER 328
Cdd:PRK08751 195 GRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQ-----QAHQWLAGTGkleegcEVVITALPLYHIFAL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 329 MVQSVVYCHGGrvgffqGDIRLLSDdmkalcPTIFPVVPRLLNRMYDKIFSQANTPLKRWLlefaakrkqaevrsgiirN 408
Cdd:PRK08751 270 TANGLVFMKIG------GCNHLISN------PRDMPGFVKELKKTRFTAFTGVNTLFNGLL------------------N 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 409 DSIWDELFFNKIQASLGGcvRMIVTGAapasptVLGFLRAALGCQVYEGYGQTECT-AGCTFTTPGDWTSGHVGAPLPCN 487
Cdd:PRK08751 320 TPGFDQIDFSSLKMTLGG--GMAVQRS------VAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLPIPST 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 488 HIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEY 567
Cdd:PRK08751 392 DACIKD-DAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-LVSGFN 469
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 327412323 568 VAPEKIENIYIRSQPVAQIYVHG----DSLKAFLVGIVVPDP 605
Cdd:PRK08751 470 VYPNEIEDVIAMMPGVLEVAAVGvpdeKSGEIVKVVIVKKDP 511
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
89-694 |
5.68e-32 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 133.44 E-value: 5.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 89 ARTMYQVFRRGLSISGNGPCLGFRKPKQPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACY 168
Cdd:PTZ00297 426 VRSLGEMWERSVTRHSTFRCLGQTSESGESEWLTYGTVDARARELGSGLLALGVRP--GDVIGVDCEASRNIVILEVACA 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 169 TYSMVVVPLydtLGPG-AIRYIINTADISTVIVDKPQKAVLLLEHVERKETpglklIILMDPFEEALKERGQK-CGVVIK 246
Cdd:PTZ00297 504 LYGFTTLPL---VGKGsTMRTLIDEHKIKVVFADRNSVAAILTCRSRKLET-----VVYTHSFYDEDDHAVARdLNITLI 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 247 SMQAVEdcgQENHQAPVPPQP--DDLSIVCFTSGTTGNPKGAML-----THGNVVADFSGFLKvteSQWAPTCADVH--I 317
Cdd:PTZ00297 576 PYEFVE---QKGRLCPVPLKEhvTTDTVFTYVVDNTTSASGDGLavvrvTHADVLRDISTLVM---TGVLPSSFKKHlmV 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 318 SYLPLAHMFERMVQSVVYCHGGRVGffQGDIRLLSDDMKALCPTIFPVVPRLlnrmydkiFSQANTPLKR---------- 387
Cdd:PTZ00297 650 HFTPFAMLFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSL--------FSTSRLQLSRanerysavys 719
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 388 WLLEfaakrKQAEVRSGII----RNDSIWDELFFNKIQASLGGCVRMIVTGAAPASPTV-----LGFLRAALGCQVYegy 458
Cdd:PTZ00297 720 WLFE-----RAFQLRSRLInihrRDSSLLRFIFFRATQELLGGCVEKIVLCVSEESTSFsllehISVCYVPCLREVF--- 791
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 459 gQTECTAGCTFTtpgdwtsghvGAPLPCNHIKLVDVEELNYWACKGEGEICVRGpnvfkgylkDPDRTKEAldsdgwlht 538
Cdd:PTZ00297 792 -FLPSEGVFCVD----------GTPAPSLQVDLEPFDEPSDGAGIGQLVLAKKG---------EPRRTLPI--------- 842
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 539 gdIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAfLVGIVVPDPEVMP-SWAQKRGI 617
Cdd:PTZ00297 843 --AAQWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEfEWRQSHCM 919
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 618 E--GTYADLCTNKDLKK----AILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEE 691
Cdd:PTZ00297 920 GegGGPARQLGWTELVAyassLLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIER 999
|
...
gi 327412323 692 LYS 694
Cdd:PTZ00297 1000 FYS 1002
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
121-588 |
1.00e-31 |
|
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: 128.65 E-value: 1.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADIstviv 200
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGP--GDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 201 dkpqkavlllehverketpglKLIILMDPFeealkergqkcgvviksmqavedcGQENHQApvppQPDDLSIVCFTSGTT 280
Cdd:cd05903 75 ---------------------KVFVVPERF------------------------RQFDPAA----MPDAVALLLFTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 281 GNPKGAMLTHGNVVADFSGFLKvtesQWAPTCADVHISYLPLAHmfermvqsvvycHGGRVGFFqgdirllsddmkaLCP 360
Cdd:cd05903 106 GEPKGVMHSHNTLSASIRQYAE----RLGLGPGDVFLVASPMAH------------QTGFVYGF-------------TLP 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 361 TIFPVvPRLLNRMYDK------------IFSQANTPLKRWLLEfaAKRKQAEVRSGIirndsiwdelffnkiqaslggcv 428
Cdd:cd05903 157 LLLGA-PVVLQDIWDPdkalalmrehgvTFMMGATPFLTDLLN--AVEEAGEPLSRL----------------------- 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 429 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGD----WTSGhvGAPLPCNHIKLVDvEELNYWACKG 504
Cdd:cd05903 211 RTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPedrrLYTD--GRPLPGVEIKVVD-DTGATLAPGV 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 505 EGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVA 584
Cdd:cd05903 288 EGELLSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVI 365
|
....
gi 327412323 585 QIYV 588
Cdd:cd05903 366 EAAV 369
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
261-607 |
1.98e-31 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 129.37 E-value: 1.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 261 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADF--------SGFLKVTE-SQWAPTCAdvhisyLPLAHMFERMVQ 331
Cdd:PRK07059 197 KPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqmeawlqPAFEKKPRpDQLNFVCA------LPLYHIFALTVC 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 332 SVVYCHGGRVGFF---QGDIRLLSDDMKALCPTIFPVVPRLLNRMYdkifsqaNTPlkrwllEFaakrkqaevrsgiirn 408
Cdd:PRK07059 271 GLLGMRTGGRNILipnPRDIPGFIKELKKYQVHIFPAVNTLYNALL-------NNP------DF---------------- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 409 dsiwDELFFNKIQASLGGcvrmivtGAAPASPTVLGFLRAAlGCQVYEGYG--QTECTAGCTFTTPGDWTsGHVGAPLPC 486
Cdd:PRK07059 322 ----DKLDFSKLIVANGG-------GMAVQRPVAERWLEMT-GCPITEGYGlsETSPVATCNPVDATEFS-GTIGLPLPS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 487 NHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGE 566
Cdd:PRK07059 389 TEVSIRD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMI-LVSGF 466
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 327412323 567 YVAPEKIENIyIRSQP----VAQIYVH----GDSLKAFlvgIVVPDPEV 607
Cdd:PRK07059 467 NVYPNEIEEV-VASHPgvleVAAVGVPdehsGEAVKLF---VVKKDPAL 511
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
269-599 |
3.13e-31 |
|
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: 124.92 E-value: 3.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 269 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSgflkvtesQWApTCADVHIS--YL---PLAHMFErmvqsvvYCHGGRVGF 343
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAA--------AWA-DCADLTEDdrYLiinPFFHTFG-------YKAGIVACL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 344 FQGdirllsddmkalcPTIFPV----VPRLLNRMYDKIFSQANTP--LKRWLLEFAAkRKQAEVRSgiirndsiwdelff 417
Cdd:cd17638 65 LTG-------------ATVVPVavfdVDAILEAIERERITVLPGPptLFQSLLDHPG-RKKFDLSS-------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 418 nkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGcTFTTPGD---WTSGHVGAPLPCNHIKLVD 493
Cdd:cd17638 117 ----------LRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVA-TMCRPGDdaeTVATTCGRACPGFEVRIAD 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 494 veelnywackgEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKI 573
Cdd:cd17638 186 -----------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEV 253
|
330 340 350
....*....|....*....|....*....|...
gi 327412323 574 ENIYIRSQPVAQIYV-------HGDSLKAFLVG 599
Cdd:cd17638 254 EGALAEHPGVAQVAVigvpderMGEVGKAFVVA 286
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
150-643 |
4.22e-31 |
|
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: 126.79 E-value: 4.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 150 IGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlllehVERKETPGLKLIILMDP 229
Cdd:TIGR01923 27 VALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL---------LEEKDFQADSLDRIEAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 230 FEEALKERGQKcgvviksmqavedcgqenhqapvppQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF---LKVTES 306
Cdd:TIGR01923 98 GRYETSLSASF-------------------------NMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSkenLGFTED 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 307 qwaptcaDVHISYLPLAHMFErmvQSVVY---CHGGRVGFFQGDIRLLsDDMKALCPTIFPVVPRLLNRMYDKifSQANT 383
Cdd:TIGR01923 153 -------DNWLLSLPLYHISG---LSILFrwlIEGATLRIVDKFNQLL-EMIANERVTHISLVPTQLNRLLDE--GGHNE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 384 PLKRWLLefaakrkqaevrsgiirndsiwdelffnkiqaslGGcvrmivtGAAPASptvlgFLRAAL--GCQVYEGYGQT 461
Cdd:TIGR01923 220 NLRKILL----------------------------------GG-------SAIPAP-----LIEEAQqyGLPIYLSYGMT 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 462 E-CTAGCTFTTPGDWTSGHVGAPLPCNHIKL-VDVEElnywackGEGEICVRGPNVFKGYLkDPDRTKEALDSDGWLHTG 539
Cdd:TIGR01923 254 EtCSQVTTATPEMLHARPDVGRPLAGREIKIkVDNKE-------GHGEIMVKGANLMKGYL-YQGELTPAFEQQGWFNTG 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 540 DIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQiyvhgdslkAFLVGivVPDPEvmpsWAQKrgieg 619
Cdd:TIGR01923 326 DIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQE---------AVVVP--KPDAE----WGQV----- 384
|
490 500
....*....|....*....|....*.
gi 327412323 620 TYADLCTNKDLKKAILEDMV--RLGK 643
Cdd:TIGR01923 385 PVAYIVSESDISQAKLIAYLteKLAK 410
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
121-590 |
7.71e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 127.58 E-value: 7.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVV---PLYDT------LGPGAIRYII- 190
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQP--GDRVGIWAPNCAEWLLTQFATARIGAILVninPAYRAseleyaLGQSGVRWVIc 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 191 ----NTADISTVIVD-KPQKAVLLLEHVERKETPGLKLIILMDPFE-------EALKERGQkcGVvikSMQAVEDcgqen 258
Cdd:PRK12583 124 adafKTSDYHAMLQElLPGLAEGQPGALACERLPELRGVVSLAPAPppgflawHELQARGE--TV---SREALAE----- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 259 HQAPVppQPDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSG-FLKVTESqwaptcaDVHISYLPLAHMFErMVQSVVY 335
Cdd:PRK12583 194 RQASL--DRDDPINIQYTSGTTGFPKGATLSHHNILnnGYFVAeSLGLTEH-------DRLCVPVPLYHCFG-MVLANLG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 336 C--HGGRVGF----FQGDIRLLSDDMKAlCPTIFPVvPRLLnrmydkiFSQANTPlKRWLLEFAAkrkqaeVRSGIIrnd 409
Cdd:PRK12583 264 CmtVGACLVYpneaFDPLATLQAVEEER-CTALYGV-PTMF-------IAELDHP-QRGNFDLSS------LRTGIM--- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 410 siwdelffnkiqaslggcvrmivtGAAPASPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGD-----WTSghVGAP 483
Cdd:PRK12583 325 ------------------------AGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSLQTTAADdlerrVET--VGRT 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 484 LPCNHIKLVDVEELNywACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkL 562
Cdd:PRK12583 379 QPHLEVKVVDPDGAT--VPRGEiGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMI-I 455
|
490 500
....*....|....*....|....*...
gi 327412323 563 AQGEYVAPEKIENIYIRSQPVAQIYVHG 590
Cdd:PRK12583 456 RGGENIYPREIEEFLFTHPAVADVQVFG 483
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
122-576 |
8.80e-31 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 127.56 E-value: 8.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 122 SYQEVADRAEFLGSGLLQHNCKACTdqfigVFAQNRPEW---IIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTV 198
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGD-----RVAFQLPGWcefTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 199 IVDKPQKAV--LLLEHVERKETPGLKLIILMDPFEEALKErgqkcgvvIKSMQAVEDcgQENHQAPVPPQPDDLSIVCFT 276
Cdd:PRK06087 126 FAPTLFKQTrpVDLILPLQNQLPQLQQIVGVDKLAPATSS--------LSLSQIIAD--YEPLTTAITTHGDELAAVLFT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 277 SGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAptcaDVHISYLPLAHmfermvqSVVYCHGGRVGFFQGDIRLLSDDMK 356
Cdd:PRK06087 196 SGTEGLPKGVMLTHNNILASERAYCARLNLTWQ----DVFMMPAPLGH-------ATGFLHGVTAPFLIGARSVLLDIFT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 357 AlcptifPVVPRLLNRmyDKI-FSQANTPLkrwllefaakrkqaevrsgiirndsIWDELFFNKIQASLGGCVRMIVTGA 435
Cdd:PRK06087 265 P------DACLALLEQ--QRCtCMLGATPF-------------------------IYDLLNLLEKQPADLSALRFFLCGG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 436 APASPTVLgflRAAL--GCQVYEGYGQTECTAGcTFTTPGD---WTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICV 510
Cdd:PRK06087 312 TTIPKKVA---RECQqrGIKLLSVYGSTESSPH-AVVNLDDplsRFMHTDGYAAAGVEIKVVD-EARKTLPPGCEGEEAS 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 327412323 511 RGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENI 576
Cdd:PRK06087 387 RGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDI 451
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
122-606 |
1.13e-30 |
|
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: 126.87 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 122 SYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLgpgAIRYIINTADIST-VIV 200
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLK--QNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIY---NERELDHSLNISKpTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 201 DKPQKAVLLLEHVERKeTPGLKLIILMDPFEEAlkeRGQKCGVVIKSMQAVEDCGQENHQAPVPPQPDDLSIVCFTSGTT 280
Cdd:cd17642 121 FCSKKGLQKVLNVQKK-LKIIKTIIILDSKEDY---KGYQCLYTFITQNLPPGFNEYDFKPPSFDRDEQVALIMNSSGST 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 281 GNPKGAMLTHGNVVADFSGFLKVT-ESQWAPTCAdvHISYLPLAHMFERMVQSVVYCHGGRVGF---FQGD--IRLLSD- 353
Cdd:cd17642 197 GLPKGVQLTHKNIVARFSHARDPIfGNQIIPDTA--ILTVIPFHHGFGMFTTLGYLICGFRVVLmykFEEElfLRSLQDy 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 354 --DMKALCPTIFPVVPR--LLNRmYD----KIFSQANTPLKRWLLEFAAKRkqaevrsgiirndsiwdelfFNkiqaslg 425
Cdd:cd17642 275 kvQSALLVPTLFAFFAKstLVDK-YDlsnlHEIASGGAPLSKEVGEAVAKR--------------------FK------- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 426 gcvrmivtgaapasptvLGFLRaalgcqvyEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKGE 505
Cdd:cd17642 327 -----------------LPGIR--------QGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNER 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 506 GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRsqpvaq 585
Cdd:cd17642 382 GELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQ------ 454
|
490 500
....*....|....*....|.
gi 327412323 586 iyvHGDSLKAFLVGIvvPDPE 606
Cdd:cd17642 455 ---HPKIFDAGVAGI--PDED 470
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
150-606 |
3.04e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 124.92 E-value: 3.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 150 IGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAvlllehverketpglkliilmdp 229
Cdd:PRK09088 50 LAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDDAVAA----------------------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 230 feealkerGQKCGVVIKSMQAVEDCGQENHQAPVPPqpDDLSIVCFTSGTTGNPKGAMLTHGN---VVADFSGFLKVtes 306
Cdd:PRK09088 107 --------GRTDVEDLAAFIASADALEPADTPSIPP--ERVSLILFTSGTSGQPKGVMLSERNlqqTAHNFGVLGRV--- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 307 qwaptcaDVHISYLPLAHMFE--RMVQSV--VYCHGGRV----GFFQG-DIRLLSDdmKALCPTIFPVVPRLLNRmydki 377
Cdd:PRK09088 174 -------DAHSSFLCDAPMFHiiGLITSVrpVLAVGGSIlvsnGFEPKrTLGRLGD--PALGITHYFCVPQMAQA----- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 378 fsqantplkrwllefaakrkqaevrsgiIRNDSIWDELFFNKIQAslggcvrmIVTGAAP-ASPTVLGFLraALGCQVYE 456
Cdd:PRK09088 240 ----------------------------FRAQPGFDAAALRHLTA--------LFTGGAPhAAEDILGWL--DDGIPMVD 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 457 GYGQTEctAGCTFTTPGDWT-----SGHVGAPLPCNHIKLVDVEELNYWAckGE-GEICVRGPNVFKGYLKDPDRTKEAL 530
Cdd:PRK09088 282 GFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVVDDQGNDCPA--GVpGELLLRGPNLSPGYWRRPQATARAF 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 327412323 531 DSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIEniyirsqpvAQIYVHGDSLKAFLVGivVPDPE 606
Cdd:PRK09088 358 TGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIE---------AVLADHPGIRECAVVG--MADAQ 421
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-590 |
3.46e-30 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 122.00 E-value: 3.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSGF-LKVTESqwaptcaDVHISYLPLAHMFErMVQSVVYC--HGGRV 341
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVnnGYFIGErLGLTEQ-------DRLCIPVPLFHCFG-SVLGVLACltHGATM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 342 GFFQgdirlLSDDMKAL--------C------PTIFPvvpRLLNRMydkifSQANTPLKRwllefaakrkqaeVRSGIIr 407
Cdd:cd05917 73 VFPS-----PSFDPLAVleaiekekCtalhgvPTMFI---AELEHP-----DFDKFDLSS-------------LRTGIM- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 408 ndsiwdelffnkiqaslggcvrmivtGAAPASPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGDWTS---GHVGAP 483
Cdd:cd05917 126 --------------------------AGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDSIEkrvNTVGRI 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 484 LPCNHIKLVDvEELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkL 562
Cdd:cd05917 180 MPHTEAKIVD-PEGGIVPPVGVpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-I 257
|
330 340
....*....|....*....|....*...
gi 327412323 563 AQGEYVAPEKIENIYIRSQPVAQIYVHG 590
Cdd:cd05917 258 RGGENIYPREIEEFLHTHPKVSDVQVVG 285
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
121-613 |
4.74e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 125.10 E-value: 4.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAE-----FLGSGLLQHNCkactdqfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADI 195
Cdd:PRK06188 38 LTYGQLADRISryiqaFEALGLGTGDA-------VALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 196 STVIVDK---PQKAVLLLEHVerketPGLKLIILMDPFEEAlkergqkcgvviksmqavEDCGQENHQAPVPP-----QP 267
Cdd:PRK06188 111 STLIVDPapfVERALALLARV-----PSLKHVLTLGPVPDG------------------VDLLAAAAKFGPAPlvaaaLP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 268 DDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLkvTESQWAPtcadvHISYL---PLAHMFERMVQSVVYchggRVGFF 344
Cdd:PRK06188 168 PDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQL--AEWEWPA-----DPRFLmctPLSHAGGAFFLPTLL----RGGTV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 345 qgdIRLLSDDMKALCPTI--------FpVVPRLLNRmydkifsqantplkrwLLEFAAKRKqaevrsgiiRNDSiwdelf 416
Cdd:PRK06188 237 ---IVLAKFDPAEVLRAIeeqritatF-LVPTMIYA----------------LLDHPDLRT---------RDLS------ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 417 fnkiqaSLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHV------GAPLPCNHIK 490
Cdd:PRK06188 282 ------SL----ETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLRVA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 491 LVDvEELNYWAcKGE-GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVA 569
Cdd:PRK06188 352 LLD-EDGREVA-QGEvGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMI-VTGGFNVF 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 327412323 570 PEKIENIYIRSQPVAQIYV-------HGDSLKAflvgIVVPDPEVMPSWAQ 613
Cdd:PRK06188 428 PREVEDVLAEHPAVAQVAVigvpdekWGEAVTA----VVVLRPGAAVDAAE 474
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
269-606 |
1.52e-29 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 122.01 E-value: 1.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 269 DLSIVCFTSGTTGNPKGAMLTHGNVVadFSGflKVTESQWAPTCADVHISYLPLAHM---FERMVQSVVycHGGRV---- 341
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLT--FAG--YYSARRFGLGEDDVYLTVLPLFHInaqAVSVLAALS--VGATLvllp 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 342 ----GFFQGDIRllsdDMKALCPTIFPVVPRLLnrmydkiFSQANTPlkrwllefaaKRKQAEVRsgiirndsiwdelff 417
Cdd:cd05934 156 rfsaSRFWSDVR----RYGATVTNYLGAMLSYL-------LAQPPSP----------DDRAHRLR--------------- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 418 nkiqaslggcvrmiVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEel 497
Cdd:cd05934 200 --------------AAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDD-- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 498 NYWACKGE-GEICVR---GPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKI 573
Cdd:cd05934 264 GQELPAGEpGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEV 341
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 327412323 574 ENIYIRSQPVAQIYVHG-------DSLKAFlvgIVVPDPE 606
Cdd:cd05934 342 ERAILRHPAVREAAVVAvpdevgeDEVKAV---VVLRPGE 378
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
122-582 |
2.31e-29 |
|
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: 121.22 E-value: 2.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 122 SYQEVADRAEFLGSGLLQHnCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLyDTLGPGA-IRYIINTADISTVIV 200
Cdd:TIGR01733 1 TYRELDERANRLARHLRAA-GGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPL-DPAYPAErLAFILEDAGARLLLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 201 DKPqkavllleHVERKETPGLKLIILMDPFEEALkergqkcgvviksmqavEDCGQENHqAPVPPQPDDLSIVCFTSGTT 280
Cdd:TIGR01733 79 DSA--------LASRLAGLVLPVILLDPLELAAL-----------------DDAPAPPP-PDAPSGPDDLAYVIYTSGST 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 281 GNPKGAMLTHGNVVAdfsgFLKVTESQWAPTCADVHISYLPLAH------MFermvqsVVYCHGGRVgffqgdiRLLSDD 354
Cdd:TIGR01733 133 GRPKGVVVTHRSLVN----LLAWLARRYGLDPDDRVLQFASLSFdasveeIF------GALLAGATL-------VVPPED 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 355 MKAlcpTIFPVVPRLLNRMYDKIFSQANTPLKRWLLEfaakrkqaevrsgiirndsiwdelffnkiQASLGGCVRMIVTG 434
Cdd:TIGR01733 196 EER---DDAALLAALIAEHPVTVLNLTPSLLALLAAA-----------------------------LPPALASLRLVILG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 435 AAPASPTVLGFLRAALG-CQVYEGYGQTECTAGCT-FTTPGDWTSGHV----GAPLPCNHIKLVDvEELNYWACKGEGEI 508
Cdd:TIGR01733 244 GEALTPALVDRWRARGPgARLINLYGPTETTVWSTaTLVDPDDAPRESpvpiGRPLANTRLYVLD-DDLRPVPVGVVGEL 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 509 CVRGPNVFKGYLKDPDRTKEA-LDSDGWL-------HTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIyIRS 580
Cdd:TIGR01733 323 YIGGPGVARGYLNRPELTAERfVPDPFAGgdgarlyRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAA-LLR 400
|
..
gi 327412323 581 QP 582
Cdd:TIGR01733 401 HP 402
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
173-610 |
2.37e-29 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 121.78 E-value: 2.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 173 VVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlLLEHVErketpgLKLIILMDPfeealkergqkcGVVIKsmqaVE 252
Cdd:cd05922 48 VFVPLNPTLKESVLRYLVADAGGRIVLADAG-----AADRLR------DALPASPDP------------GTVLD----AD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 253 DCGQENHQAP-VPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTESQWAPTCADVHISY-LPLAHMFE 327
Cdd:cd05922 101 GIRAARASAPaHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSiaeYLGITADDRALTVLPLSYDYgLSVLNTHL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 328 RMVQSVVYCHGGRVGffqgdiRLLSDDMKALCPTIFPVVP---RLLNRMydkIFSQANTPLKRWLLEFAAKRKQAEVRSg 404
Cdd:cd05922 181 LRGATLVLTNDGVLD------DAFWEDLREHGATGLAGVPstyAMLTRL---GFDPAKLPSLRYLTQAGGRLPQETIAR- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 405 iirndsiwdelffnkiqaslggcvrmivtgaapasptvlgfLRAAL-GCQVYEGYGQTECTAGCTFTTPG--DWTSGHVG 481
Cdd:cd05922 251 -----------------------------------------LRELLpGAQVYVMYGQTEATRRMTYLPPEriLEKPGSIG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 482 APLPCNHIklvDVEELNYWACK-GE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkWLPA-GTLKIIDRKKH 558
Cdd:cd05922 290 LAIPGGEF---EILDDDGTPTPpGEpGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLA-RRDEdGFLFIVGRRDR 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 327412323 559 IFKLAqGEYVAPEKIENIyIRSQP---VAQIYVHGDSLKAFLVGIVVPDPEVMPS 610
Cdd:cd05922 366 MIKLF-GNRISPTEIEAA-ARSIGliiEAAAVGLPDPLGEKLALFVTAPDKIDPK 418
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
220-578 |
3.10e-29 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 122.78 E-value: 3.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 220 GLKLIILMDPFEEALKERGQKCGVVIKSM-QAVEDC--------GQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTH 290
Cdd:PLN02246 122 GAKLIITQSCYVDKLKGLAEDDGVTVVTIdDPPEGClhfseltqADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTH 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 291 GNVVADFSGFLKVTESQWAPTCADVHISYLPLAHMFErmVQSVVYChGGRVG--------FfqgDIRLLSDDMKALCPTI 362
Cdd:PLN02246 202 KGLVTSVAQQVDGENPNLYFHSDDVILCVLPMFHIYS--LNSVLLC-GLRVGaailimpkF---EIGALLELIQRHKVTI 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 363 FPVVPrllnrmydkifsqantPLkrwLLEFAakrKQAEVRSgiirndsiwDELffnkiqASlggcVRMIVTGAAPASPTV 442
Cdd:PLN02246 276 APFVP----------------PI---VLAIA---KSPVVEK---------YDL------SS----IRMVLSGAAPLGKEL 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 443 LGFLRAALGCQVY-EGYGQTE-------CTAgctFT-TPGDWTSGHVGAPLPCNHIKLVDVE---ELNYWACkgeGEICV 510
Cdd:PLN02246 315 EDAFRAKLPNAVLgQGYGMTEagpvlamCLA---FAkEPFPVKSGSCGTVVRNAELKIVDPEtgaSLPRNQP---GEICI 388
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 327412323 511 RGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYI 578
Cdd:PLN02246 389 RGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAELEALLI 455
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
121-610 |
4.34e-29 |
|
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: 120.71 E-value: 4.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACY----TYsmvvVPLYDTLGPGAIRYIINTADIS 196
Cdd:cd05930 13 LTYAELDARANRLARYLRERGVGP--GDLVAVLLERSLEMVVAILAVLkagaAY----VPLDPSYPAERLAYILEDSGAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 197 TVIVDkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhqapvppqPDDLSIVCFT 276
Cdd:cd05930 87 LVLTD-----------------------------------------------------------------PDDLAYVIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 277 SGTTGNPKGAMLTHGNVV---ADFSGFLKVTES----QWAPTCADVHIS--YLPLAHmfermvqsvvychGGRVGFFQGD 347
Cdd:cd05930 102 SGSTGKPKGVMVEHRGLVnllLWMQEAYPLTPGdrvlQFTSFSFDVSVWeiFGALLA-------------GATLVVLPEE 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 348 IRLLSDDMKALC----PTIFPVVPRLLNRMYDKIFSQANTPLkrwllefaakrkqaevrsgiirndsiwdelffnkiqas 423
Cdd:cd05930 169 VRKDPEALADLLaeegITVLHLTPSLLRLLLQELELAALPSL-------------------------------------- 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 424 lggcvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFT--TPGDWTSGHV--GAPLPCNHIKLVDvEELN 498
Cdd:cd05930 211 -----RLVLVGGEALPPDLVrRWRELLPGARLVNLYGPTEATVDATYYrvPPDDEEDGRVpiGRPIPNTRVYVLD-ENLR 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 499 YWACKGEGEICVRGPNVFKGYLKDPDRTKEA-----LDSDGWLH-TGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEK 572
Cdd:cd05930 285 PVPPGVPGELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIELGE 363
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 327412323 573 IENIYIRSQPVAQIYV---HGDSLKAFLVGIVVPDPEVMPS 610
Cdd:cd05930 364 IEAALLAHPGVREAAVvarEDGDGEKRLVAYVVPDEGGELD 404
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
93-544 |
6.88e-29 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 121.76 E-value: 6.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 93 YQVFRRGLSISGNGPCLGFRKPKQPYQWLSYQEVADRAEFLGSGLLQHnckactdqfiGV--------FAQNRPEWIIVE 164
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRAL----------GVkkgdrvaiYLPNIPEAVIAM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 165 LACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVD----KPQKAVLLLEHVE--RKETPGLKLIILMD---------- 228
Cdd:COG0365 82 LACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITAdgglRGGKVIDLKEKVDeaLEELPSLEHVIVVGrtgadvpmeg 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 229 --PFEEALKERGQKCgvviksmqavedcgqenhqAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLK---- 302
Cdd:COG0365 162 dlDWDELLAAASAEF-------------------EPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKyvld 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 303 VTESQ--WAPtcADV----HISYL---PLAH-----MFERmvqSVVYCHGGRvgFFQgdirlLSDDMKalcPTIFPVVPR 368
Cdd:COG0365 223 LKPGDvfWCT--ADIgwatGHSYIvygPLLNgatvvLYEG---RPDFPDPGR--LWE-----LIEKYG---VTVFFTAPT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 369 LLnRMydkifsqantpLKRWLLEFAAKRKQAevrsgiirndsiwdelffnkiqaSLggcvRMIVTGAAPASPTVLGFLRA 448
Cdd:COG0365 288 AI-RA-----------LMKAGDEPLKKYDLS-----------------------SL----RLLGSAGEPLNPEVWEWWYE 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 449 ALGCQVYEGYGQTECtaGCTFTTPGDWTS---GHVGAPLPCNHIKLVDvEELNywACKG--EGEICVRG--PNVFKGYLK 521
Cdd:COG0365 329 AVGVPIVDGWGQTET--GGIFISNLPGLPvkpGSMGKPVPGYDVAVVD-EDGN--PVPPgeEGELVIKGpwPGMFRGYWN 403
|
490 500
....*....|....*....|....*
gi 327412323 522 DPDRTKEAL--DSDGWLHTGDIGKW 544
Cdd:COG0365 404 DPERYRETYfgRFPGWYRTGDGARR 428
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
261-613 |
7.79e-29 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 121.49 E-value: 7.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 261 APVPPQpDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWA-PTCADVHISYLPLAHMFermvqsvvychgG 339
Cdd:PLN02574 192 KPVIKQ-DDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEyPGSDNVYLAALPMFHIY------------G 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 340 RVGFFQGDIRL-----------LSDDMKAL---CPTIFPVVPRLLNRMYDKIFSQANTPLKrwllefaakrkqaevrsgi 405
Cdd:PLN02574 259 LSLFVVGLLSLgstivvmrrfdASDMVKVIdrfKVTHFPVVPPILMALTKKAKGVCGEVLK------------------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 406 irndsiwdelffnkiqaslggCVRMIVTGAAPAS-PTVLGFLRAALGCQVYEGYGQTECTAGCT--FTTPGDWTSGHVGA 482
Cdd:PLN02574 320 ---------------------SLKQVSCGAAPLSgKFIQDFVQTLPHVDFIQGYGMTESTAVGTrgFNTEKLSKYSSVGL 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 483 PLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKL 562
Cdd:PLN02574 379 LAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY 458
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 327412323 563 aQGEYVAPEKIENIYIrSQP----VAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQ 613
Cdd:PLN02574 459 -KGFQIAPADLEAVLI-SHPeiidAAVTAVPDKECGEIPVAFVVRRQGSTLSQEA 511
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
119-615 |
8.71e-29 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 120.47 E-value: 8.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 119 QWLSYQEVADRAEFLGSGLLQHNckACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLyDTLGPGA-IRYIINTADIST 197
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARG--VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPL-DPDYPADrLRYILEDAEPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 198 VIVDkpqkavlllehverketpglkliilmdpfeEALKERGQKCGVVIksMQAVEDCGQENHQAPVPPQPDDLSIVCFTS 277
Cdd:cd12116 88 VLTD------------------------------DALPDRLPAGLPVL--LLALAAAAAAPAAPRTPVSPDDLAYVIYTS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 278 GTTGNPKGAMLTHGNVVADFSGF------------LKVTesqwaPTCADvhIS----YLPLahmfermvqsvvyCHGGRV 341
Cdd:cd12116 136 GSTGRPKGVVVSHRNLVNFLHSMrerlglgpgdrlLAVT-----TYAFD--ISllelLLPL-------------LAGARV 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 342 GFFQGDI----RLLSDDMKALCPTIFpvvprllnrmydkifsQAnTP-LKRWLLefaakrkqaevrsgiirnDSIWDELf 416
Cdd:cd12116 196 VIAPRETqrdpEALARLIEAHSITVM----------------QA-TPaTWRMLL------------------DAGWQGR- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 417 fnkiqASLggcvRMIVTGAApaSPTVLGFLRAALGCQVYEGYGQTECT--AGCTFTTPGDwTSGHVGAPLPCNHIKLVDv 494
Cdd:cd12116 240 -----AGL----TALCGGEA--LPPDLAARLLSRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLD- 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 495 EELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH-------TGDIGKWLPAGTLKIIDRKKHIFKLaQGEY 567
Cdd:cd12116 307 AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQVKI-RGHR 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 327412323 568 VAPEKIENIYIRSQPVAQ--IYVHGDSLKAFLVGIVVPDPEVMPSWAQKR 615
Cdd:cd12116 386 IELGEIEAALAAHPGVAQaaVVVREDGGDRRLVAYVVLKAGAAPDAAALR 435
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
121-606 |
2.84e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 119.68 E-value: 2.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLgSGLLQHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PRK08314 36 ISYRELLEEAERL-AGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 201 -----DKPQKAV--LLLEHV-------ERKETPGLKLIILMDpfEEALKERGQKCGVViksmqAVEDCGQENHQA-PVPP 265
Cdd:PRK08314 115 gselaPKVAPAVgnLRLRHVivaqysdYLPAEPEIAVPAWLR--AEPPLQALAPGGVV-----AWKEALAAGLAPpPHTA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 266 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkvteSQWAP-TCADVHISYLPLAHM--FERMVQSVVYChGGRVg 342
Cdd:PRK08314 188 GPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGS-----VLWSNsTPESVVLAVLPLFHVtgMVHSMNAPIYA-GATV- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 343 ffqgdirllsddmkalcpTIFP-----VVPRLLNRMydKIFSQANTPlkRWLLEFAAKRKQAEvrsgiiRNDSiwdelff 417
Cdd:PRK08314 261 ------------------VLMPrwdreAAARLIERY--RVTHWTNIP--TMVVDFLASPGLAE------RDLS------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 418 nkiqaSLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWT-SGHVGAPLPCNHIKLVDVEE 496
Cdd:PRK08314 306 -----SL----RYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTE-TMAQTHSNPPDRPkLQCLGIPTFGVDARVIDPET 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 497 LNYWACKGEGEICVRGPNVFKGYLKDPDRTKEA---LDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKI 573
Cdd:PRK08314 376 LEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMIN-ASGFKVWPAEV 454
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 327412323 574 ENIYIRSQPVAQIYV-------HGDSLKAFlvgiVVPDPE 606
Cdd:PRK08314 455 ENLLYKHPAIQEACViatpdprRGETVKAV----VVLRPE 490
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
121-615 |
3.11e-28 |
|
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: 117.97 E-value: 3.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLGSGLlqHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:cd05935 2 LTYLELLEVVKKLASFL--SNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 201 DKPQkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhqapvppqpDDLSIVCFTSGTT 280
Cdd:cd05935 80 GSEL---------------------------------------------------------------DDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 281 GNPKGAMLTHGNVVADFSGflkvtESQWAP-TCADVHISYLPLAHM--FERMVQSVVYCHGGRVGFFQGDIRLLSDDMKA 357
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQ-----SAVWTGlTPSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMARWDRETALELIEK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 358 LCPTIFPVVPRLLNRMydkifsqANTPlkrwllefaakrkqaevrsgiirndsiwdelffnKIQASLGGCVRMIVTGAAP 437
Cdd:cd05935 172 YKVTFWTNIPTMLVDL-------LATP----------------------------------EFKTRDLSSLKVLTGGGAP 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 438 ASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFK 517
Cdd:cd05935 211 MPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFK 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 518 GYLKDPDRTKEALDSDG---WLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYV------ 588
Cdd:cd05935 291 GYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVisvpde 369
|
490 500 510
....*....|....*....|....*....|....
gi 327412323 589 -HGDSLKAFLVgiVVP------DPEVMPSWAQKR 615
Cdd:cd05935 370 rVGEEVKAFIV--LRPeyrgkvTEEDIIEWAREQ 401
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
119-615 |
5.83e-28 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 120.73 E-value: 5.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 119 QWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELA------CYtysmvvVPLyDTLGPGA-IRYIIN 191
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALGVGP--GDLVGVCLERSLEMVVALLAvlkagaAY------VPL-DPAYPAErLAYMLE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 192 TADISTVIVDkpqkavlllehverketpglkliilmdpfeEALKERGQKCGVVIKSMQAVEDCGQENHQAPVPPQPDDLS 271
Cdd:COG1020 571 DAGARLVLTQ------------------------------SALAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLA 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 272 IVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTES----QWAPTCADVHIS--YLPLahmfermvqsvvyCHGGRVG 342
Cdd:COG1020 621 YVIYTSGSTGRPKGVMVEHRALVnllAWMQRRYGLGPGdrvlQFASLSFDASVWeiFGAL-------------LSGATLV 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 343 FFQGDIRLLSDDMKALC----PTIFPVVPRLLNRMYDkifsqantplkrwllefAAKRKQAEVRsgiirndsiwdelffn 418
Cdd:COG1020 688 LAPPEARRDPAALAELLarhrVTVLNLTPSLLRALLD-----------------AAPEALPSLR---------------- 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 419 kiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF--TTPGDWTSGHV--GAPLPCNHIKLVDv 494
Cdd:COG1020 735 ----------LVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYyeVTPPDADGGSVpiGRPIANTRVYVLD- 803
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 495 EELN---YWACkgeGEICVRGPNVFKGYLKDPDRTKEA-----LDSDG--WLHTGDIGKWLPAGTLKIIDRKKHifklaQ 564
Cdd:COG1020 804 AHLQpvpVGVP---GELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNLEFLGRADD-----Q 875
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 327412323 565 ----------GEyvapekIENIyIRSQP-VAQIYV--HGDSL-KAFLVGIVVPDPEVMPSWAQKR 615
Cdd:COG1020 876 vkirgfrielGE------IEAA-LLQHPgVREAVVvaREDAPgDKRLVAYVVPEAGAAAAAALLR 933
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
255-598 |
6.41e-28 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 118.77 E-value: 6.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 255 GQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTeSQWAP-------TCADVHISYLPLAHMFE 327
Cdd:PRK12492 194 GRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACL-SQLGPdgqplmkEGQEVMIAPLPLYHIYA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 328 RMVQSVVYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLlnrmydkifsqaNTplkrwllEFAAKRKQAEVRSgiir 407
Cdd:PRK12492 273 FTANCMCMMVSGNHNVLITNPRDIPGFIKELGKWRFSALLGL------------NT-------LFVALMDHPGFKD---- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 408 ndsiwdeLFFNKIQASLGGcvrmivtGAAPASPTVLGFlRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPC 486
Cdd:PRK12492 330 -------LDFSALKLTNSG-------GTALVKATAERW-EQLTGCTIVEGYGLTETSPVASTNPYGELARlGTVGIPVPG 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 487 NHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGE 566
Cdd:PRK12492 395 TALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLI-IVSGF 472
|
330 340 350
....*....|....*....|....*....|....*....
gi 327412323 567 YVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLV 598
Cdd:PRK12492 473 NVYPNEIEDVVMAHPKVANCAAigvpderSGEAVKLFVV 511
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
158-605 |
1.30e-27 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 117.28 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 158 PEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDkPQKAVLLLEHVERKETPGLkliilmdpfeEALKER 237
Cdd:PRK07514 64 PEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCD-PANFAWLSKIAAAAGAPHV----------ETLDAD 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 238 GQkcGVViksMQAVEDCGQEnhQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgfLKVTESQWAPTCADVHI 317
Cdd:PRK07514 133 GT--GSL---LEAAAAAPDD--FETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSN----ALTLVDYWRFTPDDVLI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 318 SYLPLAHMFERMVQS-VVYCHGGRVGFFQgdiRLLSDDMKALCP--TIFPVVPRLLNRMYdkifsqANTPLKRwllEFAA 394
Cdd:PRK07514 202 HALPIFHTHGLFVATnVALLAGASMIFLP---KFDPDAVLALMPraTVMMGVPTFYTRLL------QEPRLTR---EAAA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 395 KrkqaevrsgiirndsiwdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTfTTP-- 472
Cdd:PRK07514 270 H--------------------------------MRLFISGSAPLLAETHREFQERTGHAILERYGMTE-TNMNT-SNPyd 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 473 GDWTSGHVGAPLPCNHIKLVDVE---ELNywacKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAG 548
Cdd:PRK07514 316 GERRAGTVGFPLPGVSLRVTDPEtgaELP----PGEiGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERG 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 327412323 549 TLKIIDRKKHIfkLAQGEY-VAPEKIENiYIRSQP-VAQIYVHGDSLKAF---LVGIVVPDP 605
Cdd:PRK07514 392 YVHIVGRGKDL--IISGGYnVYPKEVEG-EIDELPgVVESAVIGVPHPDFgegVTAVVVPKP 450
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
89-557 |
1.72e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 118.13 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 89 ARTMYQVFRRGLSISGNGPCLgfrkpkqpyqwlSYQEVADR---------AEFLG-----SGLLqHNCKACTDQFIGVFA 154
Cdd:PRK07529 24 PASTYELLSRAAARHPDAPAL------------SFLLDADPldrpetwtyAELLAdvtrtANLL-HSLGVGPGDVVAFLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 155 QNRPEWIIVELACYTYSmVVVPLYDTLGPGAIRYIINTADISTVIVDKP-------QKAVLLLEHVerketPGLKLIILM 227
Cdd:PRK07529 91 PNLPETHFALWGGEAAG-IANPINPLLEPEQIAELLRAAGAKVLVTLGPfpgtdiwQKVAEVLAAL-----PELRTVVEV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 228 D-------PFEEALKERGQKCGVVIKSMQA-VEDCGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsG 299
Cdd:PRK07529 165 DlarylpgPKRLAVPLIRRKAHARILDFDAeLARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVAN--A 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 300 FLKVTESQWAPTcaDVHISYLPLAHMFERMVQSVVYCHGGR---VGFFQG--DIRLLSDDMK---ALCPTIFPVVPRLLN 371
Cdd:PRK07529 243 WLGALLLGLGPG--DTVFCGLPLFHVNALLVTGLAPLARGAhvvLATPQGyrGPGVIANFWKiveRYRINFLSGVPTVYA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 372 RMydkifsqANTPlkrwllefaakrkqaevrsgiirndsiwdelffnkIQASLGGCVRMIVTGAAPASPTVLGFLRAALG 451
Cdd:PRK07529 321 AL-------LQVP-----------------------------------VDGHDISSLRYALCGAAPLPVEVFRRFEAATG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 452 CQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLVDVEEL-NYW--ACKGE-GEICVRGPNVFKGYLkDPDRT 526
Cdd:PRK07529 359 VRIVEGYGLTEATCVSSVNPPdGERRIGSVGLRLPYQRVRVVILDDAgRYLrdCAVDEvGVLCIAGPNVFSGYL-EAAHN 437
|
490 500 510
....*....|....*....|....*....|.
gi 327412323 527 KEALDSDGWLHTGDIGKWLPAGTLKIIDRKK 557
Cdd:PRK07529 438 KGLWLEDGWLNTGDLGRIDADGYFWLTGRAK 468
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
265-613 |
5.72e-27 |
|
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: 113.98 E-value: 5.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 265 PQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF---LKVTES-QWAPTCADVHISYLPLahmferMVQSVVYchGGR 340
Cdd:cd05912 74 VKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSalnLGLTEDdNWLCALPLFHISGLSI------LMRSVIY--GMT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 341 VGFFQG-DIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTPLKRWLLefaakrkqaevrsgiirndsiwdelffnk 419
Cdd:cd05912 146 VYLVDKfDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRCILL----------------------------- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 420 iqaslggcvrmivtGAAPASPTVLGFLRAaLGCQVYEGYGQTE-CTAGCTFTtPGDWTS--GHVGAPLPCNHIKLVDVEE 496
Cdd:cd05912 197 --------------GGGPAPKPLLEQCKE-KGIPVYQSYGMTEtCSQIVTLS-PEDALNkiGSAGKPLFPVELKIEDDGQ 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 497 LNYwackGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENI 576
Cdd:cd05912 261 PPY----EVGEILLKGPNVTKGYLNRPDATEESFE-NGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEV 334
|
330 340 350
....*....|....*....|....*....|....*..
gi 327412323 577 YIRSQPVAQIYVhgdslkaflVGIvvPDPEvmpsWAQ 613
Cdd:cd05912 335 LLSHPAIKEAGV---------VGI--PDDK----WGQ 356
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
259-610 |
9.02e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 114.32 E-value: 9.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 259 HQAPVPPqPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkvtESQWAPTCADVHISYLPLAHMfermvqsvvycHG 338
Cdd:PRK07787 120 HRYPEPD-PDAPALIVYTSGTTGPPKGVVLSRRAIAADLDAL----AEAWQWTADDVLVHGLPLFHV-----------HG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 339 ------------GRV---GFF--QGDIRLLSDDmkalcPTIFPVVPRllnrMYDKIfsqantplkrwllefAAKRKQAEV 401
Cdd:PRK07787 184 lvlgvlgplrigNRFvhtGRPtpEAYAQALSEG-----GTLYFGVPT----VWSRI---------------AADPEAARA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 402 RSGiirndsiwdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVG 481
Cdd:PRK07787 240 LRG-----------------------ARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVG 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 482 APLPCNHIKLVDvEELNYWACKGE--GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDR---- 555
Cdd:PRK07787 297 LPLAGVETRLVD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestd 375
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 556 --KKHIFKLAQGEyvapekIENIYIRSQPVAQIYVHG---DSLKAFLVGIVVPDPEVMPS 610
Cdd:PRK07787 376 liKSGGYRIGAGE------IETALLGHPGVREAAVVGvpdDDLGQRIVAYVVGADDVAAD 429
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
269-588 |
2.15e-26 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 113.92 E-value: 2.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 269 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTCADVHIsyLPLAHMF--ERMVQSVVYCHGGRVGFFQG 346
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMIGQVVTLGL--IPFFHIYgiTGICCATLRNKGKVVVMSRF 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 347 DIRLLSDDMKALCPTIFPVVPrllnrmydkifsqantPLKRWLLEfaakrkqaevrsgiirnDSIWDELFFNKIQaslgg 426
Cdd:PLN02330 263 ELRTFLNALITQEVSFAPIVP----------------PIILNLVK-----------------NPIVEEFDLSKLK----- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 427 cVRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTagCTFTTPGDWTSGH-------VGAPLPCNHIKLVDVEELN 498
Cdd:PLN02330 305 -LQAIMTAAAPLAPELLtAFEAKFPGVQVQEAYGLTEHS--CITLTHGDPEKGHgiakknsVGFILPNLEVKFIDPDTGR 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 499 YWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYI 578
Cdd:PLN02330 382 SLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAILL 460
|
330
....*....|
gi 327412323 579 RSQPVAQIYV 588
Cdd:PLN02330 461 THPSVEDAAV 470
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
119-606 |
3.12e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 113.03 E-value: 3.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 119 QWLSYQEVADRAEFLgSGLLQHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTV 198
Cdd:PRK06839 26 EEMTYKQLHEYVSKV-AAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 199 IVDKP-QKAVLLLEHVERKETPglkliilmdpfeealkergqkcgVVIKSMQAVEDCGQENHqapVPPQPDDLSIVCFTS 277
Cdd:PRK06839 105 FVEKTfQNMALSMQKVSYVQRV-----------------------ISITSLKEIEDRKIDNF---VEKNESASFIICYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 278 GTTGNPKGAMLTHGNVvadfsgFLKVTESQWAP--TCADVHISYLPLAHMfermvqsvvychgGRVGFFQgdirllsddm 355
Cdd:PRK06839 159 GTTGKPKGAVLTQENM------FWNALNNTFAIdlTMHDRSIVLLPLFHI-------------GGIGLFA---------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 356 kalCPTIFP----VVPRLLNRmyDKIFSQANTplKRWLLEFAAKRKQAEVRSGIIRNDSIWDElffnkiqaslggcVRMI 431
Cdd:PRK06839 210 ---FPTLFAggviIVPRKFEP--TKALSMIEK--HKVTVVMGVPTIHQALINCSKFETTNLQS-------------VRWF 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 432 VTGAAPAS-PTVLGFLRAalGCQVYEGYGQTEcTAGCTFTTPGD---WTSGHVGAPLPCNHIKLVDvEELNYWACKGEGE 507
Cdd:PRK06839 270 YNGGAPCPeELMREFIDR--GFLFGQGFGMTE-TSPTVFMLSEEdarRKVGSIGKPVLFCDYELID-ENKNKVEVGEVGE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 508 ICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIyirsqpvaqIY 587
Cdd:PRK06839 346 LLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQV---------IN 414
|
490
....*....|....*....
gi 327412323 588 VHGDSLKAFLVGivVPDPE 606
Cdd:PRK06839 415 KLSDVYEVAVVG--RQHVK 431
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
121-590 |
6.80e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 111.98 E-value: 6.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLAALGVK--KGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLIT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 201 DkpqkavlllehverketpglkliilmDPFEEALKERGQkcgVVIKSMQAvedcGQENHQAPVPPQP-DDLSIVCFTSGT 279
Cdd:PRK03640 106 D--------------------------DDFEAKLIPGIS---VKFAELMN----GPKEEAEIQEEFDlDEVATIMYTSGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 280 TGNPKGAMLTHGNVVADFSGF---LKVTESQ-WapTCAdvhisyLPLAHM--FERMVQSVVYchGGRV----GFFQGDI- 348
Cdd:PRK03640 153 TGKPKGVIQTYGNHWWSAVGSalnLGLTEDDcW--LAA------VPIFHIsgLSILMRSVIY--GMRVvlveKFDAEKIn 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 349 RLLSDDMKalcpTIFPVVPRLLNRMYDKIfSQANTPlkrwllefaakrkqaevrsgiirnDSiwdelffnkiqaslggcV 428
Cdd:PRK03640 223 KLLQTGGV----TIISVVSTMLQRLLERL-GEGTYP------------------------SS-----------------F 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 429 RMIVTGAAPASPTVLGFLRAAlGCQVYEGYGQTEcTAGCTFTTPGDWTS---GHVGAPL-PCNhIKLVDveELNYWACKG 504
Cdd:PRK03640 257 RCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLfPCE-LKIEK--DGVVVPPFE 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 505 EGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVA 584
Cdd:PRK03640 332 EGEIVVKGPNVTKGYLNREDATRETFQ-DGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPGVA 409
|
....*.
gi 327412323 585 QIYVHG 590
Cdd:PRK03640 410 EAGVVG 415
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
156-598 |
2.34e-25 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 110.54 E-value: 2.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 156 NRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDkpQKAVLLLEHVERKETPGLKLIILMDPFEEALK 235
Cdd:PRK08008 71 NCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTS--AQFYPMYRQIQQEDATPLRHICLTRVALPADD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 236 ergqkcGVV----IKSMQAVEDCGQenhqapVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLkvTESQWAPT 311
Cdd:PRK08008 149 ------GVSsftqLKAQQPATLCYA------PPLSTDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYY--SAWQCALR 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 312 CADVHISYLPLAHMFermvqsvvychggrvgfFQgdirllsddmkalCPTIFPVvprllnrmydkiFSQANTPLkrwLLE 391
Cdd:PRK08008 213 DDDVYLTVMPAFHID-----------------CQ-------------CTAAMAA------------FSAGATFV---LLE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 392 -FAAKRKQAEVRsgiirndsiwdelffnKIQASLGGCVRMIVTG--AAPASPT--------VLGFLRAA----------L 450
Cdd:PRK08008 248 kYSARAFWGQVC----------------KYRATITECIPMMIRTlmVQPPSANdrqhclreVMFYLNLSdqekdafeerF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 451 GCQVYEGYGQTECTAGCTFTTPGD---WTSghVGAPLPCNHIKLVDveELNYWACKGE-GEICVRG---PNVFKGYLKDP 523
Cdd:PRK08008 312 GVRLLTSYGMTETIVGIIGDRPGDkrrWPS--IGRPGFCYEAEIRD--DHNRPLPAGEiGEICIKGvpgKTIFKEYYLDP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 524 DRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIyIRSQP-VAQIYVHG--DSL-----KA 595
Cdd:PRK08008 388 KATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVELENI-IATHPkIQDIVVVGikDSIrdeaiKA 465
|
...
gi 327412323 596 FLV 598
Cdd:PRK08008 466 FVV 468
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
156-598 |
3.10e-25 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 108.96 E-value: 3.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 156 NRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKpqkavlllehverketpglkliilmdpfeealk 235
Cdd:cd05972 34 RVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA--------------------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 236 ergqkcgvviksmqavedcgqenhqapvppqpDDLSIVCFTSGTTGNPKGAMLTHGnvvadfsgflkvtesqwaptcadv 315
Cdd:cd05972 81 --------------------------------EDPALIYFTSGTTGLPKGVLHTHS------------------------ 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 316 hisyLPLAHMfermvQSVVYCHGGRvgffQGDIRLLSDD----MKALCPTIFPV---VPRLLN--------RMYDKI--- 377
Cdd:cd05972 105 ----YPLGHI-----PTAAYWLGLR----PDDIHWNIADpgwaKGAWSSFFGPWllgATVFVYegprfdaeRILELLery 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 378 ----FSQANTPLKRWLLEFAAKRKQAEVRSgiirndsiwdelffnkiqaslggcvrmIVTGAAPASPTVLGFLRAALGCQ 453
Cdd:cd05972 172 gvtsFCGPPTAYRMLIKQDLSSYKFSHLRL---------------------------VVSAGEPLNPEVIEWWRAATGLP 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 454 VYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNV--FKGYLKDPDRTKEALd 531
Cdd:cd05972 225 IRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIID-DDGRELPPGEEGDIAIKLPPPglFLGYVGDPEKTEASI- 302
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 327412323 532 SDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLV 598
Cdd:cd05972 303 RGDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVESALLEHPAVAEAAVvgspdpvRGEVVKAFVV 375
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
266-606 |
4.79e-25 |
|
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: 109.17 E-value: 4.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 266 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVadfsgflkvtesqwapTCADVHISYLPL----------AHMFERMVQSVVY 335
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALS----------------TSALAHGRALGLtsesrvlqfaSYTFDVSILEIFT 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 336 --CHGG---------RVGFFQGDIRllsdDMKALCPTIFPVVPRLLNRmydkifsqANTPlkrwllefaakrkqaevrsg 404
Cdd:cd05918 168 tlAAGGclcipseedRLNDLAGFIN----RLRVTWAFLTPSVARLLDP--------EDVP-------------------- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 405 iirndsiwdelffnkiqaslggCVRMIVTGAAPASPTVLGflRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAP 483
Cdd:cd05918 216 ----------------------SLRTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRP 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 484 LPC--------NHIKLVDVeelnywackGE-GEICVRGPNVFKGYLKDPDRTKEA-LDSDGWLH------------TGDI 541
Cdd:cd05918 272 LGAtcwvvdpdNHDRLVPI---------GAvGELLIEGPILARGYLNDPEKTAAAfIEDPAWLKqegsgrgrrlyrTGDL 342
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 327412323 542 GKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENiYIRSQP------VAQIYVH-GDSLKAFLVGIVVPDPE 606
Cdd:cd05918 343 VRYNPDGSLEYVGRKDTQVKI-RGQRVELGEIEH-HLRQSLpgakevVVEVVKPkDGSSSPQLVAFVVLDGS 412
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
264-604 |
9.13e-25 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 107.78 E-value: 9.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 264 PPQPDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSGF-LKVTESQ----------WAptCADVHISYLplahmfermv 330
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLnyVSQPPArLDVGPGSrvaqvlsiafDA--CIGEIFSTL---------- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 331 qsvvyCHGGRVgFFQGDIRLLSDDMKALcpTIFPVVPRLLNRMYDKIFSQantplkrwllefaakrkqaevrsgiirnds 410
Cdd:cd17653 169 -----CNGGTL-VLADPSDPFAHVARTV--DALMSTPSILSTLSPQDFPN------------------------------ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 411 iwdelffnkiqaslggcVRMIVTGAAPASPTVLGflRAALGCQVYEGYGQTECTAGCTFT--TPGDWTsgHVGAPLPCNH 488
Cdd:cd17653 211 -----------------LKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTelLPGQPV--TIGKPIPNST 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 489 IKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH------TGDIGKWLPAGTLKIIDRKKHIFKL 562
Cdd:cd17653 270 CYILD-ADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPgsrmyrTGDYGRWTEDGGLEFLGREDNQVKV 348
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 327412323 563 aQGEYVAPEKIENIYIRSQPVAQ---IYVHGDSLKAFlvgiVVPD 604
Cdd:cd17653 349 -RGFRINLEEIEEVVLQSQPEVTqaaAIVVNGRLVAF----VTPE 388
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
256-598 |
1.31e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 108.58 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 256 QENHQAPVPPQPD-DLSIVCFTSGTTGNPKGAMLTHGNVVADfsgflKVTESQWAPTCAD---VHISYLPLAHMF-ERMV 330
Cdd:PRK06710 193 EVNTGVEVPCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSN-----TLMGVQWLYNCKEgeeVVLGVLPFFHVYgMTAV 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 331 QSVVYCHGGRVGFF-QGDIRLLSDDMKALCPTIFPVVPRLLnrmydkiFSQANTPLkrwllefaakRKQAEVRSgiirnd 409
Cdd:PRK06710 268 MNLSIMQGYKMVLIpKFDMKMVFEAIKKHKVTLFPGAPTIY-------IALLNSPL----------LKEYDISS------ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 410 siwdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgctfTTPGDW-----TSGHVGAPL 484
Cdd:PRK06710 325 ------------------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSP----VTHSNFlwekrVPGSIGVPW 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 485 PCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQ 564
Cdd:PRK06710 383 PDTEAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VAS 460
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 327412323 565 GEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLV 598
Cdd:PRK06710 461 GFNVYPREVEEVLYEHEKVQEVVTigvpdpyRGETVKAFVV 501
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
269-606 |
2.38e-24 |
|
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: 104.66 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 269 DLSIVCFTSGTTGNPKGAMLTHGNVVA---DFSGFLKVTEsqwaptcADVHISYLPLAHMFERMVQSVVYCHGGR---VG 342
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAanlQLIHAMGLTE-------ADVYLNMLPLFHIAGLNLALATFHAGGAnvvME 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 343 FFQGDIRL-LSDDMKAlcpTIFPVVPRLLNRMYDkifsqantplkrwllefAAKRKQAEVRSgiIRNdsiwdelffnkiq 421
Cdd:cd17637 74 KFDPAEALeLIEEEKV---TLMGSFPPILSNLLD-----------------AAEKSGVDLSS--LRH------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 422 aslggcvrmiVTGAApaSPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDveELNYWA 501
Cdd:cd17637 119 ----------VLGLD--APETIQRFEETTGATFWSLYGQTE-TSGLVTLSPYRERPGSAGRPGPLVRVRIVD--DNDRPV 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 502 CKGE-GEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRK--KHIFKlAQGEYVAPEKIENIyI 578
Cdd:cd17637 184 PAGEtGEIVVRGPLVFQGYWNLPELTAYTFR-NGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKV-I 260
|
330 340
....*....|....*....|....*....
gi 327412323 579 RSQP-VAQIYVHGdslkaflvgivVPDPE 606
Cdd:cd17637 261 LEHPaIAEVCVIG-----------VPDPK 278
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
121-608 |
2.60e-24 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 107.59 E-value: 2.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIVELACYTYSMVVV---PLYDTlgpGAIRYIINTADIST 197
Cdd:PRK08315 44 WTYREFNEEVDALAKGLLALGIEK-GDR-VGIWAPNVPEWVLTQFATAKIGAILVtinPAYRL---SELEYALNQSGCKA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 198 -VIVDK--------------PQKAVLLLEHVERKETPGLKLIILMDpfeeALKERGqkcgvvIKSMQAVEDCGQENHQAP 262
Cdd:PRK08315 119 lIAADGfkdsdyvamlyelaPELATCEPGQLQSARLPELRRVIFLG----DEKHPG------MLNFDELLALGRAVDDAE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 263 VPP-----QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsGFLkVTESQwAPTCAD-----VhisylPLAHMFErMVQS 332
Cdd:PRK08315 189 LAArqatlDPDDPINIQYTSGTTGFPKGATLTHRNILNN--GYF-IGEAM-KLTEEDrlcipV-----PLYHCFG-MVLG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 333 VVYC--HGGRV-----GFfqgdirllsDDMKAL-------C------PTIFPVV---PRLlnRMYDkiFSQantplkrwl 389
Cdd:PRK08315 259 NLACvtHGATMvypgeGF---------DPLATLaaveeerCtalygvPTMFIAEldhPDF--ARFD--LSS--------- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 390 lefaakrkqaeVRSGIirndsiwdelffnkiqaslggcvrMivtgAAPASPT-----VLGFLRAAlgcQVYEGYGQTECT 464
Cdd:PRK08315 317 -----------LRTGI------------------------M----AGSPCPIevmkrVIDKMHMS---EVTIAYGMTETS 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 465 AGCTFTTPGD------WTsghVGAPLPCNHIKLVDVEelnywacKGE-------GEICVRGPNVFKGYLKDPDRTKEALD 531
Cdd:PRK08315 355 PVSTQTRTDDplekrvTT---VGRALPHLEVKIVDPE-------TGEtvprgeqGELCTRGYSVMKGYWNDPEKTAEAID 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 532 SDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDP----EV 607
Cdd:PRK08315 425 ADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEF---------LYTHPKIQDVQVVG--VPDEkygeEV 492
|
.
gi 327412323 608 M 608
Cdd:PRK08315 493 C 493
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
112-569 |
5.21e-24 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 106.89 E-value: 5.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 112 RKPKQPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPL---YDTLG--PGAI 186
Cdd:PRK08180 61 RGADGGWRRLTYAEALERVRAIAQALLDRGLSA--ERPLMILSGNSIEHALLALAAMYAGVPYAPVspaYSLVSqdFGKL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 187 RYIINTADISTVIVDKPQK-----AVLLLEHVE----RKETPGLKLIilmdPFEEALKERGQkcGVVIKSMQAVedcgqe 257
Cdd:PRK08180 139 RHVLELLTPGLVFADDGAAfaralAAVVPADVEvvavRGAVPGRAAT----PFAALLATPPT--AAVDAAHAAV------ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 258 nhqapvppQPDDLSIVCFTSGTTGNPKGAMLTHGNVVA------DFSGFLKVTESqwaptcadVHISYLPLAHMF--ERM 329
Cdd:PRK08180 207 --------GPDTIAKFLFTSGSTGLPKAVINTHRMLCAnqqmlaQTFPFLAEEPP--------VLVDWLPWNHTFggNHN 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 330 VQSVVYcHGGR---------VGFFQGDIRLLsddmKALCPTIFPVVPRLlnrmydkifsqantplkrWLLEFAAKRKQAE 400
Cdd:PRK08180 271 LGIVLY-NGGTlyiddgkptPGGFDETLRNL----REISPTVYFNVPKG------------------WEMLVPALERDAA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 401 VRsgiirndsiwdELFFNKiqaslggcVRMIVTGAAPASPTVLGFL----RAALGCQVY--EGYGQTECTAGCTFTTPGD 474
Cdd:PRK08180 328 LR-----------RRFFSR--------LKLLFYAGAALSQDVWDRLdrvaEATCGERIRmmTGLGMTETAPSATFTTGPL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 475 WTSGHVGAPLPCNHIKLVDVEelnywackGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWL----PAGTL 550
Cdd:PRK08180 389 SRAGNIGLPAPGCEVKLVPVG--------GKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVdpadPERGL 460
|
490
....*....|....*....
gi 327412323 551 KIIDRKKHIFKLAQGEYVA 569
Cdd:PRK08180 461 MFDGRIAEDFKLSSGTWVS 479
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
120-542 |
7.94e-24 |
|
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: 106.17 E-value: 7.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 120 WLSYQEVADRAEFLGSGLLQHNckACTDQFIGVFAQNrPEWIIVELACYTYSMVVVPLYDTLGPGA---IRYIINTADIS 196
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAVG--KPGDRVLLLAPPG-LDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 197 TVIVDKPQKAvLLLEHVERKETPGLKLIILMDPFEEALKERGQkcgvviksmqavedcgqenhqaPVPPQPDDLSIVCFT 276
Cdd:cd05931 101 VVLTTAAALA-AVRAFAASRPAAGTPRLLVVDLLPDTSAADWP----------------------PPSPDPDDIAYLQYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 277 SGTTGNPKGAMLTHGNVVADFSGFLKvtesQWAPTCADVHISYLPLAH-MfermvqsvvychgGRVG------FFQGDIR 349
Cdd:cd05931 158 SGSTGTPKGVVVTHRNLLANVRQIRR----AYGLDPGDVVVSWLPLYHdM-------------GLIGglltplYSGGPSV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 350 LLSddmkalcPTIFpvvprlLNRmydkifsqantPLkRWL-----------------LEFAAKRKQAEVRSGIirndsiw 412
Cdd:cd05931 221 LMS-------PAAF------LRR-----------PL-RWLrlisryratisaapnfaYDLCVRRVRDEDLEGL------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 413 dELffnkiqaslgGCVRMIVTGAAPASPTVL----------GFLRAAlgcqVYEGYGQTECTAGCTFTTPG--------- 473
Cdd:cd05931 269 -DL----------SSWRVALNGAEPVRPATLrrfaeafapfGFRPEA----FRPSYGLAEATLFVSGGPPGtgpvvlrvd 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 474 -DWTSGHV----------------GAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKE------AL 530
Cdd:cd05931 334 rDALAGRAvavaaddpaarelvscGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaAT 413
|
490
....*....|..
gi 327412323 531 DSDGWLHTGDIG 542
Cdd:cd05931 414 DEGGWLRTGDLG 425
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
121-607 |
1.66e-23 |
|
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: 104.25 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLyDTLGPGA-IRYIINTADISTVI 199
Cdd:cd05945 17 LTYRELKERADALAAALASLGLDA--GDPVVVYGHKSPDAIAAFLAALKAGHAYVPL-DASSPAErIREILDAAKPALLI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 200 VDkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhqapvppqPDDLSIVCFTSGT 279
Cdd:cd05945 94 AD-----------------------------------------------------------------GDDNAYIIFTSGS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 280 TGNPKGAMLTHGNVVAdfsgFLKVTESQWAPTCADVHISYLPLAhmFERMVQSVVYC--HGGrvgffqgdirllsddmka 357
Cdd:cd05945 109 TGRPKGVQISHDNLVS----FTNWMLSDFPLGPGDVFLNQAPFS--FDLSVMDLYPAlaSGA------------------ 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 358 lcpTIFPVvPRLLNRMYDKIFSQ-ANTPLKRWLlefaakrkqaevrsgiiRNDSIWDELF----FNkiQASLGGCVRMIV 432
Cdd:cd05945 165 ---TLVPV-PRDATADPKQLFRFlAEHGITVWV-----------------STPSFAAMCLlsptFT--PESLPSLRHFLF 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 433 TGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFT--TP---GDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGE 507
Cdd:cd05945 222 CGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIevTPevlDGYDRLPIGYAKPGAKLVILD-EDGRPVPPGEKGE 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 508 ICVRGPNVFKGYLKDPDRTKEALDSD---GWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVA 584
Cdd:cd05945 301 LVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIELEEIEAALRQVPGVK 379
|
490 500
....*....|....*....|....*..
gi 327412323 585 QIYV----HGDSlKAFLVGIVVPDPEV 607
Cdd:cd05945 380 EAVVvpkyKGEK-VTELIAFVVPKPGA 405
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
122-605 |
1.66e-23 |
|
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: 105.02 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 122 SYQEVADRAEFLGSGLlqHNCKACTDQFIGVFAQNRpewiIVELACYtY-----SMVVVPLYDTLGPGAIRYIINTADIS 196
Cdd:cd12119 27 TYAEVAERARRLANAL--RRLGVKPGDRVATLAWNT----HRHLELY-YavpgmGAVLHTINPRLFPEQIAYIINHAEDR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 197 TVIVDK---PQKAVLL--LEHVERketpglklIILMDPFEEALKERGQKcgvVIKSMQAVEDcgqenhQAPVPPQPD--- 268
Cdd:cd12119 100 VVFVDRdflPLLEAIAprLPTVEH--------VVVMTDDAAMPEPAGVG---VLAYEELLAA------ESPEYDWPDfde 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 269 -DLSIVCFTSGTTGNPKGAMLTHGNVVadfsgflkvtesqwaptcadvhisylplahmfermVQSVVYCHGGRVGFFQGD 347
Cdd:cd12119 163 nTAAAICYTSGTTGNPKGVVYSHRSLV-----------------------------------LHAMAALLTDGLGLSESD 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 348 irllsddmkalcpTIFPVVPrllnrMYdkifsQANTplkrWLLEFAA-----------KRKQAEVRSGIIRND------- 409
Cdd:cd12119 208 -------------VVLPVVP-----MF-----HVNA----WGLPYAAamvgaklvlpgPYLDPASLAELIEREgvtfaag 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 410 --SIWDELF--FNKIQASLGGCVRMIVTGAAPASPTVLGFlrAALGCQVYEGYGQTECTAGCTFTTPgdwTSGHV----- 480
Cdd:cd12119 261 vpTVWQGLLdhLEANGRDLSSLRRVVIGGSAVPRSLIEAF--EERGVRVIHAWGMTETSPLGTVARP---PSEHSnlsed 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 481 ---------GAPLPCNHIKLVDVE--ELNyWACKGEGEICVRGPNVFKGYLKDPDRTkEALDSDGWLHTGDIGKWLPAGT 549
Cdd:cd12119 336 eqlalrakqGRPVPGVELRIVDDDgrELP-WDGKAVGELQVRGPWVTKSYYKNDEES-EALTEDGWLRTGDVATIDEDGY 413
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 327412323 550 LKIIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVhgdslkaflvgIVVPDP 605
Cdd:cd12119 414 LTITDRSKDVIKSG-GEWISSVELENAIMAHPAVAEAAV-----------IGVPHP 457
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
162-574 |
2.78e-23 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 105.78 E-value: 2.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 162 IVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKpqkavlllEHVERKETPGLKLIILMDP---FEEALKER- 237
Cdd:PRK08633 680 LANLALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVITSR--------KFLEKLKNKGFDLELPENVkviYLEDLKAKi 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 238 --GQKC--GVVIKSMQAVEDCGQENHqapvPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD---FSGFLKVTESqwap 310
Cdd:PRK08633 752 skVDKLtaLLAARLLPARLLKRLYGP----TFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNieqISDVFNLRND---- 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 311 tcaDVHISYLPLAHMFERMVQ---------SVVYcH-----GGRVGffqgdirLLSDDMKA--LC--PTIFpvvprllnR 372
Cdd:PRK08633 824 ---DVILSSLPFFHSFGLTVTlwlpllegiKVVY-HpdptdALGIA-------KLVAKHRAtiLLgtPTFL--------R 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 373 MYdkifsqantplkrwllefaakrkqaevrsgiIRNDSIWDELFfnkiqASLggcvRMIVTGAAPASPTVLGFLRAALGC 452
Cdd:PRK08633 885 LY-------------------------------LRNKKLHPLMF-----ASL----RLVVAGAEKLKPEVADAFEEKFGI 924
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 453 QVYEGYGQTECTAGCTFTTP-----GDWT-----SGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKD 522
Cdd:PRK08633 925 RILEGYGATETSPVASVNLPdvlaaDFKRqtgskEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGD 1004
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 327412323 523 PDRTKEAL---DSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIE 574
Cdd:PRK08633 1005 PEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIG-GEMVPLGAVE 1058
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
156-576 |
3.82e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 104.09 E-value: 3.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 156 NRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADiSTVIVDKPQKAVLLLEhvERKETPGLKLIILMDPFEEAlk 235
Cdd:PRK07786 76 NRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCG-AHVVVTEAALAPVATA--VRDIVPLLSTVVVAGGSSDD-- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 236 ergqkcGVViksmqAVEDCGQENHQAPVPPQ-PDDL-SIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEsqwAPTCA 313
Cdd:PRK07786 151 ------SVL-----GYEDLLAEAGPAHAPVDiPNDSpALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNG---ADINS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 314 DVHISYLPLAHMfeRMVQSVVychggrVGFFQGdirllsddmkalCPT-IFPVVPRLLNRMYDkifsqantplkrwLLEf 392
Cdd:PRK07786 217 DVGFVGVPLFHI--AGIGSML------PGLLLG------------APTvIYPLGAFDPGQLLD-------------VLE- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 393 aakrkqAEVRSGIIRNDSIWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAgCTFTT 471
Cdd:PRK07786 263 ------AEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEMSP-VTCML 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 472 PGD---WTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSdGWLHTGDIGKWLPAG 548
Cdd:PRK07786 336 LGEdaiRKLGSVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDEEG 413
|
410 420
....*....|....*....|....*...
gi 327412323 549 TLKIIDRKKHIFkLAQGEYVAPEKIENI 576
Cdd:PRK07786 414 YVWVVDRKKDMI-ISGGENIYCAEVENV 440
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
107-605 |
4.77e-23 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 103.67 E-value: 4.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 107 PCLGFRKPKQPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTY---SMVVVPLYDTLGp 183
Cdd:cd05921 12 TWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGLSA--ERPLLILSGNSIEHALMALAAMYAgvpAAPVSPAYSLMS- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 184 gairyiintADISTvivdkpqkavllLEHVERKETPGLKLIILMDPFEEALKERGQKCGVVIKSMQAVEDCGQEN----- 258
Cdd:cd05921 89 ---------QDLAK------------LKHLFELLKPGLVFAQDAAPFARALAAIFPLGTPLVVSRNAVAGRGAISfaela 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 259 HQAP---VPP-----QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLkvtesQWAPTCAD---VHISYLPLAHMF- 326
Cdd:cd05921 148 ATPPtaaVDAafaavGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLE-----QTYPFFGEeppVLVDWLPWNHTFg 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 327 -ERMVQSVVYcHGGRV---------GFFQGDIRLLSDDMkalcPTIFPVVPrllnrmydkifsqantplKRWllefaakr 396
Cdd:cd05921 223 gNHNFNLVLY-NGGTLyiddgkpmpGGFEETLRNLREIS----PTVYFNVP------------------AGW-------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 397 kqaEVRSGIIRNDSIWDELFFNKiqaslggcVRMIVTGAAPASPTVLGFLRA----ALGCQV--YEGYGQTECTAGCTFT 470
Cdd:cd05921 272 ---EMLVAALEKDEALRRRFFKR--------LKLMFYAGAGLSQDVWDRLQAlavaTVGERIpmMAGLGATETAPTATFT 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 471 TPGDWTSGHVGAPLPCNHIKLVdveelnywACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWL----P 546
Cdd:cd05921 341 HWPTERSGLIGLPAPGTELKLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpddP 412
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 327412323 547 AGTLKIIDRKKHIFKLAQGEYVA--PekieniyIRSQPVAQI--YVHgDSL-----KAFLVGIVVPDP 605
Cdd:cd05921 413 AKGLVFDGRVAEDFKLASGTWVSvgP-------LRARAVAACapLVH-DAVvagedRAEVGALVFPDL 472
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
121-606 |
4.85e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 103.97 E-value: 4.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PRK06178 59 ITYAELDELSDRFAALLRQRGVGA-GDR-VAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 201 dkpQKAVL-LLEHVeRKETPgLKLII---LMD--------PFEEALKERGQKCGVVIKSMQAVEDCGQENHQAPvpPQPD 268
Cdd:PRK06178 137 ---LDQLApVVEQV-RAETS-LRHVIvtsLADvlpaeptlPLPDSLRAPRLAAAGAIDLLPALRACTAPVPLPP--PALD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 269 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPtcaDVHISYLPlahMFermvqsvvYCHGGRVGFfqgdi 348
Cdd:PRK06178 210 ALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGED---SVFLSFLP---EF--------WIAGENFGL----- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 349 rllsddmkalcptIFPvvprllnrmydkIFSQANTPL-KRW-LLEFAAKRKQAEVRSGIIRNDSIwDELF---------F 417
Cdd:PRK06178 271 -------------LFP------------LFSGATLVLlARWdAVAFMAAVERYRVTRTVMLVDNA-VELMdhprfaeydL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 418 NKIQASlgGCVRMIvtgaAPASPTVLGFLRAALGCQVYEG-YGQTECTAGCTFTTpGDWTSGH--------VGAPLPCNH 488
Cdd:PRK06178 325 SSLRQV--RVVSFV----KKLNPDYRQRWRALTGSVLAEAaWGMTETHTCDTFTA-GFQDDDFdllsqpvfVGLPVPGTE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 489 IKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYV 568
Cdd:PRK06178 398 FKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV-NGMSV 475
|
490 500 510
....*....|....*....|....*....|....*...
gi 327412323 569 APEKIENIYIRsqpvaqiyvHGDSLKAFLVGivVPDPE 606
Cdd:PRK06178 476 FPSEVEALLGQ---------HPAVLGSAVVG--RPDPD 502
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
265-605 |
6.21e-23 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 103.21 E-value: 6.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 265 PQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD---FSGFLKVTESqwaptcaDVHISYLPLAHMfermvqsvvychggrV 341
Cdd:PRK13295 194 PGPDDVTQLIYTSGTTGEPKGVMHTANTLMANivpYAERLGLGAD-------DVILMASPMAHQ---------------T 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 342 GFFQGDIRLLSDDMKALCPTIFPVVprllnRMYDKI------FSQANTPlkrWLLEFAakRKQAEVRSGIirndsiwdel 415
Cdd:PRK13295 252 GFMYGLMMPVMLGATAVLQDIWDPA-----RAAELIrtegvtFTMASTP---FLTDLT--RAVKESGRPV---------- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 416 ffnkiqASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPGD---WTSGHVGAPLPCNHIKLV 492
Cdd:PRK13295 312 ------SSL----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA-VTLTKLDDpdeRASTTDGCPLPGVEVRVV 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 493 DvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTkeALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEK 572
Cdd:PRK13295 381 D-ADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVE 456
|
330 340 350
....*....|....*....|....*....|....
gi 327412323 573 IENIYIRSQPVAQiyvhgdslkaflVGIV-VPDP 605
Cdd:PRK13295 457 IEALLYRHPAIAQ------------VAIVaYPDE 478
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
220-574 |
1.07e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 102.38 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 220 GLKLIILMDPFEEA---LKERGQKcgvviksMQAVEDCGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD 296
Cdd:PRK07768 108 GAKAVVVGEPFLAAapvLEEKGIR-------VLTVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYAN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 297 FSGFlkVTESQWAPTcADVHISYLPLAH-MfermvqsvvychgGRVGFfqgdirlLSDDMKALC------PTIFPVVPRL 369
Cdd:PRK07768 181 AEAM--FVAAEFDVE-TDVMVSWLPLFHdM-------------GMVGF-------LTVPMYFGAelvkvtPMDFLRDPLL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 370 LNRMYDKiFSQANTPLKRWLLEFAAKR--KQAEvrsgiirnDSIWDElffnkiqaslgGCVRMIVTGAAPASPTVL---- 443
Cdd:PRK07768 238 WAELISK-YRGTMTAAPNFAYALLARRlrRQAK--------PGAFDL-----------SSLRFALNGAEPIDPADVedll 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 444 ------GFLRAALGCqvyeGYGQTECTAGCTFTTPGD--------------------WTSGHV------GAPLPCNHIKL 491
Cdd:PRK07768 298 dagarfGLRPEAILP----AYGMAEATLAVSFSPCGAglvvdevdadllaalrravpATKGNTrrlatlGPPLPGLEVRV 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 492 VDvEELNYWACKGEGEICVRGPNVFKGYLkDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPE 571
Cdd:PRK07768 374 VD-EDGQVLPPRGVGVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPT 450
|
...
gi 327412323 572 KIE 574
Cdd:PRK07768 451 DIE 453
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
121-605 |
1.38e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 101.93 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PRK08316 37 WTYAELDAAVNRVAAALLDLGLKK-GDR-VAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 201 DkpqkaVLLLEHVErketPGLKLIiLMDPFEEALKERGQkcgVVIKSMQAVEDCGQEnhQAPVPPQP----DDLSIVCFT 276
Cdd:PRK08316 115 D-----PALAPTAE----AALALL-PVDTLILSLVLGGR---EAPGGWLDFADWAEA--GSVAEPDVeladDDLAQILYT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 277 SGTTGNPKGAMLTHGNVVADFSGflKVTESQWAPTcaDVHISYLPLAHMFERMVqsvvychggrvgFFQGDIRLLSDDMK 356
Cdd:PRK08316 180 SGTESLPKGAMLTHRALIAEYVS--CIVAGDMSAD--DIPLHALPLYHCAQLDV------------FLGPYLYVGATNVI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 357 ALCPTIfpvvprllNRMYDKIFSQANTPLkrwlleFAAKrkqaevrsgiirndSIWDELF----FNKIQASlggCVRMIV 432
Cdd:PRK08316 244 LDAPDP--------ELILRTIEAERITSF------FAPP--------------TVWISLLrhpdFDTRDLS---SLRKGY 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 433 TGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFTTPGDwtsgHVGAP----LPCNHI--KLVDvEELNYWAcKGE 505
Cdd:PRK08316 293 YGASIMPVEVLKELRERLpGLRFYNCYGQTEIAPLATVLGPEE----HLRRPgsagRPVLNVetRVVD-DDGNDVA-PGE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 506 -GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIyirsqpva 584
Cdd:PRK08316 367 vGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEA-------- 436
|
490 500
....*....|....*....|.
gi 327412323 585 qIYVHGDSLKAFLVGivVPDP 605
Cdd:PRK08316 437 -LYTHPAVAEVAVIG--LPDP 454
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-615 |
1.18e-21 |
|
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: 97.17 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsGFLKVTESQWAPTcaDVHISYLPLAHMFERMVQsvvychgGRVGFFQG 346
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYN--AWMLALNSLFDPD--DVLLCGLPLFHVNGSVVT-------LLTPLASG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 347 DIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTPLkrwllefaAKRKQAEVRSGIirndsiwdelffnkiqaslgG 426
Cdd:cd05944 70 AHVVLAGPAGYRNPGLFDNFWKLVERYRITSLSTVPTVY--------AALLQVPVNADI--------------------S 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 427 CVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLV--DVEELNYWACK 503
Cdd:cd05944 122 SLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKvlDGVGRLLRDCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 504 GE--GEICVRGPNVFKGYLKDpDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQ 581
Cdd:cd05944 202 PDevGEICVAGPGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLRHP 279
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 327412323 582 PVAQIYVHG--DSLKAFL-VGIV--VPDPEVMP----SWAQKR 615
Cdd:cd05944 280 AVAFAGAVGqpDAHAGELpVAYVqlKPGAVVEEeellAWARDH 322
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
269-685 |
1.97e-21 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 95.86 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 269 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkvTESQWAPTCADVHISYLPLAHM--FERMVQSVVycHGGRVGFFQG 346
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAG----LHSRLGFGGGDSWLLSLPLYHVggLAILVRSLL--AGAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 347 DiRLLSDDMKALCPTIFPVVPRLLNRMYDKifSQANTPLKRwllefaakrkqaevrsgiirndsiwdelffnkiqaslgg 426
Cdd:cd17630 75 N-QALAEDLAPPGVTHVSLVPTQLQRLLDS--GQGPAALKS--------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 427 cVRMIVTGAAPASPtvlGFLRAA--LGCQVYEGYGQTEcTAGCTFT-TPGDWTSGHVGAPLPCNHIKLVDveelnywack 503
Cdd:cd17630 113 -LRAVLLGGAPIPP---ELLERAadRGIPLYTTYGMTE-TASQVATkRPDGFGRGGVGVLLPGRELRIVE---------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 504 gEGEICVRGPNVFKGYLKDPdrTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIyIRSQP- 582
Cdd:cd17630 178 -DGEIWVGGASLAMGYLRGQ--LVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAA-LAAHPa 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 583 VAQIYVHGdslkaflvgivVPDPEvmpsWAQKrgiegTYADLCTNKDLKKAILEDMVRlgkeSGLHSFEQVKAIHIhsdm 662
Cdd:cd17630 253 VRDAFVVG-----------VPDEE----LGQR-----PVAVIVGRGPADPAELRAWLK----DKLARFKLPKRIYP---- 304
|
410 420
....*....|....*....|...
gi 327412323 663 fsVQNGLLTPTLKAKRPELREYF 685
Cdd:cd17630 305 --VPELPRTGGGKVDRRALRAWL 325
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
119-615 |
8.95e-21 |
|
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: 96.24 E-value: 8.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 119 QWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLyDTLGPGA-IRYIINTADIST 197
Cdd:cd17655 21 QTLTYRELNERANQLARTLREKGVGP--DTIVGIMAERSLEMIVGILGILKAGGAYLPI-DPDYPEErIQYILEDSGADI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 198 VIVDKPQKAVLLlehverketpGLKLIILMDpfEEALKErgqkcgvviksmqavedcgQENHQAPVPPQPDDLSIVCFTS 277
Cdd:cd17655 98 LLTQSHLQPPIA----------FIGLIDLLD--EDTIYH-------------------EESENLEPVSKSDDLAYVIYTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 278 GTTGNPKGAMLTHGNVVadfsgflkvtesqwaptcadvhisylplaHMFERMVQSVVYCHGGRVGFFQGdirlLSDDMka 357
Cdd:cd17655 147 GSTGKPKGVMIEHRGVV-----------------------------NLVEWANKVIYQGEHLRVALFAS----ISFDA-- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 358 lcpTIFPVVPRLL--NRMYdkIFSQANTPLKRWLLEFAAKRkqaevRSGIIR-NDSIWDELffNKIQASLGGCVRMIVTG 434
Cdd:cd17655 192 ---SVTEIFASLLsgNTLY--IVRKETVLDGQALTQYIRQN-----RITIIDlTPAHLKLL--DAADDSEGLSLKHLIVG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 435 AAPASPTVLGFL--RAALGCQVYEGYGQTECTAGCTF--TTPGDWTSGHV--GAPLPCNHIKLVDvEELNYWACKGEGEI 508
Cdd:cd17655 260 GEALSTELAKKIieLFGTNPTITNAYGPTETTVDASIyqYEPETDQQVSVpiGKPLGNTRIYILD-QYGRPQPVGVAGEL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 509 CVRGPNVFKGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQP 582
Cdd:cd17655 339 YIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-RGYRIELGEIEARLLQHPD 417
|
490 500 510
....*....|....*....|....*....|....*.
gi 327412323 583 VAQ---IYVHGDSLKAFLVGIVVPDPEVMPSWAQKR 615
Cdd:cd17655 418 IKEavvIARKDEQGQNYLCAYIVSEKELPVAQLREF 453
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
121-576 |
1.92e-20 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 96.57 E-value: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLGsGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PRK06814 659 LTYRKLLTGAFVLG-RKLKKNTPP--GENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 201 DKP--QKAVL--LLEHVERketpGLKLIILMDPFEE---ALKERGqkcgVVIKSMQAVEDCGqenhqapvpPQPDDLSIV 273
Cdd:PRK06814 736 SRAfiEKARLgpLIEALEF----GIRIIYLEDVRAQiglADKIKG----LLAGRFPLVYFCN---------RDPDDPAVI 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 274 CFTSGTTGNPKGAMLTHGNVVA---------DFSGflkvtesqwaptcADVHISYLPLAHMFermvqsvvychggrvGFF 344
Cdd:PRK06814 799 LFTSGSEGTPKGVVLSHRNLLAnraqvaariDFSP-------------EDKVFNALPVFHSF---------------GLT 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 345 QGDIRLLSDDMKAL---CPTIFPVVPRLLnrmYDK----IFSqANTPLkrwllefaakrkqaevrSGIIRNDSIWDelFF 417
Cdd:PRK06814 851 GGLVLPLLSGVKVFlypSPLHYRIIPELI---YDTnatiLFG-TDTFL-----------------NGYARYAHPYD--FR 907
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 418 NkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEEL 497
Cdd:PRK06814 908 S---------LRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGI 978
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 498 NywacKGeGEICVRGPNVFKGYLK-DPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENI 576
Cdd:PRK06814 979 D----EG-GRLFVRGPNVMLGYLRaENPGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAVEEL 1051
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
152-605 |
2.21e-20 |
|
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: 95.25 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 152 VFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKavlLLEHVE--RKETPGL-KLIILMD 228
Cdd:cd05970 77 LTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDN---IPEEIEkaAPECPSKpKLVWVGD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 229 PFEEALKERGQKCgvviksMQAVEDCgqENHQAPVPPQPDDLSIVCFTSGTTGNPKgaMLTHGNV--------------V 294
Cdd:cd05970 154 PVPEGWIDFRKLI------KNASPDF--ERPTANSYPCGEDILLVYFSSGTTGMPK--MVEHDFTyplghivtakywqnV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 295 ADFSGFLKVTESQWAPTC-ADVHISYLPLAHMFermvqsvVYCHGGrvgFFQGDI--RLLSDDMKALC--PTIFpvvprl 369
Cdd:cd05970 224 REGGLHLTVADTGWGKAVwGKIYGQWIAGAAVF-------VYDYDK---FDPKALleKLSKYGVTTFCapPTIY------ 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 370 lnrmydkifsqantplkRWLlefaakrkqaeVRSGIIRNDsiwdelfFNKIqaslggcvRMIVTGAAPASPTVLGFLRAA 449
Cdd:cd05970 288 -----------------RFL-----------IREDLSRYD-------LSSL--------RYCTTAGEALNPEVFNTFKEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 450 LGCQVYEGYGQTECTAgCTFTTPG-DWTSGHVGAPLPCNHIKLVDVEELnywACKG--EGEICVRGPN-----VFKGYLK 521
Cdd:cd05970 325 TGIKLMEGFGQTETTL-TIATFPWmEPKPGSMGKPAPGYEIDLIDREGR---SCEAgeEGEIVIRTSKgkpvgLFGGYYK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 522 DPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYVHGdslkaflvgiv 601
Cdd:cd05970 401 DAEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVESALIQHPAVLECAVTG----------- 467
|
....
gi 327412323 602 VPDP 605
Cdd:cd05970 468 VPDP 471
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
150-610 |
2.24e-20 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 95.34 E-value: 2.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 150 IGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKpqkavlLLEHVERKET-PGLKLIILMD 228
Cdd:PRK05852 71 VALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDA------DGPHDRAEPTtRWWPLTVNVG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 229 PfeealkERGQKCGVVIKSMQAVedcGQENHQAPVPP--QPDDLSIVcFTSGTTGNPKGAMLTHGNVVADFSGFlkVTES 306
Cdd:PRK05852 145 G------DSGPSGGTLSVHLDAA---TEPTPATSTPEglRPDDAMIM-FTGGTTGLPKMVPWTHANIASSVRAI--ITGY 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 307 QWAPtcADVHISYLPLAH---MFERMVQSVVycHGGRV-----GFFQGdiRLLSDDMKALCPTIFPVVPrllnrmydkif 378
Cdd:PRK05852 213 RLSP--RDATVAVMPLYHghgLIAALLATLA--SGGAVllparGRFSA--HTFWDDIKAVGATWYTAVP----------- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 379 sqantPLKRWLLEFAAKRKQAEVRSGIirndsiwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGY 458
Cdd:PRK05852 276 -----TIHQILLERAATEPSGRKPAAL-----------------------RFIRSCSAPLTAETAQALQTEFAAPVVCAF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 459 GQTECTAGCTfTTPGDWtSGHVGAPLPCN---------HIKLV--DVEELNYWACkgeGEICVRGPNVFKGYLKDPDRTK 527
Cdd:PRK05852 328 GMTEATHQVT-TTQIEG-IGQTENPVVSTglvgrstgaQIRIVgsDGLPLPAGAV---GEVWLRGTTVVRGYLGDPTITA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 528 EALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAF---LVGIVVPD 604
Cdd:PRK05852 403 ANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLASHPNVMEAAVFGVPDQLYgeaVAAVIVPR 480
|
....*.
gi 327412323 605 PEVMPS 610
Cdd:PRK05852 481 ESAPPT 486
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
267-682 |
1.57e-19 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 92.94 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVAD------FSGFlkvTESqwaptcaDVHISYLPLAH-------MFERMVQSv 333
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSALIVQslakiaIVGY---GED-------DVYLHTAPLCHigglssaLAMLMVGA- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 334 vyCHggrVGFFQGDIRLLSDDMKALCPTIFPVVPRLlnrMYDkifsqantplkrwLLEFAAKRKqaevrsgiirndsIWD 413
Cdd:PLN02860 240 --CH---VLLPKFDAKAALQAIKQHNVTSMITVPAM---MAD-------------LISLTRKSM-------------TWK 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 414 ElffnkiqaslGGCVRMIVTGAAPASP-----TVLGFLRAALgcqvYEGYGQTECTAGCTFTTPGDWT------------ 476
Cdd:PLN02860 286 V----------FPSVRKILNGGGSLSSrllpdAKKLFPNAKL----FSAYGMTEACSSLTFMTLHDPTlespkqtlqtvn 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 477 -----SGH------VGAPLPcnHIKLvdveELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWL 545
Cdd:PLN02860 352 qtkssSVHqpqgvcVGKPAP--HVEL----KIGLDESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWID 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 546 PAGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYVHGdSLKAFLVGIVVPDPEVMPSWaqkRGIEGTYADLC 625
Cdd:PLN02860 426 KAGNLWLIGRSNDRIK-TGGENVYPEEVEAVLSQHPGVASVVVVG-VPDSRLTEMVVACVRLRDGW---IWSDNEKENAK 500
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 327412323 626 TNKDLKKAILEDMVRlgkESGLHSFEQVKAIHIHSDMFSvqnglLTPTLKAKRPELR 682
Cdd:PLN02860 501 KNLTLSSETLRHHCR---EKNLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEVR 549
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
150-618 |
2.43e-19 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 91.34 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 150 IGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDkpqkavlllehverketpglkliilmdp 229
Cdd:cd05971 34 VGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTD---------------------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 230 feealkergqkcgvviksmqavedcgqenhqapvppQPDDLSIVCFTSGTTGNPKGAMLTH----GNVVADF-------- 297
Cdd:cd05971 86 ------------------------------------GSDDPALIIYTSGTTGPPKGALHAHrvllGHLPGVQfpfnlfpr 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 298 SGFLKVTESQWAPTCA--DVHISYL----P-LAHMFERmvqsvvychggrvgfFQGD--IRLLSD---DMKALCPTIFpv 365
Cdd:cd05971 130 DGDLYWTPADWAWIGGllDVLLPSLyfgvPvLAHRMTK---------------FDPKaaLDLMSRygvTTAFLPPTAL-- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 366 vprllnrmydKIFSQANTPLKRWLLEfaakrkqaevrsgiirndsiwdelffnkiqaslggcVRMIVTGAAPASPTVLGF 445
Cdd:cd05971 193 ----------KMMRQQGEQLKHAQVK------------------------------------LRAIATGGESLGEELLGW 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 446 LRAALGCQVYEGYGQTEC---TAGCTFTTPGDwtSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPN--VFKGYL 520
Cdd:cd05971 227 AREQFGVEVNEFYGQTECnlvIGNCSALFPIK--PGSMGKPIPGHRVAIVD-DNGTPLPPGEVGEIAVELPDpvAFLGYW 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 521 KDPDRTKEALDSDgWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYV-------HGDSL 593
Cdd:cd05971 304 NNPSATEKKMAGD-WLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAEIEECLLKHPAVLMAAVvgipdpiRGEIV 381
|
490 500
....*....|....*....|....*
gi 327412323 594 KAFlvgiVVPDPEVMPSWAQKRGIE 618
Cdd:cd05971 382 KAF----VVLNPGETPSDALAREIQ 402
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
121-607 |
3.03e-19 |
|
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: 91.49 E-value: 3.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELA------CYtysmvvVPLYDTLGPGAIRYIINTAD 194
Cdd:cd12117 23 LTYAELNERANRLARRLRAAGVGP--GDVVGVLAERSPELVVALLAvlkagaAY------VPLDPELPAERLAFMLADAG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 195 ISTVIVDKPQKAVLLLehverketPGLKLIILMDPFEEALKErgqkcgvviksmqavedcgqenhqAPVPPQPDDLSIVC 274
Cdd:cd12117 95 AKVLLTDRSLAGRAGG--------LEVAVVIDEALDAGPAGN------------------------PAVPVSPDDLAYVM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 275 FTSGTTGNPKGAMLTHGNVVAdfsgflKVTESQWAPTCA-DVHISYLPL---AHMFERMVQSVvycHGGRVgffqgdirl 350
Cdd:cd12117 143 YTSGSTGRPKGVAVTHRGVVR------LVKNTNYVTLGPdDRVLQTSPLafdASTFEIWGALL---NGARL--------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 351 lsddmkALCPTIFPVVPRLLnrmydkifsqantplkrwllefaakrkQAEVRSGIIrnDSIWdeL---FFNKI----QAS 423
Cdd:cd12117 205 ------VLAPKGTLLDPDAL---------------------------GALIAEEGV--TVLW--LtaaLFNQLadedPEC 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 424 LGGcVRMIVTGAAPASPT-VLGFLRAALGCQVYEGYGQTECTagcTFTT-----PGDWTSGHV--GAPLPCNHIKLVDve 495
Cdd:cd12117 248 FAG-LRELLTGGEVVSPPhVRRVLAACPGLRLVNGYGPTENT---TFTTshvvtELDEVAGSIpiGRPIANTRVYVLD-- 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 496 ELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYV 568
Cdd:cd12117 322 EDGRPVPPGVpGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI-RGFRI 400
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 327412323 569 APEKIENIyIRSQP-VAQIYV---HGDSLKAFLVGIVVPDPEV 607
Cdd:cd12117 401 ELGEIEAA-LRAHPgVREAVVvvrEDAGGDKRLVAYVVAEGAL 442
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
262-616 |
4.22e-19 |
|
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: 90.87 E-value: 4.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 262 PVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVV-------ADFSGFLKVTESQWAPTCADVhisylplahmferMVQSV- 333
Cdd:cd17651 130 DPALDADDLAYVIYTSGSTGRPKGVVMPHRSLAnlvawqaRASSLGPGARTLQFAGLGFDV-------------SVQEIf 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 334 -VYCHGGRVGFFQGDIRLLSDDMKALCPTifpvvpRLLNRMYdkifsqANTPLKRWLLEfAAKRKQAEvrsgiirndsiw 412
Cdd:cd17651 197 sTLCAGATLVLPPEEVRTDPPALAAWLDE------QRISRVF------LPTVALRALAE-HGRPLGVR------------ 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 413 delffnkiqaslGGCVRMIVTG--AAPASPTVLGFLRAALGCQVYEGYGQTE---CTAGCTFTTPGDWTS-GHVGAPLPC 486
Cdd:cd17651 252 ------------LAALRYLLTGgeQLVLTEDLREFCAGLPGLRLHNHYGPTEthvVTALSLPGDPAAWPApPPIGRPIDN 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 487 NHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKIIDRKKHIF 560
Cdd:cd17651 320 TRVYVLD-AALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQV 398
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 327412323 561 KLaQGEYVAPEKIENIYIRSQPVAQIYV------HGDslkAFLVGIVVPDPEVMPSWAQKRG 616
Cdd:cd17651 399 KI-RGFRIELGEIEAALARHPGVREAVVlaredrPGE---KRLVAYVVGDPEAPVDAAELRA 456
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
121-609 |
6.56e-19 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 90.07 E-value: 6.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVG--PESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 201 DkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhqapvppqPDDLSIVCFTSGTT 280
Cdd:cd12115 103 D-----------------------------------------------------------------PDDLAYVIYTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 281 GNPKGAMLTHGNVVA------------DFSGFLKVTesqwaPTCADVHI--SYLPLahmfermvqsvvyCHGGRVGFFQG 346
Cdd:cd12115 118 GRPKGVAIEHRNAAAflqwaaaafsaeELAGVLAST-----SICFDLSVfeLFGPL-------------ATGGKVVLADN 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 347 DIRLLsdDMKALCP-TIFPVVPRLLnrmydkifsqantplkRWLLEFaakrkqaevrsgiirndsiwdelffNKIQASlg 425
Cdd:cd12115 180 VLALP--DLPAAAEvTLINTVPSAA----------------AELLRH-------------------------DALPAS-- 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 426 gcVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFT--TPGDWTSGHVGAPLPCNHIKLVDvEELNYWAC 502
Cdd:cd12115 215 --VRVVNLAGEPLPRDLVQRLYARLqVERVVNLYGPSEDTTYSTVApvPPGASGEVSIGRPLANTQAYVLD-RALQPVPL 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 503 KGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENI 576
Cdd:cd12115 292 GVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAA 370
|
490 500 510
....*....|....*....|....*....|....*..
gi 327412323 577 yIRSQP-VAQ--IYVHGDSL-KAFLVGIVVPDPEVMP 609
Cdd:cd12115 371 -LRSIPgVREavVVAIGDAAgERRLVAYIVAEPGAAG 406
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
249-623 |
7.64e-19 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 89.83 E-value: 7.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 249 QAVEDCGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSG--FLKVTESqwaptcaDVHISylpLAH 324
Cdd:cd05919 72 DDYAYIARDCEARLVVTSADDIAYLLYSSGTTGPPKGVMHAHRDPLlfADAMAreALGLTPG-------DRVFS---SAK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 325 MFermvqsVVYCHGGRVGF--FQGDIRLLSDD----------MKALCPTIFPVVPRllnrMYDKIFSQANTPlkrwllef 392
Cdd:cd05919 142 MF------FGYGLGNSLWFplAVGASAVLNPGwptaervlatLARFRPTVLYGVPT----FYANLLDSCAGS-------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 393 aakrkQAEVRSgiIRndsiwdelffnkiqaslggcvrmIVTGAAPASPTVLG-FLRAALGCQVYEGYGQTEctAGCTFTT 471
Cdd:cd05919 204 -----PDALRS--LR-----------------------LCVSAGEALPRGLGeRWMEHFGGPILDGIGATE--VGHIFLS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 472 --PGDWTSGHVGAPLPCNHIKLVDveELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAG 548
Cdd:cd05919 252 nrPGAWRLGSTGRPVPGYEIRLVD--EEGHTIPPGEeGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 549 TLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYV----HGDSL---KAFlvgiVVPDPEVMPSWAQKRGIEGTY 621
Cdd:cd05919 329 WYTHAGRADDMLKVG-GQWVSPVEVESLIIQHPAVAEAAVvavpESTGLsrlTAF----VVLKSPAAPQESLARDIHRHL 403
|
..
gi 327412323 622 AD 623
Cdd:cd05919 404 LE 405
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
266-615 |
1.75e-18 |
|
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: 88.68 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 266 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKvtesqwaptcaDVHISYLPLAHMfermvqsvvychggRVGFFQ 345
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRR-----------EYELDSFPVRLL--------------QMASFS 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 346 GDIrLLSDDMKALCP--TIFPVVPRLL---NRMYDKIFSQ-----ANTP-LKRWLLEFAAKRKQ--AEVRSGIIRNDSIW 412
Cdd:cd17650 146 FDV-FAGDFARSLLNggTLVICPDEVKldpAALYDLILKSritlmESTPaLIRPVMAYVYRNGLdlSAMRLLIVGSDGCK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 413 DElFFNKIQASLGGCVRMIvtgaapaspTVLGFLRAALGCQVYEGYGQTECTAGctfTTPgdwtsghVGAPLPCNHIKLV 492
Cdd:cd17650 225 AQ-DFKTLAARFGQGMRII---------NSYGVTEATIDSTYYEEGRDPLGDSA---NVP-------IGRPLPNTAMYVL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 493 DvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGW------LHTGDIGKWLPAGTLKIIDRKKHIFKLaQGE 566
Cdd:cd17650 285 D-ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI-RGF 362
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 327412323 567 YVAPEKIENIYIRSQPVAQIYV---HGDSLKAFLVGIVVPDPEvmPSWAQKR 615
Cdd:cd17650 363 RIELGEIESQLARHPAIDEAVVavrEDKGGEARLCAYVVAAAT--LNTAELR 412
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
259-594 |
3.18e-18 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 89.00 E-value: 3.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 259 HQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTH----GNV-----VADFsgflkvtesqwapTCADVHISYLPLAHMFerm 329
Cdd:PRK08043 356 RLAQVKQQPEDAALILFTSGSEGHPKGVVHSHksllANVeqiktIADF-------------TPNDRFMSALPLFHSF--- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 330 vqsvvychGGRVGFFQGdirLLSDDMKALCPTI--FPVVPRLLnrmYDK----IFSQANtplkrWLLEFAakrkqaevrs 403
Cdd:PRK08043 420 --------GLTVGLFTP---LLTGAEVFLYPSPlhYRIVPELV---YDRnctvLFGTST-----FLGNYA---------- 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 404 giiRNDSIWDelFFNkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAP 483
Cdd:PRK08043 471 ---RFANPYD--FAR---------LRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRI 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 484 LPCNHIKLVDVEELNywacKGeGEICVRGPNVFKGYLK--DPDRTK-------EALDSDGWLHTGDIGKWLPAGTLKIID 554
Cdd:PRK08043 537 LPGMDARLLSVPGIE----QG-GRLQLKGPNIMNGYLRveKPGVLEvptaenaRGEMERGWYDTGDIVRFDEQGFVQIQG 611
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 327412323 555 RKKHIFKLAqGEYVAPEKIENIYIRSQPVAQiyvHGDSLK 594
Cdd:PRK08043 612 RAKRFAKIA-GEMVSLEMVEQLALGVSPDKQ---HATAIK 647
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
70-588 |
3.36e-18 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 88.66 E-value: 3.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 70 ARRSVIGSGPQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRKpkqpyQWLSYQEVADRAEFLGSGLLQHNCKAcTDQf 149
Cdd:PRK06155 1 GEPLGAGLAARAVDPLPPSERTLPAMLARQAERYPDRPLLVFGG-----TRWTYAEAARAAAAAAHALAAAGVKR-GDR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 150 IGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlLLEHVERKETPGLKL--IILM 227
Cdd:PRK06155 74 VALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAA-----LLAALEAADPGDLPLpaVWLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 228 DPFEEALKERGQKCGVVIKSMQAVedcgqenhqAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHG-------NVVADfsgf 300
Cdd:PRK06155 149 DAPASVSVPAGWSTAPLPPLDAPA---------PAAAVQPGDTAAILYTSGTTGPSKGVCCPHAqfywwgrNSAED---- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 301 LKVTESqwaptcaDVHISYLPLAH------MFERMVQSVVYCHGGRV---GFFqgdirllsDDMKALCPTIFpvvpRLLN 371
Cdd:PRK06155 216 LEIGAD-------DVLYTTLPLFHtnalnaFFQALLAGATYVLEPRFsasGFW--------PAVRRHGATVT----YLLG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 372 RMYDKIFSQANTPLKRwllefaakrkqaevrsgiirndsiwdelffnkiqaslGGCVRMIVTGAAPASptVLGFLRAALG 451
Cdd:PRK06155 277 AMVSILLSQPARESDR-------------------------------------AHRVRVALGPGVPAA--LHAAFRERFG 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 452 CQVYEGYGQTECTAGCtFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWAckGE-GEICVRG--PNVF-KGYLKDPDRTK 527
Cdd:PRK06155 318 VDLLDGYGSTETNFVI-AVTHGSQRPGSMGRLAPGFEARVVDEHDQELPD--GEpGELLLRAdePFAFaTGYFGMPEKTV 394
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 327412323 528 EALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENIyIRSQP-VAQIYV 588
Cdd:PRK06155 395 EAW-RNLWFHTGDRVVRDADGWFRFVDRIKDAIR-RRGENISSFEVEQV-LLSHPaVAAAAV 453
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
121-609 |
3.71e-18 |
|
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: 88.10 E-value: 3.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVR--PGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 201 DKPQkavlllehvERKETPGLKLIILMDPFEEALKErgqkcgvviksmqavedcgqenhQAPVPPQPDDLSIVCFTSGTT 280
Cdd:cd12114 91 DGPD---------AQLDVAVFDVLILDLDALAAPAP-----------------------PPPVDVAPDDLAYVIFTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 281 GNPKGAMLTHG---NVVADfsgflkvTESQWAPTCADVHISYLPLAHMFermvqSV-----VYCHGGRVgffqgdirlls 352
Cdd:cd12114 139 GTPKGVMISHRaalNTILD-------INRRFAVGPDDRVLALSSLSFDL-----SVydifgALSAGATL----------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 353 ddmkalcptifpVVPRLlnrmydkifSQANTPlKRWllefaakrKQAEVRSGIirndSIWdelffNKIQASLGgcvrMIV 432
Cdd:cd12114 196 ------------VLPDE---------ARRRDP-AHW--------AELIERHGV----TLW-----NSVPALLE----MLL 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 433 TgAAPASPTVLGFLRAAL-------------------GCQVYEGYGQTECTAGCTF----TTPGDWTSGHVGAPLPCNHI 489
Cdd:cd12114 233 D-VLEAAQALLPSLRLVLlsgdwipldlparlralapDARLISLGGATEASIWSIYhpidEVPPDWRSIPYGRPLANQRY 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 490 KLVD--VEELNYWackGEGEICVRGPNVFKGYLKDPDRTKEAL--DSDG--WLHTGDIGKWLPAGTLKIIDRKKHIFKLa 563
Cdd:cd12114 312 RVLDprGRDCPDW---VPGELWIGGRGVALGYLGDPELTAARFvtHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKV- 387
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 327412323 564 QGEYVAPEKIENIYIRSQPVAQ--IYVHGDSLKAFLVGIVVPDPEVMP 609
Cdd:cd12114 388 RGYRIELGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPDNDGTP 435
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
262-605 |
5.74e-18 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 87.35 E-value: 5.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 262 PVPPQPDDLSIVC-FTSGTTGNPKGAMLTH--------GNVVAdfsgflkvtesqWAptcADVHISYLPLAHMFermvqs 332
Cdd:cd12118 126 WIPPADEWDPIALnYTSGTTGRPKGVVYHHrgaylnalANILE------------WE---MKQHPVYLWTLPMF------ 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 333 vvYCHGGrvGFFQGdirllsddMKALCPTIfpVVPRLLNrmYDKIFsqantplkRWLLE-----FAAkrkqAEVRSGIIR 407
Cdd:cd12118 185 --HCNGW--CFPWT--------VAAVGGTN--VCLRKVD--AKAIY--------DLIEKhkvthFCG----APTVLNMLA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 408 NDSIWDelffnkiQASLGGCVRMIVTGAAPaSPTVLgFLRAALGCQVYEGYGQTEcTAG----CTFTTPGDWTSGHVGAP 483
Cdd:cd12118 237 NAPPSD-------ARPLPHRVHVMTAGAPP-PAAVL-AKMEELGFDVTHVYGLTE-TYGpatvCAWKPEWDELPTEERAR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 484 LPC----NHIKL--VDVEELNY-----WACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKI 552
Cdd:cd12118 307 LKArqgvRYVGLeeVDVLDPETmkpvpRDGKTIGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEI 385
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 327412323 553 IDRKKHIFkLAQGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDP 605
Cdd:cd12118 386 KDRSKDII-ISGGENISSVEVEGV---------LYKHPAVLEAAVVA--RPDE 426
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
150-605 |
8.50e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 86.86 E-value: 8.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 150 IGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAVLLLEHVerketpglklIILMDP 229
Cdd:PRK06145 55 VALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDEEFDAIVALETP----------KIVIDA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 230 FEEALKERGQKCGVVIKSMQAVedcgqenhqapvppQPDDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTES 306
Cdd:PRK06145 125 AAQADSRRLAQGGLEIPPQAAV--------------APTDLVRLMYTSGTTDRPKGVMHSYGNLHwksIDHVIALGLTAS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 307 qwaptcaDVHISYLPLAHMFERMVQSV-VYCHGGRVGF---FQGDIRLLSDDMKALCPTIFpvVPRLLNRMYdkifsQAN 382
Cdd:PRK06145 191 -------ERLLVVGPLYHVGAFDLPGIaVLWVGGTLRIhreFDPEAVLAAIERHRLTCAWM--APVMLSRVL-----TVP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 383 TPLK------RWLLefAAKRKQAEVRsgiIRNdsiwdelffnkiqaslggcvrmivtgaapasptvlgFLRAALGCQVYE 456
Cdd:PRK06145 257 DRDRfdldslAWCI--GGGEKTPESR---IRD------------------------------------FTRVFTRARYID 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 457 GYGQTECTAGCTFTTPGDWTS--GHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDG 534
Cdd:PRK06145 296 AYGLTETCSGDTLMEAGREIEkiGSTGRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGD 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 327412323 535 WLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIEN-IYIRSQ--PVAQIYVHGDSLKAFLVGIVVPDP 605
Cdd:PRK06145 374 WFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERvIYELPEvaEAAVIGVHDDRWGERITAVVVLNP 446
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
121-606 |
1.27e-17 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 86.74 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLGSGLLQHNCKActdqfiG--VFAQ--NRPEWIIVELACYtySMVVVPLYdTLgPG----AIRYIINT 192
Cdd:COG1021 51 LSYAELDRRADRLAAGLLALGLRP------GdrVVVQlpNVAEFVIVFFALF--RAGAIPVF-AL-PAhrraEISHFAEQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 193 ADISTVIVDKpqkAVLLLEHVE-----RKETPGLKLIILMDPFEEALkergqkcgvvikSMQAVEDCGQENHQAPvpPQP 267
Cdd:COG1021 121 SEAVAYIIPD---RHRGFDYRAlarelQAEVPSLRHVLVVGDAGEFT------------SLDALLAAPADLSEPR--PDP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 268 DDlsiVCF---TSGTTGNPKGAMLTHgnvvADFsgFLKVTESqwAPTCA----DVHISYLPLAHMFErM----VQSVVYc 336
Cdd:COG1021 184 DD---VAFfqlSGGTTGLPKLIPRTH----DDY--LYSVRAS--AEICGldadTVYLAALPAAHNFP-LsspgVLGVLY- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 337 HGGRVgffqgdirLLSDDMKALcpTIFP-----------VVPRLLNRMydkifsqantplkrwlLEFAAKRKQAevrsgi 405
Cdd:COG1021 251 AGGTV--------VLAPDPSPD--TAFPlierervtvtaLVPPLALLW----------------LDAAERSRYD------ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 406 irndsiwdeLffnkiqASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctaG-CTFTTPGD--WTSGH-VG 481
Cdd:COG1021 299 ---------L------SSL----RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---GlVNYTRLDDpeEVILTtQG 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 482 APL-PCNHIKLVD-----VEElnywackGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIID 554
Cdd:COG1021 357 RPIsPDDEVRIVDedgnpVPP-------GEvGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEG 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 327412323 555 RKK-HIFKlaQGEYVAPEKIENiyirsqpvaQIYVHGDSLKAFLVGivVPDPE 606
Cdd:COG1021 430 RAKdQINR--GGEKIAAEEVEN---------LLLAHPAVHDAAVVA--MPDEY 469
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
121-605 |
3.79e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 85.46 E-value: 3.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PLN03102 40 FTWPQTYDRCCRLAASLISLNIT--KNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 201 DKP-----QKAVLLLEHVERKETPGLKLIILMD----PFE-----EALKERGQKCGVVIKSMQAVEDcgqenhqapvppQ 266
Cdd:PLN03102 118 DRSfeplaREVLHLLSSEDSNLNLPVIFIHEIDfpkrPSSeeldyECLIQRGEPTPSLVARMFRIQD------------E 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 267 PDDLSIvCFTSGTTGNPKGAMLTH-GNVVADFSGFLKvtesqWAPTCADVHISYLPLAH---------MFERMVQSVVYC 336
Cdd:PLN03102 186 HDPISL-NYTSGTTADPKGVVISHrGAYLSTLSAIIG-----WEMGTCPVYLWTLPMFHcngwtftwgTAARGGTSVCMR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 337 HGGRVGFFQgDIRLLSDDMKALCPTIFpvvprllnrmydkifsqantplkRWLLEfaAKRKQAEVRSGIIRndsiwdelf 416
Cdd:PLN03102 260 HVTAPEIYK-NIEMHNVTHMCCVPTVF-----------------------NILLK--GNSLDLSPRSGPVH--------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 417 fnkiqaslggcvrmIVTGAAPAsPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGD-WTSghvgapLPCN-------- 487
Cdd:PLN03102 305 --------------VLTGGSPP-PAALVKKVQRLGFQVMHAYGLTEATGPVLFCEWQDeWNR------LPENqqmelkar 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 488 ----HIKLVDVEELNYWAC-------KGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRK 556
Cdd:PLN03102 364 qgvsILGLADVDVKNKETQesvprdgKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRS 442
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 327412323 557 KHIFkLAQGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGIvvPDP 605
Cdd:PLN03102 443 KDII-ISGGENISSVEVENV---------LYKYPKVLETAVVAM--PHP 479
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
266-606 |
1.03e-16 |
|
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: 83.13 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 266 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkvTESQWAPTCADVHISYLPLAHMFermvqSV-----VYCHGGR 340
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA----TQRWFGFNEDDVWTLFHSYAFDF-----SVweiwgALLHGGR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 341 VGFFQGDIRLLSDDMkalcptifpvvPRLLNRMYDKIFSQanTPLkrwllefAAKRKQAEVRSGIIRNDSIwdelffnki 420
Cdd:cd17643 162 LVVVPYEVARSPEDF-----------ARLLRDEGVTVLNQ--TPS-------AFYQLVEAADRDGRDPLAL--------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 421 qaslggcvRMIVTGAAPASPTVLGFLRAALGC---QVYEGYGQTECTAGCTFT--TPGDW---TSGHVGAPLPCNHIKLV 492
Cdd:cd17643 213 --------RYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFRplDAADLpaaAASPIGRPLPGLRVYVL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 493 DvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKE-------ALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQG 565
Cdd:cd17643 285 D-ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI-RG 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 327412323 566 EYVAPEKIENIYIRSQPVAQIYV---HGDSLKAFLVGIVVPDPE 606
Cdd:cd17643 363 FRIELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVADDG 406
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
121-590 |
2.35e-16 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 82.56 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRP--GQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 201 dkpqkavllleHVERKETPGLKLIILMDPFEEALKERGQKC--GVVIKsmqavedcgqenhqaPVPPQPDDLSIVCFTSG 278
Cdd:cd05923 107 -----------AVDAQVMDAIFQSGVRVLALSDLVGLGEPEsaGPLIE---------------DPPREPEQPAFVFYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 279 TTGNPKGAMLTHgNVVADFSGFLkVTESQWAPTCADVHISYLPLAHMfermvqsvvychggrVGFFQgdirLLSDDMkAL 358
Cdd:cd05923 161 TTGLPKGAVIPQ-RAAESRVLFM-STQAGLRHGRHNVVLGLMPLYHV---------------IGFFA----VLVAAL-AL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 359 CPTIFPVvprllnrmydKIFSQANtplkrwllefAAKRKQAEVRSGIIRNDSIWDELFFNKIQASLG-GCVRMIVTGAAP 437
Cdd:cd05923 219 DGTYVVV----------EEFDPAD----------ALKLIEQERVTSLFATPTHLDALAAAAEFAGLKlSSLRHVTFAGAT 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 438 ASPTVLGFLRAALGCQVYEGYGQTECTagcTFTTPGDWTSGHVGAPLPCNHIKLVDV-EELNYWACKG-EGEICVR--GP 513
Cdd:cd05923 279 MPDAVLERVNQHLPGEKVNIYGTTEAM---NSLYMRDARTGTEMRPGFFSEVRIVRIgGSPDEALANGeEGELIVAaaAD 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 327412323 514 NVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYVHG 590
Cdd:cd05923 356 AAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIG 430
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
107-568 |
2.45e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 82.79 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 107 PCLGFRKPKQ-PYQWLSYQEVADRAEFLGSGLLqhNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVP--------- 176
Cdd:PRK12582 66 PWLAQREPGHgQWRKVTYGEAKRAVDALAQALL--DLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPvspayslms 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 177 --------LYDTLGPGAI-----------RYIINTADISTVIVDKPQKAVLLLEHVERKETPglkliilmdPFEEalker 237
Cdd:PRK12582 144 hdhaklkhLFDLVKPRVVfaqsgapfaraLAALDLLDVTVVHVTGPGEGIASIAFADLAATP---------PTAA----- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 238 gqkcgvVIKSMQAVedcgqenhqapvppQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVT-ESQWAPTcaDVH 316
Cdd:PRK12582 210 ------VAAAIAAI--------------TPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRpREPDPPP--PVS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 317 ISYLPLAHMFermvqsvvychGGRVGFfQGDIR----LLSDDMKALcPTIFPVVPRLLNRMYDKIFsqANTPLKRWLLEF 392
Cdd:PRK12582 268 LDWMPWNHTM-----------GGNANF-NGLLWgggtLYIDDGKPL-PGMFEETIRNLREISPTVY--GNVPAGYAMLAE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 393 AAKRKQAEVRSgiirndsiwdelFFNKIqaslggcvRMIVTGAAPASPTVLGFLRA----ALGCQV--YEGYGQTEcTAG 466
Cdd:PRK12582 333 AMEKDDALRRS------------FFKNL--------RLMAYGGATLSDDLYERMQAlavrTTGHRIpfYTGYGATE-TAP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 467 CTFTTpgDWTS---GHVGAPLPCNHIKLVDVEElNYwackgegEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGK 543
Cdd:PRK12582 392 TTTGT--HWDTervGLIGLPLPGVELKLAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAAR 461
|
490 500
....*....|....*....|....*....
gi 327412323 544 WL----PAGTLKIIDRKKHIFKLAQGEYV 568
Cdd:PRK12582 462 FVdpddPEKGLIFDGRVAEDFKLSTGTWV 490
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
267-583 |
4.91e-16 |
|
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: 81.38 E-value: 4.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESqwapTCADVHISYLPLAHmfermvqsvvychggRVGFFQG 346
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEW----KTKDRILSWMPLTH---------------DMGLIAF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 347 DIRLLSDDMKA-LCPT-IFPVVPRLLNRMYDK----IFSQANTPLKrWLLEFAAKRKQAEvrsgiirndsiWDElffnki 420
Cdd:cd05908 166 HLAPLIAGMNQyLMPTrLFIRRPILWLKKASEhkatIVSSPNFGYK-YFLKTLKPEKAND-----------WDL------ 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 421 qaslgGCVRMIVTGAAPASP----------TVLGFLRAAlgcqVYEGYGQTECTAGCTF--------------------- 469
Cdd:cd05908 228 -----SSIRMILNGAEPIDYelchefldhmSKYGLKRNA----ILPVYGLAEASVGASLpkaqspfktitlgrrhvthge 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 470 -------TTPGDWTSGHVGAPLPCNHIKLVDveELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDI 541
Cdd:cd05908 299 pepevdkKDSECLTFVEVGKPIDETDIRICD--EDNKILPDGYiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDL 376
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 327412323 542 GkWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPV 583
Cdd:cd05908 377 G-FIRNGRLVITGREKDII-FVNGQNVYPHDIERIAEELEGV 416
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
269-576 |
6.31e-16 |
|
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: 79.61 E-value: 6.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 269 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKvteSQWAPTCADVHISYLPLAHMFE--RMVQSVVYcHGGRVGFfqG 346
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQK---EGLNWVVGDVTYLPLPATHIGGlwWILTCLIH-GGLCVTG--G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 347 DIRLLSDDMKAL---CPTIFPVVPRLLNRMYDKIFSQANTPLKRWLLEFAAKRkqaevrsgIIRNDSIWDELFFNkiqas 423
Cdd:cd17635 76 ENTTYKSLFKILttnAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSR--------AIAADVRFIEATGL----- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 424 lggcvrmivtgaapasptvlgflraalgCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDVEELNYWAc 502
Cdd:cd17635 143 ----------------------------TNTAQVYGLSETGTALCLPTDDDSIEiNAVGRPYPGVDVYLAATDGIAGPS- 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 327412323 503 KGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENI 576
Cdd:cd17635 194 ASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERI 265
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
457-613 |
9.29e-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: 9.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 457 GYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVE--ELNywacKGE-GEICVRGPNVFKGYLKDPDRTKEALdSD 533
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDgrEVP----DGEvGEIVARGPTVMAGYWNRPEVNARRT-RG 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 534 GWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqgeyvapekIENIY-------IRSQP-VAQIYVhgdslkaflvgIVVPDp 605
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSG---------AENIYpaevercLRQHPaVADAAV-----------IGVPD- 275
|
....*...
gi 327412323 606 evmPSWAQ 613
Cdd:cd17636 276 ---PRWAQ 280
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
121-609 |
1.05e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 80.56 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLGSGLLQHNckACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQG--VRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 201 DKPQKAVLL---LEHVERKETPGLKLIILMDPFEEALKERGQKCGVviksmQAVEDCGQENHQAPVPPQ-PDDLSIVCFT 276
Cdd:PRK06164 114 WPGFKGIDFaaiLAAVPPDALPPLRAIAVVDDAADATPAPAPGARV-----QLFALPDPAPPAAAGERAaDPDAGALLFT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 277 -SGTTGNPK------GAMLTHGNVVADFSGFlkvtesqwAPtcADVHISYLPLahmfermvqSVVYCHGGRVGFFQGDIR 349
Cdd:PRK06164 189 tSGTTSGPKlvlhrqATLLRHARAIARAYGY--------DP--GAVLLAALPF---------CGVFGFSTLLGALAGGAP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 350 LLSDDMKALCPTIfpvvpRLL-----------NRMYDKIFSQANTPLkrwllEFAAKRkqaevRSGIirndsiwdelffn 418
Cdd:PRK06164 250 LVCEPVFDAARTA-----RALrrhrvthtfgnDEMLRRILDTAGERA-----DFPSAR-----LFGF------------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 419 kiqASLggcvrmivtgaAPASPTVLGFLRAAlGCQVYEGYGQTECTA---GCTFTTPgdWTSGHVGAPLPCN---HIKLV 492
Cdd:PRK06164 302 ---ASF-----------APALGELAALARAR-GVPLTGLYGSSEVQAlvaLQPATDP--VSVRIEGGGRPASpeaRVRAR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 493 DVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEK 572
Cdd:PRK06164 365 DPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNPAE 443
|
490 500 510
....*....|....*....|....*....|....*....
gi 327412323 573 IENIYIRSQPVAQIYVHGDSL--KAFLVGIVVPDPEVMP 609
Cdd:PRK06164 444 IEHALEALPGVAAAQVVGATRdgKTVPVAFVIPTDGASP 482
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
27-604 |
1.07e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 81.75 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 27 ATTLVSMGALAAILAYW--FTHRPKAlQPPCNL----LMQSEEVedsggaRRSVIGSGPqllTHYYDDARTMYQVFRRGL 100
Cdd:PRK12467 453 ATDLFEATTIERLATHWrnLLEAIVA-EPRRRLgelpLLDAEER------ARELVRWNA---PATEYAPDCVHQLIEAQA 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 101 SISGNGPCLGFRKpkqpyQWLSYQEVADRAEFLGSGLLQHNckACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDT 180
Cdd:PRK12467 523 RQHPERPALVFGE-----QVLSYAELNRQANRLAHVLIAAG--VGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPE 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 181 LGPGAIRYIINTADISTVIVDKPQKAVLLLehverkeTPGLKLIILMDPfeealkergqkcgvviksmqAVEDCGQENHQ 260
Cdd:PRK12467 596 YPQDRLAYMLDDSGVRLLLTQSHLLAQLPV-------PAGLRSLCLDEP--------------------ADLLCGYSGHN 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 261 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVvadfSGFLKVTESQWAPTCADVHISYLPLAHMFERMVQSVVYCHGGR 340
Cdd:PRK12467 649 PEVALDPDNLAYVIYTSGSTGQPKGVAISHGAL----ANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGAT 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 341 VgffqgdirLLSDDMKALCPTIFpvvprllnrmYDKIFSQANTPLKrwllefaakrkqaevrsgiiRNDSIWDELFFNKI 420
Cdd:PRK12467 725 L--------HLLPPDCARDAEAF----------AALMADQGVTVLK--------------------IVPSHLQALLQASR 766
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 421 QASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTT----PGDWTSGHVGAPLPCNHIKLVDvEE 496
Cdd:PRK12467 767 VALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYElsdeERDFGNVPIGQPLANLGLYILD-HY 845
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 497 LNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSD------GWLH-TGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVA 569
Cdd:PRK12467 846 LNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDpfgadgGRLYrTGDLARYRADGVIEYLGRMDHQVKI-RGFRIE 924
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 327412323 570 PEKIENIyIRSQP-------VAQIYVHGDSLKAFLVGIVVPD 604
Cdd:PRK12467 925 LGEIEAR-LLAQPgvreavvLAQPGDAGLQLVAYLVPAAVAD 965
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
121-617 |
1.25e-15 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 80.11 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLGSGLLQhnckactdqfIGVFAQNR--------PEWIIVELACYTYSMVVVPLYDTLGPGAIRYIInt 192
Cdd:cd05959 30 LTYAELEAEARRVAGALRA----------LGVKREERvllimldtVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 193 ADI-STVIVDKPQKAVLLLEHVERKEtPGLKLIILMDPFEEALKErgqkcgvviksMQAVEDCGQENHQ-APVPPQPDDL 270
Cdd:cd05959 98 EDSrARVVVVSGELAPVLAAALTKSE-HTLVVLIVSGGAGPEAGA-----------LLLAELVAAEAEQlKPAATHADDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 271 SIVCFTSGTTGNPKGAMLTHGN--VVADFSG--FLKVTESqwaptcaDVHISYLPLAH--------MFERMVQSVVYCHG 338
Cdd:cd05959 166 AFWLYSSGSTGRPKGVVHLHADiyWTAELYArnVLGIRED-------DVCFSAAKLFFayglgnslTFPLSVGATTVLMP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 339 GRVgffqgDIRLLSDDMKALCPTIFPVVPRLLNRMydkifsqantplkrwlleFAAKRKQAEVRSGIirndsiwdelffn 418
Cdd:cd05959 239 ERP-----TPAAVFKRIRRYRPTVFFGVPTLYAAM------------------LAAPNLPSRDLSSL------------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 419 kiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTF--TTPGDWTSGHVGAPLPCNHIKLVDvEE 496
Cdd:cd05959 283 ----------RLCVSAGEALPAEVGERWKARFGLDILDGIGSTE--MLHIFlsNRPGRVRYGTTGKPVPGYEVELRD-ED 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 497 LNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSdGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENI 576
Cdd:cd05959 350 GGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQG-EWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSPFEVESA 427
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 327412323 577 YIRSQPVAQIYVHG-------DSLKAFlvgiVVPDPEVMPSWAQKRGI 617
Cdd:cd05959 428 LVQHPAVLEAAVVGvededglTKPKAF----VVLRPGYEDSEALEEEL 471
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
150-607 |
3.59e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 78.95 E-value: 3.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 150 IGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAVL--LLEHVERKETPGLKLIILM 227
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLdgLDPGVRVINVDSPAWADEL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 228 DPFEEALKErgqkcgvviksmqavedcgqenhqaPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGflkvtesq 307
Cdd:PRK07867 137 AAHRDAEPP-------------------------FRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVA--SAG-------- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 308 waptcadvhisyLPLAHMFERMVQSVVYC-----HGGRVgffqgdirllsddMKALCPTIFpvvprllnrmydkifSQAN 382
Cdd:PRK07867 182 ------------VMLAQRFGLGPDDVCYVsmplfHSNAV-------------MAGWAVALA---------------AGAS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 383 TPLKRwllEFAAKRKQAEVRS-GIIrndsiwdelFFNKIqaslGGCVRMIVtgAAP-----------------ASPTVLG 444
Cdd:PRK07867 222 IALRR---KFSASGFLPDVRRyGAT---------YANYV----GKPLSYVL--ATPerpddadnplrivygneGAPGDIA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 445 FLRAALGCQVYEGYGQTEctAGCTFTTPGDWTSGHVGaPLPCNhIKLVDVE--------------ELNYWACKGEgEICV 510
Cdd:PRK07867 284 RFARRFGCVVVDGFGSTE--GGVAITRTPDTPPGALG-PLPPG-VAIVDPDtgtecppaedadgrLLNADEAIGE-LVNT 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 511 RGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYVHG 590
Cdd:PRK07867 359 AGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPIERILLRYPDATEVAVYA 436
|
490
....*....|....*..
gi 327412323 591 dslkaflvgivVPDPEV 607
Cdd:PRK07867 437 -----------VPDPVV 442
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
121-614 |
5.35e-15 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 78.29 E-value: 5.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLGSGLlQHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PRK05620 39 TTFAAIGARAAALAHAL-HDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 201 D---KPQKAVLLlehverKETPGLKLIILMDPFEEALKERGQKCGVVIKSMQAVEDCGQENHQAPVPPQpDDLSIVCFTS 277
Cdd:PRK05620 118 DprlAEQLGEIL------KECPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALLDGRSTVYDWPELDE-TTAAAICYST 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 278 GTTGNPKGAMLTHGNVVADfSGFLKVTESqWAPTCADVHISYLPLAHMFERMVQSVVYCHGgrvgffqgdirllsddmka 357
Cdd:PRK05620 191 GTTGAPKGVVYSHRSLYLQ-SLSLRTTDS-LAVTHGESFLCCVPIYHVLSWGVPLAAFMSG------------------- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 358 lCPTIFP----VVPRLLnrmydKIFSqanTPLKRwllefaakrkqaeVRSGIirnDSIWDELFFNKIQ-----ASLggcv 428
Cdd:PRK05620 250 -TPLVFPgpdlSAPTLA-----KIIA---TAMPR-------------VAHGV---PTLWIQLMVHYLKnpperMSL---- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 429 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGA---------PLPCNHiKLVDVEELNY 499
Cdd:PRK05620 301 QEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEARWayrvsqgrfPASLEY-RIVNDGQVME 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 500 WACKGEGEICVRGPNVFKGYLKDP----------------DRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlA 563
Cdd:PRK05620 380 STDRNEGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIR-S 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 327412323 564 QGEYVAPEKIENIYIRSQPVaqiyvhgdsLKAFLVGIvvPDPEvmpsWAQK 614
Cdd:PRK05620 459 GGEWIYSAQLENYIMAAPEV---------VECAVIGY--PDDK----WGER 494
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
158-598 |
8.48e-15 |
|
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: 77.51 E-value: 8.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 158 PEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlLLEHVER--KETPGLKLIILMDP------ 229
Cdd:cd05928 78 PEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDE-----LAPEVDSvaSECPSLKTKLLVSEksrdgw 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 230 --FEEALKERGQKcgvviksmqavEDCGQENHQAPvppqpddlSIVCFTSGTTGNPKGAMLTHGN----VVADFSGFLKV 303
Cdd:cd05928 153 lnFKELLNEASTE-----------HHCVETGSQEP--------MAIYFTSGTTGSPKMAEHSHSSlglgLKVNGRYWLDL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 304 TESQWAPTCADVHISYLPLAHMFERMVQ-SVVYCHggRVGFFQGDI---RLLSDDMKALC--PTIFpvvprllnRMydki 377
Cdd:cd05928 214 TASDIMWNTSDTGWIKSAWSSLFEPWIQgACVFVH--HLPRFDPLVilkTLSSYPITTFCgaPTVY--------RM---- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 378 fsqantplkrwllefaakrkqaevrsgIIRNDsiwdelfFNKIQ-ASLGGCVrmivTGAAPASPTVLGFLRAALGCQVYE 456
Cdd:cd05928 280 ---------------------------LVQQD-------LSSYKfPSLQHCV----TGGEPLNPEVLEKWKAQTGLDIYE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 457 GYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVR-GPN----VFKGYLKDPDRTKEALD 531
Cdd:cd05928 322 GYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIID-DNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIR 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 327412323 532 SDGWLhTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLV 598
Cdd:cd05928 401 GDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYRIGPFEVESALIEHPAVVESAVvsspdpiRGEVVKAFVV 472
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
152-605 |
9.90e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 77.39 E-value: 9.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 152 VFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV--DKPqkavlllEHVE--RKETPGLKLIILM 227
Cdd:PRK07470 62 VHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMIChaDFP-------EHAAavRAASPDLTHVVAI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 228 D--PFEEAlkergqkcgvviksmqaVEDCGQENHQAPVPPQP---DDLSIVCFTSGTTGNPKGAMLTHG-------NVVA 295
Cdd:PRK07470 135 GgaRAGLD-----------------YEALVARHLGARVANAAvdhDDPCWFFFTSGTTGRPKAAVLTHGqmafvitNHLA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 296 DFsgFLKVTEsqwaptcADVHISYLPLAHM--FERMVQSVvycHGGRVgffqgdIRLLSDDMKAlcptifPVVPRLLNRM 373
Cdd:PRK07470 198 DL--MPGTTE-------QDASLVVAPLSHGagIHQLCQVA---RGAAT------VLLPSERFDP------AEVWALVERH 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 374 YDKIFSQANTPLKrWLLEFAAkrkqaevrsgIIRNDsiwdelffnkiQASLggcvRMIVTGAAPASPTVLGFLRAALGCQ 453
Cdd:PRK07470 254 RVTNLFTVPTILK-MLVEHPA----------VDRYD-----------HSSL----RYVIYAGAPMYRADQKRALAKLGKV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 454 VYEGYGQTECTAGCTFTTP-----GDWTSGHVGaplPCNH--------IKLVDVEELNywacKGE-GEICVRGPNVFKGY 519
Cdd:PRK07470 308 LVQYFGLGEVTGNITVLPPalhdaEDGPDARIG---TCGFertgmevqIQDDEGRELP----PGEtGEICVIGPAVFAGY 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 520 LKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENiyirsqpvaQIYVHGDSLKAFLVG 599
Cdd:PRK07470 381 YNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPREIEE---------KLLTHPAVSEVAVLG 449
|
....*.
gi 327412323 600 ivVPDP 605
Cdd:PRK07470 450 --VPDP 453
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
267-578 |
1.01e-14 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 77.55 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWAPTCADVHISYLPLAHMFermvqsvvychggrvGFFqg 346
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKF----FSPKEDDVMMSFLPPFHAY---------------GFN-- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 347 dirllsddmkalCPTIFPVVPRLlnrmyDKIFsqANTPLK-RWLLEFAAKRKQAEVRSGIIRNDSIwdeLFFNKIQASLG 425
Cdd:PRK06334 241 ------------SCTLFPLLSGV-----PVVF--AYNPLYpKKIVEMIDEAKVTFLGSTPVFFDYI---LKTAKKQESCL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 426 GCVRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFTT---PGDwtSGHVGAPLPCNHIKLVDvEELNYWA 501
Cdd:PRK06334 299 PSLRFVVIGGDAFKDSLYqEALKTFPHIQLRQGYGTTECSPVITINTvnsPKH--ESCVGMPIRGMDVLIVS-EETKVPV 375
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 327412323 502 CKGE-GEICVRGPNVFKGYL-KDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYI 578
Cdd:PRK06334 376 SSGEtGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSLEALESILM 453
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
276-606 |
1.72e-14 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 76.60 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 276 TSGTTGNPKGAMLTHgnvvADFSGFLKVTesqwAPTCA----DVHISYLPLAHMFERM---VQSVVYChGGRVgffqgdi 348
Cdd:cd05920 147 SGGTTGTPKLIPRTH----NDYAYNVRAS----AEVCGldqdTVYLAVLPAAHNFPLAcpgVLGTLLA-GGRV------- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 349 rLLSDDmkALCPTIFPVVPRllnrmyDKIFSQANTP--LKRWLlEFAAKRKQAEvrsgiirndsiwdelffnkiqASLgg 426
Cdd:cd05920 211 -VLAPD--PSPDAAFPLIER------EGVTVTALVPalVSLWL-DAAASRRADL---------------------SSL-- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 427 cvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHVGAPL-PCNHIKLVDvEELNYWACKG 504
Cdd:cd05920 258 --RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTrLDDPDEVIIHTQGRPMsPDDEIRVVD-EEGNPVPPGE 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 505 EGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENiyirsqpva 584
Cdd:cd05920 335 EGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVEN--------- 404
|
330 340
....*....|....*....|..
gi 327412323 585 QIYVHGDSLKAFLVGivVPDPE 606
Cdd:cd05920 405 LLLRHPAVHDAAVVA--MPDEL 424
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
263-606 |
6.23e-14 |
|
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: 74.62 E-value: 6.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 263 VPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF---LKVTES----QWAPTCADVHIS--YLPLAHMfERMVqsv 333
Cdd:cd17646 133 VPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMqdeYPLGPGdrvlQKTPLSFDVSVWelFWPLVAG-ARLV--- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 334 VYCHGGRvgffqGDIRLLSDDMKALCPTIFPVVPRLLnrmydkifsqantplkrwllefaakrkqaevrsgiirndsiwd 413
Cdd:cd17646 209 VARPGGH-----RDPAYLAALIREHGVTTCHFVPSML------------------------------------------- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 414 ELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHV--GAPLPCNHIK 490
Cdd:cd17646 241 RVFLAEPAAGSCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVThWPVRGPAETPSVpiGRPVPNTRLY 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 491 LVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH------TGDIGKWLPAGTLKIIDRKKHIFKLaQ 564
Cdd:cd17646 321 VLD-DALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKI-R 398
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 327412323 565 GEYVAPEKIENIyIRSQP-VAQIYV---HGDSLKAFLVGIVVPDPE 606
Cdd:cd17646 399 GFRVEPGEIEAA-LAAHPaVTHAVVvarAAPAGAARLVGYVVPAAG 443
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
420-588 |
7.67e-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: 7.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 420 IQASLGGC---VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTfTTPGD-WTSGHVGAPLPCNHIKLVDVE 495
Cdd:cd05974 191 IQQDLASFdvkLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVG-NSPGQpVKAGSMGRPLPGYRVALLDPD 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 496 ElnywACKGEGEICV-----RGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAP 570
Cdd:cd05974 270 G----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SSDYRISP 343
|
170
....*....|....*...
gi 327412323 571 EKIENIYIRSQPVAQIYV 588
Cdd:cd05974 344 FELESVLIEHPAVAEAAV 361
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
264-598 |
7.94e-14 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 74.88 E-value: 7.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 264 PPQPDDLSIVC-FTSGTTGNPKGAMLTH-GNVVADFSGFLKvtesqWAPTCADVHISYLPLAHmfermvqsvvyCHGGrv 341
Cdd:PLN02479 190 PPADEWQSIALgYTSGTTASPKGVVLHHrGAYLMALSNALI-----WGMNEGAVYLWTLPMFH-----------CNGW-- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 342 gffqgdirLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTplkrwllEFAAkrkqAEVRSGIIRNDSIWDELFfnkiq 421
Cdd:PLN02479 252 --------CFTWTLAALCGTNICLRQVTAKAIYSAIANYGVT-------HFCA----APVVLNTIVNAPKSETIL----- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 422 aSLGGCVRMIVTGAAPaSPTVLgFLRAALGCQVYEGYGQTEcTAG----CTFTTPGDWTSGHVGAPLPCNH--------- 488
Cdd:PLN02479 308 -PLPRVVHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSE-TYGpstvCAWKPEWDSLPPEEQARLNARQgvryigleg 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 489 IKLVDVEELNYWACKGE--GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGE 566
Cdd:PLN02479 384 LDVVDTKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGGE 461
|
330 340 350
....*....|....*....|....*....|..
gi 327412323 567 YVAPEKIENIyirsqpvaqIYVHGDSLKAFLV 598
Cdd:PLN02479 462 NISSLEVENV---------VYTHPAVLEASVV 484
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
504-559 |
5.36e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 71.90 E-value: 5.36e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 327412323 504 GE--GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHI 559
Cdd:PRK08162 385 GEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDI 441
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
119-599 |
1.07e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 71.91 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 119 QWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLyDTLGPGA-IRYIINTADIST 197
Cdd:PRK12316 2027 QHLSYAELDSRANRLAHRLRARGVGP--EVRVAIAAERSFELVVALLAVLKAGGAYVPL-DPNYPAErLAYMLEDSGAAL 2103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 198 VIVDKPQKAVLLLehverkeTPGLKLIILMDPfeEALKERGQKcgvviksmqavedcgqenhqAPVPP-QPDDLSIVCFT 276
Cdd:PRK12316 2104 LLTQRHLLERLPL-------PAGVARLPLDRD--AEWADYPDT--------------------APAVQlAGENLAYVIYT 2154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 277 SGTTGNPKGAMLTHGNVVAdfsgFLKVTESQWAPTCADVHISYLPLAhmFERMVQSVVY--CHGGRVgffqgdirLLSDD 354
Cdd:PRK12316 2155 SGSTGLPKGVAVSHGALVA----HCQAAGERYELSPADCELQFMSFS--FDGAHEQWFHplLNGARV--------LIRDD 2220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 355 MKalcptifpvvpRLLNRMYDKIFSQANTplkrwLLEFAAKRKQAEVRsgiirndsiwdelffnkiQASLGGC---VRMI 431
Cdd:PRK12316 2221 EL-----------WDPEQLYDEMERHGVT-----ILDFPPVYLQQLAE------------------HAERDGRppaVRVY 2266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 432 VTGAAPASPTVLGFLRAALGCQ-VYEGYGQTEctagcTFTTPGDWTSGH----------VGAPLPCNHIKLVDvEELNYW 500
Cdd:PRK12316 2267 CFGGEAVPAASLRLAWEALRPVyLFNGYGPTE-----AVVTPLLWKCRPqdpcgaayvpIGRALGNRRAYILD-ADLNLL 2340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 501 ACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH-------TGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKI 573
Cdd:PRK12316 2341 APGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKI-RGFRIELGEI 2419
|
490 500 510
....*....|....*....|....*....|...
gi 327412323 574 ENiYIRSQP-------VAQIYVHGDSLKAFLVG 599
Cdd:PRK12316 2420 EA-RLQAHPavreavvVAQDGASGKQLVAYVVP 2451
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
265-603 |
1.20e-12 |
|
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: 70.57 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 265 PQPDDLSIVCFTSGTTGNPKGAMLTHGNvvadFSGFLKVTESQWAPTCADVHISYLPLAHMFERM--VQSVVychggrvg 342
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGT----FAAQIDALRQLYGIRPGEVDLATFPLFALFGPAlgLTSVI-------- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 343 ffqgdirllsDDMKALCPTifPVVPRllnrmydKIFSqantPLKRWllefaakrkqaEVrSGIIRNDSIWDEL--FFNKI 420
Cdd:cd05910 150 ----------PDMDPTRPA--RADPQ-------KLVG----AIRQY-----------GV-SIVFGSPALLERVarYCAQH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 421 QASLGGcVRMIVTGAAPASPTVLGFLRAAL--GCQVYEGYGQTECTAGCT------FTTPGDWTSGH----VGAPLPCNH 488
Cdd:cd05910 195 GITLPS-LRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrelLATTTAATSGGagtcVGRPIPGVR 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 489 IKLV--DVEELNYWACKGE------GEICVRGPNVFKGYLKDPDRTKEALDSDG----WLHTGDIGKWLPAGTLKIIDRK 556
Cdd:cd05910 274 VRIIeiDDEPIAEWDDTLElprgeiGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRK 353
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 327412323 557 KHIFKLAQGEYVapekieniyirSQPVAQIY-VHGDSLKAFLVGIVVP 603
Cdd:cd05910 354 AHRVITTGGTLY-----------TEPVERVFnTHPGVRRSALVGVGKP 390
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
268-610 |
1.44e-12 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 70.20 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 268 DDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF----LKVTESqwaptcaDVHISYLPLAHMFERMVQSVVYCHGGR--V 341
Cdd:cd05958 97 DDICILAFTSGTTGAPKATMHFHRDPLASADRYavnvLRLRED-------DRFVGSPPLAFTFGLGGVLLFPFGVGAsgV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 342 GFFQGDIRLLSDDMKALCPTIFPVVPRllnrMYdkifsqantplkRWLLEFAAKRKQaevrsgiirndsiwdelffnkiq 421
Cdd:cd05958 170 LLEEATPDLLLSAIARYKPTVLFTAPT----AY------------RAMLAHPDAAGP----------------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 422 asLGGCVRMIVTgAAPASPTVLGFL-RAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDveELNYW 500
Cdd:cd05958 211 --DLSSLRKCVS-AGEALPAALHRAwKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD--DEGNP 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 501 ACKGE-GEICVRGPNVFKgYLKDPDRTKEAldSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIR 579
Cdd:cd05958 286 VPDGTiGRLAVRGPTGCR-YLADKRQRTYV--QGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQ 361
|
330 340 350
....*....|....*....|....*....|....
gi 327412323 580 SQPVAQIYVHGDSLKAFLV---GIVVPDPEVMPS 610
Cdd:cd05958 362 HPAVAECAVVGHPDESRGVvvkAFVVLRPGVIPG 395
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
86-639 |
3.14e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 70.58 E-value: 3.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 86 YDDARTMYQVFRRGLSISGNGPCLGFRKpkqpyQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVEL 165
Cdd:PRK12467 1570 YPLARLVHQLIEDQAAATPEAVALVFGE-----QELTYGELNRRANRLAHRLIALGVGP--EVLVGIAVERSLEMVVGLL 1642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 166 ACYTYSMVVVPLYDTLGPGAIRYIINTADIStvivdkpqkavLLLEHveRKETPGLKLIilmdpfeealkeRGQKCGVVI 245
Cdd:PRK12467 1643 AILKAGGAYVPLDPEYPRERLAYMIEDSGIE-----------LLLTQ--SHLQARLPLP------------DGLRSLVLD 1697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 246 KSMQAVEDCGQENHQapVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFsgflKVTESQWAPTCADVHISYLPLAhm 325
Cdd:PRK12467 1698 QEDDWLEGYSDSNPA--VNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRL----CATQEAYQLSAADVVLQFTSFA-- 1769
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 326 FERMVQSVVY--CHGGRVgffqgdirLLSDDMKALCPtifpvvprllNRMYDKIFSQANTplkrwLLEFAAKRKQAevrs 403
Cdd:PRK12467 1770 FDVSVWELFWplINGARL--------VIAPPGAHRDP----------EQLIQLIERQQVT-----TLHFVPSMLQQ---- 1822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 404 giirndsiwdelfFNKIQASLGGC--VRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAG-----CTFTTPGDW 475
Cdd:PRK12467 1823 -------------LLQMDEQVEHPlsLRRVVCGGEALEVEALRPWLERLPdTGLFNLYGPTETAVDvthwtCRRKDLEGR 1889
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 476 TSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL------DSDGWLH-TGDIGKWLPAG 548
Cdd:PRK12467 1890 DSVPIGQPIANLSTYILD-ASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgTVGSRLYrTGDLARYRADG 1968
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 549 TLKIIDRKKHIFKLaQGEYVAPEKIENiYIRSQP----VAQIYVHGDSLKAfLVGIVVPDPEVMPSWAQKRgieGTYADl 624
Cdd:PRK12467 1969 VIEYLGRIDHQVKI-RGFRIELGEIEA-RLREQGgvreAVVIAQDGANGKQ-LVAYVVPTDPGLVDDDEAQ---VALRA- 2041
|
570
....*....|....*.
gi 327412323 625 cTNKDLKKAILED-MV 639
Cdd:PRK12467 2042 -ILKNHLKASLPEyMV 2056
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-598 |
4.99e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 69.99 E-value: 4.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 3 TQEILRILRLPELGDLGQFfrSLSATTLVSMGALAAILAYWFTHRPKAL-----QPPCNLLMQS--------EEVEDSGG 69
Cdd:PRK12316 2959 QLPGLHIESFAWDGAATQF--DLALDTWESAEGLGASLTYATDLFDARTverlaRHWQNLLRGMvenpqrsvDELAMLDA 3036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 70 ARRSVIGSGPQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRKpkqpyQWLSYQEVADRAEFLGSGLLQHNCKActDQF 149
Cdd:PRK12316 3037 EERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVALAFGE-----QRLSYAELNRRANRLAHRLIERGVGP--DVL 3109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 150 IGVFAQNRPEWIIVELACYTYSMVVVPLyDTLGPGAiryiintaDISTVIVDKPQKAVLLLEHVERKETPGLKlIILMDP 229
Cdd:PRK12316 3110 VGVAVERSLEMVVGLLAILKAGGAYVPL-DPEYPEE--------RLAYMLEDSGAQLLLSQSHLRLPLAQGVQ-VLDLDR 3179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 230 FEEALKErgqkcgvviksmqavedcgqenHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNvvadFSGFLKVTESQWA 309
Cdd:PRK12316 3180 GDENYAE----------------------ANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSA----LSNHLCWMQQAYG 3233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 310 PTCADVHISYLPLAHMFERMVQSVVYCHGGRVgfFQGDIRLLSDdmkalcptifpvvPRLLNRMYDKifSQANTPLKRWl 389
Cdd:PRK12316 3234 LGVGDRVLQFTTFSFDVFVEELFWPLMSGARV--VLAGPEDWRD-------------PALLVELINS--EGVDVLHAYP- 3295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 390 lefaakrkqaevrsgiirndSIWDELFFNKIQASLGGCVRMIVTGAAPASPtvlGFLRAALGCQVYEGYGQTECTAGCTF 469
Cdd:PRK12316 3296 --------------------SMLQAFLEEEDAHRCTSLKRIVCGGEALPAD---LQQQVFAGLPLYNLYGPTEATITVTH 3352
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 470 TTPGDWTSGH--VGAPLPCNHIKLVDVeELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGW------LHTGDI 541
Cdd:PRK12316 3353 WQCVEEGKDAvpIGRPIANRACYILDG-SLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDL 3431
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 542 GKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPV---AQIYVHGDSLKAFLV 598
Cdd:PRK12316 3432 ARYRADGVIEYIGRVDHQVKI-RGFRIELGEIEARLLEHPWVreaVVLAVDGRQLVAYVV 3490
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
261-567 |
5.68e-12 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 68.77 E-value: 5.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 261 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGfLKvteSQWAPTCADVHISYLPLAHMFERM--VQSVVychg 338
Cdd:PRK09274 167 PMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEA-LR---EDYGIEPGEIDLPTFPLFALFGPAlgMTSVI---- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 339 grvgffqgdirllsDDMKALCP-TIFPvvprllnrmyDKIFSQ----------ANTPLKRWLLEFAAKRKQaevrsgiir 407
Cdd:PRK09274 239 --------------PDMDPTRPaTVDP----------AKLFAAierygvtnlfGSPALLERLGRYGEANGI--------- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 408 ndsiwdelffnkiqaSLGGCVRMIVTGAaPASPTVLGFLRAAL--GCQVYEGYGQTECTAGCT-------FTTPGDWTSG 478
Cdd:PRK09274 286 ---------------KLPSLRRVISAGA-PVPIAVIERFRAMLppDAEILTPYGATEALPISSiesreilFATRAATDNG 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 479 H---VGAPLPCNHIKLVDV--EELNYWA-----CKGE-GEICVRGPNVFKGYLKDPDRTKEA--LDSDG--WLHTGDIGk 543
Cdd:PRK09274 350 AgicVGRPVDGVEVRIIAIsdAPIPEWDdalrlATGEiGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLG- 428
|
330 340
....*....|....*....|....*
gi 327412323 544 WL-PAGTLKIIDRKKHIFKLAQGEY 567
Cdd:PRK09274 429 YLdAQGRLWFCGRKAHRVETAGGTL 453
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
258-588 |
6.13e-12 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 68.36 E-value: 6.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 258 NHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESqwapTCADVHISYLPLAHmfermV--QSVVY 335
Cdd:PRK09029 125 EGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPF----TAQDSWLLSLPLFH-----VsgQGIVW 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 336 ---CHGGRVGFfqGDIRLLSDDMK-----ALCPTifpVVPRLLNRmydkifSQANTPLKRWLLefaakrkqaevrsgiir 407
Cdd:PRK09029 196 rwlYAGATLVV--RDKQPLEQALAgcthaSLVPT---QLWRLLDN------RSEPLSLKAVLL----------------- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 408 ndsiwdelffnkiqaslGGCvrMIvtgaapasPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTSGhVGAPLPCN 487
Cdd:PRK09029 248 -----------------GGA--AI--------PVELTEQAEQQGIRCWCGYGLTE-MASTVCAKRADGLAG-VGSPLPGR 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 488 HIKLVDveelnywackgeGEICVRGPNVFKGYLKDpDRTKEALDSDGWLHTGDIGKWLpAGTLKIIDRKKHIFkLAQGEY 567
Cdd:PRK09029 299 EVKLVD------------GEIWLRGASLALGYWRQ-GQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEG 363
|
330 340
....*....|....*....|.
gi 327412323 568 VAPEKIENIYIRSQPVAQIYV 588
Cdd:PRK09029 364 IQPEEIERVINQHPLVQQVFV 384
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
121-606 |
6.96e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 68.39 E-value: 6.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLRE--GDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 201 DKPQKAVL--LLEHVERketpGLKLIILMD-------PFEEALKErgqkcgvviksmqavedcgqenhQAPVPPqPDDL- 270
Cdd:PRK08276 90 SAALADTAaeLAAELPA----GVPLLLVVAgpvpgfrSYEEALAA-----------------------QPDTPI-ADETa 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 271 -SIVCFTSGTTGNPKGAM--LTHGNVVADFSGFLKVTeSQWAPTCAD-VHISYLPLAH----MFERMVQSvvycHGGRVG 342
Cdd:PRK08276 142 gADMLYSSGTTGRPKGIKrpLPGLDPDEAPGMMLALL-GFGMYGGPDsVYLSPAPLYHtaplRFGMSALA----LGGTVV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 343 FFQgdiRLLSDDMKALCP----TIFPVVPRLLNRMydkifsqantpLKrwLLEfaakrkqaEVRSgiiRNDSiwdelffn 418
Cdd:PRK08276 217 VME---KFDAEEALALIEryrvTHSQLVPTMFVRM-----------LK--LPE--------EVRA---RYDV-------- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 419 kiqASLggcvRMIVTGAAPASPTVLgflRAAL---GCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCNhIKLVD 493
Cdd:PRK08276 262 ---SSL----RVAIHAAAPCPVEVK---RAMIdwwGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGE-VRILD 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 494 vEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkWLPA-GTLKIIDRKKHIFkLAQGEYVAPEK 572
Cdd:PRK08276 330 -EDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVG-YLDEdGYLYLTDRKSDMI-ISGGVNIYPQE 406
|
490 500 510
....*....|....*....|....*....|....
gi 327412323 573 IENIYIRSQPVAQIYVHGdslkaflvgivVPDPE 606
Cdd:PRK08276 407 IENLLVTHPKVADVAVFG-----------VPDEE 429
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
266-615 |
9.36e-12 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 67.85 E-value: 9.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 266 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKV---TES----QWAPTCADVHISYLplahmfermvqSVVYCHG 338
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEygiTSSdrvlQFASIAFDVAAEEI-----------YVTLLSG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 339 GRVGFFQGDIRLLSDDMKALCP----TIFPVVPrllnrmydkifsqantplkrwllefaakrkqaevrsgiirndSIWDE 414
Cdd:cd17644 173 ATLVLRPEEMRSSLEDFVQYIQqwqlTVLSLPP------------------------------------------AYWHL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 415 LFFNKIQASLGG--CVRMIVTGAAPASPTVLGFLRAALG--CQVYEGYGQTECTAGCTFTTPGDWTSGH-----VGAPLP 485
Cdd:cd17644 211 LVLELLLSTIDLpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 486 CNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH--------TGDIGKWLPAGTLKIIDRKK 557
Cdd:cd17644 291 NTQVYILD-ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRID 369
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 327412323 558 HIFKLaQGEYVAPEKIENIYIRSQPVAQ--IYVHGDSL-KAFLVGIVVPDPEVMPSWAQKR 615
Cdd:cd17644 370 NQVKI-RGFRIELGEIEAVLSQHNDVKTavVIVREDQPgNKRLVAYIVPHYEESPSTVELR 429
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
435-606 |
1.53e-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: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 435 AAPASPTVLGFLRAALGCQVYEGYGQTECTaGCTFTTPGDWTS--GHVGAPLPcNHIKLVDvEELNYWACKGEGEICVRG 512
Cdd:cd05929 253 AAPCPPWVKEQWIDWGGPIIWEYYGGTEGQ-GLTIINGEEWLThpGSVGRAVL-GKVHILD-EDGNEVPPGEIGEVYFAN 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 513 PNVFKgYLKDPDRTKEALDSDGWLHTGDIGkWLPA-GTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRsqpvaqiyvHGD 591
Cdd:cd05929 330 GPGFE-YTNDPEKTAAARNEGGWSTLGDVG-YLDEdGYLYLTDRRSDMI-ISGGVNIYPQEIENALIA---------HPK 397
|
170
....*....|....*
gi 327412323 592 SLKAFLVGivVPDPE 606
Cdd:cd05929 398 VLDAAVVG--VPDEE 410
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
121-605 |
3.74e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 66.06 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGP--GDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 201 DK---PQKAVLLlehverKETPGLKLIILMD------------PFEEALKErgqkcgvviksmqavedcgQENHQAPVPP 265
Cdd:PRK07798 107 ERefaPRVAEVL------PRLPKLRTLVVVEdgsgndllpgavDYEDALAA-------------------GSPERDFGER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 266 QPDDLSIVCfTSGTTGNPKGAMLTHGNV-VADFSGFLKVT-------ESQWAPTCADVHISYLPLAHMFERMVQSVVYch 337
Cdd:PRK07798 162 SPDDLYLLY-TGGTTGMPKGVMWRQEDIfRVLLGGRDFATgepiedeEELAKRAAAGPGMRRFPAPPLMHGAGQWAAF-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 338 ggrVGFFQGDIRLLSDDMKalcptifpvvprllnrmydkiFSQANtplkrwLLEFAAKRKqaeVRSGIIRNDS----IWD 413
Cdd:PRK07798 239 ---AALFSGQTVVLLPDVR---------------------FDADE------VWRTIEREK---VNVITIVGDAmarpLLD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 414 ELffnkiqASLGG----CVRMIVTGAAPASPTV-LGFLRAALGCQVYEGYGQTECTAGCTFTTPGDwtSGHVGAPL--PC 486
Cdd:PRK07798 286 AL------EARGPydlsSLFAIASGGALFSPSVkEALLELLPNVVLTDSIGSSETGFGGSGTVAKG--AVHTGGPRftIG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 487 NHIKLVDvEELNYWAcKGEGEICV--RGPNVFKGYLKDPDRTKEALDS-DG--WLHTGDIGKWLPAGTLKIIDRKKHIFK 561
Cdd:PRK07798 358 PRTVVLD-EDGNPVE-PGSGEIGWiaRRGHIPLGYYKDPEKTAETFPTiDGvrYAIPGDRARVEADGTITLLGRGSVCIN 435
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 327412323 562 LAqGEYVAPEKIENIyIRSQPvaqiyvhgDSLKAFLVGivVPDP 605
Cdd:PRK07798 436 TG-GEKVFPEEVEEA-LKAHP--------DVADALVVG--VPDE 467
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
266-615 |
4.78e-11 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 65.35 E-value: 4.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 266 QPDDLSIVCFTSGTTGNPKGAMLTH---GNVVADFSGFLKVTE----SQWAPTCADVHISYLPLAhmfermvqsvvYCHG 338
Cdd:cd17652 91 TPDNLAYVIYTSGSTGRPKGVVVTHrglANLAAAQIAAFDVGPgsrvLQFASPSFDASVWELLMA-----------LLAG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 339 GRvgffqgdirllsddmkaLCptifpVVPRLLnrmydkifSQANTPLKRWLlefaakrkQAEVRSGIIRNDSIWDELffn 418
Cdd:cd17652 160 AT-----------------LV-----LAPAEE--------LLPGEPLADLL--------REHRITHVTLPPAALAAL--- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 419 kIQASLGGCVRMIVTGAAPASPTVLgflRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLVDvEEL 497
Cdd:cd17652 199 -PPDDLPDLRTLVVAGEACPAELVD---RWAPGRRMINAYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYVLD-ARL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 498 NYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSD------GWLH-TGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAP 570
Cdd:cd17652 274 RPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKI-RGFRIEL 352
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 327412323 571 EKIENIYIRSQPVAQ--IYVHGDSL-KAFLVGIVVPDPEVMPSWAQKR 615
Cdd:cd17652 353 GEVEAALTEHPGVAEavVVVRDDRPgDKRLVAYVVPAPGAAPTAAELR 400
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
429-610 |
6.34e-11 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 65.49 E-value: 6.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 429 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCNHIKLVDvEELNYWACKGEG 506
Cdd:PRK12406 274 RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE-SGAVTFATSEDALShpGTVGKAAPGAELRFVD-EDGRPLPQGEIG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 507 EICVRGPNV--FKgYLKDPDRTKEaLDSDGWLHTGDIGkWLPA-GTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPV 583
Cdd:PRK12406 352 EIYSRIAGNpdFT-YHNKPEKRAE-IDRGGFITSGDVG-YLDAdGYLFLCDRKRDMV-ISGGVNIYPAEIEAVLHAVPGV 427
|
170 180 190
....*....|....*....|....*....|
gi 327412323 584 AQIYVHGDSLKAF---LVGIVVPDPEVMPS 610
Cdd:PRK12406 428 HDCAVFGIPDAEFgeaLMAVVEPQPGATLD 457
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
266-614 |
1.14e-10 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 64.11 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 266 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVTESQWAPTCADVHISYLPLAhmFERMVQSVV--YCHGGRVGF 343
Cdd:cd17645 102 NPDDLAYVIYTSGSTGLPKGVMIEHHNLV----NLCEWHRPYFGVTPADKSLVYASFS--FDASAWEIFphLTAGAALHV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 344 FQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTPLkRWLLEFAAKRKQAEVRsgiirndsiwdelffnkiqas 423
Cdd:cd17645 176 VPSERRLDLDALNDYFNQEGITISFLPTGAAEQFMQLDNQSL-RVLLTGGDKLKKIERK--------------------- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 424 lggcvrmivtgaapasptvlgflraalGCQVYEGYGQTECTAGCT-FTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWAC 502
Cdd:cd17645 234 ---------------------------GYKLVNNYGPTENTVVATsFEIDKPYANIPIGKPIDNTRVYILD-EALQLQPI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 503 KGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENI 576
Cdd:cd17645 286 GVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIEPF 364
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 327412323 577 ---YIRSQPVAQIYVHGDSLKAFLVGIVVP----DPEVMPSWAQK 614
Cdd:cd17645 365 lmnHPLIELAAVLAKEDADGRKYLVAYVTApeeiPHEELREWLKN 409
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
271-584 |
1.58e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 63.96 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 271 SIVCFTSGTTGNPKGAMLTH-GNVVADFSGFLkvtesqwaP--TCADVHISYLPLAHMFERMVQSVVYChGGRVGffqgd 347
Cdd:PRK07008 179 SSLCYTSGTTGNPKGALYSHrSTVLHAYGAAL--------PdaMGLSARDAVLPVVPMFHVNAWGLPYS-APLTG----- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 348 irllsddmkalCPTIFPVvPRLLNR-MYDKIFSQANTplkrwlleFAAkrkqaevrsGIirnDSIWDELFFNKIQASLG- 425
Cdd:PRK07008 245 -----------AKLVLPG-PDLDGKsLYELIEAERVT--------FSA---------GV---PTVWLGLLNHMREAGLRf 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 426 GCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPgdwTSGHVGAPLPCNH--------------IKL 491
Cdd:PRK07008 293 STLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLCKL---KWKHSQLPLDEQRkllekqgrviygvdMKI 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 492 VDVE--ELNyWACKGEGEICVRGPNVFKGYLKdpdRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVA 569
Cdd:PRK07008 370 VGDDgrELP-WDGKAFGDLQVRGPWVIDRYFR---GDASPLV-DGWFPTGDVATIDADGFMQITDRSKDVIK-SGGEWIS 443
|
330
....*....|....*
gi 327412323 570 PEKIENIYIRSQPVA 584
Cdd:PRK07008 444 SIDIENVAVAHPAVA 458
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
255-619 |
2.78e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 64.21 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 255 GQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgFLKVTESQWAPTCADVHISYLPLAhmFERMVQSV- 333
Cdd:PRK12316 4681 GFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVN----HLHATGERYELTPDDRVLQFMSFS--FDGSHEGLy 4754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 334 -VYCHGGRVgffqgdirLLSDDMKALcPTifpvvpRLLNRMYDKIFSQANTPLKRW--LLEFAAKRKQ-AEVRsgiirnd 409
Cdd:PRK12316 4755 hPLINGASV--------VIRDDSLWD-PE------RLYAEIHEHRVTVLVFPPVYLqqLAEHAERDGEpPSLR------- 4812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 410 siwdelffnkiQASLGGcvrmivTGAAPASPTVLgfLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSG----HVGAPL 484
Cdd:PRK12316 4813 -----------VYCFGG------EAVAQASYDLA--WRALKPVYLFNGYGPTETTVTVLlWKARDGDACGaaymPIGTPL 4873
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 485 PCNHIKLVDVEeLNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSD------GWLH-TGDIGKWLPAGTLKIIDRKK 557
Cdd:PRK12316 4874 GNRSGYVLDGQ-LNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDpfgapgGRLYrTGDLARYRADGVIDYLGRVD 4952
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 558 HIFKLaQGEYVAPEKIEnIYIRSQP-------VAQIYVHGdslkAFLVGIVVP-DPEVMPSWAQKRGIEG 619
Cdd:PRK12316 4953 HQVKI-RGFRIELGEIE-ARLREHPavreavvIAQEGAVG----KQLVGYVVPqDPALADADEAQAELRD 5016
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
121-606 |
3.38e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 63.02 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRpEWIIVELACYTYSmvvvplydtlgpGAIRYIINTAdistviV 200
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRA--GDGVAVLARNH-RGFVLALYAAGKV------------GARIILLNTG------F 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 201 DKPQkavlLLEHVERKetpGLKLIILMDPFEE---ALKERGQKCGVVIKSMQAVEDC------------GQENHQAPVPP 265
Cdd:PRK07788 134 SGPQ----LAEVAARE---GVKALVYDDEFTDllsALPPDLGRLRAWGGNPDDDEPSgstdetlddliaGSSTAPLPKPP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 266 QPDdlSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLkvtesqwaptcadvhiSYLPLaHMFERMVQSVVYCHGgrVGFFQ 345
Cdd:PRK07788 207 KPG--GIVILTSGTTGTPKGAPRPEPSPLAPLAGLL----------------SRVPF-RAGETTLLPAPMFHA--TGWAH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 346 GDI-----------------RLLSDDMKALCPTIFpVVPRLLNRMYDkifsqantplkrwLLEfaakrkqaEVRSgiirn 408
Cdd:PRK07788 266 LTLamalgstvvlrrrfdpeATLEDIAKHKATALV-VVPVMLSRILD-------------LGP--------EVLA----- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 409 dsiwdelffnKIQASlggCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECtAGCTFTTPGDWT--SGHVGAPLPC 486
Cdd:PRK07788 319 ----------KYDTS---SLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEV-AFATIATPEDLAeaPGTVGRPPKG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 487 NHIKLVD-----VEElnywackGE-GEICVRGPNVFKGYlKDPdRTKEALdsDGWLHTGDIGKWLPAGTLKIIDRKKHIF 560
Cdd:PRK07788 385 VTVKILDengneVPR-------GVvGRIFVGNGFPFEGY-TDG-RDKQII--DGLLSSGDVGYFDEDGLLFVDGRDDDMI 453
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 327412323 561 kLAQGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDPE 606
Cdd:PRK07788 454 -VSGGENVFPAEVEDL---------LAGHPDVVEAAVIG--VDDEE 487
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
152-295 |
4.63e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 62.61 E-value: 4.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 152 VFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADiSTVIVDKPQkavlLLEHVERKETPGLKLIILMDPFE 231
Cdd:PRK04319 103 IFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSE-AKVLITTPA----LLERKPADDLPSLKHVLLVGEDV 177
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 327412323 232 EAlkerGQKCGVVIKSM-QAVEDCgqenhqAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVA 295
Cdd:PRK04319 178 EE----GPGTLDFNALMeQASDEF------DIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQ 232
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
150-607 |
5.81e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 62.35 E-value: 5.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 150 IGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAvlLLEHVErkeTPGLKLIILMDP 229
Cdd:PRK13388 55 VGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLLVTDAEHRP--LLDGLD---LPGVRVLDVDTP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 230 -FEEALKERGqkcgvviksmqavedcgqENHQAPvPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVteSQW 308
Cdd:PRK13388 130 aYAELVAAAG------------------ALTPHR-EVDAMDPFMLIFTSGTTGAPKAVRCSHGRLA--FAGRALT--ERF 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 309 APTCADVHISYLPLAHMFERMVQ-SVVYCHGGRVGF--------FQGDIRLLSddmkalcPTIFPVVPRLLNrmYdkIFS 379
Cdd:PRK13388 187 GLTRDDVCYVSMPLFHSNAVMAGwAPAVASGAAVALpakfsasgFLDDVRRYG-------ATYFNYVGKPLA--Y--ILA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 380 Q------ANTPLKRWLLEFAAKRKQAEvrsgiirndsiwdelffnkiqaslggcvrmivtgaapasptvlgFLRAaLGCQ 453
Cdd:PRK13388 256 TperpddADNPLRVAFGNEASPRDIAE--------------------------------------------FSRR-FGCQ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 454 VYEGYGQTEctAGCTFTTPGDWTSGHVGAPLPcnHIKLVDVEE---------------LNywACKGEGEICVR-GPNVFK 517
Cdd:PRK13388 291 VEDGYGSSE--GAVIVVREPGTPPGSIGRGAP--GVAIYNPETltecavarfdahgalLN--ADEAIGELVNTaGAGFFE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 518 GYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYVHGdslkafl 597
Cdd:PRK13388 365 GYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYA------- 435
|
490
....*....|
gi 327412323 598 vgivVPDPEV 607
Cdd:PRK13388 436 ----VPDERV 441
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
267-613 |
7.42e-10 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 61.62 E-value: 7.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgFLKVTESQWAPTCADVHISYLPL----AHmfERMVQSVVycHGGRV- 341
Cdd:cd17649 93 PRQLAYVIYTSGSTGTPKGVAVSHGPLAA----HCQATAERYGLTPGDRELQFASFnfdgAH--EQLLPPLI--CGACVv 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 342 ---GFFQGDIRLLSDDMKALCPTIFPVVPRLLNRmydkifsqantpLKRWLLEFAAKRKQAevrsgiirndsiwdelffn 418
Cdd:cd17649 165 lrpDELWASADELAEMVRELGVTVLDLPPAYLQQ------------LAEEADRTGDGRPPS------------------- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 419 kiqaslggcVRMIVTGAAPASPTvlgFLRAALGCQVY--EGYGQTECTAGCT-FTTPGD----WTSGHVGAPLPCNHIKL 491
Cdd:cd17649 214 ---------LRLYIFGGEALSPE---LLRRWLKAPVRlfNAYGPTEATVTPLvWKCEAGaaraGASMPIGRPLGGRSAYI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 492 VDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL--DSDG-----WLHTGDIGKWLPAGTLKIIDRKKHIFKLaQ 564
Cdd:cd17649 282 LD-ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFvpDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-R 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 327412323 565 GEYVAPEKIENiYIRSQP----VAQIYVHGDSLKAfLVGIVVP-DPEVMPSWAQ 613
Cdd:cd17649 360 GFRIELGEIEA-ALLEHPgvreAAVVALDGAGGKQ-LVAYVVLrAAAAQPELRA 411
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
274-590 |
9.82e-10 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 61.69 E-value: 9.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 274 CFTSGTTGNPKGAMLTH-GNVVadfsgflkvtesqwaptcadvhisylplahmfermvQSVVYCHGGRVGFFQGDirlls 352
Cdd:PRK06018 183 CYTSGTTGDPKGVLYSHrSNVL------------------------------------HALMANNGDALGTSAAD----- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 353 ddmkalcpTIFPVVPrllnrMYdkifsQANTplkrWLLEFAAKRKQAEVRSGIIRND--SIWDELFFNKIQASLG----- 425
Cdd:PRK06018 222 --------TMLPVVP-----LF-----HANS----WGIAFSAPSMGTKLVMPGAKLDgaSVYELLDTEKVTFTAGvptvw 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 426 --------------GCVRMIVTGAApASPTvlGFLRA--ALGCQVYEGYGQTECTAGCTFTT--------PGDWTSGHV- 480
Cdd:PRK06018 280 lmllqymekeglklPHLKMVVCGGS-AMPR--SMIKAfeDMGVEVRHAWGMTEMSPLGTLAAlkppfsklPGDARLDVLq 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 481 --GAPLPCNHIKLVDVE--ELNyWACKGEGEICVRGPNVFKGYLKDPDrtkEALDSDGWLHTGDIGKWLPAGTLKIIDRK 556
Cdd:PRK06018 357 kqGYPPFGVEMKITDDAgkELP-WDGKTFGRLKVRGPAVAAAYYRVDG---EILDDDGFFDTGDVATIDAYGYMRITDRS 432
|
330 340 350
....*....|....*....|....*....|....
gi 327412323 557 KHIFKlAQGEYVAPEKIENIYIRSQPVAQIYVHG 590
Cdd:PRK06018 433 KDVIK-SGGEWISSIDLENLAVGHPKVAEAAVIG 465
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
255-576 |
1.19e-09 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 61.32 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 255 GQENHQAPVPPQPD-DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAptcADVHISYLPLAH-Mfermvqs 332
Cdd:PRK05851 138 AHTNRSASLTPPDSgGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAA---TDVGCSWLPLYHdM------- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 333 vvychggrvgffqGDIRLLSDDMKA----LCPTifpvvprllnrmydKIFSQAntPLK--RWLLEFAAKRKQA-EVRSGI 405
Cdd:PRK05851 208 -------------GLAFLLTAALAGaplwLAPT--------------TAFSAS--PFRwlSWLSDSRATLTAApNFAYNL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 406 IRNdsiwdelFFNKIQASLGGCVRMIVTGAAP----------ASPTVLGFLRAALGcqvyEGYGQTECTAGCTFTTPG-- 473
Cdd:PRK05851 259 IGK-------YARRVSDVDLGALRVALNGGEPvdcdgferfaTAMAPFGFDAGAAA----PSYGLAESTCAVTVPVPGig 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 474 ---------DWTSGH----VGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPdrtkeALDSDGWLHTGD 540
Cdd:PRK05851 328 lrvdevttdDGSGARrhavLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQA-----PIDPDDWFPTGD 402
|
330 340 350
....*....|....*....|....*....|....*.
gi 327412323 541 IGkWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENI 576
Cdd:PRK05851 403 LG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERV 436
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
264-557 |
1.23e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 61.17 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 264 PPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF----LKVTEsqwaptcADVHISYLPLAH-Mfermvqsvvychg 338
Cdd:PRK09192 172 RPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAIshdgLKVRP-------GDRCVSWLPFYHdM------------- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 339 GRVGFF------QgdirlLSDDmkaLCPT-IFPVVP----RLLNRMYDKI-FSQAntplkrWLLEFAAKRkqAEVRSGII 406
Cdd:PRK09192 232 GLVGFLltpvatQ-----LSVD---YLPTrDFARRPlqwlDLISRNRGTIsYSPP------FGYELCARR--VNSKDLAE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 407 RNDSIWdelffnkiqaslggcvRMIVTGAAPASPTVL----------GF-LRAALGCqvyegYGQTECTAGCTFTTPG-- 473
Cdd:PRK09192 296 LDLSCW----------------RVAGIGADMIRPDVLhqfaeafapaGFdDKAFMPS-----YGLAEATLAVSFSPLGsg 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 474 --------DWTSGH------------------VGAPLPCNHIKLVDV--EELNYwacKGEGEICVRGPNVFKGYLKDPDR 525
Cdd:PRK09192 355 ivveevdrDRLEYQgkavapgaetrrvrtfvnCGKALPGHEIEIRNEagMPLPE---RVVGHICVRGPSLMSGYFRDEES 431
|
330 340 350
....*....|....*....|....*....|..
gi 327412323 526 TKeALDSDGWLHTGDIGkWLPAGTLKIIDRKK 557
Cdd:PRK09192 432 QD-VLAADGWLDTGDLG-YLLDGYLYITGRAK 461
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
121-607 |
1.43e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 60.79 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLGSGLlqHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIv 200
Cdd:PRK13390 25 VSYRQLDDDSAALARVL--YDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLV- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 201 dkpqkAVLLLEHVERKETPGLKLIILMD-------PFEEALKERGQKCgvviksmqAVEDCGqenhqapvppqpddlSIV 273
Cdd:PRK13390 102 -----ASAALDGLAAKVGADLPLRLSFGgeidgfgSFEAALAGAGPRL--------TEQPCG---------------AVM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 274 CFTSGTTGNPKG--------AMLTHGN-VVADFSGFLKVTESqwaptcaDVHISYLPLAHMFERMVQSVVYCHGGRVGFF 344
Cdd:PRK13390 154 LYSSGTTGFPKGiqpdlpgrDVDAPGDpIVAIARAFYDISES-------DIYYSSAPIYHAAPLRWCSMVHALGGTVVLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 345 QG-DIRLLSDDMKALCPTIFPVVPRLLNRMYdkifsqantplkrwllefaakRKQAEVRSgiiRNDSiwdelffnkiqAS 423
Cdd:PRK13390 227 KRfDAQATLGHVERYRITVTQMVPTMFVRLL---------------------KLDADVRT---RYDV-----------SS 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 424 LggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVG-APLPCNHIKLVDVEELNyw 500
Cdd:PRK13390 272 L----RAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGrSVLGDLHICDDDGNELP-- 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 501 ackgEGEIcvrGPNVFK------GYLKDPDRTKEALDSDG--WLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEK 572
Cdd:PRK13390 345 ----AGRI---GTVYFErdrlpfRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQE 416
|
490 500 510
....*....|....*....|....*....|....*
gi 327412323 573 IENIYIRSQPVAQIYVHGdslkaflvgivVPDPEV 607
Cdd:PRK13390 417 TENALTMHPAVHDVAVIG-----------VPDPEM 440
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
125-621 |
1.60e-09 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 60.79 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 125 EVADRAEFLGSGLLQHNCKactdqfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQ 204
Cdd:PRK05857 50 EVGGLAADLRAQSVSRGSR------VLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVAPGS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 205 KAVLLLEHVERKETPGLKLIILMDPFEEAlkergqkCGVVIKSMQAVEDCGQenhqapvppqpDDLSIVCFTSGTTGNPK 284
Cdd:PRK05857 124 KMASSAVPEALHSIPVIAVDIAAVTRESE-------HSLDAASLAGNADQGS-----------EDPLAMIFTSGTTGEPK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 285 GAMLTHGNVVAdFSGFLKVTESQWApTCADVHISYLPLAHMFERMVQSVVYC--HGGRV---GFFQGDIR--LLSDDMKA 357
Cdd:PRK05857 186 AVLLANRTFFA-VPDILQKEGLNWV-TWVVGETTYSPLPATHIGGLWWILTClmHGGLCvtgGENTTSLLeiLTTNAVAT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 358 LCptifpVVPRLLNRM-YDKIFSQANTPLKRWLLEFAAKRKQAEVRSgiirndsiwdelffnkIQAslggcvrmivTGAA 436
Cdd:PRK05857 264 TC-----LVPTLLSKLvSELKSANATVPSLRLVGYGGSRAIAADVRF----------------IEA----------TGVR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 437 PAsptvlgflraalgcQVYeGYGQTECTAGCTFTTPGDWT---SGHVGAPLPCNHIKLVDVEELNYWACKGE-----GEI 508
Cdd:PRK05857 313 TA--------------QVY-GLSETGCTALCLPTDDGSIVkieAGAVGRPYPGVDVYLAATDGIGPTAPGAGpsasfGTL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 509 CVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPV--AQI 586
Cdd:PRK05857 378 WIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGGVNIAPDEVDRIAEGVSGVreAAC 455
|
490 500 510
....*....|....*....|....*....|....*...
gi 327412323 587 YVHGDSLKAFLVGI-VVPDPEVMPSWAQ--KRGIEGTY 621
Cdd:PRK05857 456 YEIPDEEFGALVGLaVVASAELDESAARalKHTIAARF 493
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
267-609 |
2.09e-09 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 60.49 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSG--FLKVTESQwaptcADVHISYLPLAHMFERMVQSVVYCHggrv 341
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVnlrTSLSEryFGRDNGDE-----AVLFFSNYVFDFFVEQMTLALLNGQ---- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 342 gffqgDIRLLSDDMKALCPTIfpvvPRLLNRmyDKIFSQANTPLKRWLLEFAakrkqaevrsgiirndsiwdelffnkiq 421
Cdd:cd17648 164 -----KLVVPPDEMRFDPDRF----YAYINR--EKVTYLSGTPSVLQQYDLA---------------------------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 422 aSLGGCVRMIVTGAAPASPtVLGFLRAALGCQVYEGYGQTEC--TAGCTFTTPGDWTSGHVGAPLPCNHIKLVDvEELNY 499
Cdd:cd17648 205 -RLPHLKRVDAAGEEFTAP-VFEKLRSRFAGLIINAYGPTETtvTNHKRFFPGDQRFDKSLGRPVRNTKCYVLN-DAMKR 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 500 WACKGEGEICVRGPNVFKGYLKDPDRTKE-------------ALDSDGWLH-TGDIGKWLPAGTLKIIDRKKHIFKLaQG 565
Cdd:cd17648 282 VPVGAVGELYLGGDGVARGYLNRPELTAErflpnpfqteqerARGRNARLYkTGDLVRWLPSGELEYLGRNDFQVKI-RG 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 327412323 566 EYVAPEKIENIY-----IRSQPVAQIYVHGDSLKA---FLVGIVVPDPEVMP 609
Cdd:cd17648 361 QRIEPGEVEAALasypgVRECAVVAKEDASQAQSRiqkYLVGYYLPEPGHVP 412
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
258-615 |
2.48e-09 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 59.67 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 258 NHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVA------DFSGflkvTESQWAPTCADVHISYLPLahmferMVQ 331
Cdd:PRK07824 25 DALRVGEPIDDDVALVVATSGTTGTPKGAMLTAAALTAsadathDRLG----GPGQWLLALPAHHIAGLQV------LVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 332 SVV---------YCHGGRVGFFQGDIRLLSDDMK--ALCPTifpvvpRLLNRMYDKIFSQAntplkrwLLEFAAkrkqae 400
Cdd:PRK07824 95 SVIagsepveldVSAGFDPTALPRAVAELGGGRRytSLVPM------QLAKALDDPAATAA-------LAELDA------ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 401 vrsgiirndsiwdelffnkiqaslggcvrmIVTGAAPASPTVlgfLRAA--LGCQVYEGYGQTECTAGCTFTtpgdwtsg 478
Cdd:PRK07824 156 ------------------------------VLVGGGPAPAPV---LDAAaaAGINVVRTYGMSETSGGCVYD-------- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 479 hvGAPLPCNHIKLVDveelnywackgeGEICVRGPNVFKGY--LKDPDrtkeALDSDGWLHTGDIGKwLPAGTLKIIDRK 556
Cdd:PRK07824 195 --GVPLDGVRVRVED------------GRIALGGPTLAKGYrnPVDPD----PFAEPGWFRTDDLGA-LDDGVLTVLGRA 255
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 327412323 557 KHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVHG---DSLKAFLVGIVVPDPEVMPSWAQKR 615
Cdd:PRK07824 256 DDAISTG-GLTVLPQVVEAALATHPAVADCAVFGlpdDRLGQRVVAAVVGDGGPAPTLEALR 316
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
261-598 |
2.51e-09 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 60.24 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 261 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGN--VVADFSG--FLKVTESQWAPTCADVHISY-LPLAHMFERMVQSVVY 335
Cdd:TIGR02262 154 KPAATQADDPAFWLYSSGSTGMPKGVVHTHSNpyWTAELYArnTLGIREDDVCFSAAKLFFAYgLGNALTFPMSVGATTV 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 336 CHGGR---VGFFqgdirllsDDMKALCPTIFPVVPRLlnrmYDKIFSQANTPlkrwllefaaKRKQAEVRsgiirndsiw 412
Cdd:TIGR02262 234 LMGERptpDAVF--------DRLRRHQPTIFYGVPTL----YAAMLADPNLP----------SEDQVRLR---------- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 413 delffnkiqaslggcvrmIVTGAAPASPTVLGF-LRAALGCQVYEGYGQTEctAGCTFTT--PGDWTSGHVGAPLPCNHI 489
Cdd:TIGR02262 282 ------------------LCTSAGEALPAEVGQrWQARFGVDIVDGIGSTE--MLHIFLSnlPGDVRYGTSGKPVPGYRL 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 490 KLVDveELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSdGWLHTGDigKWL--PAGTLKIIDRKKHIFKLAqGE 566
Cdd:TIGR02262 342 RLVG--DGGQDVADGEpGELLISGPSSATMYWNNRAKSRDTFQG-EWTRSGD--KYVrnDDGSYTYAGRTDDMLKVS-GI 415
|
330 340 350
....*....|....*....|....*....|....*....
gi 327412323 567 YVAPEKIENIYIRSQPVAQIYVHG----DSL---KAFLV 598
Cdd:TIGR02262 416 YVSPFEIESALIQHPAVLEAAVVGvadeDGLikpKAFVV 454
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
268-574 |
4.15e-09 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 59.41 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 268 DDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVTESQwapTCADVHISYLPLAHM-FERMVQSVV--YCHGGRvgff 344
Cdd:cd17656 128 DDLLYIIYTSGTTGKPKGVQLEHKNMV----NLLHFEREK---TNINFSDKVLQFATCsFDVCYQEIFstLLSGGT---- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 345 qgdIRLLSDDMKALCPTIFPVVPRllNRMYDKIFSQAntplkrwLLEFAAKRKQaevrsgiirndsiwdelFFNkiqaSL 424
Cdd:cd17656 197 ---LYIIREETKRDVEQLFDLVKR--HNIEVVFLPVA-------FLKFIFSERE-----------------FIN----RF 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 425 GGCVRMIVTGAAP--ASPTVLGFLRAAlGCQVYEGYG--QTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDvEELNY 499
Cdd:cd17656 244 PTCVKHIITAGEQlvITNEFKEMLHEH-NVHLHNHYGpsETHVVTTYTINPEAEIPElPPIGKPISNTWIYILD-QEQQL 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 500 WACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGW------LHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKI 573
Cdd:cd17656 322 QPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-RGYRIELGEI 400
|
.
gi 327412323 574 E 574
Cdd:cd17656 401 E 401
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
429-605 |
6.88e-09 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 58.85 E-value: 6.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 429 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT---------FTT------PGD--WTSGHVGAPLPCNHIkl 491
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAEGLVNYTrlddsderiFTTqgrpmsPDDevWVADADGNPLPQGEV-- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 492 vdveelnywackgeGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHifklaQ----GEY 567
Cdd:PRK10946 381 --------------GRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGEK 441
|
170 180 190
....*....|....*....|....*....|....*...
gi 327412323 568 VAPEKIENIYIRsqpvaqiyvHGDSLKAFLVGIvvPDP 605
Cdd:PRK10946 442 IAAEEIENLLLR---------HPAVIHAALVSM--EDE 468
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
86-615 |
7.47e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 56.12 E-value: 7.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 86 YDDARTMYQVFRRGLSISGNGPCLGFRKpkqpyQWLSYQEVADRAEFLGSGLLQhnCKACTDQFIGVFAQNRPEWIIVEL 165
Cdd:PRK12316 507 YPLQRGVHRLFEEQVERTPEAPALAFGE-----ETLDYAELNRRANRLAHALIE--RGVGPDVLVGVAMERSIEMVVALL 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 166 ACYTYSMVVVPLYDTLGPGAIRYIINTADIstvivdkpqkAVLLLEHVERKETP---GLKLIILMDP--FEEALKERGQK 240
Cdd:PRK12316 580 AILKAGGAYVPLDPEYPAERLAYMLEDSGV----------QLLLSQSHLGRKLPlaaGVQVLDLDRPaaWLEGYSEENPG 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 241 CGVViksmqavedcgqenhqapvppqPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKV-------TESQWAPTCA 313
Cdd:PRK12316 650 TELN----------------------PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAyglgvgdTVLQKTPFSF 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 314 DVHIS--YLPLAhmfermvqsvvycHGGRVgffqgdirllsddmkalcptifPVVPRLLNRMYDKIFSQANTPLKRwLLE 391
Cdd:PRK12316 708 DVSVWefFWPLM-------------SGARL----------------------VVAAPGDHRDPAKLVELINREGVD-TLH 751
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 392 FAAKRKQAEVRSGIIrndsiwdelffnkiqASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTT 471
Cdd:PRK12316 752 FVPSMLQAFLQDEDV---------------ASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWT 816
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 472 PGDWTSGHV--GAPLPCNHIKLVDVeELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL------DSDGWLHTGDIGK 543
Cdd:PRK12316 817 CVEEGGDSVpiGRPIANLACYILDA-NLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFvpspfvAGERMYRTGDLAR 895
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 327412323 544 WLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAfLVGIVVPD------PEVMPSWAQKR 615
Cdd:PRK12316 896 YRADGVIEYAGRIDHQVKL-RGLRIELGEIEARLLEHPWVREAAVLAVDGKQ-LVGYVVLEseggdwREALKAHLAAS 971
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
257-585 |
1.24e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.56 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 257 ENHQAPVPpQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgflkvtesQWAPTCA--------DVHISYLPLAH---M 325
Cdd:PRK05691 156 EAWQEPAL-QPDDIAFLQYTSGSTALPKGVQVSHGNLVAN----------EQLIRHGfgidlnpdDVIVSWLPLYHdmgL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 326 FERMVQSV---VYCHGGRVGFF--------------QGDIRLLSDDMKALCPtifpvvprllNRMYDKIFSQANtpLKRW 388
Cdd:PRK05691 225 IGGLLQPIfsgVPCVLMSPAYFlerplrwleaiseyGGTISGGPDFAYRLCS----------ERVSESALERLD--LSRW 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 389 LLEFAAkrkqaevrSGIIRNDSIwdELFFNKIQ----------ASLG-GCVRMIVTGAAPA-SPTVLGFLRAALGCQVYE 456
Cdd:PRK05691 293 RVAYSG--------SEPIRQDSL--ERFAEKFAacgfdpdsffASYGlAEATLFVSGGRRGqGIPALELDAEALARNRAE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 457 GyGQTECTAGCTFTTPGdwtsghvgaplpcNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEA---LDSD 533
Cdd:PRK05691 363 P-GTGSVLMSCGRSQPG-------------HAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfveHDGR 428
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 327412323 534 GWLHTGDIGkWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQ 585
Cdd:PRK05691 429 TWLRTGDLG-FLRDGELFVTGRLKDML-IVRGHNLYPQDIEKTVEREVEVVR 478
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
422-606 |
1.84e-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: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 422 ASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEC-TAGCTFTTPGDWT-SGHVGAPLPCNHIKLVDvEELNY 499
Cdd:cd05973 201 ARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELgMVLANHHALEHPVhAGSAGRAMPGWRVAVLD-DDGDE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 500 WACKGEGEICV---RGPNV-FKGYLKDPDRTKealdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIEN 575
Cdd:cd05973 280 LGPGEPGRLAIdiaNSPLMwFRGYQLPDTPAI----DGGYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFDVES 354
|
170 180 190
....*....|....*....|....*....|.
gi 327412323 576 IYIRSQPVAQIYVhgdslkaflvgIVVPDPE 606
Cdd:cd05973 355 ALIEHPAVAEAAV-----------IGVPDPE 374
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
416-598 |
2.07e-07 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 54.27 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 416 FFNKIqasLGGC-------VRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTEctAGCTFT--TPGDWTSGHVGAPLP 485
Cdd:PRK06060 246 FFARV---IDSCspdsfrsLRCVVSAGEALELGLAERLMEFFGgIPILDGIGSTE--VGQTFVsnRVDEWRLGTLGRVLP 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 486 CNHIKLVDVEELNYwACKGEGEICVRGPNVFKGYLKDPDrtkEALDSDGWLHTGDIGK-----WLPAGTlkiidrKKHIF 560
Cdd:PRK06060 321 PYEIRVVAPDGTTA-GPGVEGDLWVRGPAIAKGYWNRPD---SPVANEGWLDTRDRVCidsdgWVTYRC------RADDT 390
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 327412323 561 KLAQGEYVAPEKIENIYIRSQPVAQIYVHG-------DSLKAFLV 598
Cdd:PRK06060 391 EVIGGVNVDPREVERLIIEDEAVAEAAVVAvrestgaSTLQAFLV 435
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
267-598 |
8.39e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 52.86 E-value: 8.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 267 PDDLSIVCFTSGTTGNPKGAMLT-HGNVVADFSG--FLKVTE----SQWAPTCADVHISYLPLAHMFermvqsvvychGG 339
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEqRGMLNNQLSKvpYLALSEadviAQTASQSFDISVWQFLAAPLF-----------GA 3936
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 340 RVGFFQGDIrllSDDMKALCP-------TIFPVVPRLLNRMydkifsqantplkrwllefaakrkqaevrsgiIRNDsiw 412
Cdd:PRK05691 3937 RVEIVPNAI---AHDPQGLLAhvqaqgiTVLESVPSLIQGM--------------------------------LAED--- 3978
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 413 delffnkiQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF------TTPGDWTSghVGAPLPC 486
Cdd:PRK05691 3979 --------RQALDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFfrvdlaSTRGSYLP--IGSPTDN 4048
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 487 NHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL-------DSDGWLHTGDIGKWLPAGTLKIIDRKKHI 559
Cdd:PRK05691 4049 NRLYLLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFvphpfgaPGERLYRTGDLARRRSDGVLEYVGRIDHQ 4127
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 327412323 560 -----FKLAQGEYVApEKIENIYIRSQPVA-QIYVHGDSLKAFLV 598
Cdd:PRK05691 4128 vkirgYRIELGEIEA-RLHEQAEVREAAVAvQEGVNGKHLVGYLV 4171
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
483-543 |
2.41e-06 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 50.66 E-value: 2.41e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 327412323 483 PLPCNHIK-----LVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL-DSDGW--LHTGDIGK 543
Cdd:PRK04813 317 RLPIGYAKpdsplLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGY 385
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
428-575 |
5.49e-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: 5.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 428 VRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTEcTAGCTFTTPGD-WTSGHVGAPLPCNHIKLVDVEElnywacKGE 505
Cdd:cd17633 112 IKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSE-LSFITYNFNQEsRPPNSVGRPFPNVEIEIRNADG------GEI 184
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 506 GEICVRGPNVFKGYLKDPDRTKealdsDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIEN 575
Cdd:cd17633 185 GKIFVKSEMVFSGYVRGGFSNP-----DGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIES 248
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
269-606 |
1.07e-05 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 48.50 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 269 DLSIVCFTSGTTGNPKGAMLTH-----GNVVADFSGFLKVTesqwaptcaDVHISYLPLAHMFERMVQ-SVVYCHGGRVG 342
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHrrawrGGAFFAGSGGALPS---------DVLYTCLPLYHSTALIVGwSACLASGATLV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 343 F--------FQGDIRllsddmKALCpTIFPVVPRLLnrmydkifsqantplkRWLLefAAKRKQAEVRsgiirndsiwde 414
Cdd:cd05940 153 IrkkfsasnFWDDIR------KYQA-TIFQYIGELC----------------RYLL--NQPPKPTERK------------ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 415 lffNKIQASLGGCVRmivtgaapasPTVLGFLRAALGC-QVYEGYGQTECTAGCT--FTTPGdwTSGHVGAPLPCNH-IK 490
Cdd:cd05940 196 ---HKVRMIFGNGLR----------PDIWEEFKERFGVpRIAEFYAATEGNSGFInfFGKPG--AIGRNPSLLRKVApLA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 491 LV--DVEELNYW---------ACKGE-----GEICVRGPnvFKGYLKDPDRTKEAL-----DSDGWLHTGDIGKWLPAGT 549
Cdd:cd05940 261 LVkyDLESGEPIrdaegrcikVPRGEpglliSRINPLEP--FDGYTDPAATEKKILrdvfkKGDAWFNTGDLMRLDGEGF 338
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 327412323 550 LKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYVHGDSL-----KAFLVGIVVPDPE 606
Cdd:cd05940 339 WYFVDRLGDTFRW-KGENVSTTEVAAVLGAFPGVEEANVYGVQVpgtdgRAGMAAIVLQPNE 399
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
226-325 |
1.37e-05 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 48.44 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 226 LMDPFEE---ALKERGQKCGVVIKSM--QAVEDCGQENHQAPVPPQPDDLS---------IVCFTSGTTGNPKGAMLTHG 291
Cdd:cd05938 88 LQEAVEEvlpALRADGVSVWYLSHTSntEGVISLLDKVDAASDEPVPASLRahvtikspaLYIYTSGTTGLPKAARISHL 167
|
90 100 110
....*....|....*....|....*....|....
gi 327412323 292 NVVAdFSGFLKVTesqwAPTCADVHISYLPLAHM 325
Cdd:cd05938 168 RVLQ-CSGFLSLC----GVTADDVIYITLPLYHS 196
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
265-614 |
1.65e-05 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 47.76 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 265 PQPDDLSIVCfTSGTTGNPKGAMLTHGNV-VADFSGFLKVTESQ-----------------WAPTCADVHISYLpLAHMF 326
Cdd:cd05924 1 RSADDLYILY-TGGTTGMPKGVMWRQEDIfRMLMGGADFGTGEFtpsedahkaaaaaagtvMFPAPPLMHGTGS-WTAFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 327 ERMVQSVVYCHGGRvgfFQGD--IRLLSddmKALCPTIFPVVPRLLNRMYDKIFSQANTPLkrwllefaakrkqaevrsg 404
Cdd:cd05924 79 GLLGGQTVVLPDDR---FDPEevWRTIE---KHKVTSMTIVGDAMARPLIDALRDAGPYDL------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 405 iirndsiwdelffnkiqASLggcvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFTTPGdwtSGHVGAP 483
Cdd:cd05924 134 -----------------SSL----FAISSGGALLSPEVKqGLLELVPNITLVDAFGSSETGFTGSGHSAG---SGPETGP 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 484 L-PCNHIKLVDVEELNYWACK--GEGEICVRGpNVFKGYLKDPDRTKEA---LDSDGWLHTGDIGKWLPAGTLKIIDRKK 557
Cdd:cd05924 190 FtRANPDTVVLDDDGRVVPPGsgGVGWIARRG-HIPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGRGS 268
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 327412323 558 HIFKLAqGEYVAPEKIENIyIRSQP-VAQIYVHGdslkaflvgivVPDPEvmpsWAQK 614
Cdd:cd05924 269 VCINTG-GEKVFPEEVEEA-LKSHPaVYDVLVVG-----------RPDER----WGQE 309
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
425-607 |
8.60e-05 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 45.90 E-value: 8.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 425 GGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFT-TPGDWTSG--HVGAPLPCNHIKLVDVE--ELNy 499
Cdd:PRK13382 311 GRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATE--AGMIATaTPADLRAApdTAGRPAEGTEIRILDQDfrEVP- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 500 wacKGE-GEICVRGPNVFKGYlkDPDRTKEAldSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIyI 578
Cdd:PRK13382 388 ---TGEvGTIFVRNDTQFDGY--TSGSTKDF--HDGFMASGDVGYLDENGRLFVVGRDDEMI-VSGGENVYPIEVEKT-L 458
|
170 180 190
....*....|....*....|....*....|....*..
gi 327412323 579 RSQP-VAQIYV-------HGDSLKAFlvgiVVPDPEV 607
Cdd:PRK13382 459 ATHPdVAEAAVigvddeqYGQRLAAF----VVLKPGA 491
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
121-324 |
8.93e-05 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 45.64 E-value: 8.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAE-----FLGSGLLQHNCkactdqfIGVFAQNRPEWIIVELACyTYSMVVVPLYDT-LGPGAIRYIINTAD 194
Cdd:PRK08279 63 ISYAELNARANryahwAAARGVGKGDV-------VALLMENRPEYLAAWLGL-AKLGAVVALLNTqQRGAVLAHSLNLVD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 195 ISTVIVDKPqkavlLLEHVE--RKETPGLKLIILMDPFEEALKERgqkcgvVIKSMQAVEDCGQENHQAPVPPQPDDLSI 272
Cdd:PRK08279 135 AKHLIVGEE-----LVEAFEeaRADLARPPRLWVAGGDTLDDPEG------YEDLAAAAAGAPTTNPASRSGVTAKDTAF 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 327412323 273 VCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTESqwaptcaDVHISYLPLAH 324
Cdd:PRK08279 204 YIYTSGTTGLPKAAVMSHMRWLkamGGFGGLLRLTPD-------DVLYCCLPLYH 251
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
417-695 |
1.06e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 45.54 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 417 FNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPGDWTSGHVGAPLPCNHIKLVDVEE 496
Cdd:PRK07638 245 LYKENRVIENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSF-VTALVDEESERRPNSVGRPFHNVQVRICNE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 497 LNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEaLDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIEN 575
Cdd:PRK07638 324 AGEEVQKGEiGTVYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIES 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 576 IYIRSQPVAQIYVHGdslkaflvgivVPDpevmPSWAQKRG--IEGTyadlCTNKDLKKAILEDmvrlgkesgLHSFEQV 653
Cdd:PRK07638 402 VLHEHPAVDEIVVIG-----------VPD----SYWGEKPVaiIKGS----ATKQQLKSFCLQR---------LSSFKIP 453
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 327412323 654 KAIHIhsdmfsVQNGLLTPTLKAKRPELreyfKKQIEELYSI 695
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 ... |
418-582 |
1.16e-04 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 45.11 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 418 NKIQASLGGCVRMIVTGAAPASPTV----LGFLRA--ALGCQVYEGYGqTECTAGCTFTTPGDWTSGHVGAPLPCNHI-K 490
Cdd:cd05915 263 ESTGHRLKTLRRLVVGGSAAPRSLIarfeRMGVEVrqGYGLTETSPVV-VQNFVKSHLESLSEEEKLTLKAKTGLPIPlV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 491 LVDVEELNYWACKGEGE----ICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGE 566
Cdd:cd05915 342 RLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG-GE 420
|
170
....*....|....*.
gi 327412323 567 YVAPEKIENIyIRSQP 582
Cdd:cd05915 421 WISSVDLENA-LMGHP 435
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
261-557 |
1.98e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 44.55 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 261 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADF----SGFLKVTESqwAPTCADVHISYLPLAHMFERMVQSVVYC 336
Cdd:PRK05850 153 DARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFeqlmSDYFGDTGG--VPPPDTTVVSWLPFYHDMGLVLGVCAPI 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 337 HGGR-------VGFFQGDIRLLsddmkalcptifpvvpRLLNRmYDKIFSQAntPlkRWLLEFAAKRKQAEVRSGIirnd 409
Cdd:PRK05850 231 LGGCpavltspVAFLQRPARWM----------------QLLAS-NPHAFSAA--P--NFAFELAVRKTSDDDMAGL---- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 410 siwdelffnkiqaSLGGcVRMIVTGAAPASP-TVLGFLR--AALGCQ---VYEGYGQTECTAGCTFTTPGD--------- 474
Cdd:PRK05850 286 -------------DLGG-VLGIISGSERVHPaTLKRFADrfAPFNLRetaIRPSYGLAEATVYVATREPGQppesvrfdy 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 475 --WTSGHV-------GAPLPCNH------IKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALD------SD 533
Cdd:PRK05850 352 ekLSAGHAkrcetggGTPLVSYGsprsptVRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGatlvdpSP 431
|
330 340
....*....|....*....|....*....
gi 327412323 534 G-----WLHTGDIGkWLPAGTLKIIDRKK 557
Cdd:PRK05850 432 GtpegpWLRTGDLG-FISEGELFIVGRIK 459
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
121-598 |
2.61e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 44.22 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 121 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PRK13383 61 LSYRELQRATESLARRLTRDGVAP--GRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 201 DkpqkavlllehverketpglkliilmDPFEEALKERGQKCGVVIKSMQAVEDCGQENHQAPVPpqpddlSIVCFTSGTT 280
Cdd:PRK13383 139 D--------------------------NEFAERIAGADDAVAVIDPATAGAEESGGRPAVAAPG------RIVLLTSGTT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 281 GNPKGamlthgnvvadfsgflkVTESQWAPTCADVHISYLPLAHMF--ERMVQSVVYCHGGRVGFFQGDIrllsddmkAL 358
Cdd:PRK13383 187 GKPKG-----------------VPRAPQLRSAVGVWVTILDRTRLRtgSRISVAMPMFHGLGLGMLMLTI--------AL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 359 CPTIfpvvprLLNRMYDKIFSQANTPLKRwllefaakrkqAEVRSGI-IRNDSIWDelFFNKIQA-SLGGCVRMIVTGAA 436
Cdd:PRK13383 242 GGTV------LTHRHFDAEAALAQASLHR-----------ADAFTAVpVVLARILE--LPPRVRArNPLPQLRVVMSSGD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 437 PASPTVLGFLRAALGCQVYEGYGQTECTAGcTFTTPG---DWTSGhVGAPLPCNHIKLVDVEELNYwACKGEGEICVRGP 513
Cdd:PRK13383 303 RLDPTLGQRFMDTYGDILYNGYGSTEVGIG-ALATPAdlrDAPET-VGKPVAGCPVRILDRNNRPV-GPRVTGRIFVGGE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 514 NVFKGYlkdPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYV----- 588
Cdd:PRK13383 380 LAGTRY---TDGGGKAV-VDGMTSTGDMGYLDNAGRLFIVGREDDMI-ISGGENVYPRAVENALAAHPAVADNAVigvpd 454
|
490
....*....|..
gi 327412323 589 --HGDSLKAFLV 598
Cdd:PRK13383 455 erFGHRLAAFVV 466
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
268-599 |
3.75e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.00 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 268 DDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgfLKVTESQWAPTCADVHISYLPLAhmFErmvQSVVYCH-----GGRVG 342
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNTHAALAER----LQWMQATYALDDSDVLMQKAPIS--FD---VSVWECFwplitGCRLV 1343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 343 FF----QGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTPLKRWlleFAAkrkqAEVRSGIIRNdsiwdelffn 418
Cdd:PRK05691 1344 LAgpgeHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRL---FSG----GEALPAELRN---------- 1406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 419 kiqaslggcvrmivtgaapaspTVLGFLRAAlgcQVYEGYGQTECTAGCTF--TTPGDWTSGHVGAPLPCNHIKLVDvEE 496
Cdd:PRK05691 1407 ----------------------RVLQRLPQV---QLHNRYGPTETAINVTHwqCQAEDGERSPIGRPLGNVLCRVLD-AE 1460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 497 LNYWACKGEGEICVRGPNVFKGYLKDPDRTKE-----ALDSDG--WLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVA 569
Cdd:PRK05691 1461 LNLLPPGVAGELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL-RGFRVE 1539
|
330 340 350
....*....|....*....|....*....|..
gi 327412323 570 PEKIENIYIRSQPVAQ--IYVHGDSLKAFLVG 599
Cdd:PRK05691 1540 PEEIQARLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
267-590 |
5.43e-04 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 43.19 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 267 PDDLSIVCFTSGTTGNPKGAMLTHG-NVVAD--FSGFLKVTESQWAPTCadvhisyLPLAH---MFERMVQSVVycHGGR 340
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISWRrTLVTSnlLSHDLNLKNGDRTYTC-------MPLYHgtaAFLGACNCLM--SGGT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 341 VGF--------FQGDIRllsdDMKAlcpTIFPVVPRLLnrmydkifsqantplkRWLLEFAAkrkqaevrsgiirndSIW 412
Cdd:cd05937 157 LALsrkfsasqFWKDVR----DSGA---TIIQYVGELC----------------RYLLSTPP---------------SPY 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 413 DELffNKIQASLGGCVRmivtgaapasPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKL 491
Cdd:cd05937 199 DRD--HKVRVAWGNGLR----------PDIWERFRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKF 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 492 --------VDVEELNYW----------ACKGE-GEICVRGPNV----FKGYLKDPDRTKEAL------DSDGWLHTGDIG 542
Cdd:cd05937 267 enqvvlvkMDPETDDPIrdpktgfcvrAPVGEpGEMLGRVPFKnreaFQGYLHNEDATESKLvrdvfrKGDIYFRTGDLL 346
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 327412323 543 KWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYVHG 590
Cdd:cd05937 347 RQDADGRWYFLDRLGDTFRW-KSENVSTTEVADVLGAHPDIAEANVYG 393
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
263-294 |
5.67e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 43.49 E-value: 5.67e-04
10 20 30
....*....|....*....|....*....|..
gi 327412323 263 VPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVV 294
Cdd:PRK10252 593 QLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIV 624
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
517-605 |
2.31e-03 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 41.57 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412323 517 KGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIyIRSQP-VAQIYVH 589
Cdd:PRK10252 814 QGYLGRPDLTASRFIADPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKI-RGQRIELGEIDRA-MQALPdVEQAVTH 891
|
90 100
....*....|....*....|....*..
gi 327412323 590 -----------GDSLKafLVGIVVPDP 605
Cdd:PRK10252 892 acvinqaaatgGDARQ--LVGYLVSQS 916
|
|
| |
