|
Name |
Accession |
Description |
Interval |
E-value |
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
141-719 |
0e+00 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 944.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 141 QPYQWLSYKEVAERAEALGSGLLQQGCKPCTEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADI 220
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 221 STVICDKpdkartlldhverretpglssiilmdpfekeltergrrcGVRIQSMQEVEDCGRENRRAPVPPRPEDLSIVCF 300
Cdd:cd05927 81 SIVFCDA---------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 301 TSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWSPTCEDVHISYLPLAHMFERMVQSVVYCHGGRIGFFQGDIRLLSDDM 380
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 381 KALRPTIFPVVPRLLNRMYDKIFS--QADTSLKRWVLEFAARRKKAEVRNGIIRNDSLWDKLFFNKIQASLGGCVRMIVT 458
Cdd:cd05927 202 KALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 459 GAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNLIKLKDAEELNYFA--SKGEGEICVK 536
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAkdPNPRGEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 537 GPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSDPVAQVYVHGD 616
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 617 SLQAFLVGIVVPDAEAMPGWAKKR-GFDGTYEELCRNKELQKAIMEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLL 695
Cdd:cd05927 442 SLKSFLVAIVVPDPDVLKEWAASKgGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLL 521
|
570 580
....*....|....*....|....
gi 2024456367 696 TPTLKAKRPELRDYFKKQIEELYS 719
Cdd:cd05927 522 TPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
103-722 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 711.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 103 SP-QLLTHY--YDDARTMYEVFRRGFSISENGPCLGYRKPKQ----PYQWLSYKEVAERAEALGSGLLQQGCKPctEQFI 175
Cdd:PLN02736 29 SPlKLVSRFpdHPEIGTLHDNFVYAVETFRDYKYLGTRIRVDgtvgEYKWMTYGEAGTARTAIGSGLVQHGIPK--GACV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 176 GVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVICdKPDKARTLLDHVErrETPGLSSIILMDPF 255
Cdd:PLN02736 107 GLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCLS--EIPSVRLIVVVGGA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 256 EKELTERGRRCGVRIQSMQEVEDCGRENRRAPVPPRPEDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWSp 335
Cdd:PLN02736 184 DEPLPSLPSGTGVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPS- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 336 tceDVHISYLPLAHMFERMVQSVVYCHGGRIGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFSQADTS--LKRW 413
Cdd:PLN02736 263 ---DVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESggLKER 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 414 VLEFAARRKKAEVRNGiiRNDS-LWDKLFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGC 492
Cdd:PLN02736 340 LFNAAYNAKKQALENG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVI 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 493 TFTTPGDWTSGHVGAPLPCNLIKLKDAEELNYFASKG---EGEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKW 569
Cdd:PLN02736 418 SGMDEGDNLSGHVGSPNPACEVKLVDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLW 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 570 LPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSDPVAQVYVHGDSLQAFLVGIVVPDAEAMPGWAKKRGFD-GTYEE 648
Cdd:PLN02736 498 LPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQ 577
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024456367 649 LCRNKELQKAIMEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELRDYFKKQIEELYSSIS 722
Cdd:PLN02736 578 LCNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYAELA 651
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
111-719 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 531.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 111 YDDARTMYEVFRRGFSISENGPCLGYRKPKQpYQWLSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISEL 190
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVALREKEDGI-WQSLTWAEFAERVRALAAGLLALGVKP--GDRVAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 191 ACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVICDKPDKARTLLDHveRRETPGLSSIILMDPfekelteRGRRCGVRI 270
Cdd:COG1022 84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEV--RDELPSLRHIVVLDP-------RGLRDDPRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 271 QSMQEVEDCGR--------ENRRAPVppRPEDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWSPTCEDVHI 342
Cdd:COG1022 155 LSLDELLALGRevadpaelEARRAAV--KPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLER----LPLGPGDRTL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 343 SYLPLAHMFERMVQSVVYCHGGRIGFfQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFSQADTS--LKRWVLEFA-- 418
Cdd:COG1022 229 SFLPLAHVFERTVSYYALAAGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAggLKRKLFRWAla 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 419 -ARRKKAEVRNGiiRNDSLW--------DKLFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECT 489
Cdd:COG1022 308 vGRRYARARLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 490 AGCTFTTPGDWTSGHVGAPLPCNLIKLkdAEElnyfaskgeGEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKW 569
Cdd:COG1022 385 PVITVNRPGDNRIGTVGPPLPGVEVKI--AED---------GEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGEL 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 570 LPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIyIRSDP-VAQVYVHGDSlQAFLVGIVVPDAEAMPGWAKKRGFD-GTYE 647
Cdd:COG1022 454 DEDGFLRITGRKKDLIVTSGGKNVAPQPIENA-LKASPlIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGLPyTSYA 531
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024456367 648 ELCRNKELQKAIMEDMVRLGKesGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELRDYFKKQIEELYS 719
Cdd:COG1022 532 ELAQDPEVRALIQEEVDRANA--GLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYA 601
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
141-706 |
4.85e-164 |
|
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: 480.17 E-value: 4.85e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 141 QPYQWLSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADI 220
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEP--GDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 221 STVICDKPDkartlldhverretpglssiilmdpfekeltergrrcgvriqsmqevedcgrenrrapvpprpeDLSIVCF 300
Cdd:cd05907 79 KALFVEDPD----------------------------------------------------------------DLATIIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 301 TSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWSPTCEDVHISYLPLAHMFE-RMVQSVVYCHGGRIGFFQgDIRLLSDD 379
Cdd:cd05907 95 TSGTTGRPKGVMLSHRNILSNALALAER----LPATEGDRHLSFLPLAHVFErRAGLYVPLLAGARIYFAS-SAETLLDD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 380 MKALRPTIFPVVPRLLNRMYDKIFSQADTSLKRWVLEFAArrkkaevrngiirndslwdklffnkiqaslGGCVRMIVTG 459
Cdd:cd05907 170 LSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV------------------------------GGRLRFAASG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 460 AAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNLIKLKDaeelnyfaskgEGEICVKGPN 539
Cdd:cd05907 220 GAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPN 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 540 VFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSDPVAQVYVHGDSlQ 619
Cdd:cd05907 288 VMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDG-R 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 620 AFLVGIVVPDAEAMPGWAKKRG-FDGTYEELCRNKELQKAIMEDMVRLGKEsgLHSFEQVKAIHIHSDMFSVQNGLLTPT 698
Cdd:cd05907 367 PFLVALIVPDPEALEAWAEEHGiAYTDVAELAANPAVRAEIEAAVEAANAR--LSRYEQIKKFLLLPEPFTIENGELTPT 444
|
....*...
gi 2024456367 699 LKAKRPEL 706
Cdd:cd05907 445 LKLKRPVI 452
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
142-703 |
1.85e-157 |
|
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: 465.54 E-value: 1.85e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 142 PYQWLSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADIS 221
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLVELGLKP--GDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 222 TVICDkpdkartlldhverretpglssiilmdpfekeltergrrcgvriqsmqevedcgrenrrapvpPRPEDLSIVCFT 301
Cdd:cd17639 80 AIFTD---------------------------------------------------------------GKPDDLACIMYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 302 SGTTGNPKGAMLTHGNVVADFSGFLKVTESQWSPTceDVHISYLPLAHMFERMVQSVVYCHGGRIGFfqGDIRLLSD--- 378
Cdd:cd17639 97 SGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGPD--DRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDksk 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 379 -----DMKALRPTIFPVVPRLLNRMYDKIFSQADTS--LKRWVLEFAARRKKAEVRNGIirnDS-LWDKLFFNKIQASLG 450
Cdd:cd17639 173 rgckgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMggLKRTLFWTAYQSKLKALKEGP---GTpLLDELVFKKVRAALG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 451 GCVRMIVTGAAPASPTVLGFLrAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNLIKLKDAEELNYFASKGE 530
Cdd:cd17639 250 GRLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDKPP 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 531 --GEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSDPV 608
Cdd:cd17639 329 prGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLV 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 609 AQVYVHGDSLQAFLVGIVVPDAEAMPGWAKKRGF-DGTYEELCRNKELQKAIMEDMVRLGKESGLHSFEQVKAIHIHSDM 687
Cdd:cd17639 409 NNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGViNSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEE 488
|
570
....*....|....*.
gi 2024456367 688 FSVQNGLLTPTLKAKR 703
Cdd:cd17639 489 WTPENGLVTAAQKLKR 504
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
113-721 |
6.25e-153 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 459.28 E-value: 6.25e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 113 DARTMYEVFRRGFSISENGPCLGYRKPKQ----PYQWLSYKEVAERAEALGSGLLQQGCKPCTEqfIGVFAQNRPEWIIS 188
Cdd:PLN02430 40 DITTAWDIFSKSVEKYPDNKMLGWRRIVDgkvgPYMWKTYKEVYEEVLQIGSALRASGAEPGSR--VGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 189 ELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTV-ICDKpdKARTLLDhVERRETPGLSSIILMDPFEKELTERGRRCG 267
Cdd:PLN02430 118 MEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVfVQDK--KIKELLE-PDCKSAKRLKAIVSFTSVTEEESDKASQIG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 268 VRIQSMQEVEDCGRENRRAPVPPRPEDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTESQWspTCEDVHISY 344
Cdd:PLN02430 195 VKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGvdlFMEQFEDKM--THDDVYLSF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 345 LPLAHMFERMVQSVVYCHGGRIGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFS--QADTSLKRWVLEFAARRK 422
Cdd:PLN02430 273 LPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYKYK 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 423 KAEVRNGIIRNDS--LWDKLFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDW 500
Cdd:PLN02430 353 LAWMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEM 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 501 TS-GHVGAPLPCNLIKLKDAEELNY--FASKGEGEICVKGPNVFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLKI 577
Cdd:PLN02430 433 CMlGTVGAPAVYNELRLEEVPEMGYdpLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKI 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 578 IDRKKHIFKLAQGEYIAPEKIENIYIRSDPVAQVYVHGDSLQAFLVGIVVPDAEAMPGWAKKRGFDGTYEELCRNKELQK 657
Cdd:PLN02430 512 IDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKE 591
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024456367 658 AIMEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELRDYFKKQIEELYSSI 721
Cdd:PLN02430 592 HILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMYRKL 655
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
112-722 |
7.91e-153 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 459.10 E-value: 7.91e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 112 DDARTMYEVFRRGFSISENGPCLGYR-----KPKQpYQWLSYKEVAERAEALGSGLLQQGCKpcTEQFIGVFAQNRPEWI 186
Cdd:PLN02614 42 EGMDSCWDVFRMSVEKYPNNPMLGRReivdgKPGK-YVWQTYQEVYDIVIKLGNSLRSVGVK--DEAKCGIYGANSPEWI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 187 ISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVICDK---PDKARTLLDHVERRETpglssIILMDPFEKELTERG 263
Cdd:PLN02614 119 ISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEkkiSELFKTCPNSTEYMKT-----VVSFGGVSREQKEEA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 264 RRCGVRIQSMQEVEDCGrENRRAPVP-PRPEDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTES-QWSPTCEDVH 341
Cdd:PLN02614 194 ETFGLVIYAWDEFLKLG-EGKQYDLPiKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSaNAALTVKDVY 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 342 ISYLPLAHMFERMVQSVVYCHGGRIGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFSQADTS--LKRWVLEFAA 419
Cdd:PLN02614 273 LSYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGgfLKKFVFDSAF 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 420 RRKKAEVRNGI--IRNDSLWDKLFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP 497
Cdd:PLN02614 353 SYKFGNMKKGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLP 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 498 GDWTS-GHVGAPLPCNLIKLKDAEELNY--FASKGEGEICVKGPNVFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGT 574
Cdd:PLN02614 433 DELDMlGTVGPPVPNVDIRLESVPEMEYdaLASTPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGS 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 575 LKIIDRKKHIFKLAQGEYIAPEKIENIYIRSDPVAQVYVHGDSLQAFLVGIVVPDAEAMPGWAKKRGFDGTYEELCRNKE 654
Cdd:PLN02614 512 MKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEK 591
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024456367 655 LQKAIMEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELRDYFKKQIEELYSSIS 722
Cdd:PLN02614 592 AKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYKTTN 659
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
142-719 |
3.58e-148 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 446.98 E-value: 3.58e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 142 PYQWLSYKEVAERAEALGSGLLQQGCKP---CteqfiGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTA 218
Cdd:PLN02861 74 PYVWLTYKEVYDAAIRIGSAIRSRGVNPgdrC-----GIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 219 DISTVICDKpDKARTLLDhVERRETPGLSSIILMDPFEKELTERGRRCGVRIQSMQEVEDCGRENRRAPvPPRPEDLSIV 298
Cdd:PLN02861 149 EVSIAFVQE-SKISSILS-CLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLDCELP-PKQKTDICTI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 299 CFTSGTTGNPKGAMLTHGNVVADF---SGFLKVTESqwSPTCEDVHISYLPLAHMFERMVQSVVYCHGGRIGFFQGDIRL 375
Cdd:PLN02861 226 MYTSGTTGEPKGVILTNRAIIAEVlstDHLLKVTDR--VATEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQGDIRY 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 376 LSDDMKALRPTIFPVVPRLLNRMYDKIFS--QADTSLKRWVLEFAARRKKAEVRNGIIRNDS--LWDKLFFNKIQASLGG 451
Cdd:PLN02861 304 LMEDVQALKPTIFCGVPRVYDRIYTGIMQkiSSGGMLRKKLFDFAYNYKLGNLRKGLKQEEAspRLDRLVFDKIKEGLGG 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 452 CVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCtFTTPGDWTS--GHVGAPLPCNLIKLKDAEELNY--FAS 527
Cdd:PLN02861 384 RVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGC-FTSIANVFSmvGTVGVPMTTIEARLESVPEMGYdaLSD 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 528 KGEGEICVKGPNVFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSDP 607
Cdd:PLN02861 463 VPRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPL 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 608 VAQVYVHGDSLQAFLVGIVVPDAEAMPGWAKKRGFDGTYEELCRNKELQKAIMEDMVRLGKESGLHSFEQVKAIHIHSDM 687
Cdd:PLN02861 542 IASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNP 621
|
570 580 590
....*....|....*....|....*....|..
gi 2024456367 688 FSVQNGLLTPTLKAKRPELRDYFKKQIEELYS 719
Cdd:PLN02861 622 FDIERDLITPTFKLKRPQLLKYYKDCIDQLYS 653
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
104-719 |
5.34e-138 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 421.83 E-value: 5.34e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 104 PQLLTHYYDDARTMYEVFRRGFSISENGPCLGYRK--PKQ----------------PYQWLSYKEVAERAEALGSGLLQQ 165
Cdd:PLN02387 47 PELVETPWEGATTLAALFEQSCKKYSDKRLLGTRKliSREfetssdgrkfeklhlgEYEWITYGQVFERVCNFASGLVAL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 166 GCKpcTEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVICDkPDKARTLLDHVERRETpg 245
Cdd:PLN02387 127 GHN--KEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICD-SKQLKKLIDISSQLET-- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 246 LSSIILMDPFEKELTERGRR-CGVRIQSMQEVEDCGRENRRAPVPPRPEDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG 324
Cdd:PLN02387 202 VKRVIYMDDEGVDSDSSLSGsSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAG 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 325 FLKVTESQWSptcEDVHISYLPLAHMFERMVQSVVYCHGGRIGFfqGDIRLLSD-----------DMKALRPTIFPVVPR 393
Cdd:PLN02387 282 VMTVVPKLGK---NDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDtsnkikkgtkgDASALKPTLMTAVPA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 394 LLNRMYDKIFSQADTS--LKRWVLEFAARRKKAEVRN------GIIRndSLWDKLFFNKIQASLGGCVRMIVTGAAPASP 465
Cdd:PLN02387 357 ILDRVRDGVRKKVDAKggLAKKLFDIAYKRRLAAIEGswfgawGLEK--LLWDALVFKKIRAVLGGRIRFMLSGGAPLSG 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 466 TVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNLIKLKDAEELNYFASKG---EGEICVKGPNVFK 542
Cdd:PLN02387 435 DTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLISDKpmpRGEIVIGGPSVTL 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 543 GYLKDEERTSEA--LDQEG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSDPVAQVYVHGDSL 618
Cdd:PLN02387 515 GYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIMVHADPF 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 619 QAFLVGIVVPDAEAMPGWAKKRGFD-GTYEELCRNKELQKAIMEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTP 697
Cdd:PLN02387 595 HSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPAKIKLLPEPWTPESGLVTA 674
|
650 660
....*....|....*....|..
gi 2024456367 698 TLKAKRPELRDYFKKQIEELYS 719
Cdd:PLN02387 675 ALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
142-588 |
5.96e-126 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 381.28 E-value: 5.96e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 142 PYQWLSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADIS 221
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRALGVGK--GDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 222 TVICDKPDKARTLLDHVERRETPGLSSIILMDPFEKELTergrrcgvriqsMQEVEDCGRENRRAPVPPRPEDLSIVCFT 301
Cdd:pfam00501 96 VLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEP------------LPEEAKPADVPPPPPPPPDPDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 302 SGTTGNPKGAMLTHGNVVADFSGFLKVTESQWSPTCEDVHISYLPLAHMFER-MVQSVVYCHGGRIGFFQGDIRL----L 376
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALdpaaL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 377 SDDMKALRPTIFPVVPRLLNRMydkifsqadtslkrwvleFAARRKKAEVRNGiirndslwdklffnkiqaslggcVRMI 456
Cdd:pfam00501 244 LELIERYKVTVLYGVPTLLNML------------------LEAGAPKRALLSS-----------------------LRLV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 457 VTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDW---TSGHVGAPLPCNLIKLKDAEELNYFASKGEGEI 533
Cdd:pfam00501 283 LSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGEL 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2024456367 534 CVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLA 588
Cdd:pfam00501 363 CVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
85-718 |
2.56e-103 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 331.56 E-value: 2.56e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 85 QSEEVEGLDGARRSVI-------GDSPQLLTHYYDDARTMYEVFRRgfSISENGP--CLGYRKPK--------------Q 141
Cdd:PTZ00216 32 QNVPVPGTETENASAIyriagvtDEEHERLRNEWYYGPNFLQRLER--ICKERGDrrALAYRPVErvekevvkdadgkeR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 142 PY--------QWLSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRY 213
Cdd:PTZ00216 110 TMevthfnetRYITYAELWERIVNFGRGLAELGLTK--GSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAY 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 214 IVNTADISTVICDKpDKARTLLDHVERRETPGLSsIILMDpfekELTERGRRCGVRIQSMQEVEDCGRE---NRRAPVPP 290
Cdd:PTZ00216 188 ALRETECKAIVCNG-KNVPNLLRLMKSGGMPNTT-IIYLD----SLPASVDTEGCRLVAWTDVVAKGHSagsHHPLNIPE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 291 RPEDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF-LKVTESQWSPTCEDVHISYLPLAHMFERMVQSVVYCHGGRIGFf 369
Cdd:PTZ00216 262 NNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALeDRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGF- 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 370 qGDIRLLSD-------DMKALRPTIFPVVPRLLNRMYDKIFSQ--ADTSLKRWVLEFAARRKKAEVRNGiiRNDSLWDKL 440
Cdd:PTZ00216 341 -GSPRTLTDtfarphgDLTEFRPVFLIGVPRIFDTIKKAVEAKlpPVGSLKRRVFDHAYQSRLRALKEG--KDTPYWNEK 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 441 FFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCqVYEGYGQTE--CTAGCTFTtpGDWTSGHVGAPLPCNLIKLKD 518
Cdd:PTZ00216 418 VFSAPRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTEtvCCGGIQRT--GDLEPNAVGQLLKGVEMKLLD 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 519 AEELNYfASKGE--GEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPE 596
Cdd:PTZ00216 495 TEEYKH-TDTPEprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALE 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 597 KIENIYIrSDPVAQ-----VYVHGDslQAFLVGIVVPDAEAMPGWAKKRGFDGTYEELCRNKELQKAIMEDMVRLGKESG 671
Cdd:PTZ00216 574 ALEALYG-QNELVVpngvcVLVHPA--RSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAG 650
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2024456367 672 LHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELRDYFKKQIEELY 718
Cdd:PTZ00216 651 RKSFEIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
143-710 |
2.10e-81 |
|
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: 268.18 E-value: 2.10e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 143 YQWLSYKEVAERAEALGSGLLQQGCKPCTEqfIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADIST 222
Cdd:cd05932 4 VVEFTWGEVADKARRLAAALRALGLEPGSK--IALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 223 VICDKpdkartlLDHVERRET---PGLSSIILMDPFEKELTErgrrcgvriqSMQEVEDCGRENRRAPvPPRPEDLSIVC 299
Cdd:cd05932 82 LFVGK-------LDDWKAMAPgvpEGLISISLPPPSAANCQY----------QWDDLIAQHPPLEERP-TRFPEQLATLI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 300 FTSGTTGNPKGAMLTHGNVVADFSGF---LKVTEsqwsptcEDVHISYLPLAHMFERMVQSVVYCHGGRIGFFQGDIRLL 376
Cdd:cd05932 144 YTSGTTGQPKGVMLTFGSFAWAAQAGiehIGTEE-------NDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 377 SDDMKALRPTIFPVVPRLL----NRMYDKIFSQadtSLKRWVlefaarrkKAEVRNGIIRNdslwdklffnKIQASLG-G 451
Cdd:cd05932 217 VEDVQRARPTLFFSVPRLWtkfqQGVQDKIPQQ---KLNLLL--------KIPVVNSLVKR----------KVLKGLGlD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 452 CVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNLIKLKDaeelnyfaskgEG 531
Cdd:cd05932 276 QCRLAGCGSAPVPPALLEWYRS-LGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 532 EICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSDPVAQV 611
Cdd:cd05932 344 EILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMV 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 612 YVHGDSLQAfLVGIVVPDAEAMPgwakkRGFDGTYEELcrnKELQKAIMEDMvrlgkESGLHSFEQVKAIHIHSDMFSVQ 691
Cdd:cd05932 424 CVIGSGLPA-PLALVVLSEEARL-----RADAFARAEL---EASLRAHLARV-----NSTLDSHEQLAGIVVVKDPWSID 489
|
570
....*....|....*....
gi 2024456367 692 NGLLTPTLKAKRPELRDYF 710
Cdd:cd05932 490 NGILTPTLKIKRNVLEKAY 508
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
141-704 |
2.07e-78 |
|
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: 258.83 E-value: 2.07e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 141 QPYQWLSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELAcytysmvvvplydTLGPGAIRyIVNTADI 220
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKA--GEKVALFADNSPRWLIADQG-------------IMALGAVD-VVRGSDS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 221 STvicdkpDKARTLLDHVErretpglSSIILMdpfekeltergrrcgvriqsmqevedcgrENRrapvpprPEDLSIVCF 300
Cdd:cd17640 65 SV------EELLYILNHSE-------SVALVV-----------------------------END-------SDDLATIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 301 TSGTTGNPKGAMLTHGNVVADFSGFLKVTESQwsPTceDVHISYLPLAHMFERMVQSVVYCHGGRIGFfqGDIRLLSDDM 380
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQ--PG--DRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDDL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 381 KALRPTIFPVVPRLLNRMYDKIFSQAdtslkrwvlefaarRKKAEVRNGIIrndslwdkLFFnkiqaSLGGCVRMIVTGA 460
Cdd:cd17640 170 KRVKPHYIVSVPRLWESLYSGIQKQV--------------SKSSPIKQFLF--------LFF-----LSGGIFKFGISGG 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 461 APASPTVLGFLRaALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNLIKLKDAEELNYFASKGEGEICVKGPNV 540
Cdd:cd17640 223 GALPPHVDTFFE-AIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQV 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 541 FKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSDPVAQVYVHGDSlQA 620
Cdd:cd17640 302 MKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQD-QK 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 621 FLVGIVVPDAEAMPGWAKKRG--FDGTYEELCRNKELQKAI-MEDMVRLGKESGLHSFEQVKAIHIHSDMFsVQNGLLTP 697
Cdd:cd17640 381 RLGALIVPNFEELEKWAKESGvkLANDRSQLLASKKVLKLYkNEIKDEISNRPGFKSFEQIAPFALLEEPF-IENGEMTQ 459
|
....*..
gi 2024456367 698 TLKAKRP 704
Cdd:cd17640 460 TMKIKRN 466
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
146-640 |
1.23e-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: 229.70 E-value: 1.23e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVIC 225
Cdd:COG0318 25 LTYAELDARARRLAAALRALGVGP--GDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 dkpdkartlldhverretpglssiilmdpfekeltergrrcgvriqsmqevedcgrenrrapvpprpedlSIVCFTSGTT 305
Cdd:COG0318 103 ----------------------------------------------------------------------ALILYTSGTT 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 306 GNPKGAMLTHGNVVADFSGFLKVtesqWSPTCEDVHISYLPLAHMFErMVQSVVYC--HGGRI----GFfqgDIRLLSDD 379
Cdd:COG0318 113 GRPKGVMLTHRNLLANAAAIAAA----LGLTPGDVVLVALPLFHVFG-LTVGLLAPllAGATLvllpRF---DPERVLEL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 380 MKALRPTIFPVVPRLLNRMYDKI-FSQADTSlkrwvlefaarrkkaevrngiirndslwdklffnkiqaslggCVRMIVT 458
Cdd:COG0318 185 IERERVTVLFGVPTMLARLLRHPeFARYDLS------------------------------------------SLRLVVS 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 459 GAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPCNLIKLKDAE--ELnyfASKGEGEIC 534
Cdd:COG0318 223 GGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGRPLPGVEVRIVDEDgrEL---PPGEVGEIV 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 535 VKGPNVFKGYLKDEERTSEALDqEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSDPVAQVYV- 613
Cdd:COG0318 300 VRGPNVMKGYWNDPEATAEAFR-DGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEVLAAHPGVAEAAVv 377
|
490 500 510
....*....|....*....|....*....|....*
gi 2024456367 614 ------HGDSLQAFLV--GIVVPDAEAMPGWAKKR 640
Cdd:COG0318 378 gvpdekWGERVVAFVVlrPGAELDAEELRAFLRER 412
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
143-669 |
2.00e-67 |
|
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: 232.31 E-value: 2.00e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 143 YQWLSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADIST 222
Cdd:cd17641 9 WQEFTWADYADRVRAFALGLLALGVGR--GDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 223 VICDKPDKARTLLDHveRRETPGLSSIILMDPfekelteRGRR--CGVRIQSMQEVEDCGRE-NRRAP-------VPPRP 292
Cdd:cd17641 87 VIAEDEEQVDKLLEI--ADRIPSVRYVIYCDP-------RGMRkyDDPRLISFEDVVALGRAlDRRDPglyerevAAGKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 293 EDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESqwSPTceDVHISYLPLAHMFERMVQSVVYCHGGRIGFFQGD 372
Cdd:cd17641 158 EDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPL--GPG--DEYVSVLPLPWIGEQMYSVGQALVCGFIVNFPEE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 373 IRLLSDDMKALRPTIFPVVPRLLNRMYDKIFSQ-AD-TSLKRWV--------LEFAARRKKAEVRNGIIRNDS-LWDKLF 441
Cdd:cd17641 234 PETMMEDLREIGPTFVLLPPRVWEGIAADVRARmMDaTPFKRFMfelgmklgLRALDRGKRGRPVSLWLRLASwLADALL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 442 FNKIQASLG-GCVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTEcTAGCTFTTP-GDWTSGHVGAPLPCNLIKLKDa 519
Cdd:cd17641 314 FRPLRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTE-LAGAYTVHRdGDVDPDTVGVPFPGTEVRIDE- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 520 eelnyfaskgEGEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIE 599
Cdd:cd17641 391 ----------VGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIE 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024456367 600 NIYIRSDPVAQVYVHGDSlQAFLVGIVVPDAEAMPGWAKKRGFD-GTYEELCRNKELQKAIMEDMVRLGKE 669
Cdd:cd17641 461 NKLKFSPYIAEAVVLGAG-RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKVNAS 530
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
146-696 |
3.74e-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: 226.57 E-value: 3.74e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGL-LQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTAD--IST 222
Cdd:cd17632 68 ITYAELWERVGAVAAAHdPEQPVRP--GDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEprLLA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 223 VICDKPDKARTLLdhverRETPGLSSIILMDpFEKELTE--------RGRRCGVRIQSMQEVEDCGRENRRAPVPPRPED 294
Cdd:cd17632 146 VSAEHLDLAVEAV-----LEGGTPPRLVVFD-HRPEVDAhraalesaRERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 295 -----LSIVCFTSGTTGNPKGAMLTHgNVVADFsgFLKVTESQWSPTCEDVHISYLPLAHMFERMVQSVVYCHGGrIGFF 369
Cdd:cd17632 220 pdddpLALLIYTSGSTGTPKGAMYTE-RLVATF--WLKVSSIQDIRPPASITLNFMPMSHIAGRISLYGTLARGG-TAYF 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 370 QG--DIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFSQADTSLKRWV-LEFAARRKKAEVRNGIirndslwdklffnkiq 446
Cdd:cd17632 296 AAasDMSTLFDDLALVRPTELFLVPRVCDMLFQRYQAELDRRSVAGAdAETLAERVKAELRERV---------------- 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 447 asLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTtpgdwtSGHVGAPlPCNLIKLKDAEELNYFA 526
Cdd:cd17632 360 --LGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE--AGAVIL------DGVIVRP-PVLDYKLVDVPELGYFR 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 527 SKG---EGEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYI 603
Cdd:cd17632 429 TDRphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFA 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 604 RSDPVAQVYVHGDSLQAFLVGIVVPDAEAMPGWAKKRgfdgtyeelcrnkeLQKAIMEDMVRLGKESGLHSFEQVKAIHI 683
Cdd:cd17632 509 ASPLVRQIFVYGNSERAYLLAVVVPTQDALAGEDTAR--------------LRAALAESLQRIAREAGLQSYEIPRDFLI 574
|
570
....*....|...
gi 2024456367 684 HSDMFSVQNGLLT 696
Cdd:cd17632 575 ETEPFTIANGLLS 587
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
138-718 |
7.59e-65 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 226.08 E-value: 7.59e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 138 KPKQPYQWLSYKEVAERAEALGSGLLQQGckpcTEQF--IGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIV 215
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLKLG----LERFhgVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 216 NTADISTVICD---KPDKARTLLDHVerretPGLSSII-LMDPFE---------KELTERGRrcgvriqsmqEVEDCGRE 282
Cdd:cd05933 77 ETSEANILVVEnqkQLQKILQIQDKL-----PHLKAIIqYKEPLKekepnlyswDEFMELGR----------SIPDEQLD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 283 NRRAPVppRPEDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWSPTCEDVHISYLPLAHMFERMVQS-VVYC 361
Cdd:cd05933 142 AIISSQ--KPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIwLPIK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 362 HGGRIGFFQGDIR--LLSDDMKALRPTIFPVVPRLLNRMYDKI---FSQAdTSLKRWVLEFAAR------RKKAEVRNGI 430
Cdd:cd05933 220 VGGQVYFAQPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkavGAKS-GTLKRKIASWAKGvgletnLKLMGGESPS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 431 IRNDSLWDKLFFNKIQASLG--GCVRMIvTGAAPASPTVLGFLrAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAP 508
Cdd:cd05933 299 PLFYRLAKKLVFKKVRKALGldRCQKFF-TGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 509 LP-C-NLIKLKDAEelnyfaskGEGEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFK 586
Cdd:cd05933 377 LPgCkTKIHNPDAD--------GIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELII 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 587 LAQGEYIAPEKIEN-IYIRSDPVAQVYVHGDSLQaFLVGIVV------PD---------AEAMPgWAKKRGFDGTY-EEL 649
Cdd:cd05933 449 TAGGENVPPVPIEDaVKKELPIISNAMLIGDKRK-FLSMLLTlkcevnPEtgepldeltEEAIE-FCRKLGSQATRvSEI 526
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024456367 650 C--RNKELQKAIMEDMVRLGKESGLHSFEQVKAIHIHSDmFSVQNGLLTPTLKAKRPELRDYFKKQIEELY 718
Cdd:cd05933 527 AggKDPKVYEAIEEGIKRVNKKAISNAQKIQKWVILEKD-FSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
146-703 |
2.92e-60 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 209.99 E-value: 2.92e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGsgLLQQGCKPCTEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVIC 225
Cdd:cd05914 8 LTYKDLADNIAKFA--LLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 DKPDkartlldhverretpglssiilmdpfekeltergrrcgvriqsmqevedcgrenrrapvpprpeDLSIVCFTSGTT 305
Cdd:cd05914 86 SDED----------------------------------------------------------------DVALINYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 306 GNPKGAMLTHGNVVADFSG---FLKVTEsqwsptcEDVHISYLPLAHMFERMVQSVVYCHGGRIGFFQGDI---RLLSDD 379
Cdd:cd05914 102 GNSKGVMLTYRNIVSNVDGvkeVVLLGK-------GDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIpsaKIIALA 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 380 MKALRPTIfpVVPRLLNRMYDKIFSQADTSLKRWVLEfaarRKKAEVRNGIIRndslwdKLFFNKIQASLGGCVRMIVTG 459
Cdd:cd05914 175 FAQVTPTL--GVPVPLVIEKIFKMDIIPKLTLKKFKF----KLAKKINNRKIR------KLAFKKVHEAFGGNIKEFVIG 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 460 AAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNLIKLKDAEelnyfASKGEGEICVKGPN 539
Cdd:cd05914 243 GAKINPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPD-----PATGEGEIIVRGPN 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 540 VFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSDPVA--QVYVHGDS 617
Cdd:cd05914 317 VMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLesLVVVQEKK 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 618 LQAflvgIVVPDAEampgwakkrgFDGTYEELCRNKElqKAIMEDmVRLGKESGLHSFEQVKAIHIHSDMFSVqngllTP 697
Cdd:cd05914 397 LVA----LAYIDPD----------FLDVKALKQRNII--DAIKWE-VRDKVNQKVPNYKKISKVKIVKEEFEK-----TP 454
|
....*.
gi 2024456367 698 TLKAKR 703
Cdd:cd05914 455 KGKIKR 460
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
294-631 |
7.70e-59 |
|
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: 202.13 E-value: 7.70e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 294 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWSPTCEDVHISYLPLAHMFerMVQSVVYC--HGGRIGFFQG 371
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS----GGLTEGDVFLSTLPLFHIG--GLFGLLGAllAGGTVVLLPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 372 -DIRLLSDDMKALRPTIFPVVPRLLNRMydkifsqadtslkrwvLEFAARRKkaevrngiiRNDSlwdklffnkiqaslg 450
Cdd:cd04433 75 fDPEAALELIEREKVTILLGVPTLLARL----------------LKAPESAG---------YDLS--------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 451 gCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT--SGHVGAPLPCNLIKLKDaEELNYFASK 528
Cdd:cd04433 115 -SLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVD-PDGGELPPG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 529 GEGEICVKGPNVFKGYLKDEERTsEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYIRSDPV 608
Cdd:cd04433 193 EIGELVVRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPGV 270
|
330 340
....*....|....*....|...
gi 2024456367 609 AQVYVHGdslqaflvgivVPDAE 631
Cdd:cd04433 271 AEAAVVG-----------VPDPE 282
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
144-623 |
7.05e-58 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 203.56 E-value: 7.05e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 144 QWLSYKEVAERAEALGSGLLQQGCKPCTEqfIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTV 223
Cdd:cd05936 23 RKLTYRELDALAEAFAAGLQNLGVQPGDR--VALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 224 ICDkpdkartlldhverretpglssiilmDPFEkELTERGRRcgvriqsmqevedcgrenRRAPVPPRPEDLSIVCFTSG 303
Cdd:cd05936 101 IVA--------------------------VSFT-DLLAAGAP------------------LGERVALTPEDVAVLQYTSG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 304 TTGNPKGAMLTHGNVVADFSGFLKVTESQWSPtcEDVHISYLPLAHMFERMVQSVV-YCHGGRIGFFQG--DIRLLsDDM 380
Cdd:cd05936 136 TTGVPKGAMLTHRNLVANALQIKAWLEDLLEG--DDVVLAALPLFHVFGLTVALLLpLALGATIVLIPRfrPIGVL-KEI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 381 KALRPTIFPVVPRLLNRMydkifsqadtslkrwvLEFAARRKKAevrngiirndslwdklfFNKIqaslggcvRMIVTGA 460
Cdd:cd05936 213 RKHRVTIFPGVPTMYIAL----------------LNAPEFKKRD-----------------FSSL--------RLCISGG 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 461 APASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT-SGHVGAPLPCNLIKLKDAEelNYFASKGE-GEICVKGP 538
Cdd:cd05936 252 APLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRkPGSIGIPLPGTEVKIVDDD--GEELPPGEvGELWVRGP 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 539 NVFKGYLKDEERTSEALDqEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVYV----- 613
Cdd:cd05936 330 QVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGGFNVYPREVEEVLYEHPAVAEAAVvgvpd 407
|
490
....*....|..
gi 2024456367 614 --HGDSLQAFLV 623
Cdd:cd05936 408 pySGEAVKAFVV 419
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
146-640 |
1.02e-57 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 204.37 E-value: 1.02e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPCTEqfIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVIC 225
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGKGDR--VAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 dkpdkARTLLDHVERRET--PGLSSIILMDpfekelTERGRRCGVRIQSMQEVEDCGRENRRAPvPPRPEDLSIVCFTSG 303
Cdd:PRK07656 109 -----LGLFLGVDYSATTrlPALEHVVICE------TEEDDPHTEKMKTFTDFLAAGDPAERAP-EVDPDDVADILFTSG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 304 TTGNPKGAMLTHGNV---VADFSGFLKVTEsqwsptcEDVHISYLPLAHMFERMVqSVVYC--HGGRI---GFFQGD--I 373
Cdd:PRK07656 177 TTGRPKGAMLTHRQLlsnAADWAEYLGLTE-------GDRYLAANPFFHVFGYKA-GVNAPlmRGATIlplPVFDPDevF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 374 RLLSDDmkalRPTIFPVVPRLLNRMYDkifsqadtslkrwvlefAARRKKAEVrngiirndslwdklffnkiqASLggcv 453
Cdd:PRK07656 249 RLIETE----RITVLPGPPTMYNSLLQ-----------------HPDRSAEDL--------------------SSL---- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 454 RMIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGCTFTTPGD---WTSGHVGAPLPcnLIKLKDAEELNYFASKG 529
Cdd:PRK07656 284 RLAVTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIA--GVENKIVNELGEEVPVG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 530 E-GEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPV 608
Cdd:PRK07656 362 EvGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IVGGFNVYPAEVEEVLYEHPAV 440
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2024456367 609 AQVYV-------HGDSLQAFLV---GIVVpDAEAMPGWAKKR 640
Cdd:PRK07656 441 AEAAVigvpderLGEVGKAYVVlkpGAEL-TEEELIAYCREH 481
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
146-615 |
8.61e-51 |
|
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: 184.34 E-value: 8.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVIC 225
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKK--GDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 DKP--DKARTLLdhverRETPGLSSIILMDPFEKELTergrrcgvRIQSMQEVEDCGRENRRAPVPPR-PEDLSIVCFTS 302
Cdd:cd05911 89 DPDglEKVKEAA-----KELGPKDKIIVLDDKPDGVL--------SIEDLLSPTLGEEDEDLPPPLKDgKDDTAAILYSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 303 GTTGNPKGAMLTHGNVVADFSGFLKVTESQWSPtcEDVHISYLPLAHMF--ERMVQSVVYchGGRI----GFFqgdirll 376
Cdd:cd05911 156 GTTGLPKGVCLSHRNLIANLSQVQTFLYGNDGS--NDVILGFLPLYHIYglFTTLASLLN--GATViimpKFD------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 377 SDDMKAL----RPTIFPVVPRLLNRMydkifsqadtslkrwvlefaarrkkaeVRNGIIRNDSLwdklffnkiqaslgGC 452
Cdd:cd05911 225 SELFLDLiekyKITFLYLVPPIAAAL---------------------------AKSPLLDKYDL--------------SS 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 453 VRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNLIKLKDAEELNYFASKGEG 531
Cdd:cd05911 264 LRVILSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEPG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 532 EICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDPVAQV 611
Cdd:cd05911 344 EICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAVLLEHPGVADA 422
|
....
gi 2024456367 612 YVHG 615
Cdd:cd05911 423 AVIG 426
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
147-629 |
5.69e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 171.91 E-value: 5.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 147 SYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACytySM---VVVPLYDTLGPGAIRYIVNTADISTV 223
Cdd:PRK06187 33 TYAELDERVNRLANALRALGVKK--GDRVAVFDWNSHEYLEAYFAV---PKigaVLHPINIRLKPEEIAYILNDAEDRVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 224 ICDKpdkarTLLDHVE--RRETPGLSSIILMDPFEKEltergrRCGVRIQSMQEVEDCGRENRRAPvPPRPEDLSIVCFT 301
Cdd:PRK06187 108 LVDS-----EFVPLLAaiLPQLPTVRTVIVEGDGPAA------PLAPEVGEYEELLAAASDTFDFP-DIDENDAAAMLYT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 302 SGTTGNPKGAMLTHGNVvadFSGFLKVTES-QWSPtcEDVHISYLPLAHMFERMVqsvvychgGRIGFFQG--------- 371
Cdd:PRK06187 176 SGTTGHPKGVVLSHRNL---FLHSLAVCAWlKLSR--DDVYLVIVPMFHVHAWGL--------PYLALMAGakqviprrf 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 372 DIRLLSDDMKALRPTIFPVVPRLLNRMydkifSQADTSLKRWvlefaarrkkaevrngiirndslwdklfFNKIqaslgg 451
Cdd:PRK06187 243 DPENLLDLIETERVTFFFAVPTIWQML-----LKAPRAYFVD----------------------------FSSL------ 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 452 cvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGH------VGAPLPCNLIKLKDaEELNYF 525
Cdd:PRK06187 284 --RLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVLPPEDQLPGQwtkrrsAGRPLPGVEARIVD-DDGDEL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 526 ASKGE--GEICVKGPNVFKGYLKDEERTSEALDqEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYI 603
Cdd:PRK06187 361 PPDGGevGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIKDVIISG-GENIYPRELEDALY 438
|
490 500
....*....|....*....|....*.
gi 2024456367 604 RSDPVAQVYVhgdslqaflVGivVPD 629
Cdd:PRK06187 439 GHPAVAEVAV---------IG--VPD 453
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
257-720 |
1.01e-45 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 174.52 E-value: 1.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 257 KELTERGRRCGVRIQSMQEVedcgRENRRAPVPPRPED----LSIVcFTSGTTGNPKGAMLTHGNV------VADFSGFL 326
Cdd:PTZ00342 269 KDLKEKAKKLGISIILFDDM----TKNKTTNYKIQNEDpdfiTSIV-YTSGTSGKPKGVMLSNKNLyntvvpLCKHSIFK 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 327 KvtesqWSPtceDVHISYLPLAHMFERMVQSVVYCHGGRIGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFSQA 406
Cdd:PTZ00342 344 K-----YNP---KTHLSYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 407 D--TSLKRWVLE--FAARRKKaevRNGIIRNdsLWDKLFF--NKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVY 480
Cdd:PTZ00342 416 NnlPPLKRFLVKkiLSLRKSN---NNGGFSK--FLEGITHisSKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYY 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 481 EGYGQTEcTAGCTFTTPG-DWTSGHVGAPL-PCNLIKLKDAEELNYFASKGEGEICVKGPNVFKGYLKDEERTSEALDQE 558
Cdd:PTZ00342 491 QGYGLTE-TTGPIFVQHAdDNNTESIGGPIsPNTKYKVRTWETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTED 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 559 GWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSDPVAQVYVHG-DSLQAFLvGIVVPDAE------ 631
Cdd:PTZ00342 570 GYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGdDSMDGPL-AIISVDKYllfkcl 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 632 ------AMPGWAKKRGFDGTYEELCRNKELQKAIMEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNgLLTPTLKAKRPE 705
Cdd:PTZ00342 649 kddnmlESTGINEKNYLEKLTDETINNNIYVDYVKGKMLEVYKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKRFY 727
|
490
....*....|....*...
gi 2024456367 706 L-RDY--FKKQIEELYSS 720
Cdd:PTZ00342 728 VfKDYafFIDQVKKIYKN 745
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
146-630 |
8.26e-42 |
|
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: 157.77 E-value: 8.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPCTEqfIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADistvic 225
Cdd:cd17631 21 LTYAELDERVNRLAHALRALGVAKGDR--VAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSG------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 dkpdkARTLLDhverretpglssiilmdpfekeltergrrcgvriqsmqevedcgrenrrapvpprpeDLSIVCFTSGTT 305
Cdd:cd17631 93 -----AKVLFD---------------------------------------------------------DLALLMYTSGTT 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 306 GNPKGAMLTHGNVVADFSGFLkvteSQWSPTCEDVHISYLPLAHMFE-RMVQSVVYCHGGRI----GFfqgDIRLLSDDM 380
Cdd:cd17631 111 GRPKGAMLTHRNLLWNAVNAL----AALDLGPDDVLLVVAPLFHIGGlGVFTLPTLLRGGTVvilrKF---DPETVLDLI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 381 KALRPTIFPVVPRLLNRMYDK-IFSQADTSlkrwvlefaarrkkaevrngiirndslwdklffnkiqaSLggcvRMIVTG 459
Cdd:cd17631 184 ERHRVTSFFLVPTMIQALLQHpRFATTDLS--------------------------------------SL----RAVIYG 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 460 AAPASPTVLGFLRAAlGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPCNLIKLKDaEELNYFASKGEGEICVKG 537
Cdd:cd17631 222 GAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHRRklGSAGRPVFFVEVRIVD-PDGREVPPGEVGEIVVRG 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 538 PNVFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYIRSDPVAQVYVHGds 617
Cdd:cd17631 300 PHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDVLYEHPAVAEVAVIG-- 375
|
490
....*....|...
gi 2024456367 618 lqaflvgivVPDA 630
Cdd:cd17631 376 ---------VPDE 379
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
146-640 |
8.93e-40 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 152.44 E-value: 8.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALgSGLLQQGCKPCTEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVIc 225
Cdd:cd05941 12 ITYADLVARAARL-ANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 dkpdkartlldhverretpglssiilmdpfekeltergrrcgvriqsmqevedcgrenrrapvpprpeDLSIVCFTSGTT 305
Cdd:cd05941 90 --------------------------------------------------------------------DPALILYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 306 GNPKGAMLTHGNVVADfsgfLKVTESQWSPTCEDVHISYLPLAHmfermVQSVV-------YCHGGRI--GFFQGDIRLL 376
Cdd:cd05941 102 GRPKGVVLTHANLAAN----VRALVDAWRWTEDDVLLHVLPLHH-----VHGLVnallcplFAGASVEflPKFDPKEVAI 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 377 SDDMKALrpTIFPVVPRllnrMYDKIFSQADTSLKrwvlEFAARRKKAEVRngiirndslwdklffnkiqaslggcVRMI 456
Cdd:cd05941 173 SRLMPSI--TVFMGVPT----IYTRLLQYYEAHFT----DPQFARAAAAER-------------------------LRLM 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 457 VTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTTP--GDWTSGHVGAPLPCNLIKLKDAEELNYFASKGEGEIC 534
Cdd:cd05941 218 VSGSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQ 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 535 VKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKK-HIFKlAQGEYIAPEKIENIYIRSDPVAQVYV 613
Cdd:cd05941 296 VRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEIERVLLAHPGVSECAV 374
|
490 500 510
....*....|....*....|....*....|....*..
gi 2024456367 614 HGDSLQAF---LVGIVVP-------DAEAMPGWAKKR 640
Cdd:cd05941 375 IGVPDPDWgerVVAVVVLragaaalSLEELKEWAKQR 411
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
146-641 |
2.33e-39 |
|
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: 152.10 E-value: 2.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSgLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVIC 225
Cdd:cd05909 8 LTYRKLLTGAIALAR-KLAKMTKE--GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 DKP--DKARtlLDHVERRETPglSSIILMDPFEKELTeRGRRCGVRIQSMQEVEDCGRENRRAPVppRPEDLSIVCFTSG 303
Cdd:cd05909 85 SKQfiEKLK--LHHLFDVEYD--ARIVYLEDLRAKIS-KADKCKAFLAGKFPPKWLLRIFGVAPV--QPDDPAVILFTSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 304 TTGNPKGAMLTHGNVVADFSGFLKVTEsqwsPTCEDVHISYLPLAHMFermvqsvvychggriGFFQGDIRLLSDDMKAL 383
Cdd:cd05909 158 SEGLPKGVVLSHKNLLANVEQITAIFD----PNPEDVVFGALPFFHSF---------------GLTGCLWLPLLSGIKVV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 384 ---RPTIFPVVPRLLnrmYDK---IFSQADTSLkrwvlefaarrkkaevrNGIIRNdslWDKLFFnkiqASLggcvRMIV 457
Cdd:cd05909 219 fhpNPLDYKKIPELI---YDKkatILLGTPTFL-----------------RGYARA---AHPEDF----SSL----RLVV 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 458 TGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPCNLIKLKDAEELNYFASKGEGEICVK 536
Cdd:cd05909 268 AGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVR 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 537 GPNVFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSDP----VAQVY 612
Cdd:cd05909 348 GPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDILSEILPedneVAVVS 425
|
490 500 510
....*....|....*....|....*....|...
gi 2024456367 613 V----HGDSLQAFLVGIvVPDAEAMPGWAKKRG 641
Cdd:cd05909 426 VpdgrKGEKIVLLTTTT-DTDPSSLNDILKNAG 457
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
148-631 |
7.96e-36 |
|
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: 140.66 E-value: 7.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 148 YKEVAERAEALGSGLLQQGckpcteQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVICDK 227
Cdd:TIGR01923 6 DCEAAHLAKALKAQGIRSG------SRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 228 P-DKARTLLDHVERRETPGLSSIILMDPFEKEltergrrcgvriqsmqevedcgrenrrapvpprpeDLSIVCFTSGTTG 306
Cdd:TIGR01923 80 LlEEKDFQADSLDRIEAAGRYETSLSASFNMD-----------------------------------QIATLMFTSGTTG 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 307 NPKGAMLTHGNVVADFSGF---LKVTESqwsptceDVHISYLPLAHMFErmvQSVVY---CHGGRIGFFQGDIRLLsDDM 380
Cdd:TIGR01923 125 KPKAVPHTFRNHYASAVGSkenLGFTED-------DNWLLSLPLYHISG---LSILFrwlIEGATLRIVDKFNQLL-EMI 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 381 KALRPTIFPVVPRLLNRMYDKifSQADTSLKRwVLefaarrkkaevrngiirndslwdklffnkiqasLGGcvrmivtGA 460
Cdd:TIGR01923 194 ANERVTHISLVPTQLNRLLDE--GGHNENLRK-IL---------------------------------LGG-------SA 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 461 APASptvlgFLRAAL--GCQVYEGYGQTE-CTAGCTFTTPGDWTSGHVGAPLPCNLIKLKDAEElnyfasKGEGEICVKG 537
Cdd:TIGR01923 231 IPAP-----LIEEAQqyGLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIKVDNK------EGHGEIMVKG 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 538 PNVFKGYLKDEERTsEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIyirsdpvaqVYVHGDS 617
Cdd:TIGR01923 300 ANLMKGYLYQGELT-PAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETV---------LYQHPGI 368
|
490
....*....|....
gi 2024456367 618 LQAFLVGivVPDAE 631
Cdd:TIGR01923 369 QEAVVVP--KPDAE 380
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
286-632 |
9.78e-36 |
|
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: 141.60 E-value: 9.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 286 APVPP-RPEDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWSPtcEDVHISYLPLAHMFermvqsvvychgG 364
Cdd:cd05904 150 PPVVViKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDS--EDVFLCVLPMFHIY------------G 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 365 RIGFFQGDIRL-----------LSDDMKAL---RPTIFPVVPRLLnrmydkifsqadtslkrwvlefaarrkKAEVRNGI 430
Cdd:cd05904 216 LSSFALGLLRLgatvvvmprfdLEELLAAIeryKVTHLPVVPPIV---------------------------LALVKSPI 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 431 IRNDSLwdklffnkiqASLggcvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGApl 509
Cdd:cd05904 269 VDKYDL----------SSL----RQIMSGAAPLGKELIeAFRAKFPNVDLGQGYGMTESTGVVAMCFAPEKDRAKYGS-- 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 510 pCNLI------KLKDAEELNYFASKGEGEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKH 583
Cdd:cd05904 333 -VGRLvpnveaKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKE 411
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2024456367 584 IFKLaQGEYIAPEKIENIYIrSDP-VAQVYVhgdslqaflvgIVVPDAEA 632
Cdd:cd05904 412 LIKY-KGFQVAPAELEALLL-SHPeILDAAV-----------IPYPDEEA 448
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
280-632 |
2.72e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 138.36 E-value: 2.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 280 GRENRRAPVPPRPEDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWSPTCEDVhISYLPLAHMFERMVQSVV 359
Cdd:PRK05677 194 GAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEGCEIL-IAPLPLYHIYAFTFHCMA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 360 YCHGGRIGFFQGDIRLLSDDMKALRPTIFPVvprllnrmydkiFSQADTSlkrwvleFAArrkkaevrngiIRNDSLWDK 439
Cdd:PRK05677 273 MMLIGNHNILISNPRDLPAMVKELGKWKFSG------------FVGLNTL-------FVA-----------LCNNEAFRK 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 440 LFFNKIQASLGGcvRMIVTGAAPASptvlgfLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNLIKLKDa 519
Cdd:PRK05677 323 LDFSALKLTLSG--GMALQLATAER------WKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVID- 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 520 EELNYFASKGEGEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIE 599
Cdd:PRK05677 394 DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVSGFNVYPNELE 472
|
330 340 350
....*....|....*....|....*....|...
gi 2024456367 600 NIyirsdpvaqVYVHGDSLQAFLVGivVPDAEA 632
Cdd:PRK05677 473 DV---------LAALPGVLQCAAIG--VPDEKS 494
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
280-611 |
2.07e-33 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 135.77 E-value: 2.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 280 GRENRRAPVPPRPEDLSIVCFTSGTTGNPKGAMLTHGNVVADF---SGFLKVTeSQWSPTCEDVhISYLPLAHMFERMVQ 356
Cdd:PRK08751 195 GRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMqqaHQWLAGT-GKLEEGCEVV-ITALPLYHIFALTAN 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 357 SVVYCHGGRIGFFQGDIRLLSDDMKALRPTIFPVvprllnrmydkiFSQADTslkrwvlefaarrkkaeVRNGIIrNDSL 436
Cdd:PRK08751 273 GLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTA------------FTGVNT-----------------LFNGLL-NTPG 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 437 WDKLFFNKIQASLGGcvRMIVTGAapasptVLGFLRAALGCQVYEGYGQTECT-AGCTFTTPGDWTSGHVGAPLPCNLIK 515
Cdd:PRK08751 323 FDQIDFSSLKMTLGG--GMAVQRS------VAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDAC 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 516 LKDaeELNYFASKGE-GEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIA 594
Cdd:PRK08751 395 IKD--DAGTVLAIGEiGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-LVSGFNVY 471
|
330
....*....|....*..
gi 2024456367 595 PEKIENIYIRSDPVAQV 611
Cdd:PRK08751 472 PNEIEDVIAMMPGVLEV 488
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
145-630 |
2.45e-33 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 134.36 E-value: 2.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 145 WLSYKEVAERAEALGSGLLQQGCKPCTEqfIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVI 224
Cdd:cd05926 14 ALTYADLAELVDDLARQLAALGIKKGDR--VAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 225 CDKPdkarTLLDHVERRETPGLSSiilmdpfeKELTERGRRCGVRIQSMQ-EVEDCGRENRRAPVPPRPEDLSIVCFTSG 303
Cdd:cd05926 92 TPKG----ELGPASRAASKLGLAI--------LELALDVGVLIRAPSAESlSNLLADKKNAKSEGVPLPDDLALILHTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 304 TTGNPKGAMLTHGNVVADFSGFLKVtesqWSPTCEDVHISYLPLAHMFERMVQ--SVVYChGGRI----GFfqgDIRLLS 377
Cdd:cd05926 160 TTGRPKGVPLTHRNLAASATNITNT----YKLTPDDRTLVVMPLFHVHGLVASllSTLAA-GGSVvlppRF---SASTFW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 378 DDMKALRPTIFPVVPRLLnrmydKIfsqadtslkrwVLEFAARRKKAEvrngiirndslwdklfFNKIqaslggcvRMIV 457
Cdd:cd05926 232 PDVRDYNATWYTAVPTIH-----QI-----------LLNRPEPNPESP----------------PPKL--------RFIR 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 458 TGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTP---GDWTSGHVGAPlpcNLIKLKDAEEL-NYFASKGEGEI 533
Cdd:cd05926 272 SCSASLPPAVLEALEATFGAPVLEAYGMTE-AAHQMTSNPlppGPRKPGSVGKP---VGVEVRILDEDgEILPPGVVGEI 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 534 CVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSDPVAQVYV 613
Cdd:cd05926 348 CLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVLLSHPAVLEAVA 426
|
490
....*....|....*..
gi 2024456367 614 HGdslqaflvgivVPDA 630
Cdd:cd05926 427 FG-----------VPDE 432
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
280-615 |
8.52e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 133.97 E-value: 8.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 280 GRENRRAPVP-PRPEDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgflkVTESQ-WSPTCED---VHISYLPLAHMFE-R 353
Cdd:PRK05605 205 GGDGSDVSHPrPTPDDVALILYTSGTTGKPKGAQLTHRNLFAN------AAQGKaWVPGLGDgpeRVLAALPMFHAYGlT 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 354 MVQSVVYCHGGRIGFFQG-DIRLLSDDMKALRPTIFPVVPRLlnrmYDKIfsqadtslkrwvlefaarRKKAEVRNgiir 432
Cdd:PRK05605 279 LCLTLAVSIGGELVLLPApDIDLILDAMKKHPPTWLPGVPPL----YEKI------------------AEAAEERG---- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 433 ndslwdklffnkiqASLGGcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECT---AGCTFTTpgDWTSGHVGAPL 509
Cdd:PRK05605 333 --------------VDLSG-VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpiiVGNPMSD--DRRPGYVGVPF 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 510 PCNLIKLKDAEELNYFASKGE-GEICVKGPNVFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLA 588
Cdd:PRK05605 396 PDTEVRIVDPEDPDETMPDGEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELI-IT 473
|
330 340
....*....|....*....|....*..
gi 2024456367 589 QGEYIAPEKIENIYIRSDPVAQVYVHG 615
Cdd:PRK05605 474 GGFNVYPAEVEEVLREHPGVEDAAVVG 500
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
53-719 |
5.78e-32 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 133.83 E-value: 5.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 53 TALVGIGAfAAVVAYWFASRPKAV--KPPCdLRMQSEEVEGLDGarrsVIGDSP---QLLTHyyddARTMYEVFRRGFSI 127
Cdd:PTZ00297 370 MSLVLCAA-VWLLRWAQNSSIHPLlsERPF-LTVEALKEKGEEC----FALNLPreyNPLAG----VRSLGEMWERSVTR 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 128 SENGPCLGYRKPKQPYQWLSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLydtLG 207
Cdd:PTZ00297 440 HSTFRCLGQTSESGESEWLTYGTVDARARELGSGLLALGVRP--GDVIGVDCEASRNIVILEVACALYGFTTLPL---VG 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 208 PG-AIRYIVNTADISTVICDKPDKARTLLDHVERRETpglssIILMDPFEKELTER-GRRCGVRIQSMQEVEDCGrenRR 285
Cdd:PTZ00297 515 KGsTMRTLIDEHKIKVVFADRNSVAAILTCRSRKLET-----VVYTHSFYDEDDHAvARDLNITLIPYEFVEQKG---RL 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 286 APVPPRPEDLSIVCFT-------SGTTGNPKGAMLTHGNVVADFSGFLKvteSQWSPTCEDVH--ISYLPLAHMFERMVQ 356
Cdd:PTZ00297 587 CPVPLKEHVTTDTVFTyvvdnttSASGDGLAVVRVTHADVLRDISTLVM---TGVLPSSFKKHlmVHFTPFAMLFNRVFV 663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 357 SVVYCHGGRIGffQGDIRLLSDDMKALRPTIFPVVPRLlnrmydkiFSQADTSLKR----------WVLE--FAARRKKA 424
Cdd:PTZ00297 664 LGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSL--------FSTSRLQLSRanerysavysWLFEraFQLRSRLI 733
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 425 EVRNgiiRNDSLWDKLFFNKIQASLGGCVRMIVTGAAPASPTV-----LGFLRAALGCQVYegygQTECTAGCTFTtpgd 499
Cdd:PTZ00297 734 NIHR---RDSSLLRFIFFRATQELLGGCVEKIVLCVSEESTSFsllehISVCYVPCLREVF----FLPSEGVFCVD---- 802
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 500 wtsghvGAPLPCNLIKLKDAEELNYFASKGEGEICVKGpnvfkgylkDEERTSEAldqegwlhtgdIGKWLPNGTLKIID 579
Cdd:PTZ00297 803 ------GTPAPSLQVDLEPFDEPSDGAGIGQLVLAKKG---------EPRRTLPI-----------AAQWKRDRTLRLLG 856
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 580 RKKHIFKLAQGEYIAPEKIENIYIRSDPVAQVYVHGDSLQAfLVGIVVPDAEAMP-GWAKKRGF---DGTYEELCRNKEL 655
Cdd:PTZ00297 857 PPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEfEWRQSHCMgegGGPARQLGWTELV 935
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024456367 656 QKA---IMEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELRDYFKKQIEELYS 719
Cdd:PTZ00297 936 AYAsslLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIERFYS 1002
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
146-634 |
9.78e-32 |
|
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: 128.80 E-value: 9.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACY----TYsmvvVPLYDTLGPGAIRYIVNTADIS 221
Cdd:cd05930 13 LTYAELDARANRLARYLRERGVGP--GDLVAVLLERSLEMVVAILAVLkagaAY----VPLDPSYPAERLAYILEDSGAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 222 TVICDkpdkartlldhverretpglssiilmdpfekeltergrrcgvriqsmqevedcgrenrrapvpprPEDLSIVCFT 301
Cdd:cd05930 87 LVLTD-----------------------------------------------------------------PDDLAYVIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 302 SGTTGNPKGAMLTHGNVV---ADFSGFLKVTES----QWSPTCEDVHIS--YLPLAHmfermvqsvvychGGRI----GF 368
Cdd:cd05930 102 SGSTGKPKGVMVEHRGLVnllLWMQEAYPLTPGdrvlQFTSFSFDVSVWeiFGALLA-------------GATLvvlpEE 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 369 FQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFSQADTSLkrwvlefaarrkkaevrngiirndslwdklffnkiqas 448
Cdd:cd05930 169 VRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAALPSL-------------------------------------- 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 449 lggcvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFT--TPGDWTSGHV--GAPLPCNLIKLKDaEELN 523
Cdd:cd05930 211 -----RLVLVGGEALPPDLVrRWRELLPGARLVNLYGPTEATVDATYYrvPPDDEEDGRVpiGRPIPNTRVYVLD-ENLR 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 524 YFASKGEGEICVKGPNVFKGYLKDEERTSEA-----LDQEGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEK 597
Cdd:cd05930 285 PVPPGVPGELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIELGE 363
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2024456367 598 IENIYIRSDPVAQVYV---HGDSLQAFLVGIVVPDAEAMP 634
Cdd:cd05930 364 IEAALLAHPGVREAAVvarEDGDGEKRLVAYVVPDEGGEL 403
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
112-582 |
1.07e-31 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 130.09 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 112 DDARTMYEVFRRgfsISENGPCLGYRKPKQ--PYQWLSYKEVAERAEALGSGLLQQGCKPcTEQFIGVFAQNRpEWIISE 189
Cdd:cd05906 7 GAPRTLLELLLR---AAERGPTKGITYIDAdgSEEFQSYQDLLEDARRLAAGLRQLGLRP-GDSVILQFDDNE-DFIPAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 190 LACYTYSMVVVPLydtlGPGAIRYIVNTADistvicDKPDKARTLLD--HVerretpgLSSIILMDPFEKELTERGRrCG 267
Cdd:cd05906 82 WACVLAGFVPAPL----TVPPTYDEPNARL------RKLRHIWQLLGspVV-------LTDAELVAEFAGLETLSGL-PG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 268 VRIQSMQEVEDCGREnrrAPVPP-RPEDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflKVTESQWSPtcEDVHISYLP 346
Cdd:cd05906 144 IRVLSIEELLDTAAD---HDLPQsRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG--KIQHNGLTP--QDVFLNWVP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 347 LAHmfermVQSVVYCHggrigffQGDIRLLSDDMKALRPTIFPVVPRLLNRM--YDKIFSQADTSLKRWVLEFAARRKka 424
Cdd:cd05906 217 LDH-----VGGLVELH-------LRAVYLGCQQVHVPTEEILADPLRWLDLIdrYRVTITWAPNFAFALLNDLLEEIE-- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 425 evrngiirnDSLWDklffnkiqasLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYE-----GYGQTECTAGCTFTTP-- 497
Cdd:cd05906 283 ---------DGTWD----------LSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLPPdairpAFGMTETCSGVIYSRSfp 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 498 -GDWTSGH----VGAPLPCNLIKLKDAEelNYFASKGE-GEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGkWLP 571
Cdd:cd05906 344 tYDHSQALefvsLGRPIPGVSMRIVDDE--GQLLPEGEvGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLD 420
|
490
....*....|.
gi 2024456367 572 NGTLKIIDRKK 582
Cdd:cd05906 421 NGNLTITGRTK 431
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
146-653 |
1.62e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 129.89 E-value: 1.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPCTEqfIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVIC 225
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQPGDR--VGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVIC 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 DK---------------PDKARTLLDHVERRETPGLSSIILMDPFEKElterGRRCGVRIQSMQE-VEDCGRENRRAPVp 289
Cdd:PRK12583 124 ADafktsdyhamlqellPGLAEGQPGALACERLPELRGVVSLAPAPPP----GFLAWHELQARGEtVSREALAERQASL- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 290 pRPEDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSG-FLKVTEsqwsptcEDVHISYLPLAHMFErMVQSVVYC--HGG 364
Cdd:PRK12583 199 -DRDDPINIQYTSGTTGFPKGATLSHHNILnnGYFVAeSLGLTE-------HDRLCVPVPLYHCFG-MVLANLGCmtVGA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 365 RIGF----FQGDIRLLSddMKALRPTIFPVVPRL-LNRMYDKIFSQADTSlkrwvlefaarrkkaEVRNGIIrndslwdk 439
Cdd:PRK12583 270 CLVYpneaFDPLATLQA--VEEERCTALYGVPTMfIAELDHPQRGNFDLS---------------SLRTGIM-------- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 440 lffnkiqaslggcvrmivtGAAPASPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGD-----WTSghVGAPLPCNL 513
Cdd:PRK12583 325 -------------------AGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSLQTTAADdlerrVET--VGRTQPHLE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 514 IKLKDAEelNYFASKGE-GEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEY 592
Cdd:PRK12583 384 VKVVDPD--GATVPRGEiGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMI-IRGGEN 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024456367 593 IAPEKIENIYIRSDPVAQVYVHGdslqaflvgivVPD---AEAMPGWAKKR-GFDGTYEEL---CRNK 653
Cdd:PRK12583 461 IYPREIEEFLFTHPAVADVQVFG-----------VPDekyGEEIVAWVRLHpGHAASEEELrefCKAR 517
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
144-615 |
2.05e-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. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 127.41 E-value: 2.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 144 QWlSYKEVAERAEALGSGLLQQGCKPCTEqfIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTV 223
Cdd:cd05934 3 RW-TYAELLRESARIAAALAALGIRPGDR--VALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 224 ICDkpdkartlldhverretpgLSSIIlmdpfekeltergrrcgvriqsmqevedcgrenrrapvpprpedlsivcFTSG 303
Cdd:cd05934 80 VVD-------------------PASIL-------------------------------------------------YTSG 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 304 TTGNPKGAMLTHGNVVadfsgFLKVTESQWSP-TCEDVHISYLPLAHM---FERMVQSVVycHGGRIgffqgdirllsdd 379
Cdd:cd05934 92 TTGPPKGVVITHANLT-----FAGYYSARRFGlGEDDVYLTVLPLFHInaqAVSVLAALS--VGATL------------- 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 380 mkALRPTifpvvprllnrmydkifsqadtslkrwvleFAARRKKAEVRngiiRNDSLWdklfFNkiqaSLGGCVRMI--- 456
Cdd:cd05934 152 --VLLPR------------------------------FSASRFWSDVR----RYGATV----TN----YLGAMLSYLlaq 187
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 457 ------------VTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNLIKLKDAEELNy 524
Cdd:cd05934 188 ppspddrahrlrAAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQE- 266
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 525 fASKGE-GEICVK---GPNVFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIEN 600
Cdd:cd05934 267 -LPAGEpGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVER 343
|
490
....*....|....*
gi 2024456367 601 IYIRSDPVAQVYVHG 615
Cdd:cd05934 344 AILRHPAVREAAVVA 358
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
300-653 |
1.48e-30 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 123.54 E-value: 1.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 300 FTSGTTGNPKGAMLTHGNVV--ADFSGF-LKVTEsqwsptcEDVHISYLPLAHMFErMVQSVVYC--HGGRIgffqgdir 374
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVnnGYFIGErLGLTE-------QDRLCIPVPLFHCFG-SVLGVLACltHGATM-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 375 llsddmkalrptIFPvvprllnrmyDKIFSQADtslkrwVLEfAARRKKAEVRNGI----IRNDSLWDKLFFNKiqaslg 450
Cdd:cd05917 73 ------------VFP----------SPSFDPLA------VLE-AIEKEKCTALHGVptmfIAELEHPDFDKFDL------ 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 451 GCVRMIVTGAAPASPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGDWTS---GHVGAPLPCNLIKLKDAEElNYFA 526
Cdd:cd05917 118 SSLRTGIMAGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDSIEkrvNTVGRIMPHTEAKIVDPEG-GIVP 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 527 SKGE-GEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRS 605
Cdd:cd05917 197 PVGVpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGENIYPREIEEFLHTH 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2024456367 606 DPVAQVYVHGdslqaflvgivVPDA---EAMPGWAK-KRGFDGTYEEL---CRNK 653
Cdd:cd05917 276 PKVSDVQVVG-----------VPDErygEEVCAWIRlKEGAELTEEDIkayCKGK 319
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
272-623 |
2.16e-30 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 126.71 E-value: 2.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 272 SMQEVEDCGRenRRAPVPPR--PEDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgflkVTESQW--SPTCEDVH---ISY 344
Cdd:PRK08974 185 SFRSALHKGR--RMQYVKPElvPEDLAFLQYTGGTTGVAKGAMLTHRNMLAN------LEQAKAayGPLLHPGKelvVTA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 345 LPLAHMFERMVQSVVYCHGGRIGFF---QGDIRLLSDDMKALRPTIFPVVPRLLNRmydkifsqadtslkrWVlefaarr 421
Cdd:PRK08974 257 LPLYHIFALTVNCLLFIELGGQNLLitnPRDIPGFVKELKKYPFTAITGVNTLFNA---------------LL------- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 422 kkaevrngiirNDSLWDKLFFNKIQASLGGcvrmivtgAAPASPTVLGFLRAALGCQVYEGYGQTECT---AGCTFTTPG 498
Cdd:PRK08974 315 -----------NNEEFQELDFSSLKLSVGG--------GMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVNPYDLDY 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 499 dwTSGHVGAPLPCNLIKLKDaEELNYFASKGEGEICVKGPNVFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLKII 578
Cdd:PRK08974 376 --YSGSIGLPVPSTEIKLVD-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIV 451
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2024456367 579 DRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVY-------VHGDSLQAFLV 623
Cdd:PRK08974 452 DRKKDMI-LVSGFNVYPNEIEDVVMLHPKVLEVAavgvpseVSGEAVKIFVV 502
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
294-640 |
2.27e-30 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 122.22 E-value: 2.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 294 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESqwspTCEDVHISYLPLAHMFErmvqsvvYCHGGRIGFFQG-- 371
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADL----TEDDRYLIINPFFHTFG-------YKAGIVACLLTGat 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 372 -------DIRLLSDDMKALRPTIFPVVPRLLNRMYDKifsqadtslkrwvlefaARRKKAEVrngiirndslwdklffnk 444
Cdd:cd17638 70 vvpvavfDVDAILEAIERERITVLPGPPTLFQSLLDH-----------------PGRKKFDL------------------ 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 445 iqASLggcvRMIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGcTFTTPGD---WTSGHVGAPLPCNLIKLKDAe 520
Cdd:cd17638 115 --SSL----RAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVA-TMCRPGDdaeTVATTCGRACPGFEVRIADD- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 521 elnyfaskgeGEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIEN 600
Cdd:cd17638 187 ----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEG 255
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2024456367 601 IYIRSDPVAQVYV-------HGDSLQAFLVG--IVVPDAEAMPGWAKKR 640
Cdd:cd17638 256 ALAEHPGVAQVAVigvpderMGEVGKAFVVArpGVTLTEEDVIAWCRER 304
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
147-635 |
6.64e-30 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 124.56 E-value: 6.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 147 SYKEVAERAEALGSGLLQQGCKpcTEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLgpgAIRYIVNTADIS---TV 223
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLK--QNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIY---NERELDHSLNISkptIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 224 ICDKPDKARTLldHVERReTPGLSSIILMDPFEKElteRGRRCgvrIQSMQEVEDCGRENRRAPVPP---RPEDLSIVCF 300
Cdd:cd17642 121 FCSKKGLQKVL--NVQKK-LKIIKTIIILDSKEDY---KGYQC---LYTFITQNLPPGFNEYDFKPPsfdRDEQVALIMN 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 301 TSGTTGNPKGAMLTHGNVVADFSgflkvteSQWSPT-----CEDVHI-SYLPLAHMFERMVQSVVYCHGGRIGF---FQG 371
Cdd:cd17642 192 SSGSTGLPKGVQLTHKNIVARFS-------HARDPIfgnqiIPDTAIlTVIPFHHGFGMFTTLGYLICGFRVVLmykFEE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 372 D--IRLLSD---DMKALRPTIFPVVPR--LLNRmYDKifsqadTSLKRwvlefaarrkkaevrngiirndslwdklffnk 444
Cdd:cd17642 265 ElfLRSLQDykvQSALLVPTLFAFFAKstLVDK-YDL------SNLHE-------------------------------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 445 iqaslggcvrmIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNLIKLKDAEELN 523
Cdd:cd17642 306 -----------IASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 524 YFASKGEGEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYI 603
Cdd:cd17642 375 TLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILL 453
|
490 500 510
....*....|....*....|....*....|..
gi 2024456367 604 RSDPVaqvyvhgdsLQAFLVGIVVPDAEAMPG 635
Cdd:cd17642 454 QHPKI---------FDAGVAGIPDEDAGELPA 476
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
146-640 |
7.47e-30 |
|
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: 122.97 E-value: 7.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKpcTEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVIc 225
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVR--KGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 dkpdkartlldhverretpglssiilmdpfekeltergrrcgvrIQSMQEvedcgrenrrapvpprpeDLSIVCFTSGTT 305
Cdd:cd05935 79 --------------------------------------------VGSELD------------------DLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 306 GNPKGAMLTHGNVVADFSGflkvtESQWSP-TCEDVHISYLPLAHM--FERMVQSVVYCHGGRIGFFQGDIRLLSDDMKA 382
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQ-----SAVWTGlTPSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMARWDRETALELIEK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 383 LRPTIFPVVPRLLNRMYDKifsqadtslkrwvLEFAARRkkaevrngiirndslWDKLffnkiqaslggcvRMIVTGAAP 462
Cdd:cd05935 172 YKVTFWTNIPTMLVDLLAT-------------PEFKTRD---------------LSSL-------------KVLTGGGAP 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 463 ASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNLIKLKDAEELNYFASKGEGEICVKGPNVFK 542
Cdd:cd05935 211 MPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFK 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 543 GYLKDEERTSEA---LDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSDPVAQVYV------ 613
Cdd:cd05935 291 GYWNRPEETEESfieIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVisvpde 369
|
490 500 510
....*....|....*....|....*....|....
gi 2024456367 614 -HGDSLQAFLVgiVVP------DAEAMPGWAKKR 640
Cdd:cd05935 370 rVGEEVKAFIV--LRPeyrgkvTEEDIIEWAREQ 401
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
144-634 |
1.18e-29 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 123.17 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 144 QWLSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLyDTLGPGA-IRYIVNTADIST 222
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARGVGP--GDRVAVYLPRSARLVAAMLAVLKAGAAYVPL-DPDYPADrLRYILEDAEPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 223 VICDKpdkartlldhverretpglssiilmdpfekELTERGRRCGVRIqsMQEVEDCGRENRRAPVPPRPEDLSIVCFTS 302
Cdd:cd12116 88 VLTDD------------------------------ALPDRLPAGLPVL--LLALAAAAAAPAAPRTPVSPDDLAYVIYTS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 303 GTTGNPKGAMLTHGNVVADFSGF------------LKVTesqwsPTCEDvhIS----YLPLahmfermvqsvvyCHGGRI 366
Cdd:cd12116 136 GSTGRPKGVVVSHRNLVNFLHSMrerlglgpgdrlLAVT-----TYAFD--ISllelLLPL-------------LAGARV 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 367 GFFQGDI----RLLSDDMKALRPTIFpvvprllnrmydkifsQADTSLKRWVLefaarrkkaevrngiirnDSLWDKLff 442
Cdd:cd12116 196 VIAPRETqrdpEALARLIEAHSITVM----------------QATPATWRMLL------------------DAGWQGR-- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 443 nkiqASLggcvRMIVTGAApaSPTVLGFLRAALGCQVYEGYGQTECT--AGCTFTTPGDwTSGHVGAPLPCNLIKLKDAE 520
Cdd:cd12116 240 ----AGL----TALCGGEA--LPPDLAARLLSRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLDAA 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 521 eLNYFASKGEGEICVKGPNVFKGYLKDEERTSEAL-------DQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 593
Cdd:cd12116 309 -LRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFvpdpfagPGSRLYRTGDLVRRRADGRLEYLGRADGQVKI-RGHRI 386
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2024456367 594 APEKIENIYIRSDPVAQ--VYVHGDSLQAFLVGIVVPDAEAMP 634
Cdd:cd12116 387 ELGEIEAALAAHPGVAQaaVVVREDGGDRRLVAYVVLKAGAAP 429
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
144-631 |
2.21e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 122.61 E-value: 2.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 144 QWlSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTV 223
Cdd:PRK09088 22 RW-TYAELDALVGRLAAVLRRRGCVD--GERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 224 ICDkpdkartllDHVERretpglssiilmdpfekelterGRRCGVRIQSMQEVEDCGRENRRAPVPPrpEDLSIVCFTSG 303
Cdd:PRK09088 99 LGD---------DAVAA----------------------GRTDVEDLAAFIASADALEPADTPSIPP--ERVSLILFTSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 304 TTGNPKGAMLTHGN---VVADFSGFLKVtesqwsptceDVHISYLPLAHMFE--RMVQSV--VYCHGGRI----GFFQG- 371
Cdd:PRK09088 146 TSGQPKGVMLSERNlqqTAHNFGVLGRV----------DAHSSFLCDAPMFHiiGLITSVrpVLAVGGSIlvsnGFEPKr 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 372 DIRLLSDdmKALRPTIFPVVPRllnrMYDKIFSQADTSLKRWvlefaaRRKKAevrngiirndslwdklffnkiqaslgg 451
Cdd:PRK09088 216 TLGRLGD--PALGITHYFCVPQ----MAQAFRAQPGFDAAAL------RHLTA--------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 452 cvrmIVTGAAP-ASPTVLGFLraALGCQVYEGYGQTEctAGCTFTTPGDWT-----SGHVGAPLPCNLIKLKDAEElNYF 525
Cdd:PRK09088 257 ----LFTGGAPhAAEDILGWL--DDGIPMVDGFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVVDDQG-NDC 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 526 ASKGEGEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIEniyirs 605
Cdd:PRK09088 328 PAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIE------ 400
|
490 500
....*....|....*....|....*.
gi 2024456367 606 dpvAQVYVHGDSLQAFLVGivVPDAE 631
Cdd:PRK09088 401 ---AVLADHPGIRECAVVG--MADAQ 421
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
144-632 |
5.99e-29 |
|
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: 124.20 E-value: 5.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 144 QWLSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELA------CYtysmvvVPLyDTLGPGA-IRYIVN 216
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALGVGP--GDLVGVCLERSLEMVVALLAvlkagaAY------VPL-DPAYPAErLAYMLE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 217 TADISTVICDkpdkaRTLLDHVERRETPglssIILMDPfekeltergrrcgvriqsmQEVEDCGRENrrAPVPPRPEDLS 296
Cdd:COG1020 571 DAGARLVLTQ-----SALAARLPELGVP----VLALDA-------------------LALAAEPATN--PPVPVTPDDLA 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 297 IVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTES----QWSPTCEDVHIS--YLPLahmfermvqsvvyCHGGRIG 367
Cdd:COG1020 621 YVIYTSGSTGRPKGVMVEHRALVnllAWMQRRYGLGPGdrvlQFASLSFDASVWeiFGAL-------------LSGATLV 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 368 FFQGDIRL----LSDDMKALRPTIFPVVPrllnrmydkifsqadtslkrwvlefaarrkkaevrngiirndSLWDKLffn 443
Cdd:COG1020 688 LAPPEARRdpaaLAELLARHRVTVLNLTP------------------------------------------SLLRAL--- 722
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 444 kIQASLGGC--VRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTF--TTPGDWTSGHV--GAPLPCNLIKL 516
Cdd:COG1020 723 -LDAAPEALpsLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTVDSTYyeVTPPDADGGSVpiGRPIANTRVYV 801
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 517 KDAEelnyfaskGE-------GEICVKGPNVFKGYLKDEERTSEA-----LDQEG--WLHTGDIGKWLPNGTLKIIDRKK 582
Cdd:COG1020 802 LDAH--------LQpvpvgvpGELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNLEFLGRAD 873
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2024456367 583 HIFKLaQGEYIAPEKIENIyIRSDP-VAQ--VYVHGDSLQA-FLVGIVVPDAEA 632
Cdd:COG1020 874 DQVKI-RGFRIELGEIEAA-LLQHPgVREavVVAREDAPGDkRLVAYVVPEAGA 925
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
198-641 |
7.35e-29 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 120.62 E-value: 7.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 198 VVVPLYDTLGPGAIRYIVNTADISTVICDKPdkARTLLDhverretpgLSSIILMDPFEKELTERGRrcgvriqsmqeve 277
Cdd:cd05922 48 VFVPLNPTLKESVLRYLVADAGGRIVLADAG--AADRLR---------DALPASPDPGTVLDADGIR------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 278 dcGRENRRAPVPPRPEDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTESQWSPTCEDVHISY-LPLAHMFER 353
Cdd:cd05922 104 --AARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSiaeYLGITADDRALTVLPLSYDYgLSVLNTHLL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 354 MVQSVVYCHGGRIGffqgdiRLLSDDMKALRPTIFPVVPRLlnrmydkiFSQADTslkrwvlefaARRKKAEVrngiirn 433
Cdd:cd05922 182 RGATLVLTNDGVLD------DAFWEDLREHGATGLAGVPST--------YAMLTR----------LGFDPAKL------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 434 dslwdklffnkiqASLggcvRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFTTPG--DWTSGHVGAPLP 510
Cdd:cd05922 231 -------------PSL----RYLTQAGGRLPQETIARLRELLpGAQVYVMYGQTEATRRMTYLPPEriLEKPGSIGLAIP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 511 CNLIKLKDAEELNYfaSKGE-GEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAq 589
Cdd:cd05922 294 GGEFEILDDDGTPT--PPGEpGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF- 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024456367 590 GEYIAPEKIENIyIRSDPVAQVYV-------HGDSLQAFLVGIVVPDAEAMPGWAKKRG 641
Cdd:cd05922 371 GNRISPTEIEAA-ARSIGLIIEAAavglpdpLGEKLALFVTAPDKIDPKDVLRSLAERL 428
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
287-603 |
1.36e-28 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 121.10 E-value: 1.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 287 PVPP-RPEDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWS-PTCEDVHISYLPLAHMFermvqsvvychgG 364
Cdd:PLN02574 191 PKPViKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEyPGSDNVYLAALPMFHIY------------G 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 365 RIGFFQGDIRL-----------LSDDMKAL---RPTIFPVVPRLLnrmydkifsqadTSLKRwvlefAARRKKAEVRngi 430
Cdd:PLN02574 259 LSLFVVGLLSLgstivvmrrfdASDMVKVIdrfKVTHFPVVPPIL------------MALTK-----KAKGVCGEVL--- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 431 irndslwdklffnkiqaslgGCVRMIVTGAAPAS-PTVLGFLRAALGCQVYEGYGQTECTAGCT--FTTPGDWTSGHVGA 507
Cdd:PLN02574 319 --------------------KSLKQVSCGAAPLSgKFIQDFVQTLPHVDFIQGYGMTESTAVGTrgFNTEKLSKYSSVGL 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 508 PLPCNLIKLKDAEELNYFASKGEGEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKL 587
Cdd:PLN02574 379 LAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY 458
|
330
....*....|....*.
gi 2024456367 588 aQGEYIAPEKIENIYI 603
Cdd:PLN02574 459 -KGFQIAPADLEAVLI 473
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
146-659 |
1.60e-28 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 120.99 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVIC 225
Cdd:COG0365 40 LTYAELRREVNRFANALRALGVKK--GDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLIT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 D----KPDKARTLLDHVE--RRETPGLSSIILMDPFEKELTERGrrcgvrIQSMQEVEDcGRENRRAPVPPRPEDLSIVC 299
Cdd:COG0365 118 AdgglRGGKVIDLKEKVDeaLEELPSLEHVIVVGRTGADVPMEG------DLDWDELLA-AASAEFEPEPTDADDPLFIL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 300 FTSGTTGNPKGAMLTHGNVVAdfsGFLKVTESQWSPTCEDVH-----------ISYL---PLAH-----MFERmvqSVVY 360
Cdd:COG0365 191 YTSGTTGKPKGVVHTHGGYLV---HAATTAKYVLDLKPGDVFwctadigwatgHSYIvygPLLNgatvvLYEG---RPDF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 361 CHGGRIgffqgdIRLLSDdmkaLRPTIFPVVPRLLnRMydkifsqadtsLKRWVLEFAARRkkaevrngiirndSLwdkl 440
Cdd:COG0365 265 PDPGRL------WELIEK----YGVTVFFTAPTAI-RA-----------LMKAGDEPLKKY-------------DL---- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 441 ffnkiqASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECtaGCTFTTPGDWTS---GHVGAPLPCNLIKLK 517
Cdd:COG0365 306 ------SSL----RLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTET--GGIFISNLPGLPvkpGSMGKPVPGYDVAVV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 518 DAE--ELnyfASKGEGEICVKG--PNVFKGYLKDEERTSEAL--DQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGE 591
Cdd:COG0365 374 DEDgnPV---PPGEEGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVS-GH 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024456367 592 YIAPEKIENIYIRSDPVAQVYVhgdslqaflVGivVPDA---EAMPGWAK-KRGFDGTyEELcrNKELQKAI 659
Cdd:COG0365 450 RIGTAEIESALVSHPAVAEAAV---------VG--VPDEirgQVVKAFVVlKPGVEPS-DEL--AKELQAHV 507
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
293-615 |
1.85e-28 |
|
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: 118.60 E-value: 1.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 293 EDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF---LKVTEsqwsptcEDVHISYLPLAHM--FERMVQSVVYchGGRIG 367
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSalnLGLTE-------DDNWLCALPLFHIsgLSILMRSVIY--GMTVY 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 368 FFQG-DIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFSQADTSLkrwvlefaarrkkaevrngiirndslwdklffnkiq 446
Cdd:cd05912 148 LVDKfDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNL------------------------------------ 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 447 aslggcvRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTE-CTAGCTFTtPGDWTS--GHVGAPLPCNLIKLKDAEEln 523
Cdd:cd05912 192 -------RCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTEtCSQIVTLS-PEDALNkiGSAGKPLFPVELKIEDDGQ-- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 524 yfASKGEGEICVKGPNVFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYI 603
Cdd:cd05912 261 --PPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLL 336
|
330
....*....|..
gi 2024456367 604 RSDPVAQVYVHG 615
Cdd:cd05912 337 SHPAIKEAGVVG 348
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
147-613 |
2.74e-28 |
|
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: 118.14 E-value: 2.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 147 SYKEVAERAEALGSGLLQQGCkPCTEQFIGVFAQNRPEWIISELACYTYSMVVVPLyDTLGPGA-IRYIVNTADISTVIC 225
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGG-VGPGDRVAVLLERSAELVVAILAVLKAGAAYVPL-DPAYPAErLAFILEDAGARLLLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 DKPdkartlldHVERRETPGLSSIILMDPFEKELtergrrcgvriqsmqevEDCGRENRrAPVPPRPEDLSIVCFTSGTT 305
Cdd:TIGR01733 79 DSA--------LASRLAGLVLPVILLDPLELAAL-----------------DDAPAPPP-PDAPSGPDDLAYVIYTSGST 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 306 GNPKGAMLTHGNVVAdfsgFLKVTESQWSPTCEDVHISYLPLAH------MFermvqsVVYCHGGR--------IGFFQG 371
Cdd:TIGR01733 133 GRPKGVVVTHRSLVN----LLAWLARRYGLDPDDRVLQFASLSFdasveeIF------GALLAGATlvvppedeERDDAA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 372 DIRLLSDDMKAlrpTIFPVVPRLLNRMYDkifsQADTSLKRwvlefaarrkkaevrngiirndslwdklffnkiqaslgg 451
Cdd:TIGR01733 203 LLAALIAEHPV---TVLNLTPSLLALLAA----ALPPALAS--------------------------------------- 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 452 cVRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAGCT-FTTPGDWTSGHV----GAPLPCNLIKLKDaEELNYF 525
Cdd:TIGR01733 237 -LRLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWSTaTLVDPDDAPRESpvpiGRPLANTRLYVLD-DDLRPV 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 526 ASKGEGEICVKGPNVFKGYLKDEERTSE--------ALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 597
Cdd:TIGR01733 315 PVGVVGELYIGGPGVARGYLNRPELTAErfvpdpfaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGE 393
|
490
....*....|....*.
gi 2024456367 598 IENIYIRSDPVAQVYV 613
Cdd:TIGR01733 394 IEAALLRHPGVREAVV 409
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
144-615 |
3.08e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 119.19 E-value: 3.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 144 QWLSYKEVAERAEALGSGLLQQ-GCKPCTEqfIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADIsT 222
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIYElNVKKGER--IAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGT-T 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 223 VICDKPDKARTLLdhverrETPGLSSIILMdpfekeltergrrcgVRIQSMQEVEDCGRENRrapVPPRPEDLSIVCFTS 302
Cdd:PRK06839 103 VLFVEKTFQNMAL------SMQKVSYVQRV---------------ISITSLKEIEDRKIDNF---VEKNESASFIICYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 303 GTTGNPKGAMLTHGNVVADFSGFLKVTESqwspTCEDVHISYLPLAHMfermvqsvvychgGRIGFFqgdirllsddmkA 382
Cdd:PRK06839 159 GTTGKPKGAVLTQENMFWNALNNTFAIDL----TMHDRSIVLLPLFHI-------------GGIGLF------------A 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 383 LrPTIFP----VVPRLLNRmyDKIFSQADTSLKRWVLEFAARRKKaevrngiIRNDSLWDKLFFNKiqaslggcVRMIVT 458
Cdd:PRK06839 210 F-PTLFAggviIVPRKFEP--TKALSMIEKHKVTVVMGVPTIHQA-------LINCSKFETTNLQS--------VRWFYN 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 459 GAAPAS-PTVLGFLRAalGCQVYEGYGQTEcTAGCTFTTPGD---WTSGHVGAPLPCNLIKLKDaEELNYFASKGEGEIC 534
Cdd:PRK06839 272 GGAPCPeELMREFIDR--GFLFGQGFGMTE-TSPTVFMLSEEdarRKVGSIGKPVLFCDYELID-ENKNKVEVGEVGELL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 535 VKGPNVFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVYVH 614
Cdd:PRK06839 348 IRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQVINKLSDVYEVAVV 425
|
.
gi 2024456367 615 G 615
Cdd:PRK06839 426 G 426
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
280-615 |
6.62e-28 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 118.77 E-value: 6.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 280 GRENRRAPVPPRPEDLSIVCFTSGTTGNPKGAMLTHGNVVADFS---GFLKVTESQWSPTCED---VHISYLPLAHMFER 353
Cdd:PRK12492 194 GRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLqvrACLSQLGPDGQPLMKEgqeVMIAPLPLYHIYAF 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 354 MVQSVVYCHGGRIGFFQGDIRLLSDDMKALRPTIFPVVPRLlNRMYDKIFSQADtslkrwvlefaarrkkaevrngiirn 433
Cdd:PRK12492 274 TANCMCMMVSGNHNVLITNPRDIPGFIKELGKWRFSALLGL-NTLFVALMDHPG-------------------------- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 434 dslWDKLFFNKIQASLGGcvrmivtGAAPASPTVLGFlRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCN 512
Cdd:PRK12492 327 ---FKDLDFSALKLTNSG-------GTALVKATAERW-EQLTGCTIVEGYGLTETSPVASTNPYGELARlGTVGIPVPGT 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 513 LIKLKDaEELNYFASKGEGEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEY 592
Cdd:PRK12492 396 ALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLI-IVSGFN 473
|
330 340
....*....|....*....|...
gi 2024456367 593 IAPEKIENIYIRSDPVAQVYVHG 615
Cdd:PRK12492 474 VYPNEIEDVVMAHPKVANCAAIG 496
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
146-615 |
8.10e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 117.76 E-value: 8.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKpcTEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVIC 225
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLAALGVK--KGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLIT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 DkpdkartlldhverretpglssiilmDPFEKELTERGRrcgVRIQSMQEvedcGRENRRAPVPPRPED--LSIVcFTSG 303
Cdd:PRK03640 106 D--------------------------DDFEAKLIPGIS---VKFAELMN----GPKEEAEIQEEFDLDevATIM-YTSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 304 TTGNPKGAMLTHGNVVADFSGF---LKVTEsqwsptcEDVHISYLPLAHM--FERMVQSVVYchGGRIGFFQG-DIRLLS 377
Cdd:PRK03640 152 TTGKPKGVIQTYGNHWWSAVGSalnLGLTE-------DDCWLAAVPIFHIsgLSILMRSVIY--GMRVVLVEKfDAEKIN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 378 DDMKALRPTIFPVVPRLLNRMydkifsqadtslkrwvlefAARRKKAEVrngiirNDSLwdklffnkiqaslggcvRMIV 457
Cdd:PRK03640 223 KLLQTGGVTIISVVSTMLQRL-------------------LERLGEGTY------PSSF-----------------RCML 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 458 TGAAPASPTVLGFLRAAlGCQVYEGYGQTEcTAGCTFTTPGDWTS---GHVGAPL-PCNLIKLKDAEELNYFAskgEGEI 533
Cdd:PRK03640 261 LGGGPAPKPLLEQCKEK-GIPVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLfPCELKIEKDGVVVPPFE---EGEI 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 534 CVKGPNVFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVYV 613
Cdd:PRK03640 336 VVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPGVAEAGV 413
|
..
gi 2024456367 614 HG 615
Cdd:PRK03640 414 VG 415
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
146-653 |
1.08e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 118.37 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPCTEqfIGVFAQNRPEWIISELACYTYSMVVV---PLYDTlgpGAIRYIVNTADIST 222
Cdd:PRK08315 44 WTYREFNEEVDALAKGLLALGIEKGDR--VGIWAPNVPEWVLTQFATAKIGAILVtinPAYRL---SELEYALNQSGCKA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 223 VIC-------DKPDKARTL---LDHVERRET-----PGLSSIILMDPfEKElteRGrrcgvrIQSMQEVEDCGRENRRAP 287
Cdd:PRK08315 119 LIAadgfkdsDYVAMLYELapeLATCEPGQLqsarlPELRRVIFLGD-EKH---PG------MLNFDELLALGRAVDDAE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 288 VPPRPEDLSI-----VCFTSGTTGNPKGAMLTHGNVVADfsGFLkVTESQwSPTCED-----VhisylPLAHMFErMVQS 357
Cdd:PRK08315 189 LAARQATLDPddpinIQYTSGTTGFPKGATLTHRNILNN--GYF-IGEAM-KLTEEDrlcipV-----PLYHCFG-MVLG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 358 VVYC--HGGRI-----GFfqgdirllsDDMKALR-------------PTIFPVVprlLNrmyDKIFSQAD-TSLkrwvle 416
Cdd:PRK08315 259 NLACvtHGATMvypgeGF---------DPLATLAaveeerctalygvPTMFIAE---LD---HPDFARFDlSSL------ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 417 faarrkkaevRNGIirndslwdklffnkiqaslggcvrMivtgAAPASPT-----VLGFLRAAlgcQVYEGYGQTECTAG 491
Cdd:PRK08315 318 ----------RTGI------------------------M----AGSPCPIevmkrVIDKMHMS---EVTIAYGMTETSPV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 492 CTFTTPGD------WTsghVGAPLPCNLIKLKDAEelnyfasKGE-------GEICVKGPNVFKGYLKDEERTSEALDQE 558
Cdd:PRK08315 357 STQTRTDDplekrvTT---VGRALPHLEVKIVDPE-------TGEtvprgeqGELCTRGYSVMKGYWNDPEKTAEAIDAD 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 559 GWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVYVHGdslqaflvgivVPDA---EAMPG 635
Cdd:PRK08315 427 GWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEFLYTHPKIQDVQVVG-----------VPDEkygEEVCA 494
|
570 580
....*....|....*....|..
gi 2024456367 636 WAKKR-GFDGTYEEL---CRNK 653
Cdd:PRK08315 495 WIILRpGATLTEEDVrdfCRGK 516
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
146-632 |
1.28e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 117.75 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALgSGLLQQGCKPCTEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVIC 225
Cdd:PRK08314 36 ISYRELLEEAERL-AGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 D-------KPDKARTLLDHV-------ERRETPGlssiilmDPFEKELTERGRRCGVRIQSMQEVEDCGRENRRA-PVPP 290
Cdd:PRK08314 115 GselapkvAPAVGNLRLRHVivaqysdYLPAEPE-------IAVPAWLRAEPPLQALAPGGVVAWKEALAAGLAPpPHTA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 291 RPEDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkvteSQWSP-TCEDVHISYLPLAHM--FERMVQSVVYChGGRIg 367
Cdd:PRK08314 188 GPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGS-----VLWSNsTPESVVLAVLPLFHVtgMVHSMNAPIYA-GATV- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 368 ffqgdirllsddmkalrptifpVVprllnrmydkifsqadtsLKRWVLEFAARrkkAEVRNGIirndSLW--------DK 439
Cdd:PRK08314 261 ----------------------VL------------------MPRWDREAAAR---LIERYRV----THWtniptmvvDF 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 440 LFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWT-SGHVGAPL--------- 509
Cdd:PRK08314 294 LASPGLAERDLSSLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTE-TMAQTHSNPPDRPkLQCLGIPTfgvdarvid 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 510 PCNLIKLKDAEelnyfaskgEGEICVKGPNVFKGYLKDEERTSEA---LDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFK 586
Cdd:PRK08314 373 PETLEELPPGE---------VGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMIN 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2024456367 587 lAQGEYIAPEKIENIYIRSDPVAQVYV-------HGDSLQAFlvgiVVPDAEA 632
Cdd:PRK08314 444 -ASGFKVWPAEVENLLYKHPAIQEACViatpdprRGETVKAV----VVLRPEA 491
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
280-623 |
1.48e-27 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 117.81 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 280 GRENRRAPVPPRPEDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgflKVTESQWSPTCED--------VHISYLPLAHMF 351
Cdd:PRK07059 191 GARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVAN-----VLQMEAWLQPAFEkkprpdqlNFVCALPLYHIF 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 352 ERMVQSVVYCHGGRIGFF---QGDIRLLSDDMKALRPTIFPVVPRLLNRMYdkifsqadtslkrwvlefaarrkkaevrn 428
Cdd:PRK07059 266 ALTVCGLLGMRTGGRNILipnPRDIPGFIKELKKYQVHIFPAVNTLYNALL----------------------------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 429 giirNDSLWDKLFFNKIQASLGGcvrmivtGAAPASPTVLGFLRAAlGCQVYEGYG--QTECTAGCTFTTPGDWTsGHVG 506
Cdd:PRK07059 317 ----NNPDFDKLDFSKLIVANGG-------GMAVQRPVAERWLEMT-GCPITEGYGlsETSPVATCNPVDATEFS-GTIG 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 507 APLPCNLIKLKDaEELNYFASKGEGEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFk 586
Cdd:PRK07059 384 LPLPSTEVSIRD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMI- 461
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2024456367 587 LAQGEYIAPEKIENIyIRSDP----VAQVYVH----GDSLQAFLV 623
Cdd:PRK07059 462 LVSGFNVYPNEIEEV-VASHPgvleVAAVGVPdehsGEAVKLFVV 505
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
147-601 |
1.53e-27 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 117.54 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 147 SYKEVAERAEALGSGLLQQGCKPCTeqfigVFAQNRPEW---IISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTV 223
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGD-----RVAFQLPGWcefTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 224 ICDKPDKARTLLD--HVERRETPGLSSIILMDPFEKELTErgrrcgvrIQSMQEVEDcgRENRRAPVPPRPEDLSIVCFT 301
Cdd:PRK06087 126 FAPTLFKQTRPVDliLPLQNQLPQLQQIVGVDKLAPATSS--------LSLSQIIAD--YEPLTTAITTHGDELAAVLFT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 302 SGTTGNPKGAMLTHGNVVADFSGFLKVTESQWsptcEDVHISYLPLAHmfermvqSVVYCHGGRIGFFQGDIRLLSDDMK 381
Cdd:PRK06087 196 SGTEGLPKGVMLTHNNILASERAYCARLNLTW----QDVFMMPAPLGH-------ATGFLHGVTAPFLIGARSVLLDIFT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 382 ALRPTifpvvpRLLNRmydkifsQADTslkrWVL---EFaarrkkaevrngiirndsLWDKLFFNKIQASLGGCVRMIVT 458
Cdd:PRK06087 265 PDACL------ALLEQ-------QRCT----CMLgatPF------------------IYDLLNLLEKQPADLSALRFFLC 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 459 GAAPASPTVLgflRAAL--GCQVYEGYGQTECTAGcTFTTPGD---WTSGHVGAPLPCNLIKLKDaEELNYFASKGEGEI 533
Cdd:PRK06087 310 GGTTIPKKVA---RECQqrGIKLLSVYGSTESSPH-AVVNLDDplsRFMHTDGYAAAGVEIKVVD-EARKTLPPGCEGEE 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024456367 534 CVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENI 601
Cdd:PRK06087 385 ASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDI 451
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
294-632 |
1.66e-27 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 117.39 E-value: 1.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 294 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWspTCEDVHISYLPLAHMF--ERMVQSVVYCHGGRIGFFQG 371
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEM--IGQVVTLGLIPFFHIYgiTGICCATLRNKGKVVVMSRF 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 372 DIRLLSDDMKALRPTIFPVVPRL-LNRMYDKIFSQADTSlkrwvlefaarrkkaevrngiirndslwdKLffnKIQAslg 450
Cdd:PLN02330 263 ELRTFLNALITQEVSFAPIVPPIiLNLVKNPIVEEFDLS-----------------------------KL---KLQA--- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 451 gcvrmIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTagCTFTTPGDWTSGH-------VGAPLPCNLIKLKDAEEL 522
Cdd:PLN02330 308 -----IMTAAAPLAPELLtAFEAKFPGVQVQEAYGLTEHS--CITLTHGDPEKGHgiakknsVGFILPNLEVKFIDPDTG 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 523 NYFASKGEGEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIY 602
Cdd:PLN02330 381 RSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAIL 459
|
330 340 350
....*....|....*....|....*....|
gi 2024456367 603 IRSDPVAQVYVhgdslqaflvgIVVPDAEA 632
Cdd:PLN02330 460 LTHPSVEDAAV-----------VPLPDEEA 478
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
146-629 |
1.69e-27 |
|
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: 115.87 E-value: 1.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISEL------ACYtysmvvVPLyDTLGPGA-IRYIVNTA 218
Cdd:cd17653 23 LTYGELDAASNALANRLLQLGVVP--GDVVPLLSDRSLEMLVAILailkagAAY------VPL-DAKLPSArIQAILRTS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 219 DISTVICdkpdkartlldhverretpglssiilmdpfekeltergrrcgvriqsmqevedcgrenrrapvPPRPEDLSIV 298
Cdd:cd17653 94 GATLLLT---------------------------------------------------------------TDSPDDLAYI 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 299 CFTSGTTGNPKGAMLTHGNVVAdfsgFLKVTESQWSPTCEDVHISYLPLAhmFERMVQSV--VYCHGGRIgFFQGDIRLL 376
Cdd:cd17653 111 IFTSGSTGIPKGVMVPHRGVLN----YVSQPPARLDVGPGSRVAQVLSIA--FDACIGEIfsTLCNGGTL-VLADPSDPF 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 377 SDDMKALrpTIFPVVPRLLNRMYDKIFSQadtslkrwvlefaarrkkaevrngiirndslwdklffnkiqaslggcVRMI 456
Cdd:cd17653 184 AHVARTV--DALMSTPSILSTLSPQDFPN-----------------------------------------------LKTI 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 457 VTGAAPASPTVLGflRAALGCQVYEGYGQTECTAGCTFT--TPGDWTsgHVGAPLPCNLIKLKDAEELNyfASKGE-GEI 533
Cdd:cd17653 215 FLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTelLPGQPV--TIGKPIPNSTCYILDADLQP--VPEGVvGEI 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 534 CVKGPNVFKGYLKDEERTSEAL----DQEGWLH--TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDP 607
Cdd:cd17653 289 CISGVQVARGYLGNPALTASKFvpdpFWPGSRMyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEIEEVVLQSQP 367
|
490 500
....*....|....*....|....*
gi 2024456367 608 -VAQVY--VHGDSLQAFlvgiVVPD 629
Cdd:cd17653 368 eVTQAAaiVVNGRLVAF----VTPE 388
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
146-613 |
1.79e-27 |
|
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: 115.94 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTAdistvic 225
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGP--GDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRA------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 dkpdKARTLldhverretpglssiILMDPFekeltergrrcgvriqsmqevedcgRENRRAPVPprpEDLSIVCFTSGTT 305
Cdd:cd05903 73 ----KAKVF---------------VVPERF-------------------------RQFDPAAMP---DAVALLLFTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 306 GNPKGAMLTHGNVVADFSGFLKvtesQWSPTCEDVHISYLPLAHMfermvqsVVYCHGGRIGFFQGDIRLLSDDMKALRp 385
Cdd:cd05903 106 GEPKGVMHSHNTLSASIRQYAE----RLGLGPGDVFLVASPMAHQ-------TGFVYGFTLPLLLGAPVVLQDIWDPDK- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 386 tifpvVPRLLNRMYDKIFSQAD---TSLKRwVLEFAARRKKAevrngiirndslwdklffnkiqaslggcVRMIVTGAAP 462
Cdd:cd05903 174 -----ALALMREHGVTFMMGATpflTDLLN-AVEEAGEPLSR----------------------------LRTFVCGGAT 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 463 ASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGD----WTSGhvGAPLPCNLIKLKDAEElNYFASKGEGEICVKGP 538
Cdd:cd05903 220 VPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPedrrLYTD--GRPLPGVEIKVVDDTG-ATLAPGVEGELLSRGP 296
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024456367 539 NVFKGYLKDEERTSEALDqEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVYV 613
Cdd:cd05903 297 SVFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAV 369
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
146-582 |
4.98e-27 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 115.74 E-value: 4.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPCTEqfIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVIC 225
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVKPGDR--VAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVC 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 DkPDKARTLLDHVERRETPGLSSiiLMDPFEKELTERGRRCGVRIqsmqevedcgrenrrAPVPPRPEDLSIVCFTSGTT 305
Cdd:PRK07514 107 D-PANFAWLSKIAAAAGAPHVET--LDADGTGSLLEAAAAAPDDF---------------ETVPRGADDLAAILYTSGTT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 306 GNPKGAMLTHGNVVADfsgfLKVTESQWSPTCEDVHISYLPLAHMFERMVQS-VVYCHGGRIGFFQG-DIRLLSDDMKal 383
Cdd:PRK07514 169 GRSKGAMLSHGNLLSN----ALTLVDYWRFTPDDVLIHALPIFHTHGLFVATnVALLAGASMIFLPKfDPDAVLALMP-- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 384 RPTIFPVVPRLLNRMYdkifsqADTSLKRwvlEFAARrkkaevrngiirndslwdklffnkiqaslggcVRMIVTGAAPA 463
Cdd:PRK07514 243 RATVMMGVPTFYTRLL------QEPRLTR---EAAAH--------------------------------MRLFISGSAPL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 464 SPTVLGFLRAALGCQVYEGYGQTEcTAGCTfTTP--GDWTSGHVGAPLPCNLIKLKDAEELNYFASKGEGEICVKGPNVF 541
Cdd:PRK07514 282 LAETHREFQERTGHAILERYGMTE-TNMNT-SNPydGERRAGTVGFPLPGVSLRVTDPETGAELPPGEIGMIEVKGPNVF 359
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2024456367 542 KGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKK 582
Cdd:PRK07514 360 KGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGK 400
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
198-582 |
2.65e-26 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 114.67 E-value: 2.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 198 VVVPLYDTLGPGAIRYIVNTADISTVICDKPDKARTLLDHVE--RRETPGLSSIILMDPFEKELTERG-------RRCGV 268
Cdd:PRK07529 108 IANPINPLLEPEQIAELLRAAGAKVLVTLGPFPGTDIWQKVAevLAALPELRTVVEVDLARYLPGPKRlavplirRKAHA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 269 RIQSM-QEVEDCGRENRRAPVPPRPEDLSIVCFTSGTTGNPKGAMLTHGNVVADfsGFLKVTESQWSPtcEDVHISYLPL 347
Cdd:PRK07529 188 RILDFdAELARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVAN--AWLGALLLGLGP--GDTVFCGLPL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 348 AHMFERMVQSVVYCHGGR---IGFFQG--DIRLLSDDMK---ALRPTIFPVVPRLLNRMYDKIFSQADTSlkrwVLEFAA 419
Cdd:PRK07529 264 FHVNALLVTGLAPLARGAhvvLATPQGyrGPGVIANFWKiveRYRINFLSGVPTVYAALLQVPVDGHDIS----SLRYAL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 420 rrkkaevrngiirndslwdklffnkiqaslggcvrmivTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-G 498
Cdd:PRK07529 340 --------------------------------------CGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPdG 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 499 DWTSGHVGAPLPCNLIK-LKDAEELNYF--ASKGE-GEICVKGPNVFKGYLkDEERTSEALDQEGWLHTGDIGKWLPNGT 574
Cdd:PRK07529 382 ERRIGSVGLRLPYQRVRvVILDDAGRYLrdCAVDEvGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDLGRIDADGY 460
|
....*...
gi 2024456367 575 LKIIDRKK 582
Cdd:PRK07529 461 FWLTGRAK 468
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
282-603 |
7.40e-26 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 112.38 E-value: 7.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 282 ENRRAPVPPRPEDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWSPTCEDVHISYLPLAHMFErmVQSVVYC 361
Cdd:PLN02246 168 ENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYFHSDDVILCVLPMFHIYS--LNSVLLC 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 362 hGGRIG--------FfqgDIRLLSDDMKALRPTIFPVVPRLlnrmydkifsqadtslkrwVLEFAarrkkaevRNGIIRN 433
Cdd:PLN02246 246 -GLRVGaailimpkF---EIGALLELIQRHKVTIAPFVPPI-------------------VLAIA--------KSPVVEK 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 434 DSLwdklffnkiqASlggcVRMIVTGAAPASPTVLGFLRAALGCQVY-EGYGQTE-------CTAgctFT-TPGDWTSGH 504
Cdd:PLN02246 295 YDL----------SS----IRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMTEagpvlamCLA---FAkEPFPVKSGS 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 505 VGAPLPCNLIKLKDAEELNYFASKGEGEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHI 584
Cdd:PLN02246 358 CGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKEL 437
|
330
....*....|....*....
gi 2024456367 585 FKLaQGEYIAPEKIENIYI 603
Cdd:PLN02246 438 IKY-KGFQVAPAELEALLI 455
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
146-636 |
3.84e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 110.08 E-value: 3.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERA-------EALGsglLQQGCKpcteqfIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTA 218
Cdd:PRK06188 38 LTYGQLADRIsryiqafEALG---LGTGDA------VALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 219 DISTVICDK---PDKARTLLDHVerretPGLSSIILMDPFEKelterGRRCGVRIQSMqevedcgrENRRAPVPPRPEDL 295
Cdd:PRK06188 109 GISTLIVDPapfVERALALLARV-----PSLKHVLTLGPVPD-----GVDLLAAAAKF--------GPAPLVAAALPPDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 296 SIVCFTSGTTGNPKGAMLTHGNVVADFSGFLkvTESQWSPtcedvHISYL---PLAHMFERMVQSVVYcHGGRIGFFQG- 371
Cdd:PRK06188 171 AGLAYTGGTTGKPKGVMGTHRSIATMAQIQL--AEWEWPA-----DPRFLmctPLSHAGGAFFLPTLL-RGGTVIVLAKf 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 372 DIRLLSDDMKALRPTIFPVVPRLLNRMYDkifsqadtslkrwvlefAARRKKAEVrngiirndslwdklffnkiqASLgg 451
Cdd:PRK06188 243 DPAEVLRAIEEQRITATFLVPTMIYALLD-----------------HPDLRTRDL--------------------SSL-- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 452 cvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHV------GAPLPCNLIKLKDaEELNYF 525
Cdd:PRK06188 284 --ETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLRVALLD-EDGREV 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 526 ASkGE-GEICVKGPNVFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIR 604
Cdd:PRK06188 361 AQ-GEvGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMI-VTGGFNVFPREVEDVLAE 437
|
490 500 510
....*....|....*....|....*....|..
gi 2024456367 605 SDPVAQVYVHGdslqaflvgivVPDaeamPGW 636
Cdd:PRK06188 438 HPAVAQVAVIG-----------VPD----EKW 454
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
288-623 |
4.80e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 110.12 E-value: 4.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 288 VPPRPE-DLSIVCFTSGTTGNPKGAMLTHGNVVADfsgflKVTESQWSPTC---EDVHISYLPLAHMF-ERMVQSVVYCH 362
Cdd:PRK06710 200 VPCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSN-----TLMGVQWLYNCkegEEVVLGVLPFFHVYgMTAVMNLSIMQ 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 363 GGRIGFF-QGDIRLLSDDMKALRPTIFPVVPRL-LNRMYDKIFSQADTSlkrwvlefaarrkkaevrngiirndslwdkl 440
Cdd:PRK06710 275 GYKMVLIpKFDMKMVFEAIKKHKVTLFPGAPTIyIALLNSPLLKEYDIS------------------------------- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 441 ffnkiqaslggCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgctfTTPGDW-----TSGHVGAPLP---CN 512
Cdd:PRK06710 324 -----------SIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSP----VTHSNFlwekrVPGSIGVPWPdteAM 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 513 LIKLKDAEELnyfaSKGE-GEICVKGPNVFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGE 591
Cdd:PRK06710 389 IMSLETGEAL----PPGEiGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGF 462
|
330 340 350
....*....|....*....|....*....|....*....
gi 2024456367 592 YIAPEKIENIYIRSDPVAQVYV-------HGDSLQAFLV 623
Cdd:PRK06710 463 NVYPREVEEVLYEHEKVQEVVTigvpdpyRGETVKAFVV 501
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
286-635 |
2.47e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 107.00 E-value: 2.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 286 APVPPRPEDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkvtESQWSPTCEDVHISYLPLAHMfermvqsvvycHGGR 365
Cdd:PRK07787 121 RYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDAL----AEAWQWTADDVLVHGLPLFHV-----------HGLV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 366 IGFFqGDIRLLSDDMKALRPTIFPVVprllnrmydkifsqadtslkrwvlefAARRKKAEVRNGIirnDSLWDKLFFNKI 445
Cdd:PRK07787 186 LGVL-GPLRIGNRFVHTGRPTPEAYA--------------------------QALSEGGTLYFGV---PTVWSRIAADPE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 446 QASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNLIKLKDaEELNYF 525
Cdd:PRK07787 236 AARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVD-EDGGPV 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 526 ASKGE--GEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDR------KKHIFKLAQGEyiapek 597
Cdd:PRK07787 315 PHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGGYRIGAGE------ 388
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2024456367 598 IENIYIRSDPVAQVYVHG---DSLQAFLVGIVVPDAEAMPG 635
Cdd:PRK07787 389 IETALLGHPGVREAAVVGvpdDDLGQRIVAYVVGADDVAAD 429
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
146-664 |
4.65e-24 |
|
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: 105.79 E-value: 4.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGckPCTEQFIGVFAQNRPEWIISELACYTYSMVVVPLyDTLGPGA-IRYIVNTADISTVI 224
Cdd:cd05945 17 LTYRELKERADALAAALASLG--LDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPL-DASSPAErIREILDAAKPALLI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 225 CDkpdkartlldhverretpglssiilmdpfekeltergrrcgvriqsmqevedcgrenrrapvpprPEDLSIVCFTSGT 304
Cdd:cd05945 94 AD-----------------------------------------------------------------GDDNAYIIFTSGS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 305 TGNPKGAMLTHGNVVAdfsgFLKVTESQWSPTCEDVHISYLPLAhmFERMVQSVVYC--HGGrigffqgdirllsddmka 382
Cdd:cd05945 109 TGRPKGVQISHDNLVS----FTNWMLSDFPLGPGDVFLNQAPFS--FDLSVMDLYPAlaSGA------------------ 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 383 lrpTIFPVvPRLLnrmydkifsqadtslKRWVLEFAARRKKAEVrNGIIRNDSLWDKLF----FNkiQASLGGCVRMIVT 458
Cdd:cd05945 165 ---TLVPV-PRDA---------------TADPKQLFRFLAEHGI-TVWVSTPSFAAMCLlsptFT--PESLPSLRHFLFC 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 459 GAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFT--TP---GDWTSGHVGAPLPCNLIKLKDaEELNYFASKGEGEI 533
Cdd:cd05945 223 GEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIevTPevlDGYDRLPIGYAKPGAKLVILD-EDGRPVPPGEKGEL 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 534 CVKGPNVFKGYLKDEERTSEALDQE---GWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDPVAQ 610
Cdd:cd05945 302 VISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIELEEIEAALRQVPGVKE 380
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024456367 611 VYV----HGDSLQAfLVGIVVPDAEAMPGWAKkrgfdgtyeELcrNKELQKAIMEDMV 664
Cdd:cd05945 381 AVVvpkyKGEKVTE-LIAFVVPKPGAEAGLTK---------AI--KAELAERLPPYMI 426
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
147-615 |
5.96e-24 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 106.18 E-value: 5.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 147 SYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVICD 226
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKP--GDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 227 K---P--DKARTLLDHVERretpglssIILMDPFEKELTERGrrcgVRIQSMQEVedCGRENRRAPVPPRPE-DLSIVCF 300
Cdd:cd12119 105 RdflPllEAIAPRLPTVEH--------VVVMTDDAAMPEPAG----VGVLAYEEL--LAAESPEYDWPDFDEnTAAAICY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 301 TSGTTGNPKGAMLTHGNVV-----ADFSGFLKVTESqwsptceDVhisYLPLAHMFERMVQSVVYchggrIGFFQG---- 371
Cdd:cd12119 171 TSGTTGNPKGVVYSHRSLVlhamaALLTDGLGLSES-------DV---VLPVVPMFHVNAWGLPY-----AAAMVGaklv 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 372 ------DIRLLSDDMKALRPTIFPVVPRLLNRMYDkifsqadtslkrwvlefAARRKKAEVrngiirnDSLWdklffnki 445
Cdd:cd12119 236 lpgpylDPASLAELIEREGVTFAAGVPTVWQGLLD-----------------HLEANGRDL-------SSLR-------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 446 qaslggcvRMIVTGAAPASPTVLGFlrAALGCQVYEGYGQTECTAGCTFTTPgdwTSGHVGAP------------LPCNL 513
Cdd:cd12119 284 --------RVVIGGSAVPRSLIEAF--EERGVRVIHAWGMTETSPLGTVARP---PSEHSNLSedeqlalrakqgRPVPG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 514 IKLK----DAEELnyfASKGE--GEICVKGPNVFKGYLKDEErTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKL 587
Cdd:cd12119 351 VELRivddDGREL---PWDGKavGELQVRGPWVTKSYYKNDE-ESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKS 426
|
490 500
....*....|....*....|....*...
gi 2024456367 588 AqGEYIAPEKIENIYIRSDPVAQVYVHG 615
Cdd:cd12119 427 G-GEWISSVELENAIMAHPAVAEAAVIG 453
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
181-615 |
1.54e-23 |
|
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: 103.96 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 181 NRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVICDKpdkartlldhverretpglssiilmdpfekelt 260
Cdd:cd05972 34 RVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA--------------------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 261 ergrrcgvriqsmqevedcgrenrrapvpprpEDLSIVCFTSGTTGNPKGAMLTHG---NVVADFSGFLKVTESqwsptc 337
Cdd:cd05972 81 --------------------------------EDPALIYFTSGTTGLPKGVLHTHSyplGHIPTAAYWLGLRPD------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 338 eDVHIS--------------YLPLAHMFermvqSVVYCHGGRIgffqgdirllsDDMKALRptifpvvprLLNRMYDKIF 403
Cdd:cd05972 123 -DIHWNiadpgwakgawssfFGPWLLGA-----TVFVYEGPRF-----------DAERILE---------LLERYGVTSF 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 404 SQADTSLKRWVLEFAARRKKAEVRNgiirndslwdklffnkiqaslggcvrmIVTGAAPASPTVLGFLRAALGCQVYEGY 483
Cdd:cd05972 177 CGPPTAYRMLIKQDLSSYKFSHLRL---------------------------VVSAGEPLNPEVIEWWRAATGLPIRDGY 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 484 GQTECTAGCTFTTPGDWTSGHVGAPLPCNLIKLKDAEElNYFASKGEGEICVKGPNV--FKGYLKDEERTsEALDQEGWL 561
Cdd:cd05972 230 GQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDG-RELPPGEEGDIAIKLPPPglFLGYVGDPEKT-EASIRGDYY 307
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2024456367 562 HTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYIRSDPVAQVYVHG 615
Cdd:cd05972 308 LTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVESALLEHPAVAEAAVVG 360
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
146-632 |
1.74e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 105.24 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGckpcteqfIG------VFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTAD 219
Cdd:PRK07786 43 TTWRELDDRVAALAGALSRRG--------VGfgdrvlILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 220 ISTVICDKpdkARTLLDHVERRETPGLSSIILMDpfekeltergrrcGVRIQSMQEVEDCGRENRRAPVPPR-PEDL-SI 297
Cdd:PRK07786 115 AHVVVTEA---ALAPVATAVRDIVPLLSTVVVAG-------------GSSDDSVLGYEDLLAEAGPAHAPVDiPNDSpAL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 298 VCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQwspTCEDVHISYLPLAHMfeRMVQSVVychggrIGFFQGdirlls 377
Cdd:PRK07786 179 IMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGAD---INSDVGFVGVPLFHI--AGIGSML------PGLLLG------ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 378 ddmkalRPT-IFPVVPRLLNRMYDKIFSQADTSL----KRWVLEFAARRKKAevrngiiRNDSLwdklffnkiqaslggc 452
Cdd:PRK07786 242 ------APTvIYPLGAFDPGQLLDVLEAEKVTGIflvpAQWQAVCAEQQARP-------RDLAL---------------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 453 vRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAgCTFTTPGD---WTSGHVGAPLPCNLIKLKDaEELNYFASK 528
Cdd:PRK07786 293 -RVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEMSP-VTCMLLGEdaiRKLGSVGKVIPTVAARVVD-ENMNDVPVG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 529 GEGEICVKGPNVFKGYLKDEERTSEALDQeGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPV 608
Cdd:PRK07786 370 EVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPDI 447
|
490 500
....*....|....*....|....*..
gi 2024456367 609 AQVYVHGDSLQAF---LVGIVVPDAEA 632
Cdd:PRK07786 448 VEVAVIGRADEKWgevPVAVAAVRNDD 474
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
198-599 |
2.03e-23 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 106.55 E-value: 2.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 198 VVVPLYDTLGPGAIRYIVNTADISTVIcdkpdKARTLLDHVERR----ETPGLSSIILMDPFEKELTERGRRCG---VRI 270
Cdd:PRK08633 691 VPVNLNYTASEAALKSAIEQAQIKTVI-----TSRKFLEKLKNKgfdlELPENVKVIYLEDLKAKISKVDKLTAllaARL 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 271 QSMQEVEDCGRENRRapvpprPEDLSIVCFTSGTTGNPKGAMLTHGNVVAD---FSGFLKVTESqwsptceDVHISYLPL 347
Cdd:PRK08633 766 LPARLLKRLYGPTFK------PDDTATIIFSSGSEGEPKGVMLSHHNILSNieqISDVFNLRND-------DVILSSLPF 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 348 AHMFERMVQ---------SVVYcHggrigffqgdirllSDDMKAL---------RPTIFPVVPRLLnRMYdkifsqadts 409
Cdd:PRK08633 833 FHSFGLTVTlwlpllegiKVVY-H--------------PDPTDALgiaklvakhRATILLGTPTFL-RLY---------- 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 410 lkrwvlefaARRKKAevrngiirndslwDKLFFnkiqASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECT 489
Cdd:PRK08633 887 ---------LRNKKL-------------HPLMF----ASL----RLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETS 936
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 490 AGCTFTTP-----GDWT-----SGHVGAPLPCNLIKLKDAEELNYFASKGEGEICVKGPNVFKGYLKDEERTSEAL---D 556
Cdd:PRK08633 937 PVASVNLPdvlaaDFKRqtgskEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiD 1016
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2024456367 557 QEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIE 599
Cdd:PRK08633 1017 GIGWYVTGDKGHLDEDGFLTITDRYSRFAKIG-GEMVPLGAVE 1058
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
137-569 |
3.21e-23 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 104.58 E-value: 3.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 137 RKPKQPYQWLSYKEVAERAEALGSGLLQQGckpcteqfigvFAQNRPEWIISE---------LACYTYSMVVVPL---YD 204
Cdd:PRK08180 61 RGADGGWRRLTYAEALERVRAIAQALLDRG-----------LSAERPLMILSGnsiehallaLAAMYAGVPYAPVspaYS 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 205 TLG--PGAIRYIVNTADISTVICDKPDKARTLLDHVERRETPGLSSiilmdpfekelteRGRRCGVRIQSMQEVED--CG 280
Cdd:PRK08180 130 LVSqdFGKLRHVLELLTPGLVFADDGAAFARALAAVVPADVEVVAV-------------RGAVPGRAATPFAALLAtpPT 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 281 RENRRAPVPPRPEDLSIVCFTSGTTGNPKGAMLTHGNVVA------DFSGFLKVTESqwsptcedVHISYLPLAHMF--E 352
Cdd:PRK08180 197 AAVDAAHAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCAnqqmlaQTFPFLAEEPP--------VLVDWLPWNHTFggN 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 353 RMVQSVVYcHGGRI---------GFFQGDIRLLsddmKALRPTIFPVVPRLlnrmydkifsqadtslkrWVLEFAARRKK 423
Cdd:PRK08180 269 HNLGIVLY-NGGTLyiddgkptpGGFDETLRNL----REISPTVYFNVPKG------------------WEMLVPALERD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 424 AEVRngiirndslwdKLFFNKiqaslggcVRMIVTGAAPASPTVLGFL----RAALGCQVY--EGYGQTECTAGCTFTTP 497
Cdd:PRK08180 326 AALR-----------RRFFSR--------LKLLFYAGAALSQDVWDRLdrvaEATCGERIRmmTGLGMTETAPSATFTTG 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024456367 498 GDWTSGHVGAPLPCNLIKLKDAEelnyfaskGEGEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKW 569
Cdd:PRK08180 387 PLSRAGNIGLPAPGCEVKLVPVG--------GKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRF 450
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
292-640 |
3.24e-23 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 101.79 E-value: 3.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 292 PEDLSIVCFTSGTTGNPKGAMLTHGNVVADfsGFLKVTESQWSPTceDVHISYLPLAHMFERMVQsvvychgGRIGFFQG 371
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYN--AWMLALNSLFDPD--DVLLCGLPLFHVNGSVVT-------LLTPLASG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 372 DIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFSQADTSLKrwvlEFAARRKKAEVrngiirndslwdklffnkiqaslgG 451
Cdd:cd05944 70 AHVVLAGPAGYRNPGLFDNFWKLVERYRITSLSTVPTVYA----ALLQVPVNADI------------------------S 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 452 CVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNLIKLK--DAEELNYFASK 528
Cdd:cd05944 122 SLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKvlDGVGRLLRDCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 529 GE--GEICVKGPNVFKGYLkDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSD 606
Cdd:cd05944 202 PDevGEICVAGPGVFGGYL-YTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLRHP 279
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2024456367 607 PVAQVYVHG--DSLQAFL-VGIV--VPDAEAMPG----WAKKR 640
Cdd:cd05944 280 AVAFAGAVGqpDAHAGELpVAYVqlKPGAVVEEEellaWARDH 322
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
294-710 |
4.42e-23 |
|
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: 100.87 E-value: 4.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 294 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkvTESQWSPTCEDVHISYLPLAHM--FERMVQSVVychGGRIGFFQG 371
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAG----LHSRLGFGGGDSWLLSLPLYHVggLAILVRSLL---AGAELVLLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 372 DIRLLSDDMKALRPTIFPVVPRLLNRMYDKifSQADTSLKRwvlefaarrkkaevrngiirndslwdklffnkiqaslgg 451
Cdd:cd17630 74 RNQALAEDLAPPGVTHVSLVPTQLQRLLDS--GQGPAALKS--------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 452 cVRMIVTGAAPASPtvlGFLRAA--LGCQVYEGYGQTEcTAGCTFT-TPGDWTSGHVGAPLPCNLIKLKDaeelnyfask 528
Cdd:cd17630 113 -LRAVLLGGAPIPP---ELLERAadRGIPLYTTYGMTE-TASQVATkRPDGFGRGGVGVLLPGRELRIVE---------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 529 gEGEICVKGPNVFKGYLKDEERtsEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPV 608
Cdd:cd17630 178 -DGEIWVGGASLAMGYLRGQLV--PEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAV 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 609 AQVYVHG---DSLQAFLVGIVVPDAEAMPgwakkrgfdGTYEELCRNKelqkaimedmvrlgkesgLHSFEQVKAIHIhs 685
Cdd:cd17630 254 RDAFVVGvpdEELGQRPVAVIVGRGPADP---------AELRAWLKDK------------------LARFKLPKRIYP-- 304
|
410 420
....*....|....*....|....*
gi 2024456367 686 dmfsVQNGLLTPTLKAKRPELRDYF 710
Cdd:cd17630 305 ----VPELPRTGGGKVDRRALRAWL 325
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
146-615 |
5.61e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 103.47 E-value: 5.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPCTEqfIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVIC 225
Cdd:PRK08316 37 WTYAELDAAVNRVAAALLDLGLKKGDR--VAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 DkPDkartLLDHVErretpGLSSIILMDPFEKELTERGRRCGvriQSMQEVEDCGRENRRAP--VPPRPEDLSIVCFTSG 303
Cdd:PRK08316 115 D-PA----LAPTAE-----AALALLPVDTLILSLVLGGREAP---GGWLDFADWAEAGSVAEpdVELADDDLAQILYTSG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 304 TTGNPKGAMLTHGNVVADFSGflKVTESQWSPtcEDVHISYLPLAHMFERMV--QSVVYCHGGRIGFFQGDIRLLSDDMK 381
Cdd:PRK08316 182 TESLPKGAMLTHRALIAEYVS--CIVAGDMSA--DDIPLHALPLYHCAQLDVflGPYLYVGATNVILDAPDPELILRTIE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 382 ALRPTIF---PVVPRLLNRMYDkiFSQAD-TSLKrwvlefaarrkkaevrngiirndslwdKLFFnkiqaslggcvrmiv 457
Cdd:PRK08316 258 AERITSFfapPTVWISLLRHPD--FDTRDlSSLR---------------------------KGYY--------------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 458 tGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFTTPGDwtsgHVGAPLPC-----NL-IKLKDaEELNYFASKGE 530
Cdd:PRK08316 294 -GASIMPVEVLKELRERLpGLRFYNCYGQTEIAPLATVLGPEE----HLRRPGSAgrpvlNVeTRVVD-DDGNDVAPGEV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 531 GEICVKGPNVFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSDPVAQ 610
Cdd:PRK08316 368 GEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEALYTHPAVAE 445
|
....*
gi 2024456367 611 VYVHG 615
Cdd:PRK08316 446 VAVIG 450
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
291-664 |
5.62e-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: 5.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 291 RPEDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKV----TESQW----SPTCeDVHIsylplAHMFermvqsVVYCH 362
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRAlgltSESRVlqfaSYTF-DVSI-----LEIF------TTLAA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 363 GG---------RIGFFQGDIRllsdDMKA----LRPTifpvVPRLLNRmydkifsqadtslkrwvlefaarrkkAEVRng 429
Cdd:cd05918 172 GGclcipseedRLNDLAGFIN----RLRVtwafLTPS----VARLLDP--------------------------EDVP-- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 430 iirndslwdklffnkiqaslggCVRMIVTGAAPASPTVLGflRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAP 508
Cdd:cd05918 216 ----------------------SLRTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRP 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 509 LPCN--LIKLKDAEELnyfASKGE-GEICVKGPNVFKGYLKDEERTSEA-LDQEGWLH------------TGDIGKWLPN 572
Cdd:cd05918 272 LGATcwVVDPDNHDRL---VPIGAvGELLIEGPILARGYLNDPEKTAAAfIEDPAWLKqegsgrgrrlyrTGDLVRYNPD 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 573 GTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDP-----VAQVYVH-GDSLQAFLVGIVVPDAEAM---PGWAKKRGFD 643
Cdd:cd05918 349 GSLEYVGRKDTQVKI-RGQRVELGEIEHHLRQSLPgakevVVEVVKPkDGSSSPQLVAFVVLDGSSSgsgDGDSLFLEPS 427
|
410 420
....*....|....*....|...
gi 2024456367 644 GTYEELCR--NKELQKAIMEDMV 664
Cdd:cd05918 428 DEFRALVAelRSKLRQRLPSYMV 450
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
145-608 |
8.97e-23 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 103.09 E-value: 8.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 145 WLSYKEVAERAEALgSGLLQQGCKPCTEqfIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGA---IRYIVNTADIS 221
Cdd:cd05931 24 TLTYAELDRRARAI-AARLQAVGKPGDR--VLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 222 TVICDKPDKARtLLDHVERRETPGLSSIILMDPFEKELTERGRrcgvriqsmqevedcgrenrraPVPPRPEDLSIVCFT 301
Cdd:cd05931 101 VVLTTAAALAA-VRAFAASRPAAGTPRLLVVDLLPDTSAADWP----------------------PPSPDPDDIAYLQYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 302 SGTTGNPKGAMLTHGNVVADFSGFLKvtesQWSPTCEDVHISYLPLAH-MfermvqsvvychgGRIG------FFQGDIR 374
Cdd:cd05931 158 SGSTGTPKGVVVTHRNLLANVRQIRR----AYGLDPGDVVVSWLPLYHdM-------------GLIGglltplYSGGPSV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 375 LLSddmkalrPTIF---PVV-PRLLNRmYDKIFSQADTslkrWVLEFAARRKKAEVRNGIirnDsLwdklffnkiqaslg 450
Cdd:cd05931 221 LMS-------PAAFlrrPLRwLRLISR-YRATISAAPN----FAYDLCVRRVRDEDLEGL---D-L-------------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 451 GCVRMIVTGAAPASPTVL----------GFLRAAlgcqVYEGYGQTECTAGCTFTTPG----------DWTSGHV----- 505
Cdd:cd05931 271 SSWRVALNGAEPVRPATLrrfaeafapfGFRPEA----FRPSYGLAEATLFVSGGPPGtgpvvlrvdrDALAGRAvavaa 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 506 -----------GAPLPCNLIKLKDAEELNYFASKGEGEICVKGPNVFKGYLKDEERT------SEALDQEGWLHTGDIGk 568
Cdd:cd05931 347 ddpaarelvscGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATaetfgaLAATDEGGWLRTGDLG- 425
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2024456367 569 WLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSDPV 608
Cdd:cd05931 426 FLHDGELYITGRLKDLIIVR-GRNHYPQDIEATAEEAHPA 464
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
294-631 |
1.31e-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: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 294 DLSIVCFTSGTTGNPKGAMLTHGNVVA---DFSGFLKVTESqwsptceDVHISYLPLAHMFERMVQSVVYCHGGR---IG 367
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAanlQLIHAMGLTEA-------DVYLNMLPLFHIAGLNLALATFHAGGAnvvME 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 368 FFqgDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIfsqadtslkrwvlefaarrkkaevrngiIRNDSLWDKLffnkiqa 447
Cdd:cd17637 74 KF--DPAEALELIEEEKVTLMGSFPPILSNLLDAA----------------------------EKSGVDLSSL------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 448 slggcvrMIVTGAApaSPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTSGHVGAPLPCNLIKLKDaeELNYFAS 527
Cdd:cd17637 117 -------RHVLGLD--APETIQRFEETTGATFWSLYGQTE-TSGLVTLSPYRERPGSAGRPGPLVRVRIVD--DNDRPVP 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 528 KGE-GEICVKGPNVFKGYLKDEERTSEALDqEGWLHTGDIGKWLPNGTLKIIDRK--KHIFKlAQGEYIAPEKIENIYIR 604
Cdd:cd17637 185 AGEtGEIVVRGPLVFQGYWNLPELTAYTFR-NGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKVILE 262
|
330 340
....*....|....*....|....*..
gi 2024456367 605 SDPVAQVYVHGdslqaflvgivVPDAE 631
Cdd:cd17637 263 HPAIAEVCVIG-----------VPDPK 278
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
146-640 |
2.08e-22 |
|
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: 101.12 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELA------CYtysmvvVPLYDTLGPGAIRYIVNTAD 219
Cdd:cd12117 23 LTYAELNERANRLARRLRAAGVGP--GDVVGVLAERSPELVVALLAvlkagaAY------VPLDPELPAERLAFMLADAG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 220 ISTVICDKPDKARtlldhverretpglssiilmdpfekeLTERGRRCGVRIQSMQEVEDcgrenrRAPVPPRPEDLSIVC 299
Cdd:cd12117 95 AKVLLTDRSLAGR--------------------------AGGLEVAVVIDEALDAGPAG------NPAVPVSPDDLAYVM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 300 FTSGTTGNPKGAMLTHGNVVAdfsgflKVTESQW-SPTCEDVHISYLPL---AHMFERMVQSVvycHGGRIgffqgdirL 375
Cdd:cd12117 143 YTSGSTGRPKGVAVTHRGVVR------LVKNTNYvTLGPDDRVLQTSPLafdASTFEIWGALL---NGARL--------V 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 376 LSDDMKALRPtifpvvprllnrmydkifsqadTSLKRWVLEfaarrkkaevrNGIirnDSLWdkL---FFNKI----QAS 448
Cdd:cd12117 206 LAPKGTLLDP----------------------DALGALIAE-----------EGV---TVLW--LtaaLFNQLadedPEC 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 449 LGGcVRMIVTGAAPASPT-VLGFLRAALGCQVYEGYGQTECTagcTFTT-----PGDWTSGHV--GAPLPCNLIKLKDae 520
Cdd:cd12117 248 FAG-LRELLTGGEVVSPPhVRRVLAACPGLRLVNGYGPTENT---TFTTshvvtELDEVAGSIpiGRPIANTRVYVLD-- 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 521 ELNYFASKGE-GEICVKGPNVFKGYLKDEERTSE------ALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 593
Cdd:cd12117 322 EDGRPVPPGVpGELYVGGDGLALGYLNRPALTAErfvadpFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKI-RGFRI 400
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2024456367 594 APEKIENIYIRSDPVAQVYV------HGD-SLQAFLVGIVVPDAEAMPGWAKKR 640
Cdd:cd12117 401 ELGEIEAALRAHPGVREAVVvvredaGGDkRLVAYVVAEGALDAAELRAFLRER 454
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
146-634 |
3.95e-22 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 100.73 E-value: 3.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLydtlgpgairyivntadistvic 225
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGLLP--GDRVALRMGSNAEFVVALLAASRADLVVVPL----------------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 dkpDKARTLLDHVERRETPGLSSIILMDPFEKELTERGRRC--------GVRIQSMQEVE----DCGRENRRAPVPP--R 291
Cdd:PRK05852 99 ---DPALPIAEQRVRSQAAGARVVLIDADGPHDRAEPTTRWwpltvnvgGDSGPSGGTLSvhldAATEPTPATSTPEglR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 292 PEDLSIVcFTSGTTGNPKGAMLTHGNVVADFSGFlkVTESQWSPtcEDVHISYLPLAH---MFERMVQSVVycHGGRI-- 366
Cdd:PRK05852 176 PDDAMIM-FTGGTTGLPKMVPWTHANIASSVRAI--ITGYRLSP--RDATVAVMPLYHghgLIAALLATLA--SGGAVll 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 367 ---GFFQGdiRLLSDDMKALRPTIFPVVPRLlnrmYDKIFSQADTSlkrwvlefAARRKKAEVRngIIRNDSlwdklffn 443
Cdd:PRK05852 249 parGRFSA--HTFWDDIKAVGATWYTAVPTI----HQILLERAATE--------PSGRKPAALR--FIRSCS-------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 444 kiqaslggcvrmivtgaAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTfTTPGDWtSGHVGAPLPCN-LIKLKDAEEL 522
Cdd:PRK05852 305 -----------------APLTAETAQALQTEFAAPVVCAFGMTEATHQVT-TTQIEG-IGQTENPVVSTgLVGRSTGAQI 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 523 NYFASKGE-------GEICVKGPNVFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAP 595
Cdd:PRK05852 366 RIVGSDGLplpagavGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISP 443
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2024456367 596 EKIENIYIRSDPVAQVYVHGDSLQAF---LVGIVVPDAEAMP 634
Cdd:PRK05852 444 ERVEGVLASHPNVMEAAVFGVPDQLYgeaVAAVIVPRESAPP 485
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
146-641 |
1.09e-21 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 99.36 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVIC 225
Cdd:PRK13295 56 FTYRELAALVDRVAVGLARLGVGR--GDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 -------DKPDKARTLldhveRRETPGLSSIILM-----DPFEKELTERGRRcgvriqsmQEVEDCGRENRRAPvppRPE 293
Cdd:PRK13295 134 pktfrgfDHAAMARRL-----RPELPALRHVVVVggdgaDSFEALLITPAWE--------QEPDAPAILARLRP---GPD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 294 DLSIVCFTSGTTGNPKGAMLTHGNVVAD---FSGFLKVTEsqwsptcEDVHISYLPLAH----MFERMV-----QSVVYc 361
Cdd:PRK13295 198 DVTQLIYTSGTTGEPKGVMHTANTLMANivpYAERLGLGA-------DDVILMASPMAHqtgfMYGLMMpvmlgATAVL- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 362 hggrigffqGDIRllsDDMKALRptifpvvprlLNRMYDKIFSQADTSLkrwvLEFAARRKKAEVRNgiirndslwdklf 441
Cdd:PRK13295 270 ---------QDIW---DPARAAE----------LIRTEGVTFTMASTPF----LTDLTRAVKESGRP------------- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 442 fnkiQASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPGD---WTSGHVGAPLPCNLIKLKD 518
Cdd:PRK13295 311 ----VSSL----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA-VTLTKLDDpdeRASTTDGCPLPGVEVRVVD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 519 AEeLNYFASKGEGEICVKGPNVFKGYLKDEERTseALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKI 598
Cdd:PRK13295 382 AD-GAPLPAGQIGRLQVRGCSNFGGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEI 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2024456367 599 ENIYIRSDPVAQVYVHG---DSLQAFLVGIVVP------DAEAMPGWAKKRG 641
Cdd:PRK13295 458 EALLYRHPAIAQVAIVAypdERLGERACAFVVPrpgqslDFEEMVEFLKAQK 509
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
181-623 |
2.25e-21 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 98.22 E-value: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 181 NRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVICDkpDKARTLLDHVERRETPGLSSIILMDPFEKELT 260
Cdd:PRK08008 71 NCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTS--AQFYPMYRQIQQEDATPLRHICLTRVALPADD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 261 erGRRCGVRIQSMQEVEDCGRenrrapVPPRPEDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLkvTESQWSPTCEDV 340
Cdd:PRK08008 149 --GVSSFTQLKAQQPATLCYA------PPLSTDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYY--SAWQCALRDDDV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 341 HISYLPLAHMFermvqsvvychggrigfFQgdirlLSDDMKAlrptiFPVVPRLLnrmydkifsqadtslkrwVLE-FAA 419
Cdd:PRK08008 217 YLTVMPAFHID-----------------CQ-----CTAAMAA-----FSAGATFV------------------LLEkYSA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 420 RRKKAEVRngiirndslwdklffnKIQASLGGCVRMIVTG--AAPASPT--------VLGFLRAA----------LGCQV 479
Cdd:PRK08008 252 RAFWGQVC----------------KYRATITECIPMMIRTlmVQPPSANdrqhclreVMFYLNLSdqekdafeerFGVRL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 480 YEGYGQTECTAGCTFTTPGD---WTSghVGAPLPCNLIKLKDAEelNYFASKGE-GEICVKG---PNVFKGYLKDEERTS 552
Cdd:PRK08008 316 LTSYGMTETIVGIIGDRPGDkrrWPS--IGRPGFCYEAEIRDDH--NRPLPAGEiGEICIKGvpgKTIFKEYYLDPKATA 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024456367 553 EALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIyIRSDP-VAQVYVHG--DSL-----QAFLV 623
Cdd:PRK08008 392 KVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVELENI-IATHPkIQDIVVVGikDSIrdeaiKAFVV 468
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
146-634 |
2.86e-21 |
|
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: 97.39 E-value: 2.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVIC 225
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVGP--ESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 DkpdkartlldhverretpglssiilmdpfekeltergrrcgvriqsmqevedcgrenrrapvpprPEDLSIVCFTSGTT 305
Cdd:cd12115 103 D-----------------------------------------------------------------PDDLAYVIYTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 306 GNPKGAMLTHGNVVA------------DFSGFLKVTesqwsPTCEDVHI--SYLPLahmfermvqsvvyCHGGRIgffqg 371
Cdd:cd12115 118 GRPKGVAIEHRNAAAflqwaaaafsaeELAGVLAST-----SICFDLSVfeLFGPL-------------ATGGKV----- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 372 dirLLSDDMKALrptifPVVPRLlnrmydkifsqADTSLKRWVLEFAArrkkaevrngiirndSLwdkLFFNKIQASlgg 451
Cdd:cd12115 175 ---VLADNVLAL-----PDLPAA-----------AEVTLINTVPSAAA---------------EL---LRHDALPAS--- 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 452 cVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFT--TPGDWTSGHVGAPLPCNLIKLKDaEELNYFASK 528
Cdd:cd12115 215 -VRVVNLAGEPLPRDLVQRLYARLqVERVVNLYGPSEDTTYSTVApvPPGASGEVSIGRPLANTQAYVLD-RALQPVPLG 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 529 GEGEICVKGPNVFKGYLKDEERTSE-----ALDQEGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIY 602
Cdd:cd12115 293 VPGELYIGGAGVARGYLGRPGLTAErflpdPFGPGARLYrTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAAL 371
|
490 500 510
....*....|....*....|....*....|....*
gi 2024456367 603 IRSDPVAQ--VYVHGDSL-QAFLVGIVVPDAEAMP 634
Cdd:cd12115 372 RSIPGVREavVVAIGDAAgERRLVAYIVAEPGAAG 406
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
144-632 |
6.08e-21 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 96.63 E-value: 6.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 144 QWLSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLyDTLGPGA-IRYIVNTADIST 222
Cdd:cd17655 21 QTLTYRELNERANQLARTLREKGVGP--DTIVGIMAERSLEMIVGILGILKAGGAYLPI-DPDYPEErIQYILEDSGADI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 223 VICDKPDKARTLldhverretpGLSSIILMDPfekeltergrrcgvriqsmQEVEDCGRENrrAPVPPRPEDLSIVCFTS 302
Cdd:cd17655 98 LLTQSHLQPPIA----------FIGLIDLLDE-------------------DTIYHEESEN--LEPVSKSDDLAYVIYTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 303 GTTGNPKGAMLTHGNVVadfsgflkvtesqwsptcedvhisylplaHMFERMVQSVVYCHGGRIGFFQGdirlLSDDMka 382
Cdd:cd17655 147 GSTGKPKGVMIEHRGVV-----------------------------NLVEWANKVIYQGEHLRVALFAS----ISFDA-- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 383 lrpTIFPVVPRLL--NRMYdkIFSQADTSLKRWVLEFAaRRKKAEVRNGiirNDSLWDKLffNKIQASLGGCVRMIVTGA 460
Cdd:cd17655 192 ---SVTEIFASLLsgNTLY--IVRKETVLDGQALTQYI-RQNRITIIDL---TPAHLKLL--DAADDSEGLSLKHLIVGG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 461 APASPTVLGFL--RAALGCQVYEGYGQTECTAGCTF--TTPGDWTSGHV--GAPLPCNLIKLKDAEElnYFASKGE-GEI 533
Cdd:cd17655 261 EALSTELAKKIieLFGTNPTITNAYGPTETTVDASIyqYEPETDQQVSVpiGKPLGNTRIYILDQYG--RPQPVGVaGEL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 534 CVKGPNVFKGYLKDEERTSEALDQEGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDP 607
Cdd:cd17655 339 YIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-RGYRIELGEIEARLLQHPD 417
|
490 500
....*....|....*....|....*...
gi 2024456367 608 VAQ--VYVHGD-SLQAFLVGIVVPDAEA 632
Cdd:cd17655 418 IKEavVIARKDeQGQNYLCAYIVSEKEL 445
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
132-718 |
1.44e-20 |
|
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: 95.96 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 132 PCLGYRKPKQPYQWLSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTY---SMVVVPLYDTLGP 208
Cdd:cd05921 12 TWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGLSA--ERPLLILSGNSIEHALMALAAMYAgvpAAPVSPAYSLMSQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 209 --GAIRYIVNTADISTVICDKPDKARTLLDHVERRETPGLSSiilmdpfekelteRGRRCGVRIQSMQEVEDCGRENRRA 286
Cdd:cd05921 90 dlAKLKHLFELLKPGLVFAQDAAPFARALAAIFPLGTPLVVS-------------RNAVAGRGAISFAELAATPPTAAVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 287 PVPPR--PEDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWSPTCED--VHISYLPLAHMF--ERMVQSVVY 360
Cdd:cd05921 157 AAFAAvgPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQT----YPFFGEEppVLVDWLPWNHTFggNHNFNLVLY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 361 cHGGRI---------GFFQGDIRLLSDDMkalrPTIFPVVPR----LLNRMYDkifsqaDTSLKRwvlEFAARRKKAEVr 427
Cdd:cd05921 233 -NGGTLyiddgkpmpGGFEETLRNLREIS----PTVYFNVPAgwemLVAALEK------DEALRR---RFFKRLKLMFY- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 428 NGIIRNDSLWDKLffnkIQASLGGCVRMIVTGAapasptvlgflraalgcqvyeGYGQTECTAGCTFTTPGDWTSGHVGA 507
Cdd:cd05921 298 AGAGLSQDVWDRL----QALAVATVGERIPMMA---------------------GLGATETAPTATFTHWPTERSGLIGL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 508 PLPCNLIKLkdaeelnyFASKGEGEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWL----PNGTLKIIDRKKH 583
Cdd:cd05921 353 PAPGTELKL--------VPSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpddPAKGLVFDGRVAE 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 584 IFKLAQGEYIA--PekieniyIRSDPVAQV--YVHgDSL-----QAFLVGIVVPDAEAMPGWAkkRGFDGTYEELCRNKE 654
Cdd:cd05921 425 DFKLASGTWVSvgP-------LRARAVAACapLVH-DAVvagedRAEVGALVFPDLLACRRLV--GLQEASDAEVLRHAK 494
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024456367 655 LQKAIMEDMVRLGKESGLHSFEQVKAIhIHSDMFSVQNGLLTPTLKAKRPELRDYFKKQIEELY 718
Cdd:cd05921 495 VRAAFRDRLAALNGEATGSSSRIARAL-LLDEPPSIDKGEITDKGYINQRAVLERRAALVERLY 557
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
145-653 |
1.87e-20 |
|
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: 95.06 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 145 WLSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIvntadistvi 224
Cdd:cd12118 29 RYTWRQTYDRCRRLASALAALGISR--GDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFI---------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 225 cdkpdkartlLDHVErretpglSSIILMD-PFEKE-LTERGRRcgvriqsmqevedcgrenRRAPVPPRPEDLSIVC-FT 301
Cdd:cd12118 97 ----------LRHSE-------AKVLFVDrEFEYEdLLAEGDP------------------DFEWIPPADEWDPIALnYT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 302 SGTTGNPKGAMLTH--------GNVVAdfsgflkvTESQWSPtcedVHISYLPLAHmfermvqsvvyCHGGriGFFQGdi 373
Cdd:cd12118 142 SGTTGRPKGVVYHHrgaylnalANILE--------WEMKQHP----VYLWTLPMFH-----------CNGW--CFPWT-- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 374 rllsddMKALRPTIfpVVPRLLNrmYDKIFsqaDTSLKRWVLEFAArrkkAEVRNGIIRNDSLWDKLffnkiqaSLGGCV 453
Cdd:cd12118 195 ------VAAVGGTN--VCLRKVD--AKAIY---DLIEKHKVTHFCG----APTVLNMLANAPPSDAR-------PLPHRV 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 454 RMIVTGAAPaSPTVLgFLRAALGCQVYEGYGQTEcTAGCTftTPGDWTSGHVGAPLPcNLIKLKDAEELNYFASKGE--- 530
Cdd:cd12118 251 HVMTAGAPP-PAAVL-AKMEELGFDVTHVYGLTE-TYGPA--TVCAWKPEWDELPTE-ERARLKARQGVRYVGLEEVdvl 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 531 ---------------GEICVKGPNVFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAP 595
Cdd:cd12118 325 dpetmkpvprdgktiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENISS 402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024456367 596 EKIENIyirsdpvaqVYVHGDSLQAFLVGivVPDaeamPGWAK--------KRGFDGTYEEL---CRNK 653
Cdd:cd12118 403 VEVEGV---------LYKHPAVLEAAVVA--RPD----EKWGEvpcafvelKEGAKVTEEEIiafCREH 456
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
177-615 |
4.22e-20 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 94.48 E-value: 4.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 177 VFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVICDKPDkarTLLDHVE--RRETPGLSSIILMDP 254
Cdd:cd05970 77 LTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAED---NIPEEIEkaAPECPSKPKLVWVGD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 255 FEKELTERGRrcgvriqsmQEVEDCGR--ENRRAPVPPRPEDLSIVCFTSGTTGNPKgaMLTHgnvvaDFSGFLK--VTE 330
Cdd:cd05970 154 PVPEGWIDFR---------KLIKNASPdfERPTANSYPCGEDILLVYFSSGTTGMPK--MVEH-----DFTYPLGhiVTA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 331 SQWSPTCED-VHISYLPLAhmFERMVQSVVYchggriGFFQGDIRLLSDDMKALRPtifpvvprllNRMYDKIfsqadts 409
Cdd:cd05970 218 KYWQNVREGgLHLTVADTG--WGKAVWGKIY------GQWIAGAAVFVYDYDKFDP----------KALLEKL------- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 410 LKRWVLEFAArrkKAEVRNGIIRND-SLWDklfFNKIqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEC 488
Cdd:cd05970 273 SKYGVTTFCA---PPTIYRFLIREDlSRYD---LSSL--------RYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTET 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 489 TAgCTFTTPG-DWTSGHVGAPLPCNLIKLKDAEELNYFASKgEGEICV---KGPNV--FKGYLKDEERTSEALdQEGWLH 562
Cdd:cd05970 339 TL-TIATFPWmEPKPGSMGKPAPGYEIDLIDREGRSCEAGE-EGEIVIrtsKGKPVglFGGYYKDAEKTAEVW-HDGYYH 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2024456367 563 TGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYIRSDPVAQVYVHG 615
Cdd:cd05970 416 TGDAAWMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVESALIQHPAVLECAVTG 467
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
146-641 |
6.27e-20 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 95.03 E-value: 6.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGsGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVIC 225
Cdd:PRK06814 659 LTYRKLLTGAFVLG-RKLKKNTPP--GENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 DKP--DKARtLLDHVErretpGLSS---IILMDPFEKELTERGRRCGVRIQSMQEVEDCGRenrrapvppRPEDLSIVCF 300
Cdd:PRK06814 736 SRAfiEKAR-LGPLIE-----ALEFgirIIYLEDVRAQIGLADKIKGLLAGRFPLVYFCNR---------DPDDPAVILF 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 301 TSGTTGNPKGAMLTHGNVVA---------DFSGflkvtesqwsptcEDVHISYLPLAHMFermvqsvvychggriGFFQG 371
Cdd:PRK06814 801 TSGSEGTPKGVVLSHRNLLAnraqvaariDFSP-------------EDKVFNALPVFHSF---------------GLTGG 852
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 372 DIRLLSDDMKAL---RPTIFPVVPRLLnrmYDK----IFSqADTSLkrwvlefaarrkkaevrNGIIRNDSLWDklFFNk 444
Cdd:PRK06814 853 LVLPLLSGVKVFlypSPLHYRIIPELI---YDTnatiLFG-TDTFL-----------------NGYARYAHPYD--FRS- 908
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 445 iqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNLIKLKDAEELNy 524
Cdd:PRK06814 909 --------LRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGID- 979
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 525 fasKGeGEICVKGPNVFKGYLKDEE-RTSEALdQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYI 603
Cdd:PRK06814 980 ---EG-GRLFVRGPNVMLGYLRAENpGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAVEELAA 1053
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2024456367 604 RSDPvaqvyvhgDSLQAflvGIVVPDA-----------------EAMPGWAKKRG 641
Cdd:PRK06814 1054 ELWP--------DALHA---AVSIPDArkgeriillttasdatrAAFLAHAKAAG 1097
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
292-721 |
2.20e-19 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 92.55 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 292 PEDLSIVCFTSGTTGNPKGAMLTHGNVVAdfSGFLKVTESQWSPtcEDVHISYLPLAH-------MFERMVQSvvyCHGG 364
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSALIV--QSLAKIAIVGYGE--DDVYLHTAPLCHigglssaLAMLMVGA---CHVL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 365 RIGFfqgDIRLLSDDMKALRPTIFPVVPRLLnrmydkifsqADtslkrwVLEFAARRKKAEVRNgiirndslwdklffnk 444
Cdd:PLN02860 244 LPKF---DAKAALQAIKQHNVTSMITVPAMM----------AD------LISLTRKSMTWKVFP---------------- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 445 iqaslggCVRMIVTGAAPASP-----TVLGFLRAALgcqvYEGYGQTECTAGCTFTTPGDWT-----------------S 502
Cdd:PLN02860 289 -------SVRKILNGGGSLSSrllpdAKKLFPNAKL----FSAYGMTEACSSLTFMTLHDPTlespkqtlqtvnqtkssS 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 503 GH------VGAPLPCNLIKLKDAEelnyfaSKGEGEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLK 576
Cdd:PLN02860 358 VHqpqgvcVGKPAPHVELKIGLDE------SSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLW 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 577 IIDRKKHIFKlAQGEYIAPEKIENIYIRSDPVAQVYVHGdSLQAFLVGIVVPDAEAMPGWakkRGFDGTYEELCRNKELQ 656
Cdd:PLN02860 432 LIGRSNDRIK-TGGENVYPEEVEAVLSQHPGVASVVVVG-VPDSRLTEMVVACVRLRDGW---IWSDNEKENAKKNLTLS 506
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024456367 657 KAIMEDMVRlgkESGLHSFEQVKAIHIHSDMFSvqnglLTPTLKAKRPELRDYFKKQIEELYSSI 721
Cdd:PLN02860 507 SETLRHHCR---EKNLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEVRREVLSHLQSLPSNL 563
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
146-632 |
2.77e-19 |
|
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: 91.22 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLyDTLGPGA-IRYIVNTADISTVI 224
Cdd:cd17643 13 LTYGELDARANRLARTLRAEGVGP--GDRVALALPRSAELIVALLAILKAGGAYVPI-DPAYPVErIAFILADSGPSLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 225 CDkpdkartlldhverretpglssiilmdpfekeltergrrcgvriqsmqevedcgrenrrapvpprPEDLSIVCFTSGT 304
Cdd:cd17643 90 TD-----------------------------------------------------------------PDDLAYVIYTSGS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 305 TGNPKGAMLTHGNVVADFSGflkvTESQWSPTCEDVHISYLPLAHMFermvqSV-----VYCHGGRIGFFQGDIRLLSDD 379
Cdd:cd17643 105 TGRPKGVVVSHANVLALFAA----TQRWFGFNEDDVWTLFHSYAFDF-----SVweiwgALLHGGRLVVVPYEVARSPED 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 380 MkalrptifpvvPRLLNRMYDKIFSQADTSLKRWVlefaarrkkAEVRNGIIRNDSLwdklffnkiqaslggcvRMIVTG 459
Cdd:cd17643 176 F-----------ARLLRDEGVTVLNQTPSAFYQLV---------EAADRDGRDPLAL-----------------RYVIFG 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 460 AAPASPTVLGFLRAALGC---QVYEGYGQTECTAGCTFT--TPGDW---TSGHVGAPLPCNLIKLKDAEeLNYFASKGEG 531
Cdd:cd17643 219 GEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFRplDAADLpaaAASPIGRPLPGLRVYVLDAD-GRPVPPGVVG 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 532 EICVKGPNVFKGYLKDEERTSE-------ALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIR 604
Cdd:cd17643 298 ELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI-RGFRIELGEIEAALAT 376
|
490 500 510
....*....|....*....|....*....|.
gi 2024456367 605 SDPVAQVYV---HGDSLQAFLVGIVVPDAEA 632
Cdd:cd17643 377 HPSVRDAAVivrEDEPGDTRLVAYVVADDGA 407
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
274-623 |
1.41e-18 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 89.06 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 274 QEVEDCGRENRRAPVPPRPEDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSG--FLKVTEsqwsptcEDVHISylpLAH 349
Cdd:cd05919 72 DDYAYIARDCEARLVVTSADDIAYLLYSSGTTGPPKGVMHAHRDPLlfADAMAreALGLTP-------GDRVFS---SAK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 350 MFermvqsVVYCHGGRIGF--FQGDIRLLSDD----------MKALRPTIFPVVPRLLNRMYD-KIFSQADTSLKRwvle 416
Cdd:cd05919 142 MF------FGYGLGNSLWFplAVGASAVLNPGwptaervlatLARFRPTVLYGVPTFYANLLDsCAGSPDALRSLR---- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 417 faarrkkaevrngiirndslwdklffnkiqaslggcvrmIVTGAAPASPTVLG-FLRAALGCQVYEGYGQTEctAGCTFT 495
Cdd:cd05919 212 ---------------------------------------LCVSAGEALPRGLGeRWMEHFGGPILDGIGATE--VGHIFL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 496 T--PGDWTSGHVGAPLPCNLIKLKDaEELNYFASKGEGEICVKGPNVFKGYLKDEErTSEALDQEGWLHTGDIGKWLPNG 573
Cdd:cd05919 251 SnrPGAWRLGSTGRPVPGYEIRLVD-EEGHTIPPGEEGDLLVRGPSAAVGYWNNPE-KSRATFNGGWYRTGDKFCRDADG 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024456367 574 TLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSDPVAQVYV----HGDSL---QAFLV 623
Cdd:cd05919 329 WYTHAGRADDMLKVG-GQWVSPVEVESLIIQHPAVAEAAVvavpESTGLsrlTAFVV 384
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
147-623 |
1.48e-18 |
|
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: 89.03 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 147 SYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVICD 226
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEK--GDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 227 KPDkartlldhverretpglssiilmdpfekeltergrrcgvriqsmqevedcgrenrrapvpprpeDLSIVCFTSGTTG 306
Cdd:cd05971 86 GSD----------------------------------------------------------------DPALIIYTSGTTG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 307 NPKGAMLTH----GNVVAD---FSGFLKVTESQWSPT-------CEDVHISYL----P-LAHMFERmvqsvvychggrig 367
Cdd:cd05971 102 PPKGALHAHrvllGHLPGVqfpFNLFPRDGDLYWTPAdwawiggLLDVLLPSLyfgvPvLAHRMTK-------------- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 368 fFQGD--IRLLSD---DMKALRPTIFpvvprllnrmydKIFSQADTSLKRWVLEfaarrkkaevrngiirndslwdklff 442
Cdd:cd05971 168 -FDPKaaLDLMSRygvTTAFLPPTAL------------KMMRQQGEQLKHAQVK-------------------------- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 443 nkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEC---TAGCTFTTPGDwtSGHVGAPLPCNLIKLKDA 519
Cdd:cd05971 209 ----------LRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECnlvIGNCSALFPIK--PGSMGKPIPGHRVAIVDD 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 520 EElNYFASKGEGEICVKGPN--VFKGYLKDEERTsEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEK 597
Cdd:cd05971 277 NG-TPLPPGEVGEIAVELPDpvAFLGYWNNPSAT-EKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAE 353
|
490 500 510
....*....|....*....|....*....|...
gi 2024456367 598 IENIYIRSDPVAQVYV-------HGDSLQAFLV 623
Cdd:cd05971 354 IEECLLKHPAVLMAAVvgipdpiRGEIVKAFVV 386
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
146-635 |
1.80e-18 |
|
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: 89.26 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVIC 225
Cdd:cd17646 24 LTYRELDERANRLAHLLRARGVGP--EDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 DKPdkartlldhverretpglssiilmdpfekeLTERGRRcGVRIQSMQEVEDCGRENRRAPVPPRPEDLSIVCFTSGTT 305
Cdd:cd17646 102 TAD------------------------------LAARLPA-GGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGST 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 306 GNPKGAMLTHGNVVadfsgflkvtesqwsptcedvhisylplahmfermvqsvvychgGRIGFFQGDIRLLSDDmkalrp 385
Cdd:cd17646 151 GRPKGVMVTHAGIV--------------------------------------------NRLLWMQDEYPLGPGD------ 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 386 tifpvvprllnRMYDKIFSQADTSLKR--WVLEFAARRKKAEVRN--------GIIRND---------SLWDkLFFNKIQ 446
Cdd:cd17646 181 -----------RVLQKTPLSFDVSVWElfWPLVAGARLVVARPGGhrdpaylaALIREHgvttchfvpSMLR-VFLAEPA 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 447 ASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHV--GAPLPCNLIKLKDAeELN 523
Cdd:cd17646 249 AGSCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVThWPVRGPAETPSVpiGRPVPNTRLYVLDD-ALR 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 524 YFASKGEGEICVKGPNVFKGYLKDEERTSEA-----LDQEGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 597
Cdd:cd17646 328 PVPVGVPGELYLGGVQLARGYLGRPALTAERfvpdpFGPGSRMYrTGDLARWRPDGALEFLGRSDDQVKI-RGFRVEPGE 406
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2024456367 598 IENIYIRSDPVAQ--VYVHGD-SLQAFLVGIVVPDAEAMPG 635
Cdd:cd17646 407 IEAALAAHPAVTHavVVARAApAGAARLVGYVVPAAGAAGP 447
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
132-615 |
2.34e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 88.79 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 132 PCLGYRKpkqpyQWLSYKEVAERAEALGSGLLQQGCKpcTEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAI 211
Cdd:PRK06145 19 AALVYRD-----QEISYAEFHQRILQAAGMLHARGIG--QGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 212 RYIVNTADistvicdkpdkARTLLDHVERRETPGL-SSIILMDPFEKELTERGRRCGVRIQSMQevedcgrenrrapvPP 290
Cdd:PRK06145 92 AYILGDAG-----------AKLLLVDEEFDAIVALeTPKIVIDAAAQADSRRLAQGGLEIPPQA--------------AV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 291 RPEDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTEsqwsptcEDVHISYLPLAHMFERMVQSV-VYCHGGRI 366
Cdd:PRK06145 147 APTDLVRLMYTSGTTDRPKGVMHSYGNLHwksIDHVIALGLTA-------SERLLVVGPLYHVGAFDLPGIaVLWVGGTL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 367 GF---FQGDIRLLSDDMKALRPTIFpvVPRLLNRMY-----DKIfsqaDTSLKRWVLefAARRKKAEVRngiIRNdslwd 438
Cdd:PRK06145 220 RIhreFDPEAVLAAIERHRLTCAWM--APVMLSRVLtvpdrDRF----DLDSLAWCI--GGGEKTPESR---IRD----- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 439 klffnkiqaslggcvrmivtgaapasptvlgFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPCNLIKL 516
Cdd:PRK06145 284 -------------------------------FTRVFTRARYIDAYGLTETCSGDTLMEAGREIEkiGSTGRALAHVEIRI 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 517 KDaEELNYFASKGEGEICVKGPNVFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPE 596
Cdd:PRK06145 333 AD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASS 409
|
490
....*....|....*....
gi 2024456367 597 KIENIYIRSDPVAQVYVHG 615
Cdd:PRK06145 410 EVERVIYELPEVAEAAVIG 428
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
292-642 |
3.47e-18 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 87.91 E-value: 3.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 292 PEDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWSPtcedvhISYLPLAHM--------FERMVqsvvyCHG 363
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFP------VRLLQMASFsfdvfagdFARSL-----LNG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 364 GRIGFFQGDIRL----LSDDMKALRPTIFPVVPrllnrmydkifsqadtSLKRWVLEFAARRKK--AEVRNGIIRNDSLW 437
Cdd:cd17650 161 GTLVICPDEVKLdpaaLYDLILKSRITLMESTP----------------ALIRPVMAYVYRNGLdlSAMRLLIVGSDGCK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 438 DKlFFNKIQASLGGCVRMIvtgaapaspTVLGFLRAALGCQVYEGYGQTECTAGctfTTPgdwtsghVGAPLPCNLIKLK 517
Cdd:cd17650 225 AQ-DFKTLAARFGQGMRII---------NSYGVTEATIDSTYYEEGRDPLGDSA---NVP-------IGRPLPNTAMYVL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 518 DaEELNYFASKGEGEICVKGPNVFKGYLKDEERTSEALDQ------EGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGE 591
Cdd:cd17650 285 D-ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVEnpfapgERMYRTGDLARWRADGNVELLGRVDHQVKI-RGF 362
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2024456367 592 YIAPEKIENIYIRSDPVAQVYV---HGDSLQAFLVGIVVPDAEamPGWAKKRGF 642
Cdd:cd17650 363 RIELGEIESQLARHPAIDEAVVavrEDKGGEARLCAYVVAAAT--LNTAELRAF 414
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
284-610 |
3.52e-18 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 89.00 E-value: 3.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 284 RRAPVPPRPEDLSIVCFTSGTTGNPKGAMLTH----GNV-----VADFsgflkvtesqwspTCEDVHISYLPLAHMFerm 354
Cdd:PRK08043 356 RLAQVKQQPEDAALILFTSGSEGHPKGVVHSHksllANVeqiktIADF-------------TPNDRFMSALPLFHSF--- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 355 vqsvvychGGRIGffqgdirLLSDDMKALRPTIFP------VVPRLLnrmYDK----IFSQAdTSLKRWVlEFA-----A 419
Cdd:PRK08043 420 --------GLTVG-------LFTPLLTGAEVFLYPsplhyrIVPELV---YDRnctvLFGTS-TFLGNYA-RFAnpydfA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 420 RrkkaevrngiirndslwdklffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGD 499
Cdd:PRK08043 480 R--------------------------------LRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMA 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 500 WTSGHVGAPLP---CNLIKLKDAEElnyfaskgEGEICVKGPNVFKGYLKDEE---------RTSEALDQEGWLHTGDIG 567
Cdd:PRK08043 528 AKPGTVGRILPgmdARLLSVPGIEQ--------GGRLQLKGPNIMNGYLRVEKpgvlevptaENARGEMERGWYDTGDIV 599
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2024456367 568 KWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSDPVAQ 610
Cdd:PRK08043 600 RFDEQGFVQIQGRAKRFAKIA-GEMVSLEMVEQLALGVSPDKQ 641
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
293-601 |
4.77e-18 |
|
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: 86.16 E-value: 4.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 293 EDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKvteSQWSPTCEDVHISYLPLAHMFERMVQSVVYCHGGRIGFFqGD 372
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQK---EGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTG-GE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 373 IRLLSDDMKAL---RPTIFPVVPRLLNRMYDkifsqadtslkrwvlefaarrkkaEVRNGIIRNDSLwdklffnkiqasl 449
Cdd:cd17635 77 NTTYKSLFKILttnAVTTTCLVPTLLSKLVS------------------------ELKSANATVPSL------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 450 ggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNLIKLKDAEELNyFASK 528
Cdd:cd17635 120 ----RLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLPTDDDSIEiNAVGRPYPGVDVYLAATDGIA-GPSA 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024456367 529 GEGEICVKGPNVFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 601
Cdd:cd17635 195 SFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERI 265
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
146-631 |
5.04e-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: 5.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPcteqfiG--VFAQ--NRPEWIISELACYtySMVVVPLYdTLgPG----AIRYIVNT 217
Cdd:COG1021 51 LSYAELDRRADRLAAGLLALGLRP------GdrVVVQlpNVAEFVIVFFALF--RAGAIPVF-AL-PAhrraEISHFAEQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 218 ADISTVICdkPDKARtLLDHVE-----RRETPGLSSIILM-DPfekeltergrrcgvriQSMQEVEDCGRENRRAPVP-P 290
Cdd:COG1021 121 SEAVAYII--PDRHR-GFDYRAlarelQAEVPSLRHVLVVgDA----------------GEFTSLDALLAAPADLSEPrP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 291 RPEDlsiVCF---TSGTTGNPKGAMLTHgnvvAD--FSGFLKVTESQWSPtcEDVHISYLPLAHMFErM----VQSVVYc 361
Cdd:COG1021 182 DPDD---VAFfqlSGGTTGLPKLIPRTH----DDylYSVRASAEICGLDA--DTVYLAALPAAHNFP-LsspgVLGVLY- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 362 HGGRIgffqgdirLLSDDMKAL---------RPTIFPVVPRLLNRMydkifsqadtslkrwvLEFAARRKKAevrngiir 432
Cdd:COG1021 251 AGGTV--------VLAPDPSPDtafpliereRVTVTALVPPLALLW----------------LDAAERSRYD-------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 433 ndslwdkLffnkiqASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctaG-CTFTTPGD--WTSGH-VGAP 508
Cdd:COG1021 299 -------L------SSL----RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---GlVNYTRLDDpeEVILTtQGRP 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 509 L-PCNLIKLKDAEElNYFASKGEGEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKK-HIFK 586
Cdd:COG1021 359 IsPDDEVRIVDEDG-NPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKdQINR 437
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2024456367 587 laQGEYIAPEKIENIYIRsdpvaqvyvHGDSLQAFLVGivVPDAE 631
Cdd:COG1021 438 --GGEKIAAEEVENLLLA---------HPAVHDAAVVA--MPDEY 469
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
245-599 |
7.01e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 87.74 E-value: 7.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 245 GLSSIILMDPFE---KELTERGRRcgvriqsMQEVEDCGRENRRAPVPPRPEDLSIVCFTSGTTGNPKGAMLTHGNVVAD 321
Cdd:PRK07768 108 GAKAVVVGEPFLaaaPVLEEKGIR-------VLTVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYAN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 322 FSGFlkVTESQWSPTcEDVHISYLPLAH-MfermvqsvvychgGRIGFfqgdirlLSDDMKA------LRPTIFPVVPRL 394
Cdd:PRK07768 181 AEAM--FVAAEFDVE-TDVMVSWLPLFHdM-------------GMVGF-------LTVPMYFgaelvkVTPMDFLRDPLL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 395 LNRMYDKiFSQADTSLKRWVLEFAARRKKAevrngiirndslwdklffnkiQASLG----GCVRMIVTGAAPASPTVL-- 468
Cdd:PRK07768 238 WAELISK-YRGTMTAAPNFAYALLARRLRR---------------------QAKPGafdlSSLRFALNGAEPIDPADVed 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 469 --------GFLRAALGCqvyeGYGQTECTAGCTFTTPGD--------------------WTSGHV------GAPLPCNLI 514
Cdd:PRK07768 296 lldagarfGLRPEAILP----AYGMAEATLAVSFSPCGAglvvdevdadllaalrravpATKGNTrrlatlGPPLPGLEV 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 515 KLKDaEELNYFASKGEGEICVKGPNVFKGYLkDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIA 594
Cdd:PRK07768 372 RVVD-EDGQVLPPRGVGVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIY 448
|
....*
gi 2024456367 595 PEKIE 599
Cdd:PRK07768 449 PTDIE 453
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
144-636 |
8.53e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 87.40 E-value: 8.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 144 QWlSYKEVAERAEALGSGLLQQGCKPCTEqfIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTV 223
Cdd:PRK07470 32 SW-TWREIDARVDALAAALAARGVRKGDR--ILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 224 IC--DKPDKARTLldhveRRETPGLSSIILMDPFEKELtergrrcgvriqsmqEVEDCGRENRRAPVPPRPEDLSIVC-- 299
Cdd:PRK07470 109 IChaDFPEHAAAV-----RAASPDLTHVVAIGGARAGL---------------DYEALVARHLGARVANAAVDHDDPCwf 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 300 -FTSGTTGNPKGAMLTHG-------NVVADFsgFLKVTEsqwsptcEDVHISYLPLAH--------MFERMVQSVVychg 363
Cdd:PRK07470 169 fFTSGTTGRPKAAVLTHGqmafvitNHLADL--MPGTTE-------QDASLVVAPLSHgagihqlcQVARGAATVL---- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 364 grigffqgdirLLSDDMKAlrptifPVVPRLLNRMYDKIFSQADTSLKRWVLEFAARRKKaevrngiirNDSLwdklffn 443
Cdd:PRK07470 236 -----------LPSERFDP------AEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYD---------HSSL------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 444 kiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-----GDWTSGHVGaplPCNL----- 513
Cdd:PRK07470 283 ----------RYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVTGNITVLPPalhdaEDGPDARIG---TCGFertgm 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 514 -IKLKDAE--ELNYFASkgeGEICVKGPNVFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQG 590
Cdd:PRK07470 350 eVQIQDDEgrELPPGET---GEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMY-ISGG 424
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2024456367 591 EYIAPEKIENIYIRSDPVAQVYVHGdslqaflvgivVPDaeamPGW 636
Cdd:PRK07470 425 SNVYPREIEEKLLTHPAVSEVAVLG-----------VPD----PVW 455
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
146-640 |
1.61e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 86.63 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPCTEqfIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVIC 225
Cdd:PRK06178 59 ITYAELDELSDRFAALLRQRGVGAGDR--VAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 -DkpdkarTLLDHVE--RRETPgLSSII---LMD--------PFEKELTERGRRCGVRIQSMQEVEDCGRENRRAPvpPR 291
Cdd:PRK06178 137 lD------QLAPVVEqvRAETS-LRHVIvtsLADvlpaeptlPLPDSLRAPRLAAAGAIDLLPALRACTAPVPLPP--PA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 292 PEDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWSPtceDVHISYLPlahMFermvqsvvYCHGGRIGFfqg 371
Cdd:PRK06178 208 LDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGED---SVFLSFLP---EF--------WIAGENFGL--- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 372 dirllsddmkalrptIFPvvprllnrmydkIFSQADTSL-KRW----VLEFAARRKkaeVRNGIIRNDSL--------WD 438
Cdd:PRK06178 271 ---------------LFP------------LFSGATLVLlARWdavaFMAAVERYR---VTRTVMLVDNAvelmdhprFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 439 KLFFNKIQASlgGCVRMIvtgaAPASPTVLGFLRAALGCQVYEG-YGQTECTAGCTFTTpGDWTSGH--------VGAPL 509
Cdd:PRK06178 321 EYDLSSLRQV--RVVSFV----KKLNPDYRQRWRALTGSVLAEAaWGMTETHTCDTFTA-GFQDDDFdllsqpvfVGLPV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 510 PCNLIKLKDAEELNYFASKGEGEICVKGPNVFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQ 589
Cdd:PRK06178 394 PGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV-N 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024456367 590 GEYIAPEKIENIYIRSDPVAQVYVHG----DSLQ---AFLVgiVVP----DAEAMPGWAKKR 640
Cdd:PRK06178 472 GMSVFPSEVEALLGQHPAVLGSAVVGrpdpDKGQvpvAFVQ--LKPgadlTAAALQAWCREN 531
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
146-615 |
3.12e-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: 3.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADI-STVI 224
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRP--GQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMtAAVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 225 CDkpdkartlldhverrETPGLSSIIlmDPFEKELTErGRRCGVRiqsmqevEDCGRENRRAPVPPRPEDLSIVCFTSGT 304
Cdd:cd05923 107 AV---------------DAQVMDAIF--QSGVRVLAL-SDLVGLG-------EPESAGPLIEDPPREPEQPAFVFYTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 305 TGNPKGAMLTHgNVVADFSGFLkVTESQWSPTCEDVHISYLPLAHMfermvqsvvychggrIGFFQgdirLLSDDMkALR 384
Cdd:cd05923 162 TGLPKGAVIPQ-RAAESRVLFM-STQAGLRHGRHNVVLGLMPLYHV---------------IGFFA----VLVAAL-ALD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 385 PTIFPVvprllnrmydKIFSQADTSlkRWVlefaarrkKAEVRNGIIRNDSLWDKLFFNKIQASLG-GCVRMIVTGAAPA 463
Cdd:cd05923 220 GTYVVV----------EEFDPADAL--KLI--------EQERVTSLFATPTHLDALAAAAEFAGLKlSSLRHVTFAGATM 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 464 SPTVLGFLRAALGCQVYEGYGQTECTagcTFTTPGDWTSGHVGAPLPCNLIKL-KDAEELNYFASKG-EGEICVK--GPN 539
Cdd:cd05923 280 PDAVLERVNQHLPGEKVNIYGTTEAM---NSLYMRDARTGTEMRPGFFSEVRIvRIGGSPDEALANGeEGELIVAaaADA 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024456367 540 VFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVYVHG 615
Cdd:cd05923 357 AFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIG 430
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
144-613 |
3.51e-17 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 85.20 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 144 QWLSYKEVAERAEALGSGLLQQGCKPCTEqfIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTV 223
Cdd:PRK06155 45 TRWTYAEAARAAAAAAHALAAAGVKRGDR--VALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 224 ICDKPDKARtlLDHVERRETPgLSSIILMDPFEKELTERGRRCGVRIQSMQEVedcgrenrrAPVPPRPEDLSIVCFTSG 303
Cdd:PRK06155 123 VVEAALLAA--LEAADPGDLP-LPAVWLLDAPASVSVPAGWSTAPLPPLDAPA---------PAAAVQPGDTAAILYTSG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 304 TTGNPKGAMLTHG-------NVVADfsgfLKVTEsqwsptcEDVHISYLPLAH------MFERMVQSVVYCHGGRI---G 367
Cdd:PRK06155 191 TTGPSKGVCCPHAqfywwgrNSAED----LEIGA-------DDVLYTTLPLFHtnalnaFFQALLAGATYVLEPRFsasG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 368 FFqgdirllsDDMKALRPTIFpvvpRLLNRMYDKIFSQADTslkrwvlefaARRKKAEVRngiirndslwdklffnkiqA 447
Cdd:PRK06155 260 FW--------PAVRRHGATVT----YLLGAMVSILLSQPAR----------ESDRAHRVR-------------------V 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 448 SLGGCVrmivtgaapaSPTVLGFLRAALGCQVYEGYGQTECTAGCtFTTPGDWTSGHVGAPLPCNLIKLKDaEELNYFAS 527
Cdd:PRK06155 299 ALGPGV----------PAALHAAFRERFGVDLLDGYGSTETNFVI-AVTHGSQRPGSMGRLAPGFEARVVD-EHDQELPD 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 528 KGEGEICVKG--PNVF-KGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIyIR 604
Cdd:PRK06155 367 GEPGELLLRAdePFAFaTGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIKDAIR-RRGENISSFEVEQV-LL 443
|
490
....*....|
gi 2024456367 605 SDP-VAQVYV 613
Cdd:PRK06155 444 SHPaVAAAAV 453
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
146-623 |
3.90e-17 |
|
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: 85.11 E-value: 3.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVntADI-STVI 224
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVKR--EERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL--EDSrARVV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 225 CDKPDKARTLLDHVERREtPGLSSIILMDPFEKELTERGRRCGVRIQSMQEvedcgrenrrAPVPPRPEDLSIVCFTSGT 304
Cdd:cd05959 106 VVSGELAPVLAAALTKSE-HTLVVLIVSGGAGPEAGALLLAELVAAEAEQL----------KPAATHADDPAFWLYSSGS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 305 TGNPKGAMLTHGN--VVADFSG--FLKVTESqwsptceDVHISYLPLAHmfermvqsvVYCHGGRIGF---FQGDIRLLS 377
Cdd:cd05959 175 TGRPKGVVHLHADiyWTAELYArnVLGIRED-------DVCFSAAKLFF---------AYGLGNSLTFplsVGATTVLMP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 378 ---------DDMKALRPTIFPVVPRLLNRMydkifsqadtslkrwvlefaarrkkaevrngiIRNDSLWDKLFFNkiqas 448
Cdd:cd05959 239 erptpaavfKRIRRYRPTVFFGVPTLYAAM--------------------------------LAAPNLPSRDLSS----- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 449 lggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTF--TTPGDWTSGHVGAPLPCNLIKLKDaEELNYFA 526
Cdd:cd05959 282 ----LRLCVSAGEALPAEVGERWKARFGLDILDGIGSTE--MLHIFlsNRPGRVRYGTTGKPVPGYEVELRD-EDGGDVA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 527 SKGEGEICVKGPNVFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYIRSD 606
Cdd:cd05959 355 DGEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSPFEVESALVQHP 432
|
490 500
....*....|....*....|....
gi 2024456367 607 PVAQVYVHG-------DSLQAFLV 623
Cdd:cd05959 433 AVLEAAVVGvededglTKPKAFVV 456
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
144-630 |
1.26e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 84.83 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 144 QWLSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTV 223
Cdd:PRK12467 536 QVLSYAELNRQANRLAHVLIAAGVGP--DVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLL 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 224 ICDKPDKARTLLdhverreTPGLSSIILMDPfekeltergrrcgvriqsmqEVEDCGRENRRAPVPPRPEDLSIVCFTSG 303
Cdd:PRK12467 614 LTQSHLLAQLPV-------PAGLRSLCLDEP--------------------ADLLCGYSGHNPEVALDPDNLAYVIYTSG 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 304 TTGNPKGAMLTHGNVvadfSGFLKVTESQWSPTCEDVHISYLPLAHMFERMVQSVVYCHGGRIgffqgdirLLSDDMKAL 383
Cdd:PRK12467 667 STGQPKGVAISHGAL----ANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATL--------HLLPPDCAR 734
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 384 RPTIFpvvprllnrmYDKIFSQADTSLKrwvlefaarrkkaevrngiiRNDSLWDKLFFNKIQASLGGCVRMIVTGAAPA 463
Cdd:PRK12467 735 DAEAF----------AALMADQGVTVLK--------------------IVPSHLQALLQASRVALPRPQRALVCGGEALQ 784
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 464 SPTVLGFLRAALGCQVYEGYGQTECTAGCTFTT----PGDWTSGHVGAPLPCNLIKLKDAeELNYFASKGEGEICVKGPN 539
Cdd:PRK12467 785 VDLLARVRALGPGARLINHYGPTETTVGVSTYElsdeERDFGNVPIGQPLANLGLYILDH-YLNPVPVGVVGELYIGGAG 863
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 540 VFKGYLKDEERTSE-------ALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDPVAQVY 612
Cdd:PRK12467 864 LARGYHRRPALTAErfvpdpfGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKI-RGFRIELGEIEARLLAQPGVREAV 942
|
490 500
....*....|....*....|....
gi 2024456367 613 V------HGDSLQAFLVGIVVPDA 630
Cdd:PRK12467 943 VlaqpgdAGLQLVAYLVPAAVADG 966
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
132-696 |
2.02e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 83.17 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 132 PCLGYRKPKQ-PYQWLSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVP--------- 201
Cdd:PRK12582 66 PWLAQREPGHgQWRKVTYGEAKRAVDALAQALLDLGLDP--GRPVMILSGNSIEHALMTLAAMQAGVPAAPvspayslms 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 202 --------LYDTLGPGAI-----------RYIVNTADISTVICDKPdkartlldhverreTPGLSSIILMDPFEKELTEr 262
Cdd:PRK12582 144 hdhaklkhLFDLVKPRVVfaqsgapfaraLAALDLLDVTVVHVTGP--------------GEGIASIAFADLAATPPTA- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 263 grrcGVRiQSMQEVEdcgrenrrapvpprPEDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESqwSPTCE-DVH 341
Cdd:PRK12582 209 ----AVA-AAIAAIT--------------PDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPR--EPDPPpPVS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 342 ISYLPLAHMFermvqsvvychGGRIGFfQGDIR----LLSDD-----------MKALR---PTIFPVVPRLLNRMYDKIf 403
Cdd:PRK12582 268 LDWMPWNHTM-----------GGNANF-NGLLWgggtLYIDDgkplpgmfeetIRNLReisPTVYGNVPAGYAMLAEAM- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 404 sQADTSLKRWVLefaaRRKKAEVRNGIIRNDSLWDKlffnkIQAslggcvrmiVTGAAPASPTVLgflraalgcqvYEGY 483
Cdd:PRK12582 335 -EKDDALRRSFF----KNLRLMAYGGATLSDDLYER-----MQA---------LAVRTTGHRIPF-----------YTGY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 484 GQTEcTAGCTFTTpgDWTS---GHVGAPLPCnlIKLKdaeelnyFASKGEG-EICVKGPNVFKGYLKDEERTSEALDQEG 559
Cdd:PRK12582 385 GATE-TAPTTTGT--HWDTervGLIGLPLPG--VELK-------LAPVGDKyEVRVKGPNVTPGYHKDPELTAAAFDEEG 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 560 WLHTGDIGKWL----PNGTLKIIDRKKHIFKLAQGEYIAPEKieniyIRSDPVAQV--YVHgDSL-----QAFLVGIVVP 628
Cdd:PRK12582 453 FYRLGDAARFVdpddPEKGLIFDGRVAEDFKLSTGTWVSVGT-----LRPDAVAACspVIH-DAVvagqdRAFIGLLAWP 526
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024456367 629 DAEAMPGWAKKRgfDGTYEELCRNKELQKAIMEDMVRLGKESGLHSfEQVKAIHIHSDMFSVQNGLLT 696
Cdd:PRK12582 527 NPAACRQLAGDP--DAAPEDVVKHPAVLAILREGLSAHNAEAGGSS-SRIARALLMTEPPSIDAGEIT 591
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
146-634 |
2.76e-16 |
|
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: 82.32 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVIC 225
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVRP--GDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 DKPDKArtLLDHVERRETPGLSSIILMDPFekeltergrrcgvriqsmqevedcgrenrrAPVPPRPEDLSIVCFTSGTT 305
Cdd:cd12114 91 DGPDAQ--LDVAVFDVLILDLDALAAPAPP------------------------------PPVDVAPDDLAYVIFTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 306 GNPKGAMLTHG---NVVADfsgflkvTESQWSPTCEDVHISYLPLAHMFermvqSV-----VYCHGGRIGFFQGDIRLLS 377
Cdd:cd12114 139 GTPKGVMISHRaalNTILD-------INRRFAVGPDDRVLALSSLSFDL-----SVydifgALSAGATLVLPDEARRRDP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 378 DDMKAL----RPTIFPVVPRLLNRMYDkifsqadtslkrwVLEfAARRKKAEVRNGIIRNDslWdklffnkIQASLGGCV 453
Cdd:cd12114 207 AHWAELierhGVTLWNSVPALLEMLLD-------------VLE-AAQALLPSLRLVLLSGD--W-------IPLDLPARL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 454 RMIVTGAAPASptvlgflraaLGcqvyegyGQTECTAGCTF----TTPGDWTSGHVGAPLPCNLIKLKDaEELNYFASKG 529
Cdd:cd12114 264 RALAPDARLIS----------LG-------GATEASIWSIYhpidEVPPDWRSIPYGRPLANQRYRVLD-PRGRDCPDWV 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 530 EGEICVKGPNVFKGYLKDEERTSEAL----DQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRS 605
Cdd:cd12114 326 PGELWIGGRGVALGYLGDPELTAARFvthpDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKV-RGYRIELGEIEAALQAH 404
|
490 500 510
....*....|....*....|....*....|.
gi 2024456367 606 DPVAQ--VYVHGDSLQAFLVGIVVPDAEAMP 634
Cdd:cd12114 405 PGVARavVVVLGDPGGKRLAAFVVPDNDGTP 435
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
446-628 |
4.56e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 81.99 E-value: 4.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 446 QASLGGCVRMIVTGAAPasPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGD-WTSghvgapLPCNL----------- 513
Cdd:PLN03102 296 LSPRSGPVHVLTGGSPP--PAALVKKVQRLGFQVMHAYGLTEATGPVLFCEWQDeWNR------LPENQqmelkarqgvs 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 514 ------IKLKDAEELNYFASKGE--GEICVKGPNVFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLKIIDRKKHIF 585
Cdd:PLN03102 368 ilgladVDVKNKETQESVPRDGKtmGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII 446
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2024456367 586 kLAQGEYIAPEKIENIyirsdpvaqVYVHGDSLQAFLVGIVVP 628
Cdd:PLN03102 447 -ISGGENISSVEVENV---------LYKYPKVLETAVVAMPHP 479
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
292-608 |
6.70e-16 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 81.00 E-value: 6.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 292 PEDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESqwspTCEDVHISYLPLAHmfermvqsvvychggRIGFFQG 371
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEW----KTKDRILSWMPLTH---------------DMGLIAF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 372 DIRLLSDDMKA-LRPT-IFPVVPRLLNRMYDKiFSQADTSLKRWVLEFAARRKKAEVRNGiirndslWDKlffnkiqasl 449
Cdd:cd05908 166 HLAPLIAGMNQyLMPTrLFIRRPILWLKKASE-HKATIVSSPNFGYKYFLKTLKPEKAND-------WDL---------- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 450 gGCVRMIVTGAAPASP----------TVLGFLRAAlgcqVYEGYGQTECTAGCTF------TTPGDWTSGHVGAPLPCNL 513
Cdd:cd05908 228 -SSIRMILNGAEPIDYelchefldhmSKYGLKRNA----ILPVYGLAEASVGASLpkaqspFKTITLGRRHVTHGEPEPE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 514 IKLKDAE-----ELNYFASKGEGEIC----------------VKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGkWLPN 572
Cdd:cd05908 303 VDKKDSEcltfvEVGKPIDETDIRICdednkilpdgyighiqIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIRN 381
|
330 340 350
....*....|....*....|....*....|....*.
gi 2024456367 573 GTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPV 608
Cdd:cd05908 382 GRLVITGREKDII-FVNGQNVYPHDIERIAEELEGV 416
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
146-631 |
9.70e-16 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 80.30 E-value: 9.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVIC 225
Cdd:PRK09029 29 LTWQQLCARIDQLAAGFAQQGVVE--GSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEELLPSLTLDFALV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 DKPDKARTLLDHVERRETPGlssiilmdpfekeltergrrcgvriqsmqevedcgrenrRAPVPPRPEDLSIVCFTSGTT 305
Cdd:PRK09029 107 LEGENTFSALTSLHLQLVEG---------------------------------------AHAVAWQPQRLATMTLTSGST 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 306 GNPKGAMLTHGNVVADFSGFLKVTESqwspTCEDVHISYLPLAHmfermV--QSVVY---CHGGRIGFfqGDIRLLSDDM 380
Cdd:PRK09029 148 GLPKAAVHTAQAHLASAEGVLSLMPF----TAQDSWLLSLPLFH-----VsgQGIVWrwlYAGATLVV--RDKQPLEQAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 381 K-----ALRPTifpVVPRLLNRmydkifSQADTSLKRwVLefaarrkkaevrngiirndslwdklffnkiqasLGGCvrM 455
Cdd:PRK09029 217 AgcthaSLVPT---QLWRLLDN------RSEPLSLKA-VL---------------------------------LGGA--A 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 456 IvtgaapasPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTSGhVGAPLPCNLIKLKDaeelnyfaskgeGEICV 535
Cdd:PRK09029 252 I--------PVELTEQAEQQGIRCWCGYGLTE-MASTVCAKRADGLAG-VGSPLPGREVKLVD------------GEIWL 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 536 KGPNVFKGYLKDEERTSeALDQEGWLHTGDIGKWLpNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVYVhg 615
Cdd:PRK09029 310 RGASLALGYWRQGQLVP-LVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQVFV-- 384
|
490
....*....|....*.
gi 2024456367 616 dslqaflvgIVVPDAE 631
Cdd:PRK09029 385 ---------VPVADAE 391
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
146-634 |
1.55e-15 |
|
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: 80.08 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLyDTLGPGA-IRYIVNTADISTVI 224
Cdd:cd17651 21 LTYAELDRRANRLAHRLRARGVGP--GDLVALCARRSAELVVALLAILKAGAAYVPL-DPAYPAErLAFMLADAGPVLVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 225 CDKPDKARTLldhverretpglssiilmdpfekelterGRRCGVRIQSMQEVEDCGRENRRAPvpPRPEDLSIVCFTSGT 304
Cdd:cd17651 98 THPALAGELA----------------------------VELVAVTLLDQPGAAAGADAEPDPA--LDADDLAYVIYTSGS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 305 TGNPKGAMLTHGNVV-------ADFSGFLKVTESQWSPTCEDVhisylplahmferMVQSV--VYCHGGRIGFFQGDIRL 375
Cdd:cd17651 148 TGRPKGVVMPHRSLAnlvawqaRASSLGPGARTLQFAGLGFDV-------------SVQEIfsTLCAGATLVLPPEEVRT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 376 LSDDMKALrptifpvvprLLNRMYDKIFsqADTSLKRWVLEFAARrkkaevrngiirndslwdklffnkiQASLGGCVRM 455
Cdd:cd17651 215 DPPALAAW----------LDEQRISRVF--LPTVALRALAEHGRP-------------------------LGVRLAALRY 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 456 IVTG--AAPASPTVLGFLRAALGCQVYEGYGQTE---CTAGCTFTTPGDWTS-GHVGAPLPCNLIKLKDaEELNYFASKG 529
Cdd:cd17651 258 LLTGgeQLVLTEDLREFCAGLPGLRLHNHYGPTEthvVTALSLPGDPAAWPApPPIGRPIDNTRVYVLD-AALRPVPPGV 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 530 EGEICVKGPNVFKGYLKDEERTSEALDQEGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYI 603
Cdd:cd17651 337 PGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGFRIELGEIEAALA 415
|
490 500 510
....*....|....*....|....*....|....
gi 2024456367 604 RSDPVAQ--VYVHGD-SLQAFLVGIVVPDAEAMP 634
Cdd:cd17651 416 RHPGVREavVLAREDrPGEKRLVAYVVGDPEAPV 449
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
144-632 |
2.04e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 76.64 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 144 QWLSYKEVAERAEALGSGLLQQgCKPCTEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTV 223
Cdd:PRK07867 27 SFTSWREHIRGSAARAAALRAR-LDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 224 ICDkpDKARTLLDHVErretPGLSSIILMDPFEKELTErgrrcgvriqsmqevedcgrENRRAPVPPR---PEDLSIVCF 300
Cdd:PRK07867 106 LTE--SAHAELLDGLD----PGVRVINVDSPAWADELA--------------------AHRDAEPPFRvadPDDLFMLIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 301 TSGTTGNPKGAMLTHGNVVadFSGFLKVTESQWSPtcEDVHISYLPLAHMFERMVQ-SVVYCHGGRI---------GFFq 370
Cdd:PRK07867 160 TSGTSGDPKAVRCTHRKVA--SAGVMLAQRFGLGP--DDVCYVSMPLFHSNAVMAGwAVALAAGASIalrrkfsasGFL- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 371 gdirllsDDMKALRPTIFPVVPRLLNrmYdkIFS------QADTSLKrwvlefaarrkkaevrngiirndslwdklffnk 444
Cdd:PRK07867 235 -------PDVRRYGATYANYVGKPLS--Y--VLAtperpdDADNPLR--------------------------------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 445 iqaslggcvrmIVTGAAPASPTVLGFlRAALGCQVYEGYGQTEctAGCTFTTPGDWTSGHVGaPLPCNlIKLKDAEELN- 523
Cdd:PRK07867 271 -----------IVYGNEGAPGDIARF-ARRFGCVVVDGFGSTE--GGVAITRTPDTPPGALG-PLPPG-VAIVDPDTGTe 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 524 ----YFASKGE-------GEIC-VKGPNVFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGE 591
Cdd:PRK07867 335 cppaEDADGRLlnadeaiGELVnTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGE 412
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2024456367 592 YIAPEKIENIYIRSDPVAQVYVHGdslqaflvgivVPDAEA 632
Cdd:PRK07867 413 NLGTAPIERILLRYPDATEVAVYA-----------VPDPVV 442
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
146-615 |
5.77e-14 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 75.20 E-value: 5.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLlQQGCKPCTEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVIC 225
Cdd:PRK05620 39 TTFAAIGARAAALAHAL-HDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 DKPDKAR--TLLdhverRETPGLSSIILMDPFEKELTERGRRCGVRIQSMQEVEDcGRENRrAPVPPRPEDLSI-VCFTS 302
Cdd:PRK05620 118 DPRLAEQlgEIL-----KECPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALLD-GRSTV-YDWPELDETTAAaICYST 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 303 GTTGNPKGAMLTHGNVVADfSGFLKVTESqWSPTCEDVHISYLPLAHMFERMVQSVVYCHGGrigffqgdirllsddmka 382
Cdd:PRK05620 191 GTTGAPKGVVYSHRSLYLQ-SLSLRTTDS-LAVTHGESFLCCVPIYHVLSWGVPLAAFMSGT------------------ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 383 lrPTIFP----VVPRLLnrmydKIFSqadTSLKRwvlefaarrkkaeVRNGIirnDSLWDKLFFNKIQ-----ASLggcv 453
Cdd:PRK05620 251 --PLVFPgpdlSAPTLA-----KIIA---TAMPR-------------VAHGV---PTLWIQLMVHYLKnpperMSL---- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 454 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGA---------PLPCNLIKLKDAEELNY 524
Cdd:PRK05620 301 QEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEARWayrvsqgrfPASLEYRIVNDGQVMES 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 525 fASKGEGEICVKGPNVFKGYLKD-------------EERTSEALDQ---EGWLHTGDIGKWLPNGTLKIIDRKKHIFKlA 588
Cdd:PRK05620 381 -TDRNEGEIQVRGNWVTASYYHSpteegggaastfrGEDVEDANDRftaDGWLRTGDVGSVTRDGFLTIHDRARDVIR-S 458
|
490 500
....*....|....*....|....*..
gi 2024456367 589 QGEYIAPEKIENIYIRSDPVAQVYVHG 615
Cdd:PRK05620 459 GGEWIYSAQLENYIMAAPEVVECAVIG 485
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
292-603 |
1.03e-13 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 74.47 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 292 PEDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWSPTCEDVHISYLPLAHMFermvqsvvychggriGFfqG 371
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKF----FSPKEDDVMMSFLPPFHAY---------------GF--N 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 372 DIRLLSddMKALRPTIF---PVVPRLLNRMYDK---IFSQADTSLKRWVLEFAARRKKA--EVRNGIIRNDSLWDKLFfn 443
Cdd:PRK06334 241 SCTLFP--LLSGVPVVFaynPLYPKKIVEMIDEakvTFLGSTPVFFDYILKTAKKQESClpSLRFVVIGGDAFKDSLY-- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 444 kiqaslggcvrmivTGAAPASPTVlgflraalgcQVYEGYGQTECTAGCTFTT---PGDwtSGHVGAPLPcNLIKLKDAE 520
Cdd:PRK06334 317 --------------QEALKTFPHI----------QLRQGYGTTECSPVITINTvnsPKH--ESCVGMPIR-GMDVLIVSE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 521 ELNYFASKGE-GEICVKGPNVFKGYL-KDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKI 598
Cdd:PRK06334 370 ETKVPVSSGEtGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSLEAL 448
|
....*
gi 2024456367 599 ENIYI 603
Cdd:PRK06334 449 ESILM 453
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
290-641 |
2.47e-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: 72.88 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 290 PRPEDLSIVCFTSGTTGNPKGAMLTHGNvvadFSGFLKVTESQWSPTCEDVHISYLPLAHMFERM--VQSVVychggrig 367
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGT----FAAQIDALRQLYGIRPGEVDLATFPLFALFGPAlgLTSVI-------- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 368 ffqgdirllsDDMKALRPTifPVVPRllnrmydKIFSqadtslkrwvlefAARRKKAevrNGIIRNDSLWDKL--FFNKI 445
Cdd:cd05910 150 ----------PDMDPTRPA--RADPQ-------KLVG-------------AIRQYGV---SIVFGSPALLERVarYCAQH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 446 QASLGGcVRMIVTGAAPASPTVLGFLRAAL--GCQVYEGYGQTECTAGCT------FTTPGDWTSGH----VGAPLPCNL 513
Cdd:cd05910 195 GITLPS-LRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrelLATTTAATSGGagtcVGRPIPGVR 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 514 IKL-----------KDAEELNyfasKGE-GEICVKGPNVFKGYLKDEERTSEA----LDQEGWLHTGDIGKWLPNGTLKI 577
Cdd:cd05910 274 VRIieiddepiaewDDTLELP----RGEiGEITVTGPTVTPTYVNRPVATALAkiddNSEGFWHRMGDLGYLDDEGRLWF 349
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024456367 578 IDRKKHIFKLAQGEYIapekieniyirSDPVAQVY-VHGDSLQAFLVGIVVPDA-------EAMPGWAKKRG 641
Cdd:cd05910 350 CGRKAHRVITTGGTLY-----------TEPVERVFnTHPGVRRSALVGVGKPGCqlpvlcvEPLPGTITPRA 410
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
146-634 |
2.87e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 72.85 E-value: 2.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCkpCTEQFIGVFAQNRPEWIISELACYTYSMVVVPLyDTlgpgaiRYivNTADISTVIc 225
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGV--RRGDRVAVWLPNCIEWVVLFLACARLGATVIAV-NT------RY--RSHEVAHIL- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 dKPDKARTL--------------LDHVERRETPGLSSIILMDPFEKELTERGRrcGVRIQSmqevedCGRENRRAP---- 287
Cdd:PRK06164 104 -GRGRARWLvvwpgfkgidfaaiLAAVPPDALPPLRAIAVVDDAADATPAPAP--GARVQL------FALPDPAPPaaag 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 288 VPPRPEDLSIVCFT-SGTTGNPK------GAMLTHGNVVADFSGFlkvtesqwSPtcEDVHISYLPLahmfermvqSVVY 360
Cdd:PRK06164 175 ERAADPDAGALLFTtSGTTSGPKlvlhrqATLLRHARAIARAYGY--------DP--GAVLLAALPF---------CGVF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 361 CHGGRIGFFQGDIRLLSDDmkalrptIF--PVVPRLL-----------NRMYDKIFSQADTSLkrwvlEFAARRkkaevR 427
Cdd:PRK06164 236 GFSTLLGALAGGAPLVCEP-------VFdaARTARALrrhrvthtfgnDEMLRRILDTAGERA-----DFPSAR-----L 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 428 NGIirndslwdklffnkiqASLggcvrmivtgaAPASPTVLGFLRAAlGCQVYEGYGQTECTA---GCTFTTPgdWTSGH 504
Cdd:PRK06164 299 FGF----------------ASF-----------APALGELAALARAR-GVPLTGLYGSSEVQAlvaLQPATDP--VSVRI 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 505 VGAPLPCN---LIKLKDAEELNYFASKGEGEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRK 581
Cdd:PRK06164 349 EGGGRPASpeaRVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRM 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2024456367 582 KHIFKLAqGEYIAPEKIENIYIRSDPVAQVYVHGDSL--QAFLVGIVVPDAEAMP 634
Cdd:PRK06164 429 GDSLRLG-GFLVNPAEIEHALEALPGVAAAQVVGATRdgKTVPVAFVIPTDGASP 482
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
482-637 |
2.93e-13 |
|
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: 71.56 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 482 GYGQTECTAGCTFTTPGDWTSGHVGAPLPCNLIKLKDAE--ELnyfaSKGE-GEICVKGPNVFKGYLKDEERTSEALdQE 558
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDgrEV----PDGEvGEIVARGPTVMAGYWNRPEVNARRT-RG 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 559 GWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIyIRSDP-VAQVYVhgdslqaflvgIVVPDaeamPGWA 637
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSG-AENIYPAEVERC-LRQHPaVADAAV-----------IGVPD----PRWA 279
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
144-624 |
3.06e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 73.84 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 144 QWLSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLyDTLGPGA-IRYIVNTADIST 222
Cdd:PRK12316 2027 QHLSYAELDSRANRLAHRLRARGVGP--EVRVAIAAERSFELVVALLAVLKAGGAYVPL-DPNYPAErLAYMLEDSGAAL 2103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 223 VICDKPDKARTLLdhverreTPGLSSIILMDPFEkeltergrrcgvriqsMQEVEDCGRENRRAPvpprpEDLSIVCFTS 302
Cdd:PRK12316 2104 LLTQRHLLERLPL-------PAGVARLPLDRDAE----------------WADYPDTAPAVQLAG-----ENLAYVIYTS 2155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 303 GTTGNPKGAMLTHGNVVAdfsgFLKVTESQWSPTCEDVHISYLPLAhmFERMVQSVVY--CHGGRIgffqgdirLLSDDM 380
Cdd:PRK12316 2156 GSTGLPKGVAVSHGALVA----HCQAAGERYELSPADCELQFMSFS--FDGAHEQWFHplLNGARV--------LIRDDE 2221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 381 KalrptifpvvpRLLNRMYDKIFSQADTslkrwVLEFAArrkkaevrngiirndSLWDKLffnKIQASLGGC---VRMIV 457
Cdd:PRK12316 2222 L-----------WDPEQLYDEMERHGVT-----ILDFPP---------------VYLQQL---AEHAERDGRppaVRVYC 2267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 458 TGAAPASPTVLGFLRAALGCQ-VYEGYGQTEctagcTFTTPGDWTSGHV------GAPLPCNLIKLK----DAeELNYFA 526
Cdd:PRK12316 2268 FGGEAVPAASLRLAWEALRPVyLFNGYGPTE-----AVVTPLLWKCRPQdpcgaaYVPIGRALGNRRayilDA-DLNLLA 2341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 527 SKGEGEICVKGPNVFKGYLKDEERTSEALDQEGWLH-------TGDIGKWLPNGTLKIIDRKKHI-----FKLAQGEyIA 594
Cdd:PRK12316 2342 PGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQvkirgFRIELGE-IE 2420
|
490 500 510
....*....|....*....|....*....|.
gi 2024456367 595 PEKIENIYIRSDPV-AQVYVHGDSLQAFLVG 624
Cdd:PRK12316 2421 ARLQAHPAVREAVVvAQDGASGKQLVAYVVP 2451
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
445-613 |
4.45e-13 |
|
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: 71.83 E-value: 4.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 445 IQASLGGC---VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTfTTPGD-WTSGHVGAPLPCNLIKLKDAE 520
Cdd:cd05974 191 IQQDLASFdvkLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVG-NSPGQpVKAGSMGRPLPGYRVALLDPD 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 521 ElnyfASKGEGEICV-----KGPNVFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAP 595
Cdd:cd05974 270 G----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SSDYRISP 343
|
170
....*....|....*...
gi 2024456367 596 EKIENIYIRSDPVAQVYV 613
Cdd:cd05974 344 FELESVLIEHPAVAEAAV 361
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
144-642 |
4.84e-13 |
|
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: 72.08 E-value: 4.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 144 QWLSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTV 223
Cdd:cd17644 24 QQLTYEELNTKANQLAHYLQSLGVKS--ESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYILEDAQISVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 224 ICdkpdkartlldhverretpglssiilmdpfekeltergrrcgvriqsmqevedcgrenrrapvppRPEDLSIVCFTSG 303
Cdd:cd17644 102 LT-----------------------------------------------------------------QPENLAYVIYTSG 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 304 TTGNPKGAMLTHGNVVADFSGFLKV---TES----QWSPTCEDVHISYLplahmfermvqSVVYCHGGRIgffqgdirll 376
Cdd:cd17644 117 STGKPKGVMIEHQSLVNLSHGLIKEygiTSSdrvlQFASIAFDVAAEEI-----------YVTLLSGATL---------- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 377 sddmkALRPT-IFPVVPRLLNRMYDK---IFSQADTSLKRWVLEFAarrkkaevrngiirndslwdklffnKIQASLGGC 452
Cdd:cd17644 176 -----VLRPEeMRSSLEDFVQYIQQWqltVLSLPPAYWHLLVLELL-------------------------LSTIDLPSS 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 453 VRMIVTGAAPASPTVLGFLRAALG--CQVYEGYGQTECTAGCTFTTPGDWTSGH-----VGAPLPCNLIKLKDaEELNYF 525
Cdd:cd17644 226 LRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIANTQVYILD-ENLQPV 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 526 ASKGEGEICVKGPNVFKGYLKDEERTSEALDQEGWLH--------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 597
Cdd:cd17644 305 PVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKI-RGFRIELGE 383
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2024456367 598 IENIYIRSDPVAQ--VYVHGDSL-QAFLVGIVVPDAEAMPGWAKKRGF 642
Cdd:cd17644 384 IEAVLSQHNDVKTavVIVREDQPgNKRLVAYIVPHYEESPSTVELRQF 431
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
146-623 |
5.77e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 71.88 E-value: 5.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVIC 225
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRA--GDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 DkpDKARTLLDHVERrETPGLSSIIlmdpfekELTERGRRCGVRIQSMQEVEDcGRENRRAPVPPRPEdlSIVCFTSGTT 305
Cdd:PRK07788 153 D--DEFTDLLSALPP-DLGRLRAWG-------GNPDDDEPSGSTDETLDDLIA-GSSTAPLPKPPKPG--GIVILTSGTT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 306 GNPKGAMLTHGNVVADFSGFLkvtesqwsptcedvhiSYLPLaHMFERMVQSVVYCHG-----GRIGFFQG--------- 371
Cdd:PRK07788 220 GTPKGAPRPEPSPLAPLAGLL----------------SRVPF-RAGETTLLPAPMFHAtgwahLTLAMALGstvvlrrrf 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 372 DIRLLSDDMKALRPTIFPVVPRLLNRMYD---KIFSQADTSlkrwvlefaarrkkaevrngiirndSLwdklffnkiqas 448
Cdd:PRK07788 283 DPEATLEDIAKHKATALVVVPVMLSRILDlgpEVLAKYDTS-------------------------SL------------ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 449 lggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECtAGCTFTTPGDWT--SGHVGAPLPCNLIKLKDAE--ELny 524
Cdd:PRK07788 326 -----KIIFVSGSALSPELATRALEAFGPVLYNLYGSTEV-AFATIATPEDLAeaPGTVGRPPKGVTVKILDENgnEV-- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 525 faSKGE-GEICVKGPNVFKGYLKDeeRTSEALDqeGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYI 603
Cdd:PRK07788 398 --PRGVvGRIFVGNGFPFEGYTDG--RDKQIID--GLLSSGDVGYFDEDGLLFVDGRDDDMI-VSGGENVFPAEVEDLLA 470
|
490 500
....*....|....*....|....*..
gi 2024456367 604 RSDPVAQVYVHG--DS-----LQAFLV 623
Cdd:PRK07788 471 GHPDVVEAAVIGvdDEefgqrLRAFVV 497
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
146-615 |
6.89e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 71.84 E-value: 6.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVIC 225
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGP--GDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 DkpdkaRTLLDHVE--RRETPGLSSIILMDpfeKELTERGRRCGVRIQSMQEVEDCGREnrraPVPPRPEDLSIVCfTSG 303
Cdd:PRK07798 107 E-----REFAPRVAevLPRLPKLRTLVVVE---DGSGNDLLPGAVDYEDALAAGSPERD----FGERSPDDLYLLY-TGG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 304 TTGNPKGAMLTHGNV-VADFSGFLKVTesqwSPTCEDVH-----------ISYLPLAHMFERMVQSVVYchggrIGFFQG 371
Cdd:PRK07798 174 TTGMPKGVMWRQEDIfRVLLGGRDFAT----GEPIEDEEelakraaagpgMRRFPAPPLMHGAGQWAAF-----AALFSG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 372 DIRLLSDDMKalrptifpvvprllnrmydkiFSQADtslkrwVLEFAARRK--------KAEVRNGI--IRNDSLWDklf 441
Cdd:PRK07798 245 QTVVLLPDVR---------------------FDADE------VWRTIEREKvnvitivgDAMARPLLdaLEARGPYD--- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 442 fnkiqaslGGCVRMIVTGAAPASPTV-LGFLRAALGCQVYEGYGQTECTAGCTFTTPGDwtSGHVGAPL-----PCNLIk 515
Cdd:PRK07798 295 --------LSSLFAIASGGALFSPSVkEALLELLPNVVLTDSIGSSETGFGGSGTVAKG--AVHTGGPRftigpRTVVL- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 516 lkdAEELNyFASKGEGEICV--KGPNVFKGYLKDEERTSEAL---DQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqG 590
Cdd:PRK07798 364 ---DEDGN-PVEPGSGEIGWiaRRGHIPLGYYKDPEKTAETFptiDGVRYAIPGDRARVEADGTITLLGRGSVCINTG-G 438
|
490 500
....*....|....*....|....*.
gi 2024456367 591 EYIAPEKIENIyIRSDP-VAQVYVHG 615
Cdd:PRK07798 439 EKVFPEEVEEA-LKAHPdVADALVVG 463
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
111-664 |
7.83e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 72.50 E-value: 7.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 111 YDDARTMYEVFRRGFSISENGPCLGYRKpkqpyQWLSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISEL 190
Cdd:PRK12467 1570 YPLARLVHQLIEDQAAATPEAVALVFGE-----QELTYGELNRRANRLAHRLIALGVGP--EVLVGIAVERSLEMVVGLL 1642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 191 ACYTYSMVVVPLYDTLGPGAIRYIVNTADIstvicdkpdkaRTLLDH---VERRETP-GLSSIILmDPFEKELTergrrc 266
Cdd:PRK12467 1643 AILKAGGAYVPLDPEYPRERLAYMIEDSGI-----------ELLLTQshlQARLPLPdGLRSLVL-DQEDDWLE------ 1704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 267 gvriqsmqevedcGRENRRAPVPPRPEDLSIVCFTSGTTGNPKGAMLTHGNVVADFsgflKVTESQWSPTCEDVHISYLP 346
Cdd:PRK12467 1705 -------------GYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRL----CATQEAYQLSAADVVLQFTS 1767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 347 LAhmFERMVQSVVY--CHGGRIgffqgdirllsddmkALRPtifPVVPRLLNRMYDKIFSQADTslkrwVLEFAARRKKA 424
Cdd:PRK12467 1768 FA--FDVSVWELFWplINGARL---------------VIAP---PGAHRDPEQLIQLIERQQVT-----TLHFVPSMLQQ 1822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 425 evrngiirndslwdklfFNKIQASLGGC--VRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAG-----CTFTT 496
Cdd:PRK12467 1823 -----------------LLQMDEQVEHPlsLRRVVCGGEALEVEALRPWLERLPdTGLFNLYGPTETAVDvthwtCRRKD 1885
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 497 PGDWTSGHVGAPLPcNLIKLKDAEELNYFASKGEGEICVKGPNVFKGYLKDEERTSEAL------DQEGWLH-TGDIGKW 569
Cdd:PRK12467 1886 LEGRDSVPIGQPIA-NLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgTVGSRLYrTGDLARY 1964
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 570 LPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDPVAQ--VYVHGDSLQAFLVGIVVPDAEAMPGWAKKRgfdGTYE 647
Cdd:PRK12467 1965 RADGVIEYLGRIDHQVKI-RGFRIELGEIEARLREQGGVREavVIAQDGANGKQLVAYVVPTDPGLVDDDEAQ---VALR 2040
|
570
....*....|....*..
gi 2024456367 648 ELCRNkELQKAIMEDMV 664
Cdd:PRK12467 2041 AILKN-HLKASLPEYMV 2056
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
146-623 |
1.25e-12 |
|
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: 70.61 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPCTEQFigVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADistvic 225
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVF--VLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSE------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 dkpdkARTLLDHverretpglssiilmdpfeKELTERgrrcgvriqsmqevedcgrenrrapvpPRPEDLSIVCFTSGTT 305
Cdd:cd05969 73 -----AKVLITT-------------------EELYER---------------------------TDPEDPTLLHYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 306 GNPKGAMLTHGNVVADfsgflkvtesqwsptcedvhisYLPLAHMFErMVQSVVYCHGGRIGFFQGdirllsddmkalrp 385
Cdd:cd05969 102 GTPKGVLHVHDAMIFY----------------------YFTGKYVLD-LHPDDIYWCTADPGWVTG-------------- 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 386 TIFPVVPRLLNRMYDKIFsQADTSLKRW--VLEfaarRKKAEV--------RNGIIRNDSLWDKLFFNKIqaslggcvRM 455
Cdd:cd05969 145 TVYGIWAPWLNGVTNVVY-EGRFDAESWygIIE----RVKVTVwytaptaiRMLMKEGDELARKYDLSSL--------RF 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 456 IVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPCNLIKLKDaEELNYFASKGEGEIC 534
Cdd:cd05969 212 IHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYPCmPIKPGSMGKPLPGVKAAVVD-ENGNELPPGTKGILA 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 535 VKG--PNVFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSDPVAQVY 612
Cdd:cd05969 291 LKPgwPSMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHRVGPFEVESALMEHPAVAEAG 368
|
490
....*....|...
gi 2024456367 613 VHG--DSLQAFLV 623
Cdd:cd05969 369 VIGkpDPLRGEII 381
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
146-631 |
1.56e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 70.49 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPCTEqfIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVIC 225
Cdd:PRK13391 25 VTYRELDERSNRLAHLFRSLGLKRGDH--VAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALIT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 --DKPDKARTLLDHVerretPGLSSIILMDPFekelterGRRCGVriqsmQEVEDCGRENRRAPVPPRPEDLSIVcFTSG 303
Cdd:PRK13391 103 saAKLDVARALLKQC-----PGVRHRLVLDGD-------GELEGF-----VGYAEAVAGLPATPIADESLGTDML-YSSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 304 TTGNPKG--AMLTHGNVVaDFSGFLKVTESQWSPTCEDVHISYLPLAHMFERMVQSVVYCHGGRI----GFfqgdirlls 377
Cdd:PRK13391 165 TTGRPKGikRPLPEQPPD-TPLPLTAFLQRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVivmeHF--------- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 378 DDMKAL------RPTIFPVVPRLLNRMydkifsqadtsLKRwvlefaarrkKAEVRNgiiRNDslwdklffnkiQASLgg 451
Cdd:PRK13391 235 DAEQYLalieeyGVTHTQLVPTMFSRM-----------LKL----------PEEVRD---KYD-----------LSSL-- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 452 cvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCNLIKLKDA-EELnyfaSK 528
Cdd:PRK13391 278 --EVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATE-GLGFTACDSEEWLAhpGTVGRAMFGDLHILDDDgAEL----PP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 529 GE-GEICVKGPNVFKgYLKDEERTSEALDQEG-WLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSD 606
Cdd:PRK13391 351 GEpGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMI-ISGGVNIYPQEAENLLITHP 428
|
490 500
....*....|....*....|....*
gi 2024456367 607 PVAQVYVHGdslqaflvgivVPDAE 631
Cdd:PRK13391 429 KVADAAVFG-----------VPNED 442
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
132-635 |
2.41e-12 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 69.43 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 132 PCLgyRKPKQPYqwlSYKEVAERAEALGSGLLQQGCKPCTEQfIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAI 211
Cdd:cd05958 2 TCL--RSPEREW---TYRDLLALANRIANVLVGELGIVPGNR-VLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 212 RYIVNTADISTVICDKPDKARtlldhverretpglssiilmdpfekeltergrrcgvriqsmqevedcgrenrrapvppr 291
Cdd:cd05958 76 AYILDKARITVALCAHALTAS----------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 292 pEDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF----LKVTESqwsptceDVHISYLPLAHMFERMVQSVVYCHGGR-- 365
Cdd:cd05958 97 -DDICILAFTSGTTGAPKATMHFHRDPLASADRYavnvLRLRED-------DRFVGSPPLAFTFGLGGVLLFPFGVGAsg 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 366 IGFFQGDIRLLSDDMKALRPTIFPVVPRllnrMYDKIFSQADTSlkrwvlefaarrkkaevrngiirndslwdklffnki 445
Cdd:cd05958 169 VLLEEATPDLLLSAIARYKPTVLFTAPT----AYRAMLAHPDAA------------------------------------ 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 446 qASLGGCVRMIVTgAAPASPTVLGFL-RAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNLIKLKDAEELNy 524
Cdd:cd05958 209 -GPDLSSLRKCVS-AGEALPAALHRAwKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVDDEGNP- 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 525 fASKGE-GEICVKGPNvfkGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYI 603
Cdd:cd05958 286 -VPDGTiGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLL 360
|
490 500 510
....*....|....*....|....*....|....*
gi 2024456367 604 RSDPVAQVYVHGDSLQAFLV---GIVVPDAEAMPG 635
Cdd:cd05958 361 QHPAVAECAVVGHPDESRGVvvkAFVVLRPGVIPG 395
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
146-631 |
2.57e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 69.93 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVIC 225
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLRE--GDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 DKP--DKARTLLDHVERretpglssiilmdPFEKELTERGRRCGVRiqsmqEVEDCGRENRRAPVPPRPEDLSIVcFTSG 303
Cdd:PRK08276 90 SAAlaDTAAELAAELPA-------------GVPLLLVVAGPVPGFR-----SYEEALAAQPDTPIADETAGADML-YSSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 304 TTGNPKGAM--LTHGNVVADFSGFLKVTESQWSPTCEDVHISYLPLAH----MFERMVQSvvycHGGRI----GFfqgdi 373
Cdd:PRK08276 151 TTGRPKGIKrpLPGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHtaplRFGMSALA----LGGTVvvmeKF----- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 374 rllsDDMKAL------RPTIFPVVPRLLNRMydkifsqadtsLKRwvlefaarrkKAEVRNgiiRNDSlwdklffnkiqA 447
Cdd:PRK08276 222 ----DAEEALalieryRVTHSQLVPTMFVRM-----------LKL----------PEEVRA---RYDV-----------S 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 448 SLggcvRMIVTGAAPASPTVLgflRAAL---GCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCNL-IKLKDAEE 521
Cdd:PRK08276 263 SL----RVAIHAAAPCPVEVK---RAMIdwwGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGEVrILDEDGNE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 522 LnyfASKGEGEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGkWL-PNGTLKIIDRKKHIFkLAQGEYIAPEKIEN 600
Cdd:PRK08276 335 L---PPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVG-YLdEDGYLYLTDRKSDMI-ISGGVNIYPQEIEN 409
|
490 500 510
....*....|....*....|....*....|.
gi 2024456367 601 IYIRSDPVAQVYVHGdslqaflvgivVPDAE 631
Cdd:PRK08276 410 LLVTHPKVADVAVFG-----------VPDEE 429
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
529-613 |
4.87e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 69.21 E-value: 4.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 529 GE--GEICVKGPNVFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSD 606
Cdd:PRK08162 385 GEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDII-ISGGENISSIEVEDVLYRHP 462
|
....*..
gi 2024456367 607 PVAQVYV 613
Cdd:PRK08162 463 AVLVAAV 469
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
146-634 |
1.06e-11 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 67.66 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLydtlgpgairyivntadistvic 225
Cdd:cd17652 13 LTYAELNARANRLARLLAARGVGP--ERLVALALPRSAELVVAILAVLKAGAAYLPL----------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 dkpdkartlldhverretpglssiilmDP-FEKEltergrrcgvRIQSMqeVEDCgrenRRAPVPPRPEDLSIVCFTSGT 304
Cdd:cd17652 68 ---------------------------DPaYPAE----------RIAYM--LADA----RPALLLTTPDNLAYVIYTSGS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 305 TGNPKGAMLTH---GNVVADFSGFLKVTE----SQWSPTCEDVHISYLPLAhmfermvqsvvYCHGGRIGFFQGDIRL-- 375
Cdd:cd17652 105 TGRPKGVVVTHrglANLAAAQIAAFDVGPgsrvLQFASPSFDASVWELLMA-----------LLAGATLVLAPAEELLpg 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 376 --LSDDMKALRPTIFPVVPRLLNRMYDkifsqadtslkrwvlefaarrkkaevrngiirndslwdklffnkiqASLGGCV 453
Cdd:cd17652 174 epLADLLREHRITHVTLPPAALAALPP----------------------------------------------DDLPDLR 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 454 RMIVTGAAPASPTVLgflRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNLIKLKDAeELNYFASKGEGE 532
Cdd:cd17652 208 TLVVAGEACPAELVD---RWAPGRRMINAYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYVLDA-RLRPVPPGVPGE 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 533 ICVKGPNVFKGYLKDEERTSE-------ALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRS 605
Cdd:cd17652 284 LYIAGAGLARGYLNRPGLTAErfvadpfGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKI-RGFRIELGEVEAALTEH 362
|
490 500 510
....*....|....*....|....*....|..
gi 2024456367 606 DPVAQ--VYVHGDSL-QAFLVGIVVPDAEAMP 634
Cdd:cd17652 363 PGVAEavVVVRDDRPgDKRLVAYVVPAPGAAP 394
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
454-613 |
1.12e-11 |
|
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: 67.74 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 454 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHVGAPL-PCNLIKLKDaEELNYFASKGEG 531
Cdd:cd05920 258 RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTrLDDPDEVIIHTQGRPMsPDDEIRVVD-EEGNPVPPGEEG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 532 EICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSDPVAQV 611
Cdd:cd05920 337 ELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVENLLLRHPAVHDA 415
|
..
gi 2024456367 612 YV 613
Cdd:cd05920 416 AV 417
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
146-651 |
1.14e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 67.73 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVntadistviC 225
Cdd:PRK13390 25 VSYRQLDDDSAALARVLYDAGLRT--GDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIV---------G 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 DKpdKARTLldhVERRETPGLSSiilmdpfekeltERGRRCGVRIQSMQEVEDCGR-ENRRAPVPPRPEDL---SIVCFT 301
Cdd:PRK13390 94 DS--GARVL---VASAALDGLAA------------KVGADLPLRLSFGGEIDGFGSfEAALAGAGPRLTEQpcgAVMLYS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 302 SGTTGNPKG--------AMLTHGN-VVADFSGFLKVTESqwsptceDVHISYLPLAHMFERMVQSVVYCHGGRIGFFQG- 371
Cdd:PRK13390 157 SGTTGFPKGiqpdlpgrDVDAPGDpIVAIARAFYDISES-------DIYYSSAPIYHAAPLRWCSMVHALGGTVVLAKRf 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 372 DIRLLSDDMKALRPTIFPVVPRLLNRMYdkifsqadtslkrwvlefaarRKKAEVRNgiiRNDSlwdklffnkiqASLgg 451
Cdd:PRK13390 230 DAQATLGHVERYRITVTQMVPTMFVRLL---------------------KLDADVRT---RYDV-----------SSL-- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 452 cvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCNL-IKLKDAEELnyfaSK 528
Cdd:PRK13390 273 --RAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGRSVLGDLhICDDDGNEL----PA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 529 GE-GEICVKGPNVFKGYLKDEERTSEALD--QEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRS 605
Cdd:PRK13390 346 GRiGTVYFERDRLPFRYLNDPEKTAAAQHpaHPFWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQETENALTMH 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2024456367 606 DPVAQVYVHGdslqaflvgivVPDAEaMPGWAKK-----RGFDGTyEELCR 651
Cdd:PRK13390 425 PAVHDVAVIG-----------VPDPE-MGEQVKAviqlvEGIRGS-DELAR 462
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
263-631 |
1.36e-11 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 67.62 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 263 GRRCGVRIQSMQEVEDCGRENRRAPVPPRPEDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGfLKvteSQWSPTCEDVHI 342
Cdd:PRK09274 144 GGRLLWGGTTLATLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEA-LR---EDYGIEPGEIDL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 343 SYLPLAHMFERM--VQSVVychggrigffqgdirllsDDMKALRP-TIFPvvprllnrmyDKIFSQAD----TSLkrwvl 415
Cdd:PRK09274 220 PTFPLFALFGPAlgMTSVI------------------PDMDPTRPaTVDP----------AKLFAAIErygvTNL----- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 416 eFAarrkkaevrngiirNDSLWDKL--FFNKIQASLGGCVRMIVTGAaPASPTVLGFLRAAL--GCQVYEGYGQTECTAG 491
Cdd:PRK09274 267 -FG--------------SPALLERLgrYGEANGIKLPSLRRVISAGA-PVPIAVIERFRAMLppDAEILTPYGATEALPI 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 492 CT-------FTTPGDWTSGH---VGAPLPCNLIKL-----------KDAEELNyfasKGE-GEICVKGPNVFKGYLKDEE 549
Cdd:PRK09274 331 SSiesreilFATRAATDNGAgicVGRPVDGVEVRIiaisdapipewDDALRLA----TGEiGEIVVAGPMVTRSYYNRPE 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 550 RTSEA--LDQEG--WLHTGDIGkWL-PNGTLKIIDRKKHIFKLAQGEYIapekieniyirSDPVAQVY-VHGDSLQAFLV 623
Cdd:PRK09274 407 ATRLAkiPDGQGdvWHRMGDLG-YLdAQGRLWFCGRKAHRVETAGGTLY-----------TIPCERIFnTHPGVKRSALV 474
|
....*...
gi 2024456367 624 GIVVPDAE 631
Cdd:PRK09274 475 GVGVPGAQ 482
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
289-623 |
1.76e-11 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 67.18 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 289 PPRPEDLSIVC-FTSGTTGNPKGAMLTH-GNVVADFSGFLKvtesqWSPTCEDVHISYLPLAHmfermvqsvvyCHGGri 366
Cdd:PLN02479 190 PPADEWQSIALgYTSGTTASPKGVVLHHrGAYLMALSNALI-----WGMNEGAVYLWTLPMFH-----------CNGW-- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 367 gFFQGDIRLLSDDMKALRPTIFPVVprllnrmYDKIFSQAdtslkrwVLEFAArrkKAEVRNGIIrNDSLWDKLFfnkiq 446
Cdd:PLN02479 252 -CFTWTLAALCGTNICLRQVTAKAI-------YSAIANYG-------VTHFCA---APVVLNTIV-NAPKSETIL----- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 447 aSLGGCVRMIVTGAAPaSPTVLgFLRAALGCQVYEGYGQTEcTAG----CTFTTPGDWTSGHVGAPLPC----NLIKLK- 517
Cdd:PLN02479 308 -PLPRVVHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSE-TYGpstvCAWKPEWDSLPPEEQARLNArqgvRYIGLEg 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 518 ----DAEELNYFASKGE--GEICVKGPNVFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGE 591
Cdd:PLN02479 384 ldvvDTKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGGE 461
|
330 340 350
....*....|....*....|....*....|..
gi 2024456367 592 YIAPEKIENIyirsdpvaqVYVHGDSLQAFLV 623
Cdd:PLN02479 462 NISSLEVENV---------VYTHPAVLEASVV 484
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
183-623 |
1.94e-11 |
|
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: 67.11 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 183 PEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVICDkpDKARTLLDHVERrETPGLSSIILMDPFEKE--LT 260
Cdd:cd05928 78 PEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTS--DELAPEVDSVAS-ECPSLKTKLLVSEKSRDgwLN 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 261 ERGRrcgvrIQSMQEVEDCgrenrrapVPPRPEDLSIVCFTSGTTGNPKGAMLTHGN----VVADFSGFLKVTESQWSPT 336
Cdd:cd05928 155 FKEL-----LNEASTEHHC--------VETGSQEPMAIYFTSGTTGSPKMAEHSHSSlglgLKVNGRYWLDLTASDIMWN 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 337 CEDVHISYLPLAHMFERMVQ-SVVYCHggRIGFFQGDIRLlsddmKALrpTIFPVvprllnrmydKIFSQADTSLKRWVL 415
Cdd:cd05928 222 TSDTGWIKSAWSSLFEPWIQgACVFVH--HLPRFDPLVIL-----KTL--SSYPI----------TTFCGAPTVYRMLVQ 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 416 EFAARRKKAEVRNgiirndslwdklffnkiqaslggCVrmivTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFT 495
Cdd:cd05928 283 QDLSSYKFPSLQH-----------------------CV----TGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 496 TPGDWTSGHVGAPLPCNLIKLKDaEELNYFASKGEGEICVK-GPN----VFKGYLKDEERTSEALDQEGWLhTGDIGKWL 570
Cdd:cd05928 336 KGMKIKPGSMGKASPPYDVQIID-DNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIRGDFYL-TGDRGIMD 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 571 PNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVYV-------HGDSLQAFLV 623
Cdd:cd05928 414 EDGYFWFMGRADDVI-NSSGYRIGPFEVESALIEHPAVVESAVvsspdpiRGEVVKAFVV 472
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
289-599 |
4.29e-11 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 66.18 E-value: 4.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 289 PPRPEDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF----LKVTESqwsptceDVHISYLPLAH-Mfermvqsvvychg 363
Cdd:PRK09192 172 RPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAIshdgLKVRPG-------DRCVSWLPFYHdM------------- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 364 GRIGFFQGDI--RLLSDDMK----ALRP------------TI-------FPVVPRllnRMYDKifSQADTSLKRWvlefa 418
Cdd:PRK09192 232 GLVGFLLTPVatQLSVDYLPtrdfARRPlqwldlisrnrgTIsysppfgYELCAR---RVNSK--DLAELDLSCW----- 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 419 arrKKAEVRNGIIRNDSLwdKLFFNKIqaslggcvrmivtgaAPAsptvlGF-LRAALGCqvyegYGQTECTAGCTFTTP 497
Cdd:PRK09192 302 ---RVAGIGADMIRPDVL--HQFAEAF---------------APA-----GFdDKAFMPS-----YGLAEATLAVSFSPL 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 498 G----------DWTSGH------------------VGAPLPCNLIKLKDaEELNYFASKGEGEICVKGPNVFKGYLKDEE 549
Cdd:PRK09192 352 GsgivveevdrDRLEYQgkavapgaetrrvrtfvnCGKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLMSGYFRDEE 430
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2024456367 550 rTSEALDQEGWLHTGDIGkWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIE 599
Cdd:PRK09192 431 -SQDVLAADGWLDTGDLG-YLLDGYLYITGRAKDLI-IINGRNIWPQDIE 477
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
144-637 |
1.11e-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: 64.31 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 144 QWLSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTV 223
Cdd:cd17649 11 QSLSYAELDARANRLAHRLRALGVGP--EVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 224 ICDkpdkartlldhverretpglssiilmdpfekeltergrrcgvriqsmqevedcgrenrrapvppRPEDLSIVCFTSG 303
Cdd:cd17649 89 LTH----------------------------------------------------------------HPRQLAYVIYTSG 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 304 TTGNPKGAMLTHGNVVAdfsgFLKVTESQWSPTCEDVHISYLPL----AHmfERMVQSVVycHGGRI----GFFQGDIRL 375
Cdd:cd17649 105 STGTPKGVAVSHGPLAA----HCQATAERYGLTPGDRELQFASFnfdgAH--EQLLPPLI--CGACVvlrpDELWASADE 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 376 LSDDMKALRPTIFPVVPRLLNRmydkifsqadtsLKRWVLEFAARRKKAevrngiirndslwdklffnkiqaslggcVRM 455
Cdd:cd17649 177 LAEMVRELGVTVLDLPPAYLQQ------------LAEEADRTGDGRPPS----------------------------LRL 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 456 IVTGAAPASPTvlgFLRAALGCQVY--EGYGQTECTAGCT-FTTPGD----WTSGHVGAPLPCNLIKLKDAEeLNYFASK 528
Cdd:cd17649 217 YIFGGEALSPE---LLRRWLKAPVRlfNAYGPTEATVTPLvWKCEAGaaraGASMPIGRPLGGRSAYILDAD-LNPVPVG 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 529 GEGEICVKGPNVFKGYLKDEERTSEAL-----DQEG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 601
Cdd:cd17649 293 VTGELYIGGEGLARGYLGRPELTAERFvpdpfGAPGsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-RGFRIELGEIEAA 371
|
490 500 510
....*....|....*....|....*....|....*....
gi 2024456367 602 YIRSDPVAQVYV--HGDSLQAFLVGIVVP-DAEAMPGWA 637
Cdd:cd17649 372 LLEHPGVREAAVvaLDGAGGKQLVAYVVLrAAAAQPELR 410
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
144-633 |
2.34e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 64.59 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 144 QWLSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLyDTLGPGA-IRYIVNTAdist 222
Cdd:PRK12316 4575 EKLTYAELNRRANRLAHALIARGVGP--EVLVGIAMERSAEMMVGLLAVLKAGGAYVPL-DPEYPRErLAYMMEDS---- 4647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 223 vicdkpdKARTLLDH---VERRETP-GLSSIILmDPFEkeltergrrcgvriqsmqevEDCGRENRRAPVPPRPEDLSIV 298
Cdd:PRK12316 4648 -------GAALLLTQshlLQRLPIPdGLASLAL-DRDE--------------------DWEGFPAHDPAVRLHPDNLAYV 4699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 299 CFTSGTTGNPKGAMLTHGNVVAdfsgFLKVTESQWSPTCEDVHISYLPLAhmFERMVQSV--VYCHGGRIgffqgdirll 376
Cdd:PRK12316 4700 IYTSGSTGRPKGVAVSHGSLVN----HLHATGERYELTPDDRVLQFMSFS--FDGSHEGLyhPLINGASV---------- 4763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 377 sddmkALRPTIFPVVPRLLNRMYDKIFSQAD--TSLKRWVLEFAARRKK-AEVRngiirndslwdklffnkiQASLGGcv 453
Cdd:PRK12316 4764 -----VIRDDSLWDPERLYAEIHEHRVTVLVfpPVYLQQLAEHAERDGEpPSLR------------------VYCFGG-- 4818
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 454 rmivTGAAPASPTVLgfLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSG----HVGAPLPCNLIKLKDaEELNYFASK 528
Cdd:PRK12316 4819 ----EAVAQASYDLA--WRALKPVYLFNGYGPTETTVTVLlWKARDGDACGaaymPIGTPLGNRSGYVLD-GQLNPLPVG 4891
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 529 GEGEICVKGPNVFKGYLKDEERTSEAL------DQEGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 601
Cdd:PRK12316 4892 VAGELYLGGEGVARGYLERPALTAERFvpdpfgAPGGRLYrTGDLARYRADGVIDYLGRVDHQVKI-RGFRIELGEIEAR 4970
|
490 500 510
....*....|....*....|....*....|....
gi 2024456367 602 YIRSDPV--AQVYVHGDSLQAFLVGIVVPDAEAM 633
Cdd:PRK12316 4971 LREHPAVreAVVIAQEGAVGKQLVGYVVPQDPAL 5004
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
454-631 |
3.53e-10 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 63.18 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 454 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCNLIKLKDaEELNYFASKGEG 531
Cdd:PRK12406 274 RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE-SGAVTFATSEDALShpGTVGKAAPGAELRFVD-EDGRPLPQGEIG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 532 EICVKGPNV--FKGYLKDEERTseALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVA 609
Cdd:PRK12406 352 EIYSRIAGNpdFTYHNKPEKRA--EIDRGGFITSGDVGYLDADGYLFLCDRKRDMV-ISGGVNIYPAEIEAVLHAVPGVH 428
|
170 180
....*....|....*....|..
gi 2024456367 610 QVYVHGdslqaflvgivVPDAE 631
Cdd:PRK12406 429 DCAVFG-----------IPDAE 439
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
292-634 |
7.99e-10 |
|
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: 61.65 E-value: 7.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 292 PEDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSGflkvtesQWSPTCEDVHI-----SYLpLAHMFERMVQSVVYCHg 363
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVnlrTSLSE-------RYFGRDNGDEAvlffsNYV-FDFFVEQMTLALLNGQ- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 364 grigffqgDIRLLSDDMKALRPTIfpvvPRLLNRMYDKIFSQADTSLKRWvlEFAarrkkaevrngiiRNDSLwdklffn 443
Cdd:cd17648 164 --------KLVVPPDEMRFDPDRF----YAYINREKVTYLSGTPSVLQQY--DLA-------------RLPHL------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 444 kiqaslggcVRMIVTGAAPASPtVLGFLRAALGCQVYEGYGQTEC--TAGCTFTTPGDWTSGHVGAPLP---CNLikLKD 518
Cdd:cd17648 210 ---------KRVDAAGEEFTAP-VFEKLRSRFAGLIINAYGPTETtvTNHKRFFPGDQRFDKSLGRPVRntkCYV--LND 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 519 AeeLNYFASKGEGEICVKGPNVFKGYLKDEERTSE-------ALDQEGWL-------HTGDIGKWLPNGTLKIIDRKKHI 584
Cdd:cd17648 278 A--MKRVPVGAVGELYLGGDGVARGYLNRPELTAErflpnpfQTEQERARgrnarlyKTGDLVRWLPSGELEYLGRNDFQ 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024456367 585 FKLaQGEYIAPEKIENIY-----IRSDPVAQVYVHGDSL---QAFLVGIVVPDAEAMP 634
Cdd:cd17648 356 VKI-RGQRIEPGEVEAALasypgVRECAVVAKEDASQAQsriQKYLVGYYLPEPGHVP 412
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
128-629 |
8.61e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 61.97 E-value: 8.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 128 SENGPCLGYRKpkQPYQWLSY-KEVAERAEALGSglLQQGCKPCteqFIGVFAQNRPEWIISELACYTYSMVVVPLYDTL 206
Cdd:PRK13388 14 GDDTIAVRYGD--RTWTWREVlAEAAARAAALIA--LADPDRPL---HVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 207 GPGAIRYIVNTADISTVICDkpDKARTLLDHVErreTPGLSSIILMDPFEKELTERGRRCgvriqsmqevedcgrenrrA 286
Cdd:PRK13388 87 RGAALAADIRRADCQLLVTD--AEHRPLLDGLD---LPGVRVLDVDTPAYAELVAAAGAL-------------------T 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 287 PV-PPRPEDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVteSQWSPTCEDVHISYLPLAHMFERMVQ-SVVYCHGG 364
Cdd:PRK13388 143 PHrEVDAMDPFMLIFTSGTTGAPKAVRCSHGRLA--FAGRALT--ERFGLTRDDVCYVSMPLFHSNAVMAGwAPAVASGA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 365 RIgffqgdirllsddmkALRPTifpvvprllnrmydkifsqadtslkrwvleFAARRKKAEVRngiirndsLWDKLFFNK 444
Cdd:PRK13388 219 AV---------------ALPAK------------------------------FSASGFLDDVR--------RYGATYFNY 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 445 IQASLGgcvRMIVTGAAP---ASPTVLGFLRAA-----------LGCQVYEGYGQTEctAGCTFTTPGDWTSGHVGAPLP 510
Cdd:PRK13388 246 VGKPLA---YILATPERPddaDNPLRVAFGNEAsprdiaefsrrFGCQVEDGYGSSE--GAVIVVREPGTPPGSIGRGAP 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 511 CnlIKLKDAEELN-----YFASKGE--------GEICVK-GPNVFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLK 576
Cdd:PRK13388 321 G--VAIYNPETLTecavaRFDAHGAllnadeaiGELVNTaGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIY 397
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2024456367 577 IIDRKKHIFKLaQGEYIAPEKIENIYIRSDPVAQVYVHGdslqaflvgivVPD 629
Cdd:PRK13388 398 FAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYA-----------VPD 438
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
460-631 |
1.70e-09 |
|
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: 60.85 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 460 AAPASPTVLGFLRAALGCQVYEGYGQTECTaGCTFTTPGDWTS--GHVGAPLPCNL-IKLKDAEELnyfASKGEGEICVK 536
Cdd:cd05929 253 AAPCPPWVKEQWIDWGGPIIWEYYGGTEGQ-GLTIINGEEWLThpGSVGRAVLGKVhILDEDGNEV---PPGEIGEVYFA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 537 GPNVFKgYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRsdpvaqvyvHGD 616
Cdd:cd05929 329 NGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIA---------HPK 397
|
170
....*....|....*
gi 2024456367 617 SLQAFLVGivVPDAE 631
Cdd:cd05929 398 VLDAAVVG--VPDEE 410
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
296-649 |
1.75e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 60.88 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 296 SIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVTESQWSPTCEDVhisYLPLAHMFERMVQSVVYC---HGGRIgFFQG- 371
Cdd:PRK07008 179 SSLCYTSGTTGNPKGALYSHRSTV--LHAYGAALPDAMGLSARDA---VLPVVPMFHVNAWGLPYSaplTGAKL-VLPGp 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 372 --DIRLLSDDMKALRPTIFPVVPR----LLNRMydkifsqadtslkrwvlefaarrKKAEVRngiirndslwdklfFNKI 445
Cdd:PRK07008 253 dlDGKSLYELIEAERVTFSAGVPTvwlgLLNHM-----------------------REAGLR--------------FSTL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 446 QaslggcvRMIVTGAApASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPgdwTSGHVGAPLPCNL-IKLK------- 517
Cdd:PRK07008 296 R-------RTVIGGSA-CPPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLCKL---KWKHSQLPLDEQRkLLEKqgrviyg 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 518 --------DAEELNYfASKGEGEICVKGPNVFKGYLKDEErtSEALDqeGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQ 589
Cdd:PRK07008 365 vdmkivgdDGRELPW-DGKAFGDLQVRGPWVIDRYFRGDA--SPLVD--GWFPTGDVATIDADGFMQITDRSKDVIK-SG 438
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024456367 590 GEYIAPEKIENIYIRSDPVAqvyvhgdslQAFLVGIvvpdaeAMPGW--------AKKRGFDGTYEEL 649
Cdd:PRK07008 439 GEWISSIDIENVAVAHPAVA---------EAACIAC------AHPKWderpllvvVKRPGAEVTREEL 491
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
262-611 |
1.98e-09 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 60.55 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 262 RGRRCGVRIQSMQEVedcGRENRRAPVPPRP-EDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWSptcEDV 340
Cdd:PRK05851 123 RAVDSSVTVHDLATA---AHTNRSASLTPPDsGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAA---TDV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 341 HISYLPLAH-MfermvqsvvychggrigffqGDIRLLSDDMKA----LRPTifpvvprllnrmydKIFSQADTSLKRWVL 415
Cdd:PRK05851 197 GCSWLPLYHdM--------------------GLAFLLTAALAGaplwLAPT--------------TAFSASPFRWLSWLS 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 416 EFAARRKKA-EVRNGIIRNdslwdklFFNKIQASLGGCVRMIVTGAAP----------ASPTVLGFLRAALGcqvyEGYG 484
Cdd:PRK05851 243 DSRATLTAApNFAYNLIGK-------YARRVSDVDLGALRVALNGGEPvdcdgferfaTAMAPFGFDAGAAA----PSYG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 485 QTECTAGCTFTTPG-----------DWTSGH----VGAPLPCNLIKLKDAEELNYFASKGEGEICVKGPNVFKGYLKDee 549
Cdd:PRK05851 312 LAESTCAVTVPVPGiglrvdevttdDGSGARrhavLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQ-- 389
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024456367 550 rtsEALDQEGWLHTGDIGkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIyirsdpVAQV 611
Cdd:PRK05851 390 ---APIDPDDWFPTGDLG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERV------AAQV 440
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
293-634 |
2.43e-09 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 59.67 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 293 EDLSIVCFTSGTTGNPKGAMLTHGNVVA------DFSGflkvTESQWsptcedvhISYLPLAHM--FERMVQSVV----- 359
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTAsadathDRLG----GPGQW--------LLALPAHHIagLQVLVRSVIagsep 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 360 ----YCHGGRIGFFQGDIRLLSDDMK--ALRPTifpvvpRLLNRMYDkifSQADTSLKrwvlEFAArrkkaevrngiirn 433
Cdd:PRK07824 103 veldVSAGFDPTALPRAVAELGGGRRytSLVPM------QLAKALDD---PAATAALA----ELDA-------------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 434 dslwdklffnkiqaslggcvrmIVTGAAPASPTVLgflRAA--LGCQVYEGYGQTECTAGCTFTtpgdwtsghvGAPLPC 511
Cdd:PRK07824 156 ----------------------VLVGGGPAPAPVL---DAAaaAGINVVRTYGMSETSGGCVYD----------GVPLDG 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 512 NLIKLKDaeelnyfaskgeGEICVKGPNVFKGYLKDEErtSEALDQEGWLHTGDIGKwLPNGTLKIIDRKKHIFKLAqGE 591
Cdd:PRK07824 201 VRVRVED------------GRIALGGPTLAKGYRNPVD--PDPFAEPGWFRTDDLGA-LDDGVLTVLGRADDAISTG-GL 264
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2024456367 592 YIAPEKIENIYIRSDPVAQVYVHG---DSLQAFLVGIVVPDAEAMP 634
Cdd:PRK07824 265 TVLPQVVEAALATHPAVADCAVFGlpdDRLGQRVVAAVVGDGGPAP 310
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
136-320 |
4.13e-09 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 59.52 E-value: 4.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 136 YRKPKQPYQWLSYKEVAERAEALGSGLLQQGCKPCTEQFIgvFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIV 215
Cdd:PRK04319 64 RYLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFI--FMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 216 NTADiSTVICDKPDkartLLDHVERRETPGLSSIILMDpfekELTERGRRCGVRIQSMQEVEDcgrenRRAPVPPRPEDL 295
Cdd:PRK04319 142 EDSE-AKVLITTPA----LLERKPADDLPSLKHVLLVG----EDVEEGPGTLDFNALMEQASD-----EFDIEWTDREDG 207
|
170 180
....*....|....*....|....*
gi 2024456367 296 SIVCFTSGTTGNPKGAMLTHGNVVA 320
Cdd:PRK04319 208 AILHYTSGSTGKPKGVLHVHNAMLQ 232
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
292-635 |
6.01e-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: 58.72 E-value: 6.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 292 PEDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVTESQWSPTCEDVHISYLPLAhmFERMVQSVV--YCHGGRIGFF 369
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLV----NLCEWHRPYFGVTPADKSLVYASFS--FDASAWEIFphLTAGAALHVV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 370 QGDIRLlsdDMKALrptifpvvprllnrmyDKIFSQADTSLKRWVLEFAARRKKAEvrngiirNDSLwdklffnkiqasl 449
Cdd:cd17645 177 PSERRL---DLDAL----------------NDYFNQEGITISFLPTGAAEQFMQLD-------NQSL------------- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 450 ggcvRMIVTGAapaspTVLGFLRAAlGCQVYEGYGQTECTAGCTfTTPGDWTSGHVGAPLPCNLIKLKDAEELNYFASKG 529
Cdd:cd17645 218 ----RVLLTGG-----DKLKKIERK-GYKLVNNYGPTENTVVAT-SFEIDKPYANIPIGKPIDNTRVYILDEALQLQPIG 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 530 -EGEICVKGPNVFKGYLKDEERTSEA------LDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIY 602
Cdd:cd17645 287 vAGELCIAGEGLARGYLNRPELTAEKfivhpfVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIEPFL 365
|
330 340 350
....*....|....*....|....*....|....*..
gi 2024456367 603 IRSDPVAQVYV----HGDSlQAFLVGIVVPDAEAMPG 635
Cdd:cd17645 366 MNHPLIELAAVlakeDADG-RKYLVAYVTAPEEIPHE 401
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
441-623 |
1.11e-08 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 58.50 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 441 FFNKIqasLGGC-------VRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTEctAGCTFT--TPGDWTSGHVGAPLP 510
Cdd:PRK06060 246 FFARV---IDSCspdsfrsLRCVVSAGEALELGLAERLMEFFGgIPILDGIGSTE--VGQTFVsnRVDEWRLGTLGRVLP 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 511 CNLIKLKdAEELNYFASKGEGEICVKGPNVFKGYLKdeeRTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIfKLAQG 590
Cdd:PRK06060 321 PYEIRVV-APDGTTAGPGVEGDLWVRGPAIAKGYWN---RPDSPVANEGWLDTRDRVCIDSDGWVTYRCRADDT-EVIGG 395
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2024456367 591 EYIAPEKIENIYIRSDPVAQVYVHG-------DSLQAFLV 623
Cdd:PRK06060 396 VNVDPREVERLIIEDEAVAEAAVVAvrestgaSTLQAFLV 435
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
111-632 |
1.18e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 58.82 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 111 YDDARTMYEVFRRGFSISENGPCLGYRKpkqpyQWLSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISEL 190
Cdd:PRK12316 507 YPLQRGVHRLFEEQVERTPEAPALAFGE-----ETLDYAELNRRANRLAHALIERGVGP--DVLVGVAMERSIEMVVALL 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 191 ACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVICDKPDKARTLLDHverretpGLSSIILMDPfekeltergrrcgvri 270
Cdd:PRK12316 580 AILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLPLAA-------GVQVLDLDRP---------------- 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 271 qsmqEVEDCGRENRRAPVPPRPEDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKV-------TESQWSPTCEDVHIS 343
Cdd:PRK12316 637 ----AAWLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAyglgvgdTVLQKTPFSFDVSVW 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 344 --YLPLAhmfermvqsvvycHGGRIGFF-QGDIR---LLSDDMKALRPTIFPVVPRLLNRMYDKIFSQADTSLKRWVLEF 417
Cdd:PRK12316 713 efFWPLM-------------SGARLVVAaPGDHRdpaKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRRIVCSG 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 418 AARRKKAEVRngiirndslwdklffnkiqaslggcvrmiVTGAAPAsptvlgflraalgCQVYEGYGQTECTAGCTFTTP 497
Cdd:PRK12316 780 EALPADAQEQ-----------------------------VFAKLPQ-------------AGLYNLYGPTEAAIDVTHWTC 817
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 498 GDWTSGHV--GAPLPCNLIKLKDAeELNYFASKGEGEICVKGPNVFKGYLKDEERTSEAL------DQEGWLHTGDIGKW 569
Cdd:PRK12316 818 VEEGGDSVpiGRPIANLACYILDA-NLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFvpspfvAGERMYRTGDLARY 896
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024456367 570 LPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDPVAQVYVHG-DSLQafLVGIVVPDAEA 632
Cdd:PRK12316 897 RADGVIEYAGRIDHQVKL-RGLRIELGEIEARLLEHPWVREAAVLAvDGKQ--LVGYVVLESEG 957
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
299-615 |
1.43e-08 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 57.84 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 299 CFTSGTTGNPKGAMLTH-GNVVadfsgflkvtesqwsptcedvhisylplahmfermvQSVVYCHGGRIGFFQGDirlls 377
Cdd:PRK06018 183 CYTSGTTGDPKGVLYSHrSNVL------------------------------------HALMANNGDALGTSAAD----- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 378 ddmkalrpTIFPVVPRLLNRMYDKIFSqADTSLKRWVLEFAA----------RRKKAEVRNGIirnDSLWDKL--FFNKI 445
Cdd:PRK06018 222 --------TMLPVVPLFHANSWGIAFS-APSMGTKLVMPGAKldgasvyellDTEKVTFTAGV---PTVWLMLlqYMEKE 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 446 QASLGGCVRMIVTGAAPASPTVLGFLRaaLGCQVYEGYGQTEctagctfTTPgdwtSGHVGApLPCNLIKLKDAEELNYF 525
Cdd:PRK06018 290 GLKLPHLKMVVCGGSAMPRSMIKAFED--MGVEVRHAWGMTE-------MSP----LGTLAA-LKPPFSKLPGDARLDVL 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 526 ASKGE------------------------GEICVKGPNVFKGYLKDEertSEALDQEGWLHTGDIGKWLPNGTLKIIDRK 581
Cdd:PRK06018 356 QKQGYppfgvemkitddagkelpwdgktfGRLKVRGPAVAAAYYRVD---GEILDDDGFFDTGDVATIDAYGYMRITDRS 432
|
330 340 350
....*....|....*....|....*....|....
gi 2024456367 582 KHIFKlAQGEYIAPEKIENIYIRSDPVAQVYVHG 615
Cdd:PRK06018 433 KDVIK-SGGEWISSIDLENLAVGHPKVAEAAVIG 465
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
150-631 |
4.43e-08 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 56.56 E-value: 4.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 150 EVAERAEALGSGLLQQGCKpcteqfIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVIcdkpd 229
Cdd:PRK05857 50 EVGGLAADLRAQSVSRGSR------VLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAAL----- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 230 kartlldhVERRETPGLSSIilmdpfeKELTERGRRCGVRIQSMQEVEDCGRENRRAPVPPR--PEDLSIVCFTSGTTGN 307
Cdd:PRK05857 119 --------VAPGSKMASSAV-------PEALHSIPVIAVDIAAVTRESEHSLDAASLAGNADqgSEDPLAMIFTSGTTGE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 308 PKGAMLTHGNVVAdFSGFLKVTESQWSpTCEDVHISYLPLAHMFERMVQSVVYC--HGGR--IGFFQGD--IRLLSDDMK 381
Cdd:PRK05857 184 PKAVLLANRTFFA-VPDILQKEGLNWV-TWVVGETTYSPLPATHIGGLWWILTClmHGGLcvTGGENTTslLEILTTNAV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 382 ALRPtifpVVPRLLNRM-YDKIFSQADTSLKRWVLEFAARRKKAEVRngiirndslwdklfFnkIQAslggcvrmivTGA 460
Cdd:PRK05857 262 ATTC----LVPTLLSKLvSELKSANATVPSLRLVGYGGSRAIAADVR--------------F--IEA----------TGV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 461 APAsptvlgflraalgcQVYeGYGQTECTAGCTFTTPGDWT---SGHVGAPLPCNLIKLKDAEELNYFASKGE-----GE 532
Cdd:PRK05857 312 RTA--------------QVY-GLSETGCTALCLPTDDGSIVkieAGAVGRPYPGVDVYLAATDGIGPTAPGAGpsasfGT 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 533 ICVKGPNVFKGYLKDEERTSEALdQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIyirSDPVAQV- 611
Cdd:PRK05857 377 LWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGGVNIAPDEVDRI---AEGVSGVr 451
|
490 500
....*....|....*....|....*
gi 2024456367 612 ----YVHGDSLQAFLVGI-VVPDAE 631
Cdd:PRK05857 452 eaacYEIPDEEFGALVGLaVVASAE 476
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
146-640 |
4.47e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 56.16 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVIC 225
Cdd:PRK13383 61 LSYRELQRATESLARRLTRDGVAP--GRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 DKpdkartllDHVERRETPGlSSIILMDPfekeltergrrcgvriqSMQEVEDCGRENRRAPvPPRpedlsIVCFTSGTT 305
Cdd:PRK13383 139 DN--------EFAERIAGAD-DAVAVIDP-----------------ATAGAEESGGRPAVAA-PGR-----IVLLTSGTT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 306 GNPKGamlthgnvvadfsgflkVTESQWSPTCEDVHISYLPLAHMF--ERMVQSVVYCHGGRIGFFQGDIrllsddmkAL 383
Cdd:PRK13383 187 GKPKG-----------------VPRAPQLRSAVGVWVTILDRTRLRtgSRISVAMPMFHGLGLGMLMLTI--------AL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 384 RPTIfpvvprLLNRMYDKIFSQADTSLKRW------------VLEFAARrkkAEVRNGIirndslwdklffnkiqaslgG 451
Cdd:PRK13383 242 GGTV------LTHRHFDAEAALAQASLHRAdaftavpvvlarILELPPR---VRARNPL--------------------P 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 452 CVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGcTFTTPG---DWTSGhVGAPLPCNLIKLKDAEElNYFASK 528
Cdd:PRK13383 293 QLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIG-ALATPAdlrDAPET-VGKPVAGCPVRILDRNN-RPVGPR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 529 GEGEICVKGPNVFKGYLKDEERTseALDqeGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPV 608
Cdd:PRK13383 370 VTGRIFVGGELAGTRYTDGGGKA--VVD--GMTSTGDMGYLDNAGRLFIVGREDDMI-ISGGENVYPRAVENALAAHPAV 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2024456367 609 AQVYV-------HGDSLQAFLV-----GIvvpDAEAMPGWAKKR 640
Cdd:PRK13383 445 ADNAVigvpderFGHRLAAFVVlhpgsGV---DAAQLRDYLKDR 485
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
144-631 |
4.57e-08 |
|
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: 56.33 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 144 QWLSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTV 223
Cdd:cd17656 12 QKLTYRELNERSNQLARFLREKGVKK--DSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 224 IcdkpdkarTLLDHVERRETPGlSSIILMDPFE-KELTERgrrcgvrIQSMQEvedcgrenrrapvpprPEDLSIVCFTS 302
Cdd:cd17656 90 L--------TQRHLKSKLSFNK-STILLEDPSIsQEDTSN-------IDYINN----------------SDDLLYIIYTS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 303 GTTGNPKGAMLTHGNVVAdfsgflkvtesqwsptcedvhisylPLAHMFERMvqsvvychggRIGFFQGDIRLLSDDmka 382
Cdd:cd17656 138 GTTGKPKGVQLEHKNMVN-------------------------LLHFEREKT----------NINFSDKVLQFATCS--- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 383 lrptiFPVVprllnrmYDKIFSQADTSLKRWVLEFAARRKKAEVRNGIIRND--------SLWdKLFFNKIQA--SLGGC 452
Cdd:cd17656 180 -----FDVC-------YQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNievvflpvAFL-KFIFSEREFinRFPTC 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 453 VRMIVTGAAP--ASPTVLGFLRAAlGCQVYEGYG--QTECTAGCTFTTPGDWTS-GHVGAPLPCNLIKLKDAE-ELNYFA 526
Cdd:cd17656 247 VKHIITAGEQlvITNEFKEMLHEH-NVHLHNHYGpsETHVVTTYTINPEAEIPElPPIGKPISNTWIYILDQEqQLQPQG 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 527 SKGEgeICVKGPNVFKGYLKDEERTSEAL------DQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIEN 600
Cdd:cd17656 326 IVGE--LYISGASVARGYLNRQELTAEKFfpdpfdPNERMYRTGDLARYLPDGNIEFLGRADHQVKI-RGYRIELGEIEA 402
|
490 500 510
....*....|....*....|....*....|....
gi 2024456367 601 IYIRSDPVAQ--VYVHGDSL-QAFLVGIVVPDAE 631
Cdd:cd17656 403 QLLNHPGVSEavVLDKADDKgEKYLCAYFVMEQE 436
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
454-630 |
7.68e-08 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 55.77 E-value: 7.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 454 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT---------FTT------PGD--WTSGHVGAPLPcnlikl 516
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAEGLVNYTrlddsderiFTTqgrpmsPDDevWVADADGNPLP------ 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 517 kdaeelnyfasKGE-GEICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHifklaQ----GE 591
Cdd:PRK10946 377 -----------QGEvGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGE 440
|
170 180 190
....*....|....*....|....*....|....*....
gi 2024456367 592 YIAPEKIENIYIRsdpvaqvyvHGDSLQAFLVGIvvPDA 630
Cdd:PRK10946 441 KIAAEEIENLLLR---------HPAVIHAALVSM--EDE 468
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
282-599 |
1.28e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.56 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 282 ENRRAPVPPrPEDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWSPtcEDVHISYLPLAH---MFERMVQSV 358
Cdd:PRK05691 156 EAWQEPALQ-PDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNP--DDVIVSWLPLYHdmgLIGGLLQPI 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 359 ---VYCHGGRIGFFQG-DIRLLsDDMKALRPTI-----FPVvpRLLN-RMYDKIFSQADtsLKRWVLEFAARRKkaevrn 428
Cdd:PRK05691 233 fsgVPCVLMSPAYFLErPLRWL-EAISEYGGTIsggpdFAY--RLCSeRVSESALERLD--LSRWRVAYSGSEP------ 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 429 giIRNDSLwdKLFFNKIQ----------ASLG-GCVRMIVTGAAPA-SPTVLGFLRAALGCQVYEGyGQTECTAGCTFTT 496
Cdd:PRK05691 302 --IRQDSL--ERFAEKFAacgfdpdsffASYGlAEATLFVSGGRRGqGIPALELDAEALARNRAEP-GTGSVLMSCGRSQ 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 497 PGdwtsghvgaplpcNLIKLKDAEELNYFASKGEGEICVKGPNVFKGYLKDEERTSEA---LDQEGWLHTGDIGkWLPNG 573
Cdd:PRK05691 377 PG-------------HAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfveHDGRTWLRTGDLG-FLRDG 442
|
330 340
....*....|....*....|....*.
gi 2024456367 574 TLKIIDRKKHIFkLAQGEYIAPEKIE 599
Cdd:PRK05691 443 ELFVTGRLKDML-IVRGHNLYPQDIE 467
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
447-638 |
2.34e-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: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 447 ASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEC-TAGCTFTTPGDWT-SGHVGAPLP---CNLIKLkDAEE 521
Cdd:cd05973 201 ARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELgMVLANHHALEHPVhAGSAGRAMPgwrVAVLDD-DGDE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 522 LnyfaskGEGEICVKGPNV-------FKGYLKDEERTSEAldqeGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIA 594
Cdd:cd05973 280 L------GPGEPGRLAIDIansplmwFRGYQLPDTPAIDG----GYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIG 348
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2024456367 595 PEKIENIYIRSDPVAQVYV-------HGDSLQAFLVgiVVPDAEAMPGWAK 638
Cdd:cd05973 349 PFDVESALIEHPAVAEAAVigvpdpeRTEVVKAFVV--LRGGHEGTPALAD 397
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
453-600 |
2.34e-07 |
|
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: 53.18 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 453 VRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTEcTAGCTFTTPGD-WTSGHVGAPLPCNLIKLKDAEelnyfaSKGE 530
Cdd:cd17633 112 IKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSE-LSFITYNFNQEsRPPNSVGRPFPNVEIEIRNAD------GGEI 184
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 531 GEICVKGPNVFKGYLKDEErtseaLDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIEN 600
Cdd:cd17633 185 GKIFVKSEMVFSGYVRGGF-----SNPDGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIES 248
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
454-632 |
2.50e-07 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 53.84 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 454 RMIVTGAAPASPTVLGF-----LRAALGcqvyegYGQTEcTAG--CTFTtPGDWTSG--HVGAPLPCNLIKLKDAEElny 524
Cdd:PRK07445 233 RTILLGGAPAWPSLLEQarqlqLRLAPT------YGMTE-TASqiATLK-PDDFLAGnnSSGQVLPHAQITIPANQT--- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 525 faskgeGEICVKGPNVFKGYLKdeertsEALDQEGWLHTGDIGKWLPNGTLKIIDR--KKHIfklAQGEYIAPEKIENIY 602
Cdd:PRK07445 302 ------GNITIQAQSLALGYYP------QILDSQGIFETDDLGYLDAQGYLHILGRnsQKII---TGGENVYPAEVEAAI 366
|
170 180 190
....*....|....*....|....*....|....
gi 2024456367 603 IRSDPVAQVYVHG--DSL--QAfLVGIVVPDAEA 632
Cdd:PRK07445 367 LATGLVQDVCVLGlpDPHwgEV-VTAIYVPKDPS 399
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
508-664 |
2.82e-07 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 53.75 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 508 PLPCNLIK-----LKDAEELNYFASKGEGEICVKGPNVFKGYLKDEERTSEA---LDQEGWLHTGDIGKwLPNGTLKIID 579
Cdd:PRK04813 317 RLPIGYAKpdsplLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAfftFDGQPAYHTGDAGY-LEDGLLFYQG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 580 RKKHIFKLAqGEYIAPEKIENI-----YIRSDPVAQVYVHGDSLQafLVGIVVPdaeampgwaKKRGFDGTYeELCRN-- 652
Cdd:PRK04813 396 RIDFQIKLN-GYRIELEEIEQNlrqssYVESAVVVPYNKDHKVQY--LIAYVVP---------KEEDFEREF-ELTKAik 462
|
170
....*....|..
gi 2024456367 653 KELQKAIMEDMV 664
Cdd:PRK04813 463 KELKERLMEYMI 474
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
146-638 |
3.00e-06 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 50.53 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLlqQGCKPCTEQFIGVFAQNRPEWIISELACYTYSMVVVPLYDTLGPGAIRYIVNTADISTVIC 225
Cdd:PRK13382 69 LTWRELDERSDALAAAL--QALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIY 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 226 DKpdkarTLLDHVER--RETPGLSSIILMDPFEKELTergrrcgvriqsmQEVEDCGRENRRapVPPRPEDLSIVCFTSG 303
Cdd:PRK13382 147 DE-----EFSATVDRalADCPQATRIVAWTDEDHDLT-------------VEVLIAAHAGQR--PEPTGRKGRVILLTSG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 304 TTGNPKGAMLTHGNVVADFSGFLKVTEsqWSptCEDVHISYLPLAH-------MFERMVQSVVYChggRIGFFQGDIRLL 376
Cdd:PRK13382 207 TTGTPKGARRSGPGGIGTLKAILDRTP--WR--AEEPTVIVAPMFHawgfsqlVLAASLACTIVT---RRRFDPEATLDL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 377 SDdmkALRPTIFPVVPRLLNRMYDKIfsqadtslkrwvlefaarrkkAEVRNgiiRNDslwdklffnkiqaslGGCVRMI 456
Cdd:PRK13382 280 ID---RHRATGLAVVPVMFDRIMDLP---------------------AEVRN---RYS---------------GRSLRFA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 457 VTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFT-TPGDWTSG--HVGAPLPCNLIKLKDAE--ELnyfaSKGE- 530
Cdd:PRK13382 318 AASGSRMRPDVVIAFMDQFGDVIYNNYNATE--AGMIATaTPADLRAApdTAGRPAEGTEIRILDQDfrEV----PTGEv 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 531 GEICVKGPNVFKGYlkdeerTSEALDQ--EGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPV 608
Cdd:PRK13382 392 GTIFVRNDTQFDGY------TSGSTKDfhDGFMASGDVGYLDENGRLFVVGRDDEMI-VSGGENVYPIEVEKTLATHPDV 464
|
490 500 510
....*....|....*....|....*....|....*..
gi 2024456367 609 AQVYV-------HGDSLQAFLVgiVVPDAEAMPGWAK 638
Cdd:PRK13382 465 AEAAVigvddeqYGQRLAAFVV--LKPGASATPETLK 499
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
292-623 |
3.67e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 50.94 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 292 PEDLSIVCFTSGTTGNPKGAMLT-HGNVVADFSG--FLKVTE----SQWSPTCEDVHISYLPLAHMFermvqsvvychGG 364
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEqRGMLNNQLSKvpYLALSEadviAQTASQSFDISVWQFLAAPLF-----------GA 3936
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 365 RIGFFQGDI----RLLSDDMKALRPTIFPVVPRLLNRMydkifsqadtslkrwvlefaarrkkaevrngiIRNDslwdkl 440
Cdd:PRK05691 3937 RVEIVPNAIahdpQGLLAHVQAQGITVLESVPSLIQGM--------------------------------LAED------ 3978
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 441 ffnkiQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF------TTPGDWTSghVGAPLPCNLI 514
Cdd:PRK05691 3979 -----RQALDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFfrvdlaSTRGSYLP--IGSPTDNNRL 4051
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 515 KLKDaEELNYFASKGEGEICVKGPNVFKGYLKDEERTSEAL-------DQEGWLHTGDIGKWLPNGTLKIIDRKKHI--- 584
Cdd:PRK05691 4052 YLLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFvphpfgaPGERLYRTGDLARRRSDGVLEYVGRIDHQvki 4130
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2024456367 585 --FKLAQGEyIAPEKIENIYIRSDPVA-QVYVHGDSLQAFLV 623
Cdd:PRK05691 4131 rgYRIELGE-IEARLHEQAEVREAAVAvQEGVNGKHLVGYLV 4171
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
287-653 |
7.37e-06 |
|
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: 49.35 E-value: 7.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 287 PVPPRPE-DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWSPTceDVHISYLPLAHMFERMVQSVVYCHGGR 365
Cdd:cd05915 146 DPVRVPErAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEK--DVVLPVVPMFHVNAWCLPYAATLVGAK 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 366 IGFFQ--GDIRLLSDDMKALRPTIFPVVPRLLNrmydkIFSQADTSLKRwvlefaarrkkaevrngiirndslwdklffn 443
Cdd:cd05915 224 QVLPGprLDPASLVELFDGEGVTFTAGVPTVWL-----ALADYLESTGH------------------------------- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 444 kiqaSLGGCVRMIVTGAAPasPTVLGFLRAALGCQVYEGYGqteCTAGCTFTTPGDWTSGHVGAPLPCNLiKLKDAEELN 523
Cdd:cd05915 268 ----RLKTLRRLVVGGSAA--PRSLIARFERMGVEVRQGYG---LTETSPVVVQNFVKSHLESLSEEEKL-TLKAKTGLP 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 524 YFASK------------GEGE----ICVKGPNVFKGYLKDEERTSEALDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFKL 587
Cdd:cd05915 338 IPLVRlrvadeegrpvpKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKS 417
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024456367 588 AqGEYIAPEKIENIyirsdpvaqVYVHGDSLQAFLVGivVPD---AEAMPGWAKKRGFDGTYEEL---CRNK 653
Cdd:cd05915 418 G-GEWISSVDLENA---------LMGHPKVKEAAVVA--IPHpkwQERPLAVVVPRGEKPTPEELnehLLKA 477
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
442-615 |
8.36e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 49.01 E-value: 8.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 442 FNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPGDWTSGHVGAPLPCNLIKLKDAEE 521
Cdd:PRK07638 245 LYKENRVIENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSF-VTALVDEESERRPNSVGRPFHNVQVRICNE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 522 LNYFASKGE-GEICVKGPNVFKGYLKDEERTSEaLDQEGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIEN 600
Cdd:PRK07638 324 AGEEVQKGEiGTVYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIES 401
|
170
....*....|....*
gi 2024456367 601 IYIRSDPVAQVYVHG 615
Cdd:PRK07638 402 VLHEHPAVDEIVVIG 416
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
293-624 |
3.10e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 47.86 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 293 EDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgfLKVTESQWSPTCEDVHISYLPLAhmFErmvQSVVYCH-----GGRIG 367
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNTHAALAER----LQWMQATYALDDSDVLMQKAPIS--FD---VSVWECFwplitGCRLV 1343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 368 FF----QGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFSQADTSLKRwvLEFAARRKKAEVRNGIIrndslwDKLffn 443
Cdd:PRK05691 1344 LAgpgeHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRR--LFSGGEALPAELRNRVL------QRL--- 1412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 444 kiqaslggcvrmivtgaapasPTVlgflraalgcQVYEGYGQTECTAGCTF--TTPGDWTSGHVGAPLPCNLIKLKDAEe 521
Cdd:PRK05691 1413 ---------------------PQV----------QLHNRYGPTETAINVTHwqCQAEDGERSPIGRPLGNVLCRVLDAE- 1460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 522 LNYFASKGEGEICVKGPNVFKGYLKDEERTSE-----ALDQEG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIA 594
Cdd:PRK05691 1461 LNLLPPGVAGELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL-RGFRVE 1539
|
330 340 350
....*....|....*....|....*....|..
gi 2024456367 595 PEKIENIYIRSDPVAQ--VYVHGDSLQAFLVG 624
Cdd:PRK05691 1540 PEEIQARLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
290-615 |
3.37e-05 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 46.61 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 290 PRPEDLSIVCfTSGTTGNPKGAMLTHGNV-VADFSGFLKVTESQwsPTCEDVH--------ISYLPLAHMFermvqsvvy 360
Cdd:cd05924 1 RSADDLYILY-TGGTTGMPKGVMWRQEDIfRMLMGGADFGTGEF--TPSEDAHkaaaaaagTVMFPAPPLM--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 361 cHG-----GRIGFFQGdirllsddmkalrPTIFPVVPRLlnrmydkifsQADTslkrwVLEFAARRKkaeVRNGIIRNDS 435
Cdd:cd05924 69 -HGtgswtAFGGLLGG-------------QTVVLPDDRF----------DPEE-----VWRTIEKHK---VTSMTIVGDA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 436 LWDKLffnkIQASLGG------CVRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAP 508
Cdd:cd05924 117 MARPL----IDALRDAgpydlsSLFAISSGGALLSPEVKqGLLELVPNITLVDAFGSSETGFTGSGHSAGSGPETGPFTR 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 509 LPCNLIKLKDAEELNYFASKGEGEICVKGpNVFKGYLKDEERTSEA---LDQEGWLHTGDIGKWLPNGTLKIIDRKKHIF 585
Cdd:cd05924 193 ANPDTVVLDDDGRVVPPGSGGVGWIARRG-HIPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGRGSVCI 271
|
330 340 350
....*....|....*....|....*....|.
gi 2024456367 586 KLAqGEYIAPEKIENIyIRSDP-VAQVYVHG 615
Cdd:cd05924 272 NTG-GEKVFPEEVEEA-LKSHPaVYDVLVVG 300
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
258-350 |
1.56e-04 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 44.97 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 258 ELTERGRRCGVRIQSM--QEVEDCGRENRRAPVPPRPEDLS---------IVCFTSGTTGNPKGAMLTHGNVVAdFSGFL 326
Cdd:cd05938 98 ALRADGVSVWYLSHTSntEGVISLLDKVDAASDEPVPASLRahvtikspaLYIYTSGTTGLPKAARISHLRVLQ-CSGFL 176
|
90 100
....*....|....*....|....
gi 2024456367 327 KVTesqwSPTCEDVHISYLPLAHM 350
Cdd:cd05938 177 SLC----GVTADDVIYITLPLYHS 196
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
563-629 |
2.99e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 44.26 E-value: 2.99e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024456367 563 TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIyIRSDP-VAQVYVH-----------GDSLQafLVGIVVPD 629
Cdd:PRK10252 841 TGDVARWLDDGAVEYLGRSDDQLKI-RGQRIELGEIDRA-MQALPdVEQAVTHacvinqaaatgGDARQ--LVGYLVSQ 915
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
285-633 |
4.17e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 43.78 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 285 RAPVPPRPEDLSIVCF---TSGTTGNPKGAMLTHGNVVADF----SGFLKVTESQWSPTCEDVhiSYLPLAHMFERMVQS 357
Cdd:PRK05850 149 PRGSDARPRDLPSTAYlqyTSGSTRTPAGVMVSHRNVIANFeqlmSDYFGDTGGVPPPDTTVV--SWLPFYHDMGLVLGV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 358 VVYCHGGR-------IGFFQGDIRLLsddmkalrptifpvvpRLLNRmYDKIFSQAdtslKRWVLEFAARRKKAEVRNGI 430
Cdd:PRK05850 227 CAPILGGCpavltspVAFLQRPARWM----------------QLLAS-NPHAFSAA----PNFAFELAVRKTSDDDMAGL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 431 irndslwdklffnkiqaSLGGcVRMIVTGAAPASP-TVLGFLR--AALGCQ---VYEGYGQTECTAGCTFTTPGD----- 499
Cdd:PRK05850 286 -----------------DLGG-VLGIISGSERVHPaTLKRFADrfAPFNLRetaIRPSYGLAEATVYVATREPGQppesv 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 500 ------WTSGHV-------GAPL------PCNLIKLKDAEELNYFASKGEGEICVKGPNVFKGY---LKDEERT------ 551
Cdd:PRK05850 348 rfdyekLSAGHAkrcetggGTPLvsygspRSPTVRIVDPDTCIECPAGTVGEIWVHGDNVAAGYwqkPEETERTfgatlv 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 552 --SEALDQEGWLHTGDIGkWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY--IRSDPVAQVYVHGDSLQAfLVGIV- 626
Cdd:PRK05850 428 dpSPGTPEGPWLRTGDLG-FISEGELFIVGRIKDLL-IVDGRNHYPDDIEATIqeITGGRVAAISVPDDGTEK-LVAIIe 504
|
410
....*....|..
gi 2024456367 627 -----VPDAEAM 633
Cdd:PRK05850 505 lkkrgDSDEEAM 516
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
146-349 |
6.86e-04 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 42.94 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 146 LSYKEVAERAEALGSGLLQQGCKPctEQFIGVFAQNRPEWIISELACyTYSMVVVPLYDT-------------LGPGAIr 212
Cdd:PRK08279 63 ISYAELNARANRYAHWAAARGVGK--GDVVALLMENRPEYLAAWLGL-AKLGAVVALLNTqqrgavlahslnlVDAKHL- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024456367 213 yIVNTADISTVI----CDKPDKARTLLDHVERRETPGLSSIilmdpfekeltergrrcgvriqsMQEVEDCGRENRRAPV 288
Cdd:PRK08279 139 -IVGEELVEAFEearaDLARPPRLWVAGGDTLDDPEGYEDL-----------------------AAAAAGAPTTNPASRS 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024456367 289 PPRPEDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTESqwsptceDVHISYLPLAH 349
Cdd:PRK08279 195 GVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLkamGGFGGLLRLTPD-------DVLYCCLPLYH 251
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
285-319 |
8.58e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 42.72 E-value: 8.58e-04
10 20 30
....*....|....*....|....*....|....*
gi 2024456367 285 RAPVPPRPEDLSIVCFTSGTTGNPKGAMLTHGNVV 319
Cdd:PRK10252 590 APLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIV 624
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
284-316 |
1.31e-03 |
|
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: 42.18 E-value: 1.31e-03
10 20 30
....*....|....*....|....*....|...
gi 2024456367 284 RRAPVPPRPEDLSIVCFTSGTTGNPKGAMLTHG 316
Cdd:cd17634 223 EHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTG 255
|
|
| |
