|
Name |
Accession |
Description |
Interval |
E-value |
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
141-719 |
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: 926.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 141 QPYQWLSYQEVADRAEFLGSGLLQHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADI 220
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 221 STVIVDKpqkavlllehverketpglkliilmdpfeealkergqkcGVVIKSMQAVEDCGQENHQAPVPPQPDDLSIVCF 300
Cdd:cd05927 81 SIVFCDA---------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 301 TSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDM 380
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 381 KALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWLLEFAAKRKQAEVRSGIIRNDSIWDELFFNKIQASLGGCVRMIVT 458
Cdd:cd05927 202 KALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 459 GAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWA--CKGEGEICVR 536
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAkdPNPRGEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 537 GPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGD 616
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 617 SLKAFLVGIVVPDPEVMPSWA-QKRGIEGTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLL 695
Cdd:cd05927 442 SLKSFLVAIVVPDPDVLKEWAaSKGGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLL 521
|
570 580
....*....|....*....|....
gi 57165412 696 TPTLKAKRPELREYFKKQIEELYS 719
Cdd:cd05927 522 TPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
97-719 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 703.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 97 RSViGSGPQLLTHY--YDDARTMYQVFRRGLSISGNGPCLGFRKPKQ----PYQWLSYQEVADRAEFLGSGLLQHNCK-- 168
Cdd:PLN02736 25 RSA-RSPLKLVSRFpdHPEIGTLHDNFVYAVETFRDYKYLGTRIRVDgtvgEYKWMTYGEAGTARTAIGSGLVQHGIPkg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 169 ACtdqfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVdKPQKAVLLLEHVerKETPGLKL 248
Cdd:PLN02736 104 AC----VGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCL--SEIPSVRL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 249 IILMDPFEEALKERGQKCGVVIKSMQAVEDCGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKV 328
Cdd:PLN02736 177 IVVVGGADEPLPSLPSGTGVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 329 TEkvIFPrqDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QA 406
Cdd:PLN02736 257 TK--FYP--SDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNavKE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 407 NTPLKRWLLEFAAKRKQAEVRSGiiRNDS-IWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQ 485
Cdd:PLN02736 333 SGGLKERLFNAAYNAKKQALENG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGM 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 486 TECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKG---EGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH 562
Cdd:PLN02736 411 TETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLH 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 563 TGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGI 642
Cdd:PLN02736 491 TGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGI 570
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57165412 643 E-GTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 719
Cdd:PLN02736 571 KyEDLKQLCNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYA 648
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
111-719 |
2.13e-178 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 522.35 E-value: 2.13e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 111 YDDARTMYQVFRRGLSISGNGPCLGFRKPKQpYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVEL 190
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVALREKEDGI-WQSLTWAEFAERVRALAAGLLALGVKP--GDRVAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 191 ACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAVLLLEHveRKETPGLKLIILMDPfeealkeRGQKCGVVI 270
Cdd:COG1022 84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEV--RDELPSLRHIVVLDP-------RGLRDDPRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 271 KSMQAVEDCGQE-NHQAPVP-----PQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekvIFPRQDDVLISF 344
Cdd:COG1022 155 LSLDELLALGREvADPAELEarraaVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLER----LPLGPGDRTLSF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 345 LPLAHMFERVIQSVVYCHGGRVGFfQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQAN--TPLKRWLLEFA---A 419
Cdd:COG1022 231 LPLAHVFERTVSYYALAAGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEeaGGLKRKLFRWAlavG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 420 KRKQAEVRSGiiRNDSIW--------DELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAG 491
Cdd:COG1022 310 RRYARARLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 492 CTFTTPGDWTSGHVGAPLPCNHIKLVDveelnywackgEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLP 571
Cdd:COG1022 387 ITVNRPGDNRIGTVGPPLPGVEVKIAE-----------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 572 AGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKaFLVGIVVPDPEVMPSWAQKRGIE-GTYADLC 650
Cdd:COG1022 456 DGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDGRP-FLAALIVPDFEALGEWAEENGLPyTSYAELA 534
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57165412 651 TNKDLKKAILEDMVRLGKesGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 719
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 ... |
141-706 |
8.17e-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: 474.39 E-value: 8.17e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 141 QPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADI 220
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEP--GDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 221 STVIVDKPqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhqapvppqpDDLSIVCF 300
Cdd:cd05907 79 KALFVEDP----------------------------------------------------------------DDLATIIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 301 TSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAHMFERV-IQSVVYCHGGRVGFFQgDIRLLSDD 379
Cdd:cd05907 95 TSGTTGRPKGVMLSHRNILSNALALAERLP----ATEGDRHLSFLPLAHVFERRaGLYVPLLAGARIYFAS-SAETLLDD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 380 MKALCPTIFPVVPRLLNRMYDKIFSQANTPLKRWLLEFAAkrkqaevrsgiirndsiwdelffnkiqaslGGCVRMIVTG 459
Cdd:cd05907 170 LSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV------------------------------GGRLRFAASG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 460 AAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDveelnywackgEGEICVRGPN 539
Cdd:cd05907 220 GAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPN 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 540 VFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLK 619
Cdd:cd05907 288 VMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDGRP 367
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 620 aFLVGIVVPDPEVMPSWAQKRGIEG-TYADLCTNKDLKKAILEDMVRLGKEsgLHSFEQVKAIHIHSDMFSVQNGLLTPT 698
Cdd:cd05907 368 -FLVALIVPDPEALEAWAEEHGIAYtDVAELAANPAVRAEIEAAVEAANAR--LSRYEQIKKFLLLPEPFTIENGELTPT 444
|
....*...
gi 57165412 699 LKAKRPEL 706
Cdd:cd05907 445 LKLKRPVI 452
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
142-703 |
2.18e-155 |
|
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: 460.14 E-value: 2.18e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 142 PYQWLSYQEVADRAEFLGSGL----LQHNCKactdqfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINT 217
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLvelgLKPGDK------VAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 218 ADISTVIVDkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhqapvpPQPDDLSI 297
Cdd:cd17639 76 TECSAIFTD---------------------------------------------------------------GKPDDLAC 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 298 VCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPrqDDVLISFLPLAHMFERVIQSVVYCHGGRVGFfqGDIRLLS 377
Cdd:cd17639 93 IMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGP--DDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLT 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 378 DDMKALC--------PTIFPVVPRLLNRMYDKIFSQANTP--LKRWLLEFAAKRKQAEVRSGIirnDS-IWDELFFNKIQ 446
Cdd:cd17639 169 DKSKRGCkgdltefkPTLMVGVPAIWDTIRKGVLAKLNPMggLKRTLFWTAYQSKLKALKEGP---GTpLLDELVFKKVR 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 447 ASLGGCVRMIVTGAAPASPTVLGFLrAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWA 526
Cdd:cd17639 246 AALGGRLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYST 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 527 CKGE--GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIR 604
Cdd:cd17639 325 DKPPprGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRS 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 605 SQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRG-IEGTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHI 683
Cdd:cd17639 405 NPLVNNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGvINSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVL 484
|
570 580
....*....|....*....|
gi 57165412 684 HSDMFSVQNGLLTPTLKAKR 703
Cdd:cd17639 485 LDEEWTPENGLVTAAQKLKR 504
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
142-719 |
1.24e-151 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 455.84 E-value: 1.24e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 142 PYQWLSYQEVADRAEFLGSGLLQ------HNCkactdqfiGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYII 215
Cdd:PLN02861 74 PYVWLTYKEVYDAAIRIGSAIRSrgvnpgDRC--------GIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFII 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 216 NTADISTVIVDKPQKAVLLleHVERKETPGLKLIILMDPFEEALKERGQKCGVVIKSMQAVEDCGQENHQAPvPPQPDDL 295
Cdd:PLN02861 146 NHAEVSIAFVQESKISSIL--SCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLDCELP-PKQKTDI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 296 SIVCFTSGTTGNPKGAMLTHGNVVADF---SGFLKVTEKVIfpRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGD 372
Cdd:PLN02861 223 CTIMYTSGTTGEPKGVILTNRAIIAEVlstDHLLKVTDRVA--TEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQGD 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 373 IRLLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWLLEFAAKRKQAEVRSGIIRNDS--IWDELFFNKIQAS 448
Cdd:PLN02861 301 IRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQkiSSGGMLRKKLFDFAYNYKLGNLRKGLKQEEAspRLDRLVFDKIKEG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 449 LGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCtFTTPGDWTS--GHVGAPLPCNHIKLVDVEELNYWA 526
Cdd:PLN02861 381 LGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGC-FTSIANVFSmvGTVGVPMTTIEARLESVPEMGYDA 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 527 CKG--EGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIR 604
Cdd:PLN02861 460 LSDvpRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSR 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 605 SQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGIEGTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIH 684
Cdd:PLN02861 539 CPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLE 618
|
570 580 590
....*....|....*....|....*....|....*
gi 57165412 685 SDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 719
Cdd:PLN02861 619 PNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYS 653
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
83-718 |
5.04e-151 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 454.48 E-value: 5.04e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 83 LMQSEEVEDSGGARRSVigsGPQLLTHYYDDA--------RTMYQVFRRGLSISGNGPCLGFR-----KPKQpYQWLSYQ 149
Cdd:PLN02614 8 IFQVEEGKEGSDGRPSV---GPVYRSIFAKDGfpnpiegmDSCWDVFRMSVEKYPNNPMLGRReivdgKPGK-YVWQTYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 150 EVADRAEFLGSGLlqHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDkpQ 229
Cdd:PLN02614 84 EVYDIVIKLGNSL--RSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVE--E 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 230 KAVLLLEHVERKETPGLKLIILMDPFEEALKERGQKCGVVIKSMQAVEDCGqENHQAPVP-PQPDDLSIVCFTSGTTGNP 308
Cdd:PLN02614 160 KKISELFKTCPNSTEYMKTVVSFGGVSREQKEEAETFGLVIYAWDEFLKLG-EGKQYDLPiKKKSDICTIMYTSGTTGDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 309 KGAMLTHGNVVADFSG---FLKVTEKVIfpRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALCP 385
Cdd:PLN02614 239 KGVMISNESIVTLIAGvirLLKSANAAL--TVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 386 TIFPVVPRLLNRMYDKIFSQANTP--LKRWLLEFAAKRKQAEVRSGI--IRNDSIWDELFFNKIQASLGGCVRMIVTGAA 461
Cdd:PLN02614 317 TIFCAVPRVLDRVYSGLQKKLSDGgfLKKFVFDSAFSYKFGNMKKGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 462 PASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDVEELNY--WACKGEGEICVRGP 538
Cdd:PLN02614 397 PLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELDMlGTVGPPVPNVDIRLESVPEMEYdaLASTPRGEICIRGK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 539 NVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSL 618
Cdd:PLN02614 477 TLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 619 KAFLVGIVVPDPEVMPSWAQKRGIEGTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPT 698
Cdd:PLN02614 556 ESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPT 635
|
650 660
....*....|....*....|
gi 57165412 699 LKAKRPELREYFKKQIEELY 718
Cdd:PLN02614 636 FKKKRPQLLKYYQSVIDEMY 655
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
113-718 |
1.43e-150 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 453.12 E-value: 1.43e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 113 DARTMYQVFRRGLSISGNGPCLGFRKPKQ----PYQWLSYQEVADRAEFLGSGLLQHNCKACTDqfIGVFAQNRPEWIIV 188
Cdd:PLN02430 40 DITTAWDIFSKSVEKYPDNKMLGWRRIVDgkvgPYMWKTYKEVYEEVLQIGSALRASGAEPGSR--VGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 189 ELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV-DKPQKAVLlleHVERKETPGLKLIILMDPFEEALKERGQKCG 267
Cdd:PLN02430 118 MEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVqDKKIKELL---EPDCKSAKRLKAIVSFTSVTEEESDKASQIG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 268 VVIKSMQAVEDCGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTEKVIfpRQDDVLISF 344
Cdd:PLN02430 195 VKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGvdlFMEQFEDKM--THDDVYLSF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 345 LPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWLLEFAAKRK 422
Cdd:PLN02430 273 LPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYKYK 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 423 QAEVRSGIIRNDS--IWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDW 500
Cdd:PLN02430 353 LAWMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEM 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 501 TS-GHVGAPLPCNHIKLVDVEELNY--WACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKI 577
Cdd:PLN02430 433 CMlGTVGAPAVYNELRLEEVPEMGYdpLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKI 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 578 IDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGIEGTYADLCTNKDLKK 657
Cdd:PLN02430 512 IDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKE 591
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57165412 658 AILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 718
Cdd:PLN02430 592 HILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMY 652
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
104-719 |
1.27e-132 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 407.97 E-value: 1.27e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 104 PQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRK--PKQ----------------PYQWLSYQEVADRAEFLGSGLLQ- 164
Cdd:PLN02387 47 PELVETPWEGATTLAALFEQSCKKYSDKRLLGTRKliSREfetssdgrkfeklhlgEYEWITYGQVFERVCNFASGLVAl 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 165 -HNckacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQ--KAVLLLEHVERk 241
Cdd:PLN02387 127 gHN----KEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQlkKLIDISSQLET- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 242 etpgLKLIILM-DPFEEALKERGQKCGVVIKSMQAVEDCGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVA 320
Cdd:PLN02387 202 ----VKRVIYMdDEGVDSDSSLSGSSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 321 DFSGFLKVTEKVifpRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFfqGDIRLLSD-----------DMKALCPTIFP 389
Cdd:PLN02387 278 TVAGVMTVVPKL---GKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDtsnkikkgtkgDASALKPTLMT 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 390 VVPRLLNRMYDKIFSQANTP--LKRWLLEFAAKRKQAEVR------SGIIRndSIWDELFFNKIQASLGGCVRMIVTGAA 461
Cdd:PLN02387 353 AVPAILDRVRDGVRKKVDAKggLAKKLFDIAYKRRLAAIEgswfgaWGLEK--LLWDALVFKKIRAVLGGRIRFMLSGGA 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 462 PASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKG---EGEICVRGP 538
Cdd:PLN02387 431 PLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLISDKpmpRGEIVIGGP 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 539 NVFKGYLKDPDRTKEA--LDSDG--WLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVH 614
Cdd:PLN02387 511 SVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIMVH 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 615 GDSLKAFLVGIVVPDPEVMPSWAQKRGIE-GTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNG 693
Cdd:PLN02387 591 ADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPAKIKLLPEPWTPESG 670
|
650 660
....*....|....*....|....*.
gi 57165412 694 LLTPTLKAKRPELREYFKKQIEELYS 719
Cdd:PLN02387 671 LVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
142-588 |
7.42e-126 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 380.89 E-value: 7.42e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 142 PYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADIS 221
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRALGVGK--GDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 222 TVIVDKPQKAVLLLEHVERKETPGLKLIILMDPFEEALKergqkcgvviksMQAVEDCGQENHQAPVPPQPDDLSIVCFT 301
Cdd:pfam00501 96 VLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEP------------LPEEAKPADVPPPPPPPPDPDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 302 SGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERV-IQSVVYCHGGRVGFFQGDIRL----L 376
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSlGLLGPLLAGATVVLPPGFPALdpaaL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 377 SDDMKALCPTIFPVVPRLLNRMydkifsqantplkrwlleFAAKRKQAEVRSGiirndsiwdelffnkiqaslggcVRMI 456
Cdd:pfam00501 244 LELIERYKVTVLYGVPTLLNML------------------LEAGAPKRALLSS-----------------------LRLV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 457 VTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDW---TSGHVGAPLPCNHIKLVDVEELNYWACKGEGEI 533
Cdd:pfam00501 283 LSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGEL 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 57165412 534 CVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLA 588
Cdd:pfam00501 363 CVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
88-718 |
7.44e-99 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 319.61 E-value: 7.44e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 88 EVEDSGGARRSVIGSGPQL--LTHYYDDARTMYQVFRRGLSISGNGPCLGFRKPK--------------QPY-------- 143
Cdd:PTZ00216 40 ETENASAIYRIAGVTDEEHerLRNEWYYGPNFLQRLERICKERGDRRALAYRPVErvekevvkdadgkeRTMevthfnet 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 144 QWLSYQEVADRAEFLGSGL----LQHNCKactdqfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTAD 219
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLaelgLTKGSN------VAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 220 iSTVIVDKPQKAVLLLEHVERKETPGLKLIILmdpfeEALKERGQKCGVVIKSMQAVEDCG---QENHQAPVPPQPDDLS 296
Cdd:PTZ00216 194 -CKAIVCNGKNVPNLLRLMKSGGMPNTTIIYL-----DSLPASVDTEGCRLVAWTDVVAKGhsaGSHHPLNIPENNDDLA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 297 IVCFTSGTTGNPKGAMLTHGNVVADFSGF-LKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFfqGDIRL 375
Cdd:PTZ00216 268 LIMYTSGTTGDPKGVMHTHGSLTAGILALeDRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 376 LSD-------DMKALCPTIFPVVPRLLNRMydKIFSQANTP----LKRWLLEFAAKRKQAEVRSGiiRNDSIWDELFFNK 444
Cdd:PTZ00216 346 LTDtfarphgDLTEFRPVFLIGVPRIFDTI--KKAVEAKLPpvgsLKRRVFDHAYQSRLRALKEG--KDTPYWNEKVFSA 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 445 IQASLGGCVRMIVTGAAPASPTVLGFLRAALGCqVYEGYGQTE--CTAGCTFTtpGDWTSGHVGAPLPCNHIKLVDVEEL 522
Cdd:PTZ00216 422 PRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTEtvCCGGIQRT--GDLEPNAVGQLLKGVEMKLLDTEEY 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 523 NYwACKGE--GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIEN 600
Cdd:PTZ00216 499 KH-TDTPEprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEA 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 601 IYIRSQPVAQ----IYVHGDslKAFLVGIVVPDPEVMPSWAQKRGIEGTYADLCTNKDLKKAILEDMVRLGKESGLHSFE 676
Cdd:PTZ00216 578 LYGQNELVVPngvcVLVHPA--RSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFE 655
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 57165412 677 QVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 718
Cdd:PTZ00216 656 IVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
141-704 |
2.36e-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: 261.52 E-value: 2.36e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 141 QPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADI 220
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKA--GEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 221 STVIVdkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqENHqapvppqPDDLSIVCF 300
Cdd:cd17640 79 VALVV--------------------------------------------------------END-------SDDLATIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 301 TSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFfqGDIRLLSDDM 380
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLLHQIRSLSDIVP----PQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDDL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 381 KALCPTIFPVVPRLLNRMYDKIFSQ--ANTPLKRWLLEFAAkrkqaevrsgiirndsiwdelffnkiqasLGGCVRMIVT 458
Cdd:cd17640 170 KRVKPHYIVSVPRLWESLYSGIQKQvsKSSPIKQFLFLFFL-----------------------------SGGIFKFGIS 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 459 GAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGP 538
Cdd:cd17640 221 GGGALPPHVDTFFEA-IGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGP 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 539 NVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSL 618
Cdd:cd17640 300 QVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQ 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 619 KaFLVGIVVPDPEVMPSWAQKRGI---EGTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFsVQNGLL 695
Cdd:cd17640 380 K-RLGALIVPNFEELEKWAKESGVklaNDRSQLLASKKVLKLYKNEIKDEISNRPGFKSFEQIAPFALLEEPF-IENGEM 457
|
....*....
gi 57165412 696 TPTLKAKRP 704
Cdd:cd17640 458 TQTMKIKRN 466
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
143-703 |
2.96e-79 |
|
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: 262.40 E-value: 2.96e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 143 YQWLSYQEVADRAEFLGSGLLQHNCKACTDqfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADIST 222
Cdd:cd05932 4 VVEFTWGEVADKARRLAAALRALGLEPGSK--IALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 223 VIVDKpqkavllLEHVERKE--TPGLKLIILMDPFEEALKERGqkcgvviksMQAVEDCGQENHQAPvPPQPDDLSIVCF 300
Cdd:cd05932 82 LFVGK-------LDDWKAMApgVPEGLISISLPPPSAANCQYQ---------WDDLIAQHPPLEERP-TRFPEQLATLIY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 301 TSGTTGNPKGAMLTHGNvvadFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDM 380
Cdd:cd05932 145 TSGTTGQPKGVMLTFGS----FAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTFVEDV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 381 KALCPTIFPVVPRLL----NRMYDKIFSQAntpLKRWLlefaakrkQAEVRSGIIRndsiwdelffNKIQASLG-GCVRM 455
Cdd:cd05932 221 QRARPTLFFSVPRLWtkfqQGVQDKIPQQK---LNLLL--------KIPVVNSLVK----------RKVLKGLGlDQCRL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 456 IVTGAAPASPTVLGFLRaALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDveelnywackgEGEICV 535
Cdd:cd05932 280 AGCGSAPVPPALLEWYR-SLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEILV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 536 RGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHG 615
Cdd:cd05932 348 RSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 616 DSLKAfLVGIVVPDPEVMPSwaqkrgiegtyADLCTNKDLKKAILEDMVRLGKEsgLHSFEQVKAIHIHSDMFSVQNGLL 695
Cdd:cd05932 428 SGLPA-PLALVVLSEEARLR-----------ADAFARAELEASLRAHLARVNST--LDSHEQLAGIVVVKDPWSIDNGIL 493
|
....*...
gi 57165412 696 TPTLKAKR 703
Cdd:cd05932 494 TPTLKIKR 501
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
138-718 |
2.59e-69 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 238.03 E-value: 2.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 138 KPKQPYQWLSYQEVADRAE-----FLGSGLLQHNCkactdqfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIR 212
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRqaakaFLKLGLERFHG-------VGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 213 YIINTADISTVIVDKPQKAVLLLEhvERKETPGLKLII-LMDPFEEalKERGQKcgvvikSMQAVEDCG-----QENHQA 286
Cdd:cd05933 74 YVAETSEANILVVENQKQLQKILQ--IQDKLPHLKAIIqYKEPLKE--KEPNLY------SWDEFMELGrsipdEQLDAI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 287 PVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQS-VVYCHGGR 365
Cdd:cd05933 144 ISSQKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIwLPIKVGGQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 366 VGFFQGDIR--LLSDDMKALCPTIFPVVPRLLNRMYDKI---FSQAnTPLKRWLLEFAaKRKQAEV-------RSGIIRN 433
Cdd:cd05933 224 VYFAQPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkavGAKS-GTLKRKIASWA-KGVGLETnlklmggESPSPLF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 434 DSIWDELFFNKIQASLG--GCVRMIvTGAAPASPTVLGFLrAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPC 511
Cdd:cd05933 302 YRLAKKLVFKKVRKALGldRCQKFF-TGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 512 NHIKLVDVEelnywaCKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGE 591
Cdd:cd05933 380 CKTKIHNPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGE 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 592 YVAPEKIENIYIRSQP-VAQIYVHGDSLKaFLVGIVV------PD---------PEVMpSWAQKRGIEGTY-ADLCTNKD 654
Cdd:cd05933 454 NVPPVPIEDAVKKELPiISNAMLIGDKRK-FLSMLLTlkcevnPEtgepldeltEEAI-EFCRKLGSQATRvSEIAGGKD 531
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57165412 655 LK--KAILEDMVRLGKESGLHSFEQVKAIHIHSDmFSVQNGLLTPTLKAKRPELREYFKKQIEELY 718
Cdd:cd05933 532 PKvyEAIEEGIKRVNKKAISNAQKIQKWVILEKD-FSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
117-630 |
1.07e-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: 227.00 E-value: 1.07e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 117 MYQVFRRGLSISGNGPCLGFRkpkqpYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYS 196
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG-----GRRLTYAELDARARRLAAALRALGVGP--GDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 197 MVVVPLYDTLGPGAIRYIINTADISTVIVdkpqkAVLLlehverketpglkliilmdpfeealkergqkcgvviksmqav 276
Cdd:COG0318 74 AVVVPLNPRLTAEELAYILEDSGARALVT-----ALIL------------------------------------------ 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 277 edcgqenhqapvppqpddlsivcFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAHMF---ER 353
Cdd:COG0318 107 -----------------------YTSGTTGRPKGVMLTHRNLLANAAAIAAALG----LTPGDVVLVALPLFHVFgltVG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 354 VIQSVVycHGGRV----GFfqgDIRLLSDDMKALCPTIFPVVPRLLNRMYDkifsqantplkrwllefAAKRKQAEVRSg 429
Cdd:COG0318 160 LLAPLL--AGATLvllpRF---DPERVLELIERERVTVLFGVPTMLARLLR-----------------HPEFARYDLSS- 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 430 iirndsiwdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGA 507
Cdd:COG0318 217 -----------------------LRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGR 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 508 PLPCNHIKLVDVE--ELnywACKGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIF 585
Cdd:COG0318 274 PLPGVEVRIVDEDgrEL---PPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-DGWLRTGDLGRLDEDGYLYIVGRKKDMI 349
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 57165412 586 KLAqGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFlvgiVVPDP 630
Cdd:COG0318 350 ISG-GENVYPAEVEEVLAAHPGVAEAAVvgvpdekWGERVVAF----VVLRP 396
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
146-696 |
2.48e-66 |
|
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: 229.65 E-value: 2.48e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLGSgllQHNCKACTD--QFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTV 223
Cdd:cd17632 68 ITYAELWERVGAVAA---AHDPEQPVRpgDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 224 IVDKPQKAV---LLLEHverketPGLKLIILMDPFEEALKER-----------GQKCGVVIKSMQAVEDCGQENHQAPVP 289
Cdd:cd17632 145 AVSAEHLDLaveAVLEG------GTPPRLVVFDHRPEVDAHRaalesarerlaAVGIPVTTLTLIAVRGRDLPPAPLFRP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 290 PQPDD-LSIVCFTSGTTGNPKGAMLTHgNVVADFsgFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGrVGF 368
Cdd:cd17632 219 EPDDDpLALLIYTSGSTGTPKGAMYTE-RLVATF--WLKVSSIQDIRPPASITLNFMPMSHIAGRISLYGTLARGG-TAY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 369 FQG--DIRLLSDDMKALCPTIFPVVPRLlnrmYDKIFSQANTPLKRWL-----LEFAAKRKQAEVRsgiirndsiwdelf 441
Cdd:cd17632 295 FAAasDMSTLFDDLALVRPTELFLVPRV----CDMLFQRYQAELDRRSvagadAETLAERVKAELR-------------- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 442 fnkiQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTtpgdwtSGHVGAPlPCNHIKLVDVEE 521
Cdd:cd17632 357 ----ERVLGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE--AGAVIL------DGVIVRP-PVLDYKLVDVPE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 522 LNYWACKG---EGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKI 598
Cdd:cd17632 424 LGYFRTDRphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARL 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 599 ENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMpswaqkrgiegtyaDLCTNKDLKKAILEDMVRLGKESGLHSFEQV 678
Cdd:cd17632 504 EAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDAL--------------AGEDTARLRAALAESLQRIAREAGLQSYEIP 569
|
570
....*....|....*...
gi 57165412 679 KAIHIHSDMFSVQNGLLT 696
Cdd:cd17632 570 RDFLIETEPFTIANGLLS 587
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
143-669 |
4.03e-65 |
|
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: 226.15 E-value: 4.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 143 YQWLSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADIST 222
Cdd:cd17641 9 WQEFTWADYADRVRAFALGLLALGVG--RGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 223 VIVDKPQKAVLLLEHveRKETPGLKLIILMDP------------FEEALKERGQkcgvvikSMQAVEDCGQENHQAPVpp 290
Cdd:cd17641 87 VIAEDEEQVDKLLEI--ADRIPSVRYVIYCDPrgmrkyddprliSFEDVVALGR-------ALDRRDPGLYEREVAAG-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 291 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKvifpRQDDVLISFLPLAHMFER---VIQSVVycHGGRVG 367
Cdd:cd17641 156 KGEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPL----GPGDEYVSVLPLPWIGEQmysVGQALV--CGFIVN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 368 FFQgDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWL--------LEFAAKRKQAEVRSGIIRNDS-I 436
Cdd:cd17641 230 FPE-EPETMMEDLREIGPTFVLLPPRVWEGIAADVRArmMDATPFKRFMfelgmklgLRALDRGKRGRPVSLWLRLASwL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 437 WDELFFNKIQASLG-GCVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTEcTAGCTFTTP-GDWTSGHVGAPLPCNHI 514
Cdd:cd17641 309 ADALLFRPLRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTE-LAGAYTVHRdGDVDPDTVGVPFPGTEV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 515 KLVDVeelnywackgeGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVA 594
Cdd:cd17641 387 RIDEV-----------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFS 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57165412 595 PEKIENIYIRSQPVAQIYVHGDSlKAFLVGIVVPDPEVMPSWAQKRGIE-GTYADLCTNKDLKKAILEDMVRLGKE 669
Cdd:cd17641 456 PQFIENKLKFSPYIAEAVVLGAG-RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKVNAS 530
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
146-703 |
4.01e-62 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 215.00 E-value: 4.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLgSGLLQHNCKACTDQfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd05914 8 LTYKDLADNIAKF-ALLLKINGVGTGDR-VALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 226 DKPqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhqapvppqpDDLSIVCFTSGTT 305
Cdd:cd05914 86 SDE----------------------------------------------------------------DDVALINYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 306 GNPKGAMLTHGNVVADFSGfLKVTEKVifpRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDI---RLLSDDMKA 382
Cdd:cd05914 102 GNSKGVMLTYRNIVSNVDG-VKEVVLL---GKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIpsaKIIALAFAQ 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 383 LCPTIfpVVPRLLNRMYDKIFSQANTPLKRWLLEFAAKrkqaevrsgIIRNDSIWdELFFNKIQASLGGCVRMIVTGAAP 462
Cdd:cd05914 178 VTPTL--GVPVPLVIEKIFKMDIIPKLTLKKFKFKLAK---------KINNRKIR-KLAFKKVHEAFGGNIKEFVIGGAK 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 463 ASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPlpcnhIKLVDVEELNYWACKGEGEICVRGPNVFK 542
Cdd:cd05914 246 INPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKV-----IDGVEVRIDSPDPATGEGEIIVRGPNVMK 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 543 GYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVA--QIYVHGDSLKA 620
Cdd:cd05914 320 GYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLesLVVVQEKKLVA 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 621 flvgIVVPDPEVMPSWAQKrgiegtyadlctNKDLKKAILEDmVRLGKESGLHSFEQVKAIHIHSDMFSVqngllTPTLK 700
Cdd:cd05914 400 ----LAYIDPDFLDVKALK------------QRNIIDAIKWE-VRDKVNQKVPNYKKISKVKIVKEEFEK-----TPKGK 457
|
...
gi 57165412 701 AKR 703
Cdd:cd05914 458 IKR 460
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
118-623 |
1.79e-58 |
|
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: 205.10 E-value: 1.79e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 118 YQVFRRGLSISGNGPCLGFRKpkqpyQWLSYQEVADRAEFLGSGLLQHNCKaCTDQfIGVFAQNRPEWIIVELACYTYSM 197
Cdd:cd05936 2 ADLLEEAARRFPDKTALIFMG-----RKLTYRELDALAEAFAAGLQNLGVQ-PGDR-VALMLPNCPQFPIAYFGALKAGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 198 VVVPLYDTLGPGAIRYIINTADISTVIVDkpqkavlllehverketpglkliilmDPFEEALKergqkcgvviksmqave 277
Cdd:cd05936 75 VVVPLNPLYTPRELEHILNDSGAKALIVA--------------------------VSFTDLLA----------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 278 dcGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIfpRQDDVLISFLPLAHMFErviQS 357
Cdd:cd05936 112 --AGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLL--EGDDVVLAALPLFHVFG---LT 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 358 VVYCHGGRVGFFQ------GDIRLLsDDMKALCPTIFPVVPRLLNRmydkifsqantplkrwLLEFAAKRKqaEVRSGIi 431
Cdd:cd05936 185 VALLLPLALGATIvliprfRPIGVL-KEIRKHRVTIFPGVPTMYIA----------------LLNAPEFKK--RDFSSL- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 432 rndsiwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT-SGHVGAPLP 510
Cdd:cd05936 245 ----------------------RLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRkPGSIGIPLP 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 511 CNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQG 590
Cdd:cd05936 303 GTEVKIVD-DDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGG 379
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 57165412 591 EYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLV 623
Cdd:cd05936 380 FNVYPREVEEVLYEHPAVAEAAVvgvpdpySGEAVKAFVV 419
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
146-640 |
3.02e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 205.91 E-value: 3.02e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGK-GDR-VAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 226 -------DKPQKAVL-LLEHVERKETP-GLKLIILMDPFEEALKergqkcgvviksmqavedCGQENHQAPvPPQPDDLS 296
Cdd:PRK07656 109 lglflgvDYSATTRLpALEHVVICETEeDDPHTEKMKTFTDFLA------------------AGDPAERAP-EVDPDDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 297 IVCFTSGTTGNPKGAMLTHGNV---VADFSGFLKVTEKvifprqDDVLISfLPLAHMFerviqsvvychGGRVGF----- 368
Cdd:PRK07656 170 DILFTSGTTGRPKGAMLTHRQLlsnAADWAEYLGLTEG------DRYLAA-NPFFHVF-----------GYKAGVnaplm 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 369 ----------FQGD--IRLLSDDMkalcPTIFPVVPRLLNRMYDkifsqantplkrwllefAAKRKQAEVRSgiirndsi 436
Cdd:PRK07656 232 rgatilplpvFDPDevFRLIETER----ITVLPGPPTMYNSLLQ-----------------HPDRSAEDLSS-------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 437 wdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGCTFTTPGD---WTSGHVGAPLPCN 512
Cdd:PRK07656 283 ----------------LRLAVTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIAGV 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 513 HIKLVDveELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGE 591
Cdd:PRK07656 347 ENKIVN--ELGEEVPVGEvGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IVGGF 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 57165412 592 YVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLV---GIVVPDPEVMpSWAQKR 640
Cdd:PRK07656 424 NVYPAEVEEVLYEHPAVAEAAVigvpderLGEVGKAYVVlkpGAELTEEELI-AYCREH 481
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
294-631 |
4.70e-58 |
|
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: 200.20 E-value: 4.70e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 294 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekvIFPRQDDVLISFLPLAHMFerVIQSVVYC--HGGRVGFFQG 371
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS----GGLTEGDVFLSTLPLFHIG--GLFGLLGAllAGGTVVLLPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 372 -DIRLLSDDMKALCPTIFPVVPRLLNRMydkifsqantplkrwllefaakRKQAEVRSgiiRNDSiwdelffnkiqaslg 450
Cdd:cd04433 75 fDPEAALELIEREKVTILLGVPTLLARL----------------------LKAPESAG---YDLS--------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 451 gCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT--SGHVGAPLPCNHIKLVDVEElNYWACK 528
Cdd:cd04433 115 -SLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDPDG-GELPPG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 529 GEGEICVRGPNVFKGYLKDPDRTkEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSQPV 608
Cdd:cd04433 193 EIGELVVRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPGV 270
|
330 340
....*....|....*....|...
gi 57165412 609 AQIYVHGdslkaflvgivVPDPE 631
Cdd:cd04433 271 AEAAVVG-----------VPDPE 282
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
146-623 |
3.98e-57 |
|
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: 202.06 E-value: 3.98e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLK--KGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 226 DKPQKAVLLLehVERKETPGLKlIILMDPFEEALKERGQkcgvviksMQAVEDCGQENHQAPVPPQ-PDDLSIVCFTSGT 304
Cdd:cd05911 89 DPDGLEKVKE--AAKELGPKDK-IIVLDDKPDGVLSIED--------LLSPTLGEEDEDLPPPLKDgKDDTAAILYSSGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 305 TGNPKGAMLTHGNVVADFSgFLKVTEKVIFPRqDDVLISFLPLAHMFErvIQSVVYC--HGGRV----GFFqgdirllSD 378
Cdd:cd05911 158 TGLPKGVCLSHRNLIANLS-QVQTFLYGNDGS-NDVILGFLPLYHIYG--LFTTLASllNGATViimpKFD-------SE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 379 DMKALCP----TIFPVVPRLLNRMydkifsqANTPLkrwllefaakrkqaevrsgiirndsiwdelfFNKIQASlggCVR 454
Cdd:cd05911 227 LFLDLIEkykiTFLYLVPPIAAAL-------AKSPL-------------------------------LDKYDLS---SLR 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 455 MIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEI 533
Cdd:cd05911 266 VILSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEI 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 534 CVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIyIRSQP------ 607
Cdd:cd05911 346 CVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAV-LLEHPgvadaa 423
|
490
....*....|....*...
gi 57165412 608 VAQIY--VHGDSLKAFLV 623
Cdd:cd05911 424 VIGIPdeVSGELPRAYVV 441
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
111-630 |
4.58e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 174.99 E-value: 4.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 111 YDDARTMYQVFRRGLSISGNGPCLGFRKPKqpyqwLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVEL 190
Cdd:PRK06187 2 QDYPLTIGRILRHGARKHPDKEAVYFDGRR-----TTYAELDERVNRLANALRALGVKK--GDRVAVFDWNSHEYLEAYF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 191 ACytySM---VVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlLLEHVE--RKETPGLKLIILMDPFEEALkergqk 265
Cdd:PRK06187 75 AV---PKigaVLHPINIRLKPEEIAYILNDAEDRVVLVDSE-----FVPLLAaiLPQLPTVRTVIVEGDGPAAP------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 266 CGVVIKSMQAVEDCGQENHQAPvPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVvadFSGFLKVTEKVIFpRQDDVLISFL 345
Cdd:PRK06187 141 LAPEVGEYEELLAAASDTFDFP-DIDENDAAAMLYTSGTTGHPKGVVLSHRNL---FLHSLAVCAWLKL-SRDDVYLVIV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 346 PLAHmferviqsvvyCHG---GRVGFFQG---------DIRLLSDDMKALCPTIFPVVPRLLNRMydkifSQANTPLKRW 413
Cdd:PRK06187 216 PMFH-----------VHAwglPYLALMAGakqviprrfDPENLLDLIETERVTFFFAVPTIWQML-----LKAPRAYFVD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 414 LlefaakrkqaevrSGIirndsiwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT 493
Cdd:PRK06187 280 F-------------SSL-----------------------RLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVS 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 494 FTTPGDWTSGH------VGAPLPCNHIKLVDvEELNYWACKGE--GEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGD 565
Cdd:PRK06187 324 VLPPEDQLPGQwtkrrsAGRPLPGVEARIVD-DDGDELPPDGGevGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGD 401
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57165412 566 IGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDP 630
Cdd:PRK06187 402 VGYIDEDGYLYITDRIKDVIISG-GENIYPRELEDA---------LYGHPAVAEVAVIG--VPDE 454
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
146-601 |
1.13e-41 |
|
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: 158.65 E-value: 1.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLGSgLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd05909 8 LTYRKLLTGAIALAR-KLAKMTKE--GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 226 DKPQKAVLLLEHVERKETPgLKLIILmdpfeEALKER---GQKCGVVIKSMQAVEDCGQENHQAPVppQPDDLSIVCFTS 302
Cdd:cd05909 85 SKQFIEKLKLHHLFDVEYD-ARIVYL-----EDLRAKiskADKCKAFLAGKFPPKWLLRIFGVAPV--QPDDPAVILFTS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 303 GTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAHMFerviqsvvychggrvGFFQGDIRLLSDDMKA 382
Cdd:cd05909 157 GSEGLPKGVVLSHKNLLANVEQITAIFD----PNPEDVVFGALPFFHSF---------------GLTGCLWLPLLSGIKV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 383 LC---PTIFPVVPRLLnrmYDK----IFSqanTPLkrwLLEFAAKRKQAEVRSGIirndsiwdelffnkiqaslggcvRM 455
Cdd:cd05909 218 VFhpnPLDYKKIPELI---YDKkatiLLG---TPT---FLRGYARAAHPEDFSSL-----------------------RL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 456 IVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEIC 534
Cdd:cd05909 266 VVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLL 345
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57165412 535 VRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENI 601
Cdd:cd05909 346 VRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDI 410
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
241-719 |
3.68e-40 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 157.96 E-value: 3.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 241 KETPGLKLIILMDPFE---------EALKERGQKCGvvIKSMQAVEDCGQENHQAPVPPQ-PDDLSIVCFTSGTTGNPKG 310
Cdd:PTZ00342 244 NDLSNELEDISLGPLEydkeklekiKDLKEKAKKLG--ISIILFDDMTKNKTTNYKIQNEdPDFITSIVYTSGTSGKPKG 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 311 AMLTHGNV------VADFSGFLKVTEKVIFprqddvliSFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALC 384
Cdd:PTZ00342 322 VMLSNKNLyntvvpLCKHSIFKKYNPKTHL--------SYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 385 PTIFPVVPRLLNRMYDKIFSQAN--TPLKRWLlefaAKRKQAEVRSGIIRNDSIWDELFFN---KIQASLGGCVRMIVTG 459
Cdd:PTZ00342 394 GNILAGVPKVFNRIYTNIMTEINnlPPLKRFL----VKKILSLRKSNNNGGFSKFLEGITHissKIKDKVNPNLEVILNG 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 460 AAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPG-DWTSGHVGAPL-PCNHIKLVDVEELNYWACKGEGEICVRG 537
Cdd:PTZ00342 470 GGKLSPKIAEELSVLLNVNYYQGYGLTE-TTGPIFVQHAdDNNTESIGGPIsPNTKYKVRTWETYKATDTLPKGELLIKS 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 538 PNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHG-D 616
Cdd:PTZ00342 549 DSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGdD 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 617 SLKAFLvGIVVPDPEVM------PSWAQKRGI-EGTYADLCTNKDLKKAILEDMVR-----LGKESGLHSFEQVKAIHIH 684
Cdd:PTZ00342 629 SMDGPL-AIISVDKYLLfkclkdDNMLESTGInEKNYLEKLTDETINNNIYVDYVKgkmleVYKKTNLNRYNIINDIYLT 707
|
490 500 510
....*....|....*....|....*....|....*...
gi 57165412 685 SDMFSVQNgLLTPTLKAKRPEL-REY--FKKQIEELYS 719
Cdd:PTZ00342 708 SKVWDTNN-YLTPTFKVKRFYVfKDYafFIDQVKKIYK 744
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
146-634 |
1.38e-39 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 151.67 E-value: 1.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLgSGLLQHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIv 225
Cdd:cd05941 12 ITYADLVARAARL-ANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 226 dkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhqapvppqpdDLSIVCFTSGTT 305
Cdd:cd05941 90 --------------------------------------------------------------------DPALILYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 306 GNPKGAMLTHGNVVADFSGFLKVTEKvifpRQDDVLISFLPLAHMFERV--IQSVVYChGGRV---GFFQGDIRLLSDDM 380
Cdd:cd05941 102 GRPKGVVLTHANLAANVRALVDAWRW----TEDDVLLHVLPLHHVHGLVnaLLCPLFA-GASVeflPKFDPKEVAISRLM 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 381 KALcpTIFPVVPRllnrMYDKIFS--QANTPLKRWLLEFAAKRkqaevrsgiirndsiwdelffnkiqaslggcVRMIVT 458
Cdd:cd05941 177 PSI--TVFMGVPT----IYTRLLQyyEAHFTDPQFARAAAAER-------------------------------LRLMVS 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 459 GAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTTP--GDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVR 536
Cdd:cd05941 220 GSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVR 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 537 GPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKK-HIFKlAQGEYVAPEKIENIyIRSQP-VAQIYVH 614
Cdd:cd05941 298 GPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEIERV-LLAHPgVSECAVI 375
|
490 500
....*....|....*....|...
gi 57165412 615 GDSLKAF---LVGIVVPDPEVMP 634
Cdd:cd05941 376 GVPDPDWgerVVAVVVLRAGAAA 398
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
121-630 |
2.10e-39 |
|
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: 151.22 E-value: 2.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 121 FRRGLSISGNGPCLGFRKpkqpyQWLSYQEVADRAEFLGSGLlQHNCKACTDQfIGVFAQNRPEWIIVELACYTYSMVVV 200
Cdd:cd17631 1 LRRRARRHPDRTALVFGG-----RSLTYAELDERVNRLAHAL-RALGVAKGDR-VAVLSKNSPEFLELLFAAARLGAVFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 201 PLYDTLGPGAIRYIINTADiSTVIVDkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcg 280
Cdd:cd17631 74 PLNFRLTPPEVAYILADSG-AKVLFD------------------------------------------------------ 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 281 qenhqapvppqpdDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekvIFPRQDDVLISFLPLAHMFE-RVIQSVV 359
Cdd:cd17631 99 -------------DLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAA----LDLGPDDVLLVVAPLFHIGGlGVFTLPT 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 360 YCHGGRV----GFFQGDIRLLSDDMKAlcpTIFPVVPRLLNRMydkifsqANTPLkrwllefaakrkqaevrsgiirnds 435
Cdd:cd17631 162 LLRGGTVvilrKFDPETVLDLIERHRV---TSFFLVPTMIQAL-------LQHPR------------------------- 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 436 iWDELFFnkiqASLggcvRMIVTGAAPASPTVLGFLRAAlGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPCNH 513
Cdd:cd17631 207 -FATTDL----SSL----RAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHRRklGSAGRPVFFVE 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 514 IKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYV 593
Cdd:cd17631 277 VRIVD-PDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFR-DGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENV 353
|
490 500 510
....*....|....*....|....*....|....*..
gi 57165412 594 APEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDP 630
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 ... |
272-601 |
6.86e-39 |
|
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: 150.85 E-value: 6.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 272 SMQAVEDCGQENHQAPVPPQ--PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifPRQDDVLISFLPLAH 349
Cdd:cd05904 135 SLSFSDLLFEADEAEPPVVVikQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSN--SDSEDVFLCVLPMFH 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 350 MFerviqsvvychgGRVGFFQGDIRL-----------LSDDMKALCP---TIFPVVPrllnrmydkifsqantPLkrwll 415
Cdd:cd05904 213 IY------------GLSSFALGLLRLgatvvvmprfdLEELLAAIERykvTHLPVVP----------------PI----- 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 416 eFAAKRKQAEVRSGIIRndsiwdelffnkiqaSLggcvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTF 494
Cdd:cd05904 260 -VLALVKSPIVDKYDLS---------------SL----RQIMSGAAPLGKELIeAFRAKFPNVDLGQGYGMTESTGVVAM 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 495 TTP---GDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLP 571
Cdd:cd05904 320 CFApekDRAKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDE 399
|
330 340 350
....*....|....*....|....*....|
gi 57165412 572 AGTLKIIDRKKHIFKLaQGEYVAPEKIENI 601
Cdd:cd05904 400 DGYLFIVDRLKELIKY-KGFQVAPAELEAL 428
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
145-708 |
2.81e-35 |
|
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: 140.14 E-value: 2.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 145 WLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVI 224
Cdd:cd05926 14 ALTYADLAELVDDLARQLAALGIKK--GDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 225 VDKpqkaVLLLEHVERKETPGLkliilmdpfeeALKERGQKCGVVIKSMQAVE----DCGQENHQAPVPPQPDDLSIVCF 300
Cdd:cd05926 92 TPK----GELGPASRAASKLGL-----------AILELALDVGVLIRAPSAESlsnlLADKKNAKSEGVPLPDDLALILH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 301 TSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvIFPrqDDVLISFLPLAHmferVIQSVVYC-----HGGRV----GFfqg 371
Cdd:cd05926 157 TSGTTGRPKGVPLTHRNLAASATNITNTYK--LTP--DDRTLVVMPLFH----VHGLVASLlstlaAGGSVvlppRF--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 372 DIRLLSDDMKALCPTIFPVVPRLLnrmydKIfsqantplkrwLLEFAAKRKQAEvrsgiirndsiwdelfFNKIqaslgg 451
Cdd:cd05926 226 SASTFWPDVRDYNATWYTAVPTIH-----QI-----------LLNRPEPNPESP----------------PPKL------ 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 452 cvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTP---GDWTSGHVGAPlpcNHIKLVDVEElnywacK 528
Cdd:cd05926 268 --RFIRSCSASLPPAVLEALEATFGAPVLEAYGMTE-AAHQMTSNPlppGPRKPGSVGKP---VGVEVRILDE------D 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 529 GE-------GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENI 601
Cdd:cd05926 336 GEilppgvvGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGV 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 602 YIRSQPVAQIYVHGdslkaflvgivVPDP---EVMPSWAQKRgiEGTYADlctnkdlKKAILEDMvrlgkESGLHSFEQV 678
Cdd:cd05926 415 LLSHPAVLEAVAFG-----------VPDEkygEEVAAAVVLR--EGASVT-------EEELRAFC-----RKHLAAFKVP 469
|
570 580 590
....*....|....*....|....*....|
gi 57165412 679 KAIHIhsdmfsVQNGLLTPTLKAKRPELRE 708
Cdd:cd05926 470 KKVYF------VDELPKTATGKIQRRKVAE 493
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
280-629 |
4.12e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 140.91 E-value: 4.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 280 GQENHQAPVP-PQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD-FSGFLKVTEkviFPRQDDVLISFLPLAHMF--ERVI 355
Cdd:PRK05605 205 GGDGSDVSHPrPTPDDVALILYTSGTTGKPKGAQLTHRNLFANaAQGKAWVPG---LGDGPERVLAALPMFHAYglTLCL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 356 QSVVYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLlnrmYDKIfsqantplkrwlLEFAAKRkqaevrsGIirnds 435
Cdd:PRK05605 282 TLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPL----YEKI------------AEAAEER-------GV----- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 436 iwdelffnkiqaSLGGcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECT---AGCTFTTpgDWTSGHVGAPLPCN 512
Cdd:PRK05605 334 ------------DLSG-VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpiiVGNPMSD--DRRPGYVGVPFPDT 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 513 HIKLVDVEELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGE 591
Cdd:PRK05605 399 EVRIVDPEDPDETMPDGEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELI-ITGGF 476
|
330 340 350
....*....|....*....|....*....|....*...
gi 57165412 592 YVAPEKIENIyirsqpVAQiyvHGDSLKAFLVGIVVPD 629
Cdd:PRK05605 477 NVYPAEVEEV------LRE---HPGVEDAAVVGLPRED 505
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
175-668 |
5.12e-34 |
|
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: 135.27 E-value: 5.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 175 IGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlllehVERKETPGLKLIILMDP 254
Cdd:TIGR01923 27 VALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL---------LEEKDFQADSLDRIEAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 255 FEEALKERGQKcgvviksmqavedcgqenhqapvppQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkVTEKVIF 334
Cdd:TIGR01923 98 GRYETSLSASF-------------------------NMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVG---SKENLGF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 335 PRQDDVLISfLPLAH------MFERVIQsvvychGGRVGFFQGDIRLLsDDMKALCPTIFPVVPRLLNRMYDKifSQANT 408
Cdd:TIGR01923 150 TEDDNWLLS-LPLYHisglsiLFRWLIE------GATLRIVDKFNQLL-EMIANERVTHISLVPTQLNRLLDE--GGHNE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 409 PLKRWLLefaakrkqaevrsgiirndsiwdelffnkiqaslGGcvrmivtGAAPASptvlgFLRAAL--GCQVYEGYGQT 486
Cdd:TIGR01923 220 NLRKILL----------------------------------GG-------SAIPAP-----LIEEAQqyGLPIYLSYGMT 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 487 E-CTAGCTFTTPGDWTSGHVGAPLPCNHIKL-VDVEElnywackGEGEICVRGPNVFKGYLkDPDRTKEALDSDGWLHTG 564
Cdd:TIGR01923 254 EtCSQVTTATPEMLHARPDVGRPLAGREIKIkVDNKE-------GHGEIMVKGANLMKGYL-YQGELTPAFEQQGWFNTG 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 565 DIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQiyvhgdslkAFLVGivVPDPEvmpsWAQKrgieg 644
Cdd:TIGR01923 326 DIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQE---------AVVVP--KPDAE----WGQV----- 384
|
490 500
....*....|....*....|....*.
gi 57165412 645 TYADLCTNKDLKKAILEDMV--RLGK 668
Cdd:TIGR01923 385 PVAYIVSESDISQAKLIAYLteKLAK 410
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
114-719 |
9.73e-34 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 139.22 E-value: 9.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 114 ARTMYQVFRRGLSISGNGPCLGFRKPKQPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACY 193
Cdd:PTZ00297 426 VRSLGEMWERSVTRHSTFRCLGQTSESGESEWLTYGTVDARARELGSGLLALGVRP--GDVIGVDCEASRNIVILEVACA 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 194 TYSMVVVPLydtLGPG-AIRYIINTADISTVIVDKPQKAVLLLEHVERKETpglklIILMDPFEEALKERGQK-CGVVIK 271
Cdd:PTZ00297 504 LYGFTTLPL---VGKGsTMRTLIDEHKIKVVFADRNSVAAILTCRSRKLET-----VVYTHSFYDEDDHAVARdLNITLI 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 272 SMQAVEdcgQENHQAPVPPQP--DDLSIVCFTSGTTGNPKGAML-----THGNVVADFSgFLKVTEKVIFPRQDDVLISF 344
Cdd:PTZ00297 576 PYEFVE---QKGRLCPVPLKEhvTTDTVFTYVVDNTTSASGDGLavvrvTHADVLRDIS-TLVMTGVLPSSFKKHLMVHF 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 345 LPLAHMFERVIQSVVYCHGGRVGffQGDIRLLSDDMKALCPTIFPVVPRLlnrmydkiFSQANTPLKR----------WL 414
Cdd:PTZ00297 652 TPFAMLFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSL--------FSTSRLQLSRanerysavysWL 721
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 415 LEfaakrKQAEVRSGII----RNDSIWDELFFNKIQASLGGCVRMIVTGAAPASPTV-----LGFLRAALGCQVYegygQ 485
Cdd:PTZ00297 722 FE-----RAFQLRSRLInihrRDSSLLRFIFFRATQELLGGCVEKIVLCVSEESTSFsllehISVCYVPCLREVF----F 792
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 486 TECTAGCTFTtpgdwtsghvGAPLPCNHIKLVDVEELNYWACKGEGEICVRGpnvfkgylkDPDRTKEAldsdgwlhtgd 565
Cdd:PTZ00297 793 LPSEGVFCVD----------GTPAPSLQVDLEPFDEPSDGAGIGQLVLAKKG---------EPRRTLPI----------- 842
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 566 IGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAfLVGIVVPDPEVMP-SWAQKRGIE- 643
Cdd:PTZ00297 843 AAQWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEfEWRQSHCMGe 921
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 644 -GTYADLCTNKDLKK----AILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 718
Cdd:PTZ00297 922 gGGPARQLGWTELVAyassLLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIERFY 1001
|
.
gi 57165412 719 S 719
Cdd:PTZ00297 1002 S 1002
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
245-603 |
2.61e-33 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 135.11 E-value: 2.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 245 GLKLIILMDPFEEALKERGQKCGVVIKSM-QAVEDC--------GQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTH 315
Cdd:PLN02246 122 GAKLIITQSCYVDKLKGLAEDDGVTVVTIdDPPEGClhfseltqADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTH 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 316 GNVVADfsgflkVTEKV------IFPRQDDVLISFLPLAHMFErvIQSVVYChGGRVG--------FfqgDIRLLSDDMK 381
Cdd:PLN02246 202 KGLVTS------VAQQVdgenpnLYFHSDDVILCVLPMFHIYS--LNSVLLC-GLRVGaailimpkF---EIGALLELIQ 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 382 ALCPTIFPVVPrllnrmydkifsqantPLkrwLLEFAakrKQAEVRSgiirndsiwDELffnkiqASlggcVRMIVTGAA 461
Cdd:PLN02246 270 RHKVTIAPFVP----------------PI---VLAIA---KSPVVEK---------YDL------SS----IRMVLSGAA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 462 PASPTVLGFLRAALGCQVY-EGYGQTE-------CTAgctFT-TPGDWTSGHVGAPLPCNHIKLVDVE---ELNYWACkg 529
Cdd:PLN02246 309 PLGKELEDAFRAKLPNAVLgQGYGMTEagpvlamCLA---FAkEPFPVKSGSCGTVVRNAELKIVDPEtgaSLPRNQP-- 383
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57165412 530 eGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYI 603
Cdd:PLN02246 384 -GEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAELEALLI 455
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
280-623 |
5.86e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 134.51 E-value: 5.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 280 GQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGfLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVV 359
Cdd:PRK05677 194 GAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQ-CRALMGSNLNEGCEILIAPLPLYHIYAFTFHCMA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 360 YCHGGRVGFfqgdirLLSDdmkalcPTIFPVVPRLLNRMYDKIFSQANTplkrwllEFAAkrkqaevrsgiIRNDSIWDE 439
Cdd:PRK05677 273 MMLIGNHNI------LISN------PRDLPAMVKELGKWKFSGFVGLNT-------LFVA-----------LCNNEAFRK 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 440 LFFNKIQASLGGcvRMIVTGAAPASptvlgfLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDv 519
Cdd:PRK05677 323 LDFSALKLTLSG--GMALQLATAER------WKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVID- 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 520 EELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIE 599
Cdd:PRK05677 394 DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVSGFNVYPNELE 472
|
330 340 350
....*....|....*....|....*....|..
gi 57165412 600 NIyIRSQP----VAQIYV----HGDSLKAFLV 623
Cdd:PRK05677 473 DV-LAALPgvlqCAAIGVpdekSGEAIKVFVV 503
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
288-623 |
6.92e-33 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 134.03 E-value: 6.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 288 VPPQ--PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPRQDDVLISfLPLAHMFERVIQSVVYCHGGr 365
Cdd:PRK08974 199 VKPElvPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGPLLHPGKELVVTA-LPLYHIFALTVNCLLFIELG- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 366 vgffqGDIRLLSDdmkalcPTIFPVVPRLLNRMYDKIFSQANTPLKRWLlefaakrkqaevrsgiirNDSIWDELFFNKI 445
Cdd:PRK08974 277 -----GQNLLITN------PRDIPGFVKELKKYPFTAITGVNTLFNALL------------------NNEEFQELDFSSL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 446 QASLGGcvrmivtgAAPASPTVLGFLRAALGCQVYEGYGQTECT---AGCTFTTPGdwTSGHVGAPLPCNHIKLVDvEEL 522
Cdd:PRK08974 328 KLSVGG--------GMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVNPYDLDY--YSGSIGLPVPSTEIKLVD-DDG 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 523 NYWACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIY 602
Cdd:PRK08974 397 NEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMI-LVSGFNVYPNEIEDVV 474
|
330 340
....*....|....*....|....*...
gi 57165412 603 IRSQPVAQIY-------VHGDSLKAFLV 623
Cdd:PRK08974 475 MLHPKVLEVAavgvpseVSGEAVKIFVV 502
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
280-630 |
8.81e-33 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 133.85 E-value: 8.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 280 GQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADF---SGFLKVTEKVifPRQDDVLISFLPLAHMFERVIQ 356
Cdd:PRK08751 195 GRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMqqaHQWLAGTGKL--EEGCEVVITALPLYHIFALTAN 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 357 SVVYCHGGrvgffqGDIRLLSDdmkalcPTIFPVVPRLLNRMYDKIFSQANTPLKRWLlefaakrkqaevrsgiirNDSI 436
Cdd:PRK08751 273 GLVFMKIG------GCNHLISN------PRDMPGFVKELKKTRFTAFTGVNTLFNGLL------------------NTPG 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 437 WDELFFNKIQASLGGcvRMIVTGAapasptVLGFLRAALGCQVYEGYGQTECT-AGCTFTTPGDWTSGHVGAPLPCNHIK 515
Cdd:PRK08751 323 FDQIDFSSLKMTLGG--GMAVQRS------VAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDAC 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 516 LVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAP 595
Cdd:PRK08751 395 IKD-DAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-LVSGFNVYP 472
|
330 340 350
....*....|....*....|....*....|....*....
gi 57165412 596 EKIENIYIRSQPVAQIYVHG----DSLKAFLVGIVVPDP 630
Cdd:PRK08751 473 NEIEDVIAMMPGVLEVAAVGvpdeKSGEIVKVVIVKKDP 511
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
147-607 |
2.32e-32 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 130.08 E-value: 2.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 147 SYQEVADRAEFLGSGLLQHnCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLyDTLGPGA-IRYIINTADISTVIV 225
Cdd:TIGR01733 1 TYRELDERANRLARHLRAA-GGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPL-DPAYPAErLAFILEDAGARLLLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 226 DKPqkavllleHVERKETPGLKLIILMDPFEEALkergqkcgvviksmqavEDCGQENHqAPVPPQPDDLSIVCFTSGTT 305
Cdd:TIGR01733 79 DSA--------LASRLAGLVLPVILLDPLELAAL-----------------DDAPAPPP-PDAPSGPDDLAYVIYTSGST 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 306 GNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPLAH------MFerviqsVVYCHGGRVgffqgdiRLLSDD 379
Cdd:TIGR01733 133 GRPKGVVVTHRSLVN----LLAWLARRYGLDPDDRVLQFASLSFdasveeIF------GALLAGATL-------VVPPED 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 380 MKAlcpTIFPVVPRLLNRMYDKIFSQANTPLKRWLLEfaakrkqaevrsgiirndsiwdelffnkiQASLGGCVRMIVTG 459
Cdd:TIGR01733 196 EER---DDAALLAALIAEHPVTVLNLTPSLLALLAAA-----------------------------LPPALASLRLVILG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 460 AAPASPTVLGFLRAALG-CQVYEGYGQTECTAGCT-FTTPGDWTSGHV----GAPLPCNHIKLVDvEELNYWACKGEGEI 533
Cdd:TIGR01733 244 GEALTPALVDRWRARGPgARLINLYGPTETTVWSTaTLVDPDDAPRESpvpiGRPLANTRLYVLD-DDLRPVPVGVVGEL 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 534 CVRGPNVFKGYLKDPDRTKEA-LDSDGWL-------HTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIyIRS 605
Cdd:TIGR01733 323 YIGGPGVARGYLNRPELTAERfVPDPFAGgdgarlyRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAA-LLR 400
|
..
gi 57165412 606 QP 607
Cdd:TIGR01733 401 HP 402
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
146-613 |
4.99e-32 |
|
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: 129.42 E-value: 4.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADIstviv 225
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGP--GDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 226 dkpqkavlllehverketpglKLIILMDPFeealkergqkcgvviksmqavedcGQENHQApvppQPDDLSIVCFTSGTT 305
Cdd:cd05903 75 ---------------------KVFVVPERF------------------------RQFDPAA----MPDAVALLLFTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 306 GNPKGAMLTHGNVVADFSGFLkvtEKVIFPRQDDVLISfLPLAHmferviqsvvycHGGRVGFFqgdirllsddmkaLCP 385
Cdd:cd05903 106 GEPKGVMHSHNTLSASIRQYA---ERLGLGPGDVFLVA-SPMAH------------QTGFVYGF-------------TLP 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 386 TIFPVvPRLLNRMYDK------------IFSQANTPLKRWLLEfaAKRKQAEVRSGIirndsiwdelffnkiqaslggcv 453
Cdd:cd05903 157 LLLGA-PVVLQDIWDPdkalalmrehgvTFMMGATPFLTDLLN--AVEEAGEPLSRL----------------------- 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 454 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGD----WTSGhvGAPLPCNHIKLVDvEELNYWACKG 529
Cdd:cd05903 211 RTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPedrrLYTD--GRPLPGVEIKVVD-DTGATLAPGV 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 530 EGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVA 609
Cdd:cd05903 288 EGELLSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVI 365
|
....
gi 57165412 610 QIYV 613
Cdd:cd05903 366 EAAV 369
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
292-615 |
1.02e-31 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 126.62 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSGF-LKVTEkvifprqDDVLISFLPLAHMFERVIqSVVYC--HGGRV 366
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVnnGYFIGErLGLTE-------QDRLCIPVPLFHCFGSVL-GVLACltHGATM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 367 GFFQgdirlLSDDMKAL--------C------PTIFPvvpRLLNRMydkifSQANTPLKRwllefaakrkqaeVRSGIIr 432
Cdd:cd05917 73 VFPS-----PSFDPLAVleaiekekCtalhgvPTMFI---AELEHP-----DFDKFDLSS-------------LRTGIM- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 433 ndsiwdelffnkiqaslggcvrmivtGAAPASPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGDWTS---GHVGAP 508
Cdd:cd05917 126 --------------------------AGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDSIEkrvNTVGRI 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 509 LPCNHIKLVDvEELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkL 587
Cdd:cd05917 180 MPHTEAKIVD-PEGGIVPPVGVpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-I 257
|
330 340
....*....|....*....|....*...
gi 57165412 588 AQGEYVAPEKIENIYIRSQPVAQIYVHG 615
Cdd:cd05917 258 RGGENIYPREIEEFLHTHPKVSDVQVVG 285
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
294-624 |
1.23e-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: 126.08 E-value: 1.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 294 DLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTEkvifprqDDVLISFLPLAHMFErviqsvvYCHGGRVGFFQ 370
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLraaAAWADCADLTE-------DDRYLIINPFFHTFG-------YKAGIVACLLT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 371 GdirllsddmkalcPTIFPV----VPRLLNRMYDKIFSQANTP--LKRWLLEFAAkRKQAEVRSgiirndsiwdelffnk 444
Cdd:cd17638 67 G-------------ATVVPVavfdVDAILEAIERERITVLPGPptLFQSLLDHPG-RKKFDLSS---------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 445 iqaslggcVRMIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGcTFTTPGD---WTSGHVGAPLPCNHIKLVDve 520
Cdd:cd17638 117 --------LRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVA-TMCRPGDdaeTVATTCGRACPGFEVRIAD-- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 521 elnywackgEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIEN 600
Cdd:cd17638 186 ---------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEG 255
|
330 340 350
....*....|....*....|....*....|.
gi 57165412 601 IYIRSQPVAQIYV-------HGDSLKAFLVG 624
Cdd:cd17638 256 ALAEHPGVAQVAVigvpderMGEVGKAFVVA 286
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
142-582 |
1.25e-31 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 130.09 E-value: 1.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 142 PYQWLSYQEVADRAEFLGSGLLQHNCKAcTDQFIGVFAQNRpEWIIVELACYTYSMVVVPLydtlGPGAIRyiintadis 221
Cdd:cd05906 36 SEEFQSYQDLLEDARRLAAGLRQLGLRP-GDSVILQFDDNE-DFIPAFWACVLAGFVPAPL----TVPPTY--------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 222 tvivDKPQKAVLLLEHVerKETPGLKLII----LMDPFEEALKERGQkCGVVIKSMQAVEDCGqENHQAPvPPQPDDLSI 297
Cdd:cd05906 101 ----DEPNARLRKLRHI--WQLLGSPVVLtdaeLVAEFAGLETLSGL-PGIRVLSIEELLDTA-ADHDLP-QSRPDDLAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 298 VCFTSGTTGNPKGAMLTHGNVVADFSGflKVTEKVIFPrqDDVLISFLPLAHmfervIQSVVYCHggrvgffQGDIRLLS 377
Cdd:cd05906 172 LMLTSGSTGFPKAVPLTHRNILARSAG--KIQHNGLTP--QDVFLNWVPLDH-----VGGLVELH-------LRAVYLGC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 378 DDMKALCPTIFPVVPRLLNRMyDKiFSQANTplkrWLLEFA-AK-RKQAEVRSgiirnDSIWDelffnkiqasLGGCVRM 455
Cdd:cd05906 236 QQVHVPTEEILADPLRWLDLI-DR-YRVTIT----WAPNFAfALlNDLLEEIE-----DGTWD----------LSSLRYL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 456 IVTGAAPASPTVLGFLRAALGCQVYE-----GYGQTECTAGCTFTTP---GDWTSGH----VGAPLPCNHIKLVDVEEln 523
Cdd:cd05906 295 VNAGEAVVAKTIRRLLRLLEPYGLPPdairpAFGMTETCSGVIYSRSfptYDHSQALefvsLGRPIPGVSMRIVDDEG-- 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57165412 524 ywACKGEGEIC---VRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkWLPAGTLKIIDRKK 582
Cdd:cd05906 373 --QLLPEGEVGrlqVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
286-632 |
1.30e-31 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 130.14 E-value: 1.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 286 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADF--------SGFLKvtekvifPRQDDVLISF--LPLAHMFERVI 355
Cdd:PRK07059 197 KPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqmeawlqPAFEK-------KPRPDQLNFVcaLPLYHIFALTV 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 356 QSVVYCHGGRVGFF---QGDIRLLSDDMKALCPTIFPVVPRLLNRMYdkifsqaNTPlkrwllEFaakrkqaevrsgiir 432
Cdd:PRK07059 270 CGLLGMRTGGRNILipnPRDIPGFIKELKKYQVHIFPAVNTLYNALL-------NNP------DF--------------- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 433 ndsiwDELFFNKIQASLGGcvrmivtGAAPASPTVLGFLRAAlGCQVYEGYG--QTECTAGCTFTTPGDWTsGHVGAPLP 510
Cdd:PRK07059 322 -----DKLDFSKLIVANGG-------GMAVQRPVAERWLEMT-GCPITEGYGlsETSPVATCNPVDATEFS-GTIGLPLP 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 511 CNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQG 590
Cdd:PRK07059 388 STEVSIRD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMI-LVSG 465
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 57165412 591 EYVAPEKIENIyIRSQP----VAQIYVH----GDSLKAFlvgIVVPDPEV 632
Cdd:PRK07059 466 FNVYPNEIEEV-VASHPgvleVAAVGVPdehsGEAVKLF---VVKKDPAL 511
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
147-631 |
5.55e-31 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 128.03 E-value: 5.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 147 SYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLgpgAIRYIINTADIST-VIV 225
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLK--QNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIY---NERELDHSLNISKpTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 226 DKPQKAVLLLEHVERKeTPGLKLIILMDPFEEAlkeRGQKCGVVIKSMQAVEDCGQENHQAPVPPQPDDLSIVCFTSGTT 305
Cdd:cd17642 121 FCSKKGLQKVLNVQKK-LKIIKTIIILDSKEDY---KGYQCLYTFITQNLPPGFNEYDFKPPSFDRDEQVALIMNSSGST 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 306 GNPKGAMLTHGNVVADFSGflkvTEKVIF---PRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGF---FQGD--IRLLS 377
Cdd:cd17642 197 GLPKGVQLTHKNIVARFSH----ARDPIFgnqIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLmykFEEElfLRSLQ 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 378 D---DMKALCPTIFPVVPR--LLNRmYD----KIFSQANTPLKRWLLEFAAKRkqaevrsgiirndsiwdelfFNkiqas 448
Cdd:cd17642 273 DykvQSALLVPTLFAFFAKstLVDK-YDlsnlHEIASGGAPLSKEVGEAVAKR--------------------FK----- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 449 lggcvrmivtgaapasptvLGFLRaalgcqvyEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACK 528
Cdd:cd17642 327 -------------------LPGIR--------QGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 529 GEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRsqpv 608
Cdd:cd17642 380 ERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQ---- 454
|
490 500
....*....|....*....|...
gi 57165412 609 aqiyvHGDSLKAFLVGIvvPDPE 631
Cdd:cd17642 455 -----HPKIFDAGVAGI--PDED 470
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
146-615 |
6.59e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 127.97 E-value: 6.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVV---PLYDT------LGPGAIRYII- 215
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQP--GDRVGIWAPNCAEWLLTQFATARIGAILVninPAYRAseleyaLGQSGVRWVIc 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 216 ----NTADISTVIVD-KPQKAVLLLEHVERKETPGLKLIILMDPFE-------EALKERGQkcGVvikSMQAVEDcgqen 283
Cdd:PRK12583 124 adafKTSDYHAMLQElLPGLAEGQPGALACERLPELRGVVSLAPAPppgflawHELQARGE--TV---SREALAE----- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 284 HQAPVppQPDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSG-FLKVTEKvifprqdDVLISFLPLAHMFERVIqSVVY 360
Cdd:PRK12583 194 RQASL--DRDDPINIQYTSGTTGFPKGATLSHHNILnnGYFVAeSLGLTEH-------DRLCVPVPLYHCFGMVL-ANLG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 361 C--HGGRVGF----FQGDIRLLSDDMKAlCPTIFPVvPRLLnrmydkiFSQANTPlKRWLLEFAAkrkqaeVRSGIIrnd 434
Cdd:PRK12583 264 CmtVGACLVYpneaFDPLATLQAVEEER-CTALYGV-PTMF-------IAELDHP-QRGNFDLSS------LRTGIM--- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 435 siwdelffnkiqaslggcvrmivtGAAPASPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGD-----WTSghVGAP 508
Cdd:PRK12583 325 ------------------------AGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSLQTTAADdlerrVET--VGRT 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 509 LPCNHIKLVDVEELNywACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkL 587
Cdd:PRK12583 379 QPHLEVKVVDPDGAT--VPRGEiGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMI-I 455
|
490 500
....*....|....*....|....*...
gi 57165412 588 AQGEYVAPEKIENIYIRSQPVAQIYVHG 615
Cdd:PRK12583 456 RGGENIYPREIEEFLFTHPAVADVQVFG 483
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
144-631 |
7.29e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 126.85 E-value: 7.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 144 QWlSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTV 223
Cdd:PRK09088 22 RW-TYAELDALVGRLAAVLRRRGCV--DGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 224 IVDKPQKAvlllehverketpglkliilmdpfeealkerGQKCGVVIKSMQAVEDCGQENHQAPVPPqpDDLSIVCFTSG 303
Cdd:PRK09088 99 LGDDAVAA-------------------------------GRTDVEDLAAFIASADALEPADTPSIPP--ERVSLILFTSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 304 TTGNPKGAMLTHGNVVADFSGFlKVTEKVifprqdDVLISFLPLAHMFERV--IQSV--VYCHGGRV----GFFQG-DIR 374
Cdd:PRK09088 146 TSGQPKGVMLSERNLQQTAHNF-GVLGRV------DAHSSFLCDAPMFHIIglITSVrpVLAVGGSIlvsnGFEPKrTLG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 375 LLSDdmKALCPTIFPVVPRLLNRmydkifsqantplkrwllefaakrkqaevrsgiIRNDSIWDELFFNKIQAslggcvr 454
Cdd:PRK09088 219 RLGD--PALGITHYFCVPQMAQA---------------------------------FRAQPGFDAAALRHLTA------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 455 mIVTGAAP-ASPTVLGFLraALGCQVYEGYGQTEctAGCTFTTPGDWT-----SGHVGAPLPCNHIKLVDVEELNYWAck 528
Cdd:PRK09088 257 -LFTGGAPhAAEDILGWL--DDGIPMVDGFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVVDDQGNDCPA-- 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 529 GE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIEniyirsqp 607
Cdd:PRK09088 330 GVpGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIE-------- 400
|
490 500
....*....|....*....|....
gi 57165412 608 vAQIYVHGDSLKAFLVGivVPDPE 631
Cdd:PRK09088 401 -AVLADHPGIRECAVVG--MADAQ 421
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
147-601 |
9.69e-31 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 127.56 E-value: 9.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 147 SYQEVADRAEFLGSGLLQHNCKACTdqfigVFAQNRPEW---IIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTV 223
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGD-----RVAFQLPGWcefTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 224 IVDKPQKAV--LLLEHVERKETPGLKLIILMDPFEEALKErgqkcgvvIKSMQAVEDcgQENHQAPVPPQPDDLSIVCFT 301
Cdd:PRK06087 126 FAPTLFKQTrpVDLILPLQNQLPQLQQIVGVDKLAPATSS--------LSLSQIIAD--YEPLTTAITTHGDELAAVLFT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 302 SGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifprQDDVLISFLPLAHmferviqSVVYCHGGRVGFFQGDIRLLSDDMK 381
Cdd:PRK06087 196 SGTEGLPKGVMLTHNNILASERAYCARLNLT----WQDVFMMPAPLGH-------ATGFLHGVTAPFLIGARSVLLDIFT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 382 AlcptifPVVPRLLNRmyDKI-FSQANTPLkrwllefaakrkqaevrsgiirndsIWDELFFNKIQASLGGCVRMIVTGA 460
Cdd:PRK06087 265 P------DACLALLEQ--QRCtCMLGATPF-------------------------IYDLLNLLEKQPADLSALRFFLCGG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 461 APASPTVLgflRAAL--GCQVYEGYGQTECTAGcTFTTPGD---WTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICV 535
Cdd:PRK06087 312 TTIPKKVA---RECQqrGIKLLSVYGSTESSPH-AVVNLDDplsRFMHTDGYAAAGVEIKVVD-EARKTLPPGCEGEEAS 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57165412 536 RGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENI 601
Cdd:PRK06087 387 RGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDI 451
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
294-631 |
2.78e-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. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 123.94 E-value: 2.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 294 DLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVTEKVIfpRQDDVLISFLPLAHM---FERVIQSVVycHGGRV---- 366
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLT--FAGYYSARRFGL--GEDDVYLTVLPLFHInaqAVSVLAALS--VGATLvllp 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 367 ----GFFQGDIRllsdDMKALCPTIFPVVPRLLnrmydkiFSQANTPlkrwllefaaKRKQAEVRsgiirndsiwdelff 442
Cdd:cd05934 156 rfsaSRFWSDVR----RYGATVTNYLGAMLSYL-------LAQPPSP----------DDRAHRLR--------------- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 443 nkiqaslggcvrmiVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEel 522
Cdd:cd05934 200 --------------AAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDD-- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 523 NYWACKGE-GEICVR---GPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKI 598
Cdd:cd05934 264 GQELPAGEpGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEV 341
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 57165412 599 ENIYIRSQPVAQIYVHG-------DSLKAFlvgIVVPDPE 631
Cdd:cd05934 342 ERAILRHPAVREAAVVAvpdevgeDEVKAV---VVLRPGE 378
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
183-630 |
4.83e-30 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 124.60 E-value: 4.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 183 PEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDkPQKAVLLLEHVERKETPGLkliilmdpfeEALKER 262
Cdd:PRK07514 64 PEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCD-PANFAWLSKIAAAAGAPHV----------ETLDAD 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 263 GQkcGVViksMQAVEDCGQEnhQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGN------VVADFSGFlkvtekvifpR 336
Cdd:PRK07514 133 GT--GSL---LEAAAAAPDD--FETVPRGADDLAAILYTSGTTGRSKGAMLSHGNllsnalTLVDYWRF----------T 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 337 QDDVLISFLPLAH---MFerVIQSVVYCHGGRVGFFQgdiRLLSDDMKALCP--TIFPVVPRLLNRMYdkifsqANTPLK 411
Cdd:PRK07514 196 PDDVLIHALPIFHthgLF--VATNVALLAGASMIFLP---KFDPDAVLALMPraTVMMGVPTFYTRLL------QEPRLT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 412 RwllEFAAKrkqaevrsgiirndsiwdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAG 491
Cdd:PRK07514 265 R---EAAAH--------------------------------MRLFISGSAPLLAETHREFQERTGHAILERYGMTE-TNM 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 492 CTfTTP--GDWTSGHVGAPLPCNHIKLVDVE---ELNywacKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGD 565
Cdd:PRK07514 309 NT-SNPydGERRAGTVGFPLPGVSLRVTDPEtgaELP----PGEiGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGD 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 566 IGKWLPAGTLKIIDRKKHIfkLAQGEY-VAPEKIENiYIRSQP-VAQIYVHGDSLKAF---LVGIVVPDP 630
Cdd:PRK07514 384 LGKIDERGYVHIVGRGKDL--IISGGYnVYPKEVEG-EIDELPgVVESAVIGVPHPDFgegVTAVVVPKP 450
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
146-635 |
3.54e-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: 121.10 E-value: 3.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACY----TYsmvvVPLYDTLGPGAIRYIINTADIS 221
Cdd:cd05930 13 LTYAELDARANRLARYLRERGVGP--GDLVAVLLERSLEMVVAILAVLkagaAY----VPLDPSYPAERLAYILEDSGAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 222 TVIVDkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhqapvppqPDDLSIVCFT 301
Cdd:cd05930 87 LVLTD-----------------------------------------------------------------PDDLAYVIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 302 SGTTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPLAH------MFerviqsVVYCHGGRVGFFQGDIRL 375
Cdd:cd05930 102 SGSTGKPKGVMVEHRGLVN----LLLWMQEAYPLTPGDRVLQFTSFSFdvsvweIF------GALLAGATLVVLPEEVRK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 376 LSDDMKALC----PTIFPVVPRLLNRMYDKIFSQANTPLkrwllefaakrkqaevrsgiirndsiwdelffnkiqaslgg 451
Cdd:cd05930 172 DPEALADLLaeegITVLHLTPSLLRLLLQELELAALPSL----------------------------------------- 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 452 cvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFT--TPGDWTSGHV--GAPLPCNHIKLVDvEELNYWA 526
Cdd:cd05930 211 --RLVLVGGEALPPDLVrRWRELLPGARLVNLYGPTEATVDATYYrvPPDDEEDGRVpiGRPIPNTRVYVLD-ENLRPVP 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 527 CKGEGEICVRGPNVFKGYLKDPDRTKEA-----LDSDGWLH-TGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIEN 600
Cdd:cd05930 288 PGVPGELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIELGEIEA 366
|
490 500 510
....*....|....*....|....*....|....*...
gi 57165412 601 IYIRSQPVAQIYV---HGDSLKAFLVGIVVPDPEVMPS 635
Cdd:cd05930 367 ALLAHPGVREAAVvarEDGDGEKRLVAYVVPDEGGELD 404
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
118-569 |
3.68e-29 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 122.91 E-value: 3.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 118 YQVFRRGLSISGNGPCLGFRKPKQPYQWLSYQEVADRAEFLGSGLLQHnckactdqfiGV--------FAQNRPEWIIVE 189
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRAL----------GVkkgdrvaiYLPNIPEAVIAM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 190 LACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVD----KPQKAVLLLEHVE--RKETPGLKLIILMD---------- 253
Cdd:COG0365 82 LACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITAdgglRGGKVIDLKEKVDeaLEELPSLEHVIVVGrtgadvpmeg 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 254 --PFEEALKERGQKCgvviksmqavedcgqenhqAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVTEK 331
Cdd:COG0365 162 dlDWDELLAAASAEF-------------------EPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYL----VHAATTAK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 332 VIF-PRQDDVL--------------ISFLPLAH-----MFERVIqsvVYCHGGRvgFFQgdirlLSDDMKalcPTIFPVV 391
Cdd:COG0365 219 YVLdLKPGDVFwctadigwatghsyIVYGPLLNgatvvLYEGRP---DFPDPGR--LWE-----LIEKYG---VTVFFTA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 392 PRLLnRMydkifsqantpLKRWLLEFAAKRKQAevrsgiirndsiwdelffnkiqaSLggcvRMIVTGAAPASPTVLGFL 471
Cdd:COG0365 286 PTAI-RA-----------LMKAGDEPLKKYDLS-----------------------SL----RLLGSAGEPLNPEVWEWW 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 472 RAALGCQVYEGYGQTECtaGCTFTTPGDWTS---GHVGAPLPCNHIKLVDvEELNywACKG--EGEICVRG--PNVFKGY 544
Cdd:COG0365 327 YEAVGVPIVDGWGQTET--GGIFISNLPGLPvkpGSMGKPVPGYDVAVVD-EDGN--PVPPgeEGELVIKGpwPGMFRGY 401
|
490 500
....*....|....*....|....*..
gi 57165412 545 LKDPDRTKEAL--DSDGWLHTGDIGKW 569
Cdd:COG0365 402 WNDPERYRETYfgRFPGWYRTGDGARR 428
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
144-640 |
7.20e-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: 120.86 E-value: 7.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 144 QWLSYQEVADRAEFLGSGLLQHNckACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLyDTLGPGA-IRYIINTADIST 222
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARG--VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPL-DPDYPADrLRYILEDAEPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 223 VIVDkpqkavlllehverketpglkliilmdpfeEALKERGQKCGVVIksMQAVEDCGQENHQAPVPPQPDDLSIVCFTS 302
Cdd:cd12116 88 VLTD------------------------------DALPDRLPAGLPVL--LLALAAAAAAPAAPRTPVSPDDLAYVIYTS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 303 GTTGNPKGAMLTHGNVVADFSGFlkvTEKVIFPRQDDVL--------IS----FLPLahmferviqsvvyCHGGRVGFFQ 370
Cdd:cd12116 136 GSTGRPKGVVVSHRNLVNFLHSM---RERLGLGPGDRLLavttyafdISllelLLPL-------------LAGARVVIAP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 371 GDI----RLLSDDMKALCPTIFpvvprllnrmydkifsQAnTP-LKRWLLefaakrkqaevrsgiirnDSIWDELffnki 445
Cdd:cd12116 200 RETqrdpEALARLIEAHSITVM----------------QA-TPaTWRMLL------------------DAGWQGR----- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 446 qASLggcvRMIVTGAApaSPTVLGFLRAALGCQVYEGYGQTECT--AGCTFTTPGDwTSGHVGAPLPCNHIKLVDvEELN 523
Cdd:cd12116 240 -AGL----TALCGGEA--LPPDLAARLLSRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLD-AALR 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 524 YWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH-------TGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPE 596
Cdd:cd12116 311 PVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQVKI-RGHRIELG 389
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 57165412 597 KIENIYIRSQPVAQ--IYVHGDSLKAFLVGIVVPDPEVMPSWAQKR 640
Cdd:cd12116 390 EIEAALAAHPGVAQaaVVVREDGGDRRLVAYVVLKAGAAPDAAALR 435
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
146-638 |
1.35e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 120.48 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAE-----FLGSGLLQHNCkactdqfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADI 220
Cdd:PRK06188 38 LTYGQLADRISryiqaFEALGLGTGDA-------VALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 221 STVIVDK---PQKAVLLLEHVerketPGLKLIILMDPFEEAlkergqkcgvviksmqavEDCGQENHQAPVPP-----QP 292
Cdd:PRK06188 111 STLIVDPapfVERALALLARV-----PSLKHVLTLGPVPDG------------------VDLLAAAAKFGPAPlvaaaLP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 293 DDLSIVCFTSGTTGNPKGAMLTHGNVV-------ADFSgflkvtekviFPRQddvlISFL---PLAH----MFERVIQ-- 356
Cdd:PRK06188 168 PDIAGLAYTGGTTGKPKGVMGTHRSIAtmaqiqlAEWE----------WPAD----PRFLmctPLSHaggaFFLPTLLrg 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 357 -SVVYCHGgrvgfFqgdirllsdDMKALCPTI--------FpVVPRLLNRmydkifsqantplkrwLLEFAAKRKqaevr 427
Cdd:PRK06188 234 gTVIVLAK-----F---------DPAEVLRAIeeqritatF-LVPTMIYA----------------LLDHPDLRT----- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 428 sgiiRNDSiwdelffnkiqaSLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHV-- 505
Cdd:PRK06188 278 ----RDLS------------SL----ETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPkr 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 506 ----GAPLPCNHIKLVDvEELNYWAcKGE-GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDR 580
Cdd:PRK06188 338 ltscGRPTPGLRVALLD-EDGREVA-QGEvGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDR 414
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57165412 581 KKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAflvgIVVPDPEVMPSWAQ 638
Cdd:PRK06188 415 KKDMI-VTGGFNVFPREVEDVLAEHPAVAQVAVigvpdekWGEAVTA----VVVLRPGAAVDAAE 474
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
280-623 |
1.42e-28 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 121.08 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 280 GQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKV------IFPRQDDVLISFLPLAHMFER 353
Cdd:PRK12492 194 GRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLgpdgqpLMKEGQEVMIAPLPLYHIYAF 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 354 VIQSVVYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLlnrmydkifsqaNTplkrwllEFAAKRKQAEVRSgiirn 433
Cdd:PRK12492 274 TANCMCMMVSGNHNVLITNPRDIPGFIKELGKWRFSALLGL------------NT-------LFVALMDHPGFKD----- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 434 dsiwdeLFFNKIQASLGGcvrmivtGAAPASPTVLGFlRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCN 512
Cdd:PRK12492 330 ------LDFSALKLTNSG-------GTALVKATAERW-EQLTGCTIVEGYGLTETSPVASTNPYGELARlGTVGIPVPGT 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 513 HIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEY 592
Cdd:PRK12492 396 ALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLI-IVSGFN 473
|
330 340 350
....*....|....*....|....*....|....*...
gi 57165412 593 VAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLV 623
Cdd:PRK12492 474 VYPNEIEDVVMAHPKVANCAAigvpderSGEAVKLFVV 511
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
114-582 |
1.56e-28 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 121.60 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 114 ARTMYQVFRRGLSISGNGPCLgfrkpkqpyqwlSYQEVADR---------AEFLG-----SGLLqHNCKACTDQFIGVFA 179
Cdd:PRK07529 24 PASTYELLSRAAARHPDAPAL------------SFLLDADPldrpetwtyAELLAdvtrtANLL-HSLGVGPGDVVAFLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 180 QNRPEWIIVELACYTYSmVVVPLYDTLGPGAIRYIINTADISTVIVDKP-------QKAVLLLEHVerketPGLKLIILM 252
Cdd:PRK07529 91 PNLPETHFALWGGEAAG-IANPINPLLEPEQIAELLRAAGAKVLVTLGPfpgtdiwQKVAEVLAAL-----PELRTVVEV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 253 D-------PFEEALKERGQKCGVVIKSMQA-VEDCGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD-FS 323
Cdd:PRK07529 165 DlarylpgPKRLAVPLIRRKAHARILDFDAeLARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANaWL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 324 GFLkvtekVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGR---VGFFQG--DIRLLSDDMK---ALCPTIFPVVPRLL 395
Cdd:PRK07529 245 GAL-----LLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAhvvLATPQGyrGPGVIANFWKiveRYRINFLSGVPTVY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 396 NRMydkifsqANTPlkrwllefaakrkqaevrsgiirndsiwdelffnkIQASLGGCVRMIVTGAAPASPTVLGFLRAAL 475
Cdd:PRK07529 320 AAL-------LQVP-----------------------------------VDGHDISSLRYALCGAAPLPVEVFRRFEAAT 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 476 GCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLVDVEEL-NYW--ACKGE-GEICVRGPNVFKGYLkDPDR 550
Cdd:PRK07529 358 GVRIVEGYGLTEATCVSSVNPPdGERRIGSVGLRLPYQRVRVVILDDAgRYLrdCAVDEvGVLCIAGPNVFSGYL-EAAH 436
|
490 500 510
....*....|....*....|....*....|..
gi 57165412 551 TKEALDSDGWLHTGDIGKWLPAGTLKIIDRKK 582
Cdd:PRK07529 437 NKGLWLEDGWLNTGDLGRIDADGYFWLTGRAK 468
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
198-635 |
3.21e-28 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 118.70 E-value: 3.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 198 VVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlLLEHVErketpgLKLIILMDPfeealkergqkcGVVIKsmqaVE 277
Cdd:cd05922 48 VFVPLNPTLKESVLRYLVADAGGRIVLADAG-----AADRLR------DALPASPDP------------GTVLD----AD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 278 DCGQENHQAP-VPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTEkvifprqDDVLISFLPLAhmfer 353
Cdd:cd05922 101 GIRAARASAPaHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSiaeYLGITA-------DDRALTVLPLS----- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 354 viqsvvYCHGGRV---GFFQGDIRLLS----------DDMKALCPTIFPVVP---RLLNRMydkIFSQANTPLKRWLLEF 417
Cdd:cd05922 169 ------YDYGLSVlntHLLRGATLVLTndgvlddafwEDLREHGATGLAGVPstyAMLTRL---GFDPAKLPSLRYLTQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 418 AAKRKQAEVRSgiirndsiwdelffnkiqaslggcvrmivtgaapasptvlgfLRAAL-GCQVYEGYGQTECTAGCTFTT 496
Cdd:cd05922 240 GGRLPQETIAR------------------------------------------LRELLpGAQVYVMYGQTEATRRMTYLP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 497 PG--DWTSGHVGAPLPCNHIklvDVEELNYWACK-GE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkWLPA 572
Cdd:cd05922 278 PEriLEKPGSIGLAIPGGEF---EILDDDGTPTPpGEpGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLA-RRDE 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57165412 573 -GTLKIIDRKKHIFKLAqGEYVAPEKIENIyIRSQP---VAQIYVHGDSLKAFLVGIVVPDPEVMPS 635
Cdd:cd05922 354 dGFLFIVGRRDRMIKLF-GNRISPTEIEAA-ARSIGliiEAAAVGLPDPLGEKLALFVTAPDKIDPK 418
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
146-631 |
3.01e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 116.60 E-value: 3.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLgSGLLQHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK08314 36 ISYRELLEEAERL-AGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 226 -----DKPQKAV--LLLEHV-------ERKETPGLKLIILMDpfEEALKERGQKCGVViksmqAVEDCGQENHQA-PVPP 290
Cdd:PRK08314 115 gselaPKVAPAVgnLRLRHVivaqysdYLPAEPEIAVPAWLR--AEPPLQALAPGGVV-----AWKEALAAGLAPpPHTA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 291 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD-FSGFLKVTEKVifprqDDVLISFLPLAHM--FERVIQSVVYChGGRVg 367
Cdd:PRK08314 188 GPDDLAVLPYTSGTTGVPKGCMHTHRTVMANaVGSVLWSNSTP-----ESVVLAVLPLFHVtgMVHSMNAPIYA-GATV- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 368 ffqgdirllsddmkalcpTIFP-----VVPRLLNRMydKIFSQANTPlkRWLLEFAAKRKQAEvrsgiiRNDSiwdelff 442
Cdd:PRK08314 261 ------------------VLMPrwdreAAARLIERY--RVTHWTNIP--TMVVDFLASPGLAE------RDLS------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 443 nkiqaSLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWT-SGHVGAPLPCNHIKLVDVEE 521
Cdd:PRK08314 306 -----SL----RYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTE-TMAQTHSNPPDRPkLQCLGIPTFGVDARVIDPET 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 522 LNYWACKGEGEICVRGPNVFKGYLKDPDRTKEA---LDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKI 598
Cdd:PRK08314 376 LEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMIN-ASGFKVWPAEV 454
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 57165412 599 ENIYIRSQPVAQIYV-------HGDSLKAFlvgiVVPDPE 631
Cdd:PRK08314 455 ENLLYKHPAIQEACViatpdprRGETVKAV----VVLRPE 490
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
144-631 |
3.32e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 116.11 E-value: 3.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 144 QWLSYQEVADRAEFLgSGLLQHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTV 223
Cdd:PRK06839 26 EEMTYKQLHEYVSKV-AAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 224 IVDKP-QKAVLLLEHVERKETPglkliilmdpfeealkergqkcgVVIKSMQAVEDCGQENHqapVPPQPDDLSIVCFTS 302
Cdd:PRK06839 105 FVEKTfQNMALSMQKVSYVQRV-----------------------ISITSLKEIEDRKIDNF---VEKNESASFIICYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 303 GTTGNPKGAMLTHGNVvadfsgFLKVTEKV--IFPRQDDVLISFLPLAHMferviqsvvychgGRVGFFQgdirllsddm 380
Cdd:PRK06839 159 GTTGKPKGAVLTQENM------FWNALNNTfaIDLTMHDRSIVLLPLFHI-------------GGIGLFA---------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 381 kalCPTIFP----VVPRLLNRmyDKIFSQANTplKRWLLEFAAKRKQAEVRSGIIRNDSIWDElffnkiqaslggcVRMI 456
Cdd:PRK06839 210 ---FPTLFAggviIVPRKFEP--TKALSMIEK--HKVTVVMGVPTIHQALINCSKFETTNLQS-------------VRWF 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 457 VTGAAPAS-PTVLGFLRAalGCQVYEGYGQTEcTAGCTFTTPGD---WTSGHVGAPLPCNHIKLVDvEELNYWACKGEGE 532
Cdd:PRK06839 270 YNGGAPCPeELMREFIDR--GFLFGQGFGMTE-TSPTVFMLSEEdarRKVGSIGKPVLFCDYELID-ENKNKVEVGEVGE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 533 ICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIyirsqpvaqIY 612
Cdd:PRK06839 346 LLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQV---------IN 414
|
490
....*....|....*....
gi 57165412 613 VHGDSLKAFLVGivVPDPE 631
Cdd:PRK06839 415 KLSDVYEVAVVG--RQHVK 431
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
294-613 |
3.73e-27 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 116.62 E-value: 3.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 294 DLSIVCFTSGTTGNPKGAMLTHGNVVADF-SGFLKVTEKVIfprQDDVLISFLPLAHMF--ERVIQSVVYCHGGRVGFFQ 370
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTHRNLVANLcSSLFSVGPEMI---GQVVTLGLIPFFHIYgiTGICCATLRNKGKVVVMSR 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 371 GDIRLLSDDMKALCPTIFPVVPrllnrmydkifsqantPLKRWLLEfaakrkqaevrsgiirnDSIWDELFFNKIQaslg 450
Cdd:PLN02330 262 FELRTFLNALITQEVSFAPIVP----------------PIILNLVK-----------------NPIVEEFDLSKLK---- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 451 gcVRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTagCTFTTPGDWTSGH-------VGAPLPCNHIKLVDVEEL 522
Cdd:PLN02330 305 --LQAIMTAAAPLAPELLtAFEAKFPGVQVQEAYGLTEHS--CITLTHGDPEKGHgiakknsVGFILPNLEVKFIDPDTG 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 523 NYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIY 602
Cdd:PLN02330 381 RSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAIL 459
|
330
....*....|.
gi 57165412 603 IRSQPVAQIYV 613
Cdd:PLN02330 460 LTHPSVEDAAV 470
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
290-638 |
4.12e-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: 114.37 E-value: 4.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 290 PQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF---LKVTEkvifprqDDVLISFLPLAHM--FERVIQSVVYchGG 364
Cdd:cd05912 74 VKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSalnLGLTE-------DDNWLCALPLFHIsgLSILMRSVIY--GM 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 365 RVGFFQG-DIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTPLKRWLLefaakrkqaevrsgiirndsiwdelffn 443
Cdd:cd05912 145 TVYLVDKfDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRCILL---------------------------- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 444 kiqaslggcvrmivtGAAPASPTVLGFLRAaLGCQVYEGYGQTE-CTAGCTFTtPGDWTS--GHVGAPLPCNHIKLVDVE 520
Cdd:cd05912 197 ---------------GGGPAPKPLLEQCKE-KGIPVYQSYGMTEtCSQIVTLS-PEDALNkiGSAGKPLFPVELKIEDDG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 521 ELNYwackGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIEN 600
Cdd:cd05912 260 QPPY----EVGEILLKGPNVTKGYLNRPDATEESFE-NGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEE 333
|
330 340 350
....*....|....*....|....*....|....*...
gi 57165412 601 IYIRSQPVAQIYVhgdslkaflVGIvvPDPEvmpsWAQ 638
Cdd:cd05912 334 VLLSHPAIKEAGV---------VGI--PDDK----WGQ 356
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
146-640 |
8.97e-27 |
|
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: 113.73 E-value: 8.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLGSGLlqHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd05935 2 LTYLELLEVVKKLASFL--SNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 226 DKPQkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhqapvppqpDDLSIVCFTSGTT 305
Cdd:cd05935 80 GSEL---------------------------------------------------------------DDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 306 GNPKGAMLTHGNVVADFSGFLKVTEKVifprQDDVLISFLPLAHM--FERVIQSVVYCHGGRVGFFQGDIRLLSDDMKAL 383
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQSAVWTGLT----PSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMARWDRETALELIEKY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 384 CPTIFPVVPRLLNRMydkifsqANTPlkrwllefaakrkqaevrsgiirndsiwdelffnKIQASLGGCVRMIVTGAAPA 463
Cdd:cd05935 173 KVTFWTNIPTMLVDL-------LATP----------------------------------EFKTRDLSSLKVLTGGGAPM 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 464 SPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKG 543
Cdd:cd05935 212 PPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKG 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 544 YLKDPDRTKEALDSDG---WLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYV------- 613
Cdd:cd05935 292 YWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVisvpder 370
|
490 500 510
....*....|....*....|....*....|...
gi 57165412 614 HGDSLKAFLVgiVVP------DPEVMPSWAQKR 640
Cdd:cd05935 371 VGEEVKAFIV--LRPeyrgkvTEEDIIEWAREQ 401
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
284-635 |
2.55e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 113.16 E-value: 2.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 284 HQAPVPPqPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifprQDDVLISFLPLAHMFE---------RV 354
Cdd:PRK07787 120 HRYPEPD-PDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWT----ADDVLVHGLPLFHVHGlvlgvlgplRI 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 355 IQSVVycHGGRvgfF--QGDIRLLSDDmkalcPTIFPVVPRllnrMYDKIfsqantplkrwllefAAKRKQAEVRSGiir 432
Cdd:PRK07787 195 GNRFV--HTGR---PtpEAYAQALSEG-----GTLYFGVPT----VWSRI---------------AADPEAARALRG--- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 433 ndsiwdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCN 512
Cdd:PRK07787 243 --------------------ARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 513 HIKLVDvEELNYWACKGE--GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDR------KKHI 584
Cdd:PRK07787 303 ETRLVD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGG 381
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 57165412 585 FKLAQGEyvapekIENIYIRSQPVAQIYVHG---DSLKAFLVGIVVPDPEVMPS 635
Cdd:PRK07787 382 YRIGAGE------IETALLGHPGVREAAVVGvpdDDLGQRIVAYVVGADDVAAD 429
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
132-630 |
2.97e-26 |
|
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: 113.68 E-value: 2.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 132 PCLGFRKPKQPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTY---SMVVVPLYDTLGp 208
Cdd:cd05921 12 TWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGLSA--ERPLLILSGNSIEHALMALAAMYAgvpAAPVSPAYSLMS- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 209 gairyiintADISTvivdkpqkavllLEHVERKETPGLKLIILMDPFEEALKERGQKCGVVIKSMQAVEDCGQEN----- 283
Cdd:cd05921 89 ---------QDLAK------------LKHLFELLKPGLVFAQDAAPFARALAAIFPLGTPLVVSRNAVAGRGAISfaela 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 284 HQAP---VPP-----QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekviFPRQDD---VLISFLPLAHMF- 351
Cdd:cd05921 148 ATPPtaaVDAafaavGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQT-----YPFFGEeppVLVDWLPWNHTFg 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 352 -ERVIQSVVYcHGGRV---------GFFQGDIRLLSDDMkalcPTIFPVVPrllnrmydkifsqantplKRWllefaakr 421
Cdd:cd05921 223 gNHNFNLVLY-NGGTLyiddgkpmpGGFEETLRNLREIS----PTVYFNVP------------------AGW-------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 422 kqaEVRSGIIRNDSIWDELFFNKiqaslggcVRMIVTGAAPASPTVLGFLRA----ALGCQV--YEGYGQTECTAGCTFT 495
Cdd:cd05921 272 ---EMLVAALEKDEALRRRFFKR--------LKLMFYAGAGLSQDVWDRLQAlavaTVGERIpmMAGLGATETAPTATFT 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 496 TPGDWTSGHVGAPLPCNHIKLVdveelnywACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWL----P 571
Cdd:cd05921 341 HWPTERSGLIGLPAPGTELKLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpddP 412
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57165412 572 AGTLKIIDRKKHIFKLAQGEYVA--PekieniyIRSQPVAQI--YVHgDSL-----KAFLVGIVVPDP 630
Cdd:cd05921 413 AKGLVFDGRVAEDFKLASGTWVSvgP-------LRARAVAACapLVH-DAVvagedRAEVGALVFPDL 472
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
187-599 |
7.51e-26 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 114.25 E-value: 7.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 187 IVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKpqkavlllEHVERKETPGLKLIILMDP---FEEALKER- 262
Cdd:PRK08633 680 LANLALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVITSR--------KFLEKLKNKGFDLELPENVkviYLEDLKAKi 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 263 --GQKC--GVVIKSMQAVEDCGQENHqapvPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgfLKVTEKVIFPRQD 338
Cdd:PRK08633 752 skVDKLtaLLAARLLPARLLKRLYGP----TFKPDDTATIIFSSGSEGEPKGVMLSHHNILSN----IEQISDVFNLRND 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 339 DVLISFLPLAHMFERVIQ---------SVVYcH-----GGRVGffqgdirLLSDDMKA--LC--PTIFpvvprllnRMYd 400
Cdd:PRK08633 824 DVILSSLPFFHSFGLTVTlwlpllegiKVVY-HpdptdALGIA-------KLVAKHRAtiLLgtPTFL--------RLY- 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 401 kifsqantplkrwllefaakrkqaevrsgiIRNDSIWDELFfnkiqASLggcvRMIVTGAAPASPTVLGFLRAALGCQVY 480
Cdd:PRK08633 887 ------------------------------LRNKKLHPLMF-----ASL----RLVVAGAEKLKPEVADAFEEKFGIRIL 927
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 481 EGYGQTECTAGCTFTTP-----GDWT-----SGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDR 550
Cdd:PRK08633 928 EGYGATETSPVASVNLPdvlaaDFKRqtgskEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEK 1007
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 57165412 551 TKEAL---DSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIE 599
Cdd:PRK08633 1008 TAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIG-GEMVPLGAVE 1058
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
286-638 |
9.05e-26 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 112.24 E-value: 9.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 286 APVPPQpDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKV-TEKVIFPRQDDVLISFLPLAHMFerviqsvvychgG 364
Cdd:PLN02574 192 KPVIKQ-DDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFeASQYEYPGSDNVYLAALPMFHIY------------G 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 365 RVGFFQGDIRL-----------LSDDMKAL---CPTIFPVVPRLLNRMYDKIFSQANTPLKrwllefaakrkqaevrsgi 430
Cdd:PLN02574 259 LSLFVVGLLSLgstivvmrrfdASDMVKVIdrfKVTHFPVVPPILMALTKKAKGVCGEVLK------------------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 431 irndsiwdelffnkiqaslggCVRMIVTGAAPAS-PTVLGFLRAALGCQVYEGYGQTECTAGCT--FTTPGDWTSGHVGA 507
Cdd:PLN02574 320 ---------------------SLKQVSCGAAPLSgKFIQDFVQTLPHVDFIQGYGMTESTAVGTrgFNTEKLSKYSSVGL 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 508 PLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKL 587
Cdd:PLN02574 379 LAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY 458
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 57165412 588 aQGEYVAPEKIENIYIrSQP----VAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQ 638
Cdd:PLN02574 459 -KGFQIAPADLEAVLI-SHPeiidAAVTAVPDKECGEIPVAFVVRRQGSTLSQEA 511
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
144-640 |
9.24e-26 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 114.18 E-value: 9.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 144 QWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELA------CYtysmvvVPLyDTLGPGA-IRYIIN 216
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALGVGP--GDLVGVCLERSLEMVVALLAvlkagaAY------VPL-DPAYPAErLAYMLE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 217 TADISTVIVDkpqkavlllehverketpglkliilmdpfeEALKERGQKCGVVIKSMQAVEDCGQENHQAPVPPQPDDLS 296
Cdd:COG1020 571 DAGARLVLTQ------------------------------SALAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLA 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 297 IVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTEkvifprQDDVL----ISF--------LPLahmferviqsvvyC 361
Cdd:COG1020 621 YVIYTSGSTGRPKGVMVEHRALVnllAWMQRRYGLGP------GDRVLqfasLSFdasvweifGAL-------------L 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 362 HGGRVGFFQGDIRLLSDDMKALC----PTIFPVVPRLLNRMYDkifsqantplkrwllefAAKRKQAEVRsgiirndsiw 437
Cdd:COG1020 682 SGATLVLAPPEARRDPAALAELLarhrVTVLNLTPSLLRALLD-----------------AAPEALPSLR---------- 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 438 delffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF--TTPGDWTSGHV--GAPLPCNH 513
Cdd:COG1020 735 ----------------LVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYyeVTPPDADGGSVpiGRPIANTR 798
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 514 IKLVDvEELN---YWACkgeGEICVRGPNVFKGYLKDPDRTKEA-----LDSDG--WLHTGDIGKWLPAGTLKIIDRKKH 583
Cdd:COG1020 799 VYVLD-AHLQpvpVGVP---GELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNLEFLGRADD 874
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57165412 584 ifklaQ----------GEyvapekIENIyIRSQP-VAQIYV--HGDSL-KAFLVGIVVPDPEVMPSWAQKR 640
Cdd:COG1020 875 -----QvkirgfrielGE------IEAA-LLQHPgVREAVVvaREDAPgDKRLVAYVVPEAGAAAAAALLR 933
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
137-594 |
9.56e-26 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 112.66 E-value: 9.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 137 RKPKQPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPL---YDTLG--PGAI 211
Cdd:PRK08180 61 RGADGGWRRLTYAEALERVRAIAQALLDRGLSA--ERPLMILSGNSIEHALLALAAMYAGVPYAPVspaYSLVSqdFGKL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 212 RYIINTADISTVIVDKPQK-----AVLLLEHVE----RKETPGLKLIilmdPFEEALKERGQkcGVVIKSMQAVedcgqe 282
Cdd:PRK08180 139 RHVLELLTPGLVFADDGAAfaralAAVVPADVEvvavRGAVPGRAAT----PFAALLATPPT--AAVDAAHAAV------ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 283 nhqapvppQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekVIFPRQDD-VLISFLPLAHMF-ERVIQSVVY 360
Cdd:PRK08180 207 --------GPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQT---FPFLAEEPpVLVDWLPWNHTFgGNHNLGIVL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 361 CHGGR---------VGFFQGDIRLLsddmKALCPTIFPVVPRLlnrmydkifsqantplkrWLLEFAAKRKQAEVRsgii 431
Cdd:PRK08180 276 YNGGTlyiddgkptPGGFDETLRNL----REISPTVYFNVPKG------------------WEMLVPALERDAALR---- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 432 rndsiwdELFFNKiqaslggcVRMIVTGAAPASPTVLGFL----RAALGCQVY--EGYGQTECTAGCTFTTPGDWTSGHV 505
Cdd:PRK08180 330 -------RRFFSR--------LKLLFYAGAALSQDVWDRLdrvaEATCGERIRmmTGLGMTETAPSATFTTGPLSRAGNI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 506 GAPLPCNHIKLVDVEelnywackGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWL----PAGTLKIIDRK 581
Cdd:PRK08180 395 GLPAPGCEVKLVPVG--------GKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVdpadPERGLMFDGRI 466
|
490
....*....|...
gi 57165412 582 KHIFKLAQGEYVA 594
Cdd:PRK08180 467 AEDFKLSSGTWVS 479
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
146-615 |
1.30e-25 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 111.21 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLAALGVK--KGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLIT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 226 DkpqkavlllehverketpglkliilmDPFEEALKERGQkcgVVIKSMQAvedcGQENHQAPVPPQP-DDLSIVCFTSGT 304
Cdd:PRK03640 106 D--------------------------DDFEAKLIPGIS---VKFAELMN----GPKEEAEIQEEFDlDEVATIMYTSGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 305 TGNPKGAMLTHGNVVADFSGF---LKVTEKvifprqDDVLISfLPLAHM--FERVIQSVVYchGGRV----GFFQGDI-R 374
Cdd:PRK03640 153 TGKPKGVIQTYGNHWWSAVGSalnLGLTED------DCWLAA-VPIFHIsgLSILMRSVIY--GMRVvlveKFDAEKInK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 375 LLSDDMKalcpTIFPVVPRLLNRMYDKIfSQANTPlkrwllefaakrkqaevrsgiirnDSiwdelffnkiqaslggcVR 454
Cdd:PRK03640 224 LLQTGGV----TIISVVSTMLQRLLERL-GEGTYP------------------------SS-----------------FR 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 455 MIVTGAAPASPTVLGFLRAAlGCQVYEGYGQTEcTAGCTFTTPGDWTS---GHVGAPL-PCNhIKLVDveELNYWACKGE 530
Cdd:PRK03640 258 CMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLfPCE-LKIEK--DGVVVPPFEE 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 531 GEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQ 610
Cdd:PRK03640 333 GEIVVKGPNVTKGYLNREDATRETFQ-DGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPGVAE 410
|
....*
gi 57165412 611 IYVHG 615
Cdd:PRK03640 411 AGVVG 415
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
145-567 |
1.78e-25 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 111.18 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 145 WLSYQEVADRAEFLGSGLLQHNckACTDQFIGVFAQNrPEWIIVELACYTYSMVVVPLYDTLGPGA---IRYIINTADIS 221
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAVG--KPGDRVLLLAPPG-LDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 222 TVIVDKPQKAvLLLEHVERKETPGLKLIILMDPFEEALKERGQkcgvviksmqavedcgqenhqaPVPPQPDDLSIVCFT 301
Cdd:cd05931 101 VVLTTAAALA-AVRAFAASRPAAGTPRLLVVDLLPDTSAADWP----------------------PPSPDPDDIAYLQYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 302 SGTTGNPKGAMLTHGNVVADFSGFLkvteKVIFPRQDDVLISFLPLAH---MFERVIQSVVYchGGRVGFFQgdirllsd 378
Cdd:cd05931 158 SGSTGTPKGVVVTHRNLLANVRQIR----RAYGLDPGDVVVSWLPLYHdmgLIGGLLTPLYS--GGPSVLMS-------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 379 dmkalcPTIFpvvprlLNRmydkifsqantPLkRWL-----------------LEFAAKRKQAEVRSGIirndsiwdELf 441
Cdd:cd05931 224 ------PAAF------LRR-----------PL-RWLrlisryratisaapnfaYDLCVRRVRDEDLEGL--------DL- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 442 fnkiqaslgGCVRMIVTGAAPASPTVL----------GFLRAAlgcqVYEGYGQTECTAGCTFTTPG----------DWT 501
Cdd:cd05931 271 ---------SSWRVALNGAEPVRPATLrrfaeafapfGFRPEA----FRPSYGLAEATLFVSGGPPGtgpvvlrvdrDAL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 502 SGHV----------------GAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKE------ALDSDG 559
Cdd:cd05931 338 AGRAvavaaddpaarelvscGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaATDEGG 417
|
....*...
gi 57165412 560 WLHTGDIG 567
Cdd:cd05931 418 WLRTGDLG 425
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
181-623 |
1.99e-25 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 109.73 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 181 NRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKpqkavlllehverketpglkliilmdpfeealk 260
Cdd:cd05972 34 RVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA--------------------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 261 ergqkcgvviksmqavedcgqenhqapvppqpDDLSIVCFTSGTTGNPKGAMLTHG---NVVADFSGFLKVTEKVIFPRQ 337
Cdd:cd05972 81 --------------------------------EDPALIYFTSGTTGLPKGVLHTHSyplGHIPTAAYWLGLRPDDIHWNI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 338 DD------VLISFL-PLAHMFerviqSVVYCHGGRVgffqgdirllsDDMKALcptifpvvpRLLNRMYDKIFSQANTPL 410
Cdd:cd05972 129 ADpgwakgAWSSFFgPWLLGA-----TVFVYEGPRF-----------DAERIL---------ELLERYGVTSFCGPPTAY 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 411 KRWLLEFAAKRKQAEVRSgiirndsiwdelffnkiqaslggcvrmIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTA 490
Cdd:cd05972 184 RMLIKQDLSSYKFSHLRL---------------------------VVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGL 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 491 GCTFTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNV--FKGYLKDPDRTKEALdSDGWLHTGDIGK 568
Cdd:cd05972 237 TVGNFPDMPVKPGSMGRPTPGYDVAIID-DDGRELPPGEEGDIAIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDRAY 314
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57165412 569 WLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLV 623
Cdd:cd05972 315 RDEDGYFWFVGRADDIIK-SSGYRIGPFEVESALLEHPAVAEAAVvgspdpvRGEVVKAFVV 375
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
289-629 |
3.04e-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: 109.32 E-value: 3.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 289 PPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPLAhmFERVIQSV--VYCHGGRV 366
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLN----YVSQPPARLDVGPGSRVAQVLSIA--FDACIGEIfsTLCNGGTL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 367 gFFQGDIRLLSDDMKALcpTIFPVVPRLLNRMYDKIFSQantplkrwllefaakrkqaevrsgiirndsiwdelffnkiq 446
Cdd:cd17653 175 -VLADPSDPFAHVARTV--DALMSTPSILSTLSPQDFPN----------------------------------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 447 aslggcVRMIVTGAAPASPTVLGflRAALGCQVYEGYGQTECTAGCTFT--TPGDWTsgHVGAPLPCNHIKLVDvEELNY 524
Cdd:cd17653 211 ------LKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTelLPGQPV--TIGKPIPNSTCYILD-ADLQP 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 525 WACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH------TGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKI 598
Cdd:cd17653 280 VPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPgsrmyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEI 358
|
330 340 350
....*....|....*....|....*....|....
gi 57165412 599 ENIYIRSQPVAQ---IYVHGDSLKAFlvgiVVPD 629
Cdd:cd17653 359 EEVVLQSQPEVTqaaAIVVNGRLVAF----VTPE 388
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
181-623 |
6.70e-25 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 109.39 E-value: 6.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 181 NRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDkpQKAVLLLEHVERKETPGLKLIILMDPFEEALK 260
Cdd:PRK08008 71 NCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTS--AQFYPMYRQIQQEDATPLRHICLTRVALPADD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 261 ergqkcGVV----IKSMQAVEDCGQenhqapVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVTEKVIfpR 336
Cdd:PRK08008 149 ------GVSsftqLKAQQPATLCYA------PPLSTDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYYSAWQCAL--R 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 337 QDDVLISFLPLAHMFerviqsvvychggrvgfFQgdirllsddmkalCPTIFPVvprllnrmydkiFSQANTPLkrwLLE 416
Cdd:PRK08008 213 DDDVYLTVMPAFHID-----------------CQ-------------CTAAMAA------------FSAGATFV---LLE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 417 -FAAKRKQAEVRsgiirndsiwdelffnKIQASLGGCVRMIVTG--AAPASPT--------VLGFLRAA----------L 475
Cdd:PRK08008 248 kYSARAFWGQVC----------------KYRATITECIPMMIRTlmVQPPSANdrqhclreVMFYLNLSdqekdafeerF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 476 GCQVYEGYGQTECTAGCTFTTPGD---WTSghVGAPLPCNHIKLVDveELNYWACKGE-GEICVRG---PNVFKGYLKDP 548
Cdd:PRK08008 312 GVRLLTSYGMTETIVGIIGDRPGDkrrWPS--IGRPGFCYEAEIRD--DHNRPLPAGEiGEICIKGvpgKTIFKEYYLDP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 549 DRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIyIRSQP-VAQIYVHG--DSL-----KA 620
Cdd:PRK08008 388 KATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVELENI-IATHPkIQDIVVVGikDSIrdeaiKA 465
|
...
gi 57165412 621 FLV 623
Cdd:PRK08008 466 FVV 468
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
146-633 |
7.51e-25 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 109.52 E-value: 7.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIVELACYTYSMVVV---PLYDTlgpGAIRYIINTADIST 222
Cdd:PRK08315 44 WTYREFNEEVDALAKGLLALGIEK-GDR-VGIWAPNVPEWVLTQFATAKIGAILVtinPAYRL---SELEYALNQSGCKA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 223 -VIVDK--------------PQKAVLLLEHVERKETPGLKLIILMDpfeeALKERGqkcgvvIKSMQAVEDCGQENHQAP 287
Cdd:PRK08315 119 lIAADGfkdsdyvamlyelaPELATCEPGQLQSARLPELRRVIFLG----DEKHPG------MLNFDELLALGRAVDDAE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 288 VPP-----QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsGFLkVTEKVIFPRQDDVLISfLPLAHMFERVIqSVVYC- 361
Cdd:PRK08315 189 LAArqatlDPDDPINIQYTSGTTGFPKGATLTHRNILNN--GYF-IGEAMKLTEEDRLCIP-VPLYHCFGMVL-GNLACv 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 362 -HGGRV-----GFfqgdirllsDDMKAL-------C------PTIFPVV---PRLlnRMYDkiFSQantplkrwllefaa 419
Cdd:PRK08315 264 tHGATMvypgeGF---------DPLATLaaveeerCtalygvPTMFIAEldhPDF--ARFD--LSS-------------- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 420 krkqaeVRSGIirndsiwdelffnkiqasLGGcvrmivtgaapaSPtvlgflraalgC------QVYE---------GYG 484
Cdd:PRK08315 317 ------LRTGI------------------MAG------------SP-----------CpievmkRVIDkmhmsevtiAYG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 485 QTECTAGCTFTTPGD------WTsghVGAPLPCNHIKLVDVEelnywacKGE-------GEICVRGPNVFKGYLKDPDRT 551
Cdd:PRK08315 350 MTETSPVSTQTRTDDplekrvTT---VGRALPHLEVKIVDPE-------TGEtvprgeqGELCTRGYSVMKGYWNDPEKT 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 552 KEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDP- 630
Cdd:PRK08315 420 AEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEF---------LYTHPKIQDVQVVG--VPDEk 487
|
....*.
gi 57165412 631 ---EVM 633
Cdd:PRK08315 488 ygeEVC 493
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
146-631 |
9.83e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 108.98 E-value: 9.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK06178 59 ITYAELDELSDRFAALLRQRGVGA-GDR-VAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 226 dkpQKAVL-LLEHVeRKETPgLKLII---LMD--------PFEEALKERGQKCGVVIKSMQAVEDCGQENHQAPvpPQPD 293
Cdd:PRK06178 137 ---LDQLApVVEQV-RAETS-LRHVIvtsLADvlpaeptlPLPDSLRAPRLAAAGAIDLLPALRACTAPVPLPP--PALD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 294 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifpRQDDVLISFLPlahMFerviqsvvYCHGGRVGFfqgdi 373
Cdd:PRK06178 210 ALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVG---GEDSVFLSFLP---EF--------WIAGENFGL----- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 374 rllsddmkalcptIFPvvprllnrmydkIFSQANTPL-KRW-LLEFAAKRKQAEVRSGIIRNDSIwDELF---------F 442
Cdd:PRK06178 271 -------------LFP------------LFSGATLVLlARWdAVAFMAAVERYRVTRTVMLVDNA-VELMdhprfaeydL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 443 NKIQASlgGCVRMIvtgaAPASPTVLGFLRAALGCQVYEG-YGQTECTAGCTFTTpGDWTSGH--------VGAPLPCNH 513
Cdd:PRK06178 325 SSLRQV--RVVSFV----KKLNPDYRQRWRALTGSVLAEAaWGMTETHTCDTFTA-GFQDDDFdllsqpvfVGLPVPGTE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 514 IKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYV 593
Cdd:PRK06178 398 FKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV-NGMSV 475
|
490 500 510
....*....|....*....|....*....|....*...
gi 57165412 594 APEKIENIYIRsqpvaqiyvHGDSLKAFLVGivVPDPE 631
Cdd:PRK06178 476 FPSEVEALLGQ---------HPAVLGSAVVG--RPDPD 502
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
245-599 |
1.96e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 108.16 E-value: 1.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 245 GLKLIILMDPFEEA---LKERGQKcgvviksMQAVEDCGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD 321
Cdd:PRK07768 108 GAKAVVVGEPFLAAapvLEEKGIR-------VLTVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYAN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 322 FSGflkVTEKVIFPRQDDVLISFLPLAH-MferviqsvvychgGRVGFfqgdirlLSDDMKALC------PTIFPVVPRL 394
Cdd:PRK07768 181 AEA---MFVAAEFDVETDVMVSWLPLFHdM-------------GMVGF-------LTVPMYFGAelvkvtPMDFLRDPLL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 395 LNRMYDKiFSQANTPLKRWLLEFAAKR--KQAEvrsgiirnDSIWDElffnkiqaslgGCVRMIVTGAAPASPTVL---- 468
Cdd:PRK07768 238 WAELISK-YRGTMTAAPNFAYALLARRlrRQAK--------PGAFDL-----------SSLRFALNGAEPIDPADVedll 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 469 ------GFLRAALGCqvyeGYGQTECTAGCTFTTPGD--------------------WTSGHV------GAPLPCNHIKL 516
Cdd:PRK07768 298 dagarfGLRPEAILP----AYGMAEATLAVSFSPCGAglvvdevdadllaalrravpATKGNTrrlatlGPPLPGLEVRV 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 517 VDvEELNYWACKGEGEICVRGPNVFKGYLkDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPE 596
Cdd:PRK07768 374 VD-EDGQVLPPRGVGVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPT 450
|
...
gi 57165412 597 KIE 599
Cdd:PRK07768 451 DIE 453
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
290-630 |
2.77e-24 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 107.45 E-value: 2.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 290 PQPDDLSIVCFTSGTTGNPKGAMLTHGNVvadFSGFLKVTEKVIFpRQDDVLISFLPLAHMferviqsvvychggrVGFF 369
Cdd:PRK13295 194 PGPDDVTQLIYTSGTTGEPKGVMHTANTL---MANIVPYAERLGL-GADDVILMASPMAHQ---------------TGFM 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 370 QGDIRLLSDDMKALCPTIFPVVprllnRMYDKI------FSQANTPlkrWLLEFAakRKQAEVRSGIirndsiwdelffn 443
Cdd:PRK13295 255 YGLMMPVMLGATAVLQDIWDPA-----RAAELIrtegvtFTMASTP---FLTDLT--RAVKESGRPV------------- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 444 kiqASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPGD---WTSGHVGAPLPCNHIKLVDvE 520
Cdd:PRK13295 312 ---SSL----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA-VTLTKLDDpdeRASTTDGCPLPGVEVRVVD-A 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 521 ELNYWACKGEGEICVRGPNVFKGYLKDPDRTkeALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIEN 600
Cdd:PRK13295 383 DGAPLPAGQIGRLQVRGCSNFGGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEA 459
|
330 340 350
....*....|....*....|....*....|.
gi 57165412 601 IYIRSQPVAQiyvhgdslkaflVGIV-VPDP 630
Cdd:PRK13295 460 LLYRHPAIAQ------------VAIVaYPDE 478
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
147-630 |
6.74e-24 |
|
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: 106.18 E-value: 6.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 147 SYQEVADRAEFLGSGLlqHNCKACTDQFIGVFAQNRpewiIVELACYtY-----SMVVVPLYDTLGPGAIRYIINTADIS 221
Cdd:cd12119 27 TYAEVAERARRLANAL--RRLGVKPGDRVATLAWNT----HRHLELY-YavpgmGAVLHTINPRLFPEQIAYIINHAEDR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 222 TVIVDK---PQKAVLL--LEHVERketpglklIILMDPFEEALKERGQKcgvVIKSMQAVEDcgqenhQAPVPPQPD--- 293
Cdd:cd12119 100 VVFVDRdflPLLEAIAprLPTVEH--------VVVMTDDAAMPEPAGVG---VLAYEELLAA------ESPEYDWPDfde 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 294 -DLSIVCFTSGTTGNPKGAMLTHgnvvadfsgflkvtekvifpRQddvlisflplahmfeRVIQSVVYCHGGRVGFFQGD 372
Cdd:cd12119 163 nTAAAICYTSGTTGNPKGVVYSH--------------------RS---------------LVLHAMAALLTDGLGLSESD 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 373 irllsddmkalcpTIFPVVPrllnrMYdkifsQANTplkrWLLEFAA-----------KRKQAEVRSGIIRND------- 434
Cdd:cd12119 208 -------------VVLPVVP-----MF-----HVNA----WGLPYAAamvgaklvlpgPYLDPASLAELIEREgvtfaag 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 435 --SIWDELF--FNKIQASLGGCVRMIVTGAAPASPTVLGFlrAALGCQVYEGYGQTECTAGCTFTTPgdwTSGHV----- 505
Cdd:cd12119 261 vpTVWQGLLdhLEANGRDLSSLRRVVIGGSAVPRSLIEAF--EERGVRVIHAWGMTETSPLGTVARP---PSEHSnlsed 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 506 ---------GAPLPCNHIKLVDVE--ELNyWACKGEGEICVRGPNVFKGYLKDPDRTkEALDSDGWLHTGDIGKWLPAGT 574
Cdd:cd12119 336 eqlalrakqGRPVPGVELRIVDDDgrELP-WDGKAVGELQVRGPWVTKSYYKNDEES-EALTEDGWLRTGDVATIDEDGY 413
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 57165412 575 LKIIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVhgdslkaflvgIVVPDP 630
Cdd:cd12119 414 LTITDRSKDVIKSG-GEWISSVELENAIMAHPAVAEAAV-----------IGVPHP 457
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
291-631 |
1.04e-23 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 105.32 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 291 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkviFPRQDDVL----ISF-LPLAHMFerviqsVVYCHGG- 364
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALG---LTSESRVLqfasYTFdVSILEIF------TTLAAGGc 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 365 --------RVGFFQGDIRllsdDMKALCPTIFPVVPRLLNRmydkifsqANTPlkrwllefaakrkqaevrsgiirndsi 436
Cdd:cd05918 175 lcipseedRLNDLAGFIN----RLRVTWAFLTPSVARLLDP--------EDVP--------------------------- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 437 wdelffnkiqaslggCVRMIVTGAAPASPTVLGflRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPC---- 511
Cdd:cd05918 216 ---------------SLRTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRPLGAtcwv 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 512 ----NHIKLVDVeelnywackGE-GEICVRGPNVFKGYLKDPDRTKEA-LDSDGWLH------------TGDIGKWLPAG 573
Cdd:cd05918 279 vdpdNHDRLVPI---------GAvGELLIEGPILARGYLNDPEKTAAAfIEDPAWLKqegsgrgrrlyrTGDLVRYNPDG 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57165412 574 TLKIIDRKKHIFKLaQGEYVAPEKIENiYIRSQP------VAQIYVH-GDSLKAFLVGIVVPDPE 631
Cdd:cd05918 350 SLEYVGRKDTQVKI-RGQRVELGEIEH-HLRQSLpgakevVVEVVKPkDGSSSPQLVAFVVLDGS 412
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
281-623 |
1.64e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 105.50 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 281 QENHQAPVPPQPD-DLSIVCFTSGTTGNPKGAMLTHGNVVADfsGFLKVTEKVIFPRQDDVLISFLPLAHMF-ERVIQSV 358
Cdd:PRK06710 193 EVNTGVEVPCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSN--TLMGVQWLYNCKEGEEVVLGVLPFFHVYgMTAVMNL 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 359 VYCHGGRVGFF-QGDIRLLSDDMKALCPTIFPVVPRLLnrmydkiFSQANTPLkrwllefaakRKQAEVRSgiirndsiw 437
Cdd:PRK06710 271 SIMQGYKMVLIpKFDMKMVFEAIKKHKVTLFPGAPTIY-------IALLNSPL----------LKEYDISS--------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 438 delffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgctfTTPGDW-----TSGHVGAPLPCN 512
Cdd:PRK06710 325 ---------------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSP----VTHSNFlwekrVPGSIGVPWPDT 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 513 HIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEY 592
Cdd:PRK06710 386 EAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFN 463
|
330 340 350
....*....|....*....|....*....|....*...
gi 57165412 593 VAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLV 623
Cdd:PRK06710 464 VYPREVEEVLYEHEKVQEVVTigvpdpyRGETVKAFVV 501
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
181-601 |
2.94e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 104.47 E-value: 2.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 181 NRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADiSTVIVDKPQKAVLLLEhvERKETPGLKLIILMDPFEEAlk 260
Cdd:PRK07786 76 NRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCG-AHVVVTEAALAPVATA--VRDIVPLLSTVVVAGGSSDD-- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 261 ergqkcGVViksmqAVEDCGQENHQAPVPPQ-PDDL-SIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkviFPRQD 338
Cdd:PRK07786 151 ------SVL-----GYEDLLAEAGPAHAPVDiPNDSpALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNG---ADINS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 339 DVLISFLPLAHMfeRVIQSVVychggrVGFFQGdirllsddmkalCPT-IFPVVPRLLNRMYDkifsqantplkrwLLEf 417
Cdd:PRK07786 217 DVGFVGVPLFHI--AGIGSML------PGLLLG------------APTvIYPLGAFDPGQLLD-------------VLE- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 418 aakrkqAEVRSGIIRNDSIWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAgCTFTT 496
Cdd:PRK07786 263 ------AEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEMSP-VTCML 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 497 PGD---WTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSdGWLHTGDIGKWLPAG 573
Cdd:PRK07786 336 LGEdaiRKLGSVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDEEG 413
|
410 420
....*....|....*....|....*...
gi 57165412 574 TLKIIDRKKHIFkLAQGEYVAPEKIENI 601
Cdd:PRK07786 414 YVWVVDRKKDMI-ISGGENIYCAEVENV 440
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
294-631 |
8.77e-23 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 100.04 E-value: 8.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 294 DLSIVCFTSGTTGNPKGAMLTHGNVVA---DFSGFLKVTEkvifprqDDVLISFLPLAHMFERVIQSVVYCHGGR---VG 367
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAanlQLIHAMGLTE-------ADVYLNMLPLFHIAGLNLALATFHAGGAnvvME 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 368 FFQGDIRL-LSDDMKAlcpTIFPVVPRLLNRMYDkifsqantplkrwllefAAKRKQAEVRSgiIRNdsiwdelffnkiq 446
Cdd:cd17637 74 KFDPAEALeLIEEEKV---TLMGSFPPILSNLLD-----------------AAEKSGVDLSS--LRH------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 447 aslggcvrmiVTGAApaSPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDveELNYWA 526
Cdd:cd17637 119 ----------VLGLD--APETIQRFEETTGATFWSLYGQTE-TSGLVTLSPYRERPGSAGRPGPLVRVRIVD--DNDRPV 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 527 CKGE-GEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRK--KHIFKlAQGEYVAPEKIENIyI 603
Cdd:cd17637 184 PAGEtGEIVVRGPLVFQGYWNLPELTAYTFR-NGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKV-I 260
|
330 340
....*....|....*....|....*....
gi 57165412 604 RSQP-VAQIYVHGdslkaflvgivVPDPE 631
Cdd:cd17637 261 LEHPaIAEVCVIG-----------VPDPK 278
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
146-632 |
1.04e-22 |
|
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: 101.94 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLyDTLGPGA-IRYIINTADISTVI 224
Cdd:cd05945 17 LTYRELKERADALAAALASLGLDA--GDPVVVYGHKSPDAIAAFLAALKAGHAYVPL-DASSPAErIREILDAAKPALLI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 225 VDkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhqapvppqPDDLSIVCFTSGT 304
Cdd:cd05945 94 AD-----------------------------------------------------------------GDDNAYIIFTSGS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 305 TGNPKGAMLTHGNVVAdFS----GFLKVTEkvifprqDDVLISFLPLAhmFERVIQSVVYC--HGGrvgffqgdirllsd 378
Cdd:cd05945 109 TGRPKGVQISHDNLVS-FTnwmlSDFPLGP-------GDVFLNQAPFS--FDLSVMDLYPAlaSGA-------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 379 dmkalcpTIFPVvPRLLNRMYDKIFSQ-ANTPLKRWLlefaakrkqaevrsgiiRNDSIWDELF----FNkiQASLGGCV 453
Cdd:cd05945 165 -------TLVPV-PRDATADPKQLFRFlAEHGITVWV-----------------STPSFAAMCLlsptFT--PESLPSLR 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 454 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFT--TP---GDWTSGHVGAPLPCNHIKLVDvEELNYWACK 528
Cdd:cd05945 218 HFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIevTPevlDGYDRLPIGYAKPGAKLVILD-EDGRPVPPG 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 529 GEGEICVRGPNVFKGYLKDPDRTKEALDSD---GWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRS 605
Cdd:cd05945 297 EKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIELEEIEAALRQV 375
|
490 500 510
....*....|....*....|....*....|.
gi 57165412 606 QPVAQIYV----HGDSlKAFLVGIVVPDPEV 632
Cdd:cd05945 376 PGVKEAVVvpkyKGEK-VTELIAFVVPKPGA 405
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
146-630 |
1.51e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 101.93 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK08316 37 WTYAELDAAVNRVAAALLDLGLKK-GDR-VAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 226 DkpqkaVLLLEHVErketPGLKLIiLMDPFEEALKERGQkcgVVIKSMQAVEDCGQEnhQAPVPPQP----DDLSIVCFT 301
Cdd:PRK08316 115 D-----PALAPTAE----AALALL-PVDTLILSLVLGGR---EAPGGWLDFADWAEA--GSVAEPDVeladDDLAQILYT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 302 SGTTGNPKGAMLTHGNVVADFSGFLKVTEKvifpRQDDVLISFLPLAHmferviqsvvyCHggrvgffQGDIRLLSDDMK 381
Cdd:PRK08316 180 SGTESLPKGAMLTHRALIAEYVSCIVAGDM----SADDIPLHALPLYH-----------CA-------QLDVFLGPYLYV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 382 ALCPTI--FPVVPRLLnrmyDKIFSQANTPLkrwlleFAAKrkqaevrsgiirndSIWDELF----FNKIQASlggCVRM 455
Cdd:PRK08316 238 GATNVIldAPDPELIL----RTIEAERITSF------FAPP--------------TVWISLLrhpdFDTRDLS---SLRK 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 456 IVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFTTPGDwtsgHVGAP----LPCNHI--KLVDvEELNYWAcK 528
Cdd:PRK08316 291 GYYGASIMPVEVLKELRERLpGLRFYNCYGQTEIAPLATVLGPEE----HLRRPgsagRPVLNVetRVVD-DDGNDVA-P 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 529 GE-GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIyirsqp 607
Cdd:PRK08316 365 GEvGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEA------ 436
|
490 500
....*....|....*....|...
gi 57165412 608 vaqIYVHGDSLKAFLVGivVPDP 630
Cdd:PRK08316 437 ---LYTHPAVAEVAVIG--LPDP 454
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
292-640 |
1.63e-22 |
|
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: 99.86 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgfLKVTEKVIFPRQDDVLISFLPLAHMFERVIQsvvychgGRVGFFQG 371
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYN----AWMLALNSLFDPDDVLLCGLPLFHVNGSVVT-------LLTPLASG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 372 DIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTPLkrwllefaAKRKQAEVRSGIirndsiwdelffnkiqaslgG 451
Cdd:cd05944 70 AHVVLAGPAGYRNPGLFDNFWKLVERYRITSLSTVPTVY--------AALLQVPVNADI--------------------S 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 452 CVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLV--DVEELNYWACK 528
Cdd:cd05944 122 SLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKvlDGVGRLLRDCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 529 GE--GEICVRGPNVFKGYLKDpDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQ 606
Cdd:cd05944 202 PDevGEICVAGPGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLRHP 279
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 57165412 607 PVAQIYVHG--DSLKAFL-VGIV--VPDPEVMP----SWAQKR 640
Cdd:cd05944 280 AVAFAGAVGqpDAHAGELpVAYVqlKPGAVVEEeellAWARDH 322
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
146-601 |
2.09e-22 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 103.12 E-value: 2.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLGsGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK06814 659 LTYRKLLTGAFVLG-RKLKKNTPP--GENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 226 DKP--QKAVL--LLEHVERketpGLKLIILMDPFEE---ALKERGqkcgVVIKSMQAVEDCGqenhqapvpPQPDDLSIV 298
Cdd:PRK06814 736 SRAfiEKARLgpLIEALEF----GIRIIYLEDVRAQiglADKIKG----LLAGRFPLVYFCN---------RDPDDPAVI 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 299 CFTSGTTGNPKGAMLTHGNVVADFSgflKVTEKVIFPRQDDVLiSFLPLAHMFerviqsvvychggrvGFFQGDIRLLSD 378
Cdd:PRK06814 799 LFTSGSEGTPKGVVLSHRNLLANRA---QVAARIDFSPEDKVF-NALPVFHSF---------------GLTGGLVLPLLS 859
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 379 DMKAL---CPTIFPVVPRLLnrmYDK----IFSqANTPLkrwllefaakrkqaevrSGIIRNDSIWDelFFNkiqaslgg 451
Cdd:PRK06814 860 GVKVFlypSPLHYRIIPELI---YDTnatiLFG-TDTFL-----------------NGYARYAHPYD--FRS-------- 908
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 452 cVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNywacKGeG 531
Cdd:PRK06814 909 -LRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGID----EG-G 982
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57165412 532 EICVRGPNVFKGYLK-DPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENI 601
Cdd:PRK06814 983 RLFVRGPNVMLGYLRaENPGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAVEEL 1051
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
144-640 |
7.93e-22 |
|
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: 99.32 E-value: 7.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 144 QWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLyDTLGPGA-IRYIINTADIST 222
Cdd:cd17655 21 QTLTYRELNERANQLARTLREKGVGP--DTIVGIMAERSLEMIVGILGILKAGGAYLPI-DPDYPEErIQYILEDSGADI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 223 VIVDKPQKAVLLlehverketpGLKLIILMDpfEEALKErgqkcgvviksmqavedcgQENHQAPVPPQPDDLSIVCFTS 302
Cdd:cd17655 98 LLTQSHLQPPIA----------FIGLIDLLD--EDTIYH-------------------EESENLEPVSKSDDLAYVIYTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 303 GTTGNPKGAMLTHGNVVADFSGFlkvtEKVIFPRQDDVLISFLPLAhmFERVIQSVvychggrvgfFQGdirLLSDDmkA 382
Cdd:cd17655 147 GSTGKPKGVMIEHRGVVNLVEWA----NKVIYQGEHLRVALFASIS--FDASVTEI----------FAS---LLSGN--T 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 383 LCptIFPVVPRLLNRMYDKIFSQAN------TPLKRWLLEFAakrkqaevrsgiirndsiwDELFFNKIQaslggcvRMI 456
Cdd:cd17655 206 LY--IVRKETVLDGQALTQYIRQNRitiidlTPAHLKLLDAA-------------------DDSEGLSLK-------HLI 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 457 VTGAAPASPTVLGFL-RAALGCQVYEGYGQTECTAGCTF--TTPGDWTSGHV--GAPLPCNHIKLVDvEELNYWACKGEG 531
Cdd:cd17655 258 VGGEALSTELAKKIIeLFGTNPTITNAYGPTETTVDASIyqYEPETDQQVSVpiGKPLGNTRIYILD-QYGRPQPVGVAG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 532 EICVRGPNVFKGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRS 605
Cdd:cd17655 337 ELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-RGYRIELGEIEARLLQH 415
|
490 500 510
....*....|....*....|....*....|....*...
gi 57165412 606 QPVAQ---IYVHGDSLKAFLVGIVVPDPEVMPSWAQKR 640
Cdd:cd17655 416 PDIKEavvIARKDEQGQNYLCAYIVSEKELPVAQLREF 453
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
294-710 |
1.18e-21 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 96.63 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 294 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkVTEKVIFPRQDDVLISfLPLAHM--FERVIQSVVycHGGRVGFFQG 371
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAG---LHSRLGFGGGDSWLLS-LPLYHVggLAILVRSLL--AGAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 372 DiRLLSDDMKALCPTIFPVVPRLLNRMYDKifSQANTPLKRwllefaakrkqaevrsgiirndsiwdelffnkiqaslgg 451
Cdd:cd17630 75 N-QALAEDLAPPGVTHVSLVPTQLQRLLDS--GQGPAALKS--------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 452 cVRMIVTGAAPASPtvlGFLRAA--LGCQVYEGYGQTEcTAGCTFT-TPGDWTSGHVGAPLPCNHIKLVDveelnywack 528
Cdd:cd17630 113 -LRAVLLGGAPIPP---ELLERAadRGIPLYTTYGMTE-TASQVATkRPDGFGRGGVGVLLPGRELRIVE---------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 529 gEGEICVRGPNVFKGYLKDPdrTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIyIRSQP- 607
Cdd:cd17630 178 -DGEIWVGGASLAMGYLRGQ--LVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAA-LAAHPa 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 608 VAQIYVHGdslkaflvgivVPDPEvmpsWAQKrgiegTYADLCTNKDLKKAILEDMVRlgkeSGLHSFEQVKAIHIhsdm 687
Cdd:cd17630 253 VRDAFVVG-----------VPDEE----LGQR-----PVAVIVGRGPADPAELRAWLK----DKLARFKLPKRIYP---- 304
|
410 420
....*....|....*....|...
gi 57165412 688 fsVQNGLLTPTLKAKRPELREYF 710
Cdd:cd17630 305 --VPELPRTGGGKVDRRALRAWL 325
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
175-643 |
1.31e-20 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 95.19 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 175 IGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDkpqkavlllehverketpglkliilmdp 254
Cdd:cd05971 34 VGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTD---------------------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 255 feealkergqkcgvviksmqavedcgqenhqapvppQPDDLSIVCFTSGTTGNPKGAMLTH----GNVVADFSGFlkvte 330
Cdd:cd05971 86 ------------------------------------GSDDPALIIYTSGTTGPPKGALHAHrvllGHLPGVQFPF----- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 331 kVIFPRQDDVLIS-------------FLP--------LAHMFERviqsvvychggrvgfFQGD--IRLLSD---DMKALC 384
Cdd:cd05971 125 -NLFPRDGDLYWTpadwawigglldvLLPslyfgvpvLAHRMTK---------------FDPKaaLDLMSRygvTTAFLP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 385 PTIFpvvprllnrmydKIFSQANTPLKRWLLEfaakrkqaevrsgiirndsiwdelffnkiqaslggcVRMIVTGAAPAS 464
Cdd:cd05971 189 PTAL------------KMMRQQGEQLKHAQVK------------------------------------LRAIATGGESLG 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 465 PTVLGFLRAALGCQVYEGYGQTEC---TAGCTFTTPGDwtSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPN-- 539
Cdd:cd05971 221 EELLGWAREQFGVEVNEFYGQTECnlvIGNCSALFPIK--PGSMGKPIPGHRVAIVD-DNGTPLPPGEVGEIAVELPDpv 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 540 VFKGYLKDPDRTKEALDSDgWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYV------ 613
Cdd:cd05971 298 AFLGYWNNPSATEKKMAGD-WLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAEIEECLLKHPAVLMAAVvgipdp 375
|
490 500 510
....*....|....*....|....*....|.
gi 57165412 614 -HGDSLKAFlvgiVVPDPEVMPSWAQKRGIE 643
Cdd:cd05971 376 iRGEIVKAF----VVLNPGETPSDALAREIQ 402
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
274-648 |
1.88e-20 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 94.84 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 274 QAVEDCGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHgnvvADFSGFLKVTEKVIFP-RQDDVLISflpLAHMFe 352
Cdd:cd05919 72 DDYAYIARDCEARLVVTSADDIAYLLYSSGTTGPPKGVMHAH----RDPLLFADAMAREALGlTPGDRVFS---SAKMF- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 353 rviqsVVYCHGGRVGF--FQGDIRLLSDD----------MKALCPTIFPVVPRllnrMYDKIFSQANTPlkrwllefaak 420
Cdd:cd05919 144 -----FGYGLGNSLWFplAVGASAVLNPGwptaervlatLARFRPTVLYGVPT----FYANLLDSCAGS----------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 421 rkQAEVRSgiIRndsiwdelffnkiqaslggcvrmIVTGAAPASPTVLG-FLRAALGCQVYEGYGQTEctAGCTFTT--P 497
Cdd:cd05919 204 --PDALRS--LR-----------------------LCVSAGEALPRGLGeRWMEHFGGPILDGIGATE--VGHIFLSnrP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 498 GDWTSGHVGAPLPCNHIKLVDveELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLK 576
Cdd:cd05919 255 GAWRLGSTGRPVPGYEIRLVD--EEGHTIPPGEeGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYT 331
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57165412 577 IIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYV----HGDSL---KAFlvgiVVPDPEVMPSWAQKRGIEGTYAD 648
Cdd:cd05919 332 HAGRADDMLKVG-GQWVSPVEVESLIIQHPAVAEAAVvavpESTGLsrlTAF----VVLKSPAAPQESLARDIHRHLLE 405
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
175-635 |
2.92e-20 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 94.95 E-value: 2.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 175 IGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKpqkavlLLEHVERKET-PGLKLIILMD 253
Cdd:PRK05852 71 VALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDA------DGPHDRAEPTtRWWPLTVNVG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 254 PfeealkERGQKCGVVIKSMQAVedcGQENHQAPVPP--QPDDLSIVcFTSGTTGNPKGAMLTHGNVVADFSGFlkVTEK 331
Cdd:PRK05852 145 G------DSGPSGGTLSVHLDAA---TEPTPATSTPEglRPDDAMIM-FTGGTTGLPKMVPWTHANIASSVRAI--ITGY 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 332 VIFPRqdDVLISFLPLAH---MFERVIQSVVycHGGRV-----GFFQGdiRLLSDDMKALCPTIFPVVPrllnrmydkif 403
Cdd:PRK05852 213 RLSPR--DATVAVMPLYHghgLIAALLATLA--SGGAVllparGRFSA--HTFWDDIKAVGATWYTAVP----------- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 404 sqantPLKRWLLEFAAKRKQAEVRSGIirndsiwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGY 483
Cdd:PRK05852 276 -----TIHQILLERAATEPSGRKPAAL-----------------------RFIRSCSAPLTAETAQALQTEFAAPVVCAF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 484 GQTECTAGCTfTTPGDWtSGHVGAPLPCN---------HIKLV--DVEELNYWACkgeGEICVRGPNVFKGYLKDPDRTK 552
Cdd:PRK05852 328 GMTEATHQVT-TTQIEG-IGQTENPVVSTglvgrstgaQIRIVgsDGLPLPAGAV---GEVWLRGTTVVRGYLGDPTITA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 553 EALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAF---LVGIVVPD 629
Cdd:PRK05852 403 ANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLASHPNVMEAAVFGVPDQLYgeaVAAVIVPR 480
|
....*.
gi 57165412 630 PEVMPS 635
Cdd:PRK05852 481 ESAPPT 486
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
177-630 |
4.17e-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: 94.48 E-value: 4.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 177 VFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKavlLLEHVE--RKETPGL-KLIILMD 253
Cdd:cd05970 77 LTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDN---IPEEIEkaAPECPSKpKLVWVGD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 254 PFEEALKERGQKCgvviksMQAVEDCgqENHQAPVPPQPDDLSIVCFTSGTTGNPKgaMLTHgnvvaDFSgflkvtekvi 333
Cdd:cd05970 154 PVPEGWIDFRKLI------KNASPDF--ERPTANSYPCGEDILLVYFSSGTTGMPK--MVEH-----DFT---------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 334 fprqddvlisfLPLAHmfervIQSVVYCHGGRvgffQGDIRLLSDDM---KALCPTIF-------PVVprllnrMYD-KI 402
Cdd:cd05970 209 -----------YPLGH-----IVTAKYWQNVR----EGGLHLTVADTgwgKAVWGKIYgqwiagaAVF------VYDyDK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 403 FSQANtplkrwLLEFAAKRKQAE------VRSGIIRND-SIWDelfFNKIqaslggcvRMIVTGAAPASPTVLGFLRAAL 475
Cdd:cd05970 263 FDPKA------LLEKLSKYGVTTfcapptIYRFLIREDlSRYD---LSSL--------RYCTTAGEALNPEVFNTFKEKT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 476 GCQVYEGYGQTECTAgCTFTTPG-DWTSGHVGAPLPCNHIKLVDVEELnywACKG--EGEICVRGPN-----VFKGYLKD 547
Cdd:cd05970 326 GIKLMEGFGQTETTL-TIATFPWmEPKPGSMGKPAPGYEIDLIDREGR---SCEAgeEGEIVIRTSKgkpvgLFGGYYKD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 548 PDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYVHGdslkaflvgivV 627
Cdd:cd05970 402 AEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVESALIQHPAVLECAVTG-----------V 468
|
...
gi 57165412 628 PDP 630
Cdd:cd05970 469 PDP 471
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
292-707 |
6.45e-20 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 94.10 E-value: 6.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfSGFLKVTekVIFPRQDDVLISFLPLAHMFErvIQSVVY------CHggr 365
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSALIV--QSLAKIA--IVGYGEDDVYLHTAPLCHIGG--LSSALAmlmvgaCH--- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 366 VGFFQGDIRLLSDDMKALCPTIFPVVPRLlnrMYDkifsqantplkrwLLEFAAKRKqaevrsgiirndsIWDElffnki 445
Cdd:PLN02860 242 VLLPKFDAKAALQAIKQHNVTSMITVPAM---MAD-------------LISLTRKSM-------------TWKV------ 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 446 qaslGGCVRMIVTGAAPASP-----TVLGFLRAALgcqvYEGYGQTECTAGCTFTTPGDWT-----------------SG 503
Cdd:PLN02860 287 ----FPSVRKILNGGGSLSSrllpdAKKLFPNAKL----FSAYGMTEACSSLTFMTLHDPTlespkqtlqtvnqtkssSV 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 504 H------VGAPLPcnHIKLvdveELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKI 577
Cdd:PLN02860 359 HqpqgvcVGKPAP--HVEL----KIGLDESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWL 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 578 IDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYVHGdSLKAFLVGIVVPDPEVMPSWaqkRGIEGTYADLCTNKDLKK 657
Cdd:PLN02860 433 IGRSNDRIK-TGGENVYPEEVEAVLSQHPGVASVVVVG-VPDSRLTEMVVACVRLRDGW---IWSDNEKENAKKNLTLSS 507
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 57165412 658 AILEDMVRlgkESGLHSFEQVKAIHIHSDMFSvqnglLTPTLKAKRPELR 707
Cdd:PLN02860 508 ETLRHHCR---EKNLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEVR 549
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
146-632 |
6.97e-20 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 93.42 E-value: 6.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELA------CYtysmvvVPLYDTLGPGAIRYIINTAD 219
Cdd:cd12117 23 LTYAELNERANRLARRLRAAGVGP--GDVVGVLAERSPELVVALLAvlkagaAY------VPLDPELPAERLAFMLADAG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 220 ISTVIVDKPQKAVLLLehverketPGLKLIILMDPFEEALKErgqkcgvviksmqavedcgqenhqAPVPPQPDDLSIVC 299
Cdd:cd12117 95 AKVLLTDRSLAGRAGG--------LEVAVVIDEALDAGPAGN------------------------PAVPVSPDDLAYVM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 300 FTSGTTGNPKGAMLTHGNVV--ADFSGFLKVTEkvifprqDDVLISFLPL---AHMFErviqsvVY---CHGGRVgffqg 371
Cdd:cd12117 143 YTSGSTGRPKGVAVTHRGVVrlVKNTNYVTLGP-------DDRVLQTSPLafdASTFE------IWgalLNGARL----- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 372 dirllsddmkALCPTIFPVVPRLLnrmydkifsqantplkrwllefaakrkQAEVRSGIIrnDSIWdeL---FFNKI--- 445
Cdd:cd12117 205 ----------VLAPKGTLLDPDAL---------------------------GALIAEEGV--TVLW--LtaaLFNQLade 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 446 -QASLGGcVRMIVTGAAPASPT-VLGFLRAALGCQVYEGYGQTECTagcTFTT-----PGDWTSGHV--GAPLPCNHIKL 516
Cdd:cd12117 244 dPECFAG-LRELLTGGEVVSPPhVRRVLAACPGLRLVNGYGPTENT---TFTTshvvtELDEVAGSIpiGRPIANTRVYV 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 517 VDveELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKIIDRKKHIFKLaQ 589
Cdd:cd12117 320 LD--EDGRPVPPGVpGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI-R 396
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 57165412 590 GEYVAPEKIENIyIRSQP-VAQIYV---HGDSLKAFLVGIVVPDPEV 632
Cdd:cd12117 397 GFRIELGEIEAA-LRAHPgVREAVVvvrEDAGGDKRLVAYVVAEGAL 442
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
175-630 |
3.34e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 91.49 E-value: 3.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 175 IGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAVLLLEHVerketpglklIILMDP 254
Cdd:PRK06145 55 VALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDEEFDAIVALETP----------KIVIDA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 255 FEEALKERGQKCGVVIKSMQAVedcgqenhqapvppQPDDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTek 331
Cdd:PRK06145 125 AAQADSRRLAQGGLEIPPQAAV--------------APTDLVRLMYTSGTTDRPKGVMHSYGNLHwksIDHVIALGLT-- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 332 vifprQDDVLISFLPLAHMFERVIQSV-VYCHGGRVGF---FQGDIRLLSDDMKALCPTIFpvVPRLLNRMYdkifsQAN 407
Cdd:PRK06145 189 -----ASERLLVVGPLYHVGAFDLPGIaVLWVGGTLRIhreFDPEAVLAAIERHRLTCAWM--APVMLSRVL-----TVP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 408 TPLK------RWLLefAAKRKQAEVRsgiIRNdsiwdelffnkiqaslggcvrmivtgaapasptvlgFLRAALGCQVYE 481
Cdd:PRK06145 257 DRDRfdldslAWCI--GGGEKTPESR---IRD------------------------------------FTRVFTRARYID 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 482 GYGQTECTAGCTFTTPGDWTS--GHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDG 559
Cdd:PRK06145 296 AYGLTETCSGDTLMEAGREIEkiGSTGRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGD 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57165412 560 WLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIEN-IYIRSQ--PVAQIYVHGDSLKAFLVGIVVPDP 630
Cdd:PRK06145 374 WFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERvIYELPEvaEAAVIGVHDDRWGERITAVVVLNP 446
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
291-640 |
5.75e-19 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 90.22 E-value: 5.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 291 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPrqddvlISFLPLAHMferviqsvvychggRVGFFQ 370
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFP------VRLLQMASF--------------SFDVFA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 371 GDIrllsddMKALCP--TIFPVVPRLL---NRMYDKIFSQ-----ANTP-LKRWLLEFAAKRKQ--AEVRSGIIRNDSIW 437
Cdd:cd17650 151 GDF------ARSLLNggTLVICPDEVKldpAALYDLILKSritlmESTPaLIRPVMAYVYRNGLdlSAMRLLIVGSDGCK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 438 DElFFNKIQASLGGCVRMIvtgaapaspTVLGFLRAALGCQVYEGYGQTECTAGctfTTPgdwtsghVGAPLPCNHIKLV 517
Cdd:cd17650 225 AQ-DFKTLAARFGQGMRII---------NSYGVTEATIDSTYYEEGRDPLGDSA---NVP-------IGRPLPNTAMYVL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 518 DvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGW------LHTGDIGKWLPAGTLKIIDRKKHIFKLaQGE 591
Cdd:cd17650 285 D-ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI-RGF 362
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 57165412 592 YVAPEKIENIYIRSQPVAQIYV---HGDSLKAFLVGIVVPDPEvmPSWAQKR 640
Cdd:cd17650 363 RIELGEIESQLARHPAIDEAVVavrEDKGGEARLCAYVVAAAT--LNTAELR 412
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
146-634 |
6.29e-19 |
|
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: 90.41 E-value: 6.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVR--PGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 226 DKPQkavlllehvERKETPGLKLIILMDPFEEALKErgqkcgvviksmqavedcgqenhQAPVPPQPDDLSIVCFTSGTT 305
Cdd:cd12114 91 DGPD---------AQLDVAVFDVLILDLDALAAPAP-----------------------PPPVDVAPDDLAYVIFTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 306 GNPKGAMLTHG---NVVADFSGFLKVTEkvifprqDDVLISFLPLAHMFerviqSV-----VYCHGGRVgffqgdirlls 377
Cdd:cd12114 139 GTPKGVMISHRaalNTILDINRRFAVGP-------DDRVLALSSLSFDL-----SVydifgALSAGATL----------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 378 ddmkalcptifpVVPRLlnrmydkifSQANTPlKRWllefaakrKQAEVRSGIirndSIWdelffNKIQASLGgcvrMIV 457
Cdd:cd12114 196 ------------VLPDE---------ARRRDP-AHW--------AELIERHGV----TLW-----NSVPALLE----MLL 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 458 TgAAPASPTVLGFLRAAL-------------------GCQVYEGYGQTECTAGCTF----TTPGDWTSGHVGAPLPCNHI 514
Cdd:cd12114 233 D-VLEAAQALLPSLRLVLlsgdwipldlparlralapDARLISLGGATEASIWSIYhpidEVPPDWRSIPYGRPLANQRY 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 515 KLVD--VEELNYWackGEGEICVRGPNVFKGYLKDPDRTKEAL--DSDG--WLHTGDIGKWLPAGTLKIIDRKKHIFKLa 588
Cdd:cd12114 312 RVLDprGRDCPDW---VPGELWIGGRGVALGYLGDPELTAARFvtHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKV- 387
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 57165412 589 QGEYVAPEKIENIYIRSQPVAQ--IYVHGDSLKAFLVGIVVPDPEVMP 634
Cdd:cd12114 388 RGYRIELGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPDNDGTP 435
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
95-613 |
1.06e-18 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 90.20 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 95 ARRSVIGSGPQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRKpkqpyQWLSYQEVADRAEFLGSGLLQHNCKAcTDQf 174
Cdd:PRK06155 1 GEPLGAGLAARAVDPLPPSERTLPAMLARQAERYPDRPLLVFGG-----TRWTYAEAARAAAAAAHALAAAGVKR-GDR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 175 IGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlLLEHVERKETPGLKL--IILM 252
Cdd:PRK06155 74 VALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAA-----LLAALEAADPGDLPLpaVWLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 253 DPFEEALKERGQKCGVVIKSMQAVedcgqenhqAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHgnvvADFSGFLKVTEKV 332
Cdd:PRK06155 149 DAPASVSVPAGWSTAPLPPLDAPA---------PAAAVQPGDTAAILYTSGTTGPSKGVCCPH----AQFYWWGRNSAED 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 333 IFPRQDDVLISFLPLAH-----MFervIQSVVycHGGRV---------GFFqgdirllsDDMKALCPTIFpvvpRLLNRM 398
Cdd:PRK06155 216 LEIGADDVLYTTLPLFHtnalnAF---FQALL--AGATYvleprfsasGFW--------PAVRRHGATVT----YLLGAM 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 399 YDKIFSQANTPLKRwllefaakrkqaevrsgiirndsiwdelffnkiqaslGGCVRMIVTGAAPASptVLGFLRAALGCQ 478
Cdd:PRK06155 279 VSILLSQPARESDR-------------------------------------AHRVRVALGPGVPAA--LHAAFRERFGVD 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 479 VYEGYGQTECTAGCtFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWAckGE-GEICVRG--PNVF-KGYLKDPDRTKEA 554
Cdd:PRK06155 320 LLDGYGSTETNFVI-AVTHGSQRPGSMGRLAPGFEARVVDEHDQELPD--GEpGELLLRAdePFAFaTGYFGMPEKTVEA 396
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 555 LdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENIyIRSQP-VAQIYV 613
Cdd:PRK06155 397 W-RNLWFHTGDRVVRDADGWFRFVDRIKDAIR-RRGENISSFEVEQV-LLSHPaVAAAAV 453
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
291-631 |
1.15e-18 |
|
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: 89.29 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 291 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkvTEKVIFPRQDDVLISFLPLAHMFerviqSV-----VYCHGGR 365
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA----TQRWFGFNEDDVWTLFHSYAFDF-----SVweiwgALLHGGR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 366 VGFFQGDIRLLSDDMkalcptifpvvPRLLNRMYDKIFSQanTPLkrwllefAAKRKQAEVRSGIIRNDSIwdelffnki 445
Cdd:cd17643 162 LVVVPYEVARSPEDF-----------ARLLRDEGVTVLNQ--TPS-------AFYQLVEAADRDGRDPLAL--------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 446 qaslggcvRMIVTGAAPASPTVLGFLRAALGC---QVYEGYGQTECTAGCTFT--TPGDW---TSGHVGAPLPCNHIKLV 517
Cdd:cd17643 213 --------RYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFRplDAADLpaaAASPIGRPLPGLRVYVL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 518 DvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKE-------ALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQG 590
Cdd:cd17643 285 D-ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI-RG 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 57165412 591 EYVAPEKIENIYIRSQPVAQIYV---HGDSLKAFLVGIVVPDPE 631
Cdd:cd17643 363 FRIELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVADDG 406
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
287-630 |
1.16e-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: 89.67 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 287 PVPPQPDDLSIVC-FTSGTTGNPKGAMLTHGnvvadfSGFLKVTEKVIFPRQDD--VLISFLPLAHmferviqsvvyCHG 363
Cdd:cd12118 126 WIPPADEWDPIALnYTSGTTGRPKGVVYHHR------GAYLNALANILEWEMKQhpVYLWTLPMFH-----------CNG 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 364 GrvGFFQGdirllsddMKALCPTIfpVVPRLLNrmYDKIFsqantplkRWLLE-----FAAkrkqAEVRSGIIRNDSIWD 438
Cdd:cd12118 189 W--CFPWT--------VAAVGGTN--VCLRKVD--AKAIY--------DLIEKhkvthFCG----APTVLNMLANAPPSD 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 439 elffnkiQASLGGCVRMIVTGAAPaSPTVLgFLRAALGCQVYEGYGQTEcTAG----CTFTTPGDWTSGHVGAPLPC--- 511
Cdd:cd12118 243 -------ARPLPHRVHVMTAGAPP-PAAVL-AKMEELGFDVTHVYGLTE-TYGpatvCAWKPEWDELPTEERARLKArqg 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 512 -NHIKL--VDVEELNY-----WACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKH 583
Cdd:cd12118 313 vRYVGLeeVDVLDPETmkpvpRDGKTIGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKD 391
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 57165412 584 IFkLAQGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDP 630
Cdd:cd12118 392 II-ISGGENISSVEVEGV---------LYKHPAVLEAAVVA--RPDE 426
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
284-619 |
1.34e-18 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 90.54 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 284 HQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTH----GNV-----VADFSgflkvtekvifPRqdDVLISFLPLAHMFerv 354
Cdd:PRK08043 356 RLAQVKQQPEDAALILFTSGSEGHPKGVVHSHksllANVeqiktIADFT-----------PN--DRFMSALPLFHSF--- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 355 iqsvvychGGRVGFFQgdiRLLSDDMKALCPTI--FPVVPRLLnrmYDK----IFSQANtplkrWLLEFAakrkqaevrs 428
Cdd:PRK08043 420 --------GLTVGLFT---PLLTGAEVFLYPSPlhYRIVPELV---YDRnctvLFGTST-----FLGNYA---------- 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 429 giiRNDSIWDelFFNkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAP 508
Cdd:PRK08043 471 ---RFANPYD--FAR---------LRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRI 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 509 LPCNHIKLVDVEELNywacKGeGEICVRGPNVFKGYLK--DPDRTK-------EALDSDGWLHTGDIGKWLPAGTLKIID 579
Cdd:PRK08043 537 LPGMDARLLSVPGIE----QG-GRLQLKGPNIMNGYLRveKPGVLEvptaenaRGEMERGWYDTGDIVRFDEQGFVQIQG 611
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 57165412 580 RKKHIFKLAqGEYVAPEKIENIYIRSQPVAQiyvHGDSLK 619
Cdd:PRK08043 612 RAKRFAKIA-GEMVSLEMVEQLALGVSPDKQ---HATAIK 647
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
287-641 |
5.14e-18 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 87.78 E-value: 5.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 287 PVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVTEKVIFPRQDDVLISFLPLAhmFERVIQSV--VYCHGG 364
Cdd:cd17651 130 DPALDADDLAYVIYTSGSTGRPKGVVMPHRSLA----NLVAWQARASSLGPGARTLQFAGLG--FDVSVQEIfsTLCAGA 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 365 RVGFFQGDIRLLSDDMKALCPTifpvvpRLLNRMYdkifsqANTPLKRWLLEfAAKRKQAEvrsgiirndsiwdelffnk 444
Cdd:cd17651 204 TLVLPPEEVRTDPPALAAWLDE------QRISRVF------LPTVALRALAE-HGRPLGVR------------------- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 445 iqaslGGCVRMIVTG--AAPASPTVLGFLRAALGCQVYEGYGQTE---CTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVD 518
Cdd:cd17651 252 -----LAALRYLLTGgeQLVLTEDLREFCAGLPGLRLHNHYGPTEthvVTALSLPGDPAAWPApPPIGRPIDNTRVYVLD 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 519 vEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKIIDRKKHIFKLaQGEY 592
Cdd:cd17651 327 -AALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGFR 404
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 57165412 593 VAPEKIENIYIRSQPVAQIYV------HGDslkAFLVGIVVPDPEVMPSWAQKRG 641
Cdd:cd17651 405 IELGEIEAALARHPGVREAVVlaredrPGE---KRLVAYVVGDPEAPVDAAELRA 456
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
146-634 |
8.53e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 87.11 E-value: 8.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLGSGLLQHNckACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQG--VRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 226 DKPQKAVLL---LEHVERKETPGLKLIILMDPFEEALKERGQKCGVviksmQAVEDCGQENHQAPVPPQ-PDDLSIVCFT 301
Cdd:PRK06164 114 WPGFKGIDFaaiLAAVPPDALPPLRAIAVVDDAADATPAPAPGARV-----QLFALPDPAPPAAAGERAaDPDAGALLFT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 302 -SGTTGNPK------GAMLTHGNVVADFSGFlkvtekvifpRQDDVLISFLPLahmferviqSVVYCHGGRVGFFQGDIR 374
Cdd:PRK06164 189 tSGTTSGPKlvlhrqATLLRHARAIARAYGY----------DPGAVLLAALPF---------CGVFGFSTLLGALAGGAP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 375 LLSDDMKALCPTIfpvvpRLL-----------NRMYDKIFSQANTPLkrwllEFAAKRkqaevRSGIirndsiwdelffn 443
Cdd:PRK06164 250 LVCEPVFDAARTA-----RALrrhrvthtfgnDEMLRRILDTAGERA-----DFPSAR-----LFGF------------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 444 kiqASLggcvrmivtgaAPASPTVLGFLRAAlGCQVYEGYGQTECTA---GCTFTTPgdWTSGHVGAPLPCN---HIKLV 517
Cdd:PRK06164 302 ---ASF-----------APALGELAALARAR-GVPLTGLYGSSEVQAlvaLQPATDP--VSVRIEGGGRPASpeaRVRAR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 518 DVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEK 597
Cdd:PRK06164 365 DPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNPAE 443
|
490 500 510
....*....|....*....|....*....|....*....
gi 57165412 598 IENIYIRSQPVAQIYVHGDSL--KAFLVGIVVPDPEVMP 634
Cdd:PRK06164 444 IEHALEALPGVAAAQVVGATRdgKTVPVAFVIPTDGASP 482
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
146-634 |
1.27e-17 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 86.22 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVG--PESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 226 DkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhqapvppqPDDLSIVCFTSGTT 305
Cdd:cd12115 103 D-----------------------------------------------------------------PDDLAYVIYTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 306 GNPKGAMLTHGNVVA------------DFSGFLKVTEkVIFprqdDVLI--SFLPLahmferviqsvvyCHGGRVGFFQG 371
Cdd:cd12115 118 GRPKGVAIEHRNAAAflqwaaaafsaeELAGVLASTS-ICF----DLSVfeLFGPL-------------ATGGKVVLADN 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 372 DIRLLsdDMKALCP-TIFPVVPRLLnrmydkifsqantplkRWLLEFaakrkqaevrsgiirndsiwdelffNKIQASlg 450
Cdd:cd12115 180 VLALP--DLPAAAEvTLINTVPSAA----------------AELLRH-------------------------DALPAS-- 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 451 gcVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFT--TPGDWTSGHVGAPLPCNHIKLVDvEELNYWAC 527
Cdd:cd12115 215 --VRVVNLAGEPLPRDLVQRLYARLqVERVVNLYGPSEDTTYSTVApvPPGASGEVSIGRPLANTQAYVLD-RALQPVPL 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 528 KGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENI 601
Cdd:cd12115 292 GVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAA 370
|
490 500 510
....*....|....*....|....*....|....*..
gi 57165412 602 yIRSQP-VAQ--IYVHGDSL-KAFLVGIVVPDPEVMP 634
Cdd:cd12115 371 -LRSIPgVREavVVAIGDAAgERRLVAYIVAEPGAAG 406
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
146-631 |
1.35e-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: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLGSGLLQHNCKActdqfiG--VFAQ--NRPEWIIVELACYtySMVVVPLYdTLgPG----AIRYIINT 217
Cdd:COG1021 51 LSYAELDRRADRLAAGLLALGLRP------GdrVVVQlpNVAEFVIVFFALF--RAGAIPVF-AL-PAhrraEISHFAEQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 218 ADISTVIVDKpqkAVLLLEHVE-----RKETPGLKLIILMDPFEEALkergqkcgvvikSMQAVEDCGQENHQAPvpPQP 292
Cdd:COG1021 121 SEAVAYIIPD---RHRGFDYRAlarelQAEVPSLRHVLVVGDAGEFT------------SLDALLAAPADLSEPR--PDP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 293 DDlsiVCF---TSGTTGNPKGAMLTHG----NVV--ADFSGFlkvtekvifpRQDDVLISFLPLAHMF---ERVIQSVVY 360
Cdd:COG1021 184 DD---VAFfqlSGGTTGLPKLIPRTHDdylySVRasAEICGL----------DADTVYLAALPAAHNFplsSPGVLGVLY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 361 cHGGRVgffqgdirLLSDDMKALcpTIFP-----------VVPRLLNRMydkifsqantplkrwlLEFAAKRKQAevrsg 429
Cdd:COG1021 251 -AGGTV--------VLAPDPSPD--TAFPlierervtvtaLVPPLALLW----------------LDAAERSRYD----- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 430 iirndsiwdeLffnkiqASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctaG-CTFTTPGD--WTSGH-V 505
Cdd:COG1021 299 ----------L------SSL----RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---GlVNYTRLDDpeEVILTtQ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 506 GAPL-PCNHIKLVD-----VEElnywackGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKII 578
Cdd:COG1021 356 GRPIsPDDEVRIVDedgnpVPP-------GEvGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVE 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 57165412 579 DRKK-HIFKlaQGEYVAPEKIENiyirsqpvaQIYVHGDSLKAFLVGivVPDPE 631
Cdd:COG1021 429 GRAKdQINR--GGEKIAAEEVEN---------LLLAHPAVHDAAVVA--MPDEY 469
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
146-615 |
6.20e-17 |
|
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: 84.48 E-value: 6.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRP--GQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 226 dkpqkavllleHVERKETPGLKLIILMDPFEEALKERGQKC--GVVIKsmqavedcgqenhqaPVPPQPDDLSIVCFTSG 303
Cdd:cd05923 107 -----------AVDAQVMDAIFQSGVRVLALSDLVGLGEPEsaGPLIE---------------DPPREPEQPAFVFYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 304 TTGNPKGAMLTHgNVVADFSGFLKVTEKVIFPRQDdVLISFLPLAHMferviqsvvychggrVGFFQgdirLLSDDMkAL 383
Cdd:cd05923 161 TTGLPKGAVIPQ-RAAESRVLFMSTQAGLRHGRHN-VVLGLMPLYHV---------------IGFFA----VLVAAL-AL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 384 CPTIFPVvprllnrmydKIFSQANtplkrwllefAAKRKQAEVRSGIIRNDSIWDELFFNKIQASLG-GCVRMIVTGAAP 462
Cdd:cd05923 219 DGTYVVV----------EEFDPAD----------ALKLIEQERVTSLFATPTHLDALAAAAEFAGLKlSSLRHVTFAGAT 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 463 ASPTVLGFLRAALGCQVYEGYGQTECTagcTFTTPGDWTSGHVGAPLPCNHIKLVDV-EELNYWACKG-EGEICVR--GP 538
Cdd:cd05923 279 MPDAVLERVNQHLPGEKVNIYGTTEAM---NSLYMRDARTGTEMRPGFFSEVRIVRIgGSPDEALANGeEGELIVAaaAD 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57165412 539 NVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYVHG 615
Cdd:cd05923 356 AAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIG 430
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
146-630 |
9.54e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 84.30 E-value: 9.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PLN03102 40 FTWPQTYDRCCRLAASLISLNIT--KNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 226 DKP-----QKAVLLLEHVERKETPGLKLIILMD----PFE-----EALKERGQKCGVVIKSMQAVEDcgqenhqapvppQ 291
Cdd:PLN03102 118 DRSfeplaREVLHLLSSEDSNLNLPVIFIHEIDfpkrPSSeeldyECLIQRGEPTPSLVARMFRIQD------------E 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 292 PDDLSIvCFTSGTTGNPKGAMLTH-GNVVADFSGFLKvTEKVIFPrqddVLISFLPLAH---------MFERVIQSVVYC 361
Cdd:PLN03102 186 HDPISL-NYTSGTTADPKGVVISHrGAYLSTLSAIIG-WEMGTCP----VYLWTLPMFHcngwtftwgTAARGGTSVCMR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 362 HGGRVGFFQgDIRLLSDDMKALCPTIFpvvprllnrmydkifsqantplkRWLLEfaAKRKQAEVRSGIIRndsiwdelf 441
Cdd:PLN03102 260 HVTAPEIYK-NIEMHNVTHMCCVPTVF-----------------------NILLK--GNSLDLSPRSGPVH--------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 442 fnkiqaslggcvrmIVTGAAPAsPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGD-WTSghvgapLPCN-------- 512
Cdd:PLN03102 305 --------------VLTGGSPP-PAALVKKVQRLGFQVMHAYGLTEATGPVLFCEWQDeWNR------LPENqqmelkar 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 513 ----HIKLVDVEELNYWAC-------KGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRK 581
Cdd:PLN03102 364 qgvsILGLADVDVKNKETQesvprdgKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRS 442
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 57165412 582 KHIFkLAQGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGIvvPDP 630
Cdd:PLN03102 443 KDII-ISGGENISSVEVENV---------LYKYPKVLETAVVAM--PHP 479
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
294-601 |
1.32e-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: 81.92 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 294 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIfprQDDVLISFLPLAHMFERV-IQSVVYCHGGRVGFfqGD 372
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWV---VGDVTYLPLPATHIGGLWwILTCLIHGGLCVTG--GE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 373 IRLLSDDMKAL---CPTIFPVVPRLLNRMYDKIFSQANTPLKRWLLEFAAKRkqaevrsgIIRNDSIWDELFFNkiqasl 449
Cdd:cd17635 77 NTTYKSLFKILttnAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSR--------AIAADVRFIEATGL------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 450 ggcvrmivtgaapasptvlgflraalgCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDVEELNYWAcK 528
Cdd:cd17635 143 ---------------------------TNTAQVYGLSETGTALCLPTDDDSIEiNAVGRPYPGVDVYLAATDGIAGPS-A 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57165412 529 GEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENI 601
Cdd:cd17635 195 SFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERI 265
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
292-603 |
2.21e-16 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 82.94 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAHMFerviqsvvychggrvGFFqg 371
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFS----PKEDDVMMSFLPPFHAY---------------GFN-- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 372 dirllsddmkalCPTIFPVVPRLlnrmyDKIFSQanTPLK-RWLLEFAAKRKQAEVRSGIIRNDSIwdeLFFNKIQASLG 450
Cdd:PRK06334 241 ------------SCTLFPLLSGV-----PVVFAY--NPLYpKKIVEMIDEAKVTFLGSTPVFFDYI---LKTAKKQESCL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 451 GCVRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFTT---PGDwtSGHVGAPLPCNHIKLVDvEELNYWA 526
Cdd:PRK06334 299 PSLRFVVIGGDAFKDSLYqEALKTFPHIQLRQGYGTTECSPVITINTvnsPKH--ESCVGMPIRGMDVLIVS-EETKVPV 375
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57165412 527 CKGE-GEICVRGPNVFKGYL-KDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYI 603
Cdd:PRK06334 376 SSGEtGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSLEALESILM 453
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
52-629 |
2.89e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 83.67 E-value: 2.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 52 ATTLVSMGALAAILAYW--FTHRPKAlQPPCNL----LMQSEEVedsggaRRSVIGSGPqllTHYYDDARTMYQVFRRGL 125
Cdd:PRK12467 453 ATDLFEATTIERLATHWrnLLEAIVA-EPRRRLgelpLLDAEER------ARELVRWNA---PATEYAPDCVHQLIEAQA 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 126 SISGNGPCLGFRKpkqpyQWLSYQEVADRAEFLGSGLLQHNckACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDT 205
Cdd:PRK12467 523 RQHPERPALVFGE-----QVLSYAELNRQANRLAHVLIAAG--VGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPE 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 206 LGPGAIRYIINTADISTVIVDKPQKAVLLLehverkeTPGLKLIILMDPfeealkergqkcgvviksmqAVEDCGQENHQ 285
Cdd:PRK12467 596 YPQDRLAYMLDDSGVRLLLTQSHLLAQLPV-------PAGLRSLCLDEP--------------------ADLLCGYSGHN 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 286 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVvadfSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGR 365
Cdd:PRK12467 649 PEVALDPDNLAYVIYTSGSTGQPKGVAISHGAL----ANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGAT 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 366 VgffqgdirLLSDDMKALCPTIFpvvprllnrmYDKIFSQANTPLKrwllefaakrkqaevrsgiiRNDSIWDELFFNKI 445
Cdd:PRK12467 725 L--------HLLPPDCARDAEAF----------AALMADQGVTVLK--------------------IVPSHLQALLQASR 766
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 446 QASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTT----PGDWTSGHVGAPLPCNHIKLVDvEE 521
Cdd:PRK12467 767 VALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYElsdeERDFGNVPIGQPLANLGLYILD-HY 845
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 522 LNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSD------GWLH-TGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVA 594
Cdd:PRK12467 846 LNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDpfgadgGRLYrTGDLARYRADGVIEYLGRMDHQVKI-RGFRIE 924
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 57165412 595 PEKIENIyIRSQP-------VAQIYVHGDSLKAFLVGIVVPD 629
Cdd:PRK12467 925 LGEIEAR-LLAQPgvreavvLAQPGDAGLQLVAYLVPAAVAD 965
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
146-642 |
3.12e-16 |
|
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: 82.03 E-value: 3.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLGSGLLQhnckactdqfIGVFAQNR--------PEWIIVELACYTYSMVVVPLYDTLGPGAIRYIInt 217
Cdd:cd05959 30 LTYAELEAEARRVAGALRA----------LGVKREERvllimldtVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 218 ADI-STVIVDKPQKAVLLLEHVERKEtPGLKLIILMDPFEEALKErgqkcgvviksMQAVEDCGQENHQ-APVPPQPDDL 295
Cdd:cd05959 98 EDSrARVVVVSGELAPVLAAALTKSE-HTLVVLIVSGGAGPEAGA-----------LLLAELVAAEAEQlKPAATHADDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 296 SIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKvteKVIFPRQDDVLIS--------------FLPLAH------MFERVI 355
Cdd:cd05959 166 AFWLYSSGSTGRPKGVVHLHADIYWTAELYAR---NVLGIREDDVCFSaaklffayglgnslTFPLSVgattvlMPERPT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 356 QSVVYchggrvgffqgdirllsDDMKALCPTIFPVVPRLLNRMydkifsqantplkrwlleFAAKRKQAEVRSGIirnds 435
Cdd:cd05959 243 PAAVF-----------------KRIRRYRPTVFFGVPTLYAAM------------------LAAPNLPSRDLSSL----- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 436 iwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTF--TTPGDWTSGHVGAPLPCNH 513
Cdd:cd05959 283 ------------------RLCVSAGEALPAEVGERWKARFGLDILDGIGSTE--MLHIFlsNRPGRVRYGTTGKPVPGYE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 514 IKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSdGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYV 593
Cdd:cd05959 343 VELRD-EDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQG-EWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWV 419
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 57165412 594 APEKIENIYIRSQPVAQIYVHG-------DSLKAFlvgiVVPDPEVMPSWAQKRGI 642
Cdd:cd05959 420 SPFEVESALVQHPAVLEAAVVGvededglTKPKAF----VVLRPGYEDSEALEEEL 471
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
301-631 |
3.44e-16 |
|
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: 81.99 E-value: 3.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 301 TSGTTGNPKGAMLTHgnvvADFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERV---IQSVVYChGGRVgffqgdirLLS 377
Cdd:cd05920 147 SGGTTGTPKLIPRTH----NDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLAcpgVLGTLLA-GGRV--------VLA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 378 DDmkALCPTIFPVVPRllnrmyDKIFSQANTP--LKRWLlEFAAKRKQAEvrsgiirndsiwdelffnkiqASLggcvRM 455
Cdd:cd05920 214 PD--PSPDAAFPLIER------EGVTVTALVPalVSLWL-DAAASRRADL---------------------SSL----RL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 456 IVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHVGAPL-PCNHIKLVDvEELNYWACKGEGEI 533
Cdd:cd05920 260 LQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTrLDDPDEVIIHTQGRPMsPDDEIRVVD-EEGNPVPPGEEGEL 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 534 CVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENiyirsqpvaQIYV 613
Cdd:cd05920 339 LTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVEN---------LLLR 408
|
330
....*....|....*...
gi 57165412 614 HGDSLKAFLVGivVPDPE 631
Cdd:cd05920 409 HPAVHDAAVVA--MPDEL 424
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
132-593 |
4.04e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 82.40 E-value: 4.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 132 PCLGFRKPKQ-PYQWLSYQEVADRAEFLGSGLLqhNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVP--------- 201
Cdd:PRK12582 66 PWLAQREPGHgQWRKVTYGEAKRAVDALAQALL--DLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPvspayslms 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 202 --------LYDTLGPGAI-----------RYIINTADISTVIVDKPQKAVLLLEHVERKETPglkliilmdPFEEalker 262
Cdd:PRK12582 144 hdhaklkhLFDLVKPRVVfaqsgapfaraLAALDLLDVTVVHVTGPGEGIASIAFADLAATP---------PTAA----- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 263 gqkcgvVIKSMQAVedcgqenhqapvppQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekviFPRQDD--- 339
Cdd:PRK12582 210 ------VAAAIAAI--------------TPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQL-----RPREPDppp 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 340 -VLISFLPLAHMFerviqsvvychGGRVGFfQGDIR----LLSDDMKALcPTIFPVVPRLLNRMYDKIFsqANTPLKRWL 414
Cdd:PRK12582 265 pVSLDWMPWNHTM-----------GGNANF-NGLLWgggtLYIDDGKPL-PGMFEETIRNLREISPTVY--GNVPAGYAM 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 415 LEFAAKRKQAEVRSgiirndsiwdelFFNKIqaslggcvRMIVTGAAPASPTVLGFLRA----ALGCQV--YEGYGQTEc 488
Cdd:PRK12582 330 LAEAMEKDDALRRS------------FFKNL--------RLMAYGGATLSDDLYERMQAlavrTTGHRIpfYTGYGATE- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 489 TAGCTFTTpgDWTS---GHVGAPLPCNHIKLVDVEElNYwackgegEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGD 565
Cdd:PRK12582 389 TAPTTTGT--HWDTervGLIGLPLPGVELKLAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGD 458
|
490 500 510
....*....|....*....|....*....|..
gi 57165412 566 IGKWL----PAGTLKIIDRKKHIFKLAQGEYV 593
Cdd:PRK12582 459 AARFVdpddPEKGLIFDGRVAEDFKLSTGTWV 490
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
292-608 |
4.66e-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: 81.77 E-value: 4.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKvifpRQDDVLISFLPLAHmferviqsvvychggRVGFFQG 371
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEW----KTKDRILSWMPLTH---------------DMGLIAF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 372 DIRLLSDDMKA-LCPT-IFPVVPRLLNRMYDK----IFSQANTPLKrWLLEFAAKRKQAEvrsgiirndsiWDElffnki 445
Cdd:cd05908 166 HLAPLIAGMNQyLMPTrLFIRRPILWLKKASEhkatIVSSPNFGYK-YFLKTLKPEKAND-----------WDL------ 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 446 qaslgGCVRMIVTGAAPASP----------TVLGFLRAAlgcqVYEGYGQTECTAGCTF--------------------- 494
Cdd:cd05908 228 -----SSIRMILNGAEPIDYelchefldhmSKYGLKRNA----ILPVYGLAEASVGASLpkaqspfktitlgrrhvthge 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 495 -------TTPGDWTSGHVGAPLPCNHIKLVDveELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDI 566
Cdd:cd05908 299 pepevdkKDSECLTFVEVGKPIDETDIRICD--EDNKILPDGYiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDL 376
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 57165412 567 GkWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPV 608
Cdd:cd05908 377 G-FIRNGRLVITGREKDII-FVNGQNVYPHDIERIAEELEGV 416
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
293-635 |
8.64e-16 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 80.21 E-value: 8.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 293 DDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkvTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGR--VGFFQ 370
Cdd:cd05958 97 DDICILAFTSGTTGAPKATMHFHRDPLASADRY---AVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGAsgVLLEE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 371 GDIRLLSDDMKALCPTIFPVVPRllnrMYdkifsqantplkRWLLEFAAKRKQaevrsgiirndsiwdelffnkiqasLG 450
Cdd:cd05958 174 ATPDLLLSAIARYKPTVLFTAPT----AY------------RAMLAHPDAAGP-------------------------DL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 451 GCVRMIVTgAAPASPTVLGFL-RAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDveELNYWACKG 529
Cdd:cd05958 213 SSLRKCVS-AGEALPAALHRAwKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD--DEGNPVPDG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 530 E-GEICVRGPNVFKgYLKDPDRTKEAldSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSQPV 608
Cdd:cd05958 290 TiGRLAVRGPTGCR-YLADKRQRTYV--QGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQHPAV 365
|
330 340 350
....*....|....*....|....*....|
gi 57165412 609 AQIYVHGDSLKAFLV---GIVVPDPEVMPS 635
Cdd:cd05958 366 AECAVVGHPDESRGVvvkAFVVLRPGVIPG 395
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
482-638 |
9.78e-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: 9.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 482 GYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVE--ELNywacKGE-GEICVRGPNVFKGYLKDPDRTKEALdSD 558
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDgrEVP----DGEvGEIVARGPTVMAGYWNRPEVNARRT-RG 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 559 GWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqgeyvapekIENIY-------IRSQP-VAQIYVhgdslkaflvgIVVPDp 630
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSG---------AENIYpaevercLRQHPaVADAAV-----------IGVPD- 275
|
....*...
gi 57165412 631 evmPSWAQ 638
Cdd:cd17636 276 ---PRWAQ 280
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
283-613 |
2.71e-15 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 78.76 E-value: 2.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 283 NHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkVTEKVIFPRQDDVLISfLPLAHmferVI-QSVVY- 360
Cdd:PRK09029 125 EGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEG---VLSLMPFTAQDSWLLS-LPLFH----VSgQGIVWr 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 361 --CHGGRVGFfqGDIRLLSDDMK-----ALCPTifpVVPRLLNRmydkifSQANTPLKRWLLefaakrkqaevrsgiirn 433
Cdd:PRK09029 197 wlYAGATLVV--RDKQPLEQALAgcthaSLVPT---QLWRLLDN------RSEPLSLKAVLL------------------ 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 434 dsiwdelffnkiqaslGGCvrMIvtgaapasPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTSGhVGAPLPCNH 513
Cdd:PRK09029 248 ----------------GGA--AI--------PVELTEQAEQQGIRCWCGYGLTE-MASTVCAKRADGLAG-VGSPLPGRE 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 514 IKLVDveelnywackgeGEICVRGPNVFKGYLKDpDRTKEALDSDGWLHTGDIGKWLpAGTLKIIDRKKHIFkLAQGEYV 593
Cdd:PRK09029 300 VKLVD------------GEIWLRGASLALGYWRQ-GQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGI 364
|
330 340
....*....|....*....|
gi 57165412 594 APEKIENIYIRSQPVAQIYV 613
Cdd:PRK09029 365 QPEEIERVINQHPLVQQVFV 384
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
288-631 |
4.72e-15 |
|
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: 78.47 E-value: 4.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 288 VPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF-----LKVTEKVIF--PRQDDVLIS--FLPLAHMfERViqsV 358
Cdd:cd17646 133 VPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMqdeypLGPGDRVLQktPLSFDVSVWelFWPLVAG-ARL---V 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 359 VYCHGGRvgffqGDIRLLSDDMKALCPTIFPVVPRLLnrmydkifsqantplkrwllefaakrkqaevrsgiirndsiwd 438
Cdd:cd17646 209 VARPGGH-----RDPAYLAALIREHGVTTCHFVPSML------------------------------------------- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 439 ELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHV--GAPLPCNHIK 515
Cdd:cd17646 241 RVFLAEPAAGSCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVThWPVRGPAETPSVpiGRPVPNTRLY 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 516 LVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH------TGDIGKWLPAGTLKIIDRKKHIFKLaQ 589
Cdd:cd17646 321 VLD-DALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKI-R 398
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 57165412 590 GEYVAPEKIENIyIRSQP-VAQIYV---HGDSLKAFLVGIVVPDPE 631
Cdd:cd17646 399 GFRVEPGEIEAA-LAAHPaVTHAVVvarAAPAGAARLVGYVVPAAG 443
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
175-632 |
4.76e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 78.57 E-value: 4.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 175 IGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAVL--LLEHVERKETPGLKLIILM 252
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLdgLDPGVRVINVDSPAWADEL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 253 DPFEEALKErgqkcgvviksmqavedcgqenhqaPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGflkvtekv 332
Cdd:PRK07867 137 AAHRDAEPP-------------------------FRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVA--SAG-------- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 333 ifprqddvlisfLPLAHMFERVIQSVVYC-----HGGRVgffqgdirllsddMKALCPTIFpvvprllnrmydkifSQAN 407
Cdd:PRK07867 182 ------------VMLAQRFGLGPDDVCYVsmplfHSNAV-------------MAGWAVALA---------------AGAS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 408 TPLKRwllEFAAKRKQAEVRS-GIIrndsiwdelFFNKIqaslGGCVRMIVtgAAP-----------------ASPTVLG 469
Cdd:PRK07867 222 IALRR---KFSASGFLPDVRRyGAT---------YANYV----GKPLSYVL--ATPerpddadnplrivygneGAPGDIA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 470 FLRAALGCQVYEGYGQTEctAGCTFTTPGDWTSGHVGaPLPCNhIKLVDVE--------------ELNYWACKGEgEICV 535
Cdd:PRK07867 284 RFARRFGCVVVDGFGSTE--GGVAITRTPDTPPGALG-PLPPG-VAIVDPDtgtecppaedadgrLLNADEAIGE-LVNT 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 536 RGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYVHG 615
Cdd:PRK07867 359 AGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPIERILLRYPDATEVAVYA 436
|
490
....*....|....*..
gi 57165412 616 dslkaflvgivVPDPEV 632
Cdd:PRK07867 437 -----------VPDPVV 442
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
183-623 |
7.12e-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: 77.89 E-value: 7.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 183 PEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlLLEHVER--KETPGLKLIILMDP------ 254
Cdd:cd05928 78 PEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDE-----LAPEVDSvaSECPSLKTKLLVSEksrdgw 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 255 --FEEALKERGQKcgvviksmqavEDCGQENHQAPvppqpddlSIVCFTSGTTGNPKGAMLTHGN----VVADFSGFLKV 328
Cdd:cd05928 153 lnFKELLNEASTE-----------HHCVETGSQEP--------MAIYFTSGTTGSPKMAEHSHSSlglgLKVNGRYWLDL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 329 TEKVIFPRQDDVLISFLPLAHMFERVIQ-SVVYCHggRVGFFQGDI---RLLSDDMKALC--PTIFpvvprllnRMydki 402
Cdd:cd05928 214 TASDIMWNTSDTGWIKSAWSSLFEPWIQgACVFVH--HLPRFDPLVilkTLSSYPITTFCgaPTVY--------RM---- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 403 fsqantplkrwllefaakrkqaevrsgIIRNDsiwdelfFNKIQ-ASLGGCVrmivTGAAPASPTVLGFLRAALGCQVYE 481
Cdd:cd05928 280 ---------------------------LVQQD-------LSSYKfPSLQHCV----TGGEPLNPEVLEKWKAQTGLDIYE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 482 GYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVR-GPN----VFKGYLKDPDRTKEALD 556
Cdd:cd05928 322 GYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIID-DNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIR 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57165412 557 SDGWLhTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLV 623
Cdd:cd05928 401 GDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYRIGPFEVESALIEHPAVVESAVvsspdpiRGEVVKAFVV 472
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
177-630 |
9.30e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 77.77 E-value: 9.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 177 VFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV--DKPqkavlllEHVE--RKETPGLKLIILM 252
Cdd:PRK07470 62 VHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMIChaDFP-------EHAAavRAASPDLTHVVAI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 253 D--PFEEAlkergqkcgvviksmqaVEDCGQENHQAPVPPQP---DDLSIVCFTSGTTGNPKGAMLTHG-------NVVA 320
Cdd:PRK07470 135 GgaRAGLD-----------------YEALVARHLGARVANAAvdhDDPCWFFFTSGTTGRPKAAVLTHGqmafvitNHLA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 321 DfsgflkvtekvIFP--RQDDVLISFLPLAHMfERVIQSVVYCHGGRVgffqgdIRLLSDDMKAlcptifPVVPRLLNRM 398
Cdd:PRK07470 198 D-----------LMPgtTEQDASLVVAPLSHG-AGIHQLCQVARGAAT------VLLPSERFDP------AEVWALVERH 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 399 YDKIFSQANTPLKrWLLEFAAkrkqaevrsgIIRNDsiwdelffnkiQASLggcvRMIVTGAAPASPTVLGFLRAALGCQ 478
Cdd:PRK07470 254 RVTNLFTVPTILK-MLVEHPA----------VDRYD-----------HSSL----RYVIYAGAPMYRADQKRALAKLGKV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 479 VYEGYGQTECTAGCTFTTP-----GDWTSGHVGaplPCNH--------IKLVDVEELNywacKGE-GEICVRGPNVFKGY 544
Cdd:PRK07470 308 LVQYFGLGEVTGNITVLPPalhdaEDGPDARIG---TCGFertgmevqIQDDEGRELP----PGEtGEICVIGPAVFAGY 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 545 LKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENiyirsqpvaQIYVHGDSLKAFLVG 624
Cdd:PRK07470 381 YNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPREIEE---------KLLTHPAVSEVAVLG 449
|
....*.
gi 57165412 625 ivVPDP 630
Cdd:PRK07470 450 --VPDP 453
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
146-639 |
3.57e-14 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 75.97 E-value: 3.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLGSGLlQHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK05620 39 TTFAAIGARAAALAHAL-HDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 226 D---KPQKAVLLlehverKETPGLKLIILMDPFEEALKERGQKCGVVIKSMQAVEDCGQENHQAPVPPQpDDLSIVCFTS 302
Cdd:PRK05620 118 DprlAEQLGEIL------KECPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALLDGRSTVYDWPELDE-TTAAAICYST 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 303 GTTGNPKGAMLTHGNVVADfSGFLKVTEKviFPRQDDVliSFL---PLAHMFERVIQSVVYCHGgrvgffqgdirllsdd 379
Cdd:PRK05620 191 GTTGAPKGVVYSHRSLYLQ-SLSLRTTDS--LAVTHGE--SFLccvPIYHVLSWGVPLAAFMSG---------------- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 380 mkalCPTIFP----VVPRLLnrmydKIFSqanTPLKRwllefaakrkqaeVRSGIirnDSIWDELFFNKIQ-----ASLg 450
Cdd:PRK05620 250 ----TPLVFPgpdlSAPTLA-----KIIA---TAMPR-------------VAHGV---PTLWIQLMVHYLKnpperMSL- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 451 gcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGA---------PLPCNHiKLVDVEE 521
Cdd:PRK05620 301 ---QEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEARWayrvsqgrfPASLEY-RIVNDGQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 522 LNYWACKGEGEICVRGPNVFKGYLKDP----------------DRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIF 585
Cdd:PRK05620 377 VMESTDRNEGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVI 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 57165412 586 KlAQGEYVAPEKIENIYIRSQPVaqiyvhgdsLKAFLVGIvvPDPEvmpsWAQK 639
Cdd:PRK05620 457 R-SGGEWIYSAQLENYIMAAPEV---------VECAVIGY--PDDK----WGER 494
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
445-613 |
6.92e-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: 74.53 E-value: 6.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 445 IQASLGGC---VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTfTTPGD-WTSGHVGAPLPCNHIKLVDVE 520
Cdd:cd05974 191 IQQDLASFdvkLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVG-NSPGQpVKAGSMGRPLPGYRVALLDPD 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 521 ElnywACKGEGEICV-----RGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAP 595
Cdd:cd05974 270 G----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SSDYRISP 343
|
170
....*....|....*...
gi 57165412 596 EKIENIYIRSQPVAQIYV 613
Cdd:cd05974 344 FELESVLIEHPAVAEAAV 361
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
290-628 |
9.18e-14 |
|
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: 74.03 E-value: 9.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 290 PQPDDLSIVCFTSGTTGNPKGAMLTHGNvvadFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERV--IQSVVychggrvg 367
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGT----FAAQIDALRQLYGIRPGEVDLATFPLFALFGPAlgLTSVI-------- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 368 ffqgdirllsDDMKALCPTifPVVPRllnrmydKIFSqantPLKRWllefaakrkqaEVrSGIIRNDSIWDEL--FFNKI 445
Cdd:cd05910 150 ----------PDMDPTRPA--RADPQ-------KLVG----AIRQY-----------GV-SIVFGSPALLERVarYCAQH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 446 QASLGGcVRMIVTGAAPASPTVLGFLRAAL--GCQVYEGYGQTECTAGCT------FTTPGDWTSGH----VGAPLPCNH 513
Cdd:cd05910 195 GITLPS-LRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrelLATTTAATSGGagtcVGRPIPGVR 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 514 IKLV--DVEELNYWACKGE------GEICVRGPNVFKGYLKDPDRTKEALDSDG----WLHTGDIGKWLPAGTLKIIDRK 581
Cdd:cd05910 274 VRIIeiDDEPIAEWDDTLElprgeiGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRK 353
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 57165412 582 KHIFKLAQGEYVapekieniyirSQPVAQIY-VHGDSLKAFLVGIVVP 628
Cdd:cd05910 354 AHRVITTGGTLY-----------TEPVERVFnTHPGVRRSALVGVGKP 390
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
529-584 |
5.63e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 71.90 E-value: 5.63e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 57165412 529 GE--GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHI 584
Cdd:PRK08162 385 GEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDI 441
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
291-640 |
1.47e-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: 70.54 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 291 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVTEKVIFPRQDDVLISFLPLAhmFERVIQS--VVYCHGGRVGF 368
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMIEHQSLV----NLSHGLIKEYGITSSDRVLQFASIA--FDVAAEEiyVTLLSGATLVL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 369 FQGDIRLLSDDMKALCP----TIFPVVPrllnrmydkifsqantplkrwllefaakrkqaevrsgiirndSIWDELFFNK 444
Cdd:cd17644 178 RPEEMRSSLEDFVQYIQqwqlTVLSLPP------------------------------------------AYWHLLVLEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 445 IQASLGG--CVRMIVTGAAPASPTVLGFLRAALG--CQVYEGYGQTECTAGCTFTTPGDWTSGH-----VGAPLPCNHIK 515
Cdd:cd17644 216 LLSTIDLpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIANTQVY 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 516 LVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH--------TGDIGKWLPAGTLKIIDRKKHIFKL 587
Cdd:cd17644 296 ILD-ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKI 374
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 57165412 588 aQGEYVAPEKIENIYIRSQPVAQ--IYVHGDSL-KAFLVGIVVPDPEVMPSWAQKR 640
Cdd:cd17644 375 -RGFRIELGEIEAVLSQHNDVKTavVIVREDQPgNKRLVAYIVPHYEESPSTVELR 429
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
289-623 |
1.56e-12 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 70.64 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 289 PPQPDDLSIVC-FTSGTTGNPKGAMLTH-GNVVADFSGFLkvtekvIFPRQDD-VLISFLPLAHmferviqsvvyCHGGr 365
Cdd:PLN02479 190 PPADEWQSIALgYTSGTTASPKGVVLHHrGAYLMALSNAL------IWGMNEGaVYLWTLPMFH-----------CNGW- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 366 vgffqgdirLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTplkrwllEFAAkrkqAEVRSGIIRNDSIWDELFfnki 445
Cdd:PLN02479 252 ---------CFTWTLAALCGTNICLRQVTAKAIYSAIANYGVT-------HFCA----APVVLNTIVNAPKSETIL---- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 446 qaSLGGCVRMIVTGAAPaSPTVLgFLRAALGCQVYEGYGQTEcTAG----CTFTTPGDWTSGHVGAPLPCNH-------- 513
Cdd:PLN02479 308 --PLPRVVHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSE-TYGpstvCAWKPEWDSLPPEEQARLNARQgvryigle 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 514 -IKLVDVEELNYWACKGE--GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQG 590
Cdd:PLN02479 383 gLDVVDTKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGG 460
|
330 340 350
....*....|....*....|....*....|...
gi 57165412 591 EYVAPEKIENIyirsqpvaqIYVHGDSLKAFLV 623
Cdd:PLN02479 461 ENISSLEVENV---------VYTHPAVLEASVV 484
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
28-623 |
2.47e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 70.76 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 28 TQEILRILRLPELGDLGQFfrSLSATTLVSMGALAAILAYWFTHRPKAL-----QPPCNLLMQS--------EEVEDSGG 94
Cdd:PRK12316 2959 QLPGLHIESFAWDGAATQF--DLALDTWESAEGLGASLTYATDLFDARTverlaRHWQNLLRGMvenpqrsvDELAMLDA 3036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 95 ARRSVIGSGPQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRKpkqpyQWLSYQEVADRAEFLGSGLLQHNCKActDQF 174
Cdd:PRK12316 3037 EERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVALAFGE-----QRLSYAELNRRANRLAHRLIERGVGP--DVL 3109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 175 IGVFAQNRPEWIIVELACYTYSMVVVPLyDTLGPGAiryiintaDISTVIVDKPQKAVLLLEHVERKETPGLKlIILMDP 254
Cdd:PRK12316 3110 VGVAVERSLEMVVGLLAILKAGGAYVPL-DPEYPEE--------RLAYMLEDSGAQLLLSQSHLRLPLAQGVQ-VLDLDR 3179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 255 FEEALKErgqkcgvviksmqavedcgqenHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNvvadFSGFLKVTEKVIF 334
Cdd:PRK12316 3180 GDENYAE----------------------ANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSA----LSNHLCWMQQAYG 3233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 335 PRQDDVLISFLPLAHMFERVIQSVVYCHGGRVgfFQGDIRLLSDdmkalcptifpvvPRLLNRMYDKifSQANTPLKRWl 414
Cdd:PRK12316 3234 LGVGDRVLQFTTFSFDVFVEELFWPLMSGARV--VLAGPEDWRD-------------PALLVELINS--EGVDVLHAYP- 3295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 415 lefaakrkqaevrsgiirndSIWDELFFNKIQASLGGCVRMIVTGAAPASPtvlGFLRAALGCQVYEGYGQTECTAGCTF 494
Cdd:PRK12316 3296 --------------------SMLQAFLEEEDAHRCTSLKRIVCGGEALPAD---LQQQVFAGLPLYNLYGPTEATITVTH 3352
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 495 TTPGDWTSGH--VGAPLPCNHIKLVDVeELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGW------LHTGDI 566
Cdd:PRK12316 3353 WQCVEEGKDAvpIGRPIANRACYILDG-SLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDL 3431
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 567 GKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPV---AQIYVHGDSLKAFLV 623
Cdd:PRK12316 3432 ARYRADGVIEYIGRVDHQVKI-RGFRIELGEIEARLLEHPWVreaVVLAVDGRQLVAYVV 3490
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
286-592 |
3.33e-12 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 69.54 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 286 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkvteKVIFP-RQDDVLISFLPLAHMFERV--IQSVVych 362
Cdd:PRK09274 167 PMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEAL-----REDYGiEPGEIDLPTFPLFALFGPAlgMTSVI--- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 363 ggrvgffqgdirllsDDMKALCP-TIFPvvprllnrmyDKIFSQ----------ANTPLKRWLLEFAAKRKQaevrsgii 431
Cdd:PRK09274 239 ---------------PDMDPTRPaTVDP----------AKLFAAierygvtnlfGSPALLERLGRYGEANGI-------- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 432 rndsiwdelffnkiqaSLGGCVRMIVTGAaPASPTVLGFLRAAL--GCQVYEGYGQTECTAGCT-------FTTPGDWTS 502
Cdd:PRK09274 286 ----------------KLPSLRRVISAGA-PVPIAVIERFRAMLppDAEILTPYGATEALPISSiesreilFATRAATDN 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 503 GH---VGAPLPCNHIKLVDV--EELNYWA-----CKGE-GEICVRGPNVFKGYLKDPDRTKEA--LDSDG--WLHTGDIG 567
Cdd:PRK09274 349 GAgicVGRPVDGVEVRIIAIsdAPIPEWDdalrlATGEiGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLG 428
|
330 340
....*....|....*....|....*.
gi 57165412 568 kWL-PAGTLKIIDRKKHIFKLAQGEY 592
Cdd:PRK09274 429 -YLdAQGRLWFCGRKAHRVETAGGTL 453
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
146-631 |
5.76e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 68.80 E-value: 5.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRpEWIIVELACYTYSmvvvplydtlgpGAIRYIINTAdistviV 225
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRA--GDGVAVLARNH-RGFVLALYAAGKV------------GARIILLNTG------F 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 226 DKPQkavlLLEHVERKetpGLKLIILMDPFEE---ALKERGQKCGVVIKSMQAVEDC------------GQENHQAPVPP 290
Cdd:PRK07788 134 SGPQ----LAEVAARE---GVKALVYDDEFTDllsALPPDLGRLRAWGGNPDDDEPSgstdetlddliaGSSTAPLPKPP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 291 QPDdlSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLkvtEKVIFPRQDDVLISflplAHMFerviqsvvycHGgrVGFFQ 370
Cdd:PRK07788 207 KPG--GIVILTSGTTGTPKGAPRPEPSPLAPLAGLL---SRVPFRAGETTLLP----APMF----------HA--TGWAH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 371 GDI-----------------RLLSDDMKALCPTIFpVVPRLLNRMYDkifsqantplkrwLLEfaakrkqaEVRSgiirn 433
Cdd:PRK07788 266 LTLamalgstvvlrrrfdpeATLEDIAKHKATALV-VVPVMLSRILD-------------LGP--------EVLA----- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 434 dsiwdelffnKIQASlggCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECtAGCTFTTPGDWT--SGHVGAPLPC 511
Cdd:PRK07788 319 ----------KYDTS---SLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEV-AFATIATPEDLAeaPGTVGRPPKG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 512 NHIKLVD-----VEElnywackGE-GEICVRGPNVFKGYlKDPdRTKEALdsDGWLHTGDIGKWLPAGTLKIIDRKKHIF 585
Cdd:PRK07788 385 VTVKILDengneVPR-------GVvGRIFVGNGFPFEGY-TDG-RDKQII--DGLLSSGDVGYFDEDGLLFVDGRDDDMI 453
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 57165412 586 kLAQGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDPE 631
Cdd:PRK07788 454 -VSGGENVFPAEVEDL---------LAGHPDVVEAAVIG--VDDEE 487
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
144-624 |
7.45e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 69.22 E-value: 7.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 144 QWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLyDTLGPGA-IRYIINTADIST 222
Cdd:PRK12316 2027 QHLSYAELDSRANRLAHRLRARGVGP--EVRVAIAAERSFELVVALLAVLKAGGAYVPL-DPNYPAErLAYMLEDSGAAL 2103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 223 VIVDKPQKAVLLLehverkeTPGLKLIILMDPfeEALKERGQKcgvviksmqavedcgqenhqAPVPP-QPDDLSIVCFT 301
Cdd:PRK12316 2104 LLTQRHLLERLPL-------PAGVARLPLDRD--AEWADYPDT--------------------APAVQlAGENLAYVIYT 2154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 302 SGTTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPLAhmFERVIQSVVY--CHGGRVgffqgdirLLSDD 379
Cdd:PRK12316 2155 SGSTGLPKGVAVSHGALVA----HCQAAGERYELSPADCELQFMSFS--FDGAHEQWFHplLNGARV--------LIRDD 2220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 380 MKalcptifpvvpRLLNRMYDKIFSQANTplkrwLLEFAAKRKQAEVRsgiirndsiwdelffnkiQASLGGC---VRMI 456
Cdd:PRK12316 2221 EL-----------WDPEQLYDEMERHGVT-----ILDFPPVYLQQLAE------------------HAERDGRppaVRVY 2266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 457 VTGAAPASPTVLGFLRAALGCQ-VYEGYGQTEctagcTFTTPGDWTSGH----------VGAPLPCNHIKLVDvEELNYW 525
Cdd:PRK12316 2267 CFGGEAVPAASLRLAWEALRPVyLFNGYGPTE-----AVVTPLLWKCRPqdpcgaayvpIGRALGNRRAYILD-ADLNLL 2340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 526 ACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH-------TGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKI 598
Cdd:PRK12316 2341 APGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKI-RGFRIELGEI 2419
|
490 500 510
....*....|....*....|....*....|...
gi 57165412 599 ENiYIRSQP-------VAQIYVHGDSLKAFLVG 624
Cdd:PRK12316 2420 EA-RLQAHPavreavvVAQDGASGKQLVAYVVP 2451
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
146-630 |
9.76e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 67.99 E-value: 9.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGP--GDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 226 DK---PQKAVLLlehverKETPGLKLIILMD------------PFEEALKErgqkcgvviksmqavedcgQENHQAPVPP 290
Cdd:PRK07798 107 ERefaPRVAEVL------PRLPKLRTLVVVEdgsgndllpgavDYEDALAA-------------------GSPERDFGER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 291 QPDDLSIVCfTSGTTGNPKGAMLTHGNV-VADFSGFLKVTEKVIfprQDDVLIS----------FLPLAHMFERVIQSVV 359
Cdd:PRK07798 162 SPDDLYLLY-TGGTTGMPKGVMWRQEDIfRVLLGGRDFATGEPI---EDEEELAkraaagpgmrRFPAPPLMHGAGQWAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 360 YchggrVGFFQGDIRLLSDDMKalcptifpvvprllnrmydkiFSQANtplkrwLLEFAAKRKqaeVRSGIIRNDS---- 435
Cdd:PRK07798 238 F-----AALFSGQTVVLLPDVR---------------------FDADE------VWRTIEREK---VNVITIVGDAmarp 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 436 IWDELffnkiqASLGG----CVRMIVTGAAPASPTV-LGFLRAALGCQVYEGYGQTECTAGCTFTTPGDwtSGHVGAPL- 509
Cdd:PRK07798 283 LLDAL------EARGPydlsSLFAIASGGALFSPSVkEALLELLPNVVLTDSIGSSETGFGGSGTVAKG--AVHTGGPRf 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 510 -PCNHIKLVDvEELNYWAcKGEGEICV--RGPNVFKGYLKDPDRTKEALDS-DG--WLHTGDIGKWLPAGTLKIIDRKKH 583
Cdd:PRK07798 355 tIGPRTVVLD-EDGNPVE-PGSGEIGWiaRRGHIPLGYYKDPEKTAETFPTiDGvrYAIPGDRARVEADGTITLLGRGSV 432
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 57165412 584 IFKLAqGEYVAPEKIENIyIRSQPvaqiyvhgDSLKAFLVGivVPDP 630
Cdd:PRK07798 433 CINTG-GEKVFPEEVEEA-LKAHP--------DVADALVVG--VPDE 467
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
111-664 |
1.18e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 68.65 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 111 YDDARTMYQVFRRGLSISGNGPCLGFRKpkqpyQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVEL 190
Cdd:PRK12467 1570 YPLARLVHQLIEDQAAATPEAVALVFGE-----QELTYGELNRRANRLAHRLIALGVGP--EVLVGIAVERSLEMVVGLL 1642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 191 ACYTYSMVVVPLYDTLGPGAIRYIINTADIStvivdkpqkavLLLEHveRKETPGLKLIilmdpfeealkeRGQKCGVVI 270
Cdd:PRK12467 1643 AILKAGGAYVPLDPEYPRERLAYMIEDSGIE-----------LLLTQ--SHLQARLPLP------------DGLRSLVLD 1697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 271 KSMQAVEDCGQENHQapVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFsgflKVTEKVIFPRQDDVLISFLPLAhm 350
Cdd:PRK12467 1698 QEDDWLEGYSDSNPA--VNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRL----CATQEAYQLSAADVVLQFTSFA-- 1769
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 351 FERVIQSVVY--CHGGRVgffqgdirLLSDDMKALCPtifpvvprllNRMYDKIFSQANTplkrwLLEFAAKRKQAevrs 428
Cdd:PRK12467 1770 FDVSVWELFWplINGARL--------VIAPPGAHRDP----------EQLIQLIERQQVT-----TLHFVPSMLQQ---- 1822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 429 giirndsiwdelfFNKIQASLGGC--VRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAG-----CTFTTPGDW 500
Cdd:PRK12467 1823 -------------LLQMDEQVEHPlsLRRVVCGGEALEVEALRPWLERLPdTGLFNLYGPTETAVDvthwtCRRKDLEGR 1889
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 501 TSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL------DSDGWLH-TGDIGKWLPAG 573
Cdd:PRK12467 1890 DSVPIGQPIANLSTYILD-ASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgTVGSRLYrTGDLARYRADG 1968
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 574 TLKIIDRKKHIFKLaQGEYVAPEKIENiYIRSQP----VAQIYVHGDSLKAfLVGIVVPDPEVMPSWAQKRgieGTYADl 649
Cdd:PRK12467 1969 VIEYLGRIDHQVKI-RGFRIELGEIEA-RLREQGgvreAVVIAQDGANGKQ-LVAYVVPTDPGLVDDDEAQ---VALRA- 2041
|
570
....*....|....*.
gi 57165412 650 cTNKDLKKAILED-MV 664
Cdd:PRK12467 2042 -ILKNHLKASLPEyMV 2056
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
460-631 |
1.37e-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: 67.40 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 460 AAPASPTVLGFLRAALGCQVYEGYGQTECTaGCTFTTPGDWTS--GHVGAPLPcNHIKLVDvEELNYWACKGEGEICVRG 537
Cdd:cd05929 253 AAPCPPWVKEQWIDWGGPIIWEYYGGTEGQ-GLTIINGEEWLThpGSVGRAVL-GKVHILD-EDGNEVPPGEIGEVYFAN 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 538 PNVFKgYLKDPDRTKEALDSDGWLHTGDIGkWLPA-GTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRsqpvaqiyvHGD 616
Cdd:cd05929 330 GPGFE-YTNDPEKTAAARNEGGWSTLGDVG-YLDEdGYLYLTDRRSDMI-ISGGVNIYPQEIENALIA---------HPK 397
|
170
....*....|....*
gi 57165412 617 SLKAFLVGivVPDPE 631
Cdd:cd05929 398 VLDAAVVG--VPDEE 410
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
280-635 |
2.07e-11 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 67.03 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 280 GQENHQAPVPPQPDDLsivCFTSGTTGNPKGAMLTHGNVvadfsGFLKVTEKVI-----FPRQDDVLISFlPLAHmferv 354
Cdd:PRK12406 142 QQEPYDGPPVPQPQSM---IYTSGTTGHPKGVRRAAPTP-----EQAAAAEQMRaliygLKPGIRALLTG-PLYH----- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 355 iqSVVYCHGGRVGFFQGDIRLLS----DDMKALCP-----TIFpVVPRLLNRmydkifsqantplkrwLLEFAAKRKQAE 425
Cdd:PRK12406 208 --SAPNAYGLRAGRLGGVLVLQPrfdpEELLQLIErhritHMH-MVPTMFIR----------------LLKLPEEVRAKY 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 426 VRSgiirndsiwdelffnkiqaSLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--G 503
Cdd:PRK12406 269 DVS-------------------SL----RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE-SGAVTFATSEDALShpG 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 504 HVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNV--FKgYLKDPDRTKEaLDSDGWLHTGDIGkWLPA-GTLKIIDR 580
Cdd:PRK12406 325 TVGKAAPGAELRFVD-EDGRPLPQGEIGEIYSRIAGNpdFT-YHNKPEKRAE-IDRGGFITSGDVG-YLDAdGYLFLCDR 400
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 57165412 581 KKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAF---LVGIVVPDPEVMPS 635
Cdd:PRK12406 401 KRDMV-ISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFgeaLMAVVEPQPGATLD 457
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
146-631 |
4.21e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 66.08 E-value: 4.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLRE--GDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 226 DKPQKAVL--LLEHVERketpGLKLIILMD-------PFEEALKErgqkcgvviksmqavedcgqenhQAPVPPqPDDL- 295
Cdd:PRK08276 90 SAALADTAaeLAAELPA----GVPLLLVVAgpvpgfrSYEEALAA-----------------------QPDTPI-ADETa 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 296 -SIVCFTSGTTGNPKGAM--LTHGNVVADFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQgd 372
Cdd:PRK08276 142 gADMLYSSGTTGRPKGIKrpLPGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAPLRFGMSALALGGTVVVME-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 373 iRLLSDDMKALCP----TIFPVVPRLLNRMydkifsqantpLKrwLLEfaakrkqaEVRSgiiRNDSiwdelffnkiqAS 448
Cdd:PRK08276 220 -KFDAEEALALIEryrvTHSQLVPTMFVRM-----------LK--LPE--------EVRA---RYDV-----------SS 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 449 LggcvRMIVTGAAPASPTVLgflRAAL---GCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCNhIKLVDvEELN 523
Cdd:PRK08276 264 L----RVAIHAAAPCPVEVK---RAMIdwwGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGE-VRILD-EDGN 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 524 YWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkWLPA-GTLKIIDRKKHIFkLAQGEYVAPEKIENIY 602
Cdd:PRK08276 334 ELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVG-YLDEdGYLYLTDRKSDMI-ISGGVNIYPQEIENLL 411
|
490 500
....*....|....*....|....*....
gi 57165412 603 IRSQPVAQIYVHGdslkaflvgivVPDPE 631
Cdd:PRK08276 412 VTHPKVADVAVFG-----------VPDEE 429
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
296-609 |
1.11e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 64.73 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 296 SIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDIrl 375
Cdd:PRK07008 179 SSLCYTSGTTGNPKGALYSHRSTV--LHAYGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPLTGAKLVLPGPDL-- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 376 lsdDMKALcptifpvvprllnrmYDKIFSQANTplkrwlleFAAkrkqaevrsGIirnDSIWDELFFNKIQASLG-GCVR 454
Cdd:PRK07008 255 ---DGKSL---------------YELIEAERVT--------FSA---------GV---PTVWLGLLNHMREAGLRfSTLR 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 455 MIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPgdwTSGHVGAPLPCNH--------------IKLVDVE 520
Cdd:PRK07008 297 RTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLCKL---KWKHSQLPLDEQRkllekqgrviygvdMKIVGDD 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 521 --ELNyWACKGEGEICVRGPNVFKGYLKdpdRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKI 598
Cdd:PRK07008 374 grELP-WDGKAFGDLQVRGPWVIDRYFR---GDASPLV-DGWFPTGDVATIDADGFMQITDRSKDVIK-SGGEWISSIDI 447
|
330
....*....|.
gi 57165412 599 ENIYIRSQPVA 609
Cdd:PRK07008 448 ENVAVAHPAVA 458
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
286-623 |
1.31e-10 |
|
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: 64.47 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 286 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGN--VVADFSGflkvtEKVIFPRQDDVLIS--------------FLPLA- 348
Cdd:TIGR02262 154 KPAATQADDPAFWLYSSGSTGMPKGVVHTHSNpyWTAELYA-----RNTLGIREDDVCFSaaklffayglgnalTFPMSv 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 349 -----HMFERVIQSVVYchggrvgffqgdirllsDDMKALCPTIFPVVPRLlnrmYDKIFSQANTPlkrwllefaaKRKQ 423
Cdd:TIGR02262 229 gattvLMGERPTPDAVF-----------------DRLRRHQPTIFYGVPTL----YAAMLADPNLP----------SEDQ 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 424 AEVRsgiirndsiwdelffnkiqaslggcvrmIVTGAAPASPTVLGF-LRAALGCQVYEGYGQTEctAGCTFTT--PGDW 500
Cdd:TIGR02262 278 VRLR----------------------------LCTSAGEALPAEVGQrWQARFGVDIVDGIGSTE--MLHIFLSnlPGDV 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 501 TSGHVGAPLPCNHIKLVDveELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSdGWLHTGDigKWL--PAGTLKI 577
Cdd:TIGR02262 328 RYGTSGKPVPGYRLRLVG--DGGQDVADGEpGELLISGPSSATMYWNNRAKSRDTFQG-EWTRSGD--KYVrnDDGSYTY 402
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 57165412 578 IDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVHG----DSL---KAFLV 623
Cdd:TIGR02262 403 AGRTDDMLKVS-GIYVSPFEIESALIQHPAVLEAAVVGvadeDGLikpKAFVV 454
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
299-615 |
2.12e-10 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 63.62 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 299 CFTSGTTGNPKGAMLTHgnvvadfsgflkvtekvifpRQDdvlisflplahmferVIQSVVYCHGGRVGFFQGDirllsd 378
Cdd:PRK06018 183 CYTSGTTGDPKGVLYSH--------------------RSN---------------VLHALMANNGDALGTSAAD------ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 379 dmkalcpTIFPVVPrllnrMYdkifsQANTplkrWLLEFAAKRKQAEVRSGIIRND--SIWDELFFNKIQASLG------ 450
Cdd:PRK06018 222 -------TMLPVVP-----LF-----HANS----WGIAFSAPSMGTKLVMPGAKLDgaSVYELLDTEKVTFTAGvptvwl 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 451 -------------GCVRMIVTGAApASPTvlGFLRA--ALGCQVYEGYGQTECTAGCTFTT--------PGDWTSGHV-- 505
Cdd:PRK06018 281 mllqymekeglklPHLKMVVCGGS-AMPR--SMIKAfeDMGVEVRHAWGMTEMSPLGTLAAlkppfsklPGDARLDVLqk 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 506 -GAPLPCNHIKLVDVE--ELNyWACKGEGEICVRGPNVFKGYLKDPDrtkEALDSDGWLHTGDIGKWLPAGTLKIIDRKK 582
Cdd:PRK06018 358 qGYPPFGVEMKITDDAgkELP-WDGKTFGRLKVRGPAVAAAYYRVDG---EILDDDGFFDTGDVATIDAYGYMRITDRSK 433
|
330 340 350
....*....|....*....|....*....|...
gi 57165412 583 HIFKlAQGEYVAPEKIENIYIRSQPVAQIYVHG 615
Cdd:PRK06018 434 DVIK-SGGEWISSIDLENLAVGHPKVAEAAVIG 465
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
289-582 |
2.24e-10 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 63.87 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 289 PPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifpRQDDVLISFLPLAH-MferviqsvvychgGRVG 367
Cdd:PRK09192 172 RPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDGLKV---RPGDRCVSWLPFYHdM-------------GLVG 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 368 FF------QgdirlLSDDmkaLCPT-IFPVVP----RLLNRMYDKI-FSQAntplkrWLLEFAAKRkqAEVRSGIIRNDS 435
Cdd:PRK09192 236 FLltpvatQ-----LSVD---YLPTrDFARRPlqwlDLISRNRGTIsYSPP------FGYELCARR--VNSKDLAELDLS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 436 IWdelffnkiqaslggcvRMIVTGAAPASPTVL----------GF-LRAALGCqvyegYGQTECTAGCTFTTPG------ 498
Cdd:PRK09192 300 CW----------------RVAGIGADMIRPDVLhqfaeafapaGFdDKAFMPS-----YGLAEATLAVSFSPLGsgivve 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 499 ----DWTSGH------------------VGAPLPCNHIKLVDV--EELNYwacKGEGEICVRGPNVFKGYLKDPDRTKeA 554
Cdd:PRK09192 359 evdrDRLEYQgkavapgaetrrvrtfvnCGKALPGHEIEIRNEagMPLPE---RVVGHICVRGPSLMSGYFRDEESQD-V 434
|
330 340
....*....|....*....|....*...
gi 57165412 555 LDSDGWLHTGDIGkWLPAGTLKIIDRKK 582
Cdd:PRK09192 435 LAADGWLDTGDLG-YLLDGYLYITGRAK 461
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
293-599 |
2.40e-10 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 63.26 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 293 DDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVT-EKVIFPRQDDVLiSFLPLAhmFERVIQSVV--YCHGGRvgff 369
Cdd:cd17656 128 DDLLYIIYTSGTTGKPKGVQLEHKNMV----NLLHFErEKTNINFSDKVL-QFATCS--FDVCYQEIFstLLSGGT---- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 370 qgdIRLLSDDMKALCPTIFPVVPRllNRMYDKIFSQAntplkrwLLEFAAKRKQaevrsgiirndsiwdelFFNkiqaSL 449
Cdd:cd17656 197 ---LYIIREETKRDVEQLFDLVKR--HNIEVVFLPVA-------FLKFIFSERE-----------------FIN----RF 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 450 GGCVRMIVTGAAP--ASPTVLGFLRAAlGCQVYEGYG--QTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDvEELNY 524
Cdd:cd17656 244 PTCVKHIITAGEQlvITNEFKEMLHEH-NVHLHNHYGpsETHVVTTYTINPEAEIPElPPIGKPISNTWIYILD-QEQQL 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 525 WACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGW------LHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKI 598
Cdd:cd17656 322 QPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-RGYRIELGEI 400
|
.
gi 57165412 599 E 599
Cdd:cd17656 401 E 401
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
292-638 |
2.96e-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: 63.16 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPL----AHmfERVIQSVVycHGGRV- 366
Cdd:cd17649 93 PRQLAYVIYTSGSTGTPKGVAVSHGPLAA----HCQATAERYGLTPGDRELQFASFnfdgAH--EQLLPPLI--CGACVv 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 367 ---GFFQGDIRLLSDDMKALCPTIFPVVPRLLNRmydkifsqantpLKRWLLEFAAKRKQAevrsgiirndsiwdelffn 443
Cdd:cd17649 165 lrpDELWASADELAEMVRELGVTVLDLPPAYLQQ------------LAEEADRTGDGRPPS------------------- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 444 kiqaslggcVRMIVTGAAPASPTvlgFLRAALGCQVY--EGYGQTECTAGCT-FTTPGD----WTSGHVGAPLPCNHIKL 516
Cdd:cd17649 214 ---------LRLYIFGGEALSPE---LLRRWLKAPVRlfNAYGPTEATVTPLvWKCEAGaaraGASMPIGRPLGGRSAYI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 517 VDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL--DSDG-----WLHTGDIGKWLPAGTLKIIDRKKHIFKLaQ 589
Cdd:cd17649 282 LD-ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFvpDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-R 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 57165412 590 GEYVAPEKIENiYIRSQP----VAQIYVHGDSLKAfLVGIVVP-DPEVMPSWAQ 638
Cdd:cd17649 360 GFRIELGEIEA-ALLEHPgvreAAVVALDGAGGKQ-LVAYVVLrAAAAQPELRA 411
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
291-640 |
4.14e-10 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 62.66 E-value: 4.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 291 QPDDLSIVCFTSGTTGNPKGAMLTH---GNVVADFSGFLKVTEkvifprqDDVLISFLPLAhmFERVIQSVV--YCHGGR 365
Cdd:cd17652 91 TPDNLAYVIYTSGSTGRPKGVVVTHrglANLAAAQIAAFDVGP-------GSRVLQFASPS--FDASVWELLmaLLAGAT 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 366 vgffqgdirllsddmkaLCptifpVVPRLLnrmydkifSQANTPLKRWLlefaakrkQAEVRSGIIRNDSIWDELffnkI 445
Cdd:cd17652 162 -----------------LV-----LAPAEE--------LLPGEPLADLL--------REHRITHVTLPPAALAAL----P 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 446 QASLGGCVRMIVTGAAPASPTVLgflRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLVDvEELNY 524
Cdd:cd17652 200 PDDLPDLRTLVVAGEACPAELVD---RWAPGRRMINAYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYVLD-ARLRP 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 525 WACKGEGEICVRGPNVFKGYLKDPDRTKEALDSD------GWLH-TGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEK 597
Cdd:cd17652 276 VPPGVPGELYIAGAGLARGYLNRPGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKI-RGFRIELGE 354
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 57165412 598 IENIYIRSQPVAQ--IYVHGDSL-KAFLVGIVVPDPEVMPSWAQKR 640
Cdd:cd17652 355 VEAALTEHPGVAEavVVVRDDRPgDKRLVAYVVPAPGAAPTAAELR 400
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
177-320 |
4.80e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 62.61 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 177 VFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADiSTVIVDKPQkavlLLEHVERKETPGLKLIILMDPFE 256
Cdd:PRK04319 103 IFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSE-AKVLITTPA----LLERKPADDLPSLKHVLLVGEDV 177
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57165412 257 EAlkerGQKCGVVIKSM-QAVEDCgqenhqAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVA 320
Cdd:PRK04319 178 EE----GPGTLDFNALMeQASDEF------DIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQ 232
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
282-610 |
5.61e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 63.26 E-value: 5.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 282 ENHQAPVPpQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFS----GFlkvtekVIFPRQDDVLISFLPLAHMFERV--- 354
Cdd:PRK05691 156 EAWQEPAL-QPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQlirhGF------GIDLNPDDVIVSWLPLYHDMGLIggl 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 355 ---IQSVVYCHGGRVGFF--------------QGDIRLLSDDMKALCPtifpvvprllNRMYDKIFSQANtpLKRWLLEF 417
Cdd:PRK05691 229 lqpIFSGVPCVLMSPAYFlerplrwleaiseyGGTISGGPDFAYRLCS----------ERVSESALERLD--LSRWRVAY 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 418 AAkrkqaevrSGIIRNDSIwdELFFNKIQ----------ASLG-GCVRMIVTGAAPA-SPTVLGFLRAALGCQVYEGyGQ 485
Cdd:PRK05691 297 SG--------SEPIRQDSL--ERFAEKFAacgfdpdsffASYGlAEATLFVSGGRRGqGIPALELDAEALARNRAEP-GT 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 486 TECTAGCTFTTPGdwtsghvgaplpcNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEA---LDSDGWLH 562
Cdd:PRK05691 366 GSVLMSCGRSQPG-------------HAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfveHDGRTWLR 432
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 57165412 563 TGDIGkWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQ 610
Cdd:PRK05691 433 TGDLG-FLRDGELFVTGRLKDML-IVRGHNLYPQDIEKTVEREVEVVR 478
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
280-644 |
7.87e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 62.67 E-value: 7.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 280 GQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPLAhmFERVIQSV- 358
Cdd:PRK12316 4681 GFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVN----HLHATGERYELTPDDRVLQFMSFS--FDGSHEGLy 4754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 359 -VYCHGGRVgffqgdirLLSDDMKALcPTifpvvpRLLNRMYDKIFSQANTPLKRW--LLEFAAKRKQ-AEVRsgiirnd 434
Cdd:PRK12316 4755 hPLINGASV--------VIRDDSLWD-PE------RLYAEIHEHRVTVLVFPPVYLqqLAEHAERDGEpPSLR------- 4812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 435 siwdelffnkiQASLGGcvrmivTGAAPASPTVLgfLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSG----HVGAPL 509
Cdd:PRK12316 4813 -----------VYCFGG------EAVAQASYDLA--WRALKPVYLFNGYGPTETTVTVLlWKARDGDACGaaymPIGTPL 4873
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 510 PCNHIKLVDVEeLNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSD------GWLH-TGDIGKWLPAGTLKIIDRKK 582
Cdd:PRK12316 4874 GNRSGYVLDGQ-LNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDpfgapgGRLYrTGDLARYRADGVIDYLGRVD 4952
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 583 HIFKLaQGEYVAPEKIEnIYIRSQP-------VAQIYVHGdslkAFLVGIVVP-DPEVMPSWAQKRGIEG 644
Cdd:PRK12316 4953 HQVKI-RGFRIELGEIE-ARLREHPavreavvIAQEGAVG----KQLVGYVVPqDPALADADEAQAELRD 5016
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
280-601 |
1.07e-09 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 61.32 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 280 GQENHQAPVPPQPD-DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkVTEKVIFPRQDDVLISFLPLAH-Mferviqs 357
Cdd:PRK05851 138 AHTNRSASLTPPDSgGPAVLQGTAGSTGTPRTAILSPGAVLSNLRG---LNARVGLDAATDVGCSWLPLYHdM------- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 358 vvychggrvgffqGDIRLLSDDMKA----LCPTifpvvprllnrmydKIFSQAntPLK--RWLLEFAAKRKQA-EVRSGI 430
Cdd:PRK05851 208 -------------GLAFLLTAALAGaplwLAPT--------------TAFSAS--PFRwlSWLSDSRATLTAApNFAYNL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 431 IRNdsiwdelFFNKIQASLGGCVRMIVTGAAP----------ASPTVLGFLRAALGcqvyEGYGQTECTAGCTFTTPG-- 498
Cdd:PRK05851 259 IGK-------YARRVSDVDLGALRVALNGGEPvdcdgferfaTAMAPFGFDAGAAA----PSYGLAESTCAVTVPVPGig 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 499 ---------DWTSGH----VGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPdrtkeALDSDGWLHTGD 565
Cdd:PRK05851 328 lrvdevttdDGSGARrhavLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQA-----PIDPDDWFPTGD 402
|
330 340 350
....*....|....*....|....*....|....*.
gi 57165412 566 IGkWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENI 601
Cdd:PRK05851 403 LG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERV 436
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
291-639 |
1.16e-09 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 61.03 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 291 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVaDFSGFLKVTEKVIFPRQDDVLISFLPLAHMFErviqsvVYCH---GGRVG 367
Cdd:cd17645 102 NPDDLAYVIYTSGSTGLPKGVMIEHHNLV-NLCEWHRPYFGVTPADKSLVYASFSFDASAWE------IFPHltaGAALH 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 368 FFQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTPLkRWLLEFAAKRKQAEVRsgiirndsiwdelffnkiqa 447
Cdd:cd17645 175 VVPSERRLDLDALNDYFNQEGITISFLPTGAAEQFMQLDNQSL-RVLLTGGDKLKKIERK-------------------- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 448 slggcvrmivtgaapasptvlgflraalGCQVYEGYGQTECTAGCT-FTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWA 526
Cdd:cd17645 234 ----------------------------GYKLVNNYGPTENTVVATsFEIDKPYANIPIGKPIDNTRVYILD-EALQLQP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 527 CKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIEN 600
Cdd:cd17645 285 IGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIEP 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 57165412 601 I---YIRSQPVAQIYVHGDSLKAFLVGIVVP----DPEVMPSWAQK 639
Cdd:cd17645 364 FlmnHPLIELAAVLAKEDADGRKYLVAYVTApeeiPHEELREWLKN 409
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
292-634 |
4.57e-09 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 59.34 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSG--FLKVTEkvifprqDDVLISFLplAHMFE-RVIQSVVYCHGGR 365
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVnlrTSLSEryFGRDNG-------DEAVLFFS--NYVFDfFVEQMTLALLNGQ 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 366 vgffqgDIRLLSDDMKALCPTIfpvvPRLLNRmyDKIFSQANTPLKRWLLEFAakrkqaevrsgiirndsiwdelffnki 445
Cdd:cd17648 164 ------KLVVPPDEMRFDPDRF----YAYINR--EKVTYLSGTPSVLQQYDLA--------------------------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 446 qaSLGGCVRMIVTGAAPASPtVLGFLRAALGCQVYEGYGQTEC--TAGCTFTTPGDWTSGHVGAPLPCNHIKLVDvEELN 523
Cdd:cd17648 205 --RLPHLKRVDAAGEEFTAP-VFEKLRSRFAGLIINAYGPTETtvTNHKRFFPGDQRFDKSLGRPVRNTKCYVLN-DAMK 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 524 YWACKGEGEICVRGPNVFKGYLKDPDRTKE-------------ALDSDGWLH-TGDIGKWLPAGTLKIIDRKKHIFKLaQ 589
Cdd:cd17648 281 RVPVGAVGELYLGGDGVARGYLNRPELTAErflpnpfqteqerARGRNARLYkTGDLVRWLPSGELEYLGRNDFQVKI-R 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 57165412 590 GEYVAPEKIENIY-----IRSQPVAQIYVHGDSLKA---FLVGIVVPDPEVMP 634
Cdd:cd17648 360 GQRIEPGEVEAALasypgVRECAVVAKEDASQAQSRiqkYLVGYYLPEPGHVP 412
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
175-632 |
5.20e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 59.27 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 175 IGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAvlLLEHVErkeTPGLKLIILMDP 254
Cdd:PRK13388 55 VGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLLVTDAEHRP--LLDGLD---LPGVRVLDVDTP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 255 -FEEALKERGqkcgvviksmqavedcgqENHQAPvPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLkVTEKVI 333
Cdd:PRK13388 130 aYAELVAAAG------------------ALTPHR-EVDAMDPFMLIFTSGTTGAPKAVRCSHGRLA--FAGRA-LTERFG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 334 FPRqDDVLISFLPLAH----MferVIQSVVYCHGGRVGF--------FQGDIRLLSddmkalcPTIFPVVPRLLNrmYdk 401
Cdd:PRK13388 188 LTR-DDVCYVSMPLFHsnavM---AGWAPAVASGAAVALpakfsasgFLDDVRRYG-------ATYFNYVGKPLA--Y-- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 402 IFSQ------ANTPLKRWLLEFAAKRKQAEvrsgiirndsiwdelffnkiqaslggcvrmivtgaapasptvlgFLRAaL 475
Cdd:PRK13388 253 ILATperpddADNPLRVAFGNEASPRDIAE--------------------------------------------FSRR-F 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 476 GCQVYEGYGQTEctAGCTFTTPGDWTSGHVGAPLPcnHIKLVDVEE---------------LNywACKGEGEICVR-GPN 539
Cdd:PRK13388 288 GCQVEDGYGSSE--GAVIVVREPGTPPGSIGRGAP--GVAIYNPETltecavarfdahgalLN--ADEAIGELVNTaGAG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 540 VFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYVHGdslk 619
Cdd:PRK13388 362 FFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYA---- 435
|
490
....*....|...
gi 57165412 620 aflvgivVPDPEV 632
Cdd:PRK13388 436 -------VPDERV 441
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
454-630 |
7.12e-09 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 58.85 E-value: 7.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 454 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT---------FTT------PGD--WTSGHVGAPLPCNHIkl 516
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAEGLVNYTrlddsderiFTTqgrpmsPDDevWVADADGNPLPQGEV-- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 517 vdveelnywackgeGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHifklaQ----GEY 592
Cdd:PRK10946 381 --------------GRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGEK 441
|
170 180 190
....*....|....*....|....*....|....*...
gi 57165412 593 VAPEKIENIYIRsqpvaqiyvHGDSLKAFLVGIvvPDP 630
Cdd:PRK10946 442 IAAEEIENLLLR---------HPAVIHAALVSM--EDE 468
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
146-632 |
2.55e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 56.94 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAEFLGSGLlqHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIv 225
Cdd:PRK13390 25 VSYRQLDDDSAALARVL--YDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLV- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 226 dkpqkAVLLLEHVERKETPGLKLIILMD-------PFEEALKERGQKCgvviksmqAVEDCGqenhqapvppqpddlSIV 298
Cdd:PRK13390 102 -----ASAALDGLAAKVGADLPLRLSFGgeidgfgSFEAALAGAGPRL--------TEQPCG---------------AVM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 299 CFTSGTTGNPKG--------AMLTHGN-VVADFSGFLKVTEKvifprqdDVLISFLPLAHMFERVIQSVVYCHGGRVGFF 369
Cdd:PRK13390 154 LYSSGTTGFPKGiqpdlpgrDVDAPGDpIVAIARAFYDISES-------DIYYSSAPIYHAAPLRWCSMVHALGGTVVLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 370 QG-DIRLLSDDMKALCPTIFPVVPRLLNRMYdkifsqantplkrwllefaakRKQAEVRSgiiRNDSiwdelffnkiqAS 448
Cdd:PRK13390 227 KRfDAQATLGHVERYRITVTQMVPTMFVRLL---------------------KLDADVRT---RYDV-----------SS 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 449 LggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVG-APLPCNHIKLVDVEELNyw 525
Cdd:PRK13390 272 L----RAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGrSVLGDLHICDDDGNELP-- 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 526 ackgEGEIcvrGPNVFK------GYLKDPDRTKEALDSDG--WLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEK 597
Cdd:PRK13390 345 ----AGRI---GTVYFErdrlpfRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQE 416
|
490 500 510
....*....|....*....|....*....|....*
gi 57165412 598 IENIYIRSQPVAQIYVHGdslkaflvgivVPDPEV 632
Cdd:PRK13390 417 TENALTMHPAVHDVAVIG-----------VPDPEM 440
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
453-646 |
6.63e-08 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 55.78 E-value: 6.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 453 VRMIVTGAAPASPTVLGFLRAA--LGCQVYeGYGQTECTAGCTFTTPGDWT---SGHVGAPLPCNHIKLVDVEELNYWAC 527
Cdd:PRK05857 288 LRLVGYGGSRAIAADVRFIEATgvRTAQVY-GLSETGCTALCLPTDDGSIVkieAGAVGRPYPGVDVYLAATDGIGPTAP 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 528 KGE-----GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIY 602
Cdd:PRK05857 367 GAGpsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGGVNIAPDEVDRIA 444
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 57165412 603 IRSQPV--AQIYVHGDSLKAFLVGI-VVPDPEVMPSWAQ--KRGIEGTY 646
Cdd:PRK05857 445 EGVSGVreAACYEIPDEEFGALVGLaVVASAELDESAARalKHTIAARF 493
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
447-631 |
1.93e-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: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 447 ASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEC-TAGCTFTTPGDWT-SGHVGAPLPCNHIKLVDvEELNY 524
Cdd:cd05973 201 ARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELgMVLANHHALEHPVhAGSAGRAMPGWRVAVLD-DDGDE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 525 WACKGEGEICV---RGPNV-FKGYLKDPDRTKealdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIEN 600
Cdd:cd05973 280 LGPGEPGRLAIdiaNSPLMwFRGYQLPDTPAI----DGGYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFDVES 354
|
170 180 190
....*....|....*....|....*....|.
gi 57165412 601 IYIRSQPVAQIYVhgdslkaflvgIVVPDPE 631
Cdd:cd05973 355 ALIEHPAVAEAAV-----------IGVPDPE 374
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
441-623 |
2.17e-07 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 54.27 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 441 FFNKIqasLGGC-------VRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTEctAGCTFT--TPGDWTSGHVGAPLP 510
Cdd:PRK06060 246 FFARV---IDSCspdsfrsLRCVVSAGEALELGLAERLMEFFGgIPILDGIGSTE--VGQTFVsnRVDEWRLGTLGRVLP 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 511 CNHIKLVDVEELNYwACKGEGEICVRGPNVFKGYLKDPDrtkEALDSDGWLHTGDIGK-----WLPAGTlkiidrKKHIF 585
Cdd:PRK06060 321 PYEIRVVAPDGTTA-GPGVEGDLWVRGPAIAKGYWNRPD---SPVANEGWLDTRDRVCidsdgWVTYRC------RADDT 390
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 57165412 586 KLAQGEYVAPEKIENIYIRSQPVAQIYVHG-------DSLKAFLV 623
Cdd:PRK06060 391 EVIGGVNVDPREVERLIIEDEAVAEAAVVAvrestgaSTLQAFLV 435
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
251-350 |
2.50e-07 |
|
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: 53.83 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 251 LMDPFEE---ALKERGQKCGVVIKSM--QAVEDCGQENHQAPVPPQPDDLS---------IVCFTSGTTGNPKGAMLTHG 316
Cdd:cd05938 88 LQEAVEEvlpALRADGVSVWYLSHTSntEGVISLLDKVDAASDEPVPASLRahvtikspaLYIYTSGTTGLPKAARISHL 167
|
90 100 110
....*....|....*....|....*....|....
gi 57165412 317 NVVAdFSGFLKVTeKVifpRQDDVLISFLPLAHM 350
Cdd:cd05938 168 RVLQ-CSGFLSLC-GV---TADDVIYITLPLYHS 196
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
283-640 |
3.78e-07 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 52.74 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 283 NHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkVTEKVIFPRQddVLISfLPLAHM--FERVIQSVV- 359
Cdd:PRK07824 25 DALRVGEPIDDDVALVVATSGTTGTPKGAMLTAAALTASADA---THDRLGGPGQ--WLLA-LPAHHIagLQVLVRSVIa 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 360 --------YCHGGRVGFFQGDIRLLSDDMK--ALCPTifpvvpRLLNRMYDKIFSQAntplkrwLLEFAAkrkqaevrsg 429
Cdd:PRK07824 99 gsepveldVSAGFDPTALPRAVAELGGGRRytSLVPM------QLAKALDDPAATAA-------LAELDA---------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 430 iirndsiwdelffnkiqaslggcvrmIVTGAAPASPTVlgfLRAA--LGCQVYEGYGQTECTAGCTFTtpgdwtsghvGA 507
Cdd:PRK07824 156 --------------------------VLVGGGPAPAPV---LDAAaaAGINVVRTYGMSETSGGCVYD----------GV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 508 PLPCNHIKLVDveelnywackgeGEICVRGPNVFKGY--LKDPDrtkeALDSDGWLHTGDIGKwLPAGTLKIIDRKKHIF 585
Cdd:PRK07824 197 PLDGVRVRVED------------GRIALGGPTLAKGYrnPVDPD----PFAEPGWFRTDDLGA-LDDGVLTVLGRADDAI 259
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 57165412 586 KLAqGEYVAPEKIENIYIRSQPVAQIYVHG---DSLKAFLVGIVVPDPEVMPSWAQKR 640
Cdd:PRK07824 260 STG-GLTVLPQVVEAALATHPAVADCAVFGlpdDRLGQRVVAAVVGDGGPAPTLEALR 316
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
146-349 |
5.82e-07 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 52.95 E-value: 5.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 146 LSYQEVADRAE-----FLGSGLLQHNCkactdqfIGVFAQNRPEWIIVELACyTYSMVVVPLYDT-LGPGAIRYIINTAD 219
Cdd:PRK08279 63 ISYAELNARANryahwAAARGVGKGDV-------VALLMENRPEYLAAWLGL-AKLGAVVALLNTqQRGAVLAHSLNLVD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 220 ISTVIVDKPqkavlLLEHVE--RKETPGLKLIILMDPFEEALKERgqkcgvVIKSMQAVEDCGQENHQAPVPPQPDDLSI 297
Cdd:PRK08279 135 AKHLIVGEE-----LVEAFEeaRADLARPPRLWVAGGDTLDDPEG------YEDLAAAAAGAPTTNPASRSGVTAKDTAF 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 57165412 298 VCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAH 349
Cdd:PRK08279 204 YIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLR----LTPDDVLYCCLPLYH 251
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
286-582 |
6.47e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 52.64 E-value: 6.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 286 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADF----SGFLKVTEKVifPRQDDVLISFLPLAHMFERVIQSVVYC 361
Cdd:PRK05850 153 DARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFeqlmSDYFGDTGGV--PPPDTTVVSWLPFYHDMGLVLGVCAPI 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 362 HGGR-------VGFFQGDIRLLsddmkalcptifpvvpRLLNRmYDKIFSQAntPlkRWLLEFAAKRKQAEVRSGIirnd 434
Cdd:PRK05850 231 LGGCpavltspVAFLQRPARWM----------------QLLAS-NPHAFSAA--P--NFAFELAVRKTSDDDMAGL---- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 435 siwdelffnkiqaSLGGcVRMIVTGAAPASP-TVLGFLR--AALGCQ---VYEGYGQTECTAGCTFTTPGD--------- 499
Cdd:PRK05850 286 -------------DLGG-VLGIISGSERVHPaTLKRFADrfAPFNLRetaIRPSYGLAEATVYVATREPGQppesvrfdy 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 500 --WTSGHV-------GAPLPCNH------IKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALD------SD 558
Cdd:PRK05850 352 ekLSAGHAkrcetggGTPLVSYGsprsptVRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGatlvdpSP 431
|
330 340
....*....|....*....|....*....
gi 57165412 559 G-----WLHTGDIGkWLPAGTLKIIDRKK 582
Cdd:PRK05850 432 GtpegpWLRTGDLG-FISEGELFIVGRIK 459
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
111-640 |
8.66e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 52.65 E-value: 8.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 111 YDDARTMYQVFRRGLSISGNGPCLGFRKpkqpyQWLSYQEVADRAEFLGSGLLQhnCKACTDQFIGVFAQNRPEWIIVEL 190
Cdd:PRK12316 507 YPLQRGVHRLFEEQVERTPEAPALAFGE-----ETLDYAELNRRANRLAHALIE--RGVGPDVLVGVAMERSIEMVVALL 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 191 ACYTYSMVVVPLYDTLGPGAIRYIINTADIstvivdkpqkAVLLLEHVERKETP---GLKLIILMDP--FEEALKERGQK 265
Cdd:PRK12316 580 AILKAGGAYVPLDPEYPAERLAYMLEDSGV----------QLLLSQSHLGRKLPlaaGVQVLDLDRPaaWLEGYSEENPG 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 266 CGVViksmqavedcgqenhqapvppqPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifprqddvlisfL 345
Cdd:PRK12316 650 TELN----------------------PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYG--------------L 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 346 PLAhmfERVIQSVVYCHGGRVGFFQGDI----RLLsddmkalcptifpVVPRLLNRMYDKIFSQANTPLKRwLLEFAAKR 421
Cdd:PRK12316 694 GVG---DTVLQKTPFSFDVSVWEFFWPLmsgaRLV-------------VAAPGDHRDPAKLVELINREGVD-TLHFVPSM 756
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 422 KQAEVRSGIIrndsiwdelffnkiqASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT 501
Cdd:PRK12316 757 LQAFLQDEDV---------------ASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEG 821
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 502 SGHV--GAPLPCNHIKLVDVeELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL------DSDGWLHTGDIGKWLPAG 573
Cdd:PRK12316 822 GDSVpiGRPIANLACYILDA-NLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFvpspfvAGERMYRTGDLARYRADG 900
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57165412 574 TLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAfLVGIVVPD------PEVMPSWAQKR 640
Cdd:PRK12316 901 VIEYAGRIDHQVKL-RGLRIELGEIEARLLEHPWVREAAVLAVDGKQ-LVGYVVLEseggdwREALKAHLAAS 971
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
300-600 |
1.19e-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: 51.25 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 300 FTSGTTGNPKGAMLTHGNVVADFsgflKVTEKVIFPRQDDVLISFLPLAH-MFERVIQSVVYCHGGRVGFFQGDIRLLSD 378
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESF----VCNEDLFNISGEDAILAPGPLSHsLFLYGAISALYLGGTFIGQRKFNPKSWIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 379 DMKALCPTIFPVVPRLLNRMYdkifsQANTPlkrwllefaakrkQAEVRSgIIRNDSIWDELFFNKIQAslggcvrmivt 458
Cdd:cd17633 83 KINQYNATVIYLVPTMLQALA-----RTLEP-------------ESKIKS-IFSSGQKLFESTKKKLKN----------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 459 gaapasptvlGFLRAALgcqvYEGYGQTEcTAGCTFTTPGD-WTSGHVGAPLPCNHIKLVDVEElnywacKGEGEICVRG 537
Cdd:cd17633 133 ----------IFPKANL----IEFYGTSE-LSFITYNFNQEsRPPNSVGRPFPNVEIEIRNADG------GEIGKIFVKS 191
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57165412 538 PNVFKGYLKDPDRTKealdsDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIEN 600
Cdd:cd17633 192 EMVFSGYVRGGFSNP-----DGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIES 248
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
294-631 |
1.58e-06 |
|
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: 51.20 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 294 DLSIVCFTSGTTGNPKGAMLTH-----GNVVADFSGFLKvtekvifprQDDVLISFLPLAHMfERVIQSVVYC--HGGRV 366
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHrrawrGGAFFAGSGGAL---------PSDVLYTCLPLYHS-TALIVGWSAClaSGATL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 367 GF--------FQGDIRllsddmKALCpTIFPVVPRLLnrmydkifsqantplkRWLLefAAKRKQAEVRsgiirndsiwd 438
Cdd:cd05940 152 VIrkkfsasnFWDDIR------KYQA-TIFQYIGELC----------------RYLL--NQPPKPTERK----------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 439 elffNKIQASLGGCVRmivtgaapasPTVLGFLRAALGC-QVYEGYGQTECTAGCT--FTTPGdwTSGHVGAPLPCNH-I 514
Cdd:cd05940 196 ----HKVRMIFGNGLR----------PDIWEEFKERFGVpRIAEFYAATEGNSGFInfFGKPG--AIGRNPSLLRKVApL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 515 KLV--DVEELNYW---------ACKGE-----GEICVRGPnvFKGYLKDPDRTKEAL-----DSDGWLHTGDIGKWLPAG 573
Cdd:cd05940 260 ALVkyDLESGEPIrdaegrcikVPRGEpglliSRINPLEP--FDGYTDPAATEKKILrdvfkKGDAWFNTGDLMRLDGEG 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57165412 574 TLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYVHGDSL-----KAFLVGIVVPDPE 631
Cdd:cd05940 338 FWYFVDRLGDTFRW-KGENVSTTEVAAVLGAFPGVEEANVYGVQVpgtdgRAGMAAIVLQPNE 399
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
508-568 |
2.53e-06 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 50.66 E-value: 2.53e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57165412 508 PLPCNHIK-----LVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL-DSDGW--LHTGDIGK 568
Cdd:PRK04813 317 RLPIGYAKpdsplLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGY 385
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
290-639 |
1.18e-05 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 48.15 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 290 PQPDDLSIVCfTSGTTGNPKGAMLTHGNV------VADFSGFLKVTEKVIFPRQ----DDVLISFLPLAH-------MFE 352
Cdd:cd05924 1 RSADDLYILY-TGGTTGMPKGVMWRQEDIfrmlmgGADFGTGEFTPSEDAHKAAaaaaGTVMFPAPPLMHgtgswtaFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 353 RVIQSVVYCHGGRvgfFQGD--IRLLSddmKALCPTIFPVVPRLLNRMYDKIFSQANTPLkrwllefaakrkqaevrsgi 430
Cdd:cd05924 80 LLGGQTVVLPDDR---FDPEevWRTIE---KHKVTSMTIVGDAMARPLIDALRDAGPYDL-------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 431 irndsiwdelffnkiqASLggcvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFTTPGdwtSGHVGAPL 509
Cdd:cd05924 134 ----------------SSL----FAISSGGALLSPEVKqGLLELVPNITLVDAFGSSETGFTGSGHSAG---SGPETGPF 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 510 -PCNHIKLVDVEELNYWACK--GEGEICVRGpNVFKGYLKDPDRTKEA---LDSDGWLHTGDIGKWLPAGTLKIIDRKKH 583
Cdd:cd05924 191 tRANPDTVVLDDDGRVVPPGsgGVGWIARRG-HIPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGRGSV 269
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 57165412 584 IFKLAqGEYVAPEKIENIyIRSQP-VAQIYVHGdslkaflvgivVPDPEvmpsWAQK 639
Cdd:cd05924 270 CINTG-GEKVFPEEVEEA-LKSHPaVYDVLVVG-----------RPDER----WGQE 309
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
292-623 |
7.60e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 46.31 E-value: 7.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 292 PDDLSIVCFTSGTTGNPKGAMLT-HGNVVADFSG--FLKVTEKVIFPRQ-----DDVLISFLPlAHMFerviqsvvychG 363
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEqRGMLNNQLSKvpYLALSEADVIAQTasqsfDISVWQFLA-APLF-----------G 3935
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 364 GRVGFFQGDIrllSDDMKALCP-------TIFPVVPRLLNRMydkifsqantplkrwllefaakrkqaevrsgiIRNDsi 436
Cdd:PRK05691 3936 ARVEIVPNAI---AHDPQGLLAhvqaqgiTVLESVPSLIQGM--------------------------------LAED-- 3978
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 437 wdelffnkiQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF------TTPGDWTSghVGAPLP 510
Cdd:PRK05691 3979 ---------RQALDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFfrvdlaSTRGSYLP--IGSPTD 4047
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 511 CNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL-------DSDGWLHTGDIGKWLPAGTLKIIDRKKH 583
Cdd:PRK05691 4048 NNRLYLLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFvphpfgaPGERLYRTGDLARRRSDGVLEYVGRIDH 4126
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 57165412 584 I-----FKLAQGEYVApEKIENIYIRSQPVA-QIYVHGDSLKAFLV 623
Cdd:PRK05691 4127 QvkirgYRIELGEIEA-RLHEQAEVREAAVAvQEGVNGKHLVGYLV 4171
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
450-632 |
9.01e-05 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 45.90 E-value: 9.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 450 GGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFT-TPGDWTSG--HVGAPLPCNHIKLVDVE--ELNy 524
Cdd:PRK13382 311 GRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATE--AGMIATaTPADLRAApdTAGRPAEGTEIRILDQDfrEVP- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 525 wacKGE-GEICVRGPNVFKGYlkDPDRTKEAldSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIyI 603
Cdd:PRK13382 388 ---TGEvGTIFVRNDTQFDGY--TSGSTKDF--HDGFMASGDVGYLDENGRLFVVGRDDEMI-VSGGENVYPIEVEKT-L 458
|
170 180 190
....*....|....*....|....*....|....*..
gi 57165412 604 RSQP-VAQIYV-------HGDSLKAFlvgiVVPDPEV 632
Cdd:PRK13382 459 ATHPdVAEAAVigvddeqYGQRLAAF----VVLKPGA 491
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
442-720 |
1.11e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 45.54 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 442 FNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPGDWTSGHVGAPLPCNHIKLVDVEE 521
Cdd:PRK07638 245 LYKENRVIENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSF-VTALVDEESERRPNSVGRPFHNVQVRICNE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 522 LNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEaLDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIEN 600
Cdd:PRK07638 324 AGEEVQKGEiGTVYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIES 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 601 IYIRSQPVAQIYVHGdslkaflvgivVPDpevmPSWAQKRG--IEGTyadlCTNKDLKKAILEDmvrlgkesgLHSFEQV 678
Cdd:PRK07638 402 VLHEHPAVDEIVVIG-----------VPD----SYWGEKPVaiIKGS----ATKQQLKSFCLQR---------LSSFKIP 453
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 57165412 679 KAIHIhsdmfsVQNGLLTPTLKAKRPELreyfKKQIEELYSI 720
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 ... |
443-607 |
1.15e-04 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 45.50 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 443 NKIQASLGGCVRMIVTGAAPASPTV----LGFLRA--ALGCQVYEGYGqTECTAGCTFTTPGDWTSGHVGAPLPCNHI-K 515
Cdd:cd05915 263 ESTGHRLKTLRRLVVGGSAAPRSLIarfeRMGVEVrqGYGLTETSPVV-VQNFVKSHLESLSEEEKLTLKAKTGLPIPlV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 516 LVDVEELNYWACKGEGE----ICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGE 591
Cdd:cd05915 342 RLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG-GE 420
|
170
....*....|....*.
gi 57165412 592 YVAPEKIENIyIRSQP 607
Cdd:cd05915 421 WISSVDLENA-LMGHP 435
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
452-623 |
2.82e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 44.22 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 452 CVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGcTFTTPG---DWTSGhVGAPLPCNHIKLVDVEELNYwACK 528
Cdd:PRK13383 293 QLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIG-ALATPAdlrDAPET-VGKPVAGCPVRILDRNNRPV-GPR 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 529 GEGEICVRGPNVFKGYlkdPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPV 608
Cdd:PRK13383 370 VTGRIFVGGELAGTRY---TDGGGKAV-VDGMTSTGDMGYLDNAGRLFIVGREDDMI-ISGGENVYPRAVENALAAHPAV 444
|
170 180
....*....|....*....|..
gi 57165412 609 AQIYV-------HGDSLKAFLV 623
Cdd:PRK13383 445 ADNAVigvpderFGHRLAAFVV 466
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
292-615 |
3.72e-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: 43.57 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 292 PDDLSIVCFTSGTTGNPKGAMLTHG-NVVADfsgflKVTEKVIFPRQDDVLISFLPLAHMFERVIqSVVYC--HGGRVGF 368
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISWRrTLVTS-----NLLSHDLNLKNGDRTYTCMPLYHGTAAFL-GACNClmSGGTLAL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 369 --------FQGDIRllsdDMKAlcpTIFPVVPRLLnrmydkifsqantplkRWLLEFAAkrkqaevrsgiirndSIWDEL 440
Cdd:cd05937 160 srkfsasqFWKDVR----DSGA---TIIQYVGELC----------------RYLLSTPP---------------SPYDRD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 441 ffNKIQASLGGCVRmivtgaapasPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKL--- 516
Cdd:cd05937 202 --HKVRVAWGNGLR----------PDIWERFRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKFenq 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 517 -----VDVEELNYW----------ACKGE-GEICVRGPNV----FKGYLKDPDRTKEAL------DSDGWLHTGDIGKWL 570
Cdd:cd05937 270 vvlvkMDPETDDPIrdpktgfcvrAPVGEpGEMLGRVPFKnreaFQGYLHNEDATESKLvrdvfrKGDIYFRTGDLLRQD 349
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 57165412 571 PAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYVHG 615
Cdd:cd05937 350 ADGRWYFLDRLGDTFRW-KSENVSTTEVADVLGAHPDIAEANVYG 393
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
293-624 |
3.96e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.00 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 293 DDLSIVCFTSGTTGNPKGAMLTHGnVVADFSGFLKVTEKVifpRQDDVLISFLPLAhmFErviQSVVYCH-----GGRVG 367
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNTHA-ALAERLQWMQATYAL---DDSDVLMQKAPIS--FD---VSVWECFwplitGCRLV 1343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 368 FF----QGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTPLKRWlleFAAkrkqAEVRSGIIRNdsiwdelffn 443
Cdd:PRK05691 1344 LAgpgeHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRL---FSG----GEALPAELRN---------- 1406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 444 kiqaslggcvrmivtgaapaspTVLGFLRAAlgcQVYEGYGQTECTAGCTF--TTPGDWTSGHVGAPLPCNHIKLVDvEE 521
Cdd:PRK05691 1407 ----------------------RVLQRLPQV---QLHNRYGPTETAINVTHwqCQAEDGERSPIGRPLGNVLCRVLD-AE 1460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 522 LNYWACKGEGEICVRGPNVFKGYLKDPDRTKE-----ALDSDG--WLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVA 594
Cdd:PRK05691 1461 LNLLPPGVAGELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL-RGFRVE 1539
|
330 340 350
....*....|....*....|....*....|..
gi 57165412 595 PEKIENIYIRSQPVAQ--IYVHGDSLKAFLVG 624
Cdd:PRK05691 1540 PEEIQARLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
288-319 |
5.94e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 43.49 E-value: 5.94e-04
10 20 30
....*....|....*....|....*....|..
gi 57165412 288 VPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVV 319
Cdd:PRK10252 593 QLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIV 624
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
542-630 |
2.41e-03 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 41.57 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57165412 542 KGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIyIRSQP-VAQIYVH 614
Cdd:PRK10252 814 QGYLGRPDLTASRFIADPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKI-RGQRIELGEIDRA-MQALPdVEQAVTH 891
|
90 100
....*....|....*....|....*..
gi 57165412 615 -----------GDSLKafLVGIVVPDP 630
Cdd:PRK10252 892 acvinqaaatgGDARQ--LVGYLVSQS 916
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
291-319 |
9.61e-03 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 39.11 E-value: 9.61e-03
10 20
....*....|....*....|....*....
gi 57165412 291 QPDDLSIVCFTSGTTGNPKGAMLTHGNVV 319
Cdd:PRK04813 141 KGDDNYYIIFTSGTTGKPKGVQISHDNLV 169
|
|
| |
