|
Name |
Accession |
Description |
Interval |
E-value |
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
116-694 |
0e+00 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 925.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 116 QPYQWLSYQEVADRAEFLGSGLLQHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADI 195
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 196 STVIVDKpqkavlllehverketpglkliilmdpfeealkergqkcGVVIKSMQAVEDCGQENHHAPVPPQPDDLSIVCF 275
Cdd:cd05927 81 SIVFCDA---------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 276 TSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDM 355
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 356 KALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWLLEFAAKRKQAEVRSGIIRNDSIWDELFFNKIQASLGGCVRMIVT 433
Cdd:cd05927 202 KALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 434 GAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWA--CKGEGEICVR 511
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAkdPNPRGEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 512 GPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGD 591
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 592 SLKAFLVGIVVPDPEVMPSWA-QKRGIEGTYADLCTSKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLL 670
Cdd:cd05927 442 SLKSFLVAIVVPDPDVLKEWAaSKGGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLL 521
|
570 580
....*....|....*....|....
gi 966948474 671 TPTLKAKRPELREYFKKQIEELYS 694
Cdd:cd05927 522 TPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
72-694 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 696.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 72 RSViGSGPQLLTHY--YDDARTMYQVFRRGLSISGNGPCLGFRKPNQ----PYQWLSYQEVADRAEFLGSGLLQHNCK-- 143
Cdd:PLN02736 25 RSA-RSPLKLVSRFpdHPEIGTLHDNFVYAVETFRDYKYLGTRIRVDgtvgEYKWMTYGEAGTARTAIGSGLVQHGIPkg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 144 ACtdqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVdKPQKAVLLLEHVerKETPGLKL 223
Cdd:PLN02736 104 AC----VGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCL--SEIPSVRL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 224 IILMDPFEEALKERGQKCGVVIKSMQAVEDCGQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKV 303
Cdd:PLN02736 177 IVVVGGADEPLPSLPSGTGVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 304 TEkvIFPrqDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QA 381
Cdd:PLN02736 257 TK--FYP--SDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNavKE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 382 NTPLKRWLLEFAAKRKQAEVRSGiiRNDS-IWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQ 460
Cdd:PLN02736 333 SGGLKERLFNAAYNAKKQALENG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGM 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 461 TECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKG---EGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH 537
Cdd:PLN02736 411 TETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLH 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 538 TGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGI 617
Cdd:PLN02736 491 TGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGI 570
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966948474 618 E-GTYADLCTSKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 694
Cdd:PLN02736 571 KyEDLKQLCNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYA 648
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
86-694 |
1.19e-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: 1.19e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 86 YDDARTMYQVFRRGLSISGNGPCLGfRKPNQPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAEL 165
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVALR-EKEDGIWQSLTWAEFAERVRALAAGLLALGVKP--GDRVAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 166 ACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAVLLLEHveRKETPGLKLIILMDPfeealkeRGQKCGVVI 245
Cdd:COG1022 84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEV--RDELPSLRHIVVLDP-------RGLRDDPRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 246 KSMQAVEDCGQENHH------APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekvIFPRQDDVLISF 319
Cdd:COG1022 155 LSLDELLALGREVADpaeleaRRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLER----LPLGPGDRTLSF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 320 LPLAHMFERVIQSVVYCHGGRVGFfQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQAN--TPLKRWLLEFA---A 394
Cdd:COG1022 231 LPLAHVFERTVSYYALAAGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEeaGGLKRKLFRWAlavG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 395 KRKQAEVRSGiiRNDSIW--------DELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAG 466
Cdd:COG1022 310 RRYARARLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 467 CTFTTPGDWTSGHVGAPLPCNHIKLVDveelnywackgEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLP 546
Cdd:COG1022 387 ITVNRPGDNRIGTVGPPLPGVEVKIAE-----------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 547 AGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKaFLVGIVVPDPEVMPSWAQKRGIE-GTYADLC 625
Cdd:COG1022 456 DGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDGRP-FLAALIVPDFEALGEWAEENGLPyTSYAELA 534
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966948474 626 TSKDLKKAILEDMVRLGKesGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 694
Cdd:COG1022 535 QDPEVRALIQEEVDRANA--GLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYA 601
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
116-681 |
1.49e-160 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 470.15 E-value: 1.49e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 116 QPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADI 195
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEP--GDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 196 STVIVDKPqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhhapvppqpDDLSIVCF 275
Cdd:cd05907 79 KALFVEDP----------------------------------------------------------------DDLATIIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 276 TSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAHMFERV-IQSVVYCHGGRVGFFQgDIRLLSDD 354
Cdd:cd05907 95 TSGTTGRPKGVMLSHRNILSNALALAERLP----ATEGDRHLSFLPLAHVFERRaGLYVPLLAGARIYFAS-SAETLLDD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 355 MKALCPTIFPVVPRLLNRMYDKIFSQANTPLKRWLLEFAAkrkqaevrsgiirndsiwdelffnkiqaslGGCVRMIVTG 434
Cdd:cd05907 170 LSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV------------------------------GGRLRFAASG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 435 AAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDveelnywackgEGEICVRGPN 514
Cdd:cd05907 220 GAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPN 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 515 VFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLK 594
Cdd:cd05907 288 VMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDGRP 367
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 595 aFLVGIVVPDPEVMPSWAQKRGIEG-TYADLCTSKDLKKAILEDMVRLGKEsgLHSFEQVKAIHIHSDMFSVQNGLLTPT 673
Cdd:cd05907 368 -FLVALIVPDPEALEAWAEEHGIAYtDVAELAANPAVRAEIEAAVEAANAR--LSRYEQIKKFLLLPEPFTIENGELTPT 444
|
....*...
gi 966948474 674 LKAKRPEL 681
Cdd:cd05907 445 LKLKRPVI 452
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
117-678 |
4.65e-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: 458.22 E-value: 4.65e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 117 PYQWLSYQEVADRAEFLGSGL----LQHNCKactdqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINT 192
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLvelgLKPGDK------VAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 193 ADISTVIVDkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhhapvpPQPDDLSI 272
Cdd:cd17639 76 TECSAIFTD---------------------------------------------------------------GKPDDLAC 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 273 VCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPrqDDVLISFLPLAHMFERVIQSVVYCHGGRVGFfqGDIRLLS 352
Cdd:cd17639 93 IMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGP--DDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLT 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 353 DDMKALC--------PTIFPVVPRLLNRMYDKIFSQANTP--LKRWLLEFAAKRKQAEVRSGIirnDS-IWDELFFNKIQ 421
Cdd:cd17639 169 DKSKRGCkgdltefkPTLMVGVPAIWDTIRKGVLAKLNPMggLKRTLFWTAYQSKLKALKEGP---GTpLLDELVFKKVR 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 422 ASLGGCVRMIVTGAAPASPTVLGFLrAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWA 501
Cdd:cd17639 246 AALGGRLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYST 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 502 CKGE--GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIR 579
Cdd:cd17639 325 DKPPprGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRS 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 580 SQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRG-IEGTYADLCTSKDLKKAILEDMVRLGKESGLHSFEQVKAIHI 658
Cdd:cd17639 405 NPLVNNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGvINSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVL 484
|
570 580
....*....|....*....|
gi 966948474 659 HSDMFSVQNGLLTPTLKAKR 678
Cdd:cd17639 485 LDEEWTPENGLVTAAQKLKR 504
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
117-694 |
3.33e-151 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 453.91 E-value: 3.33e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 117 PYQWLSYQEVADRAEFLGSGLLQ------HNCkactdqfiGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYII 190
Cdd:PLN02861 74 PYVWLTYKEVYDAAIRIGSAIRSrgvnpgDRC--------GIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFII 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 191 NTADISTVIVDKPQKAVLLleHVERKETPGLKLIILMDPFEEALKERGQKCGVVIKSMQAVEDCGQENHHAPvPPQPDDL 270
Cdd:PLN02861 146 NHAEVSIAFVQESKISSIL--SCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLDCELP-PKQKTDI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 271 SIVCFTSGTTGNPKGAMLTHGNVVADF---SGFLKVTEKVIfpRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGD 347
Cdd:PLN02861 223 CTIMYTSGTTGEPKGVILTNRAIIAEVlstDHLLKVTDRVA--TEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQGD 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 348 IRLLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWLLEFAAKRKQAEVRSGIIRNDS--IWDELFFNKIQAS 423
Cdd:PLN02861 301 IRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQkiSSGGMLRKKLFDFAYNYKLGNLRKGLKQEEAspRLDRLVFDKIKEG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 424 LGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCtFTTPGDWTS--GHVGAPLPCNHIKLVDVEELNYWA 501
Cdd:PLN02861 381 LGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGC-FTSIANVFSmvGTVGVPMTTIEARLESVPEMGYDA 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 502 CKG--EGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIR 579
Cdd:PLN02861 460 LSDvpRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSR 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 580 SQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGIEGTYADLCTSKDLKKAILEDMVRLGKESGLHSFEQVKAIHIH 659
Cdd:PLN02861 539 CPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLE 618
|
570 580 590
....*....|....*....|....*....|....*
gi 966948474 660 SDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 694
Cdd:PLN02861 619 PNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYS 653
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
88-693 |
3.70e-151 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 453.89 E-value: 3.70e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 88 DARTMYQVFRRGLSISGNGPCLGFRKPNQ----PYQWLSYQEVADRAEFLGSGLLQHNCKACTDqfIGVFAQNRPEWIIA 163
Cdd:PLN02430 40 DITTAWDIFSKSVEKYPDNKMLGWRRIVDgkvgPYMWKTYKEVYEEVLQIGSALRASGAEPGSR--VGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 164 ELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV-DKPQKAVLlleHVERKETPGLKLIILMDPFEEALKERGQKCG 242
Cdd:PLN02430 118 MEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVqDKKIKELL---EPDCKSAKRLKAIVSFTSVTEEESDKASQIG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 243 VVIKSMQAVEDCGQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTEKVIfpRQDDVLISF 319
Cdd:PLN02430 195 VKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGvdlFMEQFEDKM--THDDVYLSF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 320 LPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWLLEFAAKRK 397
Cdd:PLN02430 273 LPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYKYK 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 398 QAEVRSGIIRNDS--IWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDW 475
Cdd:PLN02430 353 LAWMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEM 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 476 TS-GHVGAPLPCNHIKLVDVEELNY--WACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKV 552
Cdd:PLN02430 433 CMlGTVGAPAVYNELRLEEVPEMGYdpLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKI 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 553 IDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGIEGTYADLCTSKDLKK 632
Cdd:PLN02430 512 IDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKE 591
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966948474 633 AILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 693
Cdd:PLN02430 592 HILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMY 652
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
58-693 |
1.39e-150 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 452.55 E-value: 1.39e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 58 LMQSEEVEDSGGARRSVigsGPQLLTHYYDDA--------RTMYQVFRRGLSISGNGPCLGFR-----KPNQpYQWLSYQ 124
Cdd:PLN02614 8 IFQVEEGKEGSDGRPSV---GPVYRSIFAKDGfpnpiegmDSCWDVFRMSVEKYPNNPMLGRReivdgKPGK-YVWQTYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 125 EVADRAEFLGSGLlqHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDkpQ 204
Cdd:PLN02614 84 EVYDIVIKLGNSL--RSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVE--E 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 205 KAVLLLEHVERKETPGLKLIILMDPFEEALKERGQKCGVVIKSMQAVEDCGQENHHAPVPPQPDDLSIVCFTSGTTGNPK 284
Cdd:PLN02614 160 KKISELFKTCPNSTEYMKTVVSFGGVSREQKEEAETFGLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 285 GAMLTHGNVVADFSG---FLKVTEKVIfpRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALCPT 361
Cdd:PLN02614 240 GVMISNESIVTLIAGvirLLKSANAAL--TVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 362 IFPVVPRLLNRMYDKIFSQANTP--LKRWLLEFAAKRKQAEVRSGI--IRNDSIWDELFFNKIQASLGGCVRMIVTGAAP 437
Cdd:PLN02614 318 IFCAVPRVLDRVYSGLQKKLSDGgfLKKFVFDSAFSYKFGNMKKGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 438 ASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDVEELNY--WACKGEGEICVRGPN 514
Cdd:PLN02614 398 LASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELDMlGTVGPPVPNVDIRLESVPEMEYdaLASTPRGEICIRGKT 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 515 VFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLK 594
Cdd:PLN02614 478 LFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 595 AFLVGIVVPDPEVMPSWAQKRGIEGTYADLCTSKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTL 674
Cdd:PLN02614 557 SFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTF 636
|
650
....*....|....*....
gi 966948474 675 KAKRPELREYFKKQIEELY 693
Cdd:PLN02614 637 KKKRPQLLKYYQSVIDEMY 655
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
79-694 |
1.14e-132 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 407.20 E-value: 1.14e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 79 PQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRKPNQ------------------PYQWLSYQEVADRAEFLGSGLLQ- 139
Cdd:PLN02387 47 PELVETPWEGATTLAALFEQSCKKYSDKRLLGTRKLISrefetssdgrkfeklhlgEYEWITYGQVFERVCNFASGLVAl 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 140 -HNckacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQ--KAVLLLEHVERk 216
Cdd:PLN02387 127 gHN----KEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQlkKLIDISSQLET- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 217 etpgLKLIILM-DPFEEALKERGQKCGVVIKSMQAVEDCGQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVA 295
Cdd:PLN02387 202 ----VKRVIYMdDEGVDSDSSLSGSSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 296 DFSGFLKVTEKVifpRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFfqGDIRLLSD-----------DMKALCPTIFP 364
Cdd:PLN02387 278 TVAGVMTVVPKL---GKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDtsnkikkgtkgDASALKPTLMT 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 365 VVPRLLNRMYDKIFSQANTP--LKRWLLEFAAKRKQAEVR------SGIIRndSIWDELFFNKIQASLGGCVRMIVTGAA 436
Cdd:PLN02387 353 AVPAILDRVRDGVRKKVDAKggLAKKLFDIAYKRRLAAIEgswfgaWGLEK--LLWDALVFKKIRAVLGGRIRFMLSGGA 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 437 PASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKG---EGEICVRGP 513
Cdd:PLN02387 431 PLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLISDKpmpRGEIVIGGP 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 514 NVFKGYLKDPDRTKEA--LDSDG--WLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVH 589
Cdd:PLN02387 511 SVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIMVH 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 590 GDSLKAFLVGIVVPDPEVMPSWAQKRGIE-GTYADLCTSKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNG 668
Cdd:PLN02387 591 ADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPAKIKLLPEPWTPESG 670
|
650 660
....*....|....*....|....*.
gi 966948474 669 LLTPTLKAKRPELREYFKKQIEELYS 694
Cdd:PLN02387 671 LVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
117-563 |
2.94e-126 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 380.89 E-value: 2.94e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 117 PYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADIS 196
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRALGVGK--GDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 197 TVIVDKPQKAVLLLEHVERKETPGLKLIILMDPFEEALKergqkcgvviksMQAVEDCGQENHHAPVPPQPDDLSIVCFT 276
Cdd:pfam00501 96 VLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEP------------LPEEAKPADVPPPPPPPPDPDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 277 SGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERV-IQSVVYCHGGRVGFFQGDIRL----L 351
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSlGLLGPLLAGATVVLPPGFPALdpaaL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 352 SDDMKALCPTIFPVVPRLLNRMydkifsqantplkrwlleFAAKRKQAEVRSGiirndsiwdelffnkiqaslggcVRMI 431
Cdd:pfam00501 244 LELIERYKVTVLYGVPTLLNML------------------LEAGAPKRALLSS-----------------------LRLV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 432 VTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDW---TSGHVGAPLPCNHIKLVDVEELNYWACKGEGEI 508
Cdd:pfam00501 283 LSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGEL 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 966948474 509 CVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLA 563
Cdd:pfam00501 363 CVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
63-693 |
1.29e-97 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 315.76 E-value: 1.29e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 63 EVEDSGGARRSVIGSGPQL--LTHYYDDARTMYQVFRRGLSISGNGPCLGFRKPN--------------QPY-------- 118
Cdd:PTZ00216 40 ETENASAIYRIAGVTDEEHerLRNEWYYGPNFLQRLERICKERGDRRALAYRPVErvekevvkdadgkeRTMevthfnet 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 119 QWLSYQEVADRAEFLGSGL----LQHNCKactdqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTAD 194
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLaelgLTKGSN------VAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 195 iSTVIVDKPQKAVLLLEHVERKETPGLKLIILmdpfeEALKERGQKCGVVIKSMQAVEDCG---QENHHAPVPPQPDDLS 271
Cdd:PTZ00216 194 -CKAIVCNGKNVPNLLRLMKSGGMPNTTIIYL-----DSLPASVDTEGCRLVAWTDVVAKGhsaGSHHPLNIPENNDDLA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 272 IVCFTSGTTGNPKGAMLTHGNVVADFSGF-LKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFfqGDIRL 350
Cdd:PTZ00216 268 LIMYTSGTTGDPKGVMHTHGSLTAGILALeDRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 351 LSD-------DMKALCPTIFPVVPRLLNRMydKIFSQANTP----LKRWLLEFAAKRKQAEVRSGiiRNDSIWDELFFNK 419
Cdd:PTZ00216 346 LTDtfarphgDLTEFRPVFLIGVPRIFDTI--KKAVEAKLPpvgsLKRRVFDHAYQSRLRALKEG--KDTPYWNEKVFSA 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 420 IQASLGGCVRMIVTGAAPASPTVLGFLRAALGCqVYEGYGQTE--CTAGCTFTtpGDWTSGHVGAPLPCNHIKLVDVEEL 497
Cdd:PTZ00216 422 PRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTEtvCCGGIQRT--GDLEPNAVGQLLKGVEMKLLDTEEY 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 498 NYwACKGE--GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIEN 575
Cdd:PTZ00216 499 KH-TDTPEprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEA 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 576 IYIRSQPVAQ----IYVHGDslKAFLVGIVVPDPEVMPSWAQKRGIEGTYADLCTSKDLKKAILEDMVRLGKESGLHSFE 651
Cdd:PTZ00216 578 LYGQNELVVPngvcVLVHPA--RSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFE 655
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 966948474 652 QVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 693
Cdd:PTZ00216 656 IVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
116-679 |
2.03e-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: 260.75 E-value: 2.03e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 116 QPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADI 195
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKA--GEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 196 STVIVdkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqENHhapvppqPDDLSIVCF 275
Cdd:cd17640 79 VALVV--------------------------------------------------------END-------SDDLATIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 276 TSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFfqGDIRLLSDDM 355
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLLHQIRSLSDIVP----PQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDDL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 356 KALCPTIFPVVPRLLNRMYDKIFSQ--ANTPLKRWLLEFAAkrkqaevrsgiirndsiwdelffnkiqasLGGCVRMIVT 433
Cdd:cd17640 170 KRVKPHYIVSVPRLWESLYSGIQKQvsKSSPIKQFLFLFFL-----------------------------SGGIFKFGIS 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 434 GAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGP 513
Cdd:cd17640 221 GGGALPPHVDTFFEA-IGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGP 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 514 NVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSL 593
Cdd:cd17640 300 QVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQ 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 594 KaFLVGIVVPDPEVMPSWAQKRGI---EGTYADLCTSKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFsVQNGLL 670
Cdd:cd17640 380 K-RLGALIVPNFEELEKWAKESGVklaNDRSQLLASKKVLKLYKNEIKDEISNRPGFKSFEQIAPFALLEEPF-IENGEM 457
|
....*....
gi 966948474 671 TPTLKAKRP 679
Cdd:cd17640 458 TQTMKIKRN 466
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
118-678 |
5.75e-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: 260.86 E-value: 5.75e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 118 YQWLSYQEVADRAEFLGSGLLQHNCKACTDqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADIST 197
Cdd:cd05932 4 VVEFTWGEVADKARRLAAALRALGLEPGSK--IALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 198 VIVDKpqkavllLEHVERKE--TPGLKLIILMDPFEEALKERGqkcgvviksMQAVEDCGQENHHAPvPPQPDDLSIVCF 275
Cdd:cd05932 82 LFVGK-------LDDWKAMApgVPEGLISISLPPPSAANCQYQ---------WDDLIAQHPPLEERP-TRFPEQLATLIY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 276 TSGTTGNPKGAMLTHGNvvadFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDM 355
Cdd:cd05932 145 TSGTTGQPKGVMLTFGS----FAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTFVEDV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 356 KALCPTIFPVVPRLL----NRMYDKIFSQAntpLKRWLlefaakrkQAEVRSGIIRndsiwdelffNKIQASLG-GCVRM 430
Cdd:cd05932 221 QRARPTLFFSVPRLWtkfqQGVQDKIPQQK---LNLLL--------KIPVVNSLVK----------RKVLKGLGlDQCRL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 431 IVTGAAPASPTVLGFLRaALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDveelnywackgEGEICV 510
Cdd:cd05932 280 AGCGSAPVPPALLEWYR-SLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEILV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 511 RGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHG 590
Cdd:cd05932 348 RSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 591 DSLKAfLVGIVVPDPEvmpswAQKRGIEGTYADLCTSkdlKKAILEDMvrlgkESGLHSFEQVKAIHIHSDMFSVQNGLL 670
Cdd:cd05932 428 SGLPA-PLALVVLSEE-----ARLRADAFARAELEAS---LRAHLARV-----NSTLDSHEQLAGIVVVKDPWSIDNGIL 493
|
....*...
gi 966948474 671 TPTLKAKR 678
Cdd:cd05932 494 TPTLKIKR 501
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
113-693 |
3.16e-70 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 239.95 E-value: 3.16e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 113 KPNQPYQWLSYQEVADRAE-----FLGSGLLQHNCkactdqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIR 187
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRqaakaFLKLGLERFHG-------VGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 188 YIINTADISTVIVDKPQKAVLLLEhvERKETPGLKLII-LMDPFEEalKERGQKcgvvikSMQAVEDCG----QENHHAP 262
Cdd:cd05933 74 YVAETSEANILVVENQKQLQKILQ--IQDKLPHLKAIIqYKEPLKE--KEPNLY------SWDEFMELGrsipDEQLDAI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 263 VPPQ-PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQS-VVYCHGGR 340
Cdd:cd05933 144 ISSQkPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIwLPIKVGGQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 341 VGFFQGDIR--LLSDDMKALCPTIFPVVPRLLNRMYDKI---FSQAnTPLKRWLLEFAaKRKQAEV-------RSGIIRN 408
Cdd:cd05933 224 VYFAQPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkavGAKS-GTLKRKIASWA-KGVGLETnlklmggESPSPLF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 409 DSIWDELFFNKIQASLG--GCVRMIvTGAAPASPTVLGFLrAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPC 486
Cdd:cd05933 302 YRLAKKLVFKKVRKALGldRCQKFF-TGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 487 NHIKLVDVEelnywaCKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGE 566
Cdd:cd05933 380 CKTKIHNPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGE 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 567 YVAPEKIENIYIRSQP-VAQIYVHGDSLKaFLVGIVV------PD---------PEVMpSWAQKRGIEGTY-ADLCTSKD 629
Cdd:cd05933 454 NVPPVPIEDAVKKELPiISNAMLIGDKRK-FLSMLLTlkcevnPEtgepldeltEEAI-EFCRKLGSQATRvSEIAGGKD 531
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966948474 630 LK--KAILEDMVRLGKESGLHSFEQVKAIHIHSDmFSVQNGLLTPTLKAKRPELREYFKKQIEELY 693
Cdd:cd05933 532 PKvyEAIEEGIKRVNKKAISNAQKIQKWVILEKD-FSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
92-691 |
6.12e-67 |
|
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: 6.12e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 92 MYQVFRRGLSISGNGPCLGFRkpnqpYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYS 171
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG-----GRRLTYAELDARARRLAAALRALGVGP--GDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 172 MVVVPLYDTLGPGAIRYIINTADISTVIVdkpqkAVLLlehverketpglkliilmdpfeealkergqkcgvviksmqav 251
Cdd:COG0318 74 AVVVPLNPRLTAEELAYILEDSGARALVT-----ALIL------------------------------------------ 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 252 edcgqenhhapvppqpddlsivcFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAHMF---ER 328
Cdd:COG0318 107 -----------------------YTSGTTGRPKGVMLTHRNLLANAAAIAAALG----LTPGDVVLVALPLFHVFgltVG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 329 VIQSVVycHGGRV----GFfqgDIRLLSDDMKALCPTIFPVVPRLLNRMYDkifsqantplkrwllefAAKRKQAEVRSg 404
Cdd:COG0318 160 LLAPLL--AGATLvllpRF---DPERVLELIERERVTVLFGVPTMLARLLR-----------------HPEFARYDLSS- 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 405 iirndsiwdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGA 482
Cdd:COG0318 217 -----------------------LRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGR 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 483 PLPCNHIKLVDVE--ELnywACKGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKVIDRKKHIF 560
Cdd:COG0318 274 PLPGVEVRIVDEDgrEL---PPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-DGWLRTGDLGRLDEDGYLYIVGRKKDMI 349
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 561 KLAqGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFlvgiVVPDPEvmpswaqkrgiegtyADLcTSKDLKKA 633
Cdd:COG0318 350 ISG-GENVYPAEVEEVLAAHPGVAEAAVvgvpdekWGERVVAF----VVLRPG---------------AEL-DAEELRAF 408
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 966948474 634 ILEdmvRLGKesglhsFEQVKAIHIHSDMfsvqngLLTPTLKAKRPELREYFKKQIEE 691
Cdd:COG0318 409 LRE---RLAR------YKVPRRVEFVDEL------PRTASGKIDRRALRERYAAGALE 451
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
118-644 |
1.04e-66 |
|
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: 230.00 E-value: 1.04e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 118 YQWLSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADIST 197
Cdd:cd17641 9 WQEFTWADYADRVRAFALGLLALGVG--RGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 198 VIVDKPQKAVLLLEHveRKETPGLKLIILMDPfeeaLKERGQKCGVVIKSMQAVEDcGQEnHHAPVPP---------QPD 268
Cdd:cd17641 87 VIAEDEEQVDKLLEI--ADRIPSVRYVIYCDP----RGMRKYDDPRLISFEDVVAL-GRA-LDRRDPGlyerevaagKGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 269 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKvifpRQDDVLISFLPLAHMFER---VIQSVVycHGGRVGFFQ 345
Cdd:cd17641 159 DVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPL----GPGDEYVSVLPLPWIGEQmysVGQALV--CGFIVNFPE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 346 gDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWL--------LEFAAKRKQAEVRSGIIRNDS-IWDE 414
Cdd:cd17641 233 -EPETMMEDLREIGPTFVLLPPRVWEGIAADVRArmMDATPFKRFMfelgmklgLRALDRGKRGRPVSLWLRLASwLADA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 415 LFFNKIQASLG-GCVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTEcTAGCTFTTP-GDWTSGHVGAPLPCNHIKLV 492
Cdd:cd17641 312 LLFRPLRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTE-LAGAYTVHRdGDVDPDTVGVPFPGTEVRID 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 493 DVeelnywackgeGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEK 572
Cdd:cd17641 390 EV-----------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQF 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966948474 573 IENIYIRSQPVAQIYVHGDSlKAFLVGIVVPDPEVMPSWAQKRGIE-GTYADLCTSKDLKKAILEDMVRLGKE 644
Cdd:cd17641 459 IENKLKFSPYIAEAVVLGAG-RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKVNAS 530
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
121-671 |
1.62e-65 |
|
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: 226.95 E-value: 1.62e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGSgllQHNCKACTD--QFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTV 198
Cdd:cd17632 68 ITYAELWERVGAVAA---AHDPEQPVRpgDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 199 IVDKPQKAV---LLLEHverketPGLKLIILMDPFEEALKER-----------GQKCGVVIKSMQAVEDCGQENHHAPVP 264
Cdd:cd17632 145 AVSAEHLDLaveAVLEG------GTPPRLVVFDHRPEVDAHRaalesarerlaAVGIPVTTLTLIAVRGRDLPPAPLFRP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 265 PQPDD-LSIVCFTSGTTGNPKGAMLTHgNVVADFsgFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGrVGF 343
Cdd:cd17632 219 EPDDDpLALLIYTSGSTGTPKGAMYTE-RLVATF--WLKVSSIQDIRPPASITLNFMPMSHIAGRISLYGTLARGG-TAY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 344 FQG--DIRLLSDDMKALCPTIFPVVPRLlnrmYDKIFSQANTPLKRWL-----LEFAAKRKQAEVRsgiirndsiwdelf 416
Cdd:cd17632 295 FAAasDMSTLFDDLALVRPTELFLVPRV----CDMLFQRYQAELDRRSvagadAETLAERVKAELR-------------- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 417 fnkiQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTtpgdwtSGHVGAPlPCNHIKLVDVEE 496
Cdd:cd17632 357 ----ERVLGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE--AGAVIL------DGVIVRP-PVLDYKLVDVPE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 497 LNYWACKG---EGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKI 573
Cdd:cd17632 424 LGYFRTDRphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARL 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 574 ENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMpswaqkrgiegtyaDLCTSKDLKKAILEDMVRLGKESGLHSFEQV 653
Cdd:cd17632 504 EAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDAL--------------AGEDTARLRAALAESLQRIAREAGLQSYEIP 569
|
570
....*....|....*...
gi 966948474 654 KAIHIHSDMFSVQNGLLT 671
Cdd:cd17632 570 RDFLIETEPFTIANGLLS 587
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
121-678 |
4.60e-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: 214.61 E-value: 4.60e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLgSGLLQHNCKACTDQfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:cd05914 8 LTYKDLADNIAKF-ALLLKINGVGTGDR-VALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 201 DKPqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhhapvppqpDDLSIVCFTSGTT 280
Cdd:cd05914 86 SDE----------------------------------------------------------------DDVALINYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 281 GNPKGAMLTHGNVVADFSGfLKVTEKVifpRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDI---RLLSDDMKA 357
Cdd:cd05914 102 GNSKGVMLTYRNIVSNVDG-VKEVVLL---GKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIpsaKIIALAFAQ 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 358 LCPTIfpVVPRLLNRMYDKIFSQANTPLKRWLLEFAAKrkqaevrsgIIRNDSIWdELFFNKIQASLGGCVRMIVTGAAP 437
Cdd:cd05914 178 VTPTL--GVPVPLVIEKIFKMDIIPKLTLKKFKFKLAK---------KINNRKIR-KLAFKKVHEAFGGNIKEFVIGGAK 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 438 ASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPlpcnhIKLVDVEELNYWACKGEGEICVRGPNVFK 517
Cdd:cd05914 246 INPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKV-----IDGVEVRIDSPDPATGEGEIIVRGPNVMK 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 518 GYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVA--QIYVHGDSLKA 595
Cdd:cd05914 320 GYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLesLVVVQEKKLVA 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 596 flvgIVVPDPEVMPSWAQKRgiegtyadlctsKDLKKAILEDmVRLGKESGLHSFEQVKAIHIHSDMFSVqngllTPTLK 675
Cdd:cd05914 400 ----LAYIDPDFLDVKALKQ------------RNIIDAIKWE-VRDKVNQKVPNYKKISKVKIVKEEFEK-----TPKGK 457
|
...
gi 966948474 676 AKR 678
Cdd:cd05914 458 IKR 460
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
121-615 |
4.46e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 204.75 E-value: 4.46e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGK-GDR-VAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 201 -------DKPQKAVL-LLEHVERKETP-GLKLIILMDPFEEALkERGQkcgvviksmqavedcgQENHHAPVppQPDDLS 271
Cdd:PRK07656 109 lglflgvDYSATTRLpALEHVVICETEeDDPHTEKMKTFTDFL-AAGD----------------PAERAPEV--DPDDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 272 IVCFTSGTTGNPKGAMLTHGNV---VADFSGFLKVTEKvifprqDDVLISfLPLAHMFerviqsvvychGGRVGF----- 343
Cdd:PRK07656 170 DILFTSGTTGRPKGAMLTHRQLlsnAADWAEYLGLTEG------DRYLAA-NPFFHVF-----------GYKAGVnaplm 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 344 ----------FQGD--IRLLSDDMkalcPTIFPVVPRLLNRMYDkifsqantplkrwllefAAKRKQAEVRSgiirndsi 411
Cdd:PRK07656 232 rgatilplpvFDPDevFRLIETER----ITVLPGPPTMYNSLLQ-----------------HPDRSAEDLSS-------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 412 wdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGCTFTTPGD---WTSGHVGAPLPCN 487
Cdd:PRK07656 283 ----------------LRLAVTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIAGV 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 488 HIKLVDveELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGE 566
Cdd:PRK07656 347 ENKIVN--ELGEEVPVGEvGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IVGGF 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 966948474 567 YVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLV---GIVVPDPEVMpSWAQKR 615
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 ... |
269-606 |
1.08e-57 |
|
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: 198.66 E-value: 1.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 269 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekvIFPRQDDVLISFLPLAHMFerVIQSVVYC--HGGRVGFFQG 346
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS----GGLTEGDVFLSTLPLFHIG--GLFGLLGAllAGGTVVLLPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 347 -DIRLLSDDMKALCPTIFPVVPRLLNRMydkifsqantplkrwllefaakRKQAEVRSgiiRNDSiwdelffnkiqaslg 425
Cdd:cd04433 75 fDPEAALELIEREKVTILLGVPTLLARL----------------------LKAPESAG---YDLS--------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 426 gCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT--SGHVGAPLPCNHIKLVDVEElNYWACK 503
Cdd:cd04433 115 -SLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDPDG-GELPPG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 504 GEGEICVRGPNVFKGYLKDPDRTkEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAPEKIENIYIRSQPV 583
Cdd:cd04433 193 EIGELVVRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPGV 270
|
330 340
....*....|....*....|...
gi 966948474 584 AQIYVHGdslkaflvgivVPDPE 606
Cdd:cd04433 271 AEAAVVG-----------VPDPE 282
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
93-598 |
1.10e-57 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 202.79 E-value: 1.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 93 YQVFRRGLSISGNGPCLGFRKpnqpyQWLSYQEVADRAEFLGSGLLQHNCKaCTDQfIGVFAQNRPEWIIAELACYTYSM 172
Cdd:cd05936 2 ADLLEEAARRFPDKTALIFMG-----RKLTYRELDALAEAFAAGLQNLGVQ-PGDR-VALMLPNCPQFPIAYFGALKAGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 173 VVVPLYDTLGPGAIRYIINTADISTVIVDkpqkavlllehverketpglkliilmDPFEEALKergqkcgvviksmqave 252
Cdd:cd05936 75 VVVPLNPLYTPRELEHILNDSGAKALIVA--------------------------VSFTDLLA----------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 253 dcGQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIfpRQDDVLISFLPLAHMFErviQS 332
Cdd:cd05936 112 --AGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLL--EGDDVVLAALPLFHVFG---LT 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 333 VVYCHGGRVGFFQ------GDIRLLsDDMKALCPTIFPVVPRLLNRmydkifsqantplkrwLLEFAAKRKqaEVRSGIi 406
Cdd:cd05936 185 VALLLPLALGATIvliprfRPIGVL-KEIRKHRVTIFPGVPTMYIA----------------LLNAPEFKK--RDFSSL- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 407 rndsiwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT-SGHVGAPLP 485
Cdd:cd05936 245 ----------------------RLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRkPGSIGIPLP 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 486 CNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQG 565
Cdd:cd05936 303 GTEVKIVD-DDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGG 379
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 966948474 566 EYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLV 598
Cdd:cd05936 380 FNVYPREVEEVLYEHPAVAEAAVvgvpdpySGEAVKAFVV 419
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
121-598 |
6.06e-56 |
|
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: 198.21 E-value: 6.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLK--KGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 201 DKPQKAVLLLehVERKETPGLKlIILMDPFEEALKERGQkcgvvikSMQAVedCGQENHHAPVPPQ--PDDLSIVCFTSG 278
Cdd:cd05911 89 DPDGLEKVKE--AAKELGPKDK-IIVLDDKPDGVLSIED-------LLSPT--LGEEDEDLPPPLKdgKDDTAAILYSSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 279 TTGNPKGAMLTHGNVVADFSgFLKVTEKVIFPRqDDVLISFLPLAHMFErvIQSVVYC--HGGRV----GFFqgdirllS 352
Cdd:cd05911 157 TTGLPKGVCLSHRNLIANLS-QVQTFLYGNDGS-NDVILGFLPLYHIYG--LFTTLASllNGATViimpKFD-------S 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 353 DDMKALCP----TIFPVVPRLLNRMydkifsqANTPLkrwllefaakrkqaevrsgiirndsiwdelfFNKIQASlggCV 428
Cdd:cd05911 226 ELFLDLIEkykiTFLYLVPPIAAAL-------AKSPL-------------------------------LDKYDLS---SL 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 429 RMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGE 507
Cdd:cd05911 265 RVILSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 508 ICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIyIRSQP----- 582
Cdd:cd05911 345 ICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAV-LLEHPgvada 422
|
490
....*....|....*....
gi 966948474 583 -VAQIY--VHGDSLKAFLV 598
Cdd:cd05911 423 aVIGIPdeVSGELPRAYVV 441
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
86-605 |
1.69e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 173.06 E-value: 1.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 86 YDDARTMYQVFRRGLSISGNGPCLGFRKPNqpyqwLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAEL 165
Cdd:PRK06187 2 QDYPLTIGRILRHGARKHPDKEAVYFDGRR-----TTYAELDERVNRLANALRALGVKK--GDRVAVFDWNSHEYLEAYF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 166 ACytySM---VVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlLLEHVE--RKETPGLKLIILMDP----------- 229
Cdd:PRK06187 75 AV---PKigaVLHPINIRLKPEEIAYILNDAEDRVVLVDSE-----FVPLLAaiLPQLPTVRTVIVEGDgpaaplapevg 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 230 -FEEALKergqkcgvviksmqavedcGQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVvadFSGFLKVTEKVI 308
Cdd:PRK06187 147 eYEELLA-------------------AASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNL---FLHSLAVCAWLK 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 309 FpRQDDVLISFLPLAHmferviqsvvyCHG---GRVGFFQG---------DIRLLSDDMKALCPTIFPVVPRLLNRMydk 376
Cdd:PRK06187 205 L-SRDDVYLVIVPMFH-----------VHAwglPYLALMAGakqviprrfDPENLLDLIETERVTFFFAVPTIWQML--- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 377 ifSQANTPLKRWLlefaakrkqaevrSGIirndsiwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYE 456
Cdd:PRK06187 270 --LKAPRAYFVDF-------------SSL-----------------------RLVIYGGAALPPALLREFKEKFGIDLVQ 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 457 GYGQTECTAGCTFTTPGDWTSGH------VGAPLPCNHIKLVDvEELNYWACKGE--GEICVRGPNVFKGYLKDPDRTKE 528
Cdd:PRK06187 312 GYGMTETSPVVSVLPPEDQLPGQwtkrrsAGRPLPGVEARIVD-DDGDELPPDGGevGEIIVRGPWLMQGYWNRPEATAE 390
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966948474 529 ALDsDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDP 605
Cdd:PRK06187 391 TID-GGWLHTGDVGYIDEDGYLYITDRIKDVIISG-GENIYPRELEDA---------LYGHPAVAEVAVIG--VPDE 454
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
121-576 |
8.48e-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: 155.95 E-value: 8.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGSgLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:cd05909 8 LTYRKLLTGAIALAR-KLAKMTKE--GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 201 DKPQKAVLLLEHVERKETPgLKLIILmdpfeEALKER---GQKCGVVIKSMQAVEDCGQENHHAPVppQPDDLSIVCFTS 277
Cdd:cd05909 85 SKQFIEKLKLHHLFDVEYD-ARIVYL-----EDLRAKiskADKCKAFLAGKFPPKWLLRIFGVAPV--QPDDPAVILFTS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 278 GTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAHMFerviqsvvychggrvGFFQGDIRLLSDDMKA 357
Cdd:cd05909 157 GSEGLPKGVVLSHKNLLANVEQITAIFD----PNPEDVVFGALPFFHSF---------------GLTGCLWLPLLSGIKV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 358 LC---PTIFPVVPRLLnrmYDK----IFSqanTPLkrwLLEFAAKRKQAEVRSGIirndsiwdelffnkiqaslggcvRM 430
Cdd:cd05909 218 VFhpnPLDYKKIPELI---YDKkatiLLG---TPT---FLRGYARAAHPEDFSSL-----------------------RL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 431 IVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEIC 509
Cdd:cd05909 266 VVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLL 345
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966948474 510 VRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENI 576
Cdd:cd05909 346 VRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDI 410
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
216-694 |
6.10e-40 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 156.80 E-value: 6.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 216 KETPGLKLIILMDPFE---------EALKERGQKCGV-------VIKSMQAVEDCGQENhhapvppqPDDLSIVCFTSGT 279
Cdd:PTZ00342 244 NDLSNELEDISLGPLEydkeklekiKDLKEKAKKLGIsiilfddMTKNKTTNYKIQNED--------PDFITSIVYTSGT 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 280 TGNPKGAMLTHGNV------VADFSGFLKVTEKVIFprqddvliSFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSD 353
Cdd:PTZ00342 316 SGKPKGVMLSNKNLyntvvpLCKHSIFKKYNPKTHL--------SYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 354 DMKALCPTIFPVVPRLLNRMYDKIFSQAN--TPLKRWLlefaAKRKQAEVRSGIIRNDSIWDELFFN---KIQASLGGCV 428
Cdd:PTZ00342 388 DIYNSKGNILAGVPKVFNRIYTNIMTEINnlPPLKRFL----VKKILSLRKSNNNGGFSKFLEGITHissKIKDKVNPNL 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 429 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPG-DWTSGHVGAPL-PCNHIKLVDVEELNYWACKGEG 506
Cdd:PTZ00342 464 EVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTE-TTGPIFVQHAdDNNTESIGGPIsPNTKYKVRTWETYKATDTLPKG 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 507 EICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQI 586
Cdd:PTZ00342 543 ELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFC 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 587 YVHG-DSLKAFLvGIVVPDPEVM------PSWAQKRGI-EGTYADLCTSKDLKKAILEDMVR-----LGKESGLHSFEQV 653
Cdd:PTZ00342 623 VVYGdDSMDGPL-AIISVDKYLLfkclkdDNMLESTGInEKNYLEKLTDETINNNIYVDYVKgkmleVYKKTNLNRYNII 701
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 966948474 654 KAIHIHSDMFSVQNgLLTPTLKAKRPEL-REY--FKKQIEELYS 694
Cdd:PTZ00342 702 NDIYLTSKVWDTNN-YLTPTFKVKRFYVfKDYafFIDQVKKIYK 744
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
247-576 |
2.41e-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: 152.00 E-value: 2.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 247 SMQAVEDCGQENHHAPVPPQ--PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifPRQDDVLISFLPLAH 324
Cdd:cd05904 135 SLSFSDLLFEADEAEPPVVVikQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSN--SDSEDVFLCVLPMFH 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 325 MFerviqsvvychgGRVGFFQGDIRL-----------LSDDMKALCP---TIFPVVPrllnrmydkifsqantPLkrwll 390
Cdd:cd05904 213 IY------------GLSSFALGLLRLgatvvvmprfdLEELLAAIERykvTHLPVVP----------------PI----- 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 391 eFAAKRKQAEVRSGIIRndsiwdelffnkiqaSLggcvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTF 469
Cdd:cd05904 260 -VLALVKSPIVDKYDLS---------------SL----RQIMSGAAPLGKELIeAFRAKFPNVDLGQGYGMTESTGVVAM 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 470 TTP---GDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLP 546
Cdd:cd05904 320 CFApekDRAKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDE 399
|
330 340 350
....*....|....*....|....*....|
gi 966948474 547 AGTLKVIDRKKHIFKLaQGEYVAPEKIENI 576
Cdd:cd05904 400 DGYLFIVDRLKELIKY-KGFQVAPAELEAL 428
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
121-609 |
5.09e-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: 149.75 E-value: 5.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLgSGLLQHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIv 200
Cdd:cd05941 12 ITYADLVARAARL-ANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 201 dkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhhapvppqpdDLSIVCFTSGTT 280
Cdd:cd05941 90 --------------------------------------------------------------------DPALILYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 281 GNPKGAMLTHGNVVADFSGFLKVTEKvifpRQDDVLISFLPLAHMFERV--IQSVVYChGGRV---GFFQGDIRLLSDDM 355
Cdd:cd05941 102 GRPKGVVLTHANLAANVRALVDAWRW----TEDDVLLHVLPLHHVHGLVnaLLCPLFA-GASVeflPKFDPKEVAISRLM 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 356 KALcpTIFPVVPRllnrMYDKIFS--QANTPLKRWLLEFAAKRkqaevrsgiirndsiwdelffnkiqaslggcVRMIVT 433
Cdd:cd05941 177 PSI--TVFMGVPT----IYTRLLQyyEAHFTDPQFARAAAAER-------------------------------LRLMVS 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 434 GAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTTP--GDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVR 511
Cdd:cd05941 220 GSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVR 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 512 GPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKK-HIFKlAQGEYVAPEKIENIyIRSQP-VAQIYVH 589
Cdd:cd05941 298 GPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEIERV-LLAHPgVSECAVI 375
|
490 500
....*....|....*....|...
gi 966948474 590 GDSLKAF---LVGIVVPDPEVMP 609
Cdd:cd05941 376 GVPDPDWgerVVAVVVLRAGAAA 398
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
96-605 |
6.84e-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: 149.30 E-value: 6.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 96 FRRGLSISGNGPCLGFrkPNQPyqwLSYQEVADRAEFLGSGLlQHNCKACTDQfIGVFAQNRPEWIIAELACYTYSMVVV 175
Cdd:cd17631 1 LRRRARRHPDRTALVF--GGRS---LTYAELDERVNRLAHAL-RALGVAKGDR-VAVLSKNSPEFLELLFAAARLGAVFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 176 PLYDTLGPGAIRYIINTADiSTVIVDkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcg 255
Cdd:cd17631 74 PLNFRLTPPEVAYILADSG-AKVLFD------------------------------------------------------ 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 256 qenhhapvppqpdDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekvIFPRQDDVLISFLPLAHMFE-RVIQSVV 334
Cdd:cd17631 99 -------------DLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAA----LDLGPDDVLLVVAPLFHIGGlGVFTLPT 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 335 YCHGGRV----GFFQGDIRLLSDDMKAlcpTIFPVVPRLLNRMydkifsqANTPLkrwllefaakrkqaevrsgiirnds 410
Cdd:cd17631 162 LLRGGTVvilrKFDPETVLDLIERHRV---TSFFLVPTMIQAL-------LQHPR------------------------- 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 411 iWDELFFnkiqASLggcvRMIVTGAAPASPTVLGFLRAAlGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPCNH 488
Cdd:cd17631 207 -FATTDL----SSL----RAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHRRklGSAGRPVFFVE 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 489 IKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYV 568
Cdd:cd17631 277 VRIVD-PDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFR-DGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENV 353
|
490 500 510
....*....|....*....|....*....|....*..
gi 966948474 569 APEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDP 605
Cdd:cd17631 354 YPAEVEDV---------LYEHPAVAEVAVIG--VPDE 379
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
120-683 |
6.06e-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: 138.98 E-value: 6.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 120 WLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVI 199
Cdd:cd05926 14 ALTYADLAELVDDLARQLAALGIKK--GDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 200 VDKpqkaVLLLEHVERKETPGLkliilmdpfeeALKERGQKCGVVIKSMQAVEDCGQENHHAPV----PPQPDDLSIVCF 275
Cdd:cd05926 92 TPK----GELGPASRAASKLGL-----------AILELALDVGVLIRAPSAESLSNLLADKKNAksegVPLPDDLALILH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 276 TSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvIFPrqDDVLISFLPLAHmferVIQSVVYC-----HGGRV----GFfqg 346
Cdd:cd05926 157 TSGTTGRPKGVPLTHRNLAASATNITNTYK--LTP--DDRTLVVMPLFH----VHGLVASLlstlaAGGSVvlppRF--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 347 DIRLLSDDMKALCPTIFPVVPRLLnrmydKIfsqantplkrwLLEFAAKRKQAEvrsgiirndsiwdelfFNKIqaslgg 426
Cdd:cd05926 226 SASTFWPDVRDYNATWYTAVPTIH-----QI-----------LLNRPEPNPESP----------------PPKL------ 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 427 cvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTP---GDWTSGHVGAPlpcNHIKLVDVEElnywacK 503
Cdd:cd05926 268 --RFIRSCSASLPPAVLEALEATFGAPVLEAYGMTE-AAHQMTSNPlppGPRKPGSVGKP---VGVEVRILDE------D 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 504 GE-------GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENI 576
Cdd:cd05926 336 GEilppgvvGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGV 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 577 YIRSQPVAQIYVHGdslkaflvgivVPDP---EVMPSWAQKRgiEGTYADlctskdlKKAILEDMvrlgkESGLHSFEQV 653
Cdd:cd05926 415 LLSHPAVLEAVAFG-----------VPDEkygEEVAAAVVLR--EGASVT-------EEELRAFC-----RKHLAAFKVP 469
|
570 580 590
....*....|....*....|....*....|
gi 966948474 654 KAIHIhsdmfsVQNGLLTPTLKAKRPELRE 683
Cdd:cd05926 470 KKVYF------VDELPKTATGKIQRRKVAE 493
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
265-604 |
1.50e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 138.98 E-value: 1.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 265 PQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD-FSGFLKVTEkviFPRQDDVLISFLPLAHMF--ERVIQSVVYCHGGRV 341
Cdd:PRK05605 216 PTPDDVALILYTSGTTGKPKGAQLTHRNLFANaAQGKAWVPG---LGDGPERVLAALPMFHAYglTLCLTLAVSIGGELV 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 342 GFFQGDIRLLSDDMKALCPTIFPVVPRLlnrmYDKIfsqantplkrwlLEFAAKRkqaevrsGIirndsiwdelffnkiq 421
Cdd:PRK05605 293 LLPAPDIDLILDAMKKHPPTWLPGVPPL----YEKI------------AEAAEER-------GV---------------- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 422 aSLGGcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECT---AGCTFTTpgDWTSGHVGAPLPCNHIKLVDVEELN 498
Cdd:PRK05605 334 -DLSG-VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpiiVGNPMSD--DRRPGYVGVPFPDTEVRIVDPEDPD 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 499 YWACKGE-GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIy 577
Cdd:PRK05605 410 ETMPDGEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELI-ITGGFNVYPAEVEEV- 486
|
330 340
....*....|....*....|....*..
gi 966948474 578 irsqpVAQiyvHGDSLKAFLVGIVVPD 604
Cdd:PRK05605 487 -----LRE---HPGVEDAAVVGLPRED 505
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
150-615 |
8.04e-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: 134.88 E-value: 8.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 150 IGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlllehVERKETPGLKLIILMDP 229
Cdd:TIGR01923 27 VALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL---------LEEKDFQADSLDRIEAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 230 FEEALKERGQKcgvviksmqavedcgqenhhapvppQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkVTEKVIF 309
Cdd:TIGR01923 98 GRYETSLSASF-------------------------NMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVG---SKENLGF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 310 PRQDDVLISfLPLAH------MFERVIQsvvychGGRVGFFQGDIRLLsDDMKALCPTIFPVVPRLLNRMYDKifSQANT 383
Cdd:TIGR01923 150 TEDDNWLLS-LPLYHisglsiLFRWLIE------GATLRIVDKFNQLL-EMIANERVTHISLVPTQLNRLLDE--GGHNE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 384 PLKRWLLefaakrkqaevrsgiirndsiwdelffnkiqaslGGcvrmivtGAAPASptvlgFLRAAL--GCQVYEGYGQT 461
Cdd:TIGR01923 220 NLRKILL----------------------------------GG-------SAIPAP-----LIEEAQqyGLPIYLSYGMT 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 462 E-CTAGCTFTTPGDWTSGHVGAPLPCNHIKL-VDVEElnywackGEGEICVRGPNVFKGYLkDPDRTKEALDSDGWLHTG 539
Cdd:TIGR01923 254 EtCSQVTTATPEMLHARPDVGRPLAGREIKIkVDNKE-------GHGEIMVKGANLMKGYL-YQGELTPAFEQQGWFNTG 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 540 DIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYV--HGDSL-----KAFLVGIVVPDPEVMPSWA 612
Cdd:TIGR01923 326 DIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVVvpKPDAEwgqvpVAYIVSESDISQAKLIAYL 404
|
...
gi 966948474 613 QKR 615
Cdd:TIGR01923 405 TEK 407
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
89-694 |
1.92e-33 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 138.06 E-value: 1.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 89 ARTMYQVFRRGLSISGNGPCLGFRKPNQPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACY 168
Cdd:PTZ00297 426 VRSLGEMWERSVTRHSTFRCLGQTSESGESEWLTYGTVDARARELGSGLLALGVRP--GDVIGVDCEASRNIVILEVACA 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 169 TYSMVVVPLydtLGPG-AIRYIINTADISTVIVDKPQKAVLLLEHVERKETpglklIILMDPFEEALKERGQK-CGVVIK 246
Cdd:PTZ00297 504 LYGFTTLPL---VGKGsTMRTLIDEHKIKVVFADRNSVAAILTCRSRKLET-----VVYTHSFYDEDDHAVARdLNITLI 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 247 SMQAVEdcgQENHHAPVPPQP--DDLSIVCFTSGTTGNPKGAML-----THGNVVADFSgFLKVTEKVIFPRQDDVLISF 319
Cdd:PTZ00297 576 PYEFVE---QKGRLCPVPLKEhvTTDTVFTYVVDNTTSASGDGLavvrvTHADVLRDIS-TLVMTGVLPSSFKKHLMVHF 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 320 LPLAHMFERVIQSVVYCHGGRVGffQGDIRLLSDDMKALCPTIFPVVPRLlnrmydkiFSQANTPLKR----------WL 389
Cdd:PTZ00297 652 TPFAMLFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSL--------FSTSRLQLSRanerysavysWL 721
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 390 LEfaakrKQAEVRSGII----RNDSIWDELFFNKIQASLGGCVRMIVTGAAPASPTV-----LGFLRAALGCQVYegygQ 460
Cdd:PTZ00297 722 FE-----RAFQLRSRLInihrRDSSLLRFIFFRATQELLGGCVEKIVLCVSEESTSFsllehISVCYVPCLREVF----F 792
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 461 TECTAGCTFTtpgdwtsghvGAPLPCNHIKLVDVEELNYWACKGEGEICVRGpnvfkgylkDPDRTKEAldsdgwlhtgd 540
Cdd:PTZ00297 793 LPSEGVFCVD----------GTPAPSLQVDLEPFDEPSDGAGIGQLVLAKKG---------EPRRTLPI----------- 842
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 541 IGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAfLVGIVVPDPEVMP-SWAQKRGIE- 618
Cdd:PTZ00297 843 AAQWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEfEWRQSHCMGe 921
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 619 -GTYADLCTSKDLKK----AILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 693
Cdd:PTZ00297 922 gGGPARQLGWTELVAyassLLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIERFY 1001
|
.
gi 966948474 694 S 694
Cdd:PTZ00297 1002 S 1002
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
220-578 |
1.55e-32 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 132.41 E-value: 1.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 220 GLKLIILMDPFEEALKERGQKCGVVIKSM-QAVEDC--------GQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTH 290
Cdd:PLN02246 122 GAKLIITQSCYVDKLKGLAEDDGVTVVTIdDPPEGClhfseltqADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTH 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 291 GNVVADfsgflkVTEKV------IFPRQDDVLISFLPLAHMFErvIQSVVYChGGRVG--------FfqgDIRLLSDDMK 356
Cdd:PLN02246 202 KGLVTS------VAQQVdgenpnLYFHSDDVILCVLPMFHIYS--LNSVLLC-GLRVGaailimpkF---EIGALLELIQ 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 357 ALCPTIFPVVPrllnrmydkifsqantPLkrwLLEFAakrKQAEVRSgiirndsiwDELffnkiqASlggcVRMIVTGAA 436
Cdd:PLN02246 270 RHKVTIAPFVP----------------PI---VLAIA---KSPVVEK---------YDL------SS----IRMVLSGAA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 437 PASPTVLGFLRAALGCQVY-EGYGQTE-------CTAgctFT-TPGDWTSGHVGAPLPCNHIKLVDVE---ELNYWACkg 504
Cdd:PLN02246 309 PLGKELEDAFRAKLPNAVLgQGYGMTEagpvlamCLA---FAkEPFPVKSGSCGTVVRNAELKIVDPEtgaSLPRNQP-- 383
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966948474 505 eGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYI 578
Cdd:PLN02246 384 -GEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAELEALLI 455
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
122-582 |
1.56e-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: 130.46 E-value: 1.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 122 SYQEVADRAEFLGSGLLQHnCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGA-IRYIINTADISTVIV 200
Cdd:TIGR01733 1 TYRELDERANRLARHLRAA-GGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPL-DPAYPAErLAFILEDAGARLLLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 201 DKPqkavllleHVERKETPGLKLIILMDPFEEALkergqkcgvviksmqavEDCGQENHhAPVPPQPDDLSIVCFTSGTT 280
Cdd:TIGR01733 79 DSA--------LASRLAGLVLPVILLDPLELAAL-----------------DDAPAPPP-PDAPSGPDDLAYVIYTSGST 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 281 GNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPLAH------MFerviqsVVYCHGGRVgffqgdiRLLSDD 354
Cdd:TIGR01733 133 GRPKGVVVTHRSLVN----LLAWLARRYGLDPDDRVLQFASLSFdasveeIF------GALLAGATL-------VVPPED 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 355 MKAlcpTIFPVVPRLLNRMYDKIFSQANTPLKRWLLEfaakrkqaevrsgiirndsiwdelffnkiQASLGGCVRMIVTG 434
Cdd:TIGR01733 196 EER---DDAALLAALIAEHPVTVLNLTPSLLALLAAA-----------------------------LPPALASLRLVILG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 435 AAPASPTVLGFLRAALG-CQVYEGYGQTECTAGCT-FTTPGDWTSGHV----GAPLPCNHIKLVDvEELNYWACKGEGEI 508
Cdd:TIGR01733 244 GEALTPALVDRWRARGPgARLINLYGPTETTVWSTaTLVDPDDAPRESpvpiGRPLANTRLYVLD-DDLRPVPVGVVGEL 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 509 CVRGPNVFKGYLKDPDRTKEA-LDSDGWL-------HTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIyIRS 580
Cdd:TIGR01733 323 YIGGPGVARGYLNRPELTAERfVPDPFAGgdgarlyRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAA-LLR 400
|
..
gi 966948474 581 QP 582
Cdd:TIGR01733 401 HP 402
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
255-598 |
1.76e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 132.58 E-value: 1.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 255 GQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGfLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVV 334
Cdd:PRK05677 194 GAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQ-CRALMGSNLNEGCEILIAPLPLYHIYAFTFHCMA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 335 YCHGGRVGFfqgdirLLSDdmkalcPTIFPVVPRLLNRMYDKIFSQANTplkrwllEFAAkrkqaevrsgiIRNDSIWDE 414
Cdd:PRK05677 273 MMLIGNHNI------LISN------PRDLPAMVKELGKWKFSGFVGLNT-------LFVA-----------LCNNEAFRK 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 415 LFFNKIQASLGGcvRMIVTGAAPASptvlgfLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDv 494
Cdd:PRK05677 323 LDFSALKLTLSG--GMALQLATAER------WKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVID- 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 495 EELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIE 574
Cdd:PRK05677 394 DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVSGFNVYPNELE 472
|
330 340 350
....*....|....*....|....*....|..
gi 966948474 575 NIyIRSQP----VAQIYV----HGDSLKAFLV 598
Cdd:PRK05677 473 DV-LAALPgvlqCAAIGVpdekSGEAIKVFVV 503
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
263-598 |
2.16e-32 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 132.49 E-value: 2.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 263 VPPQ--PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPRQDDVLISfLPLAHMFERVIQSVVYCHGGr 340
Cdd:PRK08974 199 VKPElvPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGPLLHPGKELVVTA-LPLYHIFALTVNCLLFIELG- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 341 vgffqGDIRLLSDdmkalcPTIFPVVPRLLNRMYDKIFSQANTPLKRWLlefaakrkqaevrsgiirNDSIWDELFFNKI 420
Cdd:PRK08974 277 -----GQNLLITN------PRDIPGFVKELKKYPFTAITGVNTLFNALL------------------NNEEFQELDFSSL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 421 QASLGGcvrmivtgAAPASPTVLGFLRAALGCQVYEGYGQTECT---AGCTFTTPGdwTSGHVGAPLPCNHIKLVDvEEL 497
Cdd:PRK08974 328 KLSVGG--------GMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVNPYDLDY--YSGSIGLPVPSTEIKLVD-DDG 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 498 NYWACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIY 577
Cdd:PRK08974 397 NEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMI-LVSGFNVYPNEIEDVV 474
|
330 340
....*....|....*....|....*...
gi 966948474 578 IRSQPVAQIY-------VHGDSLKAFLV 598
Cdd:PRK08974 475 MLHPKVLEVAavgvpseVSGEAVKIFVV 502
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
117-557 |
2.46e-32 |
|
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: 132.02 E-value: 2.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 117 PYQWLSYQEVADRAEFLGSGLLQHNCKAcTDQFIGVFAQNRpEWIIAELACYTYSMVVVPLydtlGPGAIRyiintadis 196
Cdd:cd05906 36 SEEFQSYQDLLEDARRLAAGLRQLGLRP-GDSVILQFDDNE-DFIPAFWACVLAGFVPAPL----TVPPTY--------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 197 tvivDKPQKAVLLLEHVerKETPGLKLII----LMDPFEEALKERGQkCGVVIKSMQAVEDCGqENHHAPvPPQPDDLSI 272
Cdd:cd05906 101 ----DEPNARLRKLRHI--WQLLGSPVVLtdaeLVAEFAGLETLSGL-PGIRVLSIEELLDTA-ADHDLP-QSRPDDLAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 273 VCFTSGTTGNPKGAMLTHGNVVADFSGflKVTEKVIFPrqDDVLISFLPLAHmfervIQSVVYCHggrvgffQGDIRLLS 352
Cdd:cd05906 172 LMLTSGSTGFPKAVPLTHRNILARSAG--KIQHNGLTP--QDVFLNWVPLDH-----VGGLVELH-------LRAVYLGC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 353 DDMKALCPTIFPVVPRLLNRMyDKiFSQANTplkrWLLEFA-AK-RKQAEVRSgiirnDSIWDelffnkiqasLGGCVRM 430
Cdd:cd05906 236 QQVHVPTEEILADPLRWLDLI-DR-YRVTIT----WAPNFAfALlNDLLEEIE-----DGTWD----------LSSLRYL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 431 IVTGAAPASPTVLGFLRAALGCQVYE-----GYGQTECTAGCTFTTP---GDWTSGH----VGAPLPCNHIKLVDVEEln 498
Cdd:cd05906 295 VNAGEAVVAKTIRRLLRLLEPYGLPPdairpAFGMTETCSGVIYSRSfptYDHSQALefvsLGRPIPGVSMRIVDDEG-- 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966948474 499 ywACKGEGEIC---VRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkWLPAGTLKVIDRKK 557
Cdd:cd05906 373 --QLLPEGEVGrlqVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
255-605 |
2.67e-32 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 132.31 E-value: 2.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 255 GQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADF---SGFLKVTEKVifPRQDDVLISFLPLAHMFERVIQ 331
Cdd:PRK08751 195 GRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMqqaHQWLAGTGKL--EEGCEVVITALPLYHIFALTAN 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 332 SVVYCHGGrvgffqGDIRLLSDdmkalcPTIFPVVPRLLNRMYDKIFSQANTPLKRWLlefaakrkqaevrsgiirNDSI 411
Cdd:PRK08751 273 GLVFMKIG------GCNHLISN------PRDMPGFVKELKKTRFTAFTGVNTLFNGLL------------------NTPG 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 412 WDELFFNKIQASLGGcvRMIVTGAapasptVLGFLRAALGCQVYEGYGQTECT-AGCTFTTPGDWTSGHVGAPLPCNHIK 490
Cdd:PRK08751 323 FDQIDFSSLKMTLGG--GMAVQRS------VAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDAC 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 491 LVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAP 570
Cdd:PRK08751 395 IKD-DAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-LVSGFNVYP 472
|
330 340 350
....*....|....*....|....*....|....*....
gi 966948474 571 EKIENIYIRSQPVAQIYVHG----DSLKAFLVGIVVPDP 605
Cdd:PRK08751 473 NEIEDVIAMMPGVLEVAAVGvpdeKSGEIVKVVIVKKDP 511
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
269-599 |
3.79e-31 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 124.54 E-value: 3.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 269 DLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTEkvifprqDDVLISFLPLAHMFErviqsvvYCHGGRVGFFQ 345
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLraaAAWADCADLTE-------DDRYLIINPFFHTFG-------YKAGIVACLLT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 346 GdirllsddmkalcPTIFPV----VPRLLNRMYDKIFSQANTP--LKRWLLEFAAkRKQAEVRSgiirndsiwdelffnk 419
Cdd:cd17638 67 G-------------ATVVPVavfdVDAILEAIERERITVLPGPptLFQSLLDHPG-RKKFDLSS---------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 420 iqaslggcVRMIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGcTFTTPGD---WTSGHVGAPLPCNHIKLVDve 495
Cdd:cd17638 117 --------LRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVA-TMCRPGDdaeTVATTCGRACPGFEVRIAD-- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 496 elnywackgEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIEN 575
Cdd:cd17638 186 ---------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEG 255
|
330 340 350
....*....|....*....|....*....|.
gi 966948474 576 IYIRSQPVAQIYV-------HGDSLKAFLVG 599
Cdd:cd17638 256 ALAEHPGVAQVAVigvpderMGEVGKAFVVA 286
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
261-607 |
5.52e-31 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 128.21 E-value: 5.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 261 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADF--------SGFLKvtekvifPRQDDVLISF--LPLAHMFERVI 330
Cdd:PRK07059 197 KPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqmeawlqPAFEK-------KPRPDQLNFVcaLPLYHIFALTV 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 331 QSVVYCHGGRVGFF---QGDIRLLSDDMKALCPTIFPVVPRLLNRMYdkifsqaNTPlkrwllEFaakrkqaevrsgiir 407
Cdd:PRK07059 270 CGLLGMRTGGRNILipnPRDIPGFIKELKKYQVHIFPAVNTLYNALL-------NNP------DF--------------- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 408 ndsiwDELFFNKIQASLGGcvrmivtGAAPASPTVLGFLRAAlGCQVYEGYG--QTECTAGCTFTTPGDWTsGHVGAPLP 485
Cdd:PRK07059 322 -----DKLDFSKLIVANGG-------GMAVQRPVAERWLEMT-GCPITEGYGlsETSPVATCNPVDATEFS-GTIGLPLP 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 486 CNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQG 565
Cdd:PRK07059 388 STEVSIRD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMI-LVSG 465
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 966948474 566 EYVAPEKIENIyIRSQP----VAQIYVH----GDSLKAFlvgIVVPDPEV 607
Cdd:PRK07059 466 FNVYPNEIEEV-VASHPgvleVAAVGVPdehsGEAVKLF---VVKKDPAL 511
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
121-610 |
6.55e-31 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 126.10 E-value: 6.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACY----TYsmvvVPLYDTLGPGAIRYIINTADIS 196
Cdd:cd05930 13 LTYAELDARANRLARYLRERGVGP--GDLVAVLLERSLEMVVAILAVLkagaAY----VPLDPSYPAERLAYILEDSGAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 197 TVIVDkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhhapvppqPDDLSIVCFT 276
Cdd:cd05930 87 LVLTD-----------------------------------------------------------------PDDLAYVIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 277 SGTTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPLAH------MFerviqsVVYCHGGRVGFFQGDIRL 350
Cdd:cd05930 102 SGSTGKPKGVMVEHRGLVN----LLLWMQEAYPLTPGDRVLQFTSFSFdvsvweIF------GALLAGATLVVLPEEVRK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 351 LSDDMKALC----PTIFPVVPRLLNRMYDKIFSQANTPLkrwllefaakrkqaevrsgiirndsiwdelffnkiqaslgg 426
Cdd:cd05930 172 DPEALADLLaeegITVLHLTPSLLRLLLQELELAALPSL----------------------------------------- 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 427 cvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFT--TPGDWTSGHV--GAPLPCNHIKLVDvEELNYWA 501
Cdd:cd05930 211 --RLVLVGGEALPPDLVrRWRELLPGARLVNLYGPTEATVDATYYrvPPDDEEDGRVpiGRPIPNTRVYVLD-ENLRPVP 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 502 CKGEGEICVRGPNVFKGYLKDPDRTKEA-----LDSDGWLH-TGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIEN 575
Cdd:cd05930 288 PGVPGELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIELGEIEA 366
|
490 500 510
....*....|....*....|....*....|....*...
gi 966948474 576 IYIRSQPVAQIYV---HGDSLKAFLVGIVVPDPEVMPS 610
Cdd:cd05930 367 ALLAHPGVREAAVvarEDGDGEKRLVAYVVPDEGGELD 404
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
122-606 |
6.82e-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: 127.64 E-value: 6.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 122 SYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLgpgAIRYIINTADIST-VIV 200
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLK--QNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIY---NERELDHSLNISKpTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 201 DKPQKAVLLLEHVERKeTPGLKLIILMDPFEEAlkeRGQKCGVVIKSMQAVEDCGQENHHAPVPPQPDDLSIVCFTSGTT 280
Cdd:cd17642 121 FCSKKGLQKVLNVQKK-LKIIKTIIILDSKEDY---KGYQCLYTFITQNLPPGFNEYDFKPPSFDRDEQVALIMNSSGST 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 281 GNPKGAMLTHGNVVADFSGflkvTEKVIF---PRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGF---FQGD--IRLLS 352
Cdd:cd17642 197 GLPKGVQLTHKNIVARFSH----ARDPIFgnqIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLmykFEEElfLRSLQ 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 353 D---DMKALCPTIFPVVPR--LLNRmYD----KIFSQANTPLKRWLLEFAAKRkqaevrsgiirndsiwdelfFNkiqas 423
Cdd:cd17642 273 DykvQSALLVPTLFAFFAKstLVDK-YDlsnlHEIASGGAPLSKEVGEAVAKR--------------------FK----- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 424 lggcvrmivtgaapasptvLGFLRaalgcqvyEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACK 503
Cdd:cd17642 327 -------------------LPGIR--------QGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 504 GEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRsqpv 583
Cdd:cd17642 380 ERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQ---- 454
|
490 500
....*....|....*....|...
gi 966948474 584 aqiyvHGDSLKAFLVGIvvPDPE 606
Cdd:cd17642 455 -----HPKIFDAGVAGI--PDED 470
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-590 |
9.15e-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: 123.93 E-value: 9.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSGF-LKVTEkvifprqDDVLISFLPLAHMFERVIqSVVYC--HGGRV 341
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVnnGYFIGErLGLTE-------QDRLCIPVPLFHCFGSVL-GVLACltHGATM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 342 GFFQgdirlLSDDMKAL--------C------PTIFPvvpRLLNRMydkifSQANTPLKRwllefaakrkqaeVRSGIIr 407
Cdd:cd05917 73 VFPS-----PSFDPLAVleaiekekCtalhgvPTMFI---AELEHP-----DFDKFDLSS-------------LRTGIM- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 408 ndsiwdelffnkiqaslggcvrmivtGAAPASPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGDWTS---GHVGAP 483
Cdd:cd05917 126 --------------------------AGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDSIEkrvNTVGRI 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 484 LPCNHIKLVDvEELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkL 562
Cdd:cd05917 180 MPHTEAKIVD-PEGGIVPPVGVpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-I 257
|
330 340
....*....|....*....|....*...
gi 966948474 563 AQGEYVAPEKIENIYIRSQPVAQIYVHG 590
Cdd:cd05917 258 RGGENIYPREIEEFLHTHPKVSDVQVVG 285
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
121-588 |
9.96e-31 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 125.57 E-value: 9.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADIstviv 200
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGP--GDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 201 dkpqkavlllehverketpglKLIILMDPFeealkergqkcgvviksmqavedcGQENHHApvppQPDDLSIVCFTSGTT 280
Cdd:cd05903 75 ---------------------KVFVVPERF------------------------RQFDPAA----MPDAVALLLFTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 281 GNPKGAMLTHGNVVADFSGFLkvtEKVIFPRQDDVLISfLPLAHmferviqsvvycHGGRVGFFqgdirllsddmkaLCP 360
Cdd:cd05903 106 GEPKGVMHSHNTLSASIRQYA---ERLGLGPGDVFLVA-SPMAH------------QTGFVYGF-------------TLP 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 361 TIFPVvPRLLNRMYDK------------IFSQANTPLKRWLLEfaAKRKQAEVRSGIirndsiwdelffnkiqaslggcv 428
Cdd:cd05903 157 LLLGA-PVVLQDIWDPdkalalmrehgvTFMMGATPFLTDLLN--AVEEAGEPLSRL----------------------- 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 429 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGD----WTSGhvGAPLPCNHIKLVDvEELNYWACKG 504
Cdd:cd05903 211 RTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPedrrLYTD--GRPLPGVEIKVVD-DTGATLAPGV 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 505 EGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVA 584
Cdd:cd05903 288 EGELLSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVI 365
|
....
gi 966948474 585 QIYV 588
Cdd:cd05903 366 EAAV 369
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
269-606 |
3.16e-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: 3.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 269 DLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVTEKVIfpRQDDVLISFLPLAHM---FERVIQSVVycHGGRV---- 341
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLT--FAGYYSARRFGL--GEDDVYLTVLPLFHInaqAVSVLAALS--VGATLvllp 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 342 ----GFFQGDIRllsdDMKALCPTIFPVVPRLLnrmydkiFSQANTPlkrwllefaaKRKQAEVRsgiirndsiwdelff 417
Cdd:cd05934 156 rfsaSRFWSDVR----RYGATVTNYLGAMLSYL-------LAQPPSP----------DDRAHRLR--------------- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 418 nkiqaslggcvrmiVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEel 497
Cdd:cd05934 200 --------------AAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDD-- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 498 NYWACKGE-GEICVR---GPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAPEKI 573
Cdd:cd05934 264 GQELPAGEpGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEV 341
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 966948474 574 ENIYIRSQPVAQIYVHG-------DSLKAFlvgIVVPDPE 606
Cdd:cd05934 342 ERAILRHPAVREAAVVAvpdevgeDEVKAV---VVLRPGE 378
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
121-590 |
3.26e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 125.66 E-value: 3.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVV---PLYDT------LGPGAIRYII- 190
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQP--GDRVGIWAPNCAEWLLTQFATARIGAILVninPAYRAseleyaLGQSGVRWVIc 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 191 ----NTADISTVIVD-KPQKAVLLLEHVERKETPGLKLIILMDPFE-------EALKERGQkcGVVIKSMQAVEdcGQEN 258
Cdd:PRK12583 124 adafKTSDYHAMLQElLPGLAEGQPGALACERLPELRGVVSLAPAPppgflawHELQARGE--TVSREALAERQ--ASLD 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 259 HHAPVPPQpddlsivcFTSGTTGNPKGAMLTHGNVV--ADFSG-FLKVTEKvifprqdDVLISFLPLAHMFERVIqSVVY 335
Cdd:PRK12583 200 RDDPINIQ--------YTSGTTGFPKGATLSHHNILnnGYFVAeSLGLTEH-------DRLCVPVPLYHCFGMVL-ANLG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 336 C--HGGRVGF----FQGDIRLLSDDMKAlCPTIFPVvPRLLnrmydkiFSQANTPlKRWLLEFAAkrkqaeVRSGIIrnd 409
Cdd:PRK12583 264 CmtVGACLVYpneaFDPLATLQAVEEER-CTALYGV-PTMF-------IAELDHP-QRGNFDLSS------LRTGIM--- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 410 siwdelffnkiqaslggcvrmivtGAAPASPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGD-----WTSghVGAP 483
Cdd:PRK12583 325 ------------------------AGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSLQTTAADdlerrVET--VGRT 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 484 LPCNHIKLVDVEELNywACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkL 562
Cdd:PRK12583 379 QPHLEVKVVDPDGAT--VPRGEiGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMI-I 455
|
490 500
....*....|....*....|....*...
gi 966948474 563 AQGEYVAPEKIENIYIRSQPVAQIYVHG 590
Cdd:PRK12583 456 RGGENIYPREIEEFLFTHPAVADVQVFG 483
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
150-606 |
3.36e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 124.92 E-value: 3.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 150 IGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAvlllehverketpglkliilmdp 229
Cdd:PRK09088 50 LAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDDAVAA----------------------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 230 feealkerGQKCGVVIKSMQAVEDCGQENHHAPVPPqpDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlKVTEKVif 309
Cdd:PRK09088 107 --------GRTDVEDLAAFIASADALEPADTPSIPP--ERVSLILFTSGTSGQPKGVMLSERNLQQTAHNF-GVLGRV-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 310 prqdDVLISFLPLAHMFERV--IQSV--VYCHGGRV----GFFQG-DIRLLSDdmKALCPTIFPVVPRLLNRmydkifsq 380
Cdd:PRK09088 174 ----DAHSSFLCDAPMFHIIglITSVrpVLAVGGSIlvsnGFEPKrTLGRLGD--PALGITHYFCVPQMAQA-------- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 381 antplkrwllefaakrkqaevrsgiIRNDSIWDELFFNKIQAslggcvrmIVTGAAP-ASPTVLGFLraALGCQVYEGYG 459
Cdd:PRK09088 240 -------------------------FRAQPGFDAAALRHLTA--------LFTGGAPhAAEDILGWL--DDGIPMVDGFG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 460 QTEctAGCTFTTPGDWT-----SGHVGAPLPCNHIKLVDVEELNYWAckGE-GEICVRGPNVFKGYLKDPDRTKEALDSD 533
Cdd:PRK09088 285 MSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVVDDQGNDCPA--GVpGELLLRGPNLSPGYWRRPQATARAFTGD 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966948474 534 GWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIEniyirsqpvAQIYVHGDSLKAFLVGivVPDPE 606
Cdd:PRK09088 361 GWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIE---------AVLADHPGIRECAVVG--MADAQ 421
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
93-544 |
3.94e-30 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 125.61 E-value: 3.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 93 YQVFRRGLSISGNGPCLGFRKPNQPYQWLSYQEVADRAEFLGSGLLQHnckactdqfiGV--------FAQNRPEWIIAE 164
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRAL----------GVkkgdrvaiYLPNIPEAVIAM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 165 LACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVD----KPQKAVLLLEHVE--RKETPGLKLIILMD---------- 228
Cdd:COG0365 82 LACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITAdgglRGGKVIDLKEKVDeaLEELPSLEHVIVVGrtgadvpmeg 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 229 --PFEEALKERGQKCgvviksmqavedcgqenhhAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVTEK 306
Cdd:COG0365 162 dlDWDELLAAASAEF-------------------EPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYL----VHAATTAK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 307 VIF-PRQDDVL--------------ISFLPLAH-----MFERVIqsvVYCHGGRvgFFQgdirlLSDDMKalcPTIFPVV 366
Cdd:COG0365 219 YVLdLKPGDVFwctadigwatghsyIVYGPLLNgatvvLYEGRP---DFPDPGR--LWE-----LIEKYG---VTVFFTA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 367 PRLLnRMydkifsqantpLKRWLLEFAAKRKQAevrsgiirndsiwdelffnkiqaSLggcvRMIVTGAAPASPTVLGFL 446
Cdd:COG0365 286 PTAI-RA-----------LMKAGDEPLKKYDLS-----------------------SL----RLLGSAGEPLNPEVWEWW 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 447 RAALGCQVYEGYGQTECtaGCTFTTPGDWTS---GHVGAPLPCNHIKLVDvEELNywACKG--EGEICVRG--PNVFKGY 519
Cdd:COG0365 327 YEAVGVPIVDGWGQTET--GGIFISNLPGLPvkpGSMGKPVPGYDVAVVD-EDGN--PVPPgeEGELVIKGpwPGMFRGY 401
|
490 500
....*....|....*....|....*..
gi 966948474 520 LKDPDRTKEAL--DSDGWLHTGDIGKW 544
Cdd:COG0365 402 WNDPERYRETYfgRFPGWYRTGDGARR 428
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
158-605 |
7.55e-30 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 124.22 E-value: 7.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 158 PEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDkPQKAVLLLEHVERKETPGLkliilmdpfeEALKER 237
Cdd:PRK07514 64 PEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCD-PANFAWLSKIAAAAGAPHV----------ETLDAD 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 238 GQkcGVViksMQAVEDCGQEnhHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGN------VVADFSGFlkvtekvifpR 311
Cdd:PRK07514 133 GT--GSL---LEAAAAAPDD--FETVPRGADDLAAILYTSGTTGRSKGAMLSHGNllsnalTLVDYWRF----------T 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 312 QDDVLISFLPLAH---MFerVIQSVVYCHGGRVGFFQgdiRLLSDDMKALCP--TIFPVVPRLLNRMYdkifsqANTPLK 386
Cdd:PRK07514 196 PDDVLIHALPIFHthgLF--VATNVALLAGASMIFLP---KFDPDAVLALMPraTVMMGVPTFYTRLL------QEPRLT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 387 RwllEFAAKrkqaevrsgiirndsiwdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAG 466
Cdd:PRK07514 265 R---EAAAH--------------------------------MRLFISGSAPLLAETHREFQERTGHAILERYGMTE-TNM 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 467 CTfTTP--GDWTSGHVGAPLPCNHIKLVDVE---ELNywacKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGD 540
Cdd:PRK07514 309 NT-SNPydGERRAGTVGFPLPGVSLRVTDPEtgaELP----PGEiGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGD 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 541 IGKWLPAGTLKVIDRKKHIfkLAQGEY-VAPEKIENiYIRSQP-VAQIYVHGDSLKAF---LVGIVVPDP 605
Cdd:PRK07514 384 LGKIDERGYVHIVGRGKDL--IISGGYnVYPKEVEG-EIDELPgVVESAVIGVPHPDFgegVTAVVVPKP 450
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
113-576 |
3.51e-29 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 122.55 E-value: 3.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 113 KPNQPYQWlSYQEVADRAEFLGSGLLQHNCKACTdqfigVFAQNRPEW---IIAELACYTYSMVVVPLYDTLGPGAIRYI 189
Cdd:PRK06087 43 VDNHGASY-TYSALDHAASRLANWLLAKGIEPGD-----RVAFQLPGWcefTIIYLACLKVGAVSVPLLPSWREAELVWV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 190 INTADISTVIVDKPQKAV--LLLEHVERKETPGLKLIILMDPFEEALKErgqkcgvvIKSMQAVEDcgQENHHAPVPPQP 267
Cdd:PRK06087 117 LNKCQAKMFFAPTLFKQTrpVDLILPLQNQLPQLQQIVGVDKLAPATSS--------LSLSQIIAD--YEPLTTAITTHG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 268 DDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifprQDDVLISFLPLAHmferviqSVVYCHGGRVGFFQGD 347
Cdd:PRK06087 187 DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLT----WQDVFMMPAPLGH-------ATGFLHGVTAPFLIGA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 348 IRLLSDDMKAlcptifPVVPRLLNRmyDKI-FSQANTPLkrwllefaakrkqaevrsgiirndsIWDELFFNKIQASLGG 426
Cdd:PRK06087 256 RSVLLDIFTP------DACLALLEQ--QRCtCMLGATPF-------------------------IYDLLNLLEKQPADLS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 427 CVRMIVTGAAPASPTVLgflRAAL--GCQVYEGYGQTECTAGcTFTTPGD---WTSGHVGAPLPCNHIKLVDvEELNYWA 501
Cdd:PRK06087 303 ALRFFLCGGTTIPKKVA---RECQqrGIKLLSVYGSTESSPH-AVVNLDDplsRFMHTDGYAAAGVEIKVVD-EARKTLP 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966948474 502 CKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENI 576
Cdd:PRK06087 378 PGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDI 451
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
255-598 |
7.19e-29 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 121.85 E-value: 7.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 255 GQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKV------IFPRQDDVLISFLPLAHMFER 328
Cdd:PRK12492 194 GRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLgpdgqpLMKEGQEVMIAPLPLYHIYAF 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 329 VIQSVVYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLlnrmydkifsqaNTplkrwllEFAAKRKQAEVRSgiirn 408
Cdd:PRK12492 274 TANCMCMMVSGNHNVLITNPRDIPGFIKELGKWRFSALLGL------------NT-------LFVALMDHPGFKD----- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 409 dsiwdeLFFNKIQASLGGcvrmivtGAAPASPTVLGFlRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCN 487
Cdd:PRK12492 330 ------LDFSALKLTNSG-------GTALVKATAERW-EQLTGCTIVEGYGLTETSPVASTNPYGELARlGTVGIPVPGT 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 488 HIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEY 567
Cdd:PRK12492 396 ALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLI-IVSGFN 473
|
330 340 350
....*....|....*....|....*....|....*...
gi 966948474 568 VAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLV 598
Cdd:PRK12492 474 VYPNEIEDVVMAHPKVANCAAigvpderSGEAVKLFVV 511
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
89-557 |
1.74e-28 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 121.22 E-value: 1.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 89 ARTMYQVFRRGLSISGNGPCLgfrkpnqpyqwlSYQEVADR---------AEFLG-----SGLLqHNCKACTDQFIGVFA 154
Cdd:PRK07529 24 PASTYELLSRAAARHPDAPAL------------SFLLDADPldrpetwtyAELLAdvtrtANLL-HSLGVGPGDVVAFLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 155 QNRPEWIIAELACYTYSmVVVPLYDTLGPGAIRYIINTADISTVIVDKP-------QKAVLLLEHVerketPGLKLIILM 227
Cdd:PRK07529 91 PNLPETHFALWGGEAAG-IANPINPLLEPEQIAELLRAAGAKVLVTLGPfpgtdiwQKVAEVLAAL-----PELRTVVEV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 228 D-------PFEEALKERGQKCGVVIKSMQAVEDCGQENHH-APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD-FS 298
Cdd:PRK07529 165 DlarylpgPKRLAVPLIRRKAHARILDFDAELARQPGDRLfSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANaWL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 299 GFLkvtekVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGR---VGFFQG--DIRLLSDDMK---ALCPTIFPVVPRLL 370
Cdd:PRK07529 245 GAL-----LLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAhvvLATPQGyrGPGVIANFWKiveRYRINFLSGVPTVY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 371 NRMydkifsqANTPlkrwllefaakrkqaevrsgiirndsiwdelffnkIQASLGGCVRMIVTGAAPASPTVLGFLRAAL 450
Cdd:PRK07529 320 AAL-------LQVP-----------------------------------VDGHDISSLRYALCGAAPLPVEVFRRFEAAT 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 451 GCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLVDVEEL-NYW--ACKGE-GEICVRGPNVFKGYLkDPDR 525
Cdd:PRK07529 358 GVRIVEGYGLTEATCVSSVNPPdGERRIGSVGLRLPYQRVRVVILDDAgRYLrdCAVDEvGVLCIAGPNVFSGYL-EAAH 436
|
490 500 510
....*....|....*....|....*....|..
gi 966948474 526 TKEALDSDGWLHTGDIGKWLPAGTLKVIDRKK 557
Cdd:PRK07529 437 NKGLWLEDGWLNTGDLGRIDADGYFWLTGRAK 468
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
119-615 |
2.36e-28 |
|
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: 118.93 E-value: 2.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 119 QWLSYQEVADRAEFLGSGLLQHNckACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGA-IRYIINTADIST 197
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARG--VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPL-DPDYPADrLRYILEDAEPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 198 VIVDkpqkavlllehverketpglkliilmdpfeEALKERGQKCGVVIksMQAVEDCGQENHHAPVPPQPDDLSIVCFTS 277
Cdd:cd12116 88 VLTD------------------------------DALPDRLPAGLPVL--LLALAAAAAAPAAPRTPVSPDDLAYVIYTS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 278 GTTGNPKGAMLTHGNVVADFSGFlkvTEKVIFPRQDDVL--------IS----FLPLahmferviqsvvyCHGGRVGFFQ 345
Cdd:cd12116 136 GSTGRPKGVVVSHRNLVNFLHSM---RERLGLGPGDRLLavttyafdISllelLLPL-------------LAGARVVIAP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 346 GDI----RLLSDDMKALCPTIFpvvprllnrmydkifsQAnTP-LKRWLLefaakrkqaevrsgiirnDSIWDELffnki 420
Cdd:cd12116 200 RETqrdpEALARLIEAHSITVM----------------QA-TPaTWRMLL------------------DAGWQGR----- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 421 qASLggcvRMIVTGAApaSPTVLGFLRAALGCQVYEGYGQTECT--AGCTFTTPGDwTSGHVGAPLPCNHIKLVDvEELN 498
Cdd:cd12116 240 -AGL----TALCGGEA--LPPDLAARLLSRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLD-AALR 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 499 YWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH-------TGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPE 571
Cdd:cd12116 311 PVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQVKI-RGHRIELG 389
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 966948474 572 KIENIYIRSQPVAQ--IYVHGDSLKAFLVGIVVPDPEVMPSWAQKR 615
Cdd:cd12116 390 EIEAALAAHPGVAQaaVVVREDGGDRRLVAYVVLKAGAAPDAAALR 435
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
112-606 |
6.90e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 118.52 E-value: 6.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 112 RKPNQPYQW-----LSYQEVADRAEFLgSGLLQHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAI 186
Cdd:PRK08314 22 RYPDKTAIVfygraISYRELLEEAERL-AGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 187 RYIINTADISTVIV-----DKPQKAV--LLLEHV-------ERKETPGLKLIILMDpfEEALKERGQKCGVViksmqAVE 252
Cdd:PRK08314 101 AHYVTDSGARVAIVgselaPKVAPAVgnLRLRHVivaqysdYLPAEPEIAVPAWLR--AEPPLQALAPGGVV-----AWK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 253 DCGQENHHA-PVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD-FSGFLKVTEKVifprqDDVLISFLPLAHM--FER 328
Cdd:PRK08314 174 EALAAGLAPpPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANaVGSVLWSNSTP-----ESVVLAVLPLFHVtgMVH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 329 VIQSVVYChGGRVgffqgdirllsddmkalcpTIFP-----VVPRLLNRMydKIFSQANTPlkRWLLEFAAKRKQAEvrs 403
Cdd:PRK08314 249 SMNAPIYA-GATV-------------------VLMPrwdreAAARLIERY--RVTHWTNIP--TMVVDFLASPGLAE--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 404 giiRNDSiwdelffnkiqaSLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWT-SGHVGA 482
Cdd:PRK08314 302 ---RDLS------------SL----RYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTE-TMAQTHSNPPDRPkLQCLGI 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 483 PLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEA---LDSDGWLHTGDIGKWLPAGTLKVIDRKKHI 559
Cdd:PRK08314 362 PTFGVDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRM 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 966948474 560 FKlAQGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFlvgiVVPDPE 606
Cdd:PRK08314 442 IN-ASGFKVWPAEVENLLYKHPAIQEACViatpdprRGETVKAV----VVLRPE 490
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
173-610 |
7.94e-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: 117.16 E-value: 7.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 173 VVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlLLEHVErketpgLKLIILMDPfeealkergqkcGVVIKsmqaVE 252
Cdd:cd05922 48 VFVPLNPTLKESVLRYLVADAGGRIVLADAG-----AADRLR------DALPASPDP------------GTVLD----AD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 253 DCGQENHHAP-VPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTEkvifprqDDVLISFLPLAhmfer 328
Cdd:cd05922 101 GIRAARASAPaHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSiaeYLGITA-------DDRALTVLPLS----- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 329 viqsvvYCHGGRV---GFFQGDIRLLS----------DDMKALCPTIFPVVP---RLLNRMydkIFSQANTPLKRWLLEF 392
Cdd:cd05922 169 ------YDYGLSVlntHLLRGATLVLTndgvlddafwEDLREHGATGLAGVPstyAMLTRL---GFDPAKLPSLRYLTQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 393 AAKRKQAEVRSgiirndsiwdelffnkiqaslggcvrmivtgaapasptvlgfLRAAL-GCQVYEGYGQTECTAGCTFTT 471
Cdd:cd05922 240 GGRLPQETIAR------------------------------------------LRELLpGAQVYVMYGQTEATRRMTYLP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 472 PG--DWTSGHVGAPLPCNHIklvDVEELNYWACK-GE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkWLPA 547
Cdd:cd05922 278 PEriLEKPGSIGLAIPGGEF---EILDDDGTPTPpGEpGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLA-RRDE 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966948474 548 -GTLKVIDRKKHIFKLAqGEYVAPEKIENIyIRSQP---VAQIYVHGDSLKAFLVGIVVPDPEVMPS 610
Cdd:cd05922 354 dGFLFIVGRRDRMIKLF-GNRISPTEIEAA-ARSIGliiEAAAVGLPDPLGEKLALFVTAPDKIDPK 418
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
121-613 |
9.89e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 117.78 E-value: 9.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAE-----FLGSGLLQHNCkactdqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADI 195
Cdd:PRK06188 38 LTYGQLADRISryiqaFEALGLGTGDA-------VALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 196 STVIVDK---PQKAVLLLEHVerketPGLKLIILMDPFEEalkerGQKCGVVIKSMQavedcgqenhHAPVPP--QPDDL 270
Cdd:PRK06188 111 STLIVDPapfVERALALLARV-----PSLKHVLTLGPVPD-----GVDLLAAAAKFG----------PAPLVAaaLPPDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 271 SIVCFTSGTTGNPKGAMLTHGNVV-------ADFSgflkvtekviFPRQddvlISFL---PLAH----MFERVIQ---SV 333
Cdd:PRK06188 171 AGLAYTGGTTGKPKGVMGTHRSIAtmaqiqlAEWE----------WPAD----PRFLmctPLSHaggaFFLPTLLrggTV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 334 VYCHGgrvgfFqgdirllsdDMKALCPTI--------FpVVPRLLNRmydkifsqantplkrwLLEFAAKRKqaevrsgi 405
Cdd:PRK06188 237 IVLAK-----F---------DPAEVLRAIeeqritatF-LVPTMIYA----------------LLDHPDLRT-------- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 406 iRNDSiwdelffnkiqaSLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHV----- 480
Cdd:PRK06188 278 -RDLS------------SL----ETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPkrlts 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 481 -GAPLPCNHIKLVDvEELNYWAcKGE-GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKH 558
Cdd:PRK06188 341 cGRPTPGLRVALLD-EDGREVA-QGEvGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKD 417
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966948474 559 IFkLAQGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAflvgIVVPDPEVMPSWAQ 613
Cdd:PRK06188 418 MI-VTGGFNVFPREVEDVLAEHPAVAQVAVigvpdekWGEAVTA----VVVLRPGAAVDAAE 474
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
265-613 |
2.04e-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: 115.14 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 265 PQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF---LKVTEkvifprqDDVLISFLPLAHM--FERVIQSVVYchGG 339
Cdd:cd05912 74 VKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSalnLGLTE-------DDNWLCALPLFHIsgLSILMRSVIY--GM 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 340 RVGFFQG-DIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTPLKRWLLefaakrkqaevrsgiirndsiwdelffn 418
Cdd:cd05912 145 TVYLVDKfDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRCILL---------------------------- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 419 kiqaslggcvrmivtGAAPASPTVLGFLRAaLGCQVYEGYGQTE-CTAGCTFTtPGDWTS--GHVGAPLPCNHIKLVDVE 495
Cdd:cd05912 197 ---------------GGGPAPKPLLEQCKE-KGIPVYQSYGMTEtCSQIVTLS-PEDALNkiGSAGKPLFPVELKIEDDG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 496 ELNYwackGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIEN 575
Cdd:cd05912 260 QPPY----EVGEILLKGPNVTKGYLNRPDATEESFE-NGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEE 333
|
330 340 350
....*....|....*....|....*....|....*...
gi 966948474 576 IYIRSQPVAQIYVhgdslkaflVGIvvPDPEvmpsWAQ 613
Cdd:cd05912 334 VLLSHPAIKEAGV---------VGI--PDDK----WGQ 356
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
248-588 |
2.88e-27 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 116.62 E-value: 2.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 248 MQAVEDCGQENHHAPVppQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADF-SGFLKVTEKVIfprQDDVLISFLPLAHMF 326
Cdd:PLN02330 166 LEAADRAGDTSDNEEI--LQTDLCALPFSSGTTGISKGVMLTHRNLVANLcSSLFSVGPEMI---GQVVTLGLIPFFHIY 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 327 --ERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPrllnrmydkifsqantPLKRWLLEfaakrkqaevrsg 404
Cdd:PLN02330 241 giTGICCATLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVP----------------PIILNLVK------------- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 405 iirnDSIWDELFFNKIQaslggcVRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTagCTFTTPGDWTSGH---- 479
Cdd:PLN02330 292 ----NPIVEEFDLSKLK------LQAIMTAAAPLAPELLtAFEAKFPGVQVQEAYGLTEHS--CITLTHGDPEKGHgiak 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 480 ---VGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRK 556
Cdd:PLN02330 360 knsVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRI 439
|
330 340 350
....*....|....*....|....*....|..
gi 966948474 557 KHIFKLaQGEYVAPEKIENIYIRSQPVAQIYV 588
Cdd:PLN02330 440 KELIKY-KGFQVAPAELEAILLTHPSVEDAAV 470
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
121-615 |
4.37e-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: 114.50 E-value: 4.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGSGLlqHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:cd05935 2 LTYLELLEVVKKLASFL--SNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 201 DKPQkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhhapvppqpDDLSIVCFTSGTT 280
Cdd:cd05935 80 GSEL---------------------------------------------------------------DDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 281 GNPKGAMLTHGNVVADFSGFLKVTEKVifprQDDVLISFLPLAHM--FERVIQSVVYCHGGRVGFFQGDIRLLSDDMKAL 358
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQSAVWTGLT----PSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMARWDRETALELIEKY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 359 CPTIFPVVPRLLNRMydkifsqANTPlkrwllefaakrkqaevrsgiirndsiwdelffnKIQASLGGCVRMIVTGAAPA 438
Cdd:cd05935 173 KVTFWTNIPTMLVDL-------LATP----------------------------------EFKTRDLSSLKVLTGGGAPM 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 439 SPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKG 518
Cdd:cd05935 212 PPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKG 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 519 YLKDPDRTKEALDSDG---WLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYV------- 588
Cdd:cd05935 292 YWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVisvpder 370
|
490 500 510
....*....|....*....|....*....|...
gi 966948474 589 HGDSLKAFLVgiVVP------DPEVMPSWAQKR 615
Cdd:cd05935 371 VGEEVKAFIV--LRPeyrgkvTEEDIIEWAREQ 401
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
120-542 |
9.31e-27 |
|
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: 115.03 E-value: 9.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 120 WLSYQEVADRAEFLGSGLLQHNckACTDQFIGVFAQNrPEWIIAELACYTYSMVVVPLYDTLGPGA---IRYIINTADIS 196
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAVG--KPGDRVLLLAPPG-LDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 197 TVIVDKPQKAvLLLEHVERKETPGLKLIILMDPFEEALKERGQkcgvviksmqavedcgqenhhaPVPPQPDDLSIVCFT 276
Cdd:cd05931 101 VVLTTAAALA-AVRAFAASRPAAGTPRLLVVDLLPDTSAADWP----------------------PPSPDPDDIAYLQYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 277 SGTTGNPKGAMLTHGNVVADFSGFLkvteKVIFPRQDDVLISFLPLAH---MFERVIQSVVYchGGRVGFFQgdirllsd 353
Cdd:cd05931 158 SGSTGTPKGVVVTHRNLLANVRQIR----RAYGLDPGDVVVSWLPLYHdmgLIGGLLTPLYS--GGPSVLMS-------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 354 dmkalcPTIFpvvprlLNRmydkifsqantPLkRWL-----------------LEFAAKRKQAEVRSGIirndsiwdELf 416
Cdd:cd05931 224 ------PAAF------LRR-----------PL-RWLrlisryratisaapnfaYDLCVRRVRDEDLEGL--------DL- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 417 fnkiqaslgGCVRMIVTGAAPASPTVL----------GFLRAAlgcqVYEGYGQTECTAGCTFTTPG----------DWT 476
Cdd:cd05931 271 ---------SSWRVALNGAEPVRPATLrrfaeafapfGFRPEA----FRPSYGLAEATLFVSGGPPGtgpvvlrvdrDAL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 477 SGHV----------------GAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKE------ALDSDG 534
Cdd:cd05931 338 AGRAvavaaddpaarelvscGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaATDEGG 417
|
....*...
gi 966948474 535 WLHTGDIG 542
Cdd:cd05931 418 WLRTGDLG 425
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
107-693 |
1.26e-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: 114.84 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 107 PCLGFRKPNQPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTY---SMVVVPLYDTLGp 183
Cdd:cd05921 12 TWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGLSA--ERPLLILSGNSIEHALMALAAMYAgvpAAPVSPAYSLMS- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 184 gairyiintADISTvivdkpqkavllLEHVERKETPGLKLIILMDPFEEALKE-----------RGQKCG---VVIKSMQ 249
Cdd:cd05921 89 ---------QDLAK------------LKHLFELLKPGLVFAQDAAPFARALAAifplgtplvvsRNAVAGrgaISFAELA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 250 AVEDCGQ-ENHHAPVppQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekviFPRQDD---VLISFLPLAHM 325
Cdd:cd05921 148 ATPPTAAvDAAFAAV--GPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQT-----YPFFGEeppVLVDWLPWNHT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 326 F--ERVIQSVVYcHGGRV---------GFFQGDIRLLSDDMkalcPTIFPVVPrllnrmydkifsqantplKRWllefaa 394
Cdd:cd05921 221 FggNHNFNLVLY-NGGTLyiddgkpmpGGFEETLRNLREIS----PTVYFNVP------------------AGW------ 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 395 krkqaEVRSGIIRNDSIWDELFFNKiqaslggcVRMIVTGAAPASPTVLGFLRA----ALGCQV--YEGYGQTECTAGCT 468
Cdd:cd05921 272 -----EMLVAALEKDEALRRRFFKR--------LKLMFYAGAGLSQDVWDRLQAlavaTVGERIpmMAGLGATETAPTAT 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 469 FTTPGDWTSGHVGAPLPCNHIKLVdveelnywACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWL--- 545
Cdd:cd05921 339 FTHWPTERSGLIGLPAPGTELKLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpd 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 546 -PAGTLKVIDRKKHIFKLAQGEYVA--PekieniyIRSQPVAQI--YVHgDSL-----KAFLVGIVVPDPEVMPswAQKR 615
Cdd:cd05921 411 dPAKGLVFDGRVAEDFKLASGTWVSvgP-------LRARAVAACapLVH-DAVvagedRAEVGALVFPDLLACR--RLVG 480
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966948474 616 GIEGTYADLCTSKDLKKAILEDMVRLGKESGLHSFEQVKAIhIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 693
Cdd:cd05921 481 LQEASDAEVLRHAKVRAAFRDRLAALNGEATGSSSRIARAL-LLDEPPSIDKGEITDKGYINQRAVLERRAALVERLY 557
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
119-615 |
1.43e-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: 116.49 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 119 QWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELA------CYtysmvvVPLyDTLGPGA-IRYIIN 191
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALGVGP--GDLVGVCLERSLEMVVALLAvlkagaAY------VPL-DPAYPAErLAYMLE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 192 TADISTVIVDkpqkavlllehverketpglkliilmdpfeEALKERGQKCGVVIKSMQAVEDCGQENHHAPVPPQPDDLS 271
Cdd:COG1020 571 DAGARLVLTQ------------------------------SALAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLA 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 272 IVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTEkvifprQDDVL----ISF--------LPLahmferviqsvvyC 336
Cdd:COG1020 621 YVIYTSGSTGRPKGVMVEHRALVnllAWMQRRYGLGP------GDRVLqfasLSFdasvweifGAL-------------L 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 337 HGGRVGFFQGDIRLLSDDMKALC----PTIFPVVPRLLNRMYDkifsqantplkrwllefAAKRKQAEVRsgiirndsiw 412
Cdd:COG1020 682 SGATLVLAPPEARRDPAALAELLarhrVTVLNLTPSLLRALLD-----------------AAPEALPSLR---------- 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 413 delffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF--TTPGDWTSGHV--GAPLPCNH 488
Cdd:COG1020 735 ----------------LVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYyeVTPPDADGGSVpiGRPIANTR 798
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 489 IKLVDvEELN---YWACkgeGEICVRGPNVFKGYLKDPDRTKEA-----LDSDG--WLHTGDIGKWLPAGTLKVIDRKKH 558
Cdd:COG1020 799 VYVLD-AHLQpvpVGVP---GELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNLEFLGRADD 874
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966948474 559 ifklaQ----------GEyvapekIENIyIRSQP-VAQIYV--HGDSL-KAFLVGIVVPDPEVMPSWAQKR 615
Cdd:COG1020 875 -----QvkirgfrielGE------IEAA-LLQHPgVREAVVvaREDAPgDKRLVAYVVPEAGAAAAAALLR 933
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
119-606 |
2.80e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 113.03 E-value: 2.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 119 QWLSYQEVADRAEFLgSGLLQHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTV 198
Cdd:PRK06839 26 EEMTYKQLHEYVSKV-AAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 199 IVDKP-QKAVLLLEHVERKETPglkliilmdpfeealkergqkcgVVIKSMQAVEDCGQENHhapVPPQPDDLSIVCFTS 277
Cdd:PRK06839 105 FVEKTfQNMALSMQKVSYVQRV-----------------------ISITSLKEIEDRKIDNF---VEKNESASFIICYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 278 GTTGNPKGAMLTHGNVvadfsgFLKVTEKV--IFPRQDDVLISFLPLAHMferviqsvvychgGRVGFFQgdirllsddm 355
Cdd:PRK06839 159 GTTGKPKGAVLTQENM------FWNALNNTfaIDLTMHDRSIVLLPLFHI-------------GGIGLFA---------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 356 kalCPTIFP----VVPRLLNRmyDKIFSQANTplKRWLLEFAAKRKQAEVRSGIIRNDSIWDElffnkiqaslggcVRMI 431
Cdd:PRK06839 210 ---FPTLFAggviIVPRKFEP--TKALSMIEK--HKVTVVMGVPTIHQALINCSKFETTNLQS-------------VRWF 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 432 VTGAAPAS-PTVLGFLRAalGCQVYEGYGQTEcTAGCTFTTPGD---WTSGHVGAPLPCNHIKLVDvEELNYWACKGEGE 507
Cdd:PRK06839 270 YNGGAPCPeELMREFIDR--GFLFGQGFGMTE-TSPTVFMLSEEdarRKVGSIGKPVLFCDYELID-ENKNKVEVGEVGE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 508 ICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIyirsqpvaqIY 587
Cdd:PRK06839 346 LLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQV---------IN 414
|
490
....*....|....*....
gi 966948474 588 VHGDSLKAFLVGivVPDPE 606
Cdd:PRK06839 415 KLSDVYEVAVVG--RQHVK 431
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
260-610 |
3.28e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 112.78 E-value: 3.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 260 HAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifprQDDVLISFLPLAHMFE---------RVI 330
Cdd:PRK07787 120 HRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWT----ADDVLVHGLPLFHVHGlvlgvlgplRIG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 331 QSVVycHGGRvgfF--QGDIRLLSDDmkalcPTIFPVVPRllnrMYDKIfsqantplkrwllefAAKRKQAEVRSGiirn 408
Cdd:PRK07787 196 NRFV--HTGR---PtpEAYAQALSEG-----GTLYFGVPT----VWSRI---------------AADPEAARALRG---- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 409 dsiwdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNH 488
Cdd:PRK07787 243 -------------------ARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 489 IKLVDvEELNYWACKGE--GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDR------KKHIF 560
Cdd:PRK07787 304 TRLVD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGGY 382
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 966948474 561 KLAQGEyvapekIENIYIRSQPVAQIYVHG---DSLKAFLVGIVVPDPEVMPS 610
Cdd:PRK07787 383 RIGAGE------IETALLGHPGVREAAVVGvpdDDLGQRIVAYVVGADDVAAD 429
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
112-569 |
6.01e-26 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 113.05 E-value: 6.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 112 RKPNQPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPL---YDTLG--PGAI 186
Cdd:PRK08180 61 RGADGGWRRLTYAEALERVRAIAQALLDRGLSA--ERPLMILSGNSIEHALLALAAMYAGVPYAPVspaYSLVSqdFGKL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 187 RYIINTADISTVIVDKPQK-----AVLLLEHVE----RKETPGLKLIilmdPFEEALKERGQKcgvviksmqAVEDcgqe 257
Cdd:PRK08180 139 RHVLELLTPGLVFADDGAAfaralAAVVPADVEvvavRGAVPGRAAT----PFAALLATPPTA---------AVDA---- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 258 nHHAPVppQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekVIFPRQDD-VLISFLPLAHMF-ERVIQSVVY 335
Cdd:PRK08180 202 -AHAAV--GPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQT---FPFLAEEPpVLVDWLPWNHTFgGNHNLGIVL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 336 CHGGR---------VGFFQGDIRLLsddmKALCPTIFPVVPRLlnrmydkifsqantplkrWLLEFAAKRKQAEVRsgii 406
Cdd:PRK08180 276 YNGGTlyiddgkptPGGFDETLRNL----REISPTVYFNVPKG------------------WEMLVPALERDAALR---- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 407 rndsiwdELFFNKiqaslggcVRMIVTGAAPASPTVLGFL----RAALGCQVY--EGYGQTECTAGCTFTTPGDWTSGHV 480
Cdd:PRK08180 330 -------RRFFSR--------LKLLFYAGAALSQDVWDRLdrvaEATCGERIRmmTGLGMTETAPSATFTTGPLSRAGNI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 481 GAPLPCNHIKLVDVEelnywackGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWL----PAGTLKVIDRK 556
Cdd:PRK08180 395 GLPAPGCEVKLVPVG--------GKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVdpadPERGLMFDGRI 466
|
490
....*....|...
gi 966948474 557 KHIFKLAQGEYVA 569
Cdd:PRK08180 467 AEDFKLSSGTWVS 479
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
162-574 |
1.20e-25 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 113.48 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 162 IAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKpqkavlllEHVERKETPGLKLIILMDP---FEEALKER- 237
Cdd:PRK08633 680 LANLALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVITSR--------KFLEKLKNKGFDLELPENVkviYLEDLKAKi 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 238 --GQKC--GVVIKSMQAVEDCGQENHhapvPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgfLKVTEKVIFPRQD 313
Cdd:PRK08633 752 skVDKLtaLLAARLLPARLLKRLYGP----TFKPDDTATIIFSSGSEGEPKGVMLSHHNILSN----IEQISDVFNLRND 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 314 DVLISFLPLAHMFERVIQ---------SVVYcH-----GGRVGffqgdirLLSDDMKA--LC--PTIFpvvprllnRMYd 375
Cdd:PRK08633 824 DVILSSLPFFHSFGLTVTlwlpllegiKVVY-HpdptdALGIA-------KLVAKHRAtiLLgtPTFL--------RLY- 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 376 kifsqantplkrwllefaakrkqaevrsgiIRNDSIWDELFfnkiqASLggcvRMIVTGAAPASPTVLGFLRAALGCQVY 455
Cdd:PRK08633 887 ------------------------------LRNKKLHPLMF-----ASL----RLVVAGAEKLKPEVADAFEEKFGIRIL 927
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 456 EGYGQTECTAGCTFTTP-----GDWT-----SGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDR 525
Cdd:PRK08633 928 EGYGATETSPVASVNLPdvlaaDFKRqtgskEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEK 1007
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 966948474 526 TKEAL---DSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIE 574
Cdd:PRK08633 1008 TAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIG-GEMVPLGAVE 1058
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
156-598 |
1.21e-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: 110.12 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 156 NRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKpqkavlllehverketpglkliilmdpfeealk 235
Cdd:cd05972 34 RVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA--------------------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 236 ergqkcgvviksmqavedcgqenhhapvppqpDDLSIVCFTSGTTGNPKGAMLTHG---NVVADFSGFLKVTEKVIFPRQ 312
Cdd:cd05972 81 --------------------------------EDPALIYFTSGTTGLPKGVLHTHSyplGHIPTAAYWLGLRPDDIHWNI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 313 DD------VLISFL-PLAHMFerviqSVVYCHGGRVgffqgdirllsDDMKALcptifpvvpRLLNRMYDKIFSQANTPL 385
Cdd:cd05972 129 ADpgwakgAWSSFFgPWLLGA-----TVFVYEGPRF-----------DAERIL---------ELLERYGVTSFCGPPTAY 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 386 KRWLLEFAAKRKQAEVRSgiirndsiwdelffnkiqaslggcvrmIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTA 465
Cdd:cd05972 184 RMLIKQDLSSYKFSHLRL---------------------------VVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGL 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 466 GCTFTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNV--FKGYLKDPDRTKEALdSDGWLHTGDIGK 543
Cdd:cd05972 237 TVGNFPDMPVKPGSMGRPTPGYDVAIID-DDGRELPPGEEGDIAIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDRAY 314
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966948474 544 WLPAGTLKVIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLV 598
Cdd:cd05972 315 RDEDGYFWFVGRADDIIK-SSGYRIGPFEVESALLEHPAVAEAAVvgspdpvRGEVVKAFVV 375
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
261-613 |
1.26e-25 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 111.86 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 261 APVPPQpDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKV-TEKVIFPRQDDVLISFLPLAHMFerviqsvvychgG 339
Cdd:PLN02574 192 KPVIKQ-DDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFeASQYEYPGSDNVYLAALPMFHIY------------G 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 340 RVGFFQGDIRL-----------LSDDMKAL---CPTIFPVVPRLLNRMYDKIFSQANTPLKrwllefaakrkqaevrsgi 405
Cdd:PLN02574 259 LSLFVVGLLSLgstivvmrrfdASDMVKVIdrfKVTHFPVVPPILMALTKKAKGVCGEVLK------------------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 406 irndsiwdelffnkiqaslggCVRMIVTGAAPAS-PTVLGFLRAALGCQVYEGYGQTECTAGCT--FTTPGDWTSGHVGA 482
Cdd:PLN02574 320 ---------------------SLKQVSCGAAPLSgKFIQDFVQTLPHVDFIQGYGMTESTAVGTrgFNTEKLSKYSSVGL 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 483 PLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKL 562
Cdd:PLN02574 379 LAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY 458
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 966948474 563 aQGEYVAPEKIENIYIrSQP----VAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQ 613
Cdd:PLN02574 459 -KGFQIAPADLEAVLI-SHPeiidAAVTAVPDKECGEIPVAFVVRRQGSTLSQEA 511
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
121-590 |
2.06e-25 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 110.44 E-value: 2.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLAALGVK--KGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLIT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 201 DkpqkavlllehverketpglkliilmDPFEEALKERGQkcgVVIKSMQAvedcGQENHHAPVPPQP-DDLSIVCFTSGT 279
Cdd:PRK03640 106 D--------------------------DDFEAKLIPGIS---VKFAELMN----GPKEEAEIQEEFDlDEVATIMYTSGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 280 TGNPKGAMLTHGNVVADFSGF---LKVTEKvifprqDDVLISfLPLAHM--FERVIQSVVYchGGRV----GFFQGDI-R 349
Cdd:PRK03640 153 TGKPKGVIQTYGNHWWSAVGSalnLGLTED------DCWLAA-VPIFHIsgLSILMRSVIY--GMRVvlveKFDAEKInK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 350 LLSDDMKalcpTIFPVVPRLLNRMYDKIfSQANTPlkrwllefaakrkqaevrsgiirnDSiwdelffnkiqaslggcVR 429
Cdd:PRK03640 224 LLQTGGV----TIISVVSTMLQRLLERL-GEGTYP------------------------SS-----------------FR 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 430 MIVTGAAPASPTVLGFLRAAlGCQVYEGYGQTEcTAGCTFTTPGDWTS---GHVGAPL-PCNhIKLVDveELNYWACKGE 505
Cdd:PRK03640 258 CMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLfPCE-LKIEK--DGVVVPPFEE 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 506 GEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQ 585
Cdd:PRK03640 333 GEIVVKGPNVTKGYLNREDATRETFQ-DGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPGVAE 410
|
....*
gi 966948474 586 IYVHG 590
Cdd:PRK03640 411 AGVVG 415
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
156-598 |
6.31e-25 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 109.39 E-value: 6.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 156 NRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDkpQKAVLLLEHVERKETPGLKLIILMDPFEEALK 235
Cdd:PRK08008 71 NCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTS--AQFYPMYRQIQQEDATPLRHICLTRVALPADD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 236 ergqkcGVV----IKSMQAVEDCgqenhHAPvPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVTEKVIfpR 311
Cdd:PRK08008 149 ------GVSsftqLKAQQPATLC-----YAP-PLSTDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYYSAWQCAL--R 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 312 QDDVLISFLPLAHMFerviqsvvychggrvgfFQgdirllsddmkalCPTIFPVvprllnrmydkiFSQANTPLkrwLLE 391
Cdd:PRK08008 213 DDDVYLTVMPAFHID-----------------CQ-------------CTAAMAA------------FSAGATFV---LLE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 392 -FAAKRKQAEVRsgiirndsiwdelffnKIQASLGGCVRMIVTG--AAPASPT--------VLGFLRAA----------L 450
Cdd:PRK08008 248 kYSARAFWGQVC----------------KYRATITECIPMMIRTlmVQPPSANdrqhclreVMFYLNLSdqekdafeerF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 451 GCQVYEGYGQTECTAGCTFTTPGD---WTSghVGAPLPCNHIKLVDveELNYWACKGE-GEICVRG---PNVFKGYLKDP 523
Cdd:PRK08008 312 GVRLLTSYGMTETIVGIIGDRPGDkrrWPS--IGRPGFCYEAEIRD--DHNRPLPAGEiGEICIKGvpgKTIFKEYYLDP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 524 DRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIyIRSQP-VAQIYVHG--DSL-----KA 595
Cdd:PRK08008 388 KATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVELENI-IATHPkIQDIVVVGikDSIrdeaiKA 465
|
...
gi 966948474 596 FLV 598
Cdd:PRK08008 466 FVV 468
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
264-604 |
7.32e-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: 108.17 E-value: 7.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 264 PPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPLAhmFERVIQSV--VYCHGGRV 341
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLN----YVSQPPARLDVGPGSRVAQVLSIA--FDACIGEIfsTLCNGGTL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 342 gFFQGDIRLLSDDMKALcpTIFPVVPRLLNRMYDKIFSQantplkrwllefaakrkqaevrsgiirndsiwdelffnkiq 421
Cdd:cd17653 175 -VLADPSDPFAHVARTV--DALMSTPSILSTLSPQDFPN----------------------------------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 422 aslggcVRMIVTGAAPASPTVLGflRAALGCQVYEGYGQTECTAGCTFT--TPGDWTsgHVGAPLPCNHIKLVDvEELNY 499
Cdd:cd17653 211 ------LKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTelLPGQPV--TIGKPIPNSTCYILD-ADLQP 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 500 WACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH------TGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKI 573
Cdd:cd17653 280 VPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPgsrmyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEI 358
|
330 340 350
....*....|....*....|....*....|....
gi 966948474 574 ENIYIRSQPVAQ---IYVHGDSLKAFlvgiVVPD 604
Cdd:cd17653 359 EEVVLQSQPEVTqaaAIVVNGRLVAF----VTPE 388
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
156-576 |
1.05e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 108.71 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 156 NRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADiSTVIVDKPQKAVLLLEhvERKETPGLKLIILMDP------ 229
Cdd:PRK07786 76 NRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCG-AHVVVTEAALAPVATA--VRDIVPLLSTVVVAGGssddsv 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 230 --FEEALKERGQKcgvviksmqavedcgqenhHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkv 307
Cdd:PRK07786 153 lgYEDLLAEAGPA-------------------HAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNG-- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 308 iFPRQDDVLISFLPLAHMfeRVIQSVVychggrVGFFQGdirllsddmkalCPT-IFPVVPRLLNRMYDkifsqantplk 386
Cdd:PRK07786 212 -ADINSDVGFVGVPLFHI--AGIGSML------PGLLLG------------APTvIYPLGAFDPGQLLD----------- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 387 rwLLEfaakrkqAEVRSGIIRNDSIWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTA 465
Cdd:PRK07786 260 --VLE-------AEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEMSP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 466 gCTFTTPGD---WTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSdGWLHTGDIG 542
Cdd:PRK07786 331 -VTCMLLGEdaiRKLGSVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLV 407
|
410 420 430
....*....|....*....|....*....|....
gi 966948474 543 KWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENI 576
Cdd:PRK07786 408 RQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENV 440
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
220-574 |
1.16e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 108.54 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 220 GLKLIILMDPFEEA---LKERGQKcgvviksMQAVEDCGQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD 296
Cdd:PRK07768 108 GAKAVVVGEPFLAAapvLEEKGIR-------VLTVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYAN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 297 FSGflkVTEKVIFPRQDDVLISFLPLAH-MferviqsvvychgGRVGFfqgdirlLSDDMKALC------PTIFPVVPRL 369
Cdd:PRK07768 181 AEA---MFVAAEFDVETDVMVSWLPLFHdM-------------GMVGF-------LTVPMYFGAelvkvtPMDFLRDPLL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 370 LNRMYDKiFSQANTPLKRWLLEFAAKR--KQAEvrsgiirnDSIWDElffnkiqaslgGCVRMIVTGAAPASPTVL---- 443
Cdd:PRK07768 238 WAELISK-YRGTMTAAPNFAYALLARRlrRQAK--------PGAFDL-----------SSLRFALNGAEPIDPADVedll 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 444 ------GFLRAALGCqvyeGYGQTECTAGCTFTTPGD--------------------WTSGHV------GAPLPCNHIKL 491
Cdd:PRK07768 298 dagarfGLRPEAILP----AYGMAEATLAVSFSPCGAglvvdevdadllaalrravpATKGNTrrlatlGPPLPGLEVRV 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 492 VDvEELNYWACKGEGEICVRGPNVFKGYLkDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPE 571
Cdd:PRK07768 374 VD-EDGQVLPPRGVGVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPT 450
|
...
gi 966948474 572 KIE 574
Cdd:PRK07768 451 DIE 453
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
121-606 |
2.42e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 107.82 E-value: 2.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PRK06178 59 ITYAELDELSDRFAALLRQRGVGA-GDR-VAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 201 dkpQKAVL-LLEHVeRKETPgLKLII---LMD--------PFEEALKERGQKCGVVIKSMQAVEDCGQENhhAPVPPQPD 268
Cdd:PRK06178 137 ---LDQLApVVEQV-RAETS-LRHVIvtsLADvlpaeptlPLPDSLRAPRLAAAGAIDLLPALRACTAPV--PLPPPALD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 269 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifpRQDDVLISFLPlahMFerviqsvvYCHGGRVGFfqgdi 348
Cdd:PRK06178 210 ALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVG---GEDSVFLSFLP---EF--------WIAGENFGL----- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 349 rllsddmkalcptIFPvvprllnrmydkIFSQANTPL-KRW-LLEFAAKRKQAEVRSGIIRNDSIwDELF---------F 417
Cdd:PRK06178 271 -------------LFP------------LFSGATLVLlARWdAVAFMAAVERYRVTRTVMLVDNA-VELMdhprfaeydL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 418 NKIQASlgGCVRMIvtgaAPASPTVLGFLRAALGCQVYEG-YGQTECTAGCTFTTpGDWTSGH--------VGAPLPCNH 488
Cdd:PRK06178 325 SSLRQV--RVVSFV----KKLNPDYRQRWRALTGSVLAEAaWGMTETHTCDTFTA-GFQDDDFdllsqpvfVGLPVPGTE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 489 IKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYV 568
Cdd:PRK06178 398 FKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV-NGMSV 475
|
490 500 510
....*....|....*....|....*....|....*...
gi 966948474 569 APEKIENIYIRsqpvaqiyvHGDSLKAFLVGivVPDPE 606
Cdd:PRK06178 476 FPSEVEALLGQ---------HPAVLGSAVVG--RPDPD 502
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
121-608 |
6.45e-24 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 106.43 E-value: 6.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIAELACYTYSMVVV---PLYDTlgpGAIRYIINTADIST 197
Cdd:PRK08315 44 WTYREFNEEVDALAKGLLALGIEK-GDR-VGIWAPNVPEWVLTQFATAKIGAILVtinPAYRL---SELEYALNQSGCKA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 198 -VIVDK--------------PQKAVLLLEHVERKETPGLKLIILMDpfeeALKERGqkcgvvIKSMQAVEDCGQENHHAP 262
Cdd:PRK08315 119 lIAADGfkdsdyvamlyelaPELATCEPGQLQSARLPELRRVIFLG----DEKHPG------MLNFDELLALGRAVDDAE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 263 VPP-----QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsGFLkVTEKVIFPRQDDVLISfLPLAHMFERVIqSVVYC- 336
Cdd:PRK08315 189 LAArqatlDPDDPINIQYTSGTTGFPKGATLTHRNILNN--GYF-IGEAMKLTEEDRLCIP-VPLYHCFGMVL-GNLACv 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 337 -HGGRV-----GFfqgdirllsDDMKAL-------C------PTIFPVV---PRLlnRMYDkiFSQantplkrwllefaa 394
Cdd:PRK08315 264 tHGATMvypgeGF---------DPLATLaaveeerCtalygvPTMFIAEldhPDF--ARFD--LSS-------------- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 395 krkqaeVRSGIirndsiwdelffnkiqaslggcvrMivtgAAPASPT-----VLGFLRAAlgcQVYEGYGQTECTAGCTF 469
Cdd:PRK08315 317 ------LRTGI------------------------M----AGSPCPIevmkrVIDKMHMS---EVTIAYGMTETSPVSTQ 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 470 TTPGD------WTsghVGAPLPCNHIKLVDVEelnywacKGE-------GEICVRGPNVFKGYLKDPDRTKEALDSDGWL 536
Cdd:PRK08315 360 TRTDDplekrvTT---VGRALPHLEVKIVDPE-------TGEtvprgeqGELCTRGYSVMKGYWNDPEKTAEAIDADGWM 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 537 HTGDIGkwlpagtlkVIDrkkhifklAQGeYVapeKI------------ENIYIRsqpvaQI----YVHGDSLKAFLVGi 600
Cdd:PRK08315 430 HTGDLA---------VMD--------EEG-YV---NIvgrikdmiirggENIYPR-----EIeeflYTHPKIQDVQVVG- 482
|
570
....*....|..
gi 966948474 601 vVPDP----EVM 608
Cdd:PRK08315 483 -VPDEkygeEVC 493
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
263-598 |
1.05e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 105.89 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 263 VPPQPD-DLSIVCFTSGTTGNPKGAMLTHGNVVADfsGFLKVTEKVIFPRQDDVLISFLPLAHMF-ERVIQSVVYCHGGR 340
Cdd:PRK06710 200 VPCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSN--TLMGVQWLYNCKEGEEVVLGVLPFFHVYgMTAVMNLSIMQGYK 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 341 VGFF-QGDIRLLSDDMKALCPTIFPVVPRLLnrmydkiFSQANTPLkrwllefaakRKQAEVRSgiirndsiwdelffnk 419
Cdd:PRK06710 278 MVLIpKFDMKMVFEAIKKHKVTLFPGAPTIY-------IALLNSPL----------LKEYDISS---------------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 420 iqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgctfTTPGDW-----TSGHVGAPLPCNHIKLVDV 494
Cdd:PRK06710 325 --------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSP----VTHSNFlwekrVPGSIGVPWPDTEAMIMSL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 495 EELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIE 574
Cdd:PRK06710 393 ETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREVE 470
|
330 340 350
....*....|....*....|....*....|.
gi 966948474 575 NIYIRSQPVAQIYV-------HGDSLKAFLV 598
Cdd:PRK06710 471 EVLYEHEKVQEVVTigvpdpyRGETVKAFVV 501
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
265-605 |
1.18e-23 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 105.52 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 265 PQPDDLSIVCFTSGTTGNPKGAMLTHGNVvadFSGFLKVTEKVIFpRQDDVLISFLPLAHMferviqsvvychggrVGFF 344
Cdd:PRK13295 194 PGPDDVTQLIYTSGTTGEPKGVMHTANTL---MANIVPYAERLGL-GADDVILMASPMAHQ---------------TGFM 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 345 QGDIRLLSDDMKALCPTIFPVVprllnRMYDKI------FSQANTPlkrWLLEFAakRKQAEVRSGIirndsiwdelffn 418
Cdd:PRK13295 255 YGLMMPVMLGATAVLQDIWDPA-----RAAELIrtegvtFTMASTP---FLTDLT--RAVKESGRPV------------- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 419 kiqASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPGD---WTSGHVGAPLPCNHIKLVDvE 495
Cdd:PRK13295 312 ---SSL----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA-VTLTKLDDpdeRASTTDGCPLPGVEVRVVD-A 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 496 ELNYWACKGEGEICVRGPNVFKGYLKDPDRTkeALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIEN 575
Cdd:PRK13295 383 DGAPLPAGQIGRLQVRGCSNFGGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEA 459
|
330 340 350
....*....|....*....|....*....|.
gi 966948474 576 IYIRSQPVAQiyvhgdslkaflVGIV-VPDP 605
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 ... |
122-605 |
1.18e-23 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 105.41 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 122 SYQEVADRAEFLGSGLlqHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVD 201
Cdd:cd12119 27 TYAEVAERARRLANAL--RRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 202 K---PQKAVLL--LEHVERketpglklIILMDPFEEALKERGQKcgvVIKSMQAVEDcgqenhHAPVPPQPD----DLSI 272
Cdd:cd12119 105 RdflPLLEAIAprLPTVEH--------VVVMTDDAAMPEPAGVG---VLAYEELLAA------ESPEYDWPDfdenTAAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 273 VCFTSGTTGNPKGAMLTHgnvvadfsgflkvtekvifpRQddvlisflplahmfeRVIQSVVYCHGGRVGFFQGDirlls 352
Cdd:cd12119 168 ICYTSGTTGNPKGVVYSH--------------------RS---------------LVLHAMAALLTDGLGLSESD----- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 353 ddmkalcpTIFPVVPrllnrMYdkifsQANTplkrWLLEFAA-----------KRKQAEVRSGIIRND---------SIW 412
Cdd:cd12119 208 --------VVLPVVP-----MF-----HVNA----WGLPYAAamvgaklvlpgPYLDPASLAELIEREgvtfaagvpTVW 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 413 DELF--FNKIQASLGGCVRMIVTGAAPASPTVLGFlrAALGCQVYEGYGQTECTAGCTFTTPgdwTSGHV---------- 480
Cdd:cd12119 266 QGLLdhLEANGRDLSSLRRVVIGGSAVPRSLIEAF--EERGVRVIHAWGMTETSPLGTVARP---PSEHSnlsedeqlal 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 481 ----GAPLPCNHIKLVDVE--ELNyWACKGEGEICVRGPNVFKGYLKDPDRTkEALDSDGWLHTGDIGKWLPAGTLKVID 554
Cdd:cd12119 341 rakqGRPVPGVELRIVDDDgrELP-WDGKAVGELQVRGPWVTKSYYKNDEES-EALTEDGWLRTGDVATIDEDGYLTITD 418
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 966948474 555 RKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVhgdslkaflvgIVVPDP 605
Cdd:cd12119 419 RSKDVIKSG-GEWISSVELENAIMAHPAVAEAAV-----------IGVPHP 457
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
266-606 |
4.91e-23 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 103.01 E-value: 4.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 266 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkviFPRQDDVL----ISF-LPLAHMFerviqsVVYCHGG- 339
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALG---LTSESRVLqfasYTFdVSILEIF------TTLAAGGc 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 340 --------RVGFFQGDIRllsdDMKALCPTIFPVVPRLLNRmydkifsqANTPlkrwllefaakrkqaevrsgiirndsi 411
Cdd:cd05918 175 lcipseedRLNDLAGFIN----RLRVTWAFLTPSVARLLDP--------EDVP--------------------------- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 412 wdelffnkiqaslggCVRMIVTGAAPASPTVLGflRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPC---- 486
Cdd:cd05918 216 ---------------SLRTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRPLGAtcwv 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 487 ----NHIKLVDVeelnywackGE-GEICVRGPNVFKGYLKDPDRTKEA-LDSDGWLH------------TGDIGKWLPAG 548
Cdd:cd05918 279 vdpdNHDRLVPI---------GAvGELLIEGPILARGYLNDPEKTAAAfIEDPAWLKqegsgrgrrlyrTGDLVRYNPDG 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966948474 549 TLKVIDRKKHIFKLaQGEYVAPEKIENiYIRSQP------VAQIYVH-GDSLKAFLVGIVVPDPE 606
Cdd:cd05918 350 SLEYVGRKDTQVKI-RGQRVELGEIEH-HLRQSLpgakevVVEVVKPkDGSSSPQLVAFVVLDGS 412
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
121-607 |
4.98e-23 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 102.71 E-value: 4.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGA-IRYIINTADISTVI 199
Cdd:cd05945 17 LTYRELKERADALAAALASLGLDA--GDPVVVYGHKSPDAIAAFLAALKAGHAYVPL-DASSPAErIREILDAAKPALLI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 200 VDkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhhapvppqPDDLSIVCFTSGT 279
Cdd:cd05945 94 AD-----------------------------------------------------------------GDDNAYIIFTSGS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 280 TGNPKGAMLTHGNVVAdFS----GFLKVTEkvifprqDDVLISFLPLAhmFERVIQSVVYC--HGGrvgffqgdirllsd 353
Cdd:cd05945 109 TGRPKGVQISHDNLVS-FTnwmlSDFPLGP-------GDVFLNQAPFS--FDLSVMDLYPAlaSGA-------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 354 dmkalcpTIFPVvPRLLNRMYDKIFSQ-ANTPLKRWLlefaakrkqaevrsgiiRNDSIWDELF----FNkiQASLGGCV 428
Cdd:cd05945 165 -------TLVPV-PRDATADPKQLFRFlAEHGITVWV-----------------STPSFAAMCLlsptFT--PESLPSLR 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 429 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFT--TP---GDWTSGHVGAPLPCNHIKLVDvEELNYWACK 503
Cdd:cd05945 218 HFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIevTPevlDGYDRLPIGYAKPGAKLVILD-EDGRPVPPG 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 504 GEGEICVRGPNVFKGYLKDPDRTKEALDSD---GWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRS 580
Cdd:cd05945 297 EKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIELEEIEAALRQV 375
|
490 500 510
....*....|....*....|....*....|.
gi 966948474 581 QPVAQIYV----HGDSlKAFLVGIVVPDPEV 607
Cdd:cd05945 376 PGVKEAVVvpkyKGEK-VTELIAFVVPKPGA 405
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
111-615 |
6.58e-23 |
|
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: 102.79 E-value: 6.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 111 FRKPNQPY-----QWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGA 185
Cdd:cd17655 8 EKTPDHTAvvfedQTLTYRELNERANQLARTLREKGVGP--DTIVGIMAERSLEMIVGILGILKAGGAYLPI-DPDYPEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 186 -IRYIINTADISTVIVDKPQKAVLLlehverketpGLKLIILMDpfEEALKERGQkcgvviksmqavedcgqENHHAPVp 264
Cdd:cd17655 85 rIQYILEDSGADILLTQSHLQPPIA----------FIGLIDLLD--EDTIYHEES-----------------ENLEPVS- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 265 pQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkvtEKVIFPRQDDVLISFLPLAhmFERVIQSVvychggrvgfF 344
Cdd:cd17655 135 -KSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWA----NKVIYQGEHLRVALFASIS--FDASVTEI----------F 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 345 QGdirLLSDDmkALCptIFPVVPRLLNRMYDKIFSQAN------TPLKRWLLEFAakrkqaevrsgiirndsiwDELFFN 418
Cdd:cd17655 198 AS---LLSGN--TLY--IVRKETVLDGQALTQYIRQNRitiidlTPAHLKLLDAA-------------------DDSEGL 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 419 KIQaslggcvRMIVTGAAPASPTVLGFL-RAALGCQVYEGYGQTECTAGCTF--TTPGDWTSGHV--GAPLPCNHIKLVD 493
Cdd:cd17655 252 SLK-------HLIVGGEALSTELAKKIIeLFGTNPTITNAYGPTETTVDASIyqYEPETDQQVSVpiGKPLGNTRIYILD 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 494 vEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKVIDRKKHIFKLaQGEY 567
Cdd:cd17655 325 -QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-RGYR 402
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 966948474 568 VAPEKIENIYIRSQPVAQ---IYVHGDSLKAFLVGIVVPDPEVMPSWAQKR 615
Cdd:cd17655 403 IELGEIEARLLQHPDIKEavvIARKDEQGQNYLCAYIVSEKELPVAQLREF 453
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
269-606 |
1.05e-22 |
|
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: 99.65 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 269 DLSIVCFTSGTTGNPKGAMLTHGNVVA---DFSGFLKVTEkvifprqDDVLISFLPLAHMFERVIQSVVYCHGGR---VG 342
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAanlQLIHAMGLTE-------ADVYLNMLPLFHIAGLNLALATFHAGGAnvvME 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 343 FFQGDIRL-LSDDMKAlcpTIFPVVPRLLNRMYDkifsqantplkrwllefAAKRKQAEVRSgiIRNdsiwdelffnkiq 421
Cdd:cd17637 74 KFDPAEALeLIEEEKV---TLMGSFPPILSNLLD-----------------AAEKSGVDLSS--LRH------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 422 aslggcvrmiVTGAApaSPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDveELNYWA 501
Cdd:cd17637 119 ----------VLGLD--APETIQRFEETTGATFWSLYGQTE-TSGLVTLSPYRERPGSAGRPGPLVRVRIVD--DNDRPV 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 502 CKGE-GEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKVIDRK--KHIFKlAQGEYVAPEKIENIyI 578
Cdd:cd17637 184 PAGEtGEIVVRGPLVFQGYWNLPELTAYTFR-NGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKV-I 260
|
330 340
....*....|....*....|....*....
gi 966948474 579 RSQP-VAQIYVHGdslkaflvgivVPDPE 606
Cdd:cd17637 261 LEHPaIAEVCVIG-----------VPDPK 278
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
121-605 |
2.08e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 101.55 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PRK08316 37 WTYAELDAAVNRVAAALLDLGLKK-GDR-VAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 201 DkpqkaVLLLEHVErketPGLKLIiLMDPFEEALKERGQkcgVVIKSMQAVEDC--GQENHHAPVPPQPDDLSIVCFTSG 278
Cdd:PRK08316 115 D-----PALAPTAE----AALALL-PVDTLILSLVLGGR---EAPGGWLDFADWaeAGSVAEPDVELADDDLAQILYTSG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 279 TTGNPKGAMLTHGNVVADFSGFLKVTEKvifpRQDDVLISFLPLAHmferviqsvvyCHggrvgffQGDIRLLSDDMKAL 358
Cdd:PRK08316 182 TESLPKGAMLTHRALIAEYVSCIVAGDM----SADDIPLHALPLYH-----------CA-------QLDVFLGPYLYVGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 359 CPTI--FPVVPRLLnrmyDKIFSQANTPLkrwlleFAAKrkqaevrsgiirndSIWDELF----FNKIQASlggCVRMIV 432
Cdd:PRK08316 240 TNVIldAPDPELIL----RTIEAERITSF------FAPP--------------TVWISLLrhpdFDTRDLS---SLRKGY 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 433 TGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFTTPGDwtsgHVGAP----LPCNHI--KLVDvEELNYWAcKGE 505
Cdd:PRK08316 293 YGASIMPVEVLKELRERLpGLRFYNCYGQTEIAPLATVLGPEE----HLRRPgsagRPVLNVetRVVD-DDGNDVA-PGE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 506 -GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIyirsqpva 584
Cdd:PRK08316 367 vGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEA-------- 436
|
490 500
....*....|....*....|.
gi 966948474 585 qIYVHGDSLKAFLVGivVPDP 605
Cdd:PRK08316 437 -LYTHPAVAEVAVIG--LPDP 454
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-615 |
7.24e-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: 97.94 E-value: 7.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgfLKVTEKVIFPRQDDVLISFLPLAHMFERVIQsvvychgGRVGFFQG 346
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYN----AWMLALNSLFDPDDVLLCGLPLFHVNGSVVT-------LLTPLASG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 347 DIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTPLkrwllefaAKRKQAEVRSGIirndsiwdelffnkiqaslgG 426
Cdd:cd05944 70 AHVVLAGPAGYRNPGLFDNFWKLVERYRITSLSTVPTVY--------AALLQVPVNADI--------------------S 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 427 CVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLV--DVEELNYWACK 503
Cdd:cd05944 122 SLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKvlDGVGRLLRDCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 504 GE--GEICVRGPNVFKGYLKDpDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQ 581
Cdd:cd05944 202 PDevGEICVAGPGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLRHP 279
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 966948474 582 PVAQIYVHG--DSLKAFL-VGIV--VPDPEVMP----SWAQKR 615
Cdd:cd05944 280 AVAFAGAVGqpDAHAGELpVAYVqlKPGAVVEEeellAWARDH 322
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
121-576 |
9.60e-22 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 100.81 E-value: 9.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGsGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PRK06814 659 LTYRKLLTGAFVLG-RKLKKNTPP--GENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 201 DKP--QKAVL--LLEHVERketpGLKLIILMDPFEE---ALKERGqkcgVVIKSMQAVEDCGqenhhapvpPQPDDLSIV 273
Cdd:PRK06814 736 SRAfiEKARLgpLIEALEF----GIRIIYLEDVRAQiglADKIKG----LLAGRFPLVYFCN---------RDPDDPAVI 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 274 CFTSGTTGNPKGAMLTHGNVVADFSgflKVTEKVIFPRQDDVLiSFLPLAHMFerviqsvvychggrvGFFQGDIRLLSD 353
Cdd:PRK06814 799 LFTSGSEGTPKGVVLSHRNLLANRA---QVAARIDFSPEDKVF-NALPVFHSF---------------GLTGGLVLPLLS 859
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 354 DMKAL---CPTIFPVVPRLLnrmYDK----IFSqANTPLkrwllefaakrkqaevrSGIIRNDSIWDelFFNkiqaslgg 426
Cdd:PRK06814 860 GVKVFlypSPLHYRIIPELI---YDTnatiLFG-TDTFL-----------------NGYARYAHPYD--FRS-------- 908
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 427 cVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNywacKGeG 506
Cdd:PRK06814 909 -LRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGID----EG-G 982
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966948474 507 EICVRGPNVFKGYLK-DPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENI 576
Cdd:PRK06814 983 RLFVRGPNVMLGYLRaENPGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAVEEL 1051
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
269-610 |
1.38e-21 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 96.25 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 269 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkVTEKVIFPRQDDVLISfLPLAHM--FERVIQSVVycHGGRVGFFQG 346
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAG---LHSRLGFGGGDSWLLS-LPLYHVggLAILVRSLL--AGAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 347 DiRLLSDDMKALCPTIFPVVPRLLNRMYDKifSQANTPLKRwllefaakrkqaevrsgiirndsiwdelffnkiqaslgg 426
Cdd:cd17630 75 N-QALAEDLAPPGVTHVSLVPTQLQRLLDS--GQGPAALKS--------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 427 cVRMIVTGAAPASPtvlGFLRAA--LGCQVYEGYGQTEcTAGCTFT-TPGDWTSGHVGAPLPCNHIKLVDveelnywack 503
Cdd:cd17630 113 -LRAVLLGGAPIPP---ELLERAadRGIPLYTTYGMTE-TASQVATkRPDGFGRGGVGVLLPGRELRIVE---------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 504 gEGEICVRGPNVFKGYLKDPdrTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIyIRSQP- 582
Cdd:cd17630 178 -DGEIWVGGASLAMGYLRGQ--LVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAA-LAAHPa 252
|
330 340 350
....*....|....*....|....*....|.
gi 966948474 583 VAQIYVHG---DSLKAFLVGIVVPDPEVMPS 610
Cdd:cd17630 253 VRDAFVVGvpdEELGQRPVAVIVGRGPADPA 283
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
150-618 |
6.41e-21 |
|
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: 95.96 E-value: 6.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 150 IGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDkpqkavlllehverketpglkliilmdp 229
Cdd:cd05971 34 VGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTD---------------------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 230 feealkergqkcgvviksmqavedcgqenhhapvppQPDDLSIVCFTSGTTGNPKGAMLTH----GNVVADFSGFlkvte 305
Cdd:cd05971 86 ------------------------------------GSDDPALIIYTSGTTGPPKGALHAHrvllGHLPGVQFPF----- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 306 kVIFPRQDDVLIS-------------FLP--------LAHMFERviqsvvychggrvgfFQGD--IRLLSD---DMKALC 359
Cdd:cd05971 125 -NLFPRDGDLYWTpadwawigglldvLLPslyfgvpvLAHRMTK---------------FDPKaaLDLMSRygvTTAFLP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 360 PTIFpvvprllnrmydKIFSQANTPLKRWLLEfaakrkqaevrsgiirndsiwdelffnkiqaslggcVRMIVTGAAPAS 439
Cdd:cd05971 189 PTAL------------KMMRQQGEQLKHAQVK------------------------------------LRAIATGGESLG 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 440 PTVLGFLRAALGCQVYEGYGQTEC---TAGCTFTTPGDwtSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPN-- 514
Cdd:cd05971 221 EELLGWAREQFGVEVNEFYGQTECnlvIGNCSALFPIK--PGSMGKPIPGHRVAIVD-DNGTPLPPGEVGEIAVELPDpv 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 515 VFKGYLKDPDRTKEALDSDgWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYV------ 588
Cdd:cd05971 298 AFLGYWNNPSATEKKMAGD-WLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAEIEECLLKHPAVLMAAVvgipdp 375
|
490 500 510
....*....|....*....|....*....|.
gi 966948474 589 -HGDSLKAFlvgiVVPDPEVMPSWAQKRGIE 618
Cdd:cd05971 376 iRGEIVKAF----VVLNPGETPSDALAREIQ 402
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
150-610 |
7.27e-21 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 96.88 E-value: 7.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 150 IGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKpqkavlLLEHVERKET-PGLKLIILMD 228
Cdd:PRK05852 71 VALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDA------DGPHDRAEPTtRWWPLTVNVG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 229 PfeealkERGQKCGVVIKSMqaveDCGQENHHAPVPPQ---PDDLSIVcFTSGTTGNPKGAMLTHGNVVADFSGFlkVTE 305
Cdd:PRK05852 145 G------DSGPSGGTLSVHL----DAATEPTPATSTPEglrPDDAMIM-FTGGTTGLPKMVPWTHANIASSVRAI--ITG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 306 KVIFPRqdDVLISFLPLAH---MFERVIQSVVycHGGRV-----GFFQGdiRLLSDDMKALCPTIFPVVPrllnrmydki 377
Cdd:PRK05852 212 YRLSPR--DATVAVMPLYHghgLIAALLATLA--SGGAVllparGRFSA--HTFWDDIKAVGATWYTAVP---------- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 378 fsqantPLKRWLLEFAAKRKQAEVRSGIirndsiwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEG 457
Cdd:PRK05852 276 ------TIHQILLERAATEPSGRKPAAL-----------------------RFIRSCSAPLTAETAQALQTEFAAPVVCA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 458 YGQTECTAGCTfTTPGDWtSGHVGAPLPCN---------HIKLV--DVEELNYWACkgeGEICVRGPNVFKGYLKDPDRT 526
Cdd:PRK05852 327 FGMTEATHQVT-TTQIEG-IGQTENPVVSTglvgrstgaQIRIVgsDGLPLPAGAV---GEVWLRGTTVVRGYLGDPTIT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 527 KEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAF---LVGIVVP 603
Cdd:PRK05852 402 AANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLASHPNVMEAAVFGVPDQLYgeaVAAVIVP 479
|
....*..
gi 966948474 604 DPEVMPS 610
Cdd:PRK05852 480 RESAPPT 486
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
249-623 |
2.16e-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: 94.45 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 249 QAVEDCGQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHgnvvADFSGFLKVTEKVIFP-RQDDVLISflpLAHMFe 327
Cdd:cd05919 72 DDYAYIARDCEARLVVTSADDIAYLLYSSGTTGPPKGVMHAH----RDPLLFADAMAREALGlTPGDRVFS---SAKMF- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 328 rviqsVVYCHGGRVGF--FQGDIRLLSDD----------MKALCPTIFPVVPRllnrMYDKIFSQANTPlkrwllefaak 395
Cdd:cd05919 144 -----FGYGLGNSLWFplAVGASAVLNPGwptaervlatLARFRPTVLYGVPT----FYANLLDSCAGS----------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 396 rkQAEVRSgiIRndsiwdelffnkiqaslggcvrmIVTGAAPASPTVLG-FLRAALGCQVYEGYGQTEctAGCTFTT--P 472
Cdd:cd05919 204 --PDALRS--LR-----------------------LCVSAGEALPRGLGeRWMEHFGGPILDGIGATE--VGHIFLSnrP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 473 GDWTSGHVGAPLPCNHIKLVDveELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLK 551
Cdd:cd05919 255 GAWRLGSTGRPVPGYEIRLVD--EEGHTIPPGEeGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYT 331
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966948474 552 VIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYV----HGDSL---KAFlvgiVVPDPEVMPSWAQKRGIEGTYAD 623
Cdd:cd05919 332 HAGRADDMLKVG-GQWVSPVEVESLIIQHPAVAEAAVvavpESTGLsrlTAF----VVLKSPAAPQESLARDIHRHLLE 405
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
152-605 |
3.14e-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: 94.87 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 152 VFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKavlLLEHVE--RKETPGL-KLIILMD 228
Cdd:cd05970 77 LTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDN---IPEEIEkaAPECPSKpKLVWVGD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 229 PFEEALKERGQKCgvviksMQAVEDCgqENHHAPVPPQPDDLSIVCFTSGTTGNPKgaMLTHgnvvaDFSgflkvtekvi 308
Cdd:cd05970 154 PVPEGWIDFRKLI------KNASPDF--ERPTANSYPCGEDILLVYFSSGTTGMPK--MVEH-----DFT---------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 309 fprqddvlisfLPLAHmfervIQSVVYCHGGRvgffQGDIRLLSDDM---KALCPTIF-------PVVprllnrMYD-KI 377
Cdd:cd05970 209 -----------YPLGH-----IVTAKYWQNVR----EGGLHLTVADTgwgKAVWGKIYgqwiagaAVF------VYDyDK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 378 FSQANtplkrwLLEFAAKRKQAE------VRSGIIRND-SIWDelfFNKIqaslggcvRMIVTGAAPASPTVLGFLRAAL 450
Cdd:cd05970 263 FDPKA------LLEKLSKYGVTTfcapptIYRFLIREDlSRYD---LSSL--------RYCTTAGEALNPEVFNTFKEKT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 451 GCQVYEGYGQTECTAgCTFTTPG-DWTSGHVGAPLPCNHIKLVDVEELnywACKG--EGEICVRGPN-----VFKGYLKD 522
Cdd:cd05970 326 GIKLMEGFGQTETTL-TIATFPWmEPKPGSMGKPAPGYEIDLIDREGR---SCEAgeEGEIVIRTSKgkpvgLFGGYYKD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 523 PDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYVHGdslkaflvgivV 602
Cdd:cd05970 402 AEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVESALIQHPAVLECAVTG-----------V 468
|
...
gi 966948474 603 PDP 605
Cdd:cd05970 469 PDP 471
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
121-607 |
3.55e-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: 94.19 E-value: 3.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELA------CYtysmvvVPLYDTLGPGAIRYIINTAD 194
Cdd:cd12117 23 LTYAELNERANRLARRLRAAGVGP--GDVVGVLAERSPELVVALLAvlkagaAY------VPLDPELPAERLAFMLADAG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 195 ISTVIVDKPQKAVLLLehverketPGLKLIILMDPFEEALKErgqkcgvviksmqavedcgqenhhAPVPPQPDDLSIVC 274
Cdd:cd12117 95 AKVLLTDRSLAGRAGG--------LEVAVVIDEALDAGPAGN------------------------PAVPVSPDDLAYVM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 275 FTSGTTGNPKGAMLTHGNVV--ADFSGFLKVTEkvifprqDDVLISFLPL---AHMFErviqsvVY---CHGGRVgffqg 346
Cdd:cd12117 143 YTSGSTGRPKGVAVTHRGVVrlVKNTNYVTLGP-------DDRVLQTSPLafdASTFE------IWgalLNGARL----- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 347 dirllsddmkALCPTIFPVVPRLLnrmydkifsqantplkrwllefaakrkQAEVRSGIIrnDSIWdeL---FFNKI--- 420
Cdd:cd12117 205 ----------VLAPKGTLLDPDAL---------------------------GALIAEEGV--TVLW--LtaaLFNQLade 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 421 -QASLGGcVRMIVTGAAPASPT-VLGFLRAALGCQVYEGYGQTECTagcTFTT-----PGDWTSGHV--GAPLPCNHIKL 491
Cdd:cd12117 244 dPECFAG-LRELLTGGEVVSPPhVRRVLAACPGLRLVNGYGPTENT---TFTTshvvtELDEVAGSIpiGRPIANTRVYV 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 492 VDveELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKVIDRKKHIFKLaQ 564
Cdd:cd12117 320 LD--EDGRPVPPGVpGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI-R 396
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 966948474 565 GEYVAPEKIENIyIRSQP-VAQIYV---HGDSLKAFLVGIVVPDPEV 607
Cdd:cd12117 397 GFRIELGEIEAA-LRAHPgVREAVVvvrEDAGGDKRLVAYVVAEGAL 442
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
267-590 |
9.50e-20 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 93.32 E-value: 9.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfSGFLKVTekVIFPRQDDVLISFLPLAHMFErvIQSVVY------CHggr 340
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSALIV--QSLAKIA--IVGYGEDDVYLHTAPLCHIGG--LSSALAmlmvgaCH--- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 341 VGFFQGDIRLLSDDMKALCPTIFPVVPRLlnrMYDkifsqantplkrwLLEFAAKRKqaevrsgiirndsIWDElffnki 420
Cdd:PLN02860 242 VLLPKFDAKAALQAIKQHNVTSMITVPAM---MAD-------------LISLTRKSM-------------TWKV------ 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 421 qaslGGCVRMIVTGAAPASP-----TVLGFLRAALgcqvYEGYGQTECTAGCTFTTPGDWT-----------------SG 478
Cdd:PLN02860 287 ----FPSVRKILNGGGSLSSrllpdAKKLFPNAKL----FSAYGMTEACSSLTFMTLHDPTlespkqtlqtvnqtkssSV 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 479 H------VGAPLPcnHIKLvdveELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKV 552
Cdd:PLN02860 359 HqpqgvcVGKPAP--HVEL----KIGLDESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWL 432
|
330 340 350
....*....|....*....|....*....|....*...
gi 966948474 553 IDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYVHG 590
Cdd:PLN02860 433 IGRSNDRIK-TGGENVYPEEVEAVLSQHPGVASVVVVG 469
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
150-605 |
2.19e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 91.87 E-value: 2.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 150 IGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAVLLLEHverketpglKLIILMDP 229
Cdd:PRK06145 55 VALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDEEFDAIVALET---------PKIVIDAA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 230 FEEALKERGQKcgvviksmqavedcgqenhHAPVPPQ----PDDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLK 302
Cdd:PRK06145 126 AQADSRRLAQG-------------------GLEIPPQaavaPTDLVRLMYTSGTTDRPKGVMHSYGNLHwksIDHVIALG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 303 VTekvifprQDDVLISFLPLAHMFERVIQSV-VYCHGGRVGF---FQGDIRLLSDDMKALCPTIFpvVPRLLNRMYdkif 378
Cdd:PRK06145 187 LT-------ASERLLVVGPLYHVGAFDLPGIaVLWVGGTLRIhreFDPEAVLAAIERHRLTCAWM--APVMLSRVL---- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 379 sQANTPLK------RWLLefAAKRKQAEVRsgiIRNdsiwdelffnkiqaslggcvrmivtgaapasptvlgFLRAALGC 452
Cdd:PRK06145 254 -TVPDRDRfdldslAWCI--GGGEKTPESR---IRD------------------------------------FTRVFTRA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 453 QVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL 530
Cdd:PRK06145 292 RYIDAYGLTETCSGDTLMEAGREIEkiGSTGRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966948474 531 dSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIEN-IYIRSQ--PVAQIYVHGDSLKAFLVGIVVPDP 605
Cdd:PRK06145 371 -YGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERvIYELPEvaEAAVIGVHDDRWGERITAVVVLNP 446
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
121-609 |
5.55e-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: 5.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVR--PGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 201 DKPQkavlllehvERKETPGLKLIILMDPFEEALKERgqkcgvviksmqavedcgqenhhAPVPPQPDDLSIVCFTSGTT 280
Cdd:cd12114 91 DGPD---------AQLDVAVFDVLILDLDALAAPAPP-----------------------PPVDVAPDDLAYVIFTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 281 GNPKGAMLTHG---NVVADFSGFLKVTEkvifprqDDVLISFLPLAHMFerviqSV-----VYCHGGRVgffqgdirlls 352
Cdd:cd12114 139 GTPKGVMISHRaalNTILDINRRFAVGP-------DDRVLALSSLSFDL-----SVydifgALSAGATL----------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 353 ddmkalcptifpVVPRLlnrmydkifSQANTPlKRWllefaakrKQAEVRSGIirndSIWdelffNKIQASLGgcvrMIV 432
Cdd:cd12114 196 ------------VLPDE---------ARRRDP-AHW--------AELIERHGV----TLW-----NSVPALLE----MLL 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 433 TgAAPASPTVLGFLRAAL-------------------GCQVYEGYGQTECTAGCTF----TTPGDWTSGHVGAPLPCNHI 489
Cdd:cd12114 233 D-VLEAAQALLPSLRLVLlsgdwipldlparlralapDARLISLGGATEASIWSIYhpidEVPPDWRSIPYGRPLANQRY 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 490 KLVD--VEELNYWackGEGEICVRGPNVFKGYLKDPDRTKEAL--DSDG--WLHTGDIGKWLPAGTLKVIDRKKHIFKLa 563
Cdd:cd12114 312 RVLDprGRDCPDW---VPGELWIGGRGVALGYLGDPELTAARFvtHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKV- 387
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 966948474 564 QGEYVAPEKIENIYIRSQPVAQ--IYVHGDSLKAFLVGIVVPDPEVMP 609
Cdd:cd12114 388 RGYRIELGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPDNDGTP 435
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
266-615 |
6.46e-19 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 90.22 E-value: 6.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 266 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPrqddvlISFLPLAHMferviqsvvychggRVGFFQ 345
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFP------VRLLQMASF--------------SFDVFA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 346 GDIrllsddMKALCP--TIFPVVPRLL---NRMYDKIFSQ-----ANTP-LKRWLLEFAAKRKQ--AEVRSGIIRNDSIW 412
Cdd:cd17650 151 GDF------ARSLLNggTLVICPDEVKldpAALYDLILKSritlmESTPaLIRPVMAYVYRNGLdlSAMRLLIVGSDGCK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 413 DElFFNKIQASLGGCVRMIvtgaapaspTVLGFLRAALGCQVYEGYGQTECTAGctfTTPgdwtsghVGAPLPCNHIKLV 492
Cdd:cd17650 225 AQ-DFKTLAARFGQGMRII---------NSYGVTEATIDSTYYEEGRDPLGDSA---NVP-------IGRPLPNTAMYVL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 493 DvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGW------LHTGDIGKWLPAGTLKVIDRKKHIFKLaQGE 566
Cdd:cd17650 285 D-ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI-RGF 362
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 966948474 567 YVAPEKIENIYIRSQPVAQIYV---HGDSLKAFLVGIVVPDPEvmPSWAQKR 615
Cdd:cd17650 363 RIELGEIESQLARHPAIDEAVVavrEDKGGEARLCAYVVAAAT--LNTAELR 412
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
266-606 |
1.12e-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: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 266 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkvTEKVIFPRQDDVLISFLPLAHMFerviqSV-----VYCHGGR 340
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA----TQRWFGFNEDDVWTLFHSYAFDF-----SVweiwgALLHGGR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 341 VGFFQGDIRLLSDDMkalcptifpvvPRLLNRMYDKIFSQanTPLkrwllefAAKRKQAEVRSGIIRNDSIwdelffnki 420
Cdd:cd17643 162 LVVVPYEVARSPEDF-----------ARLLRDEGVTVLNQ--TPS-------AFYQLVEAADRDGRDPLAL--------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 421 qaslggcvRMIVTGAAPASPTVLGFLRAALGC---QVYEGYGQTECTAGCTFT--TPGDW---TSGHVGAPLPCNHIKLV 492
Cdd:cd17643 213 --------RYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFRplDAADLpaaAASPIGRPLPGLRVYVL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 493 DvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKE-------ALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQG 565
Cdd:cd17643 285 D-ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI-RG 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 966948474 566 EYVAPEKIENIYIRSQPVAQIYV---HGDSLKAFLVGIVVPDPE 606
Cdd:cd17643 363 FRIELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVADDG 406
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
121-609 |
3.71e-18 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 87.76 E-value: 3.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVG--PESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 201 DkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhhapvppqPDDLSIVCFTSGTT 280
Cdd:cd12115 103 D-----------------------------------------------------------------PDDLAYVIYTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 281 GNPKGAMLTHGNVVA------------DFSGFLKVTEkVIFprqdDVLI--SFLPLahmferviqsvvyCHGGRVGFFQG 346
Cdd:cd12115 118 GRPKGVAIEHRNAAAflqwaaaafsaeELAGVLASTS-ICF----DLSVfeLFGPL-------------ATGGKVVLADN 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 347 DIRLLsdDMKALCP-TIFPVVPRLLnrmydkifsqantplkRWLLEFaakrkqaevrsgiirndsiwdelffNKIQASlg 425
Cdd:cd12115 180 VLALP--DLPAAAEvTLINTVPSAA----------------AELLRH-------------------------DALPAS-- 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 426 gcVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFT--TPGDWTSGHVGAPLPCNHIKLVDvEELNYWAC 502
Cdd:cd12115 215 --VRVVNLAGEPLPRDLVQRLYARLqVERVVNLYGPSEDTTYSTVApvPPGASGEVSIGRPLANTQAYVLD-RALQPVPL 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 503 KGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENI 576
Cdd:cd12115 292 GVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAA 370
|
490 500 510
....*....|....*....|....*....|....*..
gi 966948474 577 yIRSQP-VAQ--IYVHGDSL-KAFLVGIVVPDPEVMP 609
Cdd:cd12115 371 -LRSIPgVREavVVAIGDAAgERRLVAYIVAEPGAAG 406
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
120-605 |
4.44e-18 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 87.74 E-value: 4.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 120 WLSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVI 199
Cdd:cd12118 29 RYTWRQTYDRCRRLASALAALGIS--RGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 200 VDKPqkavlllehverketpglkliilmdpFE-EALKERGQKcgvviksmqavedcgqenHHAPVPPQPDDLSIVC-FTS 277
Cdd:cd12118 107 VDRE--------------------------FEyEDLLAEGDP------------------DFEWIPPADEWDPIALnYTS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 278 GTTGNPKGAMLTHGnvvadfSGFLKVTEKVIFPRQDD--VLISFLPLAHmferviqsvvyCHGGrvGFFQGdirllsddM 355
Cdd:cd12118 143 GTTGRPKGVVYHHR------GAYLNALANILEWEMKQhpVYLWTLPMFH-----------CNGW--CFPWT--------V 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 356 KALCPTIfpVVPRLLNrmYDKIFsqantplkRWLLE-----FAAkrkqAEVRSGIIRNDSIWDelffnkiQASLGGCVRM 430
Cdd:cd12118 196 AAVGGTN--VCLRKVD--AKAIY--------DLIEKhkvthFCG----APTVLNMLANAPPSD-------ARPLPHRVHV 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 431 IVTGAAPaSPTVLgFLRAALGCQVYEGYGQTEcTAG----CTFTTPGDWTSGHVGAPLPC----NHIKL--VDVEELNY- 499
Cdd:cd12118 253 MTAGAPP-PAAVL-AKMEELGFDVTHVYGLTE-TYGpatvCAWKPEWDELPTEERARLKArqgvRYVGLeeVDVLDPETm 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 500 ----WACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIEN 575
Cdd:cd12118 330 kpvpRDGKTIGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENISSVEVEG 407
|
490 500 510
....*....|....*....|....*....|
gi 966948474 576 IyirsqpvaqIYVHGDSLKAFLVGivVPDP 605
Cdd:cd12118 408 V---------LYKHPAVLEAAVVA--RPDE 426
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
121-606 |
5.14e-18 |
|
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: 87.89 E-value: 5.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGSGLLQHNCKActdqfiG--VFAQ--NRPEWIIAELACYtySMVVVPLYdTLgPG----AIRYIINT 192
Cdd:COG1021 51 LSYAELDRRADRLAAGLLALGLRP------GdrVVVQlpNVAEFVIVFFALF--RAGAIPVF-AL-PAhrraEISHFAEQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 193 ADISTVIVDKpqkAVLLLEHVE-----RKETPGLKLIILMDPFEEalkergqkcgvviksMQAVEDCGQENHHAPVP-PQ 266
Cdd:COG1021 121 SEAVAYIIPD---RHRGFDYRAlarelQAEVPSLRHVLVVGDAGE---------------FTSLDALLAAPADLSEPrPD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 267 PDDlsiVCF---TSGTTGNPKGAMLTHG----NVV--ADFSGFlkvtekvifpRQDDVLISFLPLAHMF---ERVIQSVV 334
Cdd:COG1021 183 PDD---VAFfqlSGGTTGLPKLIPRTHDdylySVRasAEICGL----------DADTVYLAALPAAHNFplsSPGVLGVL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 335 YcHGGRVgffqgdirLLSDDMKALcpTIFP-----------VVPRLLNRMydkifsqantplkrwlLEFAAKRKQAevrs 403
Cdd:COG1021 250 Y-AGGTV--------VLAPDPSPD--TAFPlierervtvtaLVPPLALLW----------------LDAAERSRYD---- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 404 giirndsiwdeLffnkiqASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctaG-CTFTTPGD--WTSGH- 479
Cdd:COG1021 299 -----------L------SSL----RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---GlVNYTRLDDpeEVILTt 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 480 VGAPL-PCNHIKLVD-----VEElnywackGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKV 552
Cdd:COG1021 355 QGRPIsPDDEVRIVDedgnpVPP-------GEvGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVV 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 966948474 553 IDRKK-HIFKlaQGEYVAPEKIENiyirsqpvaQIYVHGDSLKAFLVGivVPDPE 606
Cdd:COG1021 428 EGRAKdQINR--GGEKIAAEEVEN---------LLLAHPAVHDAAVVA--MPDEY 469
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
70-588 |
6.27e-18 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 87.51 E-value: 6.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 70 ARRSVIGSGPQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRKpnqpyQWLSYQEVADRAEFLGSGLLQHNCKAcTDQf 149
Cdd:PRK06155 1 GEPLGAGLAARAVDPLPPSERTLPAMLARQAERYPDRPLLVFGG-----TRWTYAEAARAAAAAAHALAAAGVKR-GDR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 150 IGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlLLEHVERKETPGLKL--IILM 227
Cdd:PRK06155 74 VALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAA-----LLAALEAADPGDLPLpaVWLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 228 DPFEEALKERGQKCGVVIKSMQAVedcgqenhhAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHgnvvADFSGFLKVTEKV 307
Cdd:PRK06155 149 DAPASVSVPAGWSTAPLPPLDAPA---------PAAAVQPGDTAAILYTSGTTGPSKGVCCPH----AQFYWWGRNSAED 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 308 IFPRQDDVLISFLPLAH-----MFervIQSVVycHGGRV---------GFFqgdirllsDDMKALCPTIFpvvpRLLNRM 373
Cdd:PRK06155 216 LEIGADDVLYTTLPLFHtnalnAF---FQALL--AGATYvleprfsasGFW--------PAVRRHGATVT----YLLGAM 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 374 YDKIFSQANTPLKRwllefaakrkqaevrsgiirndsiwdelffnkiqaslGGCVRMIVTGAAPASptVLGFLRAALGCQ 453
Cdd:PRK06155 279 VSILLSQPARESDR-------------------------------------AHRVRVALGPGVPAA--LHAAFRERFGVD 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 454 VYEGYGQTECTAGCtFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWAckGE-GEICVRG--PNVF-KGYLKDPDRTKEA 529
Cdd:PRK06155 320 LLDGYGSTETNFVI-AVTHGSQRPGSMGRLAPGFEARVVDEHDQELPD--GEpGELLLRAdePFAFaTGYFGMPEKTVEA 396
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 530 LdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAPEKIENIyIRSQP-VAQIYV 588
Cdd:PRK06155 397 W-RNLWFHTGDRVVRDADGWFRFVDRIKDAIR-RRGENISSFEVEQV-LLSHPaVAAAAV 453
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
262-616 |
6.88e-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: 87.01 E-value: 6.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 262 PVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVTEKVIFPRQDDVLISFLPLAhmFERVIQSV--VYCHGG 339
Cdd:cd17651 130 DPALDADDLAYVIYTSGSTGRPKGVVMPHRSLA----NLVAWQARASSLGPGARTLQFAGLG--FDVSVQEIfsTLCAGA 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 340 RVGFFQGDIRLLSDDMKALCPTifpvvpRLLNRMYdkifsqANTPLKRWLLEfAAKRKQAEvrsgiirndsiwdelffnk 419
Cdd:cd17651 204 TLVLPPEEVRTDPPALAAWLDE------QRISRVF------LPTVALRALAE-HGRPLGVR------------------- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 420 iqaslGGCVRMIVTG--AAPASPTVLGFLRAALGCQVYEGYGQTE---CTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVD 493
Cdd:cd17651 252 -----LAALRYLLTGgeQLVLTEDLREFCAGLPGLRLHNHYGPTEthvVTALSLPGDPAAWPApPPIGRPIDNTRVYVLD 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 494 vEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKVIDRKKHIFKLaQGEY 567
Cdd:cd17651 327 -AALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGFR 404
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 966948474 568 VAPEKIENIYIRSQPVAQIYV------HGDslkAFLVGIVVPDPEVMPSWAQKRG 616
Cdd:cd17651 405 IELGEIEAALARHPGVREAVVlaredrPGE---KRLVAYVVGDPEAPVDAAELRA 456
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
259-594 |
1.20e-17 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 87.07 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 259 HHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTH----GNV-----VADFSgflkvtekvifPRqdDVLISFLPLAHMFerv 329
Cdd:PRK08043 356 RLAQVKQQPEDAALILFTSGSEGHPKGVVHSHksllANVeqiktIADFT-----------PN--DRFMSALPLFHSF--- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 330 iqsvvychGGRVGFFQGdirLLSDDMKALCPTI--FPVVPRLLnrmYDK----IFSQANtplkrWLLEFAakrkqaevrs 403
Cdd:PRK08043 420 --------GLTVGLFTP---LLTGAEVFLYPSPlhYRIVPELV---YDRnctvLFGTST-----FLGNYA---------- 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 404 giiRNDSIWDelFFNkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAP 483
Cdd:PRK08043 471 ---RFANPYD--FAR---------LRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRI 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 484 LPCNHIKLVDVEELNywacKGeGEICVRGPNVFKGYLK--DPDRTK-------EALDSDGWLHTGDIGKWLPAGTLKVID 554
Cdd:PRK08043 537 LPGMDARLLSVPGIE----QG-GRLQLKGPNIMNGYLRveKPGVLEvptaenaRGEMERGWYDTGDIVRFDEQGFVQIQG 611
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 966948474 555 RKKHIFKLAqGEYVAPEKIENIYIRSQPVAQiyvHGDSLK 594
Cdd:PRK08043 612 RAKRFAKIA-GEMVSLEMVEQLALGVSPDKQ---HATAIK 647
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
27-604 |
1.65e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 87.52 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 27 ATTLVSMGALAAILAYW--FTHRPKAlQPPCNL----LMQSEEVedsggaRRSVIGSGPqllTHYYDDARTMYQVFRRGL 100
Cdd:PRK12467 453 ATDLFEATTIERLATHWrnLLEAIVA-EPRRRLgelpLLDAEER------ARELVRWNA---PATEYAPDCVHQLIEAQA 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 101 SISGNGPCLGFRKpnqpyQWLSYQEVADRAEFLGSGLLQHNckACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDT 180
Cdd:PRK12467 523 RQHPERPALVFGE-----QVLSYAELNRQANRLAHVLIAAG--VGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPE 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 181 LGPGAIRYIINTADISTVIVDKPQKAVLLLehverkeTPGLKLIILMDPfeealkergqkcgvviksmqAVEDCGQENHH 260
Cdd:PRK12467 596 YPQDRLAYMLDDSGVRLLLTQSHLLAQLPV-------PAGLRSLCLDEP--------------------ADLLCGYSGHN 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 261 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVvadfSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGR 340
Cdd:PRK12467 649 PEVALDPDNLAYVIYTSGSTGQPKGVAISHGAL----ANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGAT 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 341 VgffqgdirLLSDDMKALCPTIFpvvprllnrmYDKIFSQANTPLKrwllefaakrkqaevrsgiiRNDSIWDELFFNKI 420
Cdd:PRK12467 725 L--------HLLPPDCARDAEAF----------AALMADQGVTVLK--------------------IVPSHLQALLQASR 766
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 421 QASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTT----PGDWTSGHVGAPLPCNHIKLVDvEE 496
Cdd:PRK12467 767 VALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYElsdeERDFGNVPIGQPLANLGLYILD-HY 845
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 497 LNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSD------GWLH-TGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVA 569
Cdd:PRK12467 846 LNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDpfgadgGRLYrTGDLARYRADGVIEYLGRMDHQVKI-RGFRIE 924
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 966948474 570 PEKIENIyIRSQP-------VAQIYVHGDSLKAFLVGIVVPD 604
Cdd:PRK12467 925 LGEIEAR-LLAQPgvreavvLAQPGDAGLQLVAYLVPAAVAD 965
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
121-609 |
2.08e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 85.95 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGSGLLQHNckACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQG--VRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 201 DKPQKAVLL---LEHVERKETPGLKLIILMDPFEEALKERGQKCGVviksmQAVEDCGQENHHAPVPPQ-PDDLSIVCFT 276
Cdd:PRK06164 114 WPGFKGIDFaaiLAAVPPDALPPLRAIAVVDDAADATPAPAPGARV-----QLFALPDPAPPAAAGERAaDPDAGALLFT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 277 -SGTTGNPK------GAMLTHGNVVADFSGFlkvtekvifpRQDDVLISFLPLahmferviqSVVYCHGGRVGFFQGDIR 349
Cdd:PRK06164 189 tSGTTSGPKlvlhrqATLLRHARAIARAYGY----------DPGAVLLAALPF---------CGVFGFSTLLGALAGGAP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 350 LLSDDMKALCPTIfpvvpRLL-----------NRMYDKIFSQANTPLkrwllEFAAKRkqaevRSGIirndsiwdelffn 418
Cdd:PRK06164 250 LVCEPVFDAARTA-----RALrrhrvthtfgnDEMLRRILDTAGERA-----DFPSAR-----LFGF------------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 419 kiqASLggcvrmivtgaAPASPTVLGFLRAAlGCQVYEGYGQTECTA---GCTFTTPgdWTSGHVGAPLPCN---HIKLV 492
Cdd:PRK06164 302 ---ASF-----------APALGELAALARAR-GVPLTGLYGSSEVQAlvaLQPATDP--VSVRIEGGGRPASpeaRVRAR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 493 DVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEK 572
Cdd:PRK06164 365 DPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNPAE 443
|
490 500 510
....*....|....*....|....*....|....*....
gi 966948474 573 IENIYIRSQPVAQIYVHGDSL--KAFLVGIVVPDPEVMP 609
Cdd:PRK06164 444 IEHALEALPGVAAAQVVGATRdgKTVPVAFVIPTDGASP 482
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
121-590 |
2.84e-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: 85.25 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRP--GQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 201 dkpqkavllleHVERKETPGLKLIILMDPFEEALKERGQKC--GVVIKsmqavedcgqenhhaPVPPQPDDLSIVCFTSG 278
Cdd:cd05923 107 -----------AVDAQVMDAIFQSGVRVLALSDLVGLGEPEsaGPLIE---------------DPPREPEQPAFVFYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 279 TTGNPKGAMLTHgNVVADFSGFLKVTEKVIFPRQDdVLISFLPLAHMferviqsvvychggrVGFFQgdirLLSDDMkAL 358
Cdd:cd05923 161 TTGLPKGAVIPQ-RAAESRVLFMSTQAGLRHGRHN-VVLGLMPLYHV---------------IGFFA----VLVAAL-AL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 359 CPTIFPVvprllnrmydKIFSQANtplkrwllefAAKRKQAEVRSGIIRNDSIWDELFFNKIQASLG-GCVRMIVTGAAP 437
Cdd:cd05923 219 DGTYVVV----------EEFDPAD----------ALKLIEQERVTSLFATPTHLDALAAAAEFAGLKlSSLRHVTFAGAT 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 438 ASPTVLGFLRAALGCQVYEGYGQTECTagcTFTTPGDWTSGHVGAPLPCNHIKLVDV-EELNYWACKG-EGEICVR--GP 513
Cdd:cd05923 279 MPDAVLERVNQHLPGEKVNIYGTTEAM---NSLYMRDARTGTEMRPGFFSEVRIVRIgGSPDEALANGeEGELIVAaaAD 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966948474 514 NVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYVHG 590
Cdd:cd05923 356 AAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIG 430
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
121-605 |
7.97e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 84.30 E-value: 7.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PLN03102 40 FTWPQTYDRCCRLAASLISLNIT--KNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 201 DKP-----QKAVLLLEHVERKETPGLKLIILMD----PFE-----EALKERGQKCGVVIKSMQAVEDcgqenHHAPVPpq 266
Cdd:PLN03102 118 DRSfeplaREVLHLLSSEDSNLNLPVIFIHEIDfpkrPSSeeldyECLIQRGEPTPSLVARMFRIQD-----EHDPIS-- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 267 pddlsiVCFTSGTTGNPKGAMLTH-GNVVADFSGFLKvTEKVIFPrqddVLISFLPLAH---------MFERVIQSVVYC 336
Cdd:PLN03102 191 ------LNYTSGTTADPKGVVISHrGAYLSTLSAIIG-WEMGTCP----VYLWTLPMFHcngwtftwgTAARGGTSVCMR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 337 HGGRVGFFQgDIRLLSDDMKALCPTIFpvvprllnrmydkifsqantplkRWLLEfaAKRKQAEVRSGIIRndsiwdelf 416
Cdd:PLN03102 260 HVTAPEIYK-NIEMHNVTHMCCVPTVF-----------------------NILLK--GNSLDLSPRSGPVH--------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 417 fnkiqaslggcvrmIVTGAAPAsPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGD-WTSghvgapLPCN-------- 487
Cdd:PLN03102 305 --------------VLTGGSPP-PAALVKKVQRLGFQVMHAYGLTEATGPVLFCEWQDeWNR------LPENqqmelkar 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 488 ----HIKLVDVEELNYWAC-------KGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRK 556
Cdd:PLN03102 364 qgvsILGLADVDVKNKETQesvprdgKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRS 442
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 966948474 557 KHIFkLAQGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGIvvPDP 605
Cdd:PLN03102 443 KDII-ISGGENISSVEVENV---------LYKYPKVLETAVVAM--PHP 479
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
276-606 |
1.22e-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: 83.15 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 276 TSGTTGNPKGAMLTHgnvvADFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERV---IQSVVYChGGRVgffqgdirLLS 352
Cdd:cd05920 147 SGGTTGTPKLIPRTH----NDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLAcpgVLGTLLA-GGRV--------VLA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 353 DDmkALCPTIFPVVPRllnrmyDKIFSQANTP--LKRWLlEFAAKRKQAEvrsgiirndsiwdelffnkiqASLggcvRM 430
Cdd:cd05920 214 PD--PSPDAAFPLIER------EGVTVTALVPalVSLWL-DAAASRRADL---------------------SSL----RL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 431 IVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHVGAPL-PCNHIKLVDvEELNYWACKGEGEI 508
Cdd:cd05920 260 LQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTrLDDPDEVIIHTQGRPMsPDDEIRVVD-EEGNPVPPGEEGEL 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 509 CVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENiyirsqpvaQIYV 588
Cdd:cd05920 339 LTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVEN---------LLLR 408
|
330
....*....|....*...
gi 966948474 589 HGDSLKAFLVGivVPDPE 606
Cdd:cd05920 409 HPAVHDAAVVA--MPDEL 424
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
269-576 |
1.40e-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: 81.54 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 269 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIfprQDDVLISFLPLAHMFERV-IQSVVYCHGGRVGFfqGD 347
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWV---VGDVTYLPLPATHIGGLWwILTCLIHGGLCVTG--GE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 348 IRLLSDDMKAL---CPTIFPVVPRLLNRMYDKIFSQANTPLKRWLLEFAAKRkqaevrsgIIRNDSIWDELFFNkiqasl 424
Cdd:cd17635 77 NTTYKSLFKILttnAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSR--------AIAADVRFIEATGL------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 425 ggcvrmivtgaapasptvlgflraalgCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDVEELNYWAcK 503
Cdd:cd17635 143 ---------------------------TNTAQVYGLSETGTALCLPTDDDSIEiNAVGRPYPGVDVYLAATDGIAGPS-A 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966948474 504 GEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENI 576
Cdd:cd17635 195 SFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERI 265
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
267-578 |
2.50e-16 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 82.56 E-value: 2.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAHMFerviqsvvychggrvGFFqg 346
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFS----PKEDDVMMSFLPPFHAY---------------GFN-- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 347 dirllsddmkalCPTIFPVVPRLlnrmyDKIFSQanTPLK-RWLLEFAAKRKQAEVRSGIIRNDSIwdeLFFNKIQASLG 425
Cdd:PRK06334 241 ------------SCTLFPLLSGV-----PVVFAY--NPLYpKKIVEMIDEAKVTFLGSTPVFFDYI---LKTAKKQESCL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 426 GCVRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFTT---PGDwtSGHVGAPLPCNHIKLVDvEELNYWA 501
Cdd:PRK06334 299 PSLRFVVIGGDAFKDSLYqEALKTFPHIQLRQGYGTTECSPVITINTvnsPKH--ESCVGMPIRGMDVLIVS-EETKVPV 375
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966948474 502 CKGE-GEICVRGPNVFKGYL-KDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYI 578
Cdd:PRK06334 376 SSGEtGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSLEALESILM 453
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
267-671 |
2.92e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 82.79 E-value: 2.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekviFPRQDD----VLISFLPLAHMFerviqsvvychGGRVG 342
Cdd:PRK12582 219 PDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQL-----RPREPDppppVSLDWMPWNHTM-----------GGNAN 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 343 FfQGDIR----LLSDDMKALcPTIFPVVPRLLNRMYDKIFsqANTPLKRWLLEFAAKRKQAEVRSgiirndsiwdelFFN 418
Cdd:PRK12582 283 F-NGLLWgggtLYIDDGKPL-PGMFEETIRNLREISPTVY--GNVPAGYAMLAEAMEKDDALRRS------------FFK 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 419 KIqaslggcvRMIVTGAAPASPTVLGFLRA----ALGCQV--YEGYGQTEcTAGCTFTTpgDWTS---GHVGAPLPCNHI 489
Cdd:PRK12582 347 NL--------RLMAYGGATLSDDLYERMQAlavrTTGHRIpfYTGYGATE-TAPTTTGT--HWDTervGLIGLPLPGVEL 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 490 KLVDVEElNYwackgegEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWL----PAGTLKVIDRKKHIFKLAQG 565
Cdd:PRK12582 416 KLAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdpddPEKGLIFDGRVAEDFKLSTG 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 566 EYV--APEKIENIYIRSQPVAQIYVHGDSlKAFLVGIVVPDPEVMPSWAQKRGieGTYADLCTSKDLKKAILEDMVRLGK 643
Cdd:PRK12582 488 TWVsvGTLRPDAVAACSPVIHDAVVAGQD-RAFIGLLAWPNPAACRQLAGDPD--AAPEDVVKHPAVLAILREGLSAHNA 564
|
410 420
....*....|....*....|....*...
gi 966948474 644 ESGLHSfEQVKAIHIHSDMFSVQNGLLT 671
Cdd:PRK12582 565 EAGGSS-SRIARALLMTEPPSIDAGEIT 591
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
267-583 |
8.19e-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: 80.61 E-value: 8.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKvifpRQDDVLISFLPLAHmferviqsvvychggRVGFFQG 346
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEW----KTKDRILSWMPLTH---------------DMGLIAF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 347 DIRLLSDDMKA-LCPT-IFPVVPRLLNRMYDK----IFSQANTPLKrWLLEFAAKRKQAEvrsgiirndsiWDElffnki 420
Cdd:cd05908 166 HLAPLIAGMNQyLMPTrLFIRRPILWLKKASEhkatIVSSPNFGYK-YFLKTLKPEKAND-----------WDL------ 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 421 qaslgGCVRMIVTGAAPASP----------TVLGFLRAAlgcqVYEGYGQTECTAGCTF--------------------- 469
Cdd:cd05908 228 -----SSIRMILNGAEPIDYelchefldhmSKYGLKRNA----ILPVYGLAEASVGASLpkaqspfktitlgrrhvthge 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 470 -------TTPGDWTSGHVGAPLPCNHIKLVDveELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDI 541
Cdd:cd05908 299 pepevdkKDSECLTFVEVGKPIDETDIRICD--EDNKILPDGYiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDL 376
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 966948474 542 GkWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPV 583
Cdd:cd05908 377 G-FIRNGRLVITGREKDII-FVNGQNVYPHDIERIAEELEGV 416
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
268-610 |
8.45e-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: 8.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 268 DDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkvTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGR--VGFFQ 345
Cdd:cd05958 97 DDICILAFTSGTTGAPKATMHFHRDPLASADRY---AVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGAsgVLLEE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 346 GDIRLLSDDMKALCPTIFPVVPRllnrMYdkifsqantplkRWLLEFAAKRKQaevrsgiirndsiwdelffnkiqasLG 425
Cdd:cd05958 174 ATPDLLLSAIARYKPTVLFTAPT----AY------------RAMLAHPDAAGP-------------------------DL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 426 GCVRMIVTgAAPASPTVLGFL-RAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDveELNYWACKG 504
Cdd:cd05958 213 SSLRKCVS-AGEALPAALHRAwKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD--DEGNPVPDG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 505 E-GEICVRGPNVFKgYLKDPDRTKEAldSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRSQPV 583
Cdd:cd05958 290 TiGRLAVRGPTGCR-YLADKRQRTYV--QGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQHPAV 365
|
330 340 350
....*....|....*....|....*....|
gi 966948474 584 AQIYVHGDSLKAFLV---GIVVPDPEVMPS 610
Cdd:cd05958 366 AECAVVGHPDESRGVvvkAFVVLRPGVIPG 395
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
121-617 |
8.64e-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: 80.88 E-value: 8.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGSGLLQhnckactdqfIGVFAQNR--------PEWIIAELACYTYSMVVVPLYDTLGPGAIRYIInt 192
Cdd:cd05959 30 LTYAELEAEARRVAGALRA----------LGVKREERvllimldtVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 193 ADI-STVIVDKPQKAVLLLEHVERKEtPGLKLIILMDPFEEALKErgqkcgvviksMQAVEDCGQENHH-APVPPQPDDL 270
Cdd:cd05959 98 EDSrARVVVVSGELAPVLAAALTKSE-HTLVVLIVSGGAGPEAGA-----------LLLAELVAAEAEQlKPAATHADDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 271 SIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKvteKVIFPRQDDVLIS--------------FLPLAH------MFERVI 330
Cdd:cd05959 166 AFWLYSSGSTGRPKGVVHLHADIYWTAELYAR---NVLGIREDDVCFSaaklffayglgnslTFPLSVgattvlMPERPT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 331 QSVVYchggrvgffqgdirllsDDMKALCPTIFPVVPRLLNRMydkifsqantplkrwlleFAAKRKQAEVRSGIirnds 410
Cdd:cd05959 243 PAAVF-----------------KRIRRYRPTVFFGVPTLYAAM------------------LAAPNLPSRDLSSL----- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 411 iwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTF--TTPGDWTSGHVGAPLPCNH 488
Cdd:cd05959 283 ------------------RLCVSAGEALPAEVGERWKARFGLDILDGIGSTE--MLHIFlsNRPGRVRYGTTGKPVPGYE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 489 IKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSdGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYV 568
Cdd:cd05959 343 VELRD-EDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQG-EWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWV 419
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 966948474 569 APEKIENIYIRSQPVAQIYVHG-------DSLKAFlvgiVVPDPEVMPSWAQKRGI 617
Cdd:cd05959 420 SPFEVESALVQHPAVLEAAVVGvededglTKPKAF----VVLRPGYEDSEALEEEL 471
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
457-613 |
1.16e-15 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 78.88 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 457 GYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVE--ELNywacKGE-GEICVRGPNVFKGYLKDPDRTKEALdSD 533
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDgrEVP----DGEvGEIVARGPTVMAGYWNRPEVNARRT-RG 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 534 GWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqgeyvapekIENIY-------IRSQP-VAQIYVhgdslkaflvgIVVPDp 605
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSG---------AENIYpaevercLRQHPaVADAAV-----------IGVPD- 275
|
....*...
gi 966948474 606 evmPSWAQ 613
Cdd:cd17636 276 ---PRWAQ 280
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
121-606 |
1.67e-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: 79.63 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:cd17646 24 LTYRELDERANRLAHLLRARGVGP--EDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 201 DKPQKAVLllehverketPGLKLIILMDPfeealkergqkcgvviksmqavEDCGQENHHAP-VPPQPDDLSIVCFTSGT 279
Cdd:cd17646 102 TADLAARL----------PAGGDVALLGD----------------------EALAAPPATPPlVPPRPDNLAYVIYTSGS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 280 TGNPKGAMLTHGNVVADFSGF-----LKVTEKVIF--PRQDDVLIS--FLPLAHMfERViqsVVYCHGGRvgffqGDIRL 350
Cdd:cd17646 150 TGRPKGVMVTHAGIVNRLLWMqdeypLGPGDRVLQktPLSFDVSVWelFWPLVAG-ARL---VVARPGGH-----RDPAY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 351 LSDDMKALCPTIFPVVPRLLnrmydkifsqantplkrwllefaakrkqaevrsgiirndsiwdELFFNKIQASLGGCVRM 430
Cdd:cd17646 221 LAALIREHGVTTCHFVPSML-------------------------------------------RVFLAEPAAGSCASLRR 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 431 IVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHV--GAPLPCNHIKLVDvEELNYWACKGEGE 507
Cdd:cd17646 258 VFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVThWPVRGPAETPSVpiGRPVPNTRLYVLD-DALRPVPVGVPGE 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 508 ICVRGPNVFKGYLKDPDRTKEALDSDGWLH------TGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIyIRSQ 581
Cdd:cd17646 337 LYLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKI-RGFRVEPGEIEAA-LAAH 414
|
490 500
....*....|....*....|....*....
gi 966948474 582 P-VAQIYV---HGDSLKAFLVGIVVPDPE 606
Cdd:cd17646 415 PaVTHAVVvarAAPAGAARLVGYVVPAAG 443
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
150-607 |
8.41e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 77.80 E-value: 8.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 150 IGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAVL--LLEHVERKETPGLKLIILM 227
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLdgLDPGVRVINVDSPAWADEL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 228 DPFEEALKErgqkcgvviksmqavedcgqenhhaPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGflkvtekv 307
Cdd:PRK07867 137 AAHRDAEPP-------------------------FRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVA--SAG-------- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 308 ifprqddvlisfLPLAHMFERVIQSVVYC-----HGGRVgffqgdirllsddMKALCPTIFpvvprllnrmydkifSQAN 382
Cdd:PRK07867 182 ------------VMLAQRFGLGPDDVCYVsmplfHSNAV-------------MAGWAVALA---------------AGAS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 383 TPLKRwllEFAAKRKQAEVRS-GIIrndsiwdelFFNKIqaslGGCVRMIVtgAAP-----------------ASPTVLG 444
Cdd:PRK07867 222 IALRR---KFSASGFLPDVRRyGAT---------YANYV----GKPLSYVL--ATPerpddadnplrivygneGAPGDIA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 445 FLRAALGCQVYEGYGQTEctAGCTFTTPGDWTSGHVGaPLPCNhIKLVDVE--------------ELNYWACKGEgEICV 510
Cdd:PRK07867 284 RFARRFGCVVVDGFGSTE--GGVAITRTPDTPPGALG-PLPPG-VAIVDPDtgtecppaedadgrLLNADEAIGE-LVNT 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 511 RGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYVHG 590
Cdd:PRK07867 359 AGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPIERILLRYPDATEVAVYA 436
|
490
....*....|....*..
gi 966948474 591 dslkaflvgivVPDPEV 607
Cdd:PRK07867 437 -----------VPDPVV 442
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
262-588 |
1.08e-14 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 76.83 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 262 PVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkVTEKVIFPRQDDVLISfLPLAHmferVI-QSVVY---CH 337
Cdd:PRK09029 129 AVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEG---VLSLMPFTAQDSWLLS-LPLFH----VSgQGIVWrwlYA 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 338 GGRVGFfqGDIRLLSDDMK-----ALCPTifpVVPRLLNRmydkifSQANTPLKRWLLefaakrkqaevrsgiirndsiw 412
Cdd:PRK09029 201 GATLVV--RDKQPLEQALAgcthaSLVPT---QLWRLLDN------RSEPLSLKAVLL---------------------- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 413 delffnkiqaslGGCvrMIvtgaapasPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTSGhVGAPLPCNHIKLV 492
Cdd:PRK09029 248 ------------GGA--AI--------PVELTEQAEQQGIRCWCGYGLTE-MASTVCAKRADGLAG-VGSPLPGREVKLV 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 493 DveelnywackgeGEICVRGPNVFKGYLKDpDRTKEALDSDGWLHTGDIGKWLpAGTLKVIDRKKHIFkLAQGEYVAPEK 572
Cdd:PRK09029 304 D------------GEIWLRGASLALGYWRQ-GQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEE 368
|
330
....*....|....*.
gi 966948474 573 IENIYIRSQPVAQIYV 588
Cdd:PRK09029 369 IERVINQHPLVQQVFV 384
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
152-605 |
3.17e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 75.85 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 152 VFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV--DKPqkavlllEHVE--RKETPGLKLIILM 227
Cdd:PRK07470 62 VHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMIChaDFP-------EHAAavRAASPDLTHVVAI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 228 D--PFEEAlkergqkcgvviksmqaVEDCGQENHHAPVPPQP---DDLSIVCFTSGTTGNPKGAMLTHG-------NVVA 295
Cdd:PRK07470 135 GgaRAGLD-----------------YEALVARHLGARVANAAvdhDDPCWFFFTSGTTGRPKAAVLTHGqmafvitNHLA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 296 DfsgflkvtekvIFP--RQDDVLISFLPLAHMfERVIQSVVYCHGGRVgffqgdIRLLSDDMKAlcptifPVVPRLLNRM 373
Cdd:PRK07470 198 D-----------LMPgtTEQDASLVVAPLSHG-AGIHQLCQVARGAAT------VLLPSERFDP------AEVWALVERH 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 374 YDKIFSQANTPLKrWLLEFAAkrkqaevrsgIIRNDsiwdelffnkiQASLggcvRMIVTGAAPASPTVLGFLRAALGCQ 453
Cdd:PRK07470 254 RVTNLFTVPTILK-MLVEHPA----------VDRYD-----------HSSL----RYVIYAGAPMYRADQKRALAKLGKV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 454 VYEGYGQTECTAGCTFTTP-----GDWTSGHVGaplPCNH--------IKLVDVEELNywacKGE-GEICVRGPNVFKGY 519
Cdd:PRK07470 308 LVQYFGLGEVTGNITVLPPalhdaEDGPDARIG---TCGFertgmevqIQDDEGRELP----PGEtGEICVIGPAVFAGY 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 520 LKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENiyirsqpvaQIYVHGDSLKAFLVG 599
Cdd:PRK07470 381 YNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPREIEE---------KLLTHPAVSEVAVLG 449
|
....*.
gi 966948474 600 ivVPDP 605
Cdd:PRK07470 450 --VPDP 453
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
158-598 |
3.56e-14 |
|
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: 75.58 E-value: 3.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 158 PEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlLLEHVER--KETPGLKLIILMDPfeealk 235
Cdd:cd05928 78 PEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDE-----LAPEVDSvaSECPSLKTKLLVSE------ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 236 ERGQKCGVVIKSMQAVEDcgqenHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGN----VVADFSGFLKVTEKVIFPR 311
Cdd:cd05928 147 KSRDGWLNFKELLNEAST-----EHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSlglgLKVNGRYWLDLTASDIMWN 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 312 QDDVLISFLPLAHMFERVIQ-SVVYCHggRVGFFQGDI---RLLSDDMKALC--PTIFpvvprllnRMydkifsqantpl 385
Cdd:cd05928 222 TSDTGWIKSAWSSLFEPWIQgACVFVH--HLPRFDPLVilkTLSSYPITTFCgaPTVY--------RM------------ 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 386 krwllefaakrkqaevrsgIIRNDsiwdelfFNKIQ-ASLGGCVrmivTGAAPASPTVLGFLRAALGCQVYEGYGQTECT 464
Cdd:cd05928 280 -------------------LVQQD-------LSSYKfPSLQHCV----TGGEPLNPEVLEKWKAQTGLDIYEGYGQTETG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 465 AGCTFTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVR-GPN----VFKGYLKDPDRTKEALDSDGWLhTG 539
Cdd:cd05928 330 LICANFKGMKIKPGSMGKASPPYDVQIID-DNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIRGDFYL-TG 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966948474 540 DIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLV 598
Cdd:cd05928 408 DRGIMDEDGYFWFMGRADDVI-NSSGYRIGPFEVESALIEHPAVVESAVvsspdpiRGEVVKAFVV 472
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
420-588 |
7.95e-14 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 74.14 E-value: 7.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 420 IQASLGGC---VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTfTTPGD-WTSGHVGAPLPCNHIKLVDVE 495
Cdd:cd05974 191 IQQDLASFdvkLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVG-NSPGQpVKAGSMGRPLPGYRVALLDPD 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 496 ElnywACKGEGEICV-----RGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAP 570
Cdd:cd05974 270 G----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SSDYRISP 343
|
170
....*....|....*...
gi 966948474 571 EKIENIYIRSQPVAQIYV 588
Cdd:cd05974 344 FELESVLIEHPAVAEAAV 361
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
121-606 |
1.00e-13 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 73.69 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGSGLLQHNCKACTDQFigVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYiintadistviv 200
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVF--VLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRD------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 201 dkpqkavlllehveRKETPGLKLIILmdpfEEALKERgqkcgvviksmqavedcgqenhhapvpPQPDDLSIVCFTSGTT 280
Cdd:cd05969 67 --------------RLENSEAKVLIT----TEELYER---------------------------TDPEDPTLLHYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 281 GNPKGAMLTHGNVVADFsgflkVTEKVIFP-RQDDVLIS--------------FLPLAHMfervIQSVVYchGGRVgffq 345
Cdd:cd05969 102 GTPKGVLHVHDAMIFYY-----FTGKYVLDlHPDDIYWCtadpgwvtgtvygiWAPWLNG----VTNVVY--EGRF---- 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 346 gDIRLLSDDMKALCPTIFPVVPRLLnRMydkifsqantpLKRWLLEFAAKrkqaevrsgiirndsiWDElffnkiqASLg 425
Cdd:cd05969 167 -DAESWYGIIERVKVTVWYTAPTAI-RM-----------LMKEGDELARK----------------YDL-------SSL- 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 426 gcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPCNHIKLVDvEELNYWACKG 504
Cdd:cd05969 210 ---RFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYPCmPIKPGSMGKPLPGVKAAVVD-ENGNELPPGT 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 505 EGEICVRG--PNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRSQP 582
Cdd:cd05969 286 KGILALKPgwPSMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHRVGPFEVESALMEHPA 363
|
490 500
....*....|....*....|....
gi 966948474 583 VAQIYVHGdslkaflvgivVPDPE 606
Cdd:cd05969 364 VAEAGVIG-----------KPDPL 376
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
265-603 |
1.47e-13 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 73.26 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 265 PQPDDLSIVCFTSGTTGNPKGAMLTHGNvvadFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERV--IQSVVychggrvg 342
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGT----FAAQIDALRQLYGIRPGEVDLATFPLFALFGPAlgLTSVI-------- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 343 ffqgdirllsDDMKALCPTifPVVPRllnrmydKIFSqantPLKRWllefaakrkqaEVrSGIIRNDSIWDEL--FFNKI 420
Cdd:cd05910 150 ----------PDMDPTRPA--RADPQ-------KLVG----AIRQY-----------GV-SIVFGSPALLERVarYCAQH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 421 QASLGGcVRMIVTGAAPASPTVLGFLRAAL--GCQVYEGYGQTECTAGCT------FTTPGDWTSGH----VGAPLPCNH 488
Cdd:cd05910 195 GITLPS-LRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrelLATTTAATSGGagtcVGRPIPGVR 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 489 IKLV--DVEELNYWACKGE------GEICVRGPNVFKGYLKDPDRTKEALDSDG----WLHTGDIGKWLPAGTLKVIDRK 556
Cdd:cd05910 274 VRIIeiDDEPIAEWDDTLElprgeiGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRK 353
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 966948474 557 KHIFKLAQGEYVapekieniyirSQPVAQIY-VHGDSLKAFLVGIVVP 603
Cdd:cd05910 354 AHRVITTGGTLY-----------TEPVERVFnTHPGVRRSALVGVGKP 390
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
121-636 |
3.05e-13 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 72.89 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGSGLlQHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PRK05620 39 TTFAAIGARAAALAHAL-HDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 201 D---KPQKAVLLlehverKETPGLKLIILMDPFEEALKERGQKCGVVIKSMQAVEDcGQENHHaPVPPQP-DDLSIVCFT 276
Cdd:PRK05620 118 DprlAEQLGEIL------KECPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALLD-GRSTVY-DWPELDeTTAAAICYS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 277 SGTTGNPKGAMLTHGNVVADfSGFLKVTEKviFPRQDDVliSFL---PLAHMFERVIQSVVYCHGgrvgffqgdirllsd 353
Cdd:PRK05620 190 TGTTGAPKGVVYSHRSLYLQ-SLSLRTTDS--LAVTHGE--SFLccvPIYHVLSWGVPLAAFMSG--------------- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 354 dmkalCPTIFP----VVPRLLnrmydKIFSqanTPLKRwllefaakrkqaeVRSGIirnDSIWDELFFNKIQ-----ASL 424
Cdd:PRK05620 250 -----TPLVFPgpdlSAPTLA-----KIIA---TAMPR-------------VAHGV---PTLWIQLMVHYLKnpperMSL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 425 ggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGA---------PLPCNHiKLVDVE 495
Cdd:PRK05620 301 ----QEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEARWayrvsqgrfPASLEY-RIVNDG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 496 ELNYWACKGEGEICVRGPNVFKGYLKDP----------------DRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHI 559
Cdd:PRK05620 376 QVMESTDRNEGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDV 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 560 FKlAQGEYVAPEKIENIYIRSQPVaqiyvhgdsLKAFLVGIvvPDPEvmpsWAQK--------RGIEGTYAdlcTSKDLK 631
Cdd:PRK05620 456 IR-SGGEWIYSAQLENYIMAAPEV---------VECAVIGY--PDDK----WGERplavtvlaPGIEPTRE---TAERLR 516
|
....*
gi 966948474 632 KAILE 636
Cdd:PRK05620 517 DQLRD 521
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
119-599 |
4.02e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 73.45 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 119 QWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGA-IRYIINTADIST 197
Cdd:PRK12316 2027 QHLSYAELDSRANRLAHRLRARGVGP--EVRVAIAAERSFELVVALLAVLKAGGAYVPL-DPNYPAErLAYMLEDSGAAL 2103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 198 VIVDKPQKAVLLLehverkeTPGLKLIILMDPfeEALKERGQkcgvviksmqavedcgqenHHAPVPPQPDDLSIVCFTS 277
Cdd:PRK12316 2104 LLTQRHLLERLPL-------PAGVARLPLDRD--AEWADYPD-------------------TAPAVQLAGENLAYVIYTS 2155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 278 GTTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPLAhmFERVIQSVVY--CHGGRVgffqgdirLLSDDM 355
Cdd:PRK12316 2156 GSTGLPKGVAVSHGALVA----HCQAAGERYELSPADCELQFMSFS--FDGAHEQWFHplLNGARV--------LIRDDE 2221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 356 KalcptifpvvpRLLNRMYDKIFSQANTplkrwLLEFAAKRKQAEVRsgiirndsiwdelffnkiQASLGGC---VRMIV 432
Cdd:PRK12316 2222 L-----------WDPEQLYDEMERHGVT-----ILDFPPVYLQQLAE------------------HAERDGRppaVRVYC 2267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 433 TGAAPASPTVLGFLRAALGCQ-VYEGYGQTEctagcTFTTPGDWTSGH----------VGAPLPCNHIKLVDvEELNYWA 501
Cdd:PRK12316 2268 FGGEAVPAASLRLAWEALRPVyLFNGYGPTE-----AVVTPLLWKCRPqdpcgaayvpIGRALGNRRAYILD-ADLNLLA 2341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 502 CKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH-------TGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIE 574
Cdd:PRK12316 2342 PGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKI-RGFRIELGEIE 2420
|
490 500 510
....*....|....*....|....*....|..
gi 966948474 575 NiYIRSQP-------VAQIYVHGDSLKAFLVG 599
Cdd:PRK12316 2421 A-RLQAHPavreavvVAQDGASGKQLVAYVVP 2451
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-598 |
8.58e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 72.30 E-value: 8.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 3 TQEILRILRLPELGDLGQFfrSLSATTLVSMGALAAILAYWFTHRPKAL-----QPPCNLLMQS--------EEVEDSGG 69
Cdd:PRK12316 2959 QLPGLHIESFAWDGAATQF--DLALDTWESAEGLGASLTYATDLFDARTverlaRHWQNLLRGMvenpqrsvDELAMLDA 3036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 70 ARRSVIGSGPQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRKpnqpyQWLSYQEVADRAEFLGSGLLQHNCKActDQF 149
Cdd:PRK12316 3037 EERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVALAFGE-----QRLSYAELNRRANRLAHRLIERGVGP--DVL 3109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 150 IGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGAiryiintaDISTVIVDKPQKAVLLLEHVERKETPGLKlIILMDP 229
Cdd:PRK12316 3110 VGVAVERSLEMVVGLLAILKAGGAYVPL-DPEYPEE--------RLAYMLEDSGAQLLLSQSHLRLPLAQGVQ-VLDLDR 3179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 230 FEEALKErgqkcgvviksmqavedcgqenHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNvvadFSGFLKVTEKVIF 309
Cdd:PRK12316 3180 GDENYAE----------------------ANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSA----LSNHLCWMQQAYG 3233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 310 PRQDDVLISFLPLAHMFERVIQSVVYCHGGRVgfFQGDIRLLSDdmkalcptifpvvPRLLNRMYDKifSQANTPLKRWl 389
Cdd:PRK12316 3234 LGVGDRVLQFTTFSFDVFVEELFWPLMSGARV--VLAGPEDWRD-------------PALLVELINS--EGVDVLHAYP- 3295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 390 lefaakrkqaevrsgiirndSIWDELFFNKIQASLGGCVRMIVTGAAPASPtvlGFLRAALGCQVYEGYGQTECTAGCTF 469
Cdd:PRK12316 3296 --------------------SMLQAFLEEEDAHRCTSLKRIVCGGEALPAD---LQQQVFAGLPLYNLYGPTEATITVTH 3352
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 470 TTPGDWTSGH--VGAPLPCNHIKLVDVeELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGW------LHTGDI 541
Cdd:PRK12316 3353 WQCVEEGKDAvpIGRPIANRACYILDG-SLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDL 3431
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 542 GKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPV---AQIYVHGDSLKAFLV 598
Cdd:PRK12316 3432 ARYRADGVIEYIGRVDHQVKI-RGFRIELGEIEARLLEHPWVreaVVLAVDGRQLVAYVV 3490
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
266-615 |
1.27e-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: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 266 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVTEKVIFPRQDDVLISFLPLAhmFERVIQS--VVYCHGGRVGF 343
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMIEHQSLV----NLSHGLIKEYGITSSDRVLQFASIA--FDVAAEEiyVTLLSGATLVL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 344 FQGDIRLLSDDMKALCP----TIFPVVPrllnrmydkifsqantplkrwllefaakrkqaevrsgiirndSIWDELFFNK 419
Cdd:cd17644 178 RPEEMRSSLEDFVQYIQqwqlTVLSLPP------------------------------------------AYWHLLVLEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 420 IQASLGG--CVRMIVTGAAPASPTVLGFLRAALG--CQVYEGYGQTECTAGCTFTTPGDWTSGH-----VGAPLPCNHIK 490
Cdd:cd17644 216 LLSTIDLpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIANTQVY 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 491 LVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH--------TGDIGKWLPAGTLKVIDRKKHIFKL 562
Cdd:cd17644 296 ILD-ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKI 374
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 966948474 563 aQGEYVAPEKIENIYIRSQPVAQ--IYVHGDSL-KAFLVGIVVPDPEVMPSWAQKR 615
Cdd:cd17644 375 -RGFRIELGEIEAVLSQHNDVKTavVIVREDQPgNKRLVAYIVPHYEESPSTVELR 429
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
121-605 |
1.37e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 70.68 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGP--GDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 201 DK---PQKAVLLlehverKETPGLKLIILMD------------PFEEALKErgqkcgvviksmqavedcgQENHHAPVPP 265
Cdd:PRK07798 107 ERefaPRVAEVL------PRLPKLRTLVVVEdgsgndllpgavDYEDALAA-------------------GSPERDFGER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 266 QPDDLSIVCfTSGTTGNPKGAMLTHGNV-VADFSGFLKVTEKVIfprQDDVLIS----------FLPLAHMFERVIQSVV 334
Cdd:PRK07798 162 SPDDLYLLY-TGGTTGMPKGVMWRQEDIfRVLLGGRDFATGEPI---EDEEELAkraaagpgmrRFPAPPLMHGAGQWAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 335 YchggrVGFFQGDIRLLSDDMKalcptifpvvprllnrmydkiFSQANtplkrwLLEFAAKRKqaeVRSGIIRNDS---- 410
Cdd:PRK07798 238 F-----AALFSGQTVVLLPDVR---------------------FDADE------VWRTIEREK---VNVITIVGDAmarp 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 411 IWDELffnkiqASLGG----CVRMIVTGAAPASPTV-LGFLRAALGCQVYEGYGQTECTAGCTFTTPGDwtSGHVGAPL- 484
Cdd:PRK07798 283 LLDAL------EARGPydlsSLFAIASGGALFSPSVkEALLELLPNVVLTDSIGSSETGFGGSGTVAKG--AVHTGGPRf 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 485 -PCNHIKLVDvEELNYWAcKGEGEICV--RGPNVFKGYLKDPDRTKEALDS-DG--WLHTGDIGKWLPAGTLKVIDRKKH 558
Cdd:PRK07798 355 tIGPRTVVLD-EDGNPVE-PGSGEIGWiaRRGHIPLGYYKDPEKTAETFPTiDGvrYAIPGDRARVEADGTITLLGRGSV 432
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 966948474 559 IFKLAqGEYVAPEKIENIyIRSQPvaqiyvhgDSLKAFLVGivVPDP 605
Cdd:PRK07798 433 CINTG-GEKVFPEEVEEA-LKAHP--------DVADALVVG--VPDE 467
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
118-598 |
1.75e-12 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 70.26 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 118 YQWLsyqEVADRAEFLGSGLLQHNCKA-CTdqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADIS 196
Cdd:PLN02479 46 YTWA---QTYQRCRRLASALAKRSIGPgST---VAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 197 TVIVDkpQKAVLLLEH----VERKETPGLK---LIILMDP------FEEALKeRGqkcgvVIKSMQAVEDCGQEnhHAPV 263
Cdd:PLN02479 120 VVMVD--QEFFTLAEEalkiLAEKKKSSFKpplLIVIGDPtcdpksLQYALG-KG-----AIEYEKFLETGDPE--FAWK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 264 PPQPDDLSIVC-FTSGTTGNPKGAMLTH-GNVVADFSGFLkvtekvIFPRQDD-VLISFLPLAHmferviqsvvyCHGGr 340
Cdd:PLN02479 190 PPADEWQSIALgYTSGTTASPKGVVLHHrGAYLMALSNAL------IWGMNEGaVYLWTLPMFH-----------CNGW- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 341 vgffqgdirLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTplkrwllEFAAkrkqAEVRSGIIRNDSIWDELFfnki 420
Cdd:PLN02479 252 ---------CFTWTLAALCGTNICLRQVTAKAIYSAIANYGVT-------HFCA----APVVLNTIVNAPKSETIL---- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 421 qaSLGGCVRMIVTGAAPaSPTVLgFLRAALGCQVYEGYGQTEcTAG----CTFTTPGDWTSGHVGAPLPCNH-------- 488
Cdd:PLN02479 308 --PLPRVVHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSE-TYGpstvCAWKPEWDSLPPEEQARLNARQgvryigle 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 489 -IKLVDVEELNYWACKGE--GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQG 565
Cdd:PLN02479 383 gLDVVDTKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGG 460
|
490 500 510
....*....|....*....|....*....|...
gi 966948474 566 EYVAPEKIENIyirsqpvaqIYVHGDSLKAFLV 598
Cdd:PLN02479 461 ENISSLEVENV---------VYTHPAVLEASVV 484
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
121-606 |
2.32e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 69.96 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACytySMVvvplydtlgpGAIRYIINTAdistviV 200
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRA--GDGVAVLARNHRGFVLALYAA---GKV----------GARIILLNTG------F 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 201 DKPQkavlLLEHVERKetpGLKLIILMDPFEE---ALKERGQKCGVVIKSMQAVEDC------------GQENHHAPVPP 265
Cdd:PRK07788 134 SGPQ----LAEVAARE---GVKALVYDDEFTDllsALPPDLGRLRAWGGNPDDDEPSgstdetlddliaGSSTAPLPKPP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 266 QPDdlSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLkvtEKVIFPRQDDVLISflplAHMFerviqsvvycHGgrVGFFQ 345
Cdd:PRK07788 207 KPG--GIVILTSGTTGTPKGAPRPEPSPLAPLAGLL---SRVPFRAGETTLLP----APMF----------HA--TGWAH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 346 GDI-----------------RLLSDDMKALCPTIFpVVPRLLNRMYDkifsqantplkrwLLEfaakrkqaEVRSgiirn 408
Cdd:PRK07788 266 LTLamalgstvvlrrrfdpeATLEDIAKHKATALV-VVPVMLSRILD-------------LGP--------EVLA----- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 409 dsiwdelffnKIQASlggCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECtAGCTFTTPGDWT--SGHVGAPLPC 486
Cdd:PRK07788 319 ----------KYDTS---SLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEV-AFATIATPEDLAeaPGTVGRPPKG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 487 NHIKLVD-----VEElnywackGE-GEICVRGPNVFKGYlKDPdRTKEALdsDGWLHTGDIGKWLPAGTLKVIDRKKHIF 560
Cdd:PRK07788 385 VTVKILDengneVPR-------GVvGRIFVGNGFPFEGY-TDG-RDKQII--DGLLSSGDVGYFDEDGLLFVDGRDDDMI 453
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 966948474 561 kLAQGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDPE 606
Cdd:PRK07788 454 -VSGGENVFPAEVEDL---------LAGHPDVVEAAVIG--VDDEE 487
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
261-567 |
2.42e-12 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 69.93 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 261 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkvteKVIFP-RQDDVLISFLPLAHMFERV--IQSVVych 337
Cdd:PRK09274 167 PMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEAL-----REDYGiEPGEIDLPTFPLFALFGPAlgMTSVI--- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 338 ggrvgffqgdirllsDDMKALCP-TIFPvvprllnrmyDKIFSQ----------ANTPLKRWLLEFAAKRKQaevrsgii 406
Cdd:PRK09274 239 ---------------PDMDPTRPaTVDP----------AKLFAAierygvtnlfGSPALLERLGRYGEANGI-------- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 407 rndsiwdelffnkiqaSLGGCVRMIVTGAaPASPTVLGFLRAAL--GCQVYEGYGQTECTAGCT-------FTTPGDWTS 477
Cdd:PRK09274 286 ----------------KLPSLRRVISAGA-PVPIAVIERFRAMLppDAEILTPYGATEALPISSiesreilFATRAATDN 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 478 GH---VGAPLPCNHIKLVDV--EELNYWA-----CKGE-GEICVRGPNVFKGYLKDPDRTKEA--LDSDG--WLHTGDIG 542
Cdd:PRK09274 349 GAgicVGRPVDGVEVRIIAIsdAPIPEWDdalrlATGEiGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLG 428
|
330 340
....*....|....*....|....*.
gi 966948474 543 kWL-PAGTLKVIDRKKHIFKLAQGEY 567
Cdd:PRK09274 429 -YLdAQGRLWFCGRKAHRVETAGGTL 453
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
504-559 |
2.87e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 69.59 E-value: 2.87e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 966948474 504 GE--GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHI 559
Cdd:PRK08162 385 GEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDI 441
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
86-639 |
3.07e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 70.58 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 86 YDDARTMYQVFRRGLSISGNGPCLGFRKpnqpyQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAEL 165
Cdd:PRK12467 1570 YPLARLVHQLIEDQAAATPEAVALVFGE-----QELTYGELNRRANRLAHRLIALGVGP--EVLVGIAVERSLEMVVGLL 1642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 166 ACYTYSMVVVPLYDTLGPGAIRYIINTADIStvivdkpqkavLLLEHveRKETPGLKLIilmdpfeealkeRGQKCgVVI 245
Cdd:PRK12467 1643 AILKAGGAYVPLDPEYPRERLAYMIEDSGIE-----------LLLTQ--SHLQARLPLP------------DGLRS-LVL 1696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 246 KSMQAVEDcGQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFsgflKVTEKVIFPRQDDVLISFLPLAhm 325
Cdd:PRK12467 1697 DQEDDWLE-GYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRL----CATQEAYQLSAADVVLQFTSFA-- 1769
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 326 FERVIQSVVY--CHGGRVgffqgdirLLSDDMKALCPtifpvvprllNRMYDKIFSQANTplkrwLLEFAAKRKQAevrs 403
Cdd:PRK12467 1770 FDVSVWELFWplINGARL--------VIAPPGAHRDP----------EQLIQLIERQQVT-----TLHFVPSMLQQ---- 1822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 404 giirndsiwdelfFNKIQASLGGC--VRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAG-----CTFTTPGDW 475
Cdd:PRK12467 1823 -------------LLQMDEQVEHPlsLRRVVCGGEALEVEALRPWLERLPdTGLFNLYGPTETAVDvthwtCRRKDLEGR 1889
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 476 TSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL------DSDGWLH-TGDIGKWLPAG 548
Cdd:PRK12467 1890 DSVPIGQPIANLSTYILD-ASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgTVGSRLYrTGDLARYRADG 1968
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 549 TLKVIDRKKHIFKLaQGEYVAPEKIENiYIRSQP----VAQIYVHGDSLKAfLVGIVVPDPEVMPSWAQKRgieGTYADl 624
Cdd:PRK12467 1969 VIEYLGRIDHQVKI-RGFRIELGEIEA-RLREQGgvreAVVIAQDGANGKQ-LVAYVVPTDPGLVDDDEAQ---VALRA- 2041
|
570
....*....|....*.
gi 966948474 625 cTSKDLKKAILED-MV 639
Cdd:PRK12467 2042 -ILKNHLKASLPEyMV 2056
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
435-606 |
1.91e-11 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 67.02 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 435 AAPASPTVLGFLRAALGCQVYEGYGQTECTaGCTFTTPGDWTS--GHVGAPLPcNHIKLVDvEELNYWACKGEGEICVRG 512
Cdd:cd05929 253 AAPCPPWVKEQWIDWGGPIIWEYYGGTEGQ-GLTIINGEEWLThpGSVGRAVL-GKVHILD-EDGNEVPPGEIGEVYFAN 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 513 PNVFKgYLKDPDRTKEALDSDGWLHTGDIGkWLPA-GTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRsqpvaqiyvHGD 591
Cdd:cd05929 330 GPGFE-YTNDPEKTAAARNEGGWSTLGDVG-YLDEdGYLYLTDRRSDMI-ISGGVNIYPQEIENALIA---------HPK 397
|
170
....*....|....*
gi 966948474 592 SLKAFLVGivVPDPE 606
Cdd:cd05929 398 VLDAAVVG--VPDEE 410
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
152-295 |
5.50e-11 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 65.69 E-value: 5.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 152 VFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADiSTVIVDKPQkavlLLEHVERKETPGLKLIILMDPFE 231
Cdd:PRK04319 103 IFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSE-AKVLITTPA----LLERKPADDLPSLKHVLLVGEDV 177
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966948474 232 EAlkerGQKCGVVIKSMQAVEDcgqenHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVA 295
Cdd:PRK04319 178 EE----GPGTLDFNALMEQASD-----EFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQ 232
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
261-598 |
1.28e-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: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 261 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGN--VVADFSGflkvtEKVIFPRQDDVLIS--------------FLPLA- 323
Cdd:TIGR02262 154 KPAATQADDPAFWLYSSGSTGMPKGVVHTHSNpyWTAELYA-----RNTLGIREDDVCFSaaklffayglgnalTFPMSv 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 324 -----HMFERVIQSVVYchggrvgffqgdirllsDDMKALCPTIFPVVPRLlnrmYDKIFSQANTPlkrwllefaaKRKQ 398
Cdd:TIGR02262 229 gattvLMGERPTPDAVF-----------------DRLRRHQPTIFYGVPTL----YAAMLADPNLP----------SEDQ 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 399 AEVRsgiirndsiwdelffnkiqaslggcvrmIVTGAAPASPTVLGF-LRAALGCQVYEGYGQTEctAGCTFTT--PGDW 475
Cdd:TIGR02262 278 VRLR----------------------------LCTSAGEALPAEVGQrWQARFGVDIVDGIGSTE--MLHIFLSnlPGDV 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 476 TSGHVGAPLPCNHIKLVDveELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSdGWLHTGDigKWL--PAGTLKV 552
Cdd:TIGR02262 328 RYGTSGKPVPGYRLRLVG--DGGQDVADGEpGELLISGPSSATMYWNNRAKSRDTFQG-EWTRSGD--KYVrnDDGSYTY 402
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 966948474 553 IDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVHG----DSL---KAFLV 598
Cdd:TIGR02262 403 AGRTDDMLKVS-GIYVSPFEIESALIQHPAVLEAAVVGvadeDGLikpKAFVV 454
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
255-610 |
1.41e-10 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 64.33 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 255 GQENHHAPVPPQPDDLsivCFTSGTTGNPKGAMLTHGNVvadfsGFLKVTEKVI-----FPRQDDVLISFlPLAHmferv 329
Cdd:PRK12406 142 QQEPYDGPPVPQPQSM---IYTSGTTGHPKGVRRAAPTP-----EQAAAAEQMRaliygLKPGIRALLTG-PLYH----- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 330 iqSVVYCHGGRVGFFQGDIRLLS----DDMKALCP-----TIFpVVPRLLNRmydkifsqantplkrwLLEFAAKRKQAE 400
Cdd:PRK12406 208 --SAPNAYGLRAGRLGGVLVLQPrfdpEELLQLIErhritHMH-MVPTMFIR----------------LLKLPEEVRAKY 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 401 VRSgiirndsiwdelffnkiqaSLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--G 478
Cdd:PRK12406 269 DVS-------------------SL----RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE-SGAVTFATSEDALShpG 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 479 HVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNV--FKgYLKDPDRTKEaLDSDGWLHTGDIGkWLPA-GTLKVIDR 555
Cdd:PRK12406 325 TVGKAAPGAELRFVD-EDGRPLPQGEIGEIYSRIAGNpdFT-YHNKPEKRAE-IDRGGFITSGDVG-YLDAdGYLFLCDR 400
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 966948474 556 KKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAF---LVGIVVPDPEVMPS 610
Cdd:PRK12406 401 KRDMV-ISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFgeaLMAVVEPQPGATLD 457
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
119-613 |
2.05e-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: 63.54 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 119 QWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTV 198
Cdd:cd17649 11 QSLSYAELDARANRLAHRLRALGVGP--EVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 199 IvdkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqeNHHapvppqPDDLSIVCFTSG 278
Cdd:cd17649 89 L----------------------------------------------------------THH------PRQLAYVIYTSG 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 279 TTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPL----AHmfERVIQSVVycHGGRV----GFFQGDIRL 350
Cdd:cd17649 105 STGTPKGVAVSHGPLAA----HCQATAERYGLTPGDRELQFASFnfdgAH--EQLLPPLI--CGACVvlrpDELWASADE 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 351 LSDDMKALCPTIFPVVPRLLNRmydkifsqantpLKRWLLEFAAKRKQAevrsgiirndsiwdelffnkiqaslggcVRM 430
Cdd:cd17649 177 LAEMVRELGVTVLDLPPAYLQQ------------LAEEADRTGDGRPPS----------------------------LRL 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 431 IVTGAAPASPTvlgFLRAALGCQVY--EGYGQTECTAGCT-FTTPGD----WTSGHVGAPLPCNHIKLVDvEELNYWACK 503
Cdd:cd17649 217 YIFGGEALSPE---LLRRWLKAPVRlfNAYGPTEATVTPLvWKCEAGaaraGASMPIGRPLGGRSAYILD-ADLNPVPVG 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 504 GEGEICVRGPNVFKGYLKDPDRTKEAL--DSDG-----WLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENi 576
Cdd:cd17649 293 VTGELYIGGEGLARGYLGRPELTAERFvpDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-RGFRIELGEIEA- 370
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 966948474 577 YIRSQP----VAQIYVHGDSLKAfLVGIVVP-DPEVMPSWAQ 613
Cdd:cd17649 371 ALLEHPgvreAAVVALDGAGGKQ-LVAYVVLrAAAAQPELRA 411
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
268-574 |
2.86e-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: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 268 DDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVT-EKVIFPRQDDVLiSFLPLAhmFERVIQSVV--YCHGGRvgff 344
Cdd:cd17656 128 DDLLYIIYTSGTTGKPKGVQLEHKNMV----NLLHFErEKTNINFSDKVL-QFATCS--FDVCYQEIFstLLSGGT---- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 345 qgdIRLLSDDMKALCPTIFPVVPRllNRMYDKIFSQAntplkrwLLEFAAKRKQaevrsgiirndsiwdelFFNkiqaSL 424
Cdd:cd17656 197 ---LYIIREETKRDVEQLFDLVKR--HNIEVVFLPVA-------FLKFIFSERE-----------------FIN----RF 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 425 GGCVRMIVTGAAP--ASPTVLGFLRAAlGCQVYEGYG--QTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDvEELNY 499
Cdd:cd17656 244 PTCVKHIITAGEQlvITNEFKEMLHEH-NVHLHNHYGpsETHVVTTYTINPEAEIPElPPIGKPISNTWIYILD-QEQQL 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 500 WACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGW------LHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKI 573
Cdd:cd17656 322 QPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-RGYRIELGEI 400
|
.
gi 966948474 574 E 574
Cdd:cd17656 401 E 401
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
150-607 |
3.06e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 63.12 E-value: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 150 IGVFAQNRPEWII----AELACYTysmvVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAvlLLEHVErkeTPGLKLII 225
Cdd:PRK13388 55 VGVLLGNTPEMLFwlaaAALGGYV----LVGLNTTRRGAALAADIRRADCQLLVTDAEHRP--LLDGLD---LPGVRVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 226 LMDPfeealkergqkcgvviKSMQAVEDCGQENHHAPVppQPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLkVTE 305
Cdd:PRK13388 126 VDTP----------------AYAELVAAAGALTPHREV--DAMDPFMLIFTSGTTGAPKAVRCSHGRLA--FAGRA-LTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 306 KVIFPRqDDVLISFLPLAH----MferVIQSVVYCHGGRVGF--------FQGDIRLLSddmkalcPTIFPVVPRLLNrm 373
Cdd:PRK13388 185 RFGLTR-DDVCYVSMPLFHsnavM---AGWAPAVASGAAVALpakfsasgFLDDVRRYG-------ATYFNYVGKPLA-- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 374 YdkIFSQ------ANTPLKRWLLEFAAKRKQAEvrsgiirndsiwdelffnkiqaslggcvrmivtgaapasptvlgFLR 447
Cdd:PRK13388 252 Y--ILATperpddADNPLRVAFGNEASPRDIAE--------------------------------------------FSR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 448 AaLGCQVYEGYGQTEctAGCTFTTPGDWTSGHVGAPLPcnHIKLVDVEE---------------LNywACKGEGEICVR- 511
Cdd:PRK13388 286 R-FGCQVEDGYGSSE--GAVIVVREPGTPPGSIGRGAP--GVAIYNPETltecavarfdahgalLN--ADEAIGELVNTa 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 512 GPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYVHGd 591
Cdd:PRK13388 359 GAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYA- 435
|
490
....*....|....*.
gi 966948474 592 slkaflvgivVPDPEV 607
Cdd:PRK13388 436 ----------VPDERV 441
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
264-557 |
3.38e-10 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 63.10 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 264 PPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifpRQDDVLISFLPLAH-MferviqsvvychgGRVG 342
Cdd:PRK09192 172 RPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDGLKV---RPGDRCVSWLPFYHdM-------------GLVG 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 343 FF------QgdirlLSDDmkaLCPT-IFPVVP----RLLNRMYDKI-FSQAntplkrWLLEFAAKRkqAEVRSGIIRNDS 410
Cdd:PRK09192 236 FLltpvatQ-----LSVD---YLPTrDFARRPlqwlDLISRNRGTIsYSPP------FGYELCARR--VNSKDLAELDLS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 411 IWdelffnkiqaslggcvRMIVTGAAPASPTVL----------GF-LRAALGCqvyegYGQTECTAGCTFTTPG------ 473
Cdd:PRK09192 300 CW----------------RVAGIGADMIRPDVLhqfaeafapaGFdDKAFMPS-----YGLAEATLAVSFSPLGsgivve 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 474 ----DWTSGH------------------VGAPLPCNHIKLVDV--EELNYwacKGEGEICVRGPNVFKGYLKDPDRTKeA 529
Cdd:PRK09192 359 evdrDRLEYQgkavapgaetrrvrtfvnCGKALPGHEIEIRNEagMPLPE---RVVGHICVRGPSLMSGYFRDEESQD-V 434
|
330 340
....*....|....*....|....*...
gi 966948474 530 LDSDGWLHTGDIGkWLPAGTLKVIDRKK 557
Cdd:PRK09192 435 LAADGWLDTGDLG-YLLDGYLYITGRAK 461
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
271-584 |
4.13e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 62.80 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 271 SIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDIrl 350
Cdd:PRK07008 179 SSLCYTSGTTGNPKGALYSHRSTV--LHAYGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPLTGAKLVLPGPDL-- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 351 lsdDMKALcptifpvvprllnrmYDKIFSQANTplkrwlleFAAkrkqaevrsGIirnDSIWDELFFNKIQASLG-GCVR 429
Cdd:PRK07008 255 ---DGKSL---------------YELIEAERVT--------FSA---------GV---PTVWLGLLNHMREAGLRfSTLR 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 430 MIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPgdwTSGHVGAPLPCNH--------------IKLVDVE 495
Cdd:PRK07008 297 RTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLCKL---KWKHSQLPLDEQRkllekqgrviygvdMKIVGDD 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 496 --ELNyWACKGEGEICVRGPNVFKGYLKdpdRTKEALDsDGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAPEKI 573
Cdd:PRK07008 374 grELP-WDGKAFGDLQVRGPWVIDRYFR---GDASPLV-DGWFPTGDVATIDADGFMQITDRSKDVIK-SGGEWISSIDI 447
|
330
....*....|.
gi 966948474 574 ENIYIRSQPVA 584
Cdd:PRK07008 448 ENVAVAHPAVA 458
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
266-615 |
4.41e-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: 62.27 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 266 QPDDLSIVCFTSGTTGNPKGAMLTH---GNVVADFSGFLKVTEkvifprqDDVLISFLPLAhmFERVIQSVV--YCHGGR 340
Cdd:cd17652 91 TPDNLAYVIYTSGSTGRPKGVVVTHrglANLAAAQIAAFDVGP-------GSRVLQFASPS--FDASVWELLmaLLAGAT 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 341 vgffqgdirllsddmkaLCptifpVVPRLLnrmydkifSQANTPLKRWLlefaakrkQAEVRSGIIRNDSIWDELffnkI 420
Cdd:cd17652 162 -----------------LV-----LAPAEE--------LLPGEPLADLL--------REHRITHVTLPPAALAAL----P 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 421 QASLGGCVRMIVTGAAPASPTVLgflRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLVDvEELNY 499
Cdd:cd17652 200 PDDLPDLRTLVVAGEACPAELVD---RWAPGRRMINAYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYVLD-ARLRP 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 500 WACKGEGEICVRGPNVFKGYLKDPDRTKEALDSD------GWLH-TGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEK 572
Cdd:cd17652 276 VPPGVPGELYIAGAGLARGYLNRPGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKI-RGFRIELGE 354
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 966948474 573 IENIYIRSQPVAQ--IYVHGDSL-KAFLVGIVVPDPEVMPSWAQKR 615
Cdd:cd17652 355 VEAALTEHPGVAEavVVVRDDRPgDKRLVAYVVPAPGAAPTAAELR 400
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
260-619 |
6.18e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 63.05 E-value: 6.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 260 HAP-VPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPLAhmFERVIQSV--VYC 336
Cdd:PRK12316 4685 HDPaVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVN----HLHATGERYELTPDDRVLQFMSFS--FDGSHEGLyhPLI 4758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 337 HGGRVgffqgdirLLSDDMKALcPTifpvvpRLLNRMYDKIFSQANTPLKRW--LLEFAAKRKQ-AEVRsgiirndsiwd 413
Cdd:PRK12316 4759 NGASV--------VIRDDSLWD-PE------RLYAEIHEHRVTVLVFPPVYLqqLAEHAERDGEpPSLR----------- 4812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 414 elffnkiQASLGGcvrmivTGAAPASPTVLgfLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSG----HVGAPLPCNH 488
Cdd:PRK12316 4813 -------VYCFGG------EAVAQASYDLA--WRALKPVYLFNGYGPTETTVTVLlWKARDGDACGaaymPIGTPLGNRS 4877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 489 IKLVDVEeLNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSD------GWLH-TGDIGKWLPAGTLKVIDRKKHIFK 561
Cdd:PRK12316 4878 GYVLDGQ-LNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDpfgapgGRLYrTGDLARYRADGVIDYLGRVDHQVK 4956
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966948474 562 LaQGEYVAPEKIEnIYIRSQP-------VAQIYVHGdslkAFLVGIVVP-DPEVMPSWAQKRGIEG 619
Cdd:PRK12316 4957 I-RGFRIELGEIE-ARLREHPavreavvIAQEGAVG----KQLVGYVVPqDPALADADEAQAELRD 5016
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
255-576 |
7.69e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 61.71 E-value: 7.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 255 GQENHHAPVPPQPD-DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkVTEKVIFPRQDDVLISFLPLAH-Mferviqs 332
Cdd:PRK05851 138 AHTNRSASLTPPDSgGPAVLQGTAGSTGTPRTAILSPGAVLSNLRG---LNARVGLDAATDVGCSWLPLYHdM------- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 333 vvychggrvgffqGDIRLLSDDMKA----LCPTifpvvprllnrmydKIFSQAntPLK--RWLLEFAAKRKQA-EVRSGI 405
Cdd:PRK05851 208 -------------GLAFLLTAALAGaplwLAPT--------------TAFSAS--PFRwlSWLSDSRATLTAApNFAYNL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 406 IRNdsiwdelFFNKIQASLGGCVRMIVTGAAP----------ASPTVLGFLRAALGcqvyEGYGQTECTAGCTFTTPG-- 473
Cdd:PRK05851 259 IGK-------YARRVSDVDLGALRVALNGGEPvdcdgferfaTAMAPFGFDAGAAA----PSYGLAESTCAVTVPVPGig 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 474 ---------DWTSGH----VGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPdrtkeALDSDGWLHTGD 540
Cdd:PRK05851 328 lrvdevttdDGSGARrhavLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQA-----PIDPDDWFPTGD 402
|
330 340 350
....*....|....*....|....*....|....*.
gi 966948474 541 IGkWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENI 576
Cdd:PRK05851 403 LG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERV 436
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
121-585 |
7.91e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 62.49 E-value: 7.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGSGLLQHncKACTDQFIGVFAQNrPEWIIAELACYTYSMVVVPLYDtlgPGAIR--------YIINT 192
Cdd:PRK05691 41 LSYRDLDLRARTIAAALQAR--ASFGDRAVLLFPSG-PDYVAAFFGCLYAGVIAVPAYP---PESARrhhqerllSIIAD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 193 ADISTVIVDKP-QKAVLLLEHVERKETPGLkliILMDPFEEALKERGQKCGVviksmqavedcgqenhhapvppQPDDLS 271
Cdd:PRK05691 115 AEPRLLLTVADlRDSLLQMEELAAANAPEL---LCVDTLDPALAEAWQEPAL----------------------QPDDIA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 272 IVCFTSGTTGNPKGAMLTHGNVVADFS----GFlkvtekVIFPRQDDVLISFLPLAHMFERV------IQSVVYCHGGRV 341
Cdd:PRK05691 170 FLQYTSGSTALPKGVQVSHGNLVANEQlirhGF------GIDLNPDDVIVSWLPLYHDMGLIggllqpIFSGVPCVLMSP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 342 GFF--------------QGDIRLLSDDMKALCPtifpvvprllNRMYDKIFSQANtpLKRWLLEFAAkrkqaevrSGIIR 407
Cdd:PRK05691 244 AYFlerplrwleaiseyGGTISGGPDFAYRLCS----------ERVSESALERLD--LSRWRVAYSG--------SEPIR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 408 NDSIwdELFFNKIQ----------ASLG-GCVRMIVTGAAPA-SPTVLGFLRAALGCQVYEGyGQTECTAGCTFTTPGdw 475
Cdd:PRK05691 304 QDSL--ERFAEKFAacgfdpdsffASYGlAEATLFVSGGRRGqGIPALELDAEALARNRAEP-GTGSVLMSCGRSQPG-- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 476 tsghvgaplpcNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEA---LDSDGWLHTGDIGkWLPAGTLKV 552
Cdd:PRK05691 379 -----------HAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfveHDGRTWLRTGDLG-FLRDGELFV 446
|
490 500 510
....*....|....*....|....*....|...
gi 966948474 553 IDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQ 585
Cdd:PRK05691 447 TGRLKDML-IVRGHNLYPQDIEKTVEREVEVVR 478
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
121-606 |
9.14e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 61.46 E-value: 9.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLRE--GDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 201 DKPQKAVL--LLEHVERketpGLKLIILMD-------PFEEALKErgqkcgvviksmqavedcgqenhHAPVPPqPDDL- 270
Cdd:PRK08276 90 SAALADTAaeLAAELPA----GVPLLLVVAgpvpgfrSYEEALAA-----------------------QPDTPI-ADETa 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 271 -SIVCFTSGTTGNPKGAM--LTHGNVVADFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQgd 347
Cdd:PRK08276 142 gADMLYSSGTTGRPKGIKrpLPGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAPLRFGMSALALGGTVVVME-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 348 iRLLSDDMKALCP----TIFPVVPRLLNRMydkifsqantpLKrwLLEfaakrkqaEVRSgiiRNDSiwdelffnkiqAS 423
Cdd:PRK08276 220 -KFDAEEALALIEryrvTHSQLVPTMFVRM-----------LK--LPE--------EVRA---RYDV-----------SS 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 424 LggcvRMIVTGAAPASPTVLgflRAAL---GCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCNhIKLVDvEELN 498
Cdd:PRK08276 264 L----RVAIHAAAPCPVEVK---RAMIdwwGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGE-VRILD-EDGN 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 499 YWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkWLPA-GTLKVIDRKKHIFkLAQGEYVAPEKIENIY 577
Cdd:PRK08276 334 ELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVG-YLDEdGYLYLTDRKSDMI-ISGGVNIYPQEIENLL 411
|
490 500
....*....|....*....|....*....
gi 966948474 578 IRSQPVAQIYVHGdslkaflvgivVPDPE 606
Cdd:PRK08276 412 VTHPKVADVAVFG-----------VPDEE 429
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
274-590 |
9.32e-10 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 61.69 E-value: 9.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 274 CFTSGTTGNPKGAMLTHgnvvadfsgflkvtekvifpRQDdvlisflplahmferVIQSVVYCHGGRVGFFQGDirllsd 353
Cdd:PRK06018 183 CYTSGTTGDPKGVLYSH--------------------RSN---------------VLHALMANNGDALGTSAAD------ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 354 dmkalcpTIFPVVPrllnrMYdkifsQANTplkrWLLEFAAKRKQAEVRSGIIRND--SIWDELFFNKIQASLG------ 425
Cdd:PRK06018 222 -------TMLPVVP-----LF-----HANS----WGIAFSAPSMGTKLVMPGAKLDgaSVYELLDTEKVTFTAGvptvwl 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 426 -------------GCVRMIVTGAApASPTvlGFLRA--ALGCQVYEGYGQTECTAGCTFTT--------PGDWTSGHV-- 480
Cdd:PRK06018 281 mllqymekeglklPHLKMVVCGGS-AMPR--SMIKAfeDMGVEVRHAWGMTEMSPLGTLAAlkppfsklPGDARLDVLqk 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 481 -GAPLPCNHIKLVDVE--ELNyWACKGEGEICVRGPNVFKGYLKDPDrtkEALDSDGWLHTGDIGKWLPAGTLKVIDRKK 557
Cdd:PRK06018 358 qGYPPFGVEMKITDDAgkELP-WDGKTFGRLKVRGPAVAAAYYRVDG---EILDDDGFFDTGDVATIDAYGYMRITDRSK 433
|
330 340 350
....*....|....*....|....*....|...
gi 966948474 558 HIFKlAQGEYVAPEKIENIYIRSQPVAQIYVHG 590
Cdd:PRK06018 434 DVIK-SGGEWISSIDLENLAVGHPKVAEAAVIG 465
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
266-614 |
1.51e-09 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 60.65 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 266 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVaDFSGFLKVTEKVIFPRQDDVLISFLPLAHMFErviqsvVYCH---GGRVG 342
Cdd:cd17645 102 NPDDLAYVIYTSGSTGLPKGVMIEHHNLV-NLCEWHRPYFGVTPADKSLVYASFSFDASAWE------IFPHltaGAALH 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 343 FFQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTPLkRWLLEFAAKRKQAEVRsgiirndsiwdelffnkiqa 422
Cdd:cd17645 175 VVPSERRLDLDALNDYFNQEGITISFLPTGAAEQFMQLDNQSL-RVLLTGGDKLKKIERK-------------------- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 423 slggcvrmivtgaapasptvlgflraalGCQVYEGYGQTECTAGCT-FTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWA 501
Cdd:cd17645 234 ----------------------------GYKLVNNYGPTENTVVATsFEIDKPYANIPIGKPIDNTRVYILD-EALQLQP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 502 CKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIEN 575
Cdd:cd17645 285 IGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIEP 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 966948474 576 I---YIRSQPVAQIYVHGDSLKAFLVGIVVP----DPEVMPSWAQK 614
Cdd:cd17645 364 FlmnHPLIELAAVLAKEDADGRKYLVAYVTApeeiPHEELREWLKN 409
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
429-605 |
2.27e-09 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 60.39 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 429 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT---------FTT------PGD--WTSGHVGAPLPCNHIkl 491
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAEGLVNYTrlddsderiFTTqgrpmsPDDevWVADADGNPLPQGEV-- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 492 vdveelnywackgeGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHifklaQ----GEY 567
Cdd:PRK10946 381 --------------GRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGEK 441
|
170 180 190
....*....|....*....|....*....|....*...
gi 966948474 568 VAPEKIENIYIRsqpvaqiyvHGDSLKAFLVGIvvPDP 605
Cdd:PRK10946 442 IAAEEIENLLLR---------HPAVIHAALVSM--EDE 468
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
267-609 |
4.38e-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: 4.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 267 PDDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSG--FLKVTEkvifprqDDVLISFLplAHMFE-RVIQSVVYCHGGR 340
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVnlrTSLSEryFGRDNG-------DEAVLFFS--NYVFDfFVEQMTLALLNGQ 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 341 vgffqgDIRLLSDDMKALCPTIfpvvPRLLNRmyDKIFSQANTPLKRWLLEFAakrkqaevrsgiirndsiwdelffnki 420
Cdd:cd17648 164 ------KLVVPPDEMRFDPDRF----YAYINR--EKVTYLSGTPSVLQQYDLA--------------------------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 421 qaSLGGCVRMIVTGAAPASPtVLGFLRAALGCQVYEGYGQTEC--TAGCTFTTPGDWTSGHVGAPLPCNHIKLVDvEELN 498
Cdd:cd17648 205 --RLPHLKRVDAAGEEFTAP-VFEKLRSRFAGLIINAYGPTETtvTNHKRFFPGDQRFDKSLGRPVRNTKCYVLN-DAMK 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 499 YWACKGEGEICVRGPNVFKGYLKDPDRTKE-------------ALDSDGWLH-TGDIGKWLPAGTLKVIDRKKHIFKLaQ 564
Cdd:cd17648 281 RVPVGAVGELYLGGDGVARGYLNRPELTAErflpnpfqteqerARGRNARLYkTGDLVRWLPSGELEYLGRNDFQVKI-R 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 966948474 565 GEYVAPEKIENIY-----IRSQPVAQIYVHGDSLKA---FLVGIVVPDPEVMP 609
Cdd:cd17648 360 GQRIEPGEVEAALasypgVRECAVVAKEDASQAQSRiqkYLVGYYLPEPGHVP 412
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
262-607 |
3.98e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 56.56 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 262 PVPPQPDDlSIVCFTSGTTGNPKG--------AMLTHGN-VVADFSGFLKVTEKvifprqdDVLISFLPLAHMFERVIQS 332
Cdd:PRK13390 143 RLTEQPCG-AVMLYSSGTTGFPKGiqpdlpgrDVDAPGDpIVAIARAFYDISES-------DIYYSSAPIYHAAPLRWCS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 333 VVYCHGGRVGFFQG-DIRLLSDDMKALCPTIFPVVPRLLNRMYdkifsqantplkrwllefaakRKQAEVRSgiiRNDSi 411
Cdd:PRK13390 215 MVHALGGTVVLAKRfDAQATLGHVERYRITVTQMVPTMFVRLL---------------------KLDADVRT---RYDV- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 412 wdelffnkiqASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVG-APLPCNH 488
Cdd:PRK13390 270 ----------SSL----RAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGrSVLGDLH 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 489 IKLVDVEELNywackgEGEIcvrGPNVFK------GYLKDPDRTKEALDSDG--WLHTGDIGKWLPAGTLKVIDRKKHIF 560
Cdd:PRK13390 335 ICDDDGNELP------AGRI---GTVYFErdrlpfRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI 405
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 966948474 561 kLAQGEYVAPEKIENIYIRSQPVAQIYVHGdslkaflvgivVPDPEV 607
Cdd:PRK13390 406 -ISGGVNIYPQETENALTMHPAVHDVAVIG-----------VPDPEM 440
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
125-621 |
7.43e-08 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 55.40 E-value: 7.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 125 EVADRAEFLGSGLLQHNCKactdqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQ 204
Cdd:PRK05857 50 EVGGLAADLRAQSVSRGSR------VLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVAPGS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 205 KAVLLLEHVERKETPGLKLIILMDPFEEAlkergqkCGVVIKSMQAVEDCGQenhhapvppqpDDLSIVCFTSGTTGNPK 284
Cdd:PRK05857 124 KMASSAVPEALHSIPVIAVDIAAVTRESE-------HSLDAASLAGNADQGS-----------EDPLAMIFTSGTTGEPK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 285 GAMLTHGNVVA--DF---SGFLKVTEKVifprqDDVLISFLPLAHM------FERVIQSVVYCHGGRVGFFQGDIrLLSD 353
Cdd:PRK05857 186 AVLLANRTFFAvpDIlqkEGLNWVTWVV-----GETTYSPLPATHIgglwwiLTCLMHGGLCVTGGENTTSLLEI-LTTN 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 354 DMKALCptifpVVPRLLNRM-YDKIFSQANTPLKRWLLEFAAKRKQAEVRSgiirndsiwdelffnkIQAslggcvrmiv 432
Cdd:PRK05857 260 AVATTC-----LVPTLLSKLvSELKSANATVPSLRLVGYGGSRAIAADVRF----------------IEA---------- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 433 TGAAPAsptvlgflraalgcQVYeGYGQTECTAGCTFTTPGDWT---SGHVGAPLPCNHIKLVDVEELNYWACKGE---- 505
Cdd:PRK05857 309 TGVRTA--------------QVY-GLSETGCTALCLPTDDGSIVkieAGAVGRPYPGVDVYLAATDGIGPTAPGAGpsas 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 506 -GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPV- 583
Cdd:PRK05857 374 fGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGGVNIAPDEVDRIAEGVSGVr 451
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 966948474 584 -AQIYVHGDSLKAFLVGI-VVPDPEVMPSWAQ--KRGIEGTY 621
Cdd:PRK05857 452 eAACYEIPDEEFGALVGLaVVASAELDESAARalKHTIAARF 493
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
86-615 |
1.45e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 55.35 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 86 YDDARTMYQVFRRGLSISGNGPCLGFRKpnqpyQWLSYQEVADRAEFLGSGLLQhnCKACTDQFIGVFAQNRPEWIIAEL 165
Cdd:PRK12316 507 YPLQRGVHRLFEEQVERTPEAPALAFGE-----ETLDYAELNRRANRLAHALIE--RGVGPDVLVGVAMERSIEMVVALL 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 166 ACYTYSMVVVPLYDTLGPGAIRYIINTADIstvivdkpqkAVLLLEHVERKETP---GLKLIILMDP--FEEALKERGQK 240
Cdd:PRK12316 580 AILKAGGAYVPLDPEYPAERLAYMLEDSGV----------QLLLSQSHLGRKLPlaaGVQVLDLDRPaaWLEGYSEENPG 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 241 CGVViksmqavedcgqenhhapvppqPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifprqddvlisfL 320
Cdd:PRK12316 650 TELN----------------------PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYG--------------L 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 321 PLAhmfERVIQSVVYCHGGRVGFFQGDI----RLLsddmkalcptifpVVPRLLNRMYDKIFSQANTPLKRwLLEFAAKR 396
Cdd:PRK12316 694 GVG---DTVLQKTPFSFDVSVWEFFWPLmsgaRLV-------------VAAPGDHRDPAKLVELINREGVD-TLHFVPSM 756
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 397 KQAEVRSGIIrndsiwdelffnkiqASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT 476
Cdd:PRK12316 757 LQAFLQDEDV---------------ASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEG 821
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 477 SGHV--GAPLPCNHIKLVDVeELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL------DSDGWLHTGDIGKWLPAG 548
Cdd:PRK12316 822 GDSVpiGRPIANLACYILDA-NLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFvpspfvAGERMYRTGDLARYRADG 900
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966948474 549 TLKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAfLVGIVVPD------PEVMPSWAQKR 615
Cdd:PRK12316 901 VIEYAGRIDHQVKL-RGLRIELGEIEARLLEHPWVREAAVLAVDGKQ-LVGYVVLEseggdwREALKAHLAAS 971
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
416-598 |
2.07e-07 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 54.27 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 416 FFNKIqasLGGC-------VRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTEctAGCTFT--TPGDWTSGHVGAPLP 485
Cdd:PRK06060 246 FFARV---IDSCspdsfrsLRCVVSAGEALELGLAERLMEFFGgIPILDGIGSTE--VGQTFVsnRVDEWRLGTLGRVLP 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 486 CNHIKLVDVEELNYwACKGEGEICVRGPNVFKGYLKDPDrtkEALDSDGWLHTGDIGK-----WLPAGTlkvidrKKHIF 560
Cdd:PRK06060 321 PYEIRVVAPDGTTA-GPGVEGDLWVRGPAIAKGYWNRPD---SPVANEGWLDTRDRVCidsdgWVTYRC------RADDT 390
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 966948474 561 KLAQGEYVAPEKIENIYIRSQPVAQIYVHG-------DSLKAFLV 598
Cdd:PRK06060 391 EVIGGVNVDPREVERLIIEDEAVAEAAVVAvrestgaSTLQAFLV 435
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
268-615 |
2.14e-07 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 53.51 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 268 DDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkVTEKVIFPRQddVLISfLPLAHM--FERVIQSVV---------YC 336
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTASADA---THDRLGGPGQ--WLLA-LPAHHIagLQVLVRSVIagsepveldVS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 337 HGGRVGFFQGDIRLLSDDMK--ALCPTifpvvpRLLNRMYDKIFSQAntplkrwLLEFAAkrkqaevrsgiirndsiwde 414
Cdd:PRK07824 109 AGFDPTALPRAVAELGGGRRytSLVPM------QLAKALDDPAATAA-------LAELDA-------------------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 415 lffnkiqaslggcvrmIVTGAAPASPTVlgfLRAA--LGCQVYEGYGQTECTAGCTFTtpgdwtsghvGAPLPCNHIKLV 492
Cdd:PRK07824 156 ----------------VLVGGGPAPAPV---LDAAaaAGINVVRTYGMSETSGGCVYD----------GVPLDGVRVRVE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 493 DveelnywackgeGEICVRGPNVFKGY--LKDPDrtkeALDSDGWLHTGDIGKwLPAGTLKVIDRKKHIFKLAqGEYVAP 570
Cdd:PRK07824 207 D------------GRIALGGPTLAKGYrnPVDPD----PFAEPGWFRTDDLGA-LDDGVLTVLGRADDAISTG-GLTVLP 268
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 966948474 571 EKIENIYIRSQPVAQIYVHG---DSLKAFLVGIVVPDPEVMPSWAQKR 615
Cdd:PRK07824 269 QVVEAALATHPAVADCAVFGlpdDRLGQRVVAAVVGDGGPAPTLEALR 316
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
422-606 |
2.28e-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: 53.68 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 422 ASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEC-TAGCTFTTPGDWT-SGHVGAPLPCNHIKLVDvEELNY 499
Cdd:cd05973 201 ARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELgMVLANHHALEHPVhAGSAGRAMPGWRVAVLD-DDGDE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 500 WACKGEGEICV---RGPNV-FKGYLKDPDRTKealdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIEN 575
Cdd:cd05973 280 LGPGEPGRLAIdiaNSPLMwFRGYQLPDTPAI----DGGYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFDVES 354
|
170 180 190
....*....|....*....|....*....|.
gi 966948474 576 IYIRSQPVAQIYVhgdslkaflvgIVVPDPE 606
Cdd:cd05973 355 ALIEHPAVAEAAV-----------IGVPDPE 374
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
121-324 |
3.22e-07 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 53.72 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAE-----FLGSGLLQHNCkactdqfIGVFAQNRPEWIIAELACyTYSMVVVPLYDT-LGPGAIRYIINTAD 194
Cdd:PRK08279 63 ISYAELNARANryahwAAARGVGKGDV-------VALLMENRPEYLAAWLGL-AKLGAVVALLNTqQRGAVLAHSLNLVD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 195 ISTVIVDKPqkavlLLEHVE--RKETPGLKLIILMDPFEEALKERgqkcgvVIKSMQAVEDCGQENHHAPVPPQPDDLSI 272
Cdd:PRK08279 135 AKHLIVGEE-----LVEAFEeaRADLARPPRLWVAGGDTLDDPEG------YEDLAAAAAGAPTTNPASRSGVTAKDTAF 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 966948474 273 VCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAH 324
Cdd:PRK08279 204 YIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLR----LTPDDVLYCCLPLYH 251
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
226-325 |
6.09e-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: 52.68 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 226 LMDPFEE---ALKERGQKCGVVIKSM--QAVEDCGQENHHAPVPPQPDDLS---------IVCFTSGTTGNPKGAMLTHG 291
Cdd:cd05938 88 LQEAVEEvlpALRADGVSVWYLSHTSntEGVISLLDKVDAASDEPVPASLRahvtikspaLYIYTSGTTGLPKAARISHL 167
|
90 100 110
....*....|....*....|....*....|....
gi 966948474 292 NVVAdFSGFLKVTeKVifpRQDDVLISFLPLAHM 325
Cdd:cd05938 168 RVLQ-CSGFLSLC-GV---TADDVIYITLPLYHS 196
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
261-324 |
1.23e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 51.87 E-value: 1.23e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966948474 261 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADF----SGFLKVTEKVifPRQDDVLISFLPLAH 324
Cdd:PRK05850 153 DARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFeqlmSDYFGDTGGV--PPPDTTVVSWLPFYH 218
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
269-606 |
1.87e-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: 50.82 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 269 DLSIVCFTSGTTGNPKGAMLTH-----GNVVADFSGFLKvtekvifprQDDVLISFLPLAHMfERVIQSVVYC--HGGRV 341
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHrrawrGGAFFAGSGGAL---------PSDVLYTCLPLYHS-TALIVGWSAClaSGATL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 342 GF--------FQGDIRllsddmKALCpTIFPVVPRLLnrmydkifsqantplkRWLLefAAKRKQAEVRsgiirndsiwd 413
Cdd:cd05940 152 VIrkkfsasnFWDDIR------KYQA-TIFQYIGELC----------------RYLL--NQPPKPTERK----------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 414 elffNKIQASLGGCVRmivtgaapasPTVLGFLRAALGC-QVYEGYGQTECTAGCT--FTTPGdwTSGHVGAPLPCNH-I 489
Cdd:cd05940 196 ----HKVRMIFGNGLR----------PDIWEEFKERFGVpRIAEFYAATEGNSGFInfFGKPG--AIGRNPSLLRKVApL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 490 KLV--DVEELNYW---------ACKGE-----GEICVRGPnvFKGYLKDPDRTKEAL-----DSDGWLHTGDIGKWLPAG 548
Cdd:cd05940 260 ALVkyDLESGEPIrdaegrcikVPRGEpglliSRINPLEP--FDGYTDPAATEKKILrdvfkKGDAWFNTGDLMRLDGEG 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966948474 549 TLKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYVHGDSL-----KAFLVGIVVPDPE 606
Cdd:cd05940 338 FWYFVDRLGDTFRW-KGENVSTTEVAAVLGAFPGVEEANVYGVQVpgtdgRAGMAAIVLQPNE 399
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
483-543 |
2.41e-06 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 50.66 E-value: 2.41e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966948474 483 PLPCNHIK-----LVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL-DSDGW--LHTGDIGK 543
Cdd:PRK04813 317 RLPIGYAKpdsplLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGY 385
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
275-575 |
3.11e-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: 49.71 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 275 FTSGTTGNPKGAMLTHGNVVADFsgflKVTEKVIFPRQDDVLISFLPLAH-MFERVIQSVVYCHGGRVGFFQGDIRLLSD 353
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESF----VCNEDLFNISGEDAILAPGPLSHsLFLYGAISALYLGGTFIGQRKFNPKSWIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 354 DMKALCPTIFPVVPRLLNRMYdkifsQANTPlkrwllefaakrkQAEVRSgIIRNDSIWDELFFNKIQAslggcvrmivt 433
Cdd:cd17633 83 KINQYNATVIYLVPTMLQALA-----RTLEP-------------ESKIKS-IFSSGQKLFESTKKKLKN----------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 434 gaapasptvlGFLRAALgcqvYEGYGQTEcTAGCTFTTPGD-WTSGHVGAPLPCNHIKLVDVEElnywacKGEGEICVRG 512
Cdd:cd17633 133 ----------IFPKANL----IEFYGTSE-LSFITYNFNQEsRPPNSVGRPFPNVEIEIRNADG------GEIGKIFVKS 191
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966948474 513 PNVFKGYLKDPDRTKealdsDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIEN 575
Cdd:cd17633 192 EMVFSGYVRGGFSNP-----DGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIES 248
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
265-614 |
8.32e-06 |
|
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: 48.53 E-value: 8.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 265 PQPDDLSIVCfTSGTTGNPKGAMLTHGNV------VADFSGFLKVTEKVIFPRQ----DDVLISFLPLAH-------MFE 327
Cdd:cd05924 1 RSADDLYILY-TGGTTGMPKGVMWRQEDIfrmlmgGADFGTGEFTPSEDAHKAAaaaaGTVMFPAPPLMHgtgswtaFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 328 RVIQSVVYCHGGRvgfFQGD--IRLLSddmKALCPTIFPVVPRLLNRMYDKIFSQANTPLkrwllefaakrkqaevrsgi 405
Cdd:cd05924 80 LLGGQTVVLPDDR---FDPEevWRTIE---KHKVTSMTIVGDAMARPLIDALRDAGPYDL-------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 406 irndsiwdelffnkiqASLggcvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFTTPGdwtSGHVGAPL 484
Cdd:cd05924 134 ----------------SSL----FAISSGGALLSPEVKqGLLELVPNITLVDAFGSSETGFTGSGHSAG---SGPETGPF 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 485 -PCNHIKLVDVEELNYWACK--GEGEICVRGpNVFKGYLKDPDRTKEA---LDSDGWLHTGDIGKWLPAGTLKVIDRKKH 558
Cdd:cd05924 191 tRANPDTVVLDDDGRVVPPGsgGVGWIARRG-HIPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGRGSV 269
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 966948474 559 IFKLAqGEYVAPEKIENIyIRSQP-VAQIYVHGdslkaflvgivVPDPEvmpsWAQK 614
Cdd:cd05924 270 CINTG-GEKVFPEEVEEA-LKSHPaVYDVLVVG-----------RPDER----WGQE 309
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
122-610 |
3.10e-05 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 47.19 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 122 SYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIIntADISTVIVd 201
Cdd:cd17634 86 SYRELHREVCRFAGTLLDLGVKK--GDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRI--IDSSSRLL- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 202 kpqkaVLLLEHVERKETPGLKLIIlmdpfEEALKERGQKC-GVVIKSMQAVEDCGQEN--------------HHAPVPPQ 266
Cdd:cd17634 161 -----ITADGGVRAGRSVPLKKNV-----DDALNPNVTSVeHVIVLKRTGSDIDWQEGrdlwwrdliakaspEHQPEAMN 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 267 PDDLSIVCFTSGTTGNPKGAMLTHGnvvadfsGFLkvtekvIFPRQDdvlisflpLAHMFERVIQSVVYChGGRVGFFQG 346
Cdd:cd17634 231 AEDPLFILYTSGTTGKPKGVLHTTG-------GYL------VYAATT--------MKYVFDYGPGDIYWC-TADVGWVTG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 347 DIRLLSDDMkALCPTIF-----PVVPRlLNRMYDKIFSQANTPLkrWLLEFAAKRKQAEVRSGIIRNDsiwdelffnkiQ 421
Cdd:cd17634 289 HSYLLYGPL-ACGATTLlyegvPNWPT-PARMWQVVDKHGVNIL--YTAPTAIRALMAAGDDAIEGTD-----------R 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 422 ASLggcvRMIVTGAAPASPTVLGFLRAALG---CQVYEGYGQTECTAGCTFTTPG--DWTSGHVGAPLPCNHIKLVDvEE 496
Cdd:cd17634 354 SSL----RILGSVGEPINPEAYEWYWKKIGkekCPVVDTWWQTETGGFMITPLPGaiELKAGSATRPVFGVQPAVVD-NE 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 497 LNYWACKGEGEICVRG--PNVFKGYLKDPDRTKEALDS--DGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEK 572
Cdd:cd17634 429 GHPQPGGTEGNLVITDpwPGQTRTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVA-GHRLGTAE 507
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 966948474 573 IENIYIRSQPVAQIYVHG--DSLKA-FLVGIVVPDPEVMPS 610
Cdd:cd17634 508 IESVLVAHPKVAEAAVVGipHAIKGqAPYAYVVLNHGVEPS 548
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
425-607 |
4.43e-05 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 46.68 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 425 GGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFT-TPGDWTSG--HVGAPLPCNHIKLVDVE--ELNy 499
Cdd:PRK13382 311 GRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATE--AGMIATaTPADLRAApdTAGRPAEGTEIRILDQDfrEVP- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 500 wacKGE-GEICVRGPNVFKGYlkDPDRTKEAldSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIyI 578
Cdd:PRK13382 388 ---TGEvGTIFVRNDTQFDGY--TSGSTKDF--HDGFMASGDVGYLDENGRLFVVGRDDEMI-VSGGENVYPIEVEKT-L 458
|
170 180 190
....*....|....*....|....*....|....*..
gi 966948474 579 RSQP-VAQIYV-------HGDSLKAFlvgiVVPDPEV 607
Cdd:PRK13382 459 ATHPdVAEAAVigvddeqYGQRLAAF----VVLKPGA 491
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
267-598 |
7.19e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 46.31 E-value: 7.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 267 PDDLSIVCFTSGTTGNPKGAMLT-HGNVVADFSG--FLKVTEKVIFPRQ-----DDVLISFLPlAHMFerviqsvvychG 338
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEqRGMLNNQLSKvpYLALSEADVIAQTasqsfDISVWQFLA-APLF-----------G 3935
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 339 GRVGFFQGDIrllSDDMKALCP-------TIFPVVPRLLNRMydkifsqantplkrwllefaakrkqaevrsgiIRNDsi 411
Cdd:PRK05691 3936 ARVEIVPNAI---AHDPQGLLAhvqaqgiTVLESVPSLIQGM--------------------------------LAED-- 3978
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 412 wdelffnkiQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF------TTPGDWTSghVGAPLP 485
Cdd:PRK05691 3979 ---------RQALDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFfrvdlaSTRGSYLP--IGSPTD 4047
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 486 CNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL-------DSDGWLHTGDIGKWLPAGTLKVIDRKKH 558
Cdd:PRK05691 4048 NNRLYLLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFvphpfgaPGERLYRTGDLARRRSDGVLEYVGRIDH 4126
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 966948474 559 I-----FKLAQGEYVApEKIENIYIRSQPVA-QIYVHGDSLKAFLV 598
Cdd:PRK05691 4127 QvkirgYRIELGEIEA-RLHEQAEVREAAVAvQEGVNGKHLVGYLV 4171
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
417-695 |
9.75e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 45.54 E-value: 9.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 417 FNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPGDWTSGHVGAPLPCNHIKLVDVEE 496
Cdd:PRK07638 245 LYKENRVIENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSF-VTALVDEESERRPNSVGRPFHNVQVRICNE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 497 LNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEaLDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIEN 575
Cdd:PRK07638 324 AGEEVQKGEiGTVYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIES 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 576 IYIRSQPVAQIYVHGdslkaflvgivVPDpevmPSWAQKRG--IEGTyadlCTSKDLKKAILEDmvrlgkesgLHSFEQV 653
Cdd:PRK07638 402 VLHEHPAVDEIVVIG-----------VPD----SYWGEKPVaiIKGS----ATKQQLKSFCLQR---------LSSFKIP 453
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 966948474 654 KAIHIhsdmfsVQNGLLTPTLKAKRPELreyfKKQIEELYSI 695
Cdd:PRK07638 454 KEWHF------VDEIPYTNSGKIARMEA----KSWIENQEKI 485
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
418-582 |
1.38e-04 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 45.11 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 418 NKIQASLGGCVRMIVTGAAPASPTV----LGFLRA--ALGCQVYEGYGqTECTAGCTFTTPGDWTSGHVGAPLPCNHI-K 490
Cdd:cd05915 263 ESTGHRLKTLRRLVVGGSAAPRSLIarfeRMGVEVrqGYGLTETSPVV-VQNFVKSHLESLSEEEKLTLKAKTGLPIPlV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 491 LVDVEELNYWACKGEGE----ICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGE 566
Cdd:cd05915 342 RLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG-GE 420
|
170
....*....|....*.
gi 966948474 567 YVAPEKIENIyIRSQP 582
Cdd:cd05915 421 WISSVDLENA-LMGHP 435
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
121-598 |
2.50e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 44.22 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 121 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PRK13383 61 LSYRELQRATESLARRLTRDGVAP--GRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 201 DkpqkavlllehverketpglkliilmDPFEEALKERGQKCGVVIKSMQAVEDCGQENHHAPVPpqpddlSIVCFTSGTT 280
Cdd:PRK13383 139 D--------------------------NEFAERIAGADDAVAVIDPATAGAEESGGRPAVAAPG------RIVLLTSGTT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 281 GNPKGAmlthgnvvadfsgflkvtekvifPRQDDVLISFLPLAHMFERVIQSVvychGGRVGFFQGDIRLLSDDMKALCP 360
Cdd:PRK13383 187 GKPKGV-----------------------PRAPQLRSAVGVWVTILDRTRLRT----GSRISVAMPMFHGLGLGMLMLTI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 361 TIFPVVprLLNRMYDKIFSQANTPLKRwllefaakrkqAEVRSGI-IRNDSIWDelFFNKIQA-SLGGCVRMIVTGAAPA 438
Cdd:PRK13383 240 ALGGTV--LTHRHFDAEAALAQASLHR-----------ADAFTAVpVVLARILE--LPPRVRArNPLPQLRVVMSSGDRL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 439 SPTVLGFLRAALGCQVYEGYGQTECTAGcTFTTPG---DWTSGhVGAPLPCNHIKLVDVEELNYwACKGEGEICVRGPNV 515
Cdd:PRK13383 305 DPTLGQRFMDTYGDILYNGYGSTEVGIG-ALATPAdlrDAPET-VGKPVAGCPVRILDRNNRPV-GPRVTGRIFVGGELA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 516 FKGYlkdPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYV------- 588
Cdd:PRK13383 382 GTRY---TDGGGKAV-VDGMTSTGDMGYLDNAGRLFIVGREDDMI-ISGGENVYPRAVENALAAHPAVADNAVigvpder 456
|
490
....*....|
gi 966948474 589 HGDSLKAFLV 598
Cdd:PRK13383 457 FGHRLAAFVV 466
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
268-599 |
4.19e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.00 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 268 DDLSIVCFTSGTTGNPKGAMLTHGnVVADFSGFLKVTEKVifpRQDDVLISFLPLAhmFErviQSVVYCH-----GGRVG 342
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNTHA-ALAERLQWMQATYAL---DDSDVLMQKAPIS--FD---VSVWECFwplitGCRLV 1343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 343 FF----QGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTPLKRWlleFAAkrkqAEVRSGIIRNdsiwdelffn 418
Cdd:PRK05691 1344 LAgpgeHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRL---FSG----GEALPAELRN---------- 1406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 419 kiqaslggcvrmivtgaapaspTVLGFLRAAlgcQVYEGYGQTECTAGCTF--TTPGDWTSGHVGAPLPCNHIKLVDvEE 496
Cdd:PRK05691 1407 ----------------------RVLQRLPQV---QLHNRYGPTETAINVTHwqCQAEDGERSPIGRPLGNVLCRVLD-AE 1460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 497 LNYWACKGEGEICVRGPNVFKGYLKDPDRTKE-----ALDSDG--WLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVA 569
Cdd:PRK05691 1461 LNLLPPGVAGELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL-RGFRVE 1539
|
330 340 350
....*....|....*....|....*....|..
gi 966948474 570 PEKIENIYIRSQPVAQ--IYVHGDSLKAFLVG 599
Cdd:PRK05691 1540 PEEIQARLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
267-590 |
4.41e-04 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 43.19 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 267 PDDLSIVCFTSGTTGNPKGAMLTHG-NVVADfsgflKVTEKVIFPRQDDVLISFLPLAHMFERVIqSVVYC--HGGRVGF 343
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISWRrTLVTS-----NLLSHDLNLKNGDRTYTCMPLYHGTAAFL-GACNClmSGGTLAL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 344 --------FQGDIRllsdDMKAlcpTIFPVVPRLLnrmydkifsqantplkRWLLEFAAkrkqaevrsgiirndSIWDEL 415
Cdd:cd05937 160 srkfsasqFWKDVR----DSGA---TIIQYVGELC----------------RYLLSTPP---------------SPYDRD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 416 ffNKIQASLGGCVRmivtgaapasPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKL--- 491
Cdd:cd05937 202 --HKVRVAWGNGLR----------PDIWERFRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKFenq 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 492 -----VDVEELNYW----------ACKGE-GEICVRGPNV----FKGYLKDPDRTKEAL------DSDGWLHTGDIGKWL 545
Cdd:cd05937 270 vvlvkMDPETDDPIrdpktgfcvrAPVGEpGEMLGRVPFKnreaFQGYLHNEDATESKLvrdvfrKGDIYFRTGDLLRQD 349
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 966948474 546 PAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYVHG 590
Cdd:cd05937 350 ADGRWYFLDRLGDTFRW-KSENVSTTEVADVLGAHPDIAEANVYG 393
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
263-294 |
5.67e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 43.49 E-value: 5.67e-04
10 20 30
....*....|....*....|....*....|..
gi 966948474 263 VPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVV 294
Cdd:PRK10252 593 QLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIV 624
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
517-605 |
2.27e-03 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 41.57 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 517 KGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIyIRSQP-VAQIYVH 589
Cdd:PRK10252 814 QGYLGRPDLTASRFIADPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKI-RGQRIELGEIDRA-MQALPdVEQAVTH 891
|
90 100
....*....|....*....|....*..
gi 966948474 590 -----------GDSLKafLVGIVVPDP 605
Cdd:PRK10252 892 acvinqaaatgGDARQ--LVGYLVSQS 916
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
113-294 |
3.66e-03 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 40.26 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 113 KPNQP-YQWL----SYQEVADRAEFLGSGLLQHncKACTDQFIGVFAQNRPEWIIAELAC----YTYsmvvVPLYDTLGP 183
Cdd:PRK04813 15 QPDFPaYDYLgeklTYGQLKEDSDALAAFIDSL--KLPDKSPIIVFGHMSPEMLATFLGAvkagHAY----IPVDVSSPA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966948474 184 GAIRYIINTADISTVI--VDKPqkavlllehVERKETPGLKLIILMDPFEEalkergqkcGVVIKSMQAVEDcgqenhha 261
Cdd:PRK04813 89 ERIEMIIEVAKPSLIIatEELP---------LEILGIPVITLDELKDIFAT---------GNPYDFDHAVKG-------- 142
|
170 180 190
....*....|....*....|....*....|...
gi 966948474 262 pvppqpDDLSIVCFTSGTTGNPKGAMLTHGNVV 294
Cdd:PRK04813 143 ------DDNYYIIFTSGTTGKPKGVQISHDNLV 169
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