|
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 ... |
101-678 |
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: 875.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 101 QPYRWLSYKQVSDRAEYLGSCLLHKGYKSSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADI 180
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 181 AMVICDtpqkasvlienvekgftpslkvvilmdpfdddlkqrgekSGIEILSLYDAENLGKEHFRKPVPPSPEDLSIICF 260
Cdd:cd05927 81 SIVFCD---------------------------------------AGVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 261 TSGTTGDPKGAMITHQNIVSNASAFLKCVEHTFEPTPDDVTISYLPLAHMFERVVQTVVYCCGARVGFFQGNIRLLADDM 340
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 341 NTLKPTLFPTVPRVLNRIYDKVQN--EAKTPLKKFLLNLAVASKFKELQKGIIRRDSFWDKLIFAKIQASLGGRVRIIVT 418
Cdd:cd05927 202 KALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 419 GAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTSPGDWTSGHVGAPLTCNYVKLEDVADMDYFS--VNNEGEICIK 496
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAkdPNPRGEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 497 GTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAQGEYIAPEKIENIYNRSRPVLQIFVHGE 576
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 577 SLRSSLVGVVVPDPDVLPSFAA-KLGVKGSFEELCQNQVVRKAILEDLQKIGKESGLKTFEQVKAVFLHPEPFSIENGLL 655
Cdd:cd05927 442 SLKSFLVAIVVPDPDVLKEWAAsKGGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLL 521
|
570 580
....*....|....*....|...
gi 1622967304 656 TPTLKAKRGELSKYFRTQIDSLY 678
Cdd:cd05927 522 TPTFKLKRPQLKKYYKKQIDEMY 544
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
66-681 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 696.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 66 LISHC--FSDATTMYEVFQRGLAISDNGPCLGYRKPNQ----PYRWLSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFA 139
Cdd:PLN02736 33 LVSRFpdHPEIGTLHDNFVYAVETFRDYKYLGTRIRVDgtvgEYKWMTYGEAGTARTAIGSGLVQHGIP--KGACVGLYF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 140 QNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVICdTPQKASVLIENVEKgfTPSLKVVILMDPFDDDL 219
Cdd:PLN02736 111 INRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCLSE--IPSVRLIVVVGGADEPL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 220 KQRGEKSGIEILSLYDAENLGKEHFRKPVPPSPEDLSIICFTSGTTGDPKGAMITHQNIVSNASAFlkCVEHTFEPTpdD 299
Cdd:PLN02736 188 PSLPSGTGVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGS--SLSTKFYPS--D 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 300 VTISYLPLAHMFERVVQTVVYCCGARVGFFQGNIRLLADDMNTLKPTLFPTVPRVLNRIYDKVQNEAKT--PLKKFLLNL 377
Cdd:PLN02736 264 VHISYLPLAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKEsgGLKERLFNA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 378 AVASKFKELQKGiiRRDS-FWDKLIFAKIQASLGGRVRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTS 456
Cdd:PLN02736 344 AYNAKKQALENG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMD 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 457 PGDWTSGHVGAPLTCNYVKLEDVADMDYFSVNN---EGEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNG 533
Cdd:PLN02736 422 EGDNLSGHVGSPNPACEVKLVDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGG 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 534 TLKIIDRKKNIFKLAQGEYIAPEKIENIYNRSRPVLQIFVHGESLRSSLVGVVVPDPDVLPSFAAKLGVK-GSFEELCQN 612
Cdd:PLN02736 502 RLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQLCND 581
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622967304 613 QVVRKAILEDLQKIGKESGLKTFEQVKAVFLHPEPFSIENGLLTPTLKAKRGELSKYFRTQIDSLYEHI 681
Cdd:PLN02736 582 PRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYAEL 650
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
72-680 |
7.20e-178 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 519.66 E-value: 7.20e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 72 SDATTMYEVFQRGLAISDNGPCLGYrKPNQPYRWLSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELA 151
Cdd:COG1022 8 PPADTLPDLLRRRAARFPDRVALRE-KEDGIWQSLTWAEFAERVRALAAGLLALGVK--PGDRVAILSDNRPEWVIADLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 152 CYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVICDTPQKASVLIENVEKgfTPSLKVVILMDPfdddlkqRGEKSGIEIL 231
Cdd:COG1022 85 ILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDE--LPSLRHIVVLDP-------RGLRDDPRLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 232 SLYDAENLGKEHF------RKPVPPSPEDLSIICFTSGTTGDPKGAMITHQNIVSNASAFLKCvehtFEPTPDDVTISYL 305
Cdd:COG1022 156 SLDELLALGREVAdpaeleARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLER----LPLGPGDRTLSFL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 306 PLAHMFERVVQTVVYCCGARVGFfQGNIRLLADDMNTLKPTLFPTVPRVLNRIYDKVQN--EAKTPLKKFLLNLAVA--- 380
Cdd:COG1022 232 PLAHVFERTVSYYALAAGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAkaEEAGGLKRKLFRWALAvgr 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 381 SKFKELQKGiiRRDSFW--------DKLIFAKIQASLGGRVRIIVTGAAPISAPVMTFFRAaMGCQVYEAYGQTECTAGC 452
Cdd:COG1022 311 RYARARLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPVI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 453 TFTSPGDWTSGHVGAPLTCNYVKLEDvadmdyfsvnnEGEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPN 532
Cdd:COG1022 388 TVNRPGDNRIGTVGPPLPGVEVKIAE-----------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDED 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 533 GTLKIIDRKKNIFKLAQGEYIAPEKIENIYNRSRPVLQIFVHGESlRSSLVGVVVPDPDVLPSFAAKLGVK-GSFEELCQ 611
Cdd:COG1022 457 GFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGLPyTSYAELAQ 535
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622967304 612 NQVVRKAILEDLQKIGKesGLKTFEQVKAVFLHPEPFSIENGLLTPTLKAKRGELSKYFRTQIDSLYEH 680
Cdd:COG1022 536 DPEVRALIQEEVDRANA--GLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYAG 602
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
72-679 |
9.91e-161 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 477.77 E-value: 9.91e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 72 SDATTMYEVFQRGLAISDNGPCLGYRKPNQ----PYRWLSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWII 147
Cdd:PLN02430 39 SDITTAWDIFSKSVEKYPDNKMLGWRRIVDgkvgPYMWKTYKEVYEEVLQIGSALRASGAE--PGSRVGIYGSNCPQWIV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 148 SELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVICDTPQKASVLieNVEKGFTPSLKVVILMDPFDDDLKQRGEKSG 227
Cdd:PLN02430 117 AMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDKKIKELL--EPDCKSAKRLKAIVSFTSVTEEESDKASQIG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 228 IEILSLYDAENLGKEHFRKPVPPSPEDLSIICFTSGTTGDPKGAMITHQNIVSNASAFLKCVEHtFEP--TPDDVTISYL 305
Cdd:PLN02430 195 VKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVDLFMEQ-FEDkmTHDDVYLSFL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 306 PLAHMFERVVQTVVYCCGARVGFFQGNIRLLADDMNTLKPTLFPTVPRVLNRIYDKVQN--EAKTPLKKFLLNLAVASKF 383
Cdd:PLN02430 274 PLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYKYKL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 384 KELQKGIIRRDS--FWDKLIFAKIQASLGGRVRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTSPGDWT 461
Cdd:PLN02430 354 AWMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMC 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 462 S-GHVGAPLTCNYVKLEDVADMDY--FSVNNEGEICIKGTNVFKGYLKDPEKTQEALdSDGWLHTGDIGRWLPNGTLKII 538
Cdd:PLN02430 434 MlGTVGAPAVYNELRLEEVPEMGYdpLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKII 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 539 DRKKNIFKLAQGEYIAPEKIENIYNRSRPVLQIFVHGESLRSSLVGVVVPDPDVLPSFAAKLGVKGSFEELCQNQVVRKA 618
Cdd:PLN02430 513 DRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKEH 592
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622967304 619 ILEDLQKIGKESGLKTFEQVKAVFLHPEPFSIENGLLTPTLKAKRGELSKYFRTQIDSLYE 679
Cdd:PLN02430 593 ILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMYR 653
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
102-666 |
2.48e-159 |
|
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: 468.62 E-value: 2.48e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 102 PYRWLSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIA 181
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLVELGLK--PGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 182 MVICDtpqkasvlienvekgftpslkvvilmdpfdddlkqrgeksgieilslydaenlgkehfrkpvpPSPEDLSIICFT 261
Cdd:cd17639 80 AIFTD---------------------------------------------------------------GKPDDLACIMYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 262 SGTTGDPKGAMITHQNIVSNASAFLKCVEHTfePTPDDVTISYLPLAHMFERVVQTVVYCCGARVGFfqGNIRLLAD--- 338
Cdd:cd17639 97 SGSTGNPKGVMLTHGNLVAGIAGLGDRVPEL--LGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDksk 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 339 -----DMNTLKPTLFPTVPRVLNRIYDKVQNE--AKTPLKKFLLNLAVASKFKELQKGIirrDS-FWDKLIFAKIQASLG 410
Cdd:cd17639 173 rgckgDLTEFKPTLMVGVPAIWDTIRKGVLAKlnPMGGLKRTLFWTAYQSKLKALKEGP---GTpLLDELVFKKVRAALG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 411 GRVRIIVTGAAPISAPVMTFFrAAMGCQVYEAYGQTECTAGCTFTSPGDWTSGHVGAPLTCNYVKLEDVADMDYFSVNNE 490
Cdd:cd17639 250 GRLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDKPP 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 491 --GEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAQGEYIAPEKIENIYNRSRPV 568
Cdd:cd17639 329 prGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLV 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 569 LQIFVHGESLRSSLVGVVVPDPDVLPSFAAKLGVKGS-FEELCQNQVVRKAILEDLQKIGKESGLKTFEQVKAVFLHPEP 647
Cdd:cd17639 409 NNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGVINSeWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEE 488
|
570
....*....|....*....
gi 1622967304 648 FSIENGLLTPTLKAKRGEL 666
Cdd:cd17639 489 WTPENGLVTAAQKLKRKEI 507
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
101-666 |
4.09e-158 |
|
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: 463.61 E-value: 4.09e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 101 QPYRWLSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADI 180
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVE--PGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 181 AMVICDTPqkasvlienvekgftpslkvvilmdpfdddlkqrgeksgieilslydaenlgkehfrkpvppspEDLSIICF 260
Cdd:cd05907 79 KALFVEDP----------------------------------------------------------------DDLATIIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 261 TSGTTGDPKGAMITHQNIVSNASAFLkcveHTFEPTPDDVTISYLPLAHMFERV-VQTVVYCCGARVGFFQGnIRLLADD 339
Cdd:cd05907 95 TSGTTGRPKGVMLSHRNILSNALALA----ERLPATEGDRHLSFLPLAHVFERRaGLYVPLLAGARIYFASS-AETLLDD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 340 MNTLKPTLFPTVPRVLNRIYDKVQNEAKTPLKKFLLNLAVaskfkelqkgiirrdsfwdklifakiqaslGGRVRIIVTG 419
Cdd:cd05907 170 LSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV------------------------------GGRLRFAASG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 420 AAPISAPVMTFFRAAmGCQVYEAYGQTECTAGCTFTSPGDWTSGHVGAPLTCNYVKLEDvadmdyfsvnnEGEICIKGTN 499
Cdd:cd05907 220 GAPLPAELLHFFRAL-GIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPN 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 500 VFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAQGEYIAPEKIENIYNRSRPVLQIFVHGESlR 579
Cdd:cd05907 288 VMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDG-R 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 580 SSLVGVVVPDPDVLPSFAAKLGVKG-SFEELCQNQVVRKAILEDLQKIGKEsgLKTFEQVKAVFLHPEPFSIENGLLTPT 658
Cdd:cd05907 367 PFLVALIVPDPEALEAWAEEHGIAYtDVAELAANPAVRAEIEAAVEAANAR--LSRYEQIKKFLLLPEPFTIENGELTPT 444
|
....*...
gi 1622967304 659 LKAKRGEL 666
Cdd:cd05907 445 LKLKRPVI 452
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
78-683 |
2.07e-154 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 461.80 E-value: 2.07e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 78 YEVFQRGLAISDNGPCLGYR-----KPNQpYRWLSYKQVSDRAEYLGSCLLHKGYKSspDQFVGIFAQNRPEWIISELAC 152
Cdd:PLN02614 48 WDVFRMSVEKYPNNPMLGRReivdgKPGK-YVWQTYQEVYDIVIKLGNSLRSVGVKD--EAKCGIYGANSPEWIISMEAC 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 153 YTYSMVAVPLYDTLGPEAIVYIVNKADIAMVICDTpQKASVLIENVEKGfTPSLKVVILMDPFDDDLKQRGEKSGIEILS 232
Cdd:PLN02614 125 NAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEE-KKISELFKTCPNS-TEYMKTVVSFGGVSREQKEEAETFGLVIYA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 233 LYDAENLGK-EHFRKPVPpSPEDLSIICFTSGTTGDPKGAMITHQNIVSNASAFLKCVEHTFEP-TPDDVTISYLPLAHM 310
Cdd:PLN02614 203 WDEFLKLGEgKQYDLPIK-KKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANAAlTVKDVYLSYLPLAHI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 311 FERVVQTVVYCCGARVGFFQGNIRLLADDMNTLKPTLFPTVPRVLNRIYDKVQNEAKTP--LKKFLLNLAVASKFKELQK 388
Cdd:PLN02614 282 FDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGgfLKKFVFDSAFSYKFGNMKK 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 389 GI--IRRDSFWDKLIFAKIQASLGGRVRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTSPGDWTS-GHV 465
Cdd:PLN02614 362 GQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELDMlGTV 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 466 GAPLTCNYVKLEDVADMDYFSVNN--EGEICIKGTNVFKGYLKDPEKTQEALdSDGWLHTGDIGRWLPNGTLKIIDRKKN 543
Cdd:PLN02614 442 GPPVPNVDIRLESVPEMEYDALAStpRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRKKN 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 544 IFKLAQGEYIAPEKIENIYNRSRPVLQIFVHGESLRSSLVGVVVPDPDVLPSFAAKLGVKGSFEELCQNQVVRKAILEDL 623
Cdd:PLN02614 521 IFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEFILGEL 600
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 624 QKIGKESGLKTFEQVKAVFLHPEPFSIENGLLTPTLKAKRGELSKYFRTQIDSLYEHIQD 683
Cdd:PLN02614 601 VKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYKTTNE 660
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
102-678 |
2.90e-154 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 461.23 E-value: 2.90e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 102 PYRWLSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIA 181
Cdd:PLN02861 74 PYVWLTYKEVYDAAIRIGSAIRSRGVN--PGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 182 MVICDTPQKASVLieNVEKGFTPSLKVVILMDPFDDDLKQRGEKSGIEILSLYDAENLGKEHFRKPvPPSPEDLSIICFT 261
Cdd:PLN02861 152 IAFVQESKISSIL--SCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLDCELP-PKQKTDICTIMYT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 262 SGTTGDPKGAMITHQNIVsnasAFLKCVEHTFEPT-----PDDVTISYLPLAHMFERVVQTvvYCC--GARVGFFQGNIR 334
Cdd:PLN02861 229 SGTTGEPKGVILTNRAII----AEVLSTDHLLKVTdrvatEEDSYFSYLPLAHVYDQVIET--YCIskGASIGFWQGDIR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 335 LLADDMNTLKPTLFPTVPRVLNRIY----DKVQneAKTPLKKFLLNLAVASKFKELQKGIIRRDS--FWDKLIFAKIQAS 408
Cdd:PLN02861 303 YLMEDVQALKPTIFCGVPRVYDRIYtgimQKIS--SGGMLRKKLFDFAYNYKLGNLRKGLKQEEAspRLDRLVFDKIKEG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 409 LGGRVRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCtFTSPGDWTS--GHVGAPLTCNYVKLEDVADMDYFS 486
Cdd:PLN02861 381 LGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGC-FTSIANVFSmvGTVGVPMTTIEARLESVPEMGYDA 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 487 VNN--EGEICIKGTNVFKGYLKDPEKTQEALdSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAQGEYIAPEKIENIYNR 564
Cdd:PLN02861 460 LSDvpRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSR 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 565 SRPVLQIFVHGESLRSSLVGVVVPDPDVLPSFAAKLGVKGSFEELCQNQVVRKAILEDLQKIGKESGLKTFEQVKAVFLH 644
Cdd:PLN02861 539 CPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLE 618
|
570 580 590
....*....|....*....|....*....|....
gi 1622967304 645 PEPFSIENGLLTPTLKAKRGELSKYFRTQIDSLY 678
Cdd:PLN02861 619 PNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLY 652
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
102-548 |
1.74e-134 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 401.69 E-value: 1.74e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 102 PYRWLSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIA 181
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRALGVG--KGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 182 MVICDTPQKASVLIENVEKGFTPSLKVVILMDPFDDDLKqrgeksgieilsLYDAENLGKEHFRKPVPPSPEDLSIICFT 261
Cdd:pfam00501 96 VLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEP------------LPEEAKPADVPPPPPPPPDPDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 262 SGTTGDPKGAMITHQNIVSNASAFLKCVEHTFEPTPDDVTISYLPLAHMFERVVQT-VVYCCGARVGFFQGNIRL----L 336
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLlGPLLAGATVVLPPGFPALdpaaL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 337 ADDMNTLKPTLFPTVPRVLNRIydkvqneaktplkkfllnlavaskfkeLQKGIIRRDSFwdklifakiqaslgGRVRII 416
Cdd:pfam00501 244 LELIERYKVTVLYGVPTLLNML---------------------------LEAGAPKRALL--------------SSLRLV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 417 VTGAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTSPGDW---TSGHVGAPLTCNYVKLEDVADMDYFSVNNEGEI 493
Cdd:pfam00501 283 LSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGEL 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1622967304 494 CIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLA 548
Cdd:pfam00501 363 CVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
47-679 |
1.68e-132 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 406.42 E-value: 1.68e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 47 QSVGIEGGARKGVSQKNN---DLISHCFSDATTMYEVFQRGLAISDNGPCLGYRKPNQ------------------PYRW 105
Cdd:PLN02387 27 RGVPVDVGGEPGYAIRNArfpELVETPWEGATTLAALFEQSCKKYSDKRLLGTRKLISrefetssdgrkfeklhlgEYEW 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYKSspDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVIC 185
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNK--EERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVIC 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 DTPQ--KASVLIENVEkgftpSLKVVILMDPFDDDLKQRGEK-SGIEILSLYDAENLGKEHFRKPVPPSPEDLSIICFTS 262
Cdd:PLN02387 185 DSKQlkKLIDISSQLE-----TVKRVIYMDDEGVDSDSSLSGsSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 263 GTTGDPKGAMITHQNIVSNASAFLKCVEhtfEPTPDDVTISYLPLAHMFERVVQTVVYCCGARVGFfqGNIRLLAD---- 338
Cdd:PLN02387 260 GSTGLPKGVMMTHGNIVATVAGVMTVVP---KLGKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDtsnk 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 339 -------DMNTLKPTLFPTVPRVLNRIYDKVQN--EAKTPLKKFLLNLAVASKFKELQK------GIIRrdSFWDKLIFA 403
Cdd:PLN02387 335 ikkgtkgDASALKPTLMTAVPAILDRVRDGVRKkvDAKGGLAKKLFDIAYKRRLAAIEGswfgawGLEK--LLWDALVFK 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 404 KIQASLGGRVRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTSPGDWTSGHVGAPLTCNYVKLEDVADMD 483
Cdd:PLN02387 413 KIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGG 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 484 YFSVNN---EGEICIKGTNVFKGYLKDPEKTQEA--LDSDG--WLHTGDIGRWLPNGTLKIIDRKKNIFKLAQGEYIAPE 556
Cdd:PLN02387 493 YLISDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLG 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 557 KIENIYNRSRPVLQIFVHGESLRSSLVGVVVPDPDVLPSFAAKLGVK-GSFEELCQNQVVRKAILEDLQKIGKESGLKTF 635
Cdd:PLN02387 573 KVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKF 652
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1622967304 636 EQVKAVFLHPEPFSIENGLLTPTLKAKRGELSKYFRTQIDSLYE 679
Cdd:PLN02387 653 EIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
104-679 |
2.25e-106 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 338.49 E-value: 2.25e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 104 RWLSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMV 183
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLAELGLT--KGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 184 ICDTpQKASVLIENVEKGFTPSLKVVILmdpfdDDLKQRGEKSGIEILSLYDAENLGKE---HFRKPVPPSPEDLSIICF 260
Cdd:PTZ00216 198 VCNG-KNVPNLLRLMKSGGMPNTTIIYL-----DSLPASVDTEGCRLVAWTDVVAKGHSagsHHPLNIPENNDDLALIMY 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 261 TSGTTGDPKGAMITHQNIVSNASAflkcVEHTF-----EPTPDDVTISYLPLAHMFERVVQTVVYCCGARVGFfqGNIRL 335
Cdd:PTZ00216 272 TSGTTGDPKGVMHTHGSLTAGILA----LEDRLndligPPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRT 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 336 LAD-------DMNTLKPTLFPTVPRVLNRIYDKVqnEAKTP----LKKFLLNLAVASKFKELQKGiirRDS-FWDKLIFA 403
Cdd:PTZ00216 346 LTDtfarphgDLTEFRPVFLIGVPRIFDTIKKAV--EAKLPpvgsLKRRVFDHAYQSRLRALKEG---KDTpYWNEKVFS 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 404 KIQASLGGRVRIIVTGAAPISAPVMTFFRAAMGCqVYEAYGQTE--CTAGCTFTspGDWTSGHVGAPLTCNYVKLEDVad 481
Cdd:PTZ00216 421 APRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTEtvCCGGIQRT--GDLEPNAVGQLLKGVEMKLLDT-- 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 482 mDYFSVNNE----GEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAQGEYIAPEK 557
Cdd:PTZ00216 496 -EEYKHTDTpeprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEA 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 558 IENIYNrSRPVLQ-----IFVHgeSLRSSLVGVVVPDPDVLPSFAAKLGVKGSFEELCQNQVVRKAILEDLQKIGKESGL 632
Cdd:PTZ00216 575 LEALYG-QNELVVpngvcVLVH--PARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGR 651
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1622967304 633 KTFEQVKAVFLHPEPFSIENGLLTPTLKAKRGELSKYFRTQIDSLYE 679
Cdd:PTZ00216 652 KSFEIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELFA 698
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
106-670 |
1.89e-80 |
|
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: 264.72 E-value: 1.89e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVIC 185
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLE--PGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 ----DTPQKASVLIENVEKGFTPSLKVVILMDPFDDDLKQrgeksgieilslydAENLGKEhfrkpVPPSPEDLSIICFT 261
Cdd:cd05932 85 gkldDWKAMAPGVPEGLISISLPPPSAANCQYQWDDLIAQ--------------HPPLEER-----PTRFPEQLATLIYT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 262 SGTTGDPKGAMITHQNIVSNASAFLKcvehTFEPTPDDVTISYLPLAHMFERVVQTVVYCCGARVGFFQGNIRLLADDMN 341
Cdd:cd05932 146 SGTTGQPKGVMLTFGSFAWAAQAGIE----HIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTFVEDVQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 342 TLKPTLFPTVPRVLNRIYDKVQNeaKTPLKKF--LLNLAVASKfkelqkgIIRRdsfwdklifaKIQASLG-GRVRIIVT 418
Cdd:cd05932 222 RARPTLFFSVPRLWTKFQQGVQD--KIPQQKLnlLLKIPVVNS-------LVKR----------KVLKGLGlDQCRLAGC 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 419 GAAPISAPVMTFFRAaMGCQVYEAYGQTECTAGCTFTSPGDWTSGHVGAPLTCNYVKLEDvadmdyfsvnnEGEICIKGT 498
Cdd:cd05932 283 GSAPVPPALLEWYRS-LGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEILVRSP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 499 NVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAQGEYIAPEKIENIYNRSRPVLQIFVHGESL 578
Cdd:cd05932 351 ALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSGL 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 579 RSSLVgvvvpdpdvlpsfaakLGVKGSFEELCQNQVVRKAILEDLQKI--GKESGLKTFEQVKAVFLHPEPFSIENGLLT 656
Cdd:cd05932 431 PAPLA----------------LVVLSEEARLRADAFARAELEASLRAHlaRVNSTLDSHEQLAGIVVVKDPWSIDNGILT 494
|
570
....*....|....
gi 1622967304 657 PTLKAKRGELSKYF 670
Cdd:cd05932 495 PTLKIKRNVLEKAY 508
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
101-663 |
3.83e-80 |
|
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: 262.68 E-value: 3.83e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 101 QPYRWLSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADI 180
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVK--AGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 181 AMVIcdtpqkasvlIENvekgftpslkvvilmdpfdddlkqrgeksgieilslydaenlgkehfrkpvppSPEDLSIICF 260
Cdd:cd17640 79 VALV----------VEN-----------------------------------------------------DSDDLATIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 261 TSGTTGDPKGAMITHQNIVSNASAFLKCVEhtfePTPDDVTISYLPLAHMFERVVQTVVYCCGARVGFfqGNIRLLADDM 340
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLLHQIRSLSDIVP----PQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDDL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 341 NTLKPTLFPTVPRVLNRIYDKVQNE--AKTPLKKFLLNLAVaskfkelqkgiirrdsfwdklifakiqasLGGRVRIIVT 418
Cdd:cd17640 170 KRVKPHYIVSVPRLWESLYSGIQKQvsKSSPIKQFLFLFFL-----------------------------SGGIFKFGIS 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 419 GAAPISAPVMTFFRAAmGCQVYEAYGQTECTAGCTFTSPGDWTSGHVGAPLTCNYVKLEDVADMDYFSVNNEGEICIKGT 498
Cdd:cd17640 221 GGGALPPHVDTFFEAI-GIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGP 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 499 NVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAQGEYIAPEKIENIYNRSRPVLQIFVHGESL 578
Cdd:cd17640 300 QVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQ 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 579 RsSLVGVVVPDPDVLPSFAAKLGVK--GSFEELCQNQVVRKAI-LEDLQKIGKESGLKTFEQVKAVFLHPEPFsIENGLL 655
Cdd:cd17640 380 K-RLGALIVPNFEELEKWAKESGVKlaNDRSQLLASKKVLKLYkNEIKDEISNRPGFKSFEQIAPFALLEEPF-IENGEM 457
|
....*...
gi 1622967304 656 TPTLKAKR 663
Cdd:cd17640 458 TQTMKIKR 465
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
106-663 |
5.92e-70 |
|
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: 235.41 E-value: 5.92e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVIC 185
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVG--TGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 DtpqkasvlienvekgftpslkvvilmdpfdddlkqrgeksgieilslydaenlgkehfrkpvppSPEDLSIICFTSGTT 265
Cdd:cd05914 86 S----------------------------------------------------------------DEDDVALINYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 266 GDPKGAMITHQNIVSNASAflkcVEHTFEPTPDDVTISYLPLAHMFErVVQTVVY--CCGARVgFFQGNI---RLLADDM 340
Cdd:cd05914 102 GNSKGVMLTYRNIVSNVDG----VKEVVLLGKGDKILSILPLHHIYP-LTFTLLLplLNGAHV-VFLDKIpsaKIIALAF 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 341 NTLKPTLFPTVPRVLNRIYdkvqneaktplKKFLLNLAVASKFKELQKGIIRRDSFWdKLIFAKIQASLGGRVRIIVTGA 420
Cdd:cd05914 176 AQVTPTLGVPVPLVIEKIF-----------KMDIIPKLTLKKFKFKLAKKINNRKIR-KLAFKKVHEAFGGNIKEFVIGG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 421 APISAPVMTFFRAaMGCQVYEAYGQTECTAGCTFTSPGDWTSGHVGAPLtcnyvKLEDVADMDYFSVNNEGEICIKGTNV 500
Cdd:cd05914 244 AKINPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVI-----DGVEVRIDSPDPATGEGEIIVRGPNV 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 501 FKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAQGEYIAPEKIENIYNRSRPVLqifvhgESLRS 580
Cdd:cd05914 318 MKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVL------ESLVV 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 581 SLVGVVVPDPDVLPSFAAKLGVKgsfeelcqNQVVRKAILED-LQKIGKEsgLKTFEQVKAVFLHPEPFSienglLTPTL 659
Cdd:cd05914 392 VQEKKLVALAYIDPDFLDVKALK--------QRNIIDAIKWEvRDKVNQK--VPNYKKISKVKIVKEEFE-----KTPKG 456
|
....
gi 1622967304 660 KAKR 663
Cdd:cd05914 457 KIKR 460
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
103-560 |
7.79e-69 |
|
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: 235.39 E-value: 7.79e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 103 YRWLSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAM 182
Cdd:cd17641 9 WQEFTWADYADRVRAFALGLLALGVG--RGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 183 VICDTPQKASVLIENVEKgfTPSLKVVILMDP-----FDDDlkqrgeksgiEILSLYDAENLGKEHFRKPvpP------- 250
Cdd:cd17641 87 VIAEDEEQVDKLLEIADR--IPSVRYVIYCDPrgmrkYDDP----------RLISFEDVVALGRALDRRD--Pglyerev 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 251 ---SPEDLSIICFTSGTTGDPKGAMITHQNIVSNASAFLKcvehtFEP-TPDDVTISYLPLAHMFER---VVQTVVycCG 323
Cdd:cd17641 153 aagKGEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLA-----ADPlGPGDEYVSVLPLPWIGEQmysVGQALV--CG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 324 ARVGFFQGNIRLLADdMNTLKPTLFPTVPRVLNRIYDKVQN--EAKTPLKKFLLNL-------AVASKFKELQKGIIRRD 394
Cdd:cd17641 226 FIVNFPEEPETMMED-LREIGPTFVLLPPRVWEGIAADVRArmMDATPFKRFMFELgmklglrALDRGKRGRPVSLWLRL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 395 SFW--DKLIFAKIQASLG-GRVRIIVTGAAPISAPVMTFFRAaMGCQVYEAYGQTEcTAGCTFTSP-GDWTSGHVGAPLT 470
Cdd:cd17641 305 ASWlaDALLFRPLRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTE-LAGAYTVHRdGDVDPDTVGVPFP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 471 CNYVKledvadmdyfsVNNEGEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAQG 550
Cdd:cd17641 383 GTEVR-----------IDEVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDG 451
|
490
....*....|
gi 1622967304 551 EYIAPEKIEN 560
Cdd:cd17641 452 TRFSPQFIEN 461
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
98-678 |
1.44e-68 |
|
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: 235.33 E-value: 1.44e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 98 KPNQPYRWLSYKQVSDRAEYLGSCLLHKGYksspDQF--VGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIV 175
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLKLGL----ERFhgVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 176 N--KADIAMVicDTPQKASVLIEnvEKGFTPSLKVVI-LMDPFDDdlKQRGEKSGIEILSLYDAENLGKEHFRKPVPpSP 252
Cdd:cd05933 77 EtsEANILVV--ENQKQLQKILQ--IQDKLPHLKAIIqYKEPLKE--KEPNLYSWDEFMELGRSIPDEQLDAIISSQ-KP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 253 EDLSIICFTSGTTGDPKGAMITHQNIVSNASAFLKCVEHTFEPTPDDVTISYLPLAHMferVVQTV-VYCC---GARVGF 328
Cdd:cd05933 150 NQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHI---AAQILdIWLPikvGGQVYF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 329 FQGNiRLLADDMNTLK---PTLFPTVPRVLNRIYDKVQ-NEAK-TPLKKFLLNLAVASKFK---ELQKGIIRRDSFW--- 397
Cdd:cd05933 227 AQPD-ALKGTLVKTLRevrPTAFMGVPRVWEKIQEKMKaVGAKsGTLKRKIASWAKGVGLEtnlKLMGGESPSPLFYrla 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 398 DKLIFAKIQASLG-GRVRIIVTGAAPISAPVMTFFrAAMGCQVYEAYGQTECTAGCTFTSPGDWTSGHVGAPLTCNYVKL 476
Cdd:cd05933 306 KKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 477 EDVADmdyfsvNNEGEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAQGEYIAPE 556
Cdd:cd05933 385 HNPDA------DGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPV 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 557 KIENIYNRSRPVLQ-IFVHGE---------SLRSSLVGVVVPDPDVLPS----FAAKLGVKGS-FEELC--QNQVVRKAI 619
Cdd:cd05933 459 PIEDAVKKELPIISnAMLIGDkrkflsmllTLKCEVNPETGEPLDELTEeaieFCRKLGSQATrVSEIAggKDPKVYEAI 538
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622967304 620 LEDLQKIGKESGLKTFEQVKAVFLhPEPFSIENGLLTPTLKAKRGELSKYFRTQIDSLY 678
Cdd:cd05933 539 EEGIKRVNKKAISNAQKIQKWVIL-EKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
104-561 |
2.64e-66 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 225.07 E-value: 2.64e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 104 RWLSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMV 183
Cdd:COG0318 23 RRLTYAELDARARRLAAALRALGVG--PGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 184 ICdtpqkasvlienvekgftpslkvvilmdpfdddlkqrgeksgieilslydaenlgkehfrkpvppspedlSIICFTSG 263
Cdd:COG0318 101 VT----------------------------------------------------------------------ALILYTSG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 264 TTGDPKGAMITHQNIVSNASAFLkcveHTFEPTPDDVTISYLPLAHMFERVVQTVVY-CCGARV----GFfqgNIRLLAD 338
Cdd:COG0318 111 TTGRPKGVMLTHRNLLANAAAIA----AALGLTPGDVVLVALPLFHVFGLTVGLLAPlLAGATLvllpRF---DPERVLE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 339 DMNTLKPTLFPTVPRVLNRiydkvqneaktplkkfLLNLAVASKFKelqkgiirrdsfwdkliFAkiqaslggRVRIIVT 418
Cdd:COG0318 184 LIERERVTVLFGVPTMLAR----------------LLRHPEFARYD-----------------LS--------SLRLVVS 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 419 GAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTSPGDWTS--GHVGAPLTCNYVKLEDVADMDyFSVNNEGEICIK 496
Cdd:COG0318 223 GGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGRPLPGVEVRIVDEDGRE-LPPGEVGEIVVR 301
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622967304 497 GTNVFKGYLKDPEKTQEALDsDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENI 561
Cdd:COG0318 302 GPNVMKGYWNDPEATAEAFR-DGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEV 364
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
106-656 |
5.10e-66 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 228.11 E-value: 5.10e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGScLLHKGYKSSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVIC 185
Cdd:cd17632 68 ITYAELWERVGAVAA-AHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 DTPQKAsVLIENVEKGFTPSLKVVILMDPFDDDLKQ-----RGEKSGIEILSLYDAENLGKEHFRKPVPPSPED-----L 255
Cdd:cd17632 147 SAEHLD-LAVEAVLEGGTPPRLVVFDHRPEVDAHRAalesaRERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEpdddpL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 256 SIICFTSGTTGDPKGAMITHQNIvsnASAFLKcVEHTFEPTPDD-VTISYLPLAHMFERVVQTVVYCCGArVGFFQGnir 334
Cdd:cd17632 226 ALLIYTSGSTGTPKGAMYTERLV---ATFWLK-VSSIQDIRPPAsITLNFMPMSHIAGRISLYGTLARGG-TAYFAA--- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 335 llADDMNTL-------KPTLFPTVPRVLNRIYDKVQNEaktpLKKFLLNLAVASKFKELQKGIIRRDSfwdklifakiqa 407
Cdd:cd17632 298 --ASDMSTLfddlalvRPTELFLVPRVCDMLFQRYQAE----LDRRSVAGADAETLAERVKAELRERV------------ 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 408 sLGGRVRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTEctAGCTFTSpgdwtsGHVGAPLTCNYvKLEDVADMDYFSV 487
Cdd:cd17632 360 -LGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE--AGAVILD------GVIVRPPVLDY-KLVDVPELGYFRT 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 488 NN---EGEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAQGEYIAPEKIENIYNR 564
Cdd:cd17632 430 DRphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFAA 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 565 SRPVLQIFVHGESLRSSLvgvvvpDPDVLPSFAAKLGVkgsfeelcQNQVVRKAILEDLQKIGKESGLKTFEQVKAVFLH 644
Cdd:cd17632 510 SPLVRQIFVYGNSERAYL------LAVVVPTQDALAGE--------DTARLRAALAESLQRIAREAGLQSYEIPRDFLIE 575
|
570
....*....|..
gi 1622967304 645 PEPFSIENGLLT 656
Cdd:cd17632 576 TEPFTIANGLLS 587
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
254-575 |
4.13e-61 |
|
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: 207.52 E-value: 4.13e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 254 DLSIICFTSGTTGDPKGAMITHQNIVSNASAFLkcveHTFEPTPDDVTISYLPLAHMFERVVQTVVYCCGARVGFFQG-N 332
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALA----ASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKfD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 333 IRLLADDMNTLKPTLFPTVPRVLNRIyDKVQNEAKTPLkkfllnlavaskfkelqkgiirrdsfwdklifakiqASLggr 412
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTLLARL-LKAPESAGYDL------------------------------------SSL--- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 413 vRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTSPGDWT--SGHVGAPLTCNYVKLEDVADmDYFSVNNE 490
Cdd:cd04433 117 -RALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDPDG-GELPPGEI 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 491 GEICIKGTNVFKGYLKDPEKTQEALDsDGWLHTGDIGRWLPNGTLKIIDRKKNIFKlAQGEYIAPEKIENIYNRSRPVLQ 570
Cdd:cd04433 195 GELVVRGPSVMKGYWNNPEATAAVDE-DGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPGVAE 272
|
....*
gi 1622967304 571 IFVHG 575
Cdd:cd04433 273 AAVVG 277
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
104-576 |
1.50e-55 |
|
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: 196.63 E-value: 1.50e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 104 RWLSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIamv 183
Cdd:cd05936 23 RKLTYRELDALAEAFAAGLQNLGVQ--PGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGA--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 184 icdtpqkasvlienvekgftpslKVVILMDPFDDDLKQrGEKSGieilslydaenlgkehfrKPVPPSPEDLSIICFTSG 263
Cdd:cd05936 98 -----------------------KALIVAVSFTDLLAA-GAPLG------------------ERVALTPEDVAVLQYTSG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 264 TTGDPKGAMITHQNIVSNASAflkCVEHTFEP-TPDDVTISYLPLAHMFErvvQTVVYCCGARVGFFQ------GNIRLL 336
Cdd:cd05936 136 TTGVPKGAMLTHRNLVANALQ---IKAWLEDLlEGDDVVLAALPLFHVFG---LTVALLLPLALGATIvliprfRPIGVL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 337 aDDMNTLKPTLFPTVPRVLNRIydkVQNEAKtplKKFLLNlavaskfkelqkgiirrdsfwdklifakiqaslggRVRII 416
Cdd:cd05936 210 -KEIRKHRVTIFPGVPTMYIAL---LNAPEF---KKRDFS-----------------------------------SLRLC 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 417 VTGAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTSPGDWT-SGHVGAPLTCNYVKLEDvADMDYFSVNNEGEICI 495
Cdd:cd05936 248 ISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRkPGSIGIPLPGTEVKIVD-DDGEELPPGEVGELWV 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 496 KGTNVFKGYLKDPEKTQEALDsDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENIYNRSRPVLQIFVHG 575
Cdd:cd05936 327 RGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGGFNVYPREVEEVLYEHPAVAEAAVVG 404
|
.
gi 1622967304 576 E 576
Cdd:cd05936 405 V 405
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
106-545 |
7.85e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 192.81 E-value: 7.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVIC 185
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIG--KGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 dtpqkASVLIENVEKG--FTPSLKVVILMDPFDDDLKQRGEKSGIEILSLydaenlGKEHFRKPvPPSPEDLSIICFTSG 263
Cdd:PRK07656 109 -----LGLFLGVDYSAttRLPALEHVVICETEEDDPHTEKMKTFTDFLAA------GDPAERAP-EVDPDDVADILFTSG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 264 TTGDPKGAMITHQNIVSNASAFLKCvehtFEPTPDDVTISYLPLAHMFervvqtvvyccGARVGffqgnirLLADDMN-- 341
Cdd:PRK07656 177 TTGRPKGAMLTHRQLLSNAADWAEY----LGLTEGDRYLAANPFFHVF-----------GYKAG-------VNAPLMRga 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 342 TLKPTLFPTVPRVLNRIydkvQNEAKT-----P-LKKFLLNLAVASKFKelqkgiirrdsfwdklifakiQASLggrvRI 415
Cdd:PRK07656 235 TILPLPVFDPDEVFRLI----ETERITvlpgpPtMYNSLLQHPDRSAED---------------------LSSL----RL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 416 IVTGAAPISAPVMTFFRAAMGCQ-VYEAYGQTECTAGCTFTSPGD---WTSGHVGAPltCNYVKLEDVADMDYFSVNNE- 490
Cdd:PRK07656 286 AVTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTA--IAGVENKIVNELGEEVPVGEv 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1622967304 491 GEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIF 545
Cdd:PRK07656 364 GELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF 418
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
106-561 |
5.69e-53 |
|
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: 190.12 E-value: 5.69e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVIC 185
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLK--KGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 DTPQKASVLieNVEKGFTPSLKVvILMDPFDDDLkqrgeksgIEILSLYDAENLGKEHFRKPVPP-SPEDLSIICFTSGT 264
Cdd:cd05911 89 DPDGLEKVK--EAAKELGPKDKI-IVLDDKPDGV--------LSIEDLLSPTLGEEDEDLPPPLKdGKDDTAAILYSSGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 265 TGDPKGAMITHQNIVSNasaFLKCVEHTFEPT-PDDVTISYLPLAHMFErvVQTVVYC--CGARV----GFFqgnIRLLA 337
Cdd:cd05911 158 TGLPKGVCLSHRNLIAN---LSQVQTFLYGNDgSNDVILGFLPLYHIYG--LFTTLASllNGATViimpKFD---SELFL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 338 DDMNTLKPTLFPTVPRVLNRIydkvqneAKTP-LKKFLLnlavaskfkelqkgiirrdsfwdklifakiqASLggrvRII 416
Cdd:cd05911 230 DLIEKYKITFLYLVPPIAAAL-------AKSPlLDKYDL-------------------------------SSL----RVI 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 417 VTGAAPISAPVMTFFRA-AMGCQVYEAYGQTECTAGCTFTSPGDWTSGHVGAPLTcNY-VKLEDVADMDYFSVNNEGEIC 494
Cdd:cd05911 268 LSGGAPLSKELQELLAKrFPNATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLP-NVeAKIVDDDGKDSLGPNEPGEIC 346
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622967304 495 IKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIENI 561
Cdd:cd05911 347 VRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAV 412
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
107-561 |
9.14e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 176.15 E-value: 9.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 107 SYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACytySM---VAVPLYDTLGPEAIVYIVNKADIAMV 183
Cdd:PRK06187 33 TYAELDERVNRLANALRALGVK--KGDRVAVFDWNSHEYLEAYFAV---PKigaVLHPINIRLKPEEIAYILNDAEDRVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 184 ICDtpqkASV--LIENVeKGFTPSLKVVILMDpfDDDLKQRGEKSGiEILSLYDAENlgkEHFRKPvPPSPEDLSIICFT 261
Cdd:PRK06187 108 LVD----SEFvpLLAAI-LPQLPTVRTVIVEG--DGPAAPLAPEVG-EYEELLAAAS---DTFDFP-DIDENDAAAMLYT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 262 SGTTGDPKGAMITHQNIVSNASAflkcVEHTFEPTPDDVTISYLPLAHMFERVVQTVVYCCGAR---VGFFQgnIRLLAD 338
Cdd:PRK06187 176 SGTTGHPKGVVLSHRNLFLHSLA----VCAWLKLSRDDVYLVIVPMFHVHAWGLPYLALMAGAKqviPRRFD--PENLLD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 339 DMNTLKPTLFPTVPRVLNriydkvqneaktplkkFLLNlAVASKFKELQkgiirrdsfwdklifakiqaslggRVRIIVT 418
Cdd:PRK06187 250 LIETERVTFFFAVPTIWQ----------------MLLK-APRAYFVDFS------------------------SLRLVIY 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 419 GAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTSPGDWTSGH------VGAPLTCNYVKLEDvADMDYFSVNNE-- 490
Cdd:PRK06187 289 GGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVLPPEDQLPGQwtkrrsAGRPLPGVEARIVD-DDGDELPPDGGev 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622967304 491 GEICIKGTNVFKGYLKDPEKTQEALDsDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENI 561
Cdd:PRK06187 368 GEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIKDVIISG-GENIYPRELEDA 436
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
106-561 |
4.44e-42 |
|
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: 159.42 E-value: 4.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVsdraeYLGSCLLHKGYK--SSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMV 183
Cdd:cd05909 8 LTYRKL-----LTGAIALARKLAkmTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 184 IcdtpqKASVLIE--NVEKGFTPSLKVVILmdpFDDDLKQR---GEKSGIEILSLYDAENLGKEHFRKPVppSPEDLSII 258
Cdd:cd05909 83 L-----TSKQFIEklKLHHLFDVEYDARIV---YLEDLRAKiskADKCKAFLAGKFPPKWLLRIFGVAPV--QPDDPAVI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 259 CFTSGTTGDPKGAMITHQNIVSNASAFLKCvehtFEPTPDDVTISYLPLAHMFERVVQTVV-YCCGARVgFFQGNirlla 337
Cdd:cd05909 153 LFTSGSEGLPKGVVLSHKNLLANVEQITAI----FDPNPEDVVFGALPFFHSFGLTGCLWLpLLSGIKV-VFHPN----- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 338 ddmntlkPTLFPTVPRVlnrIYD-KVQNEAKTPLkkFLlnlavaskfkelqKGIIRRdsfWDKLIFAkiqaslggRVRII 416
Cdd:cd05909 223 -------PLDYKKIPEL---IYDkKATILLGTPT--FL-------------RGYARA---AHPEDFS--------SLRLV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 417 VTGAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTSPG-DWTSGHVGAPLTCNYVKLEDVADMDYFSVNNEGEICI 495
Cdd:cd05909 267 VAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLV 346
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622967304 496 KGTNVFKGYLKDPEKTQEALdSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENI 561
Cdd:cd05909 347 RGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDI 410
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
106-560 |
7.67e-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: 7.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADiamvic 185
Cdd:cd17631 21 LTYAELDERVNRLAHALRALGVA--KGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSG------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 dtpqkASVLIEnvekgftpslkvvilmdpfdddlkqrgeksgieilslydaenlgkehfrkpvppspeDLSIICFTSGTT 265
Cdd:cd17631 93 -----AKVLFD---------------------------------------------------------DLALLMYTSGTT 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 266 GDPKGAMITHQNIVSNASAFLkcveHTFEPTPDDVTISYLPLAHmferVVQTVVYCC-----GARV----GFFQGNI-RL 335
Cdd:cd17631 111 GRPKGAMLTHRNLLWNAVNAL----AALDLGPDDVLLVVAPLFH----IGGLGVFTLptllrGGTVvilrKFDPETVlDL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 336 LADDmntlKPTLFPTVPRVLNriydkvqneaktplkkFLLNLAVASKfkelqkgiiRRDSfwdklifakiqaslggRVRI 415
Cdd:cd17631 183 IERH----RVTSFFLVPTMIQ----------------ALLQHPRFAT---------TDLS----------------SLRA 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 416 IVTGAAPISAPVMTFFRAAmGCQVYEAYGQTECTAGCTFTSPGDWTS--GHVGAPLTCNYVKLEDvADMDYFSVNNEGEI 493
Cdd:cd17631 218 VIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHRRklGSAGRPVFFVEVRIVD-PDGREVPPGEVGEI 295
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622967304 494 CIKGTNVFKGYLKDPEKTQEALDsDGWLHTGDIGRWLPNGTLKIIDRKKNIFKlAQGEYIAPEKIEN 560
Cdd:cd17631 296 VVRGPHVMAGYWNRPEATAAAFR-DGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVED 360
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
190-561 |
1.34e-41 |
|
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: 158.55 E-value: 1.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 190 KASVLI---ENVEKgfTPSLKV-VILMDPFDDDLkqrgeksgieiLSLYDAENLGKEHFRKPVPPSPEDLSIICFTSGTT 265
Cdd:cd05904 104 GAKLAFttaELAEK--LASLALpVVLLDSAEFDS-----------LSFSDLLFEADEAEPPVVVIKQDDVAALLYSSGTT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 266 GDPKGAMITHQNIVSNASAFLKCVEHTFEPtpDDVTISYLPLAHMFERvvqTVVYCCGARVG--------FfqgNIRLLA 337
Cdd:cd05904 171 GRSKGVMLTHRNLIAMVAQFVAGEGSNSDS--EDVFLCVLPMFHIYGL---SSFALGLLRLGatvvvmprF---DLEELL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 338 DDMNTLKPTLFPTVPRVLnriydkvqneaktplkkflLNLAVASKFKELQKgiirrdsfwdklifakiqASLggrvRIIV 417
Cdd:cd05904 243 AAIERYKVTHLPVVPPIV-------------------LALVKSPIVDKYDL------------------SSL----RQIM 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 418 TGAAPISAPVMTFFRAAM-GCQVYEAYGQTECTAGCTFTSPGDWTSGHVG-----APLTCnyVKLEDVADMDYFSVNNEG 491
Cdd:cd05904 282 SGAAPLGKELIEAFRAKFpNVDLGQGYGMTESTGVVAMCFAPEKDRAKYGsvgrlVPNVE--AKIVDPETGESLPPNQTG 359
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 492 EICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIENI 561
Cdd:cd05904 360 ELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEAL 428
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
218-562 |
5.07e-40 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 157.19 E-value: 5.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 218 DLKQRGEKSGIEILSLYDAENLGKEHFrKPVPPSPEDLSIICFTSGTTGDPKGAMITHQNI------VSNASAFLKcveh 291
Cdd:PTZ00342 270 DLKEKAKKLGISIILFDDMTKNKTTNY-KIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLyntvvpLCKHSIFKK---- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 292 tFEPtpdDVTISYLPLAHMFERVVQTVVYCCGARVGFFQGNIRLLADDMNTLKPTLFPTVPRVLNRIYDKVQNEAK--TP 369
Cdd:PTZ00342 345 -YNP---KTHLSYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINnlPP 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 370 LKKFLLNLAVA----------SKFKELQKGIIRRdsfwdklIFAKIQASLggrvRIIVTGAAPISAPVMTFFRAAMGCQV 439
Cdd:PTZ00342 421 LKRFLVKKILSlrksnnnggfSKFLEGITHISSK-------IKDKVNPNL----EVILNGGGKLSPKIAEELSVLLNVNY 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 440 YEAYGQTECTAGCTFTSPGDWTSGHVGAPLTCNyVKLEDVADMDYFSVNN--EGEICIKGTNVFKGYLKDPEKTQEALDS 517
Cdd:PTZ00342 490 YQGYGLTETTGPIFVQHADDNNTESIGGPISPN-TKYKVRTWETYKATDTlpKGELLIKSDSIFSGYFLEKEQTKNAFTE 568
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1622967304 518 DGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAQGEYIAPEKIENIY 562
Cdd:PTZ00342 569 DGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLY 613
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
106-560 |
7.13e-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: 152.06 E-value: 7.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQ-VSDRAEYlgSCLLHKGYKSSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVI 184
Cdd:cd05941 12 ITYADlVARAARL--ANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 185 cdtpqkasvlienvekgftpslkvvilmdpfdddlkqrgeksgieilslydaenlgkehfrkpvppspeDLSIICFTSGT 264
Cdd:cd05941 90 ---------------------------------------------------------------------DPALILYTSGT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 265 TGDPKGAMITHQNIVSNasafLKCVEHTFEPTPDDVTISYLPLAHMFERVVqtVVYC---CGARV---GFFQGNIRLLAD 338
Cdd:cd05941 101 TGRPKGVVLTHANLAAN----VRALVDAWRWTEDDVLLHVLPLHHVHGLVN--ALLCplfAGASVeflPKFDPKEVAISR 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 339 DMNTLkpTLFPTVPRVLNRIYDkvqneaktplkkfllnlAVASKFKELQKgiIRRDSFwdklifakiqaslgGRVRIIVT 418
Cdd:cd05941 175 LMPSI--TVFMGVPTIYTRLLQ-----------------YYEAHFTDPQF--ARAAAA--------------ERLRLMVS 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 419 GAAPISAPVMTFFRAAMGCQVYEAYGQTEctAGCTFTSP--GDWTSGHVGAPLTCNYVKLEDVADMDYFSVNNEGEICIK 496
Cdd:cd05941 220 GSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVR 297
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622967304 497 GTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKK-NIFKlAQGEYIAPEKIEN 560
Cdd:cd05941 298 GPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEIER 361
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
108-573 |
4.14e-38 |
|
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: 147.21 E-value: 4.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 108 YKQVSDRAEYLGSCLLHKGyksspdQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVICDt 187
Cdd:TIGR01923 6 DCEAAHLAKALKAQGIRSG------SRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 188 pqkasvlienvekgftpslkvvilmDPFdddlkqrgEKSGIEILSLYDAENLGKEHFRKPVPPSPEDLSIICFTSGTTGD 267
Cdd:TIGR01923 79 -------------------------SLL--------EEKDFQADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 268 PKGAMITHQNIVSNASAflkcVEHTFEPTPDDVTISYLPLAHM--FERVVQTVVYCCGARV--GFFQgnirlLADDMNTL 343
Cdd:TIGR01923 126 PKAVPHTFRNHYASAVG----SKENLGFTEDDNWLLSLPLYHIsgLSILFRWLIEGATLRIvdKFNQ-----LLEMIANE 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 344 KPTLFPTVPRVLNRIYDKVQNEakTPLKKFLLnlavaskfkelqkgiirrdsfwdklifakiqaslggrvriivtGAAPI 423
Cdd:TIGR01923 197 RVTHISLVPTQLNRLLDEGGHN--ENLRKILL-------------------------------------------GGSAI 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 424 SAPVMtffRAAM--GCQVYEAYGQTE-CTAGCTFTSPGDWTSGHVGAPLTCNYVKLEdVADMDyfsvnNEGEICIKGTNV 500
Cdd:TIGR01923 232 PAPLI---EEAQqyGLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIK-VDNKE-----GHGEIMVKGANL 302
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622967304 501 FKGYLkDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENIYNRSRPVLQIFV 573
Cdd:TIGR01923 303 MKGYL-YQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVV 373
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
105-570 |
1.30e-36 |
|
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: 143.99 E-value: 1.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 105 WLSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVI 184
Cdd:cd05926 14 ALTYADLAELVDDLARQLAALGIK--KGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 185 CDtpqkasvlienvEKGFTPSLKVVILMDPFDDDLkqrGEKSGIEILSLyDAENLGKEHFRKPV-----PPSPEDLSIIC 259
Cdd:cd05926 92 TP------------KGELGPASRAASKLGLAILEL---ALDVGVLIRAP-SAESLSNLLADKKNaksegVPLPDDLALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 260 FTSGTTGDPKGAMITHQNIVSNASAflkcVEHTFEPTPDDVTISYLPLAHMFERVVQ--TVVYCCGARV--------GFF 329
Cdd:cd05926 156 HTSGTTGRPKGVPLTHRNLAASATN----ITNTYKLTPDDRTLVVMPLFHVHGLVASllSTLAAGGSVVlpprfsasTFW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 330 QgnirlladDMNTLKPTLFPTVPRVLnriydkvqneaktplkKFLLNLAVASKFKELQKgiirrdsfwdklifakiqasl 409
Cdd:cd05926 232 P--------DVRDYNATWYTAVPTIH----------------QILLNRPEPNPESPPPK--------------------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 410 ggrVRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTEcTAGCTFTSP---GDWTSGHVGAPltcNYVKLEDV-ADMDYF 485
Cdd:cd05926 267 ---LRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTE-AAHQMTSNPlppGPRKPGSVGKP---VGVEVRILdEDGEIL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 486 SVNNEGEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENIYNRS 565
Cdd:cd05926 340 PPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVLLSH 418
|
....*
gi 1622967304 566 RPVLQ 570
Cdd:cd05926 419 PAVLE 423
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
108-561 |
1.12e-35 |
|
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: 141.90 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 108 YKQVSDR--------------AEYL-GSCLLH---KGYKSSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPE 169
Cdd:cd17642 27 YASVPGTiaftdahtgvnysyAEYLeMSVRLAealKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNER 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 170 AIVYIVNKADIAMVICD--TPQKasvlIENVEKGFtPSLKVVILMDPFDDdlkQRGEKSGIEILSLYDAENLGKEHFRKP 247
Cdd:cd17642 107 ELDHSLNISKPTIVFCSkkGLQK----VLNVQKKL-KIIKTIIILDSKED---YKGYQCLYTFITQNLPPGFNEYDFKPP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 248 VPPSPEDLSIICFTSGTTGDPKGAMITHQNIVSNasaFLKCVEHTF--EPTPDDVTISYLPLAHMFERVVQTVVYCCGAR 325
Cdd:cd17642 179 SFDRDEQVALIMNSSGSTGLPKGVQLTHKNIVAR---FSHARDPIFgnQIIPDTAILTVIPFHHGFGMFTTLGYLICGFR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 326 VGFfqgnirlladdMNTLKPTLFptvprvLNRIYD-KVQNEAKTP-LKKFLLNLAVASKFkELQKgiirrdsfwdklifa 403
Cdd:cd17642 256 VVL-----------MYKFEEELF------LRSLQDyKVQSALLVPtLFAFFAKSTLVDKY-DLSN--------------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 404 kiqaslggrVRIIVTGAAPISAPVMTFFRAAMGCQ-VYEAYGQTECTAGCTFTSPGDWTSGHVGAPLTCNYVKLEDVADM 482
Cdd:cd17642 303 ---------LHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTG 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622967304 483 DYFSVNNEGEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIENI 561
Cdd:cd17642 374 KTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESI 451
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
235-561 |
2.20e-34 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 138.47 E-value: 2.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 235 DAENLGKEHFRKPVPPSPEDLSIICFTSGTTGDPKGAMITHQNIVSN---ASAFLKcVEHTFEPTpDDVTISYLPLAHMF 311
Cdd:PRK08751 190 EALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANmqqAHQWLA-GTGKLEEG-CEVVITALPLYHIF 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 312 ERVVQTVVYCCGARVGFFQGNIRLLADDMNTLKPTLFPTVPRVlNRIYDKVQNeakTPlkkfllnlavaskfkelqkgii 391
Cdd:PRK08751 268 ALTANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGV-NTLFNGLLN---TP---------------------- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 392 rrdsFWDKLIFAKIQASLGGrvriivtGAApISAPVMTFFRAAMGCQVYEAYGQTECT-AGCTFTSPGDWTSGHVGAPLT 470
Cdd:PRK08751 322 ----GFDQIDFSSLKMTLGG-------GMA-VQRSVAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLPIP 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 471 CNYVKLEDVADmDYFSVNNEGEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQG 550
Cdd:PRK08751 390 STDACIKDDAG-TVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-LVSG 467
|
330
....*....|.
gi 1622967304 551 EYIAPEKIENI 561
Cdd:PRK08751 468 FNVYPNEIEDV 478
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
252-575 |
9.22e-34 |
|
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: 132.40 E-value: 9.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 252 PEDLSIICFTSGTTGDPKGAMITHQNIVSNASAflkcVEHTFEPTPDDVTISYLPLAHMFERVVqtvvyccgarvgffqG 331
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYF----IGERLGLTEQDRLCIPVPLFHCFGSVL---------------G 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 332 NIRLLADDMNTLKPTLFPTVPRVLNRIydkvQNEAKTPLKkfllnlAVASKF-KELqkGIIRRDSFwdklifakiqaSLG 410
Cdd:cd05917 62 VLACLTHGATMVFPSPSFDPLAVLEAI----EKEKCTALH------GVPTMFiAEL--EHPDFDKF-----------DLS 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 411 gRVRIIVTGAAPISAPVMTFFRAAMGC-QVYEAYGQTECTAGCTFTSPGDWTS---GHVGAPLTCNYVKLEDVADMDYFS 486
Cdd:cd05917 119 -SLRTGIMAGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDSIEkrvNTVGRIMPHTEAKIVDPEGGIVPP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 487 VNNEGEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENIYNRSR 566
Cdd:cd05917 198 VGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGENIYPREIEEFLHTHP 276
|
....*....
gi 1622967304 567 PVLQIFVHG 575
Cdd:cd05917 277 KVSDVQVVG 285
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
104-575 |
1.08e-33 |
|
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: 133.96 E-value: 1.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 104 RWlSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMV 183
Cdd:cd05934 3 RW-TYAELLRESARIAAALAALGIR--PGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 184 ICDTpqkASVLienvekgftpslkvvilmdpfdddlkqrgeksgieilslydaenlgkehfrkpvppspedlsiicFTSG 263
Cdd:cd05934 80 VVDP---ASIL-----------------------------------------------------------------YTSG 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 264 TTGDPKGAMITHQNIVSNASAFLkcveHTFEPTPDDVTISYLPLAHM---FERVVQTVVycCGARV---------GFFqg 331
Cdd:cd05934 92 TTGPPKGVVITHANLTFAGYYSA----RRFGLGEDDVYLTVLPLFHInaqAVSVLAALS--VGATLvllprfsasRFW-- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 332 nirllaDDMNTLKPTLFPTVPRVLNRIYdkVQNEAKTPlkkfllnlavaskfkelqkgiirRDsfwdklifakiqaslgG 411
Cdd:cd05934 164 ------SDVRRYGATVTNYLGAMLSYLL--AQPPSPDD-----------------------RA----------------H 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 412 RVRIIvtGAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTSPGDWTSGHVGAPLTCNYVKLEDVADMDyFSVNNEG 491
Cdd:cd05934 197 RLRAA--YGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQE-LPAGEPG 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 492 EICIKGTN---VFKGYLKDPEKTQEALdSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKlAQGEYIAPEKIENIYNRSRPV 568
Cdd:cd05934 274 ELVIRGLRgwgFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVERAILRHPAV 351
|
....*..
gi 1622967304 569 LQIFVHG 575
Cdd:cd05934 352 REAAVVA 358
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
235-570 |
1.75e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 135.66 E-value: 1.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 235 DAENLGKEHFRKPVPPSPEDLSIICFTSGTTGDPKGAMITHQNIVSNasaFLKC-------VEHTFEptpddVTISYLPL 307
Cdd:PRK05677 189 DALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVAN---MLQCralmgsnLNEGCE-----ILIAPLPL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 308 AHMFervvqTVVYCCGARvgffqgnirLLADDMNTLKPTlfptvPRVLNRIydkVQNEAKTPLKKFL-LN-LAVAskfke 385
Cdd:PRK05677 261 YHIY-----AFTFHCMAM---------MLIGNHNILISN-----PRDLPAM---VKELGKWKFSGFVgLNtLFVA----- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 386 lqkgIIRRDSFwDKLIFAKIQASLGGrvriivtGAAPISApVMTFFRAAMGCQVYEAYGQTECTAGCTFTSPGDWTSGHV 465
Cdd:PRK05677 314 ----LCNNEAF-RKLDFSALKLTLSG-------GMALQLA-TAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTI 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 466 GAPLTCNYVKLEDVADMDyFSVNNEGEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIF 545
Cdd:PRK05677 381 GIPVPSTLCKVIDDDGNE-LPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI 459
|
330 340
....*....|....*....|....*
gi 1622967304 546 kLAQGEYIAPEKIENIYNRSRPVLQ 570
Cdd:PRK05677 460 -LVSGFNVYPNELEDVLAALPGVLQ 483
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
76-575 |
2.97e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 134.90 E-value: 2.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 76 TMYEVFQRGLAISDNGPCLGYRkpNQPYRWlSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTY 155
Cdd:PRK12583 19 TIGDAFDATVARFPDREALVVR--HQALRY-TWRQLADAVDRLARGLLALGVQ--PGDRVGIWAPNCAEWLLTQFATARI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 156 SMVAVPLYDTLGPEAIVYIVNKADIAMVICDTPQKAS--------VLIENVEKGFT-------PSLKVVILMDPFD---- 216
Cdd:PRK12583 94 GAILVNINPAYRASELEYALGQSGVRWVICADAFKTSdyhamlqeLLPGLAEGQPGalacerlPELRGVVSLAPAPppgf 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 217 ---DDLKQRGEKSGIEILSLYDAEnlgkehfrkpvpPSPEDLSIICFTSGTTGDPKGAMITHQNIVSNAsAFlkcVEHTF 293
Cdd:PRK12583 174 lawHELQARGETVSREALAERQAS------------LDRDDPINIQYTSGTTGFPKGATLSHHNILNNG-YF---VAESL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 294 EPTPDDVTISYLPLAHMFERVVQTVVycC---GARVGFFQGNIRLLAddmnTLKptlfptvprvlnriydKVQNEAKTPL 370
Cdd:PRK12583 238 GLTEHDRLCVPVPLYHCFGMVLANLG--CmtvGACLVYPNEAFDPLA----TLQ----------------AVEEERCTAL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 371 KkfllnlAVASKF-KELQKGiiRRDSFwDklifakiQASLggrvRIIVTGAAPISAPVMTFFRAAMGC-QVYEAYGQTEC 448
Cdd:PRK12583 296 Y------GVPTMFiAELDHP--QRGNF-D-------LSSL----RTGIMAGAPCPIEVMRRVMDEMHMaEVQIAYGMTET 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 449 TAGCTFTSPGD-----WTSghVGAPLTCNYVKLEDvADMDYFSVNNEGEICIKGTNVFKGYLKDPEKTQEALDSDGWLHT 523
Cdd:PRK12583 356 SPVSLQTTAADdlerrVET--VGRTQPHLEVKVVD-PDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHT 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1622967304 524 GDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENIYNRSRPVLQIFVHG 575
Cdd:PRK12583 433 GDLATMDEQGYVRIVGRSKDMI-IRGGENIYPREIEEFLFTHPAVADVQVFG 483
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
96-561 |
1.37e-32 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 132.95 E-value: 1.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 96 YRKPNQPYRWlSYKQVSDRAEYLGSCLLHKGYKSSpdqfvGIFAQNRPEW---IISELACYTYSMVAVPLYDTLGPEAIV 172
Cdd:PRK06087 41 AVVDNHGASY-TYSALDHAASRLANWLLAKGIEPG-----DRVAFQLPGWcefTIIYLACLKVGAVSVPLLPSWREAELV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 173 YIVNKADIAMVICDTPQKASvlieNVEKGFT------PSLKVVILMDpfdddlKQRGEKSGI---EILSLYdaenlgkEH 243
Cdd:PRK06087 115 WVLNKCQAKMFFAPTLFKQT----RPVDLILplqnqlPQLQQIVGVD------KLAPATSSLslsQIIADY-------EP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 244 FRKPVPPSPEDLSIICFTSGTTGDPKGAMITHQNIVSNASAFLKcvehTFEPTPDDVTISYLPLAHMfervvqtvvyccg 323
Cdd:PRK06087 178 LTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCA----RLNLTWQDVFMMPAPLGHA------------- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 324 arVGFFQGNIR-LLADDMNTLKPTLFP-TVPRVLNRiyDKVQ-NEAKTPlkkFLLNLavaskFKELQKGIIRRDSfwdkl 400
Cdd:PRK06087 241 --TGFLHGVTApFLIGARSVLLDIFTPdACLALLEQ--QRCTcMLGATP---FIYDL-----LNLLEKQPADLSA----- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 401 ifakiqaslggrVRIIVTGAAPISAPVMtffRAAM--GCQVYEAYGQTECTAGcTFTSPGD---WTSGHVGAPLTCNYVK 475
Cdd:PRK06087 304 ------------LRFFLCGGTTIPKKVA---RECQqrGIKLLSVYGSTESSPH-AVVNLDDplsRFMHTDGYAAAGVEIK 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 476 ledVADMDYFSV--NNEGEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYI 553
Cdd:PRK06087 368 ---VVDEARKTLppGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENI 443
|
....*...
gi 1622967304 554 APEKIENI 561
Cdd:PRK06087 444 SSREVEDI 451
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
158-560 |
3.34e-32 |
|
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: 130.25 E-value: 3.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 158 VAVPLYDTLGPEAIVYIVNKADIAMVICDTPqkasvlienvekgftpslkvviLMDPFDDDLKQrgekSGIEILSlYDAE 237
Cdd:cd05922 48 VFVPLNPTLKESVLRYLVADAGGRIVLADAG----------------------AADRLRDALPA----SPDPGTV-LDAD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 238 NL-GKEHFRKPVPPSPEDLSIICFTSGTTGDPKGAMITHQNIVSNASAflkcVEHTFEPTPDDVTISYLPLAHMFERVVQ 316
Cdd:cd05922 101 GIrAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARS----IAEYLGITADDRALTVLPLSYDYGLSVL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 317 TVVYCCGARVGFFQGNI--RLLADDMNTLKPTLFPTVP---RVLNRI-YDKvqneAKTPLKKFLlnlavaskfkelqkgi 390
Cdd:cd05922 177 NTHLLRGATLVLTNDGVldDAFWEDLREHGATGLAGVPstyAMLTRLgFDP----AKLPSLRYL---------------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 391 irrdsfwdklifakiqASLGGRVRiivtgAAPISApvmtfFRAAM-GCQVYEAYGQTECTAGCTFTSPG--DWTSGHVGA 467
Cdd:cd05922 237 ----------------TQAGGRLP-----QETIAR-----LRELLpGAQVYVMYGQTEATRRMTYLPPEriLEKPGSIGL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 468 PLT-CNYVKLEDvaDMDYFSVNNEGEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFK 546
Cdd:cd05922 291 AIPgGEFEILDD--DGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIK 368
|
410
....*....|....
gi 1622967304 547 LAqGEYIAPEKIEN 560
Cdd:cd05922 369 LF-GNRISPTEIEA 381
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
78-561 |
5.24e-32 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 131.39 E-value: 5.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 78 YEVFQRGLAISDNGPCLGYRKPNQPYRWLSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSM 157
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRALGVK--KGDRVAIYLPNIPEAVIAMLACARIGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 158 VAVPLYDTLGPEAIVYIVNKADIAMVICDT----PQKASVLIENVEK--GFTPSLKVVILMDPFDDDLKQRGEKSgieil 231
Cdd:COG0365 90 VHSPVFPGFGAEALADRIEDAEAKVLITADgglrGGKVIDLKEKVDEalEELPSLEHVIVVGRTGADVPMEGDLD----- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 232 slYDAENLGKEHFRKPVPPSPEDLSIICFTSGTTGDPKGAMITHQNIVSNASAFLKcveHTFEPTPDDV--TIS------ 303
Cdd:COG0365 165 --WDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAK---YVLDLKPGDVfwCTAdigwat 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 304 ------YLPLAHmfervvqtvvyccGARVGFFQGniRLLADDMNTL-------KPTLFPTVPRVLNRIydkvQNEAKTPL 370
Cdd:COG0365 240 ghsyivYGPLLN-------------GATVVLYEG--RPDFPDPGRLweliekyGVTVFFTAPTAIRAL----MKAGDEPL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 371 KKFLLnlavaskfkelqkgiirrdsfwdklifakiqASLggrvRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTECta 450
Cdd:COG0365 301 KKYDL-------------------------------SSL----RLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTET-- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 451 GCTFTSPGDWTS---GHVGAPLTCNYVKL-----EDVADmdyfsvNNEGEICIKG--TNVFKGYLKDPEKTQEAL--DSD 518
Cdd:COG0365 344 GGIFISNLPGLPvkpGSMGKPVPGYDVAVvdedgNPVPP------GEEGELVIKGpwPGMFRGYWNDPERYRETYfgRFP 417
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1622967304 519 GWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENI 561
Cdd:COG0365 418 GWYRTGDGARRDEDGYFWILGRSDDVINVS-GHRIGTAEIESA 459
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
254-575 |
2.84e-31 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 124.92 E-value: 2.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 254 DLSIICFTSGTTGDPKGAMITHQNIVSNASAFLKCVEhtfePTPDDVTISYLPLAHMFErvvqtvvYCCGARVGFFQGNi 333
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCAD----LTEDDRYLIINPFFHTFG-------YKAGIVACLLTGA- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 334 rlladdmnTLKPTLFPTVPRVLNRIYDKVQNEAKTPLKKFLLNLAVASkfkelqkgiirRDSFwdKLifakiqASLggrv 413
Cdd:cd17638 69 --------TVVPVAVFDVDAILEAIERERITVLPGPPTLFQSLLDHPG-----------RKKF--DL------SSL---- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 414 RIIVTGAAPISAPVMTFFRAAMGCQ-VYEAYGQTECTAGcTFTSPGD---WTSGHVGAPLTCNYVKLEDvadmdyfsvnn 489
Cdd:cd17638 118 RAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVA-TMCRPGDdaeTVATTCGRACPGFEVRIAD----------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 490 EGEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENIYNRSRPVL 569
Cdd:cd17638 186 DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGALAEHPGVA 264
|
....*.
gi 1622967304 570 QIFVHG 575
Cdd:cd17638 265 QVAVIG 270
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
106-575 |
3.33e-31 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 128.05 E-value: 3.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKgYKSSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVIC 185
Cdd:PRK06839 28 MTYKQLHEYVSKVAAYLIYE-LNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 DTPQKASVLienvekgftpSLKVVILMDPFdddlkqrgeksgIEILSLYDAENLGKEHFrkpVPPSPEDLSIICFTSGTT 265
Cdd:PRK06839 107 EKTFQNMAL----------SMQKVSYVQRV------------ISITSLKEIEDRKIDNF---VEKNESASFIICYTSGTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 266 GDPKGAMITHQNIVSNAsaflkcVEHTF--EPTPDDVTISYLPLAHMfervvqtvvyccgarvgffqGNIRLLAddmntl 343
Cdd:PRK06839 162 GKPKGAVLTQENMFWNA------LNNTFaiDLTMHDRSIVLLPLFHI--------------------GGIGLFA------ 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 344 KPTLFPTVPRVLNRIYDKVQNEAKTPLKKFLLNLAVASKFKELQKGIIRRDSFWDKlifakiqaslggrVRIIVTGAAPI 423
Cdd:PRK06839 210 FPTLFAGGVIIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQS-------------VRWFYNGGAPC 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 424 SAPVMTFFRAaMGCQVYEAYGQTECTAGCTFTSPGDW--TSGHVGAPLTCNYVKLEDVADMDyFSVNNEGEICIKGTNVF 501
Cdd:PRK06839 277 PEELMREFID-RGFLFGQGFGMTETSPTVFMLSEEDArrKVGSIGKPVLFCDYELIDENKNK-VEVGEVGELLIRGPNVM 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622967304 502 KGYLKDPEKTQEALdSDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENIYNRSRPVLQIFVHG 575
Cdd:PRK06839 355 KEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQVINKLSDVYEVAVVG 426
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
143-542 |
1.60e-30 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 126.14 E-value: 1.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 143 PEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVICDtPQKASVLIENVEKGFTPSLKvvilmdPFDDDlkqr 222
Cdd:PRK07514 64 PEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCD-PANFAWLSKIAAAAGAPHVE------TLDAD---- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 223 geKSGieilSLYDAENLGKEHFRkPVPPSPEDLSIICFTSGTTGDPKGAMITHQNIVSNASAFLKCvehtFEPTPDDVTI 302
Cdd:PRK07514 133 --GTG----SLLEAAAAAPDDFE-TVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDY----WRFTPDDVLI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 303 SYLPLAH---MFerVVQTVVYCCGARVGFFQgniRLLADDMNTLKP--TLFPTVPRVLNRIydkVQNEAKTPlkkfllnl 377
Cdd:PRK07514 202 HALPIFHthgLF--VATNVALLAGASMIFLP---KFDPDAVLALMPraTVMMGVPTFYTRL---LQEPRLTR-------- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 378 avaskfkelqkgiirrdsfwdklifakiqaSLGGRVRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTEctaGCTFTS- 456
Cdd:PRK07514 266 ------------------------------EAAAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTE---TNMNTSn 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 457 P--GDWTSGHVGAPLTCNYVKLEDVADMDYFSVNNEGEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGT 534
Cdd:PRK07514 313 PydGERRAGTVGFPLPGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGY 392
|
....*...
gi 1622967304 535 LKIIDRKK 542
Cdd:PRK07514 393 VHIVGRGK 400
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
106-573 |
4.13e-30 |
|
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: 123.64 E-value: 4.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKAdiamvic 185
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVG--PGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRA------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 dtpqKASVLienvekgFTPSLkvvilmdpfdddlkqrgeksgieilslydaenlgkehFRKPVP-PSPEDLSIICFTSGT 264
Cdd:cd05903 73 ----KAKVF-------VVPER-------------------------------------FRQFDPaAMPDAVALLLFTSGT 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 265 TGDPKGAMITHQNIVSNASAFLkcvEHtFEPTPDDVTISYLPLAHmfervvQTvvyccgarvGFFQGnirlladdmnTLK 344
Cdd:cd05903 105 TGEPKGVMHSHNTLSASIRQYA---ER-LGLGPGDVFLVASPMAH------QT---------GFVYG----------FTL 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 345 PTLFPTvPRVLNRIYD-----KVQNE-------AKTPlkkFLLNLAVASKFkelqkgiirrdsfwdklifakiQASLGGR 412
Cdd:cd05903 156 PLLLGA-PVVLQDIWDpdkalALMREhgvtfmmGATP---FLTDLLNAVEE----------------------AGEPLSR 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 413 VRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTSPGD----WTSGhvGAPLTCNYVKLEDvADMDYFSVN 488
Cdd:cd05903 210 LRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPedrrLYTD--GRPLPGVEIKVVD-DTGATLAPG 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 489 NEGEICIKGTNVFKGYLKDPEKTQEALDsDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENIYNRSRPV 568
Cdd:cd05903 287 VEGELLSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGV 364
|
....*
gi 1622967304 569 LQIFV 573
Cdd:cd05903 365 IEAAV 369
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
246-561 |
6.73e-30 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 124.75 E-value: 6.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 246 KPVPPSPEDLSIICFTSGTTGDPKGAMITHQNIVSN---ASAFLKCVeHTFEPTPDD-VTISYLPLAHMFervVQTVVYC 321
Cdd:PRK07059 197 KPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANvlqMEAWLQPA-FEKKPRPDQlNFVCALPLYHIF---ALTVCGL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 322 CGARVG---FFQGNIRLLADDMNTLKPTLFPTVPRVlNRIYDKvqneaktplkkfLLNlavASKFkelqkgiirrdsfwD 398
Cdd:PRK07059 273 LGMRTGgrnILIPNPRDIPGFIKELKKYQVHIFPAV-NTLYNA------------LLN---NPDF--------------D 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 399 KLIFAKIQASLGGrvriivtGAApISAPVMTFFRAAMGCQVYEAYGQTEcTAGCTFTSPGDWT--SGHVGAPLTCNYVKL 476
Cdd:PRK07059 323 KLDFSKLIVANGG-------GMA-VQRPVAERWLEMTGCPITEGYGLSE-TSPVATCNPVDATefSGTIGLPLPSTEVSI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 477 EDVADMDyFSVNNEGEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPE 556
Cdd:PRK07059 394 RDDDGND-LPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMI-LVSGFNVYPN 471
|
....*
gi 1622967304 557 KIENI 561
Cdd:PRK07059 472 EIEEV 476
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
96-561 |
8.51e-30 |
|
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: 123.89 E-value: 8.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 96 YRKPNQPYRWLSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEwiisELACYtY---SMVAV--PLYDTLGPEA 170
Cdd:cd12119 16 SRTHEGEVHRYTYAEVAERARRLANALRRLGVK--PGDRVATLAWNTHR----HLELY-YavpGMGAVlhTINPRLFPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 171 IVYIVNKADIAMVICDT---PqkasvLIENVeKGFTPSLKVVILMDPFDDdlkqRGEKSGIEILSlYDAEnLGKEHFRKP 247
Cdd:cd12119 89 IAYIINHAEDRVVFVDRdflP-----LLEAI-APRLPTVEHVVVMTDDAA----MPEPAGVGVLA-YEEL-LAAESPEYD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 248 VPPSPE-DLSIICFTSGTTGDPKGAMITHQNIVSNASAFLkcvehtfepTPDDVTIS----YLPLAHMFERVVQTVVYC- 321
Cdd:cd12119 157 WPDFDEnTAAAICYTSGTTGNPKGVVYSHRSLVLHAMAAL---------LTDGLGLSesdvVLPVVPMFHVNAWGLPYAa 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 322 --CGARV----GFFQGniRLLADDMNTLKPTLFPTVPRVLNriydkvqneaktplkkFLLNlAVASKFKELQKGiirrds 395
Cdd:cd12119 228 amVGAKLvlpgPYLDP--ASLAELIEREGVTFAAGVPTVWQ----------------GLLD-HLEANGRDLSSL------ 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 396 fwdklifakiqaslggrVRIIVTGAAPISAPVMTFfrAAMGCQVYEAYGQTECTAGCTFTSPgdwTSGHVGAPLTCNY-- 473
Cdd:cd12119 283 -----------------RRVVIGGSAVPRSLIEAF--EERGVRVIHAWGMTETSPLGTVARP---PSEHSNLSEDEQLal 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 474 ------------VKLED----VADMDYFSVnneGEICIKGTNVFKGYLKDPEKTqEALDSDGWLHTGDIGRWLPNGTLKI 537
Cdd:cd12119 341 rakqgrpvpgveLRIVDddgrELPWDGKAV---GELQVRGPWVTKSYYKNDEES-EALTEDGWLRTGDVATIDEDGYLTI 416
|
490 500
....*....|....*....|....
gi 1622967304 538 IDRKKNIFKLAqGEYIAPEKIENI 561
Cdd:cd12119 417 TDRSKDVIKSG-GEWISSVELENA 439
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
232-544 |
9.42e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 124.34 E-value: 9.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 232 SLYDAENLGKEHFRKPVPPSPEDLSIICFTSGTTGDPKGAMITHQNIVSNAS---AFLKCVehtfePTPDDVTISYLPLA 308
Cdd:PRK05605 198 TLVDAAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqgkAWVPGL-----GDGPERVLAALPMF 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 309 HMFE-RVVQTVVYCCGAR-VGFFQGNIRLLADDMNTLKPTLFPTVPRvlnrIYDKVQNEAKtplkkfllnlavaskfkel 386
Cdd:PRK05605 273 HAYGlTLCLTLAVSIGGElVLLPAPDIDLILDAMKKHPPTWLPGVPP----LYEKIAEAAE------------------- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 387 QKGIirrdsfwdklifakiqaSLGGrVRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTECT---AGCTFTSpgDWTSG 463
Cdd:PRK05605 330 ERGV-----------------DLSG-VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpiiVGNPMSD--DRRPG 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 464 HVGAPLTCNYVKledVADMDYFSVN----NEGEICIKGTNVFKGYLKDPEKTQEALdSDGWLHTGDIGRWLPNGTLKIID 539
Cdd:PRK05605 390 YVGVPFPDTEVR---IVDPEDPDETmpdgEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVD 465
|
....*
gi 1622967304 540 RKKNI 544
Cdd:PRK05605 466 RIKEL 470
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
231-561 |
2.86e-29 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 123.01 E-value: 2.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 231 LSLYDAENLGKEHFRKPVPPSPEDLSIICFTSGTTGDPKGAMITHQNIVSNASAFLKCVE------HTFEPTPDDVTISY 304
Cdd:PRK12492 185 VPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSqlgpdgQPLMKEGQEVMIAP 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 305 LPLAHMFErvvqtvvyccgarvgfFQGNIRLLaddMNTLKPTLFPTVPRVLNRIYDKVQN---EAKTPLKKFLLNLAVAS 381
Cdd:PRK12492 265 LPLYHIYA----------------FTANCMCM---MVSGNHNVLITNPRDIPGFIKELGKwrfSALLGLNTLFVALMDHP 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 382 KFKELQkgiirrdsfwdkliFAKIQASLGGrvriivtGAAPISApVMTFFRAAMGCQVYEAYGQTECTAGCTFTSPGDWT 461
Cdd:PRK12492 326 GFKDLD--------------FSALKLTNSG-------GTALVKA-TAERWEQLTGCTIVEGYGLTETSPVASTNPYGELA 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 462 S-GHVGAPLTCNYVKLEDvADMDYFSVNNEGEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDR 540
Cdd:PRK12492 384 RlGTVGIPVPGTALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDR 462
|
330 340
....*....|....*....|.
gi 1622967304 541 KKNIFkLAQGEYIAPEKIENI 561
Cdd:PRK12492 463 KKDLI-IVSGFNVYPNEIEDV 482
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
106-575 |
8.37e-29 |
|
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: 119.89 E-value: 8.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYKSSpdQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVIc 185
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKG--DRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 dtpqkasvlienvekgftpslkvvilmdpfdddlkqrgeksgieilslydaenlgkehfrkpVPPSPEDLSIICFTSGTT 265
Cdd:cd05935 79 --------------------------------------------------------------VGSELDDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 266 GDPKGAMITHQNIVSNASAflkcVEHTFEPTPDDVTISYLPLAHM--FERVVQTVVYCCGARVGFFQGNIRLLADDMNTL 343
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQ----SAVWTGLTPSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMARWDRETALELIEKY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 344 KPTLFPTVPRVLNRIYDKVQNEAktplkkfllnlavaskfkelqkgiirRDsfWDKLifakiqaslggrvRIIVTGAAPI 423
Cdd:cd05935 173 KVTFWTNIPTMLVDLLATPEFKT--------------------------RD--LSSL-------------KVLTGGGAPM 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 424 SAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTSPGDWTSGHVGAPLTCNYVKLEDVADMDYFSVNNEGEICIKGTNVFKG 503
Cdd:cd05935 212 PPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKG 291
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622967304 504 YLKDPEKTQEALDSDG---WLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENIYNRSRPVLQIFVHG 575
Cdd:cd05935 292 YWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVIS 365
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
104-535 |
9.91e-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: 123.04 E-value: 9.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 104 RWLSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELA------CYtysmvaVPLyDTLGPEA-IVYIVN 176
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALGVG--PGDLVGVCLERSLEMVVALLAvlkagaAY------VPL-DPAYPAErLAYMLE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 177 KADIAMVICDTPQKASVlienvekgftPSLKV-VILMDPfdddlkqrgeksgiEILSLYDAENLgkehfrkPVPPSPEDL 255
Cdd:COG1020 571 DAGARLVLTQSALAARL----------PELGVpVLALDA--------------LALAAEPATNP-------PVPVTPDDL 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 256 SIICFTSGTTGDPKGAMITHQNIVsnasAFLKCVEHTFEPTPDDV-----TIS--------YLPLahmfervvqtvvyCC 322
Cdd:COG1020 620 AYVIYTSGSTGRPKGVMVEHRALV----NLLAWMQRRYGLGPGDRvlqfaSLSfdasvweiFGAL-------------LS 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 323 GARVGFFQGNIRL----LADDMNTLKPTLFPTVPrvlnriydkvqneaktplkkfllnlavaskfkelqkgiirrdSFWD 398
Cdd:COG1020 683 GATLVLAPPEARRdpaaLAELLARHRVTVLNLTP------------------------------------------SLLR 720
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 399 KLIFAKIQASLGgrVRIIVTGAAPISAPVMTFFRAAM-GCQVYEAYGQTECTAGCTF--TSPGDWTSGHV--GAPL--TC 471
Cdd:COG1020 721 ALLDAAPEALPS--LRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTVDSTYyeVTPPDADGGSVpiGRPIanTR 798
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622967304 472 NYV---KLEDVAdmdyfsVNNEGEICIKGTNVFKGYLKDPEKTQEA-----LDSDG--WLHTGDIGRWLPNGTL 535
Cdd:COG1020 799 VYVldaHLQPVP------VGVPGELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNL 866
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
254-561 |
1.35e-28 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 120.85 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 254 DLSIICFTSGTTGDPKGAMITHQNIVSNASAFLKCVEHtfEPTPDDVTISYLPLAHMFervvQTVVYCC------GARVG 327
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGP--EMIGQVVTLGLIPFFHIY----GITGICCatlrnkGKVVV 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 328 FFQGNIRLLADDMNTLKPTLFPTVPRVLnriydkvqneaktplkkflLNLAvaskfkelqkgiirRDSFWDKLIFAKIqa 407
Cdd:PLN02330 259 MSRFELRTFLNALITQEVSFAPIVPPII-------------------LNLV--------------KNPIVEEFDLSKL-- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 408 slggRVRIIVTGAAPISAPVMTFFRAAM-GCQVYEAYGQTECTagCTFTSPGDWTSGH-------VGAPLTCNYVKLEDV 479
Cdd:PLN02330 304 ----KLQAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEHS--CITLTHGDPEKGHgiakknsVGFILPNLEVKFIDP 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 480 ADMDYFSVNNEGEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIE 559
Cdd:PLN02330 378 DTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELE 456
|
..
gi 1622967304 560 NI 561
Cdd:PLN02330 457 AI 458
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
99-560 |
2.34e-28 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 119.92 E-value: 2.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 99 PNQPYRWlSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAV---PLYDTlgpEAIVYIV 175
Cdd:PRK08315 38 RDQGLRW-TYREFNEEVDALAKGLLALGIE--KGDRVGIWAPNVPEWVLTQFATAKIGAILVtinPAYRL---SELEYAL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 176 NKADIAMVIC-----DT----------PQKASVLIENVEKGFTPSLKVVILMDpfddDLKQRGEKSGIEILSLYDAENLG 240
Cdd:PRK08315 112 NQSGCKALIAadgfkDSdyvamlyelaPELATCEPGQLQSARLPELRRVIFLG----DEKHPGMLNFDELLALGRAVDDA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 241 KEHFRKPVPpSPEDLSIICFTSGTTGDPKGAMITHQNIVSNASAFLKCVEHTFEptpDDVTISyLPLAHMFERV--VQTV 318
Cdd:PRK08315 188 ELAARQATL-DPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEE---DRLCIP-VPLYHCFGMVlgNLAC 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 319 VYCCGARV----GFfqgnirllaDDMNTLKPtlfptvprvlnriydkVQNEAKTPLKkfllnlAVASKF-KELqkgiirr 393
Cdd:PRK08315 263 VTHGATMVypgeGF---------DPLATLAA----------------VEEERCTALY------GVPTMFiAEL------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 394 dsfwDKLIFAKIQASlggRVRiivTG---AAPISAPVMTFFRAAMGC-QVYEAYGQTECTAGCTFTSPGD------WTSG 463
Cdd:PRK08315 305 ----DHPDFARFDLS---SLR---TGimaGSPCPIEVMKRVIDKMHMsEVTIAYGMTETSPVSTQTRTDDplekrvTTVG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 464 HVGAPLTcnyVKLEDVADMDYFSVNNEGEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKN 543
Cdd:PRK08315 375 RALPHLE---VKIVDPETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKD 451
|
490
....*....|....*..
gi 1622967304 544 IFkLAQGEYIAPEKIEN 560
Cdd:PRK08315 452 MI-IRGGENIYPREIEE 467
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
106-561 |
5.55e-28 |
|
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: 117.63 E-value: 5.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGykSSPDQFVGIFAQNRPEWIISELACY----TYsmvaVPLYDTLGPEAIVYIVNKADIA 181
Cdd:cd05930 13 LTYAELDARANRLARYLRERG--VGPGDLVAVLLERSLEMVVAILAVLkagaAY----VPLDPSYPAERLAYILEDSGAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 182 MVICDtpqkasvlienvekgftpslkvvilmdpfdddlkqrgeksgieilslydaenlgkehfrkpvppsPEDLSIICFT 261
Cdd:cd05930 87 LVLTD-----------------------------------------------------------------PDDLAYVIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 262 SGTTGDPKGAMITHQNIVSnasaFLKCVEHTFEPTPDDVTISYLPLAH-MFerVVQTVVY-CCGARV----GFFQGNIRL 335
Cdd:cd05930 102 SGSTGKPKGVMVEHRGLVN----LLLWMQEAYPLTPGDRVLQFTSFSFdVS--VWEIFGAlLAGATLvvlpEEVRKDPEA 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 336 LADDMNTLKPTLFPTVPRVLNRIYDKVQNEAKTPLkkfllnlavaskfkelqkgiirrdsfwdklifakiqaslggrvRI 415
Cdd:cd05930 176 LADLLAEEGITVLHLTPSLLRLLLQELELAALPSL-------------------------------------------RL 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 416 IVTGAAPISAPVMT-FFRAAMGCQVYEAYGQTECTAGCTFT--SPGDWTSGHV--GAPLTCNYVKLEDvADMDYFSVNNE 490
Cdd:cd05930 213 VLVGGEALPPDLVRrWRELLPGARLVNLYGPTEATVDATYYrvPPDDEEDGRVpiGRPIPNTRVYVLD-ENLRPVPPGVP 291
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622967304 491 GEICIKGTNVFKGYLKDPEKTQEA-----LDSDGWLH-TGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENI 561
Cdd:cd05930 292 GELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIELGEIEAA 367
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
131-542 |
1.33e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 118.13 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 131 PDQFVGIFAQNRPEWIISELACYTYSMVAvPLYDTLGPEAIVYIVNKADIAMVIC-------DTPQKASVLIENVekgft 203
Cdd:PRK07529 82 PGDVVAFLLPNLPETHFALWGGEAAGIAN-PINPLLEPEQIAELLRAAGAKVLVTlgpfpgtDIWQKVAEVLAAL----- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 204 PSLKVVILMDPFDD-------DLKQRGEKSGIEILSlYDAE--NLGKEHFRKPVPPSPEDLSIICFTSGTTGDPKGAMIT 274
Cdd:PRK07529 156 PELRTVVEVDLARYlpgpkrlAVPLIRRKAHARILD-FDAElaRQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHT 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 275 HQNIVSNA---SAFLKCvehtfepTPDDVTISYLPLAHMFERVV---------QTVVYCC--GAR-VGFFQGNIRLLAdd 339
Cdd:PRK07529 235 HGNEVANAwlgALLLGL-------GPGDTVFCGLPLFHVNALLVtglaplargAHVVLATpqGYRgPGVIANFWKIVE-- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 340 mnTLKPTLFPTVPRVLNriydkvqneaktplkkfllnlavaskfkelqkgiirrdsfwdklifAKIQASLGGR----VRI 415
Cdd:PRK07529 306 --RYRINFLSGVPTVYA----------------------------------------------ALLQVPVDGHdissLRY 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 416 IVTGAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTSP-GDWTSGHVGAPLTCNYVKLEDV-ADMDYFS---VNNE 490
Cdd:PRK07529 338 ALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPdGERRIGSVGLRLPYQRVRVVILdDAGRYLRdcaVDEV 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1622967304 491 GEICIKGTNVFKGYLkDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKK 542
Cdd:PRK07529 418 GVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAK 468
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
106-578 |
1.49e-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: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGykSSPDQFVGIFAQNRPEWIISEL------ACYtysmvaVPLYDTLGPEAIVYIVNKAD 179
Cdd:cd17653 23 LTYGELDAASNALANRLLQLG--VVPGDVVPLLSDRSLEMLVAILailkagAAY------VPLDAKLPSARIQAILRTSG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 180 IAMVICdtpqkasvlienvekgftpslkvvilmdpfdddlkqrgeksgieilslydaenlgkehfrkpvPPSPEDLSIIC 259
Cdd:cd17653 95 ATLLLT---------------------------------------------------------------TDSPDDLAYII 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 260 FTSGTTGDPKGAMITHQNIVSNASAflkcVEHTFEPTPDDvtisylplahmfeRVVQ--TVVYCCGARVGF---FQGNIR 334
Cdd:cd17653 112 FTSGSTGIPKGVMVPHRGVLNYVSQ----PPARLDVGPGS-------------RVAQvlSIAFDACIGEIFstlCNGGTL 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 335 LLADDMNTL-----KPTLFPTVPRVLnriydkvqneaktplkkfllnlavaskfkelqkGIIRRDSFwdklifakiqasl 409
Cdd:cd17653 175 VLADPSDPFahvarTVDALMSTPSIL---------------------------------STLSPQDF------------- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 410 gGRVRIIVTGAAPISAPVMTffRAAMGCQVYEAYGQTECTAGCTFTS--PGDWTsgHVGAPLTCNYVKLEDvADMDYFSV 487
Cdd:cd17653 209 -PNLKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTEllPGQPV--TIGKPIPNSTCYILD-ADLQPVPE 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 488 NNEGEICIKGTNVFKGYLKDPEKTQEALDSDGWLH------TGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIENI 561
Cdd:cd17653 283 GVVGEICISGVQVARGYLGNPALTASKFVPDPFWPgsrmyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEIEEV 361
|
490 500
....*....|....*....|
gi 1622967304 562 YNRSRPVLQ---IFVHGESL 578
Cdd:cd17653 362 VLQSQPEVTqaaAIVVNGRL 381
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
158-540 |
2.05e-27 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 118.87 E-value: 2.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 158 VAVPLYDTLGPEAIVYIVNKADIAMVIcdTPQKasvLIENVE-KGFTPSLKV---VILMDpfddDLKQRgeKSGIEILSL 233
Cdd:PRK08633 691 VPVNLNYTASEAALKSAIEQAQIKTVI--TSRK---FLEKLKnKGFDLELPEnvkVIYLE----DLKAK--ISKVDKLTA 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 234 YDAENLGKEHFRKPV---PPSPEDLSIICFTSGTTGDPKGAMITHQNIVSNasafLKCVEHTFEPTPDDVTISYLPLAHM 310
Cdd:PRK08633 760 LLAARLLPARLLKRLygpTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSN----IEQISDVFNLRNDDVILSSLPFFHS 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 311 FERVVQT-VVYCCGARVGFF------QGNIRLLADDMNTL---KPTLFptvprvlnRIYDKVqneaktplKKFllnlava 380
Cdd:PRK08633 836 FGLTVTLwLPLLEGIKVVYHpdptdaLGIAKLVAKHRATIllgTPTFL--------RLYLRN--------KKL------- 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 381 skfkelqkgiirrdsfwDKLIFAKIqaslggrvRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTECT--AGCT---FT 455
Cdd:PRK08633 893 -----------------HPLMFASL--------RLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSpvASVNlpdVL 947
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 456 SPGDWT-----SGHVGAPLTCNYVKLEDVADMDYFSVNNEGEICIKGTNVFKGYLKDPEKTQEAL---DSDGWLHTGDIG 527
Cdd:PRK08633 948 AADFKRqtgskEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKG 1027
|
410
....*....|...
gi 1622967304 528 RWLPNGTLKIIDR 540
Cdd:PRK08633 1028 HLDEDGFLTITDR 1040
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
107-559 |
3.29e-27 |
|
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: 114.67 E-value: 3.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 107 SYKQVSDRAEYLGSCLLHKGyKSSPDQFVGIFAQNRPEWIISELACY----TYsmvaVPLyDTLGPEA-IVYIVNKADIA 181
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAG-GVGPGDRVAVLLERSAELVVAILAVLkagaAY----VPL-DPAYPAErLAFILEDAGAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 182 MVICDtPQKASVLIENVekgftpsLKVVILMDPFDDDLkqrgeksgieilslyDAENLGKEHfrkPVPPSPEDLSIICFT 261
Cdd:TIGR01733 75 LLLTD-SALASRLAGLV-------LPVILLDPLELAAL---------------DDAPAPPPP---DAPSGPDDLAYVIYT 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 262 SGTTGDPKGAMITHQNIVSNASAFLKCvehtFEPTPDDVTISYLPLAH---MFE-----RVVQTVVYCCGARVGFFQgni 333
Cdd:TIGR01733 129 SGSTGRPKGVVVTHRSLVNLLAWLARR----YGLDPDDRVLQFASLSFdasVEEifgalLAGATLVVPPEDEERDDA--- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 334 RLLADDMNTLKPTLFPTVPrvlnriydkvqneaktplkkfllnlavaskfkelqkgiirrdSFWDKLIFAKIQASLGgrV 413
Cdd:TIGR01733 202 ALLAALIAEHPVTVLNLTP------------------------------------------SLLALLAAALPPALAS--L 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 414 RIIVTGAAPISAPVMTFFRAAMG-CQVYEAYGQTECTAGCTFTS-PGDWTSGHV----GAPLTCNYVKLEDvADMDYFSV 487
Cdd:TIGR01733 238 RLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWSTATLvDPDDAPRESpvpiGRPLANTRLYVLD-DDLRPVPV 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 488 NNEGEICIKGTNVFKGYLKDPEKTQEA-LDSDGWL-------HTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIE 559
Cdd:TIGR01733 317 GVVGELYIGGPGVARGYLNRPELTAERfVPDPFAGgdgarlyRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIE 395
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
207-559 |
3.85e-27 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 116.23 E-value: 3.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 207 KVVILMDPFDDDLKQRGEKSGIEILSLyDAENLGKEHFRK----------PVPPSPEDLSIICFTSGTTGDPKGAMITHQ 276
Cdd:PLN02246 124 KLIITQSCYVDKLKGLAEDDGVTVVTI-DDPPEGCLHFSEltqadenelpEVEISPDDVVALPYSSGTTGLPKGVMLTHK 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 277 NIVSNASAFLKCVEHTFEPTPDDVTISYLPLAHMFErvvQTVVYCCGARVGF-------FQgnIRLLADDMNTLKPTLFP 349
Cdd:PLN02246 203 GLVTSVAQQVDGENPNLYFHSDDVILCVLPMFHIYS---LNSVLLCGLRVGAailimpkFE--IGALLELIQRHKVTIAP 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 350 TVPRVLNRIydkvqneAKTPlkkfllnlavaskfkelqkgiirrdsfwdklIFAKIQASlggRVRIIVTGAAPISAPVMT 429
Cdd:PLN02246 278 FVPPIVLAI-------AKSP-------------------------------VVEKYDLS---SIRMVLSGAAPLGKELED 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 430 FFRAAMGCQVY-EAYGQTE-------CTAgctFT-SPGDWTSGHVGAPLTCNYVKLEDVADMDYFSVNNEGEICIKGTNV 500
Cdd:PLN02246 317 AFRAKLPNAVLgQGYGMTEagpvlamCLA---FAkEPFPVKSGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQI 393
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622967304 501 FKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIE 559
Cdd:PLN02246 394 MKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAELE 451
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
135-545 |
6.20e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 115.47 E-value: 6.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 135 VGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVICDT---PQKASVLIENVekgftPSLKVVIL 211
Cdd:PRK06188 65 VALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGISTLIVDPapfVERALALLARV-----PSLKHVLT 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 212 MDPFDDdlkqrgeksGIEILSLYDAENLgkehfRKPVPPS-PEDLSIICFTSGTTGDPKGAMITHQNIVSNASAFLKcve 290
Cdd:PRK06188 140 LGPVPD---------GVDLLAAAAKFGP-----APLVAAAlPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLA--- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 291 hTFEpTPDDvtISYL---PLAH----MFERVVQ---TVVYCCGARVGFFqgnIRLLADDMNTLkpTLFptVPRVLNRIYD 360
Cdd:PRK06188 203 -EWE-WPAD--PRFLmctPLSHaggaFFLPTLLrggTVIVLAKFDPAEV---LRAIEEQRITA--TFL--VPTMIYALLD 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 361 kvqneaktplkkfllnlavaskfkelQKGIIRRDsfwdklifakiQASLggrvRIIVTGAAPISaPVmtffRAAMGCQVY 440
Cdd:PRK06188 272 --------------------------HPDLRTRD-----------LSSL----ETVYYGASPMS-PV----RLAEAIERF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 441 -----EAYGQTECTAGCTFTSPGDWTSGHVGAPLTCNY------VKLEDvADMDYFSVNNEGEICIKGTNVFKGYLKDPE 509
Cdd:PRK06188 306 gpifaQYYGQTEAPMVITYLRKRDHDPDDPKRLTSCGRptpglrVALLD-EDGREVAQGEVGEICVRGPLVMDGYWNRPE 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1622967304 510 KTQEALdSDGWLHTGDIGRWLPNGTLKIIDRKK--------NIF 545
Cdd:PRK06188 385 ETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKdmivtggfNVF 427
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
104-571 |
8.44e-27 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 115.03 E-value: 8.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 104 RWLSYKQVSDRAEYLGSCLLHKGyksSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEA---IVYIVNKADI 180
Cdd:cd05931 23 ETLTYAELDRRARAIAARLQAVG---KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 181 AMVICDTPQKASV--LIENVEKGFTPSLKVVilmDPFDDDlkqrgeksgieilslyDAENLGkehfrkPVPPSPEDLSII 258
Cdd:cd05931 100 RVVLTTAAALAAVraFAASRPAAGTPRLLVV---DLLPDT----------------SAADWP------PPSPDPDDIAYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 259 CFTSGTTGDPKGAMITHQNIVSNASAFLKCvehtFEPTPDDVTISYLPLAH---MFERVVQTVVycCGARVGFFQgnirl 335
Cdd:cd05931 155 QYTSGSTGTPKGVVVTHRNLLANVRQIRRA----YGLDPGDVVVSWLPLYHdmgLIGGLLTPLY--SGGPSVLMS----- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 336 laddmntlkPTLFptvprvlnriydkvqneaktplkkfllnlavaskfkelqkgiIRRDSFWDKLI------------FA 403
Cdd:cd05931 224 ---------PAAF------------------------------------------LRRPLRWLRLIsryratisaapnFA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 404 ------KIQ-ASLGG----RVRIIVTGAAPISAPVMTFFRAAMG-----CQ-VYEAYGQTECTAGCTFTSPGD------- 459
Cdd:cd05931 253 ydlcvrRVRdEDLEGldlsSWRVALNGAEPVRPATLRRFAEAFApfgfrPEaFRPSYGLAEATLFVSGGPPGTgpvvlrv 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 460 -----WTSGHVGAPLTCNYVKL----EDVADMDYFSVNNE----------GEICIKGTNVFKGYLKDPEKTQE------A 514
Cdd:cd05931 333 drdalAGRAVAVAADDPAARELvscgRPLPDQEVRIVDPEtgrelpdgevGEIWVRGPSVASGYWGRPEATAEtfgalaA 412
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622967304 515 LDSDGWLHTGDIGRWLPN-----GTLK--IIDRKKNIFklaqgeyiaPEKIENIYNRSRPVLQI 571
Cdd:cd05931 413 TDEGGWLRTGDLGFLHDGelyitGRLKdlIIVRGRNHY---------PQDIEATAEEAHPALRP 467
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
106-564 |
1.10e-26 |
|
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: 114.35 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLyDTLGP-EAIVYIVNKADIAMVI 184
Cdd:cd17655 23 LTYRELNERANQLARTLREKGVG--PDTIVGIMAERSLEMIVGILGILKAGGAYLPI-DPDYPeERIQYILEDSGADILL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 185 CDTPQKASVLienvekgftpSLKVVILMDpfDDDLKQrgeksgieilslYDAENLgkehfrkPVPPSPEDLSIICFTSGT 264
Cdd:cd17655 100 TQSHLQPPIA----------FIGLIDLLD--EDTIYH------------EESENL-------EPVSKSDDLAYVIYTSGS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 265 TGDPKGAMITHQNIVSNASAFLKCVEHTfepTPDDVtISYLPLAhmFERVVQTV--VYCCGArvgffqgnirlladdmnt 342
Cdd:cd17655 149 TGKPKGVMIEHRGVVNLVEWANKVIYQG---EHLRV-ALFASIS--FDASVTEIfaSLLSGN------------------ 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 343 lkpTLFptvprvlnrIYDKVQNEAKTPLKKFllnlavaskFKELQKGIIRRDSFWDKLIfAKIQASLGGRVRIIVTGAAP 422
Cdd:cd17655 205 ---TLY---------IVRKETVLDGQALTQY---------IRQNRITIIDLTPAHLKLL-DAADDSEGLSLKHLIVGGEA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 423 ISAPVMTFF--RAAMGCQVYEAYGQTECTAGCTF--TSPGDWTSGHV--GAPLTCNYVKLEDvADMDYFSVNNEGEICIK 496
Cdd:cd17655 263 LSTELAKKIieLFGTNPTITNAYGPTETTVDASIyqYEPETDQQVSVpiGKPLGNTRIYILD-QYGRPQPVGVAGELYIG 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622967304 497 GTNVFKGYLKDPEKTQEALDSDGWL------HTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIENIYNR 564
Cdd:cd17655 342 GEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-RGYRIELGEIEARLLQ 414
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
125-559 |
2.16e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 113.36 E-value: 2.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 125 KGYKSSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVICDTPQKASVLIENVEKGFTP 204
Cdd:PRK09088 40 RRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDDAVAAGRTDVEDLAAFIA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 205 SLKVVILMDpfdddlkqrgeksgieilslydaenlgkehfRKPVPPspEDLSIICFTSGTTGDPKGAMITHQNIVSNASA 284
Cdd:PRK09088 120 SADALEPAD-------------------------------TPSIPP--ERVSLILFTSGTSGQPKGVMLSERNLQQTAHN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 285 F--LKCVEHTfeptpddvtISYLPLAHMFervvQTVVYCCGARVGFFQGNIRLLADDmntLKPTlfptvpRVLNRIYDkv 362
Cdd:PRK09088 167 FgvLGRVDAH---------SSFLCDAPMF----HIIGLITSVRPVLAVGGSILVSNG---FEPK------RTLGRLGD-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 363 qneaktplkkflLNLAVASKFKELQKG-IIRRDSFWDklifakiqASLGGRVRIIVTGAAPISAPVMTFFRAAmGCQVYE 441
Cdd:PRK09088 223 ------------PALGITHYFCVPQMAqAFRAQPGFD--------AAALRHLTALFTGGAPHAAEDILGWLDD-GIPMVD 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 442 AYGQTEctAGCTFTSPGDWT-----SGHVGAPLTCNYVKLEDVADMDyFSVNNEGEICIKGTNVFKGYLKDPEKTQEALD 516
Cdd:PRK09088 282 GFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVVDDQGND-CPAGVPGELLLRGPNLSPGYWRRPQATARAFT 358
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1622967304 517 SDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIE 559
Cdd:PRK09088 359 GDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIE 400
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
104-561 |
3.42e-26 |
|
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: 112.78 E-value: 3.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 104 RWLSYKQVSDRAEYLGSCLLHKGYksSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMV 183
Cdd:cd12118 28 RRYTWRQTYDRCRRLASALAALGI--SRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 184 ICDTPqkasvlienvekgftpslkvvilmdpFD-DDLKQRGEKSgieilslydaenlgkehfRKPVPPSPEDLSI-ICFT 261
Cdd:cd12118 106 FVDRE--------------------------FEyEDLLAEGDPD------------------FEWIPPADEWDPIaLNYT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 262 SGTTGDPKGAMITHQnivsnaSAFLKCVEH--TFEPTPDDVTISYLPLAHM----FervVQTVVYCCGARVGFFQGNIRL 335
Cdd:cd12118 142 SGTTGRPKGVVYHHR------GAYLNALANilEWEMKQHPVYLWTLPMFHCngwcF---PWTVAAVGGTNVCLRKVDAKA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 336 LADDMNTLKPTLFPTVPRVLNRIYDKVQNEAKtplkkfllnlavaskfkelqkgiirrdsfwdklifakiqaSLGGRVRI 415
Cdd:cd12118 213 IYDLIEKHKVTHFCGAPTVLNMLANAPPSDAR----------------------------------------PLPHRVHV 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 416 IVTGAAPisAPVMTFFRAAMGCQVYEAYGQTEcTAG----CTFTSPGDWTSGHVGAPLTC----NYVKLE--DVAD---M 482
Cdd:cd12118 253 MTAGAPP--PAAVLAKMEELGFDVTHVYGLTE-TYGpatvCAWKPEWDELPTEERARLKArqgvRYVGLEevDVLDpetM 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 483 DYFSVNNE--GEICIKGTNVFKGYLKDPEKTQEALdSDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIEN 560
Cdd:cd12118 330 KPVPRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENISSVEVEG 407
|
.
gi 1622967304 561 I 561
Cdd:cd12118 408 V 408
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
251-575 |
5.20e-26 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 112.84 E-value: 5.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 251 SPEDLSIICFTSGTTGDPKGAMITHQNIVSNasafLKCVEHTFEPTPDD---VTISYLPLAHMFERVVQTVVyccgarvg 327
Cdd:PRK08974 204 VPEDLAFLQYTGGTTGVAKGAMLTHRNMLAN----LEQAKAAYGPLLHPgkeLVVTALPLYHIFALTVNCLL-------- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 328 FFQGNIRlladdmntlkpTLFPTVPRVLNRIydkVQNEAKTPLKKF-----LLNLAVASK-FKELQkgiirrdsfwdkli 401
Cdd:PRK08974 272 FIELGGQ-----------NLLITNPRDIPGF---VKELKKYPFTAItgvntLFNALLNNEeFQELD-------------- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 402 FAKIQASLGGrvriivtgAAPISAPVMTFFRAAMGCQVYEAYGQTECT---AGCTFTSPGdwTSGHVGAPLTCNYVKLED 478
Cdd:PRK08974 324 FSSLKLSVGG--------GMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVNPYDLDY--YSGSIGLPVPSTEIKLVD 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 479 VADMDyFSVNNEGEICIKGTNVFKGYLKDPEKTQEALdSDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKI 558
Cdd:PRK08974 394 DDGNE-VPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMI-LVSGFNVYPNEI 470
|
330
....*....|....*..
gi 1622967304 559 ENIYNRSRPVLQIFVHG 575
Cdd:PRK08974 471 EDVVMLHPKVLEVAAVG 487
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
253-562 |
5.58e-26 |
|
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: 110.90 E-value: 5.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 253 EDLSIICFTSGTTGDPKGAMITHQNIVSNASAflkCVEhTFEPTPDDVTISYLPLAHM--FERVVQTVVYCCGARV--GF 328
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIG---SAL-NLGLTEDDNWLCALPLFHIsgLSILMRSVIYGMTVYLvdKF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 329 fqgNIRLLADDMNTLKPTLFPTVPRVLNRIYDKVQNEAKTPLKKFLLnlavaskfkelqkgiirrdsfwdklifakiqas 408
Cdd:cd05912 153 ---DAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRCILL--------------------------------- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 409 lggrvriivtGAAPISAPVMTFFRAaMGCQVYEAYGQTE-CTAGCTFtSPGDWTS--GHVGAPLTCNYVKLEDvadmDYF 485
Cdd:cd05912 197 ----------GGGPAPKPLLEQCKE-KGIPVYQSYGMTEtCSQIVTL-SPEDALNkiGSAGKPLFPVELKIED----DGQ 260
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622967304 486 SVNNEGEICIKGTNVFKGYLKDPEKTQEALDsDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENIY 562
Cdd:cd05912 261 PPYEVGEILLKGPNVTKGYLNRPDATEESFE-NGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVL 335
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
104-573 |
8.52e-26 |
|
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: 111.23 E-value: 8.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 104 RWLSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLyDTLGPEA-IVYIVNKADIAM 182
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARGVG--PGDRVAVYLPRSARLVAAMLAVLKAGAAYVPL-DPDYPADrLRYILEDAEPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 183 VICDTPqkasvlienvekgftpslkvviLMDPFDDDLKqrgeksGIEILSLYDAENLGkehfRKPVPPSPEDLSIICFTS 262
Cdd:cd12116 88 VLTDDA----------------------LPDRLPAGLP------VLLLALAAAAAAPA----APRTPVSPDDLAYVIYTS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 263 GTTGDPKGAMITHQNIVSnasaFLKCVEHTFEPTPDD----VT-----IS----YLPLahmfervvqtvvyCCGARVGFF 329
Cdd:cd12116 136 GSTGRPKGVVVSHRNLVN----FLHSMRERLGLGPGDrllaVTtyafdISllelLLPL-------------LAGARVVIA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 330 QGNI----RLLADDMNTLKPTLfptvprvlnriydkVQneaKTPlkkfllnlavaskfkelqkgiirrdSFWDKLIFAKI 405
Cdd:cd12116 199 PRETqrdpEALARLIEAHSITV--------------MQ---ATP-------------------------ATWRMLLDAGW 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 406 QASLGgrVRIIVTGAA--PISAPVMTffraAMGCQVYEAYGQTECT--AGCTFTSPGDwTSGHVGAPLTCNYVKLEDvAD 481
Cdd:cd12116 237 QGRAG--LTALCGGEAlpPDLAARLL----SRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLD-AA 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 482 MDYFSVNNEGEICIKGTNVFKGYLKDPEKTQEALDSDGWLH-------TGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIA 554
Cdd:cd12116 309 LRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQVKI-RGHRIE 387
|
490
....*....|....*....
gi 1622967304 555 PEKIENIYNRSRPVLQIFV 573
Cdd:cd12116 388 LGEIEAALAAHPGVAQAAV 406
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
98-561 |
4.38e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 109.87 E-value: 4.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 98 KPNQP-YRWL----SYKQVSDRAEYLGSCLLHKGYkSSPDQfVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIV 172
Cdd:PRK07786 30 QPDAPaLRFLgnttTWRELDDRVAALAGALSRRGV-GFGDR-VLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 173 YIVNKADIAMVICD---TPQKASVlienveKGFTPSLKVVILM-DPFDDDlkqrgeksgieILSLYDAENLGKEhfrkPV 248
Cdd:PRK07786 108 FLVSDCGAHVVVTEaalAPVATAV------RDIVPLLSTVVVAgGSSDDS-----------VLGYEDLLAEAGP----AH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 249 PPS--PEDL-SIICFTSGTTGDPKGAMITHQNIVSNAsafLKCVEHTFEPTPDDVTISYLPLAHMfervvqtvvyccgAR 325
Cdd:PRK07786 167 APVdiPNDSpALIMYTSGTTGRPKGAVLTHANLTGQA---MTCLRTNGADINSDVGFVGVPLFHI-------------AG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 326 VGffqgnirlladdmnTLKPTLFPTVPRVLNriydkvqneaktPLKKF----LLNLAVASKFkelqKGIIRRDSFWDKLI 401
Cdd:PRK07786 231 IG--------------SMLPGLLLGAPTVIY------------PLGAFdpgqLLDVLEAEKV----TGIFLVPAQWQAVC 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 402 FAKIQASLGGRVRIIVTGAAPISAPVMTFFRAAM-GCQVYEAYGQTECTAgCTFTSPGD---WTSGHVGAPLTCNYVKLE 477
Cdd:PRK07786 281 AEQQARPRDLALRVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEMSP-VTCMLLGEdaiRKLGSVGKVIPTVAARVV 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 478 DvADMDYFSVNNEGEICIKGTNVFKGYLKDPEKTQEALDSdGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEK 557
Cdd:PRK07786 360 D-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGENIYCAE 436
|
....
gi 1622967304 558 IENI 561
Cdd:PRK07786 437 VENV 440
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
211-542 |
2.24e-24 |
|
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: 107.75 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 211 LMDPFDDDLKQRGEKsGIEILSLYDAENLGKEHfrkPVPPS-PEDLSIICFTSGTTGDPKGAMITHQNIVSNASAflKCV 289
Cdd:cd05906 128 LVAEFAGLETLSGLP-GIRVLSIEELLDTAADH---DLPQSrPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG--KIQ 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 290 EHTFepTPDDVTISYLPLAHmfervVQTVVYCcgarvgffqgNIR---LLADDMNTLKPTLFPTVPRVLNRIyDKVQnEA 366
Cdd:cd05906 202 HNGL--TPQDVFLNWVPLDH-----VGGLVEL----------HLRavyLGCQQVHVPTEEILADPLRWLDLI-DRYR-VT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 367 KTPLKKFLLNLAVASkfkeLQKgiiRRDSFWDKlifakiqaslgGRVRIIVTGAAPISAPV-MTFFRAAMGCQVYE---- 441
Cdd:cd05906 263 ITWAPNFAFALLNDL----LEE---IEDGTWDL-----------SSLRYLVNAGEAVVAKTiRRLLRLLEPYGLPPdair 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 442 -AYGQTECTAGCTFTSP---GDWTSGH----VGAPLTCNYVKLEDVADmDYFSVNNEGEICIKGTNVFKGYLKDPEKTQE 513
Cdd:cd05906 325 pAFGMTETCSGVIYSRSfptYDHSQALefvsLGRPIPGVSMRIVDDEG-QLLPEGEVGRLQVRGPVVTKGYYNNPEANAE 403
|
330 340
....*....|....*....|....*....
gi 1622967304 514 ALDSDGWLHTGDIGrWLPNGTLKIIDRKK 542
Cdd:cd05906 404 AFTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
97-570 |
2.48e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 107.74 E-value: 2.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 97 RKPNQPYRW-----LSYKQVSDRAEYLGSCLLHKGYKSSPDQfVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAI 171
Cdd:PRK08314 22 RYPDKTAIVfygraISYRELLEEAERLAGYLQQECGVRKGDR-VLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 172 VYIVNKADIAMVICdtpqkASVLIENVEKGF-TPSLKVVIL---MDPFDDD--------LKQRGEKSGIEILSLYD-AEN 238
Cdd:PRK08314 101 AHYVTDSGARVAIV-----GSELAPKVAPAVgNLRLRHVIVaqySDYLPAEpeiavpawLRAEPPLQALAPGGVVAwKEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 239 LGKEHFRKPVPPSPEDLSIICFTSGTTGDPKGAMITHQNIVSNASAFlkcvEHTFEPTPDDVTISYLPLAHM--FERVVQ 316
Cdd:PRK08314 176 LAAGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGS----VLWSNSTPESVVLAVLPLFHVtgMVHSMN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 317 TVVYCCGARVGFFQGNIRLLADDMNTLKPTLFPTVPrvlnriydkvqneakTPLKKFLLNLAVASkfkelqkgiirRDsf 396
Cdd:PRK08314 252 APIYAGATVVLMPRWDREAAARLIERYRVTHWTNIP---------------TMVVDFLASPGLAE-----------RD-- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 397 wdklifakiQASLggrvRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTEcTAGCTFTSPGDWT-SGHVGAPLTCNYVK 475
Cdd:PRK08314 304 ---------LSSL----RYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTE-TMAQTHSNPPDRPkLQCLGIPTFGVDAR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 476 LEDVADMDYFSVNNEGEICIKGTNVFKGYLKDPEKTQEA---LDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKlAQGEY 552
Cdd:PRK08314 370 VIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMIN-ASGFK 448
|
490
....*....|....*...
gi 1622967304 553 IAPEKIENIYNRSRPVLQ 570
Cdd:PRK08314 449 VWPAEVENLLYKHPAIQE 466
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
250-541 |
2.66e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 106.61 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 250 PSPEDLSIICFTSGTTGDPKGAMITHQNIVSNasafLKCVEHTFEPTPDDVTISYLPLAHMFERVVQTVvyccgarvgff 329
Cdd:PRK07787 125 PDPDAPALIVYTSGTTGPPKGVVLSRRAIAAD----LDALAEAWQWTADDVLVHGLPLFHVHGLVLGVL----------- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 330 qGNIRLLADDMNTLKP-------------TLFPTVPRVLNRIYDkvqneaktplkkfllNLAVASKFkelqkgiirrdsf 396
Cdd:PRK07787 190 -GPLRIGNRFVHTGRPtpeayaqalseggTLYFGVPTVWSRIAA---------------DPEAARAL------------- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 397 wdklifakiqaslgGRVRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTSPGDWTSGHVGAPLTCNYVKL 476
Cdd:PRK07787 241 --------------RGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRL 306
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622967304 477 EDVAD----MDYFSVnneGEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRK 541
Cdd:PRK07787 307 VDEDGgpvpHDGETV---GELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRE 372
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
250-573 |
4.70e-24 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 106.68 E-value: 4.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 250 PSPEDLSIICFTSGTTGDPKGAMITHQNIVSNasaFLKCVEHtFEPTPDDVTISYLPLAHmfervvQTvvyccgarvGFF 329
Cdd:PRK13295 194 PGPDDVTQLIYTSGTTGEPKGVMHTANTLMAN---IVPYAER-LGLGADDVILMASPMAH------QT---------GFM 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 330 QGnirlladdmntlkpTLFPTVPR---VLNRIYDK------VQNE------AKTPlkkFLLNLAVASKFKelqkgiirrd 394
Cdd:PRK13295 255 YG--------------LMMPVMLGataVLQDIWDParaaelIRTEgvtftmASTP---FLTDLTRAVKES---------- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 395 sfwdklifAKIQASLggrvRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTECTAgCTFTSPGD---WTSGHVGAPLTC 471
Cdd:PRK13295 308 --------GRPVSSL----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA-VTLTKLDDpdeRASTTDGCPLPG 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 472 NYVKLEDvADMDYFSVNNEGEICIKGTNVFKGYLKDPEKTqeALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGE 551
Cdd:PRK13295 375 VEVRVVD-ADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGE 450
|
330 340
....*....|....*....|..
gi 1622967304 552 YIAPEKIENIYNRSRPVLQIFV 573
Cdd:PRK13295 451 NIPVVEIEALLYRHPAIAQVAI 472
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
104-562 |
6.26e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 106.17 E-value: 6.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 104 RWLSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMV 183
Cdd:PRK08316 35 RSWTYAELDAAVNRVAAALLDLGLK--KGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 184 ICDtpqkaSVLIENVEKGFTPSLKVVILMDPFDDDlkQRGEKSGIEILSLYDAENlgkehfrkPVPPSP----EDLSIIC 259
Cdd:PRK08316 113 LVD-----PALAPTAEAALALLPVDTLILSLVLGG--REAPGGWLDFADWAEAGS--------VAEPDVeladDDLAQIL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 260 FTSGTTGDPKGAMITHQNIVSNasaFLKCVeHTFEPTPDDVTISYLPLAHmfervvqtvvycCGARVGFFqgNIRLLADD 339
Cdd:PRK08316 178 YTSGTESLPKGAMLTHRALIAE---YVSCI-VAGDMSADDIPLHALPLYH------------CAQLDVFL--GPYLYVGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 340 MNTLKPTlfPTVPRVLNRIydkvqnEAKtplkkfllnlavaskfkelqkgiiRRDSF------WDKLI----FAKiqASL 409
Cdd:PRK08316 240 TNVILDA--PDPELILRTI------EAE------------------------RITSFfapptvWISLLrhpdFDT--RDL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 410 GGrVRIIVTGAAPISAPVMTFFRAAM-GCQVYEAYGQTECTAGCTFTSPGDwtsgHVGAPLTCN----YV--KLEDvADM 482
Cdd:PRK08316 286 SS-LRKGYYGASIMPVEVLKELRERLpGLRFYNCYGQTEIAPLATVLGPEE----HLRRPGSAGrpvlNVetRVVD-DDG 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 483 DYFSVNNEGEICIKGTNVFKGYLKDPEKTQEALdSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIEN-I 561
Cdd:PRK08316 360 NDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEaL 437
|
.
gi 1622967304 562 Y 562
Cdd:PRK08316 438 Y 438
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
248-575 |
1.70e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 105.12 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 248 VPPSPE-DLSIICFTSGTTGDPKGAMITHQNIVSNA----SAFLKCVEHtfeptpDDVTISYLPLAHMF-ERVVQTVVYC 321
Cdd:PRK06710 200 VPCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSNTlmgvQWLYNCKEG------EEVVLGVLPFFHVYgMTAVMNLSIM 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 322 CGARVGFF-QGNIRLLADDMNTLKPTLFPTVPRvlnrIYDKVQNeakTPLKKfllNLAVASkfkelqkgiirrdsfwdkl 400
Cdd:PRK06710 274 QGYKMVLIpKFDMKMVFEAIKKHKVTLFPGAPT----IYIALLN---SPLLK---EYDISS------------------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 401 ifakiqaslggrVRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTECTAgcTFTSPGDW---TSGHVGAPLTCNYVKLE 477
Cdd:PRK06710 325 ------------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSP--VTHSNFLWekrVPGSIGVPWPDTEAMIM 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 478 DVADMDYFSVNNEGEICIKGTNVFKGYLKDPEKTQEALdSDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEK 557
Cdd:PRK06710 391 SLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPRE 468
|
330
....*....|....*...
gi 1622967304 558 IENIYNRSRPVLQIFVHG 575
Cdd:PRK06710 469 VEEVLYEHEKVQEVVTIG 486
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
207-559 |
1.77e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 105.08 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 207 KVVILMDPFDDdLKQRGEKSGIEILSLydAENLGKEHFRkPVPPSPEDLSIICFTSGTTGDPKGAMITHQNIVSNASAFL 286
Cdd:PRK07768 110 KAVVVGEPFLA-AAPVLEEKGIRVLTV--ADLLAADPID-PVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMF 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 287 KCVEHTFEptpDDVTISYLPLAH-MfervvqtvvyccgARVGFFqgnirlladdmntlkptlfpTVPRVLNRIYDKVqne 365
Cdd:PRK07768 186 VAAEFDVE---TDVMVSWLPLFHdM-------------GMVGFL--------------------TVPMYFGAELVKV--- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 366 akTPLkKFLlnlavaskfkelqkgiiRRDSFWDKLI------------FAkiqASLGGR---------------VRIIVT 418
Cdd:PRK07768 227 --TPM-DFL-----------------RDPLLWAELIskyrgtmtaapnFA---YALLARrlrrqakpgafdlssLRFALN 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 419 GAAPIS-APVMTFFRA---------AMGCqvyeAYGQTECTAGCTFTSPGD--------------------WTSGHV--- 465
Cdd:PRK07768 284 GAEPIDpADVEDLLDAgarfglrpeAILP----AYGMAEATLAVSFSPCGAglvvdevdadllaalrravpATKGNTrrl 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 466 ---GAPLTCNYVKL--EDVADMDYFSVnneGEICIKGTNVFKGYLkDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDR 540
Cdd:PRK07768 360 atlGPPLPGLEVRVvdEDGQVLPPRGV---GVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGR 435
|
410
....*....|....*....
gi 1622967304 541 KKNIFKLAqGEYIAPEKIE 559
Cdd:PRK07768 436 VKDVIIMA-GRNIYPTDIE 453
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
106-568 |
3.04e-23 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 103.10 E-value: 3.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGykSSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVIC 185
Cdd:cd05945 17 LTYRELKERADALAAALASLG--LDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPALLIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 DtpqkasvlienvekgftpslkvvilmdpfdddlkqrgeksgieilslydaenlgkehfrkpvppsPEDLSIICFTSGTT 265
Cdd:cd05945 95 D-----------------------------------------------------------------GDDNAYIIFTSGST 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 266 GDPKGAMITHQNIVS----NASAFLKcvehtfepTPDDVTISYLPLAhmFERVVQTVVYC--CGArvgffqgnirlladd 339
Cdd:cd05945 110 GRPKGVQISHDNLVSftnwMLSDFPL--------GPGDVFLNQAPFS--FDLSVMDLYPAlaSGA--------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 340 mntlkpTLFPtVPRvlnriydkvqneaktplkkfllnlAVASKFKELQKGIIRRD--------SFWDKLI----FAkiQA 407
Cdd:cd05945 165 ------TLVP-VPR------------------------DATADPKQLFRFLAEHGitvwvstpSFAAMCLlsptFT--PE 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 408 SLGGRVRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCTFT-----SPGDWTSGHVGAPLTCNYVKLEDvADM 482
Cdd:cd05945 212 SLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIevtpeVLDGYDRLPIGYAKPGAKLVILD-EDG 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 483 DYFSVNNEGEICIKGTNVFKGYLKDPEKTQEALDSD---GWLHTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIE 559
Cdd:cd05945 291 RPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIELEEIE 369
|
....*....
gi 1622967304 560 NIYNRSRPV 568
Cdd:cd05945 370 AALRQVPGV 378
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
106-560 |
5.67e-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: 102.03 E-value: 5.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQV---SDR-AEYLGSCLLHKGYKsspdqfVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIA 181
Cdd:cd05972 1 WSFRELkreSAKaANVLAKLGLRKGDR------VAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 182 MVICDTpqkasvlienvekgftpslkvvilmdpfdddlkqrgeksgieilslydaenlgkehfrkpvppspEDLSIICFT 261
Cdd:cd05972 75 AIVTDA-----------------------------------------------------------------EDPALIYFT 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 262 SGTTGDPKGAMITHqnivsnasaflkcvehtfeptpddvtiSYlPLAHMfervvQTVVYCCGARVGFFQGNIRLLADDMN 341
Cdd:cd05972 90 SGTTGLPKGVLHTH---------------------------SY-PLGHI-----PTAAYWLGLRPDDIHWNIADPGWAKG 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 342 TLKPTLFPT---VPRVLN--------RIYDKVQNE-------AKTPLKKFLLNLAVASKFKELqkgiirrdsfwdklifa 403
Cdd:cd05972 137 AWSSFFGPWllgATVFVYegprfdaeRILELLERYgvtsfcgPPTAYRMLIKQDLSSYKFSHL----------------- 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 404 kiqaslggrvRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTSPGDWTSGHVGAPLTCNYVKLEDvADMD 483
Cdd:cd05972 200 ----------RLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIID-DDGR 268
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622967304 484 YFSVNNEGEICIKGTNV--FKGYLKDPEKTQEALdSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKlAQGEYIAPEKIEN 560
Cdd:cd05972 269 ELPPGEEGDIAIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVES 345
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
254-576 |
8.48e-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: 99.71 E-value: 8.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 254 DLSIICFTSGTTGDPKGAMITHQNIVSNASAFlkcveHTFEP-TPDDVTISYLPLAHM--FERVVQTVVycCGARVGFFQ 330
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGL-----HSRLGfGGGDSWLLSLPLYHVggLAILVRSLL--AGAELVLLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 331 GNiRLLADDMNTLKPTLFPTVPrvlnriydkvqneakTPLKKFLLNLAVASKFKelqkgiirrdsfwdklifakiqaslg 410
Cdd:cd17630 74 RN-QALAEDLAPPGVTHVSLVP---------------TQLQRLLDSGQGPAALK-------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 411 gRVRIIVTGAAPISAPVMTFFrAAMGCQVYEAYGQTEcTAGCTFTS-PGDWTSGHVGAPLtcNYVKLEDVADmdyfsvnn 489
Cdd:cd17630 112 -SLRAVLLGGAPIPPELLERA-ADRGIPLYTTYGMTE-TASQVATKrPDGFGRGGVGVLL--PGRELRIVED-------- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 490 eGEICIKGTNVFKGYLKDPEktQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENIYNRSRPVL 569
Cdd:cd17630 179 -GEIWVGGASLAMGYLRGQL--VPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAVR 254
|
....*..
gi 1622967304 570 QIFVHGE 576
Cdd:cd17630 255 DAFVVGV 261
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
251-541 |
1.02e-22 |
|
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: 101.85 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 251 SPEDLSIICFTSGTTGDPKGAMITHQNIVSNASAFLKCVE------------HTFeptpdDVTI--SYLPLAHMFervvq 316
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGltsesrvlqfasYTF-----DVSIleIFTTLAAGG----- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 317 TVvyCCGARvgffqgNIRL--LADDMNTLKPT---LFPTVPRVLNRiydkvqneAKTPlkkfllnlavaskfkelqkgii 391
Cdd:cd05918 174 CL--CIPSE------EDRLndLAGFINRLRVTwafLTPSVARLLDP--------EDVP---------------------- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 392 rrdsfwdklifakiqaslggRVRIIVTGAAPISAPVMTFFraAMGCQVYEAYGQTECTAGCTFTSPG-DWTSGHVGAPLT 470
Cdd:cd05918 216 --------------------SLRTLVLGGEALTQSDVDTW--ADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRPLG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 471 CN-YVKleDVADMDYFS-VNNEGEICIKGTNVFKGYLKDPEKTQEA-LDSDGWLH------------TGDIGRWLPNGTL 535
Cdd:cd05918 274 ATcWVV--DPDNHDRLVpIGAVGELLIEGPILARGYLNDPEKTAAAfIEDPAWLKqegsgrgrrlyrTGDLVRYNPDGSL 351
|
....*.
gi 1622967304 536 KIIDRK 541
Cdd:cd05918 352 EYVGRK 357
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
178-561 |
1.22e-22 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 102.61 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 178 ADIAMVICDT-PQKASVLIENVEKGFTPSLKVVILMDPFDDDLKqRGEKSGIEILSLYDAENLgkehfrkPVPP-SPEDL 255
Cdd:PLN02574 129 GEIKKRVVDCsVGLAFTSPENVEKLSPLGVPVIGVPENYDFDSK-RIEFPKFYELIKEDFDFV-------PKPViKQDDV 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 256 SIICFTSGTTGDPKGAMITHQNIVSNASAFLKCVEHTFE-PTPDDVTISYLPLAHMFERVVQTV-VYCCGARVGFFQgni 333
Cdd:PLN02574 201 AAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEyPGSDNVYLAALPMFHIYGLSLFVVgLLSLGSTIVVMR--- 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 334 RLLADDM----NTLKPTLFPTVPRVLNRIYDKVQNEAKTPLKKfllnlavaskfkelqkgiirrdsfwdklifakiqasl 409
Cdd:PLN02574 278 RFDASDMvkviDRFKVTHFPVVPPILMALTKKAKGVCGEVLKS------------------------------------- 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 410 ggrVRIIVTGAAPISAP-VMTFFRAAMGCQVYEAYGQTECTAGCT--FTSPGDWTSGHVGAPLTCNYVKLEDVADMDYFS 486
Cdd:PLN02574 321 ---LKQVSCGAAPLSGKfIQDFVQTLPHVDFIQGYGMTESTAVGTrgFNTEKLSKYSSVGLLAPNMQAKVVDWSTGCLLP 397
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622967304 487 VNNEGEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIENI 561
Cdd:PLN02574 398 PGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQIAPADLEAV 471
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
106-577 |
1.29e-22 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 101.58 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYKSspDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVIC 185
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLAALGVKK--GDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLIT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 DtpqkasvlienveKGFTPSLKVVILMDpFDDdlKQRGEKSGIEILSLYDAEnlgkehfrkpvppspeDLSIICFTSGTT 265
Cdd:PRK03640 106 D-------------DDFEAKLIPGISVK-FAE--LMNGPKEEAEIQEEFDLD----------------EVATIMYTSGTT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 266 GDPKGAMITHQNIVSNA--SAF---LkcvehtfepTPDDVTISYLPLAHM--FERVVQTVVYccGARVGFFQgniRLLAD 338
Cdd:PRK03640 154 GKPKGVIQTYGNHWWSAvgSALnlgL---------TEDDCWLAAVPIFHIsgLSILMRSVIY--GMRVVLVE---KFDAE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 339 DMNTL----KPTLFPTVPRVLNRIYDKVQnEAKTPlkkfllnlavaskfkelqkgiirrDSFwdklifakiqaslggrvR 414
Cdd:PRK03640 220 KINKLlqtgGVTIISVVSTMLQRLLERLG-EGTYP------------------------SSF-----------------R 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 415 IIVTGAAPISAPVMTffraamGCQ-----VYEAYGQTE-CTAGCTFtSPGDWTS--GHVGAPLTCNYVKLEDvaDMDYFS 486
Cdd:PRK03640 258 CMLLGGGPAPKPLLE------QCKekgipVYQSYGMTEtASQIVTL-SPEDALTklGSAGKPLFPCELKIEK--DGVVVP 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 487 VNNEGEICIKGTNVFKGYLKDPEKTQEALDsDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENIYNRSR 566
Cdd:PRK03640 329 PFEEGEIVVKGPNVTKGYLNREDATRETFQ-DGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHP 406
|
490
....*....|.
gi 1622967304 567 PVLQIFVHGES 577
Cdd:PRK03640 407 GVAEAGVVGVP 417
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
252-564 |
6.68e-22 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 97.94 E-value: 6.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 252 PEDLSIICFTSGTTGDPKGAMITHQNIVSNAsaflKCVEHTFEPTPDDVTISYLPLAHMFERVVQTVVyccgarvGFFQG 331
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNA----WMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLT-------PLASG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 332 NIRLLADDMNTLKPTLFPTVPRVLNRIydkvqneaktplkKFLLNLAVASKFKELQKGIIRRDSfwdklifakiqaslgG 411
Cdd:cd05944 70 AHVVLAGPAGYRNPGLFDNFWKLVERY-------------RITSLSTVPTVYAALLQVPVNADI---------------S 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 412 RVRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTSP-GDWTSGHVGAPLTCNYVKLEdVADMDYF----- 485
Cdd:cd05944 122 SLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIK-VLDGVGRllrdc 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622967304 486 SVNNEGEICIKGTNVFKGYLKDpEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENIYNR 564
Cdd:cd05944 201 APDEVGEICVAGPGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLR 277
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
254-561 |
8.39e-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: 96.96 E-value: 8.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 254 DLSIICFTSGTTGDPKGAMITHQNIVSNASAFLkcveHTFEPTPDDVTISYLPLAHMFERVVQTVVYCCGARvgffqgNI 333
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLI----HAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGA------NV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 334 RL-------LADDMNTLKPTLFPTVPRVLNRIYDKVqneAKTPLKkfllnlavaskfkelqkgiirrdsfwdklifakiQ 406
Cdd:cd17637 71 VMekfdpaeALELIEEEKVTLMGSFPPILSNLLDAA---EKSGVD----------------------------------L 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 407 ASLGgrvriIVTGaapISAP-VMTFFRAAMGCQVYEAYGQTEcTAGCTFTSPGDWTSGHVGAPLTCNYVKLEDvaDMDYF 485
Cdd:cd17637 114 SSLR-----HVLG---LDAPeTIQRFEETTGATFWSLYGQTE-TSGLVTLSPYRERPGSAGRPGPLVRVRIVD--DNDRP 182
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622967304 486 S-VNNEGEICIKGTNVFKGYLKDPEKTQEALDsDGWLHTGDIGRWLPNGTLKIIDRK--KNIFKlAQGEYIAPEKIENI 561
Cdd:cd17637 183 VpAGETGEIVVRGPLVFQGYWNLPELTAYTFR-NGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKV 259
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
74-678 |
2.65e-21 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 99.54 E-value: 2.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 74 ATTMYEVFQRGLAISDNGPCLGYRKPNQPYRWLSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACY 153
Cdd:PTZ00297 426 VRSLGEMWERSVTRHSTFRCLGQTSESGESEWLTYGTVDARARELGSGLLALGVR--PGDVIGVDCEASRNIVILEVACA 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 154 TYSMVAVPLYDTlgPEAIVYIVNKADIAMVICDTPQKASVLIENvekgfTPSLKVVILMDPFDDDLKQRGEKS-GIEILS 232
Cdd:PTZ00297 504 LYGFTTLPLVGK--GSTMRTLIDEHKIKVVFADRNSVAAILTCR-----SRKLETVVYTHSFYDEDDHAVARDlNITLIP 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 233 LYDAENLGKehfRKPVPPSPEDLSIICFT-------SGTTGDPKGAMITHQNIVSNASAFL--KCVEHTFEptpDDVTIS 303
Cdd:PTZ00297 577 YEFVEQKGR---LCPVPLKEHVTTDTVFTyvvdnttSASGDGLAVVRVTHADVLRDISTLVmtGVLPSSFK---KHLMVH 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 304 YLPLAHMFERVVQTVVYCCGARVGFFQGniRLLADDMNTLKPTLFPTVPRVL--NRIYDKVQNEAKTPLKKFLLNLAVas 381
Cdd:PTZ00297 651 FTPFAMLFNRVFVLGLFAHGSAVATVDA--AHLQRAFVKFQPTILVAAPSLFstSRLQLSRANERYSAVYSWLFERAF-- 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 382 kfkELQKGII---RRDSFWDKLIFAK-IQASLGGRVRIIVTGAAPISApvmtffraamgcqvyeAYGQTECTAGCTftsp 457
Cdd:PTZ00297 727 ---QLRSRLInihRRDSSLLRFIFFRaTQELLGGCVEKIVLCVSEEST----------------SFSLLEHISVCY---- 783
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 458 gdwtsghvgAPLTCnyvkledvadmDYFSVNNEGEICIKGTNVfKGYLKDPEKTQEALDSDGW-----------LHTGDI 526
Cdd:PTZ00297 784 ---------VPCLR-----------EVFFLPSEGVFCVDGTPA-PSLQVDLEPFDEPSDGAGIgqlvlakkgepRRTLPI 842
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 527 -GRWLPNGTLKIIDRKKNIFKLAQGEYIAPEKIENIYNRSRPVLQIFVHGESLRSSLVGVVVPDPDV----LPSFAAKLG 601
Cdd:PTZ00297 843 aAQWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRPIIAIVSPNRDTVefewRQSHCMGEG 922
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 602 VKGSfEELCQNQVVRKA---ILEDLQKIGKESGLKTFEQVKAVFLHPEPFSIENGLLTPTLKAKRGELSKYFRTQIDSLY 678
Cdd:PTZ00297 923 GGPA-RQLGWTELVAYAsslLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIERFY 1001
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
135-575 |
2.80e-21 |
|
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: 97.95 E-value: 2.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 135 VGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVICDTPQKASVLIEN-VEKGFTPSLKVVI--- 210
Cdd:cd05970 75 VMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDNIPEEIEKaAPECPSKPKLVWVgdp 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 211 LMDPFDDDLKQRGEKSGIeilslydaenlgkehFRKPVPPSP---EDLSIICFTSGTTGDPKgaMITHQNIVSNASAFLK 287
Cdd:cd05970 155 VPEGWIDFRKLIKNASPD---------------FERPTANSYpcgEDILLVYFSSGTTGMPK--MVEHDFTYPLGHIVTA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 288 CVEHTFEPTPDDVTISYLPLAhmfeRVVQTVVY---CCGARVGFFqgnirlladDMNTLKPtlfptvprvlNRIYDKVQN 364
Cdd:cd05970 218 KYWQNVREGGLHLTVADTGWG----KAVWGKIYgqwIAGAAVFVY---------DYDKFDP----------KALLEKLSK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 365 EAKTPLkkfllnLAVASKFKELqkgiIRRD-SFWDkliFAKIqaslggrvRIIVTGAAPISAPVMTFFRAAMGCQVYEAY 443
Cdd:cd05970 275 YGVTTF------CAPPTIYRFL----IREDlSRYD---LSSL--------RYCTTAGEALNPEVFNTFKEKTGIKLMEGF 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 444 GQTECTAgCTFTSPG-DWTSGHVGAPLTCNYVKLEDvADMDYFSVNNEGEICI-----KGTNVFKGYLKDPEKTQEALdS 517
Cdd:cd05970 334 GQTETTL-TIATFPWmEPKPGSMGKPAPGYEIDLID-REGRSCEAGEEGEIVIrtskgKPVGLFGGYYKDAEKTAEVW-H 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622967304 518 DGWLHTGDIGRWLPNGTLKIIDRKKNIFKlAQGEYIAPEKIENIYNRSRPVLQIFVHG 575
Cdd:cd05970 411 DGYYHTGDAAWMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVESALIQHPAVLECAVTG 467
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
106-573 |
3.90e-21 |
|
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: 97.27 E-value: 3.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELA------CYtysmvaVPLYDTLGPEAIVYIVNKAD 179
Cdd:cd12117 23 LTYAELNERANRLARRLRAAGVG--PGDVVGVLAERSPELVVALLAvlkagaAY------VPLDPELPAERLAFMLADAG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 180 IAMVICDtpqkasvlienveKGFTPSLKVVILMDPFDDDLKQRgeksgieilslyDAENLgkehfrkPVPPSPEDLSIIC 259
Cdd:cd12117 95 AKVLLTD-------------RSLAGRAGGLEVAVVIDEALDAG------------PAGNP-------AVPVSPDDLAYVM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 260 FTSGTTGDPKGAMITHQNIVSnasaflkCVEHT--FEPTPDDVTISYLPL---AHMFErvvqtvVYCC---GARVgffqg 331
Cdd:cd12117 143 YTSGSTGRPKGVAVTHRGVVR-------LVKNTnyVTLGPDDRVLQTSPLafdASTFE------IWGAllnGARL----- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 332 nirLLADdmntlkptlfPTVPRVLNRIYDKVQNEAKTPLkkFLlnlaVASKFKELqkgiirrdsfwdklifAKIQASLGG 411
Cdd:cd12117 205 ---VLAP----------KGTLLDPDALGALIAEEGVTVL--WL----TAALFNQL----------------ADEDPECFA 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 412 RVRIIVTGAAPISAP-VMTFFRAAMGCQVYEAYGQTECTagcTFTS-----PGDWTSGHV--GAPL--TCNYVkledvad 481
Cdd:cd12117 250 GLRELLTGGEVVSPPhVRRVLAACPGLRLVNGYGPTENT---TFTTshvvtELDEVAGSIpiGRPIanTRVYV------- 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 482 MDYFS----VNNEGEICIKGTNVFKGYLKDPEKTQEALDSDGWL------HTGDIGRWLPNGTLKIIDRKKNIFKLaQGE 551
Cdd:cd12117 320 LDEDGrpvpPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI-RGF 398
|
490 500
....*....|....*....|..
gi 1622967304 552 YIAPEKIENIYNRSRPVLQIFV 573
Cdd:cd12117 399 RIELGEIEAALRAHPGVREAVV 420
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
141-561 |
7.71e-21 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 96.68 E-value: 7.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 141 NRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVICDtpQKASVLIENVEKGFTPSLKVVILMDPfdddlk 220
Cdd:PRK08008 71 NCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTS--AQFYPMYRQIQQEDATPLRHICLTRV------ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 221 QRGEKSGIeiLSLYDAENLGKEHFRKPVPPSPEDLSIICFTSGTTGDPKGAMITHQNIVSNA--SAFLKCVehtfepTPD 298
Cdd:PRK08008 143 ALPADDGV--SSFTQLKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGyySAWQCAL------RDD 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 299 DVTISYLPLAHM-FERVVQTVVYCCGARVGF--------FQGNIRLLaddmntlKPTLFPTVPRVLNRIY--DKVQNEAK 367
Cdd:PRK08008 215 DVYLTVMPAFHIdCQCTAAMAAFSAGATFVLlekysaraFWGQVCKY-------RATITECIPMMIRTLMvqPPSANDRQ 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 368 TPLKK--FLLNLAVASKfkelqkgiirrdsfwdklifakiQAslggrvriivtgaapisapvmtfFRAAMGCQVYEAYGQ 445
Cdd:PRK08008 288 HCLREvmFYLNLSDQEK-----------------------DA-----------------------FEERFGVRLLTSYGM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 446 TECTAGCTFTSPGD---WTSghVGAPLTCNYVKLEDvADMDYFSVNNEGEICIKGT---NVFKGYLKDPEKTQEALDSDG 519
Cdd:PRK08008 322 TETIVGIIGDRPGDkrrWPS--IGRPGFCYEAEIRD-DHNRPLPAGEIGEICIKGVpgkTIFKEYYLDPKATAKVLEADG 398
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1622967304 520 WLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENI 561
Cdd:PRK08008 399 WLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVELENI 439
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
106-575 |
1.39e-20 |
|
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: 95.65 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVIc 185
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLR--PGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAV- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 dtpqkASVLIENVEKGFTPSLKVVILmdpfdDDLKQRGEksgieilslydAENLGKehFRKPVPPSPEDLSIICFTSGTT 265
Cdd:cd05923 106 -----IAVDAQVMDAIFQSGVRVLAL-----SDLVGLGE-----------PESAGP--LIEDPPREPEQPAFVFYTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 266 GDPKGAMITHQNIVSNASAFLKCVEHTFepTPDDVTISYLPLAHMfervvqtvvyccgarVGFFqgNIRLLADDMNTlkp 345
Cdd:cd05923 163 GLPKGAVIPQRAAESRVLFMSTQAGLRH--GRHNVVLGLMPLYHV---------------IGFF--AVLVAALALDG--- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 346 tlFPTVPRvlnriYDKVQNEAKTPLKKFLLNL-AVASKFKELQKGII---RRDSFWDKLIFAkiqaslggrvriivtGAA 421
Cdd:cd05923 221 --TYVVVE-----EFDPADALKLIEQERVTSLfATPTHLDALAAAAEfagLKLSSLRHVTFA---------------GAT 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 422 pISAPVMTFFRAAMGCQVYEAYGQTECTagcTFTSPGDWTSGHVGAPLTCNYVKLEDV--ADMDYFSVNNEGEICIK--G 497
Cdd:cd05923 279 -MPDAVLERVNQHLPGEKVNIYGTTEAM---NSLYMRDARTGTEMRPGFFSEVRIVRIggSPDEALANGEEGELIVAaaA 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622967304 498 TNVFKGYLKDPEKTQEALdSDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENIYNRSRPVLQIFVHG 575
Cdd:cd05923 355 DAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIG 430
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
253-561 |
2.10e-20 |
|
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: 93.09 E-value: 2.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 253 EDLSIICFTSGTTGDPKGAMITHQNIVSNASAFLKcveHTFEPTPDDVTISYLPLAHMFERV-VQTVVYCCGARVgFFQG 331
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQK---EGLNWVVGDVTYLPLPATHIGGLWwILTCLIHGGLCV-TGGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 332 NIRL--LADDMNTLKPTLFPTVPRVLNRIYDKVQNEAKTPLKkflLNLavaskfkelqkgiirrdsfwdklifakiqasl 409
Cdd:cd17635 77 NTTYksLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPS---LRL-------------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 410 ggrvrIIVTGAAPISAPVmTFFRAAMGCQVYEAYGQTECTAGCTF-TSPGDWTSGHVGAPLTCNYVKledVADMDYFSVN 488
Cdd:cd17635 122 -----IGYGGSRAIAADV-RFIEATGLTNTAQVYGLSETGTALCLpTDDDSIEINAVGRPYPGVDVY---LAATDGIAGP 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622967304 489 N--EGEICIKGTNVFKGYLKDPEKTQEALdSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENI 561
Cdd:cd17635 193 SasFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERI 265
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
106-573 |
7.50e-20 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 93.93 E-value: 7.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLhkGYKSSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVIC 185
Cdd:PLN03102 40 FTWPQTYDRCCRLAASLI--SLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 D---TPQKASVLIENVEKGFTPSLKVVILMD------PFDDDLK-----QRGEKSGIEILSLYDAENlgkEHfrkpvppS 251
Cdd:PLN03102 118 DrsfEPLAREVLHLLSSEDSNLNLPVIFIHEidfpkrPSSEELDyecliQRGEPTPSLVARMFRIQD---EH-------D 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 252 PEDLSiicFTSGTTGDPKGAMITHQNI-VSNASAFLKCVEHTFEptpddVTISYLPlahMFERVVQTVVYCCGARVGffq 330
Cdd:PLN03102 188 PISLN---YTSGTTADPKGVVISHRGAyLSTLSAIIGWEMGTCP-----VYLWTLP---MFHCNGWTFTWGTAARGG--- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 331 gnirlladdmnTLKPTLFPTVPRvlnrIYDKVQNEAKTPLKkfllnlAVASKFKELQKGIiRRDsfwdklifakiQASLG 410
Cdd:PLN03102 254 -----------TSVCMRHVTAPE----IYKNIEMHNVTHMC------CVPTVFNILLKGN-SLD-----------LSPRS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 411 GRVRIIVTGAAPISAPVMTFFRaaMGCQVYEAYGQTECTAGCTFTSPGD-WTS--GHVGAPLTCNY-VKLEDVADMDyfs 486
Cdd:PLN03102 301 GPVHVLTGGSPPPAALVKKVQR--LGFQVMHAYGLTEATGPVLFCEWQDeWNRlpENQQMELKARQgVSILGLADVD--- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 487 VNNE-------------GEICIKGTNVFKGYLKDPEKTQEALdSDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYI 553
Cdd:PLN03102 376 VKNKetqesvprdgktmGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGENI 453
|
490 500
....*....|....*....|
gi 1622967304 554 APEKIENIYNRSRPVLQIFV 573
Cdd:PLN03102 454 SSVEVENVLYKYPKVLETAV 473
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
106-561 |
1.00e-19 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 92.72 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVIC 185
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVR--PGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 DTPQkasvlienvekgftPSLKVVILMDPFDDDLKQRGEKsgieilslydaenlgkehFRKPVPPSPEDLSIICFTSGTT 265
Cdd:cd12114 91 DGPD--------------AQLDVAVFDVLILDLDALAAPA------------------PPPPVDVAPDDLAYVIFTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 266 GDPKGAMITHQNivsnASAFLKCVEHTFEPTPDDVTISYLPLAHMFErvvqtvVY------CCGARVGFFQGNIR----L 335
Cdd:cd12114 139 GTPKGVMISHRA----ALNTILDINRRFAVGPDDRVLALSSLSFDLS------VYdifgalSAGATLVLPDEARRrdpaH 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 336 LADDMNTLKPTLFPTVPRVLNRIYDKVQNEAKTPLKkflLNLAVASkfkelqkGiirrDsfWdklifakIQASLGGRVRI 415
Cdd:cd12114 209 WAELIERHGVTLWNSVPALLEMLLDVLEAAQALLPS---LRLVLLS-------G----D--W-------IPLDLPARLRA 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 416 IVTGAAPISapvmtffraaMGcqvyeayGQTECTAGCTF----TSPGDWTSGHVGAPLTCNYvkledvadmdYFSVNN-- 489
Cdd:cd12114 266 LAPDARLIS----------LG-------GATEASIWSIYhpidEVPPDWRSIPYGRPLANQR----------YRVLDPrg 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 490 -------EGEICIKGTNVFKGYLKDPEKTQEAL--DSDG--WLHTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKI 558
Cdd:cd12114 319 rdcpdwvPGELWIGGRGVALGYLGDPELTAARFvtHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKV-RGYRIELGEI 397
|
...
gi 1622967304 559 ENI 561
Cdd:cd12114 398 EAA 400
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
106-575 |
3.05e-19 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 91.77 E-value: 3.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLlHKGYKSSPDQFVGIFAQNRPEWIISELAcyTYSMVAV--PLYDTLGPEAIVYIVNKADIAMV 183
Cdd:PRK05620 39 TTFAAIGARAAALAHAL-HDELGITGDQRVGSMMYNCAEHLEVLFA--VACMGAVfnPLNKQLMNDQIVHIINHAEDEVI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 184 ICDtPQKASVLIENVEKgfTPSLKVVILMDPFDDDLKQRGEKSGIEILSlYDAENLGKE-HFRKPVPPSpEDLSIICFTS 262
Cdd:PRK05620 116 VAD-PRLAEQLGEILKE--CPCVRAVVFIGPSDADSAAAHMPEGIKVYS-YEALLDGRStVYDWPELDE-TTAAAICYST 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 263 GTTGDPKGAMITHQNI--------------VSNASAFLKCVehtfeptpddvtisylPLAHMFERVVQTVVYCCGARVGF 328
Cdd:PRK05620 191 GTTGAPKGVVYSHRSLylqslslrttdslaVTHGESFLCCV----------------PIYHVLSWGVPLAAFMSGTPLVF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 329 FQGNIR--LLADDMNTLKPTLFPTVPRVLNRIydkVQNEAKTPLKKFLLnlavaskfkelqkgiirrdsfwdklifakiq 406
Cdd:PRK05620 255 PGPDLSapTLAKIIATAMPRVAHGVPTLWIQL---MVHYLKNPPERMSL------------------------------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 407 aslggrvRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTSPGDWTSGHVGA---------PLTCNYVKLE 477
Cdd:PRK05620 301 -------QEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEARWayrvsqgrfPASLEYRIVN 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 478 D---VADMDyfsvNNEGEICIKGTNVFKGYLKDP----------------EKTQEALDSDGWLHTGDIGRWLPNGTLKII 538
Cdd:PRK05620 374 DgqvMESTD----RNEGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIH 449
|
490 500 510
....*....|....*....|....*....|....*..
gi 1622967304 539 DRKKNIFKlAQGEYIAPEKIENIYNRSRPVLQIFVHG 575
Cdd:PRK05620 450 DRARDVIR-SGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
106-559 |
4.74e-19 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 90.45 E-value: 4.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVIC 185
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVG--PESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 DtpqkasvlienvekgftpslkvvilmdpfdddlkqrgeksgieilslydaenlgkehfrkpvppsPEDLSIICFTSGTT 265
Cdd:cd12115 103 D-----------------------------------------------------------------PDDLAYVIYTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 266 GDPKGAMITHqnivSNASAFLKCVEHTFepTPDDVT-------ISY-LPLAHMFervvqtVVYCCGARVgFFQGNIRLLA 337
Cdd:cd12115 118 GRPKGVAIEH----RNAAAFLQWAAAAF--SAEELAgvlastsICFdLSVFELF------GPLATGGKV-VLADNVLALP 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 338 DDMNTLKPTLFPTVPRVLNRI--YDKVQNEAKTplkkflLNLAVASKFKELqkgiirrdsfwdkliFAKIQASLGGRvri 415
Cdd:cd12115 185 DLPAAAEVTLINTVPSAAAELlrHDALPASVRV------VNLAGEPLPRDL---------------VQRLYARLQVE--- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 416 ivtgaapisapvmtffraamgcQVYEAYGQTECTAGCTFT--SPGDWTSGHVGAPLTCNYVKLEDvADMDYFSVNNEGEI 493
Cdd:cd12115 241 ----------------------RVVNLYGPSEDTTYSTVApvPPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVPGEL 297
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622967304 494 CIKGTNVFKGYLKDPEKTQEALDSDGWL------HTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIE 559
Cdd:cd12115 298 YIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIE 368
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
92-554 |
4.77e-19 |
|
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: 91.34 E-value: 4.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 92 PCLGYRKPNQPYRWLSYKQVSDRAEYLGSCLLhkGYKSSPDQFVGIFAQNRPEWIISELACYTysmVAVPLydtlGPEAI 171
Cdd:cd05921 12 TWLAEREGNGGWRRVTYAEALRQVRAIAQGLL--DLGLSAERPLLILSGNSIEHALMALAAMY---AGVPA----APVSP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 172 VYIVNKADIAMV--ICDTPQKASVLIENVEKgFTPSLKVVILMDPfdDDLKQRGEKSGIEILSLydaENLGKEHFRKPVP 249
Cdd:cd05921 83 AYSLMSQDLAKLkhLFELLKPGLVFAQDAAP-FARALAAIFPLGT--PLVVSRNAVAGRGAISF---AELAATPPTAAVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 250 PS-----PEDLSIICFTSGTTGDPKGAMITHQNIVSNASAFLKCveHTFEPTPDDVTISYLPLAHMF--ERVVQTVVYCC 322
Cdd:cd05921 157 AAfaavgPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQT--YPFFGEEPPVLVDWLPWNHTFggNHNFNLVLYNG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 323 GA--------RVGFFQGNIRLLADdmntLKPTLFPTVPRVLNRIYDKVQNEAkTPLKKFLLNLAVAskfkeLQKGIIRRD 394
Cdd:cd05921 235 GTlyiddgkpMPGGFEETLRNLRE----ISPTVYFNVPAGWEMLVAALEKDE-ALRRRFFKRLKLM-----FYAGAGLSQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 395 SFWDKLIfAKIQASLGGRVRIivtgaapisapvmtffraamgcqvYEAYGQTECTAGCTFTSPGDWTSGHVGAPLTCNYV 474
Cdd:cd05921 305 DVWDRLQ-ALAVATVGERIPM------------------------MAGLGATETAPTATFTHWPTERSGLIGLPAPGTEL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 475 KLedvadmdyFSVNNEGEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWL----PNGTLKIIDRKKNIFKLAQG 550
Cdd:cd05921 360 KL--------VPSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpddPAKGLVFDGRVAEDFKLASG 431
|
....
gi 1622967304 551 EYIA 554
Cdd:cd05921 432 TWVS 435
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
252-569 |
6.94e-19 |
|
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: 90.24 E-value: 6.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 252 PEDLSIICFTSGTTGDPKGAMITHQNIVSNASAFLKCVEHTFEptpdDVTISYLPLAHmfervvqtvvyccgaRVGFFQG 331
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTK----DRILSWMPLTH---------------DMGLIAF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 332 NIRLLADDMNTLkptLFPTvprvlnRIYdkvqneaktpLKKFLLNLAVASKFKelqKGIIRRDSFWDKLIFAKIQASLG- 410
Cdd:cd05908 166 HLAPLIAGMNQY---LMPT------RLF----------IRRPILWLKKASEHK---ATIVSSPNFGYKYFLKTLKPEKAn 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 411 ----GRVRIIVTGAAPISAPVMTFFRAAMGC------QVYEAYGQTECTAGCTF-------------------------- 454
Cdd:cd05908 224 dwdlSSIRMILNGAEPIDYELCHEFLDHMSKyglkrnAILPVYGLAEASVGASLpkaqspfktitlgrrhvthgepepev 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 455 --TSPGDWTSGHVGAPLTCNYVKLED----VADMDYFsvnneGEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGr 528
Cdd:cd05908 304 dkKDSECLTFVEVGKPIDETDIRICDednkILPDGYI-----GHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG- 377
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1622967304 529 WLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENIYNRSRPVL 569
Cdd:cd05908 378 FIRNGRLVITGREKDII-FVNGQNVYPHDIERIAEELEGVE 417
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
102-559 |
1.14e-18 |
|
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: 89.74 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 102 PYRWLSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVnkADI- 180
Cdd:cd05959 26 DAGSLTYAELEAEARRVAGALRALGVK--REERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL--EDSr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 181 AMVICDTPQKASVLIENVEKGfTPSLKVVILMDPfdddlkqRGEKSGIEILSLYDAENLGKEhfrKPVPPSPEDLSIICF 260
Cdd:cd05959 102 ARVVVVSGELAPVLAAALTKS-EHTLVVLIVSGG-------AGPEAGALLLAELVAAEAEQL---KPAATHADDPAFWLY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 261 TSGTTGDPKGAMITHQNIVSNASAFLKCVEHTfepTPDDVTISYLPLAHmfervvqtvVYCCGARVGF---FQGNIRLLA 337
Cdd:cd05959 171 SSGSTGRPKGVVHLHADIYWTAELYARNVLGI---REDDVCFSAAKLFF---------AYGLGNSLTFplsVGATTVLMP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 338 ---------DDMNTLKPTLFPTVPRVLNRiydkvqneaktplkkfLLNLAVASKfkelqkgiiRRDSfwdklifakiqas 408
Cdd:cd05959 239 erptpaavfKRIRRYRPTVFFGVPTLYAA----------------MLAAPNLPS---------RDLS------------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 409 lggRVRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTEctAGCTFTS--PGDWTSGHVGAPLTCNYVKL-----EDVAD 481
Cdd:cd05959 281 ---SLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTE--MLHIFLSnrPGRVRYGTTGKPVPGYEVELrdedgGDVAD 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622967304 482 mdyfsvNNEGEICIKGTNVFKGYLKDPEKTQEALDSdGWLHTGDIGRWLPNGTLKIIDRKKNIFKlAQGEYIAPEKIE 559
Cdd:cd05959 356 ------GEPGELYVRGPSSATMYWNNRDKTRDTFQG-EWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSPFEVE 425
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
247-575 |
1.76e-18 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 89.18 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 247 PVPPSPEDL----SIICFTSGTTGDPKGAMITHQNIVSNASAFLKcvehTFEPTPDDVTISYLPLAH---MFERVVQTVV 319
Cdd:PRK05852 166 PATSTPEGLrpddAMIMFTGGTTGLPKMVPWTHANIASSVRAIIT----GYRLSPRDATVAVMPLYHghgLIAALLATLA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 320 ycCGARV-----GFFQGniRLLADDMNTLKPTLFPTVPRVlnriydkvqneaktplKKFLLNLAvaskfkelqkgiirrd 394
Cdd:PRK05852 242 --SGGAVllparGRFSA--HTFWDDIKAVGATWYTAVPTI----------------HQILLERA---------------- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 395 sfwDKLIFAKIQASLggrvRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTSPGDWTSGH-----VGAPL 469
Cdd:PRK05852 286 ---ATEPSGRKPAAL----RFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVTTTQIEGIGQTEnpvvsTGLVG 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 470 TCNYVKLEDV-ADMDYFSVNNEGEICIKGTNVFKGYLKDPEKTQEALdSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLA 548
Cdd:PRK05852 359 RSTGAQIRIVgSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG 437
|
330 340
....*....|....*....|....*..
gi 1622967304 549 qGEYIAPEKIENIYNRSRPVLQIFVHG 575
Cdd:PRK05852 438 -GEKISPERVEGVLASHPNVMEAAVFG 463
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
97-529 |
2.06e-18 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 89.55 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 97 RKPNQPYRWLSYKQVSDRAEYLGSCLLHKGYksSPDQFVGIFAQNRPEWIISELACYT-----------YSMVAVPL--- 162
Cdd:PRK08180 61 RGADGGWRRLTYAEALERVRAIAQALLDRGL--SAERPLMILSGNSIEHALLALAAMYagvpyapvspaYSLVSQDFgkl 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 163 ---YDTLGPeAIVYIvnkADI-----AMVICDTPQKASVLIENVEKGFTPSlkvvilmdPFDDDLKQRGeksGIEILSLY 234
Cdd:PRK08180 139 rhvLELLTP-GLVFA---DDGaafarALAAVVPADVEVVAVRGAVPGRAAT--------PFAALLATPP---TAAVDAAH 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 235 DAENlgkehfrkpvppsPEDLSIICFTSGTTGDPKGAMITHQNIVSNASAFLKCVeHTFEPTPDdVTISYLPLAHMF--E 312
Cdd:PRK08180 204 AAVG-------------PDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTF-PFLAEEPP-VLVDWLPWNHTFggN 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 313 RVVQTVVYCCGA--------RVGFFQGNIRLLADdmntLKPTLFPTVPrvlnriydkvqneaktplKKFLLNLAVASKFK 384
Cdd:PRK08180 269 HNLGIVLYNGGTlyiddgkpTPGGFDETLRNLRE----ISPTVYFNVP------------------KGWEMLVPALERDA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 385 ELqkgiirRDSFwdkliFAkiqaslggRVRIIVTGAAPISAPV------MTffRAAMGCQVY--EAYGQTECTAGCTFTS 456
Cdd:PRK08180 327 AL------RRRF-----FS--------RLKLLFYAGAALSQDVwdrldrVA--EATCGERIRmmTGLGMTETAPSATFTT 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622967304 457 PGDWTSGHVGAPLTCNYVKLedvadmdyfsVNNEG--EICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRW 529
Cdd:PRK08180 386 GPLSRAGNIGLPAPGCEVKL----------VPVGGklEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRF 450
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
106-540 |
3.31e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 89.84 E-value: 3.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYksSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVIC 185
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGV--GPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLT 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 DTPQKASVLIENvekgftpSLKVVILMDPFDddlkqrgeksgieILSLYDAENlgkehfrKPVPPSPEDLSIICFTSGTT 265
Cdd:PRK12467 616 QSHLLAQLPVPA-------GLRSLCLDEPAD-------------LLCGYSGHN-------PEVALDPDNLAYVIYTSGST 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 266 GDPKGAMITHQNIVSnasaFLKCVEHTFEPTPDDVTISYLPLAHMFERVVQTVVYCCGARVgffqgnirLLADDMNTLKP 345
Cdd:PRK12467 669 GQPKGVAISHGALAN----YVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATL--------HLLPPDCARDA 736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 346 TLFptvprvlnriYDKVQNEAKTPLKKFllnlavaskfkelqkgiirrDSFWDKLIFAKIQASLGGRVRIIVTGAA-PIS 424
Cdd:PRK12467 737 EAF----------AALMADQGVTVLKIV--------------------PSHLQALLQASRVALPRPQRALVCGGEAlQVD 786
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 425 APVMtFFRAAMGCQVYEAYGQTECTAGCTF----TSPGDWTSGHVGAPLTCNYVKLEDvADMDYFSVNNEGEICIKGTNV 500
Cdd:PRK12467 787 LLAR-VRALGPGARLINHYGPTETTVGVSTyelsDEERDFGNVPIGQPLANLGLYILD-HYLNPVPVGVVGELYIGGAGL 864
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1622967304 501 FKGYLKDPEKTQEALDSD------GWLH-TGDIGRWLPNGTLKIIDR 540
Cdd:PRK12467 865 ARGYHRRPALTAERFVPDpfgadgGRLYrTGDLARYRADGVIEYLGR 911
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
106-567 |
8.54e-18 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 88.10 E-value: 8.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGScLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVIC 185
Cdd:PRK06814 659 LTYRKLLTGAFVLGR-KLKKNTP--PGENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 DTP--QKA--SVLIENVEKGFtpslKVVILmdpfdDDLKQRgeksgieiLSLYDaENLGKEHFRKPVPP----SPEDLSI 257
Cdd:PRK06814 736 SRAfiEKArlGPLIEALEFGI----RIIYL-----EDVRAQ--------IGLAD-KIKGLLAGRFPLVYfcnrDPDDPAV 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 258 ICFTSGTTGDPKGAMITHQNIVSNASAFLKCVEHtfepTPDDVTISYLPLAHMFervvqtvvyccgarvGFFQGNIRLLa 337
Cdd:PRK06814 798 ILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDF----SPEDKVFNALPVFHSF---------------GLTGGLVLPL- 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 338 ddMNTLKPTLFPT------VPRVlnrIYDkvqneaktplkkflLNLAVaskfkelqkgIIRRDSFWDKliFAKIQASLGG 411
Cdd:PRK06814 858 --LSGVKVFLYPSplhyriIPEL---IYD--------------TNATI----------LFGTDTFLNG--YARYAHPYDF 906
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 412 R-VRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTSPGDWTSGHVGAPLTCNYVKLEDVAdmdyfSVNNE 490
Cdd:PRK06814 907 RsLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVP-----GIDEG 981
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622967304 491 GEICIKGTNVFKGYLKdPEK--TQEALdSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENIYNRSRP 567
Cdd:PRK06814 982 GRLFVRGPNVMLGYLR-AENpgVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAVEELAAELWP 1057
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
248-580 |
8.56e-18 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 87.84 E-value: 8.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 248 VPPSPEDLSIICFTSGTTGDPKGAMITHQNIVSNASAfLKCVEhtfEPTPDDVTISYLPLAHMFERVVQTVV-YCCGARV 326
Cdd:PRK08043 360 VKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQ-IKTIA---DFTPNDRFMSALPLFHSFGLTVGLFTpLLTGAEV 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 327 GFFQgnirlladdmntlKPTLFPTVPRVlnrIYDK---VQNEAKTplkkFLLNLAvaskfkelqkgiirrdSFWDKLIFA 403
Cdd:PRK08043 436 FLYP-------------SPLHYRIVPEL---VYDRnctVLFGTST----FLGNYA----------------RFANPYDFA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 404 kiqaslggRVRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTSPGDWTSGHVGAPLTCNYVKLEDVADMD 483
Cdd:PRK08043 480 --------RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIE 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 484 yfsvnNEGEICIKGTNVFKGYLK-------------DPEKTQEAldsdGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqG 550
Cdd:PRK08043 552 -----QGGRLQLKGPNIMNGYLRvekpgvlevptaeNARGEMER----GWYDTGDIVRFDEQGFVQIQGRAKRFAKIA-G 621
|
330 340 350
....*....|....*....|....*....|
gi 1622967304 551 EYIAPEKIENIYNRSRPVLQifvHGESLRS 580
Cdd:PRK08043 622 EMVSLEMVEQLALGVSPDKQ---HATAIKS 648
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
252-561 |
1.17e-17 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 86.79 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 252 PEDLSIICFTSGTTGDPKGAMITHQNIVSNASAFLKCvehtFEPTPDDVTISYLPLAHMFErvvqtvVYCCgarvgffqg 331
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKF----FSPKEDDVMMSFLPPFHAYG------FNSC--------- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 332 nirlladdmntlkpTLFPT---VPRVLnriydkvqneAKTPLK-KFLLNLAVASKFKELQKGIIrrdsFWDKLI-FAKIQ 406
Cdd:PRK06334 243 --------------TLFPLlsgVPVVF----------AYNPLYpKKIVEMIDEAKVTFLGSTPV----FFDYILkTAKKQ 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 407 ASLGGRVRIIVTGAapiSAPVMTFFRAAMG----CQVYEAYGQTECTAGCTFT---SPGDwtSGHVGAPltcnyvkledV 479
Cdd:PRK06334 295 ESCLPSLRFVVIGG---DAFKDSLYQEALKtfphIQLRQGYGTTECSPVITINtvnSPKH--ESCVGMP----------I 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 480 ADMDYFSVNNE----------GEICIKGTNVFKGYL-KDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLA 548
Cdd:PRK06334 360 RGMDVLIVSEEtkvpvssgetGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG 439
|
330
....*....|...
gi 1622967304 549 qGEYIAPEKIENI 561
Cdd:PRK06334 440 -AEMVSLEALESI 451
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
102-573 |
1.29e-17 |
|
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: 85.98 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 102 PYRWLSYKQVSDRAEYLGSCLlhKGYKSSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIA 181
Cdd:cd05919 7 ADRSVTYGQLHDGANRLGSAL--RNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 182 MVICDTpqkasvlienvekgftpslkvvilmdpfdddlkqrgeksgieilslydaenlgkehfrkpvppspEDLSIICFT 261
Cdd:cd05919 85 LVVTSA-----------------------------------------------------------------DDIAYLLYS 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 262 SGTTGDPKGAMITHQNIVSNASAFlkCVEhTFEPTPDDVTISylpLAHMFervvqtVVYCCGARVGF--FQGNIRLLADD 339
Cdd:cd05919 100 SGTTGPPKGVMHAHRDPLLFADAM--ARE-ALGLTPGDRVFS---SAKMF------FGYGLGNSLWFplAVGASAVLNPG 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 340 -------MNTL---KPTLFPTVPRvlnrIYDKVQNEAKTPlkkfllnlavaskfkelqkgiirRDSFWDklifakiqasl 409
Cdd:cd05919 168 wptaervLATLarfRPTVLYGVPT----FYANLLDSCAGS-----------------------PDALRS----------- 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 410 ggrVRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTEctAGCTFTS--PGDWTSGHVGAPLTCNYVKLEDvADMDYFSV 487
Cdd:cd05919 210 ---LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATE--VGHIFLSnrPGAWRLGSTGRPVPGYEIRLVD-EEGHTIPP 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 488 NNEGEICIKGTNVFKGYLKDPEKTQEALdSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENIYNRSRP 567
Cdd:cd05919 284 GEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVESLIIQHPA 361
|
....*.
gi 1622967304 568 VLQIFV 573
Cdd:cd05919 362 VAEAAV 367
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
106-569 |
1.75e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 86.25 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVIC 185
Cdd:PRK06178 59 ITYAELDELSDRFAALLRQRGVG--AGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 -DT--PQKASVLIE-NVEKGFTPSLKVVI-----LMDPFDDDLKQRGEKSGIEILSLYDAEnlgkehfRKPVP---PSPE 253
Cdd:PRK06178 137 lDQlaPVVEQVRAEtSLRHVIVTSLADVLpaeptLPLPDSLRAPRLAAAGAIDLLPALRAC-------TAPVPlppPALD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 254 DLSIICFTSGTTGDPKGAMITHQNIVSNASAFLKCvehTFEPTPDDVTISYLPlahMFervvqtvvYCCGARVG-----F 328
Cdd:PRK06178 210 ALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAV---AVVGGEDSVFLSFLP---EF--------WIAGENFGllfplF 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 329 FQGNIRLLA--DDMNTLKptlfpTVPRV-LNRIYDKVQNEAKtplkkfLLNLAVASKF--KELQKgiIRRDSFWDKLifa 403
Cdd:PRK06178 276 SGATLVLLArwDAVAFMA-----AVERYrVTRTVMLVDNAVE------LMDHPRFAEYdlSSLRQ--VRVVSFVKKL--- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 404 kiqaSLGGRVRiivtgaapisapvmtfFRAAMGCQVYEA-YGQTECTAGCTFTSpGDWTSGH--------VGAPLTCNYV 474
Cdd:PRK06178 340 ----NPDYRQR----------------WRALTGSVLAEAaWGMTETHTCDTFTA-GFQDDDFdllsqpvfVGLPVPGTEF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 475 KLEDVADMDYFSVNNEGEICIKGTNVFKGYLKDPEKTQEALdSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIA 554
Cdd:PRK06178 399 KICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV-NGMSVF 476
|
490
....*....|....*
gi 1622967304 555 PEKIENIYNRSRPVL 569
Cdd:PRK06178 477 PSEVEALLGQHPAVL 491
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
103-573 |
2.55e-17 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 85.67 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 103 YRWLsykQVSDRAEYLGSCLLHKGYksSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAM 182
Cdd:PLN02479 46 YTWA---QTYQRCRRLASALAKRSI--GPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 183 VICD------TPQKASVLIENVEKGFTPSLKVVILMDPFDDDLKQRGEKSGI----EILSLYDAENLGKehfrkpvPPSP 252
Cdd:PLN02479 121 VMVDqefftlAEEALKILAEKKKSSFKPPLLIVIGDPTCDPKSLQYALGKGAieyeKFLETGDPEFAWK-------PPAD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 253 EDLSI-ICFTSGTTGDPKGAMITHQnivsnaSAFLKCVEH--TFEPTPDDVTISYLPLAHMFERVVQ-TVVYCCGARVGF 328
Cdd:PLN02479 194 EWQSIaLGYTSGTTASPKGVVLHHR------GAYLMALSNalIWGMNEGAVYLWTLPMFHCNGWCFTwTLAALCGTNICL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 329 FQGNIRLLADDMNTLKPTLFPTVPRVLNRIYDKVQNEAKTPLKKFllnlavaskfkelqkgiirrdsfwdklifakiqas 408
Cdd:PLN02479 268 RQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETILPLPRV----------------------------------- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 409 lggrVRIIVTGAAPisAPVMTFFRAAMGCQVYEAYGQTEcTAG----CTFTSPGDWTSGHVGAPLTC----NYVKLE--D 478
Cdd:PLN02479 313 ----VHVMTAGAAP--PPSVLFAMSEKGFRVTHTYGLSE-TYGpstvCAWKPEWDSLPPEEQARLNArqgvRYIGLEglD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 479 VAD---MDYFSVNNE--GEICIKGTNVFKGYLKDPEKTQEALdSDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYI 553
Cdd:PLN02479 386 VVDtktMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGGENI 463
|
490 500
....*....|....*....|
gi 1622967304 554 APEKIENIYNRSRPVLQIFV 573
Cdd:PLN02479 464 SSLEVENVVYTHPAVLEASV 483
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
106-547 |
2.92e-17 |
|
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: 85.18 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIamvic 185
Cdd:cd17644 26 LTYEELNTKANQLAHYLQSLGVK--SESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYILEDAQI----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 dtpqkaSVLIENvekgftpslkvvilmdpfdddlkqrgeksgieilslydaenlgkehfrkpvppsPEDLSIICFTSGTT 265
Cdd:cd17644 99 ------SVLLTQ------------------------------------------------------PENLAYVIYTSGST 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 266 GDPKGAMITHQNIVSNASAFLKCVehtFEPTPDDVTIsYLPLAhmFERVVQT--VVYCCGARVgffqgnirlladdmnTL 343
Cdd:cd17644 119 GKPKGVMIEHQSLVNLSHGLIKEY---GITSSDRVLQ-FASIA--FDVAAEEiyVTLLSGATL---------------VL 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 344 KPT-LFPTVPRVLnriyDKVQNEAKTplkkfLLNLAVAskfkelqkgiirrdsFWDKLIFAKIQASLGG--RVRIIVTGA 420
Cdd:cd17644 178 RPEeMRSSLEDFV----QYIQQWQLT-----VLSLPPA---------------YWHLLVLELLLSTIDLpsSLRLVIVGG 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 421 APISAPVMTFFRAAMG--CQVYEAYGQTECTAGCTFTSPGDWTSGH-----VGAPLTCNYVKLEDvADMDYFSVNNEGEI 493
Cdd:cd17644 234 EAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIANTQVYILD-ENLQPVPVGVPGEL 312
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622967304 494 CIKGTNVFKGYLKDPEKTQEALDSDGWLH--------TGDIGRWLPNGTLKIIDRKKNIFKL 547
Cdd:cd17644 313 HIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKI 374
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
104-569 |
5.05e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 84.61 E-value: 5.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 104 RWLSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEwiiselacytysMV----AVP--------LYDTLGPEAI 171
Cdd:PRK08162 42 RRRTWAETYARCRRLASALARRGIG--RGDTVAVLLPNIPA------------MVeahfGVPmagavlntLNTRLDAASI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 172 VYIVNKADIAMVICDTP-----QKASVLIENvekgftPSLKVVilmdpfDDDLkqrGEKSGIEILSLYDAENL---GKEH 243
Cdd:PRK08162 108 AFMLRHGEAKVLIVDTEfaevaREALALLPG------PKPLVI------DVDD---PEYPGGRFIGALDYEAFlasGDPD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 244 FrKPVPPSPEDLSI-ICFTSGTTGDPKGAMITHQ----NIVSNASAFlkcvehtfEPTPDDVTISYLPLAHmfervvqtv 318
Cdd:PRK08162 173 F-AWTLPADEWDAIaLNYTSGTTGNPKGVVYHHRgaylNALSNILAW--------GMPKHPVYLWTLPMFH--------- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 319 vyCCG--------ARVGFfqgNI-------RLLADDMNTLKPTLFPTVPRVLNriydkvqneaktplkkFLLNLAVASKf 383
Cdd:PRK08162 235 --CNGwcfpwtvaARAGT---NVclrkvdpKLIFDLIREHGVTHYCGAPIVLS----------------ALINAPAEWR- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 384 kelqkgiirrdsfwdklifakiqASLGGRVRIIVTGAAPISAPV--MtffrAAMGCQVYEAYGQTEcTAG----CTFTSP 457
Cdd:PRK08162 293 -----------------------AGIDHPVHAMVAGAAPPAAVIakM----EEIGFDLTHVYGLTE-TYGpatvCAWQPE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 458 GDWTSGHVGAPLT----CNYVKLEDVADMDYFSV-----NNE--GEICIKGTNVFKGYLKDPEKTQEALdSDGWLHTGDI 526
Cdd:PRK08162 345 WDALPLDERAQLKarqgVRYPLQEGVTVLDPDTMqpvpaDGEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDL 423
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1622967304 527 GRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENIYNRSRPVL 569
Cdd:PRK08162 424 AVLHPDGYIKIKDRSKDII-ISGGENISSIEVEDVLYRHPAVL 465
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
104-561 |
6.58e-17 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 84.47 E-value: 6.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 104 RWLSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNrpewiiSELacYTYSMVAVPLydtLGpeAIVYIVN------K 177
Cdd:PLN02860 31 RRRTGHEFVDGVLSLAAGLLRLGLR--NGDVVAIAALN------SDL--YLEWLLAVAC---AG--GIVAPLNyrwsfeE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 178 ADIAM-----VICDTPQKASVLIENVEKGFTPSLKVVILMDPFDDDlkqrgekSGIEILSLYDAENLGKEHFRKPVPP-- 250
Cdd:PLN02860 96 AKSAMllvrpVMLVTDETCSSWYEELQNDRLPSLMWQVFLESPSSS-------VFIFLNSFLTTEMLKQRALGTTELDya 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 251 -SPEDLSIICFTSGTTGDPKGAMITHQNIVSNASAFLKCVEHtfepTPDDVTISYLPLAHMFE-RVVQTVVYCCGARVGF 328
Cdd:PLN02860 169 wAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGY----GEDDVYLHTAPLCHIGGlSSALAMLMVGACHVLL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 329 FQGNIRLLADDMNTLKPTLFPTVPRVLNRIYDkvqneaktplkkfllnlavaskfkelqkgIIRRDSFWDklifakiqas 408
Cdd:PLN02860 245 PKFDAKAALQAIKQHNVTSMITVPAMMADLIS-----------------------------LTRKSMTWK---------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 409 lGGR-VRIIVTGAAPISAPVM-----TFFRAAmgcqVYEAYGQTECTAGCTFTSPGDWT---------------SGHVGA 467
Cdd:PLN02860 286 -VFPsVRKILNGGGSLSSRLLpdakkLFPNAK----LFSAYGMTEACSSLTFMTLHDPTlespkqtlqtvnqtkSSSVHQ 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 468 PL-TC-----NYVKLEDVADmdyfSVNNEGEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRK 541
Cdd:PLN02860 361 PQgVCvgkpaPHVELKIGLD----ESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRS 436
|
490 500
....*....|....*....|
gi 1622967304 542 KNIFKlAQGEYIAPEKIENI 561
Cdd:PLN02860 437 NDRIK-TGGENVYPEEVEAV 455
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
106-559 |
6.70e-17 |
|
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: 83.93 E-value: 6.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVic 185
Cdd:cd17651 21 LTYAELDRRANRLAHRLRARGVG--PGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLV-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 dtpqkasVLIENVEKGFTPSLKVVILMDPFdddlkqrgeksgiEILSLYDAEnlgkehfrKPVPPSPEDLSIICFTSGTT 265
Cdd:cd17651 97 -------LTHPALAGELAVELVAVTLLDQP-------------GAAAGADAE--------PDPALDADDLAYVIYTSGST 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 266 GDPKGAMITHQNIVSnasaFLKCVEHTFEPTPDDVTISYLPLAhmFERVVQTV--VYCCGARVGFFQGNIRL----LADD 339
Cdd:cd17651 149 GRPKGVVMPHRSLAN----LVAWQARASSLGPGARTLQFAGLG--FDVSVQEIfsTLCAGATLVLPPEEVRTdppaLAAW 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 340 MNTlkptlfptvpRVLNRIYdkvqneAKTPLKKFLLNLAVAskfkelqkgiirrdsfwdklifakiQASLGGRVRIIVTG 419
Cdd:cd17651 223 LDE----------QRISRVF------LPTVALRALAEHGRP-------------------------LGVRLAALRYLLTG 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 420 --AAPISAPVMTFFRAAMGCQVYEAYGQTE---CTAGCTFTSPGDWTS-GHVGAPLTCNYVKLEDvADMDYFSVNNEGEI 493
Cdd:cd17651 262 geQLVLTEDLREFCAGLPGLRLHNHYGPTEthvVTALSLPGDPAAWPApPPIGRPIDNTRVYVLD-AALRPVPPGVPGEL 340
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622967304 494 CIKGTNVFKGYLKDPEKTQEALDSDGWL------HTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIE 559
Cdd:cd17651 341 YIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGFRIELGEIE 411
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
252-559 |
1.14e-16 |
|
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: 82.90 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 252 PEDLSIICFTSGTTGDPKGAMITHQNIVSNASAFLKcvehtfEPTPDDVTISYLPLAHM--------FERVVQT--VVYC 321
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRR------EYELDSFPVRLLQMASFsfdvfagdFARSLLNggTLVI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 322 CGARVGFfqgNIRLLADDMNTLKPTLFPTVPRVLNRIYDKVQNEAKTPlkKFLLNLAVASKFKELQkgiirrdsfWdkli 401
Cdd:cd17650 166 CPDEVKL---DPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDL--SAMRLLIVGSDGCKAQ---------D---- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 402 FAKIQASLGGRVRIIvtgaapisapvmtffraamgcqvyEAYGQTECTAGCTFTSPGDWTSGH-----VGAPL--TCNYV 474
Cdd:cd17650 228 FKTLAARFGQGMRII------------------------NSYGVTEATIDSTYYEEGRDPLGDsanvpIGRPLpnTAMYV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 475 KLEDvadMDYFSVNNEGEICIKGTNVFKGYLKDPEKTQEALDSDGW------LHTGDIGRWLPNGTLKIIDRKKNIFKLa 548
Cdd:cd17650 284 LDER---LQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI- 359
|
330
....*....|.
gi 1622967304 549 QGEYIAPEKIE 559
Cdd:cd17650 360 RGFRIELGEIE 370
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
139-559 |
1.63e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 79.70 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 139 AQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVIC--DTPQKASVLienveKGFTPSLKVVILMD--P 214
Cdd:PRK07470 64 SRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMIChaDFPEHAAAV-----RAASPDLTHVVAIGgaR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 215 FDDDlkqrgeksgieilslYDAenLGKEHFRKPVPPSPEDLSIIC---FTSGTTGDPKGAMITHQN---IVSNASAFLkc 288
Cdd:PRK07470 139 AGLD---------------YEA--LVARHLGARVANAAVDHDDPCwffFTSGTTGRPKAAVLTHGQmafVITNHLADL-- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 289 vehTFEPTPDDVTISYLPLAHmfervvqtvvyccGArvgffqgNIRLLADDMNTLKPTLFPTVPRVLNRIYD-----KVQ 363
Cdd:PRK07470 200 ---MPGTTEQDASLVVAPLSH-------------GA-------GIHQLCQVARGAATVLLPSERFDPAEVWAlverhRVT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 364 NEAKTP--LKKFLLNLAVAskfkelqkgiiRRDsfwdklifakiQASLggrvRIIVTGAAPISAPVMTFFRAAMGCQVYE 441
Cdd:PRK07470 257 NLFTVPtiLKMLVEHPAVD-----------RYD-----------HSSL----RYVIYAGAPMYRADQKRALAKLGKVLVQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 442 AYGQTECTAGCT-----FTSPGDWTSGHVGaplTCNY------VKLEDvADMDYFSVNNEGEICIKGTNVFKGYLKDPEK 510
Cdd:PRK07470 311 YFGLGEVTGNITvlppaLHDAEDGPDARIG---TCGFertgmeVQIQD-DEGRELPPGETGEICVIGPAVFAGYYNNPEA 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1622967304 511 TQEALdSDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIE 559
Cdd:PRK07470 387 NAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPREIE 433
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
107-575 |
2.04e-15 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 79.01 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 107 SYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVICD 186
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLE--KGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 187 tpqkasvlienvekgftpslkvvilmdpfdddlkqrgeksgieilslydaenlgkehfrkpvppSPEDLSIICFTSGTTG 266
Cdd:cd05971 86 ----------------------------------------------------------------GSDDPALIIYTSGTTG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 267 DPKGAMITHQNIVSNasafLKCVEHTFEPTPDDVTISYLPlahmfervvqtvvyccgARVGFFQGnirLLaddmNTLKPT 346
Cdd:cd05971 102 PPKGALHAHRVLLGH----LPGVQFPFNLFPRDGDLYWTP-----------------ADWAWIGG---LL----DVLLPS 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 347 LFPTVPRVLNRiydkvqneaktpLKKFllnlaVASKFKELQKGIIRRDSFWD----KLI-FAKIQASLGG-RVRIIVTGA 420
Cdd:cd05971 154 LYFGVPVLAHR------------MTKF-----DPKAALDLMSRYGVTTAFLPptalKMMrQQGEQLKHAQvKLRAIATGG 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 421 APISAPVMTFFRAAMGCQVYEAYGQTEC---TAGCTFTSPGDwtSGHVGAPLTCNYVKLEDVADMDyFSVNNEGEICIK- 496
Cdd:cd05971 217 ESLGEELLGWAREQFGVEVNEFYGQTECnlvIGNCSALFPIK--PGSMGKPIPGHRVAIVDDNGTP-LPPGEVGEIAVEl 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 497 -GTNVFKGYLKDPEKTQEALDSDgWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENIYNRSRPVLQIFVHG 575
Cdd:cd05971 294 pDPVAFLGYWNNPSATEKKMAGD-WLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAEIEECLLKHPAVLMAAVVG 371
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
106-560 |
2.10e-15 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 79.24 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVIC 185
Cdd:cd17646 24 LTYRELDERANRLAHLLRARGVG--PEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 DTPQKAsvlienvekGFTPSLKVVILMDpfdddlkqrgeksgiEILSLYDAEnlgkehfRKPVPPSPEDLSIICFTSGTT 265
Cdd:cd17646 102 TADLAA---------RLPAGGDVALLGD---------------EALAAPPAT-------PPLVPPRPDNLAYVIYTSGST 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 266 GDPKGAMITHQNIVSNasafLKCVEHTFEPTPDDVTISYLPLAhmFERVVQTVVY--CCGARVGFFQ----GNIRLLADD 339
Cdd:cd17646 151 GRPKGVMVTHAGIVNR----LLWMQDEYPLGPGDRVLQKTPLS--FDVSVWELFWplVAGARLVVARpgghRDPAYLAAL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 340 MNTLKPTLFPTVPRVLnriydkvqneaktplKKFLLNLAVASKfkelqkgiirrdsfwdklifakiqASLggrvRIIVTG 419
Cdd:cd17646 225 IREHGVTTCHFVPSML---------------RVFLAEPAAGSC------------------------ASL----RRVFCS 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 420 AAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCT-FTSPGDWTSGHV--GAPL--TCNYVkLEDvaDMDYFSVNNEGEIC 494
Cdd:cd17646 262 GEALPPELAARFLALPGAELHNLYGPTEAAIDVThWPVRGPAETPSVpiGRPVpnTRLYV-LDD--ALRPVPVGVPGELY 338
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622967304 495 IKGTNVFKGYLKDPEKTQEALDSDGWLH------TGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIEN 560
Cdd:cd17646 339 LGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKI-RGFRVEPGEIEA 409
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
106-547 |
2.25e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 80.77 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYksSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLyDTLGP-EAIVYIVNKADIAMVI 184
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGV--GPEVRVAIAAERSFELVVALLAVLKAGGAYVPL-DPNYPaERLAYMLEDSGAALLL 2105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 185 CDTPQKASVLIenvekgftPSLKVVILMDPfDDDLKQRGEKsgieilslydaenlgkehfRKPVPPSPEDLSIICFTSGT 264
Cdd:PRK12316 2106 TQRHLLERLPL--------PAGVARLPLDR-DAEWADYPDT-------------------APAVQLAGENLAYVIYTSGS 2157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 265 TGDPKGAMITHQNIVsnasAFLKCVEHTFEPTPDDVTISYLPLAhmFERVVQTVVY--CCGARVGFFQGNIRL---LADD 339
Cdd:PRK12316 2158 TGLPKGVAVSHGALV----AHCQAAGERYELSPADCELQFMSFS--FDGAHEQWFHplLNGARVLIRDDELWDpeqLYDE 2231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 340 MNTLKPTLFPTVPRVLNRIYDKVQNEAKTPlkkfllnlavaskfkelqkgiirrdsfwdklifakiqaslggRVRIIVTG 419
Cdd:PRK12316 2232 MERHGVTILDFPPVYLQQLAEHAERDGRPP------------------------------------------AVRVYCFG 2269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 420 AAPISAPVMTFFRAAMGCQ-VYEAYGQTECTA-----GCTFTSPGDWTSGHVGAPLTCNYVKLEDvADMDYFSVNNEGEI 493
Cdd:PRK12316 2270 GEAVPAASLRLAWEALRPVyLFNGYGPTEAVVtpllwKCRPQDPCGAAYVPIGRALGNRRAYILD-ADLNLLAPGMAGEL 2348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622967304 494 CIKGTNVFKGYLKDPEKTQEALDSDGWLH-------TGDIGRWLPNGTLKIIDRKKNIFKL 547
Cdd:PRK12316 2349 YLGGEGLARGYLNRPGLTAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKI 2409
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
106-560 |
2.83e-15 |
|
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: 78.75 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVIC 185
Cdd:cd17645 24 LTYKQLNEKANQLARHLRGKGVK--PDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 DtpqkasvlienvekgftpslkvvilmdpfdddlkqrgeksgieilslydaenlgkehfrkpvppsPEDLSIICFTSGTT 265
Cdd:cd17645 102 N-----------------------------------------------------------------PDDLAYVIYTSGST 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 266 GDPKGAMITHQNIVSNASAFLKCvehtFEPTPDDVTISYLPLAhmFERVVQTVV--YCCGARVGFFQGNIRLLADDMNtl 343
Cdd:cd17645 117 GLPKGVMIEHHNLVNLCEWHRPY----FGVTPADKSLVYASFS--FDASAWEIFphLTAGAALHVVPSERRLDLDALN-- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 344 kptlfptvprvlnriyDKVQNEAKTPLkkfLLNLAVASKFKELQKgiirrDSFwdklifakiqaslggrvRIIVTGAAPI 423
Cdd:cd17645 189 ----------------DYFNQEGITIS---FLPTGAAEQFMQLDN-----QSL-----------------RVLLTGGDKL 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 424 SAPVMTffraamGCQVYEAYGQTECTAGCT-FTSPGDWTSGHVGAPLTCNYVKLEDvADMDYFSVNNEGEICIKGTNVFK 502
Cdd:cd17645 228 KKIERK------GYKLVNNYGPTENTVVATsFEIDKPYANIPIGKPIDNTRVYILD-EALQLQPIGVAGELCIAGEGLAR 300
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622967304 503 GYLKDPEKTQEALDSDGWL------HTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIEN 560
Cdd:cd17645 301 GYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIEP 363
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
102-559 |
2.40e-14 |
|
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: 75.59 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 102 PYRWLSYKQVSDRAEYLGSCLLHKGyKSSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIA 181
Cdd:cd05958 7 PEREWTYRDLLALANRIANVLVGEL-GIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARIT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 182 MVICDTPQKASvlienvekgftpslkvvilmdpfdddlkqrgeksgieilslydaenlgkehfrkpvppspEDLSIICFT 261
Cdd:cd05958 86 VALCAHALTAS------------------------------------------------------------DDICILAFT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 262 SGTTGDPKGAMITHQNIVSNASAFLKcveHTFEPTPDDVTISYLPLAHMFER-VVQTVVYCCGARVGFFQGNIrllADDM 340
Cdd:cd05958 106 SGTTGAPKATMHFHRDPLASADRYAV---NVLRLREDDRFVGSPPLAFTFGLgGVLLFPFGVGASGVLLEEAT---PDLL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 341 NTL----KPTLFPTVPrvlnriydkvqneakTPLKKFLLNLAVAskfkelqkgiirrdsfwdklifakiqASLGGRVRII 416
Cdd:cd05958 180 LSAiaryKPTVLFTAP---------------TAYRAMLAHPDAA--------------------------GPDLSSLRKC 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 417 VTGAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTSPGDWTSGHVGAPLTCNYVKLEDvADMDYFSVNNEGEICIK 496
Cdd:cd05958 219 VSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD-DEGNPVPDGTIGRLAVR 297
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622967304 497 GTNvfkGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIE 559
Cdd:cd05958 298 GPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVE 356
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
106-559 |
2.63e-14 |
|
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: 75.97 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADiamvic 185
Cdd:cd17656 14 LTYRELNERSNQLARFLREKGVK--KDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSG------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 dtpqkASVLIENVEKGFTPSL-KVVILMDpfDDDLKQRgeksgieilslyDAENLGKEHfrkpvppSPEDLSIICFTSGT 264
Cdd:cd17656 86 -----VRVVLTQRHLKSKLSFnKSTILLE--DPSISQE------------DTSNIDYIN-------NSDDLLYIIYTSGT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 265 TGDPKGAMITHQNIVSnasaflkCVEHTFEPTPDDVTISYLPLAHM-FERVVQTVV--YCCGarvgffqGNIRLLADDMN 341
Cdd:cd17656 140 TGKPKGVQLEHKNMVN-------LLHFEREKTNINFSDKVLQFATCsFDVCYQEIFstLLSG-------GTLYIIREETK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 342 TLKPTLFPTVprvlnriydkvqneAKTPLKKFLLNLAvaskfkelqkgiirrdsFWdKLIFAKIQA--SLGGRVRIIVTG 419
Cdd:cd17656 206 RDVEQLFDLV--------------KRHNIEVVFLPVA-----------------FL-KFIFSEREFinRFPTCVKHIITA 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 420 AAP--ISAPVMTFFRAAmGCQVYEAYGQTECTAGCTFT-SPGDWTSGH--VGAPLTCNYVKLEDvADMDYFSVNNEGEIC 494
Cdd:cd17656 254 GEQlvITNEFKEMLHEH-NVHLHNHYGPSETHVVTTYTiNPEAEIPELppIGKPISNTWIYILD-QEQQLQPQGIVGELY 331
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622967304 495 IKGTNVFKGYLKDPEKTQEALDSDGW------LHTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIE 559
Cdd:cd17656 332 ISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-RGYRIELGEIE 401
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
247-573 |
2.84e-14 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 75.68 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 247 PVPPSPEDLSIICFTSGTTGDPKGAMITHQNIVSNASAFLKCVehTFEPTpDDVTISyLPLAHmfervV--QTVVY---C 321
Cdd:PRK09029 129 AVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLM--PFTAQ-DSWLLS-LPLFH-----VsgQGIVWrwlY 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 322 CGARVGFfqGNIRLLADDMN-----TLkptlfptVPRVLNRIYDkvQNEAKTPLKKFLLNLAVaskfkelqkgiirrdsf 396
Cdd:PRK09029 200 AGATLVV--RDKQPLEQALAgcthaSL-------VPTQLWRLLD--NRSEPLSLKAVLLGGAA----------------- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 397 wdklifakIQASLggrvriivTGAApisapvmtffrAAMGCQVYEAYGQTEcTAGCTFTSPGDWTSGhVGAPLTCNYVKL 476
Cdd:PRK09029 252 --------IPVEL--------TEQA-----------EQQGIRCWCGYGLTE-MASTVCAKRADGLAG-VGSPLPGREVKL 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 477 EDvadmdyfsvnneGEICIKGTNVFKGYLKDpEKTQEALDSDGWLHTGDIGRWLpNGTLKIIDRKKNIFkLAQGEYIAPE 556
Cdd:PRK09029 303 VD------------GEIWLRGASLALGYWRQ-GQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPE 367
|
330
....*....|....*..
gi 1622967304 557 KIENIYNRSRPVLQIFV 573
Cdd:PRK09029 368 EIERVINQHPLVQQVFV 384
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
104-559 |
3.13e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 75.94 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 104 RWLSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMV 183
Cdd:PRK06164 34 RPLSRAELRALVDRLAAWLAAQGVR--RGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 184 ICDTPQK----ASVLiENVEKGFTPSLKVVILMDPFDDDLKQRGEKSGIEILSLYDAEnlgkEHFRKPVPPSPEDLSIIC 259
Cdd:PRK06164 112 VVWPGFKgidfAAIL-AAVPPDALPPLRAIAVVDDAADATPAPAPGARVQLFALPDPA----PPAAAGERAADPDAGALL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 260 FT-SGTTGDPK------GAMITHQNIVSNASAFlkcvehtfepTPDDVTISYLPLahmfervvqtvvycCGArVGFfqgn 332
Cdd:PRK06164 187 FTtSGTTSGPKlvlhrqATLLRHARAIARAYGY----------DPGAVLLAALPF--------------CGV-FGF---- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 333 irlladdmNTLKPTLFPTVPRVLNRIYDKVQNEAKtplkkfLLNLAVASKFKElqkgiirrDSFWDKLIFAKIQASLGGR 412
Cdd:PRK06164 238 --------STLLGALAGGAPLVCEPVFDAARTARA------LRRHRVTHTFGN--------DEMLRRILDTAGERADFPS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 413 VRIIVTGA-APISAPVMTFFRAAmGCQVYEAYGQTECTA---GCTFTSPGD--WTSGhvGAPLTCN-YVKLEDVADMDYF 485
Cdd:PRK06164 296 ARLFGFASfAPALGELAALARAR-GVPLTGLYGSSEVQAlvaLQPATDPVSvrIEGG--GRPASPEaRVRARDPQDGALL 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622967304 486 SVNNEGEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIE 559
Cdd:PRK06164 373 PDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNPAEIE 445
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
104-278 |
3.19e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 75.69 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 104 RWLSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMV 183
Cdd:PRK07798 27 RRLTYAELEERANRLAHYLIAQGLG--PGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 184 ICD---TPQKASVLIEnvekgfTPSLKVVILMDpfDDDlkqrGEKSGIEILSLYDAENLGKEHfRKPVPPSPEDLSIICf 260
Cdd:PRK07798 105 VYErefAPRVAEVLPR------LPKLRTLVVVE--DGS----GNDLLPGAVDYEDALAAGSPE-RDFGERSPDDLYLLY- 170
|
170
....*....|....*...
gi 1622967304 261 TSGTTGDPKGAMITHQNI 278
Cdd:PRK07798 171 TGGTTGMPKGVMWRQEDI 188
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
97-561 |
3.73e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 75.31 E-value: 3.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 97 RKPNQP---YR--WLSYKQVSDRAEYLGSCLlhKGYKSSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAI 171
Cdd:PRK06145 14 RTPDRAalvYRdqEISYAEFHQRILQAAGML--HARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 172 VYIVNKADIAMVICDTPQKASVLIEnvekgfTPslKVVIlmdpfdDDLKQRgeksgieilslyDAENLGKEHfrKPVPP- 250
Cdd:PRK06145 92 AYILGDAGAKLLLVDEEFDAIVALE------TP--KIVI------DAAAQA------------DSRRLAQGG--LEIPPq 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 251 ---SPEDLSIICFTSGTTGDPKGAMITHQNIvsnasaFLKCVEHTFE--PTPDDVTISYLPLAHmfervvqtvVYCC--- 322
Cdd:PRK06145 144 aavAPTDLVRLMYTSGTTDRPKGVMHSYGNL------HWKSIDHVIAlgLTASERLLVVGPLYH---------VGAFdlp 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 323 GARVGFFQGNIRLLAD-DMNTL-------KPTLFPTVPRVLNRIydkvqneaktplkkfllnLAVASkfkelqkgiirRD 394
Cdd:PRK06145 209 GIAVLWVGGTLRIHREfDPEAVlaaierhRLTCAWMAPVMLSRV------------------LTVPD-----------RD 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 395 SFwdklifakiqaSLGGRVRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTSPGDWTS--GHVGAPLTcn 472
Cdd:PRK06145 260 RF-----------DLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREIEkiGSTGRALA-- 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 473 YVKLEdVADMD--YFSVNNEGEICIKGTNVFKGYLKDPEKTQEALdSDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQG 550
Cdd:PRK06145 327 HVEIR-IADGAgrWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGG 403
|
490
....*....|.
gi 1622967304 551 EYIAPEKIENI 561
Cdd:PRK06145 404 ENIASSEVERV 414
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
106-559 |
4.46e-14 |
|
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: 75.04 E-value: 4.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVIC 185
Cdd:cd17643 13 LTYGELDARANRLARTLRAEGVG--PGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLLLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 DtpqkasvlienvekgftpslkvvilmdpfdddlkqrgeksgieilslydaenlgkehfrkpvppsPEDLSIICFTSGTT 265
Cdd:cd17643 91 D-----------------------------------------------------------------PDDLAYVIYTSGST 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 266 GDPKGAMITHqnivSNASAFLKCVEHTFEPTPDDVTI---SY----------LPLAHmfervvqtvvyccGARVgffqgn 332
Cdd:cd17643 106 GRPKGVVVSH----ANVLALFAATQRWFGFNEDDVWTlfhSYafdfsvweiwGALLH-------------GGRL------ 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 333 irLLADDMNTLKPTLFPTVPR-----VLNriydkvqneaKTPlkkfllnlavaSKFKELqkgiirrdsfwdklifakIQA 407
Cdd:cd17643 163 --VVVPYEVARSPEDFARLLRdegvtVLN----------QTP-----------SAFYQL------------------VEA 201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 408 SLGG-----RVRIIVTGAAPISAPVMTFFRAAMGC---QVYEAYGQTECTAGCTFT--SPGDW---TSGHVGAPLTCNYV 474
Cdd:cd17643 202 ADRDgrdplALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFRplDAADLpaaAASPIGRPLPGLRV 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 475 KLEDvADMDYFSVNNEGEICIKGTNVFKGYLKDPEKTQE-------ALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKL 547
Cdd:cd17643 282 YVLD-ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI 360
|
490
....*....|..
gi 1622967304 548 aQGEYIAPEKIE 559
Cdd:cd17643 361 -RGFRIELGEIE 371
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
249-559 |
7.25e-14 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 74.66 E-value: 7.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 249 PPSPEDLSIICFTSGTTGDPKGAMITHQNIVSNASAFlkcVEHTFEPTPDDVTISYLPLAH-MfervvqtvvyccgARVG 327
Cdd:PRK09192 172 RPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAI---SHDGLKVRPGDRCVSWLPFYHdM-------------GLVG 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 328 FFqgnirlLADDMNTLKPTLFPTvprvlnriydkvQNEAKTPLKKFLL------NLAVASKFK-ELqkgIIRRDSFWDKl 400
Cdd:PRK09192 236 FL------LTPVATQLSVDYLPT------------RDFARRPLQWLDLisrnrgTISYSPPFGyEL---CARRVNSKDL- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 401 ifAKIQASlggRVRIIVTGAAPISAPVMTFF-----------RAAMGCqvyeaYGQTECTAGCTFTSPG----------D 459
Cdd:PRK09192 294 --AELDLS---CWRVAGIGADMIRPDVLHQFaeafapagfddKAFMPS-----YGLAEATLAVSFSPLGsgivveevdrD 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 460 WTSGH------------------VGAPLTCNYVKLEDVADmdyfSVNNE---GEICIKGTNVFKGYLKDPEkTQEALDSD 518
Cdd:PRK09192 364 RLEYQgkavapgaetrrvrtfvnCGKALPGHEIEIRNEAG----MPLPErvvGHICVRGPSLMSGYFRDEE-SQDVLAAD 438
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1622967304 519 GWLHTGDIGrWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIE 559
Cdd:PRK09192 439 GWLDTGDLG-YLLDGYLYITGRAKDLI-IINGRNIWPQDIE 477
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
135-575 |
1.02e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 74.33 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 135 VGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVICDTPQKASVlienveKGFTPSLKVVILMDP 214
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELL------DGLDPGVRVINVDSP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 215 FDDDLkqrgeksgieiLSLYDAENLGkehfrkPVPPSPEDLSIICFTSGTTGDPKGAMITHQNIVSNASAFlkcVEHtFE 294
Cdd:PRK07867 131 AWADE-----------LAAHRDAEPP------FRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVML---AQR-FG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 295 PTPDDVTISYLPLAHMfERVVQ--TVVYCCGARV---------GFFqgnirllaDDMNTLKPTLFPTVPRVLNRIY--DK 361
Cdd:PRK07867 190 LGPDDVCYVSMPLFHS-NAVMAgwAVALAAGASIalrrkfsasGFL--------PDVRRYGATYANYVGKPLSYVLatPE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 362 VQNEAKTPLKKFLLNLAVAskfkelqkGIIRRdsfwdklifakiqaslggrvriivtgaapisapvmtfFRAAMGCQVYE 441
Cdd:PRK07867 261 RPDDADNPLRIVYGNEGAP--------GDIAR-------------------------------------FARRFGCVVVD 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 442 AYGQTEctAGCTFTSPGDWTSGHVGaPLTCNyVKLEDV--------ADMDYFSVNNE----GEIC-IKGTNVFKGYLKDP 508
Cdd:PRK07867 296 GFGSTE--GGVAITRTPDTPPGALG-PLPPG-VAIVDPdtgtecppAEDADGRLLNAdeaiGELVnTAGPGGFEGYYNDP 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622967304 509 EKTQEALdSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIENIYNRSRPVLQIFVHG 575
Cdd:PRK07867 372 EADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPIERILLRYPDATEVAVYA 436
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
104-559 |
1.09e-13 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 74.02 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 104 RWLSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPL-YDTLGPEaIVYIVNKADIAM 182
Cdd:PRK06155 45 TRWTYAEAARAAAAAAHALAAAGVK--RGDRVALMCGNRIEFLDVFLGCAWLGAIAVPInTALRGPQ-LEHILRNSGARL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 183 VICDTPQKAsvLIENVEKGFTPSLKVVILmdpfdddlkqrGEKSGIEILSLYDAENLGKEHFRKP-VPPSPEDLSIICFT 261
Cdd:PRK06155 122 LVVEAALLA--ALEAADPGDLPLPAVWLL-----------DAPASVSVPAGWSTAPLPPLDAPAPaAAVQPGDTAAILYT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 262 SGTTGDPKGAMITHqnivsnASAFL--KCVEHTFEPTPDDVTISYLPLAHMfervvqtvvyccGARVGFFQGnirLLADD 339
Cdd:PRK06155 189 SGTTGPSKGVCCPH------AQFYWwgRNSAEDLEIGADDVLYTTLPLFHT------------NALNAFFQA---LLAGA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 340 MNTLKPTLFPTvprvlnRIYDKVQNEAKTPLkkFLLNlAVASKFKELQKGIIRRDSfwdklifakiqaslggRVRIIVTG 419
Cdd:PRK06155 248 TYVLEPRFSAS------GFWPAVRRHGATVT--YLLG-AMVSILLSQPARESDRAH----------------RVRVALGP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 420 AAPisAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTSPGD--WTSGHVGAPLTCNYVKLEDVADMDyfsvNNEGEICIKG 497
Cdd:PRK06155 303 GVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQrpGSMGRLAPGFEARVVDEHDQELPD----GEPGELLLRA 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622967304 498 TNVF---KGYLKDPEKTQEALdSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKlAQGEYIAPEKIE 559
Cdd:PRK06155 377 DEPFafaTGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIKDAIR-RRGENISSFEVE 439
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
92-553 |
5.40e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 72.00 E-value: 5.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 92 PCLGYRKPNQ-PYRWLSYKQVSDRAEYLGSCLLHKGYksSPDQFVGIFAQNRPEWIISELACYTysmVAVPLydtlGPEA 170
Cdd:PRK12582 66 PWLAQREPGHgQWRKVTYGEAKRAVDALAQALLDLGL--DPGRPVMILSGNSIEHALMTLAAMQ---AGVPA----APVS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 171 IVYIVNKADIAMV--ICDTPQKASVLIENVEKgFTPSLKVVILMDPfdddlkqrgeksgiEILSLY-DAENLGKEHFRKP 247
Cdd:PRK12582 137 PAYSLMSHDHAKLkhLFDLVKPRVVFAQSGAP-FARALAALDLLDV--------------TVVHVTgPGEGIASIAFADL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 248 V--PP-----------SPEDLSIICFTSGTTGDPKGAMITHQNIVSNASAflkcVEHTFEPTPDD---VTISYLPLAHMF 311
Cdd:PRK12582 202 AatPPtaavaaaiaaiTPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAM----QEQLRPREPDPpppVSLDWMPWNHTM 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 312 ervvqtvvyccGARVGFfQGNIR----LLADD--------MNTLK------PTLFPTVPRVLNRIYDKVQNEAKTpLKKF 373
Cdd:PRK12582 278 -----------GGNANF-NGLLWgggtLYIDDgkplpgmfEETIRnlreisPTVYGNVPAGYAMLAEAMEKDDAL-RRSF 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 374 LLNLAVASkfkelQKGIIRRDSFWDKLIFAKIQASlGGRVriivtgaapisaPVMTffraamgcqvyeAYGQTEcTAGCT 453
Cdd:PRK12582 345 FKNLRLMA-----YGGATLSDDLYERMQALAVRTT-GHRI------------PFYT------------GYGATE-TAPTT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 454 FTSpgDWTS---GHVGAPLTCNYVKLEDVADmdyfsvnnEGEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWL 530
Cdd:PRK12582 394 TGT--HWDTervGLIGLPLPGVELKLAPVGD--------KYEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFV 463
|
490 500
....*....|....*....|....*..
gi 1622967304 531 ----PNGTLKIIDRKKNIFKLAQGEYI 553
Cdd:PRK12582 464 dpddPEKGLIFDGRVAEDFKLSTGTWV 490
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
251-561 |
1.04e-12 |
|
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: 70.89 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 251 SPEDLSIICFTSGTTGDPKGAMITHQNIVSNASAFlkcVEHTFEPTPDDVTISYLPlAHMFERVVQTVVyccgarVGFFQ 330
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSL---SERYFGRDNGDEAVLFFS-NYVFDFFVEQMT------LALLN 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 331 GN-IRLLADDMNTLKPTLFPTVPRvlnriyDKVQNEAKTPlkkfllnlAVASKFkELQkgiiRRDSFwdklifakiqasl 409
Cdd:cd17648 162 GQkLVVPPDEMRFDPDRFYAYINR------EKVTYLSGTP--------SVLQQY-DLA----RLPHL------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 410 ggrVRIIVTGAApISAPVMTFFRAAMGCQVYEAYGQTEC--TAGCTFTSPGDWTSGHVGAPL--TCNYVkLEDvaDMDYF 485
Cdd:cd17648 210 ---KRVDAAGEE-FTAPVFEKLRSRFAGLIINAYGPTETtvTNHKRFFPGDQRFDKSLGRPVrnTKCYV-LND--AMKRV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 486 SVNNEGEICIKGTNVFKGYLKDPEKTQE-------------ALDSDGWLH-TGDIGRWLPNGTLKIIDRKKNIFKLaQGE 551
Cdd:cd17648 283 PVGAVGELYLGGDGVARGYLNRPELTAErflpnpfqteqerARGRNARLYkTGDLVRWLPSGELEYLGRNDFQVKI-RGQ 361
|
330
....*....|
gi 1622967304 552 YIAPEKIENI 561
Cdd:cd17648 362 RIEPGEVEAA 371
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
106-540 |
1.32e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 71.73 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVIC 185
Cdd:PRK12467 1600 LTYGELNRRANRLAHRLIALGVG--PEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLT 1677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 DTPQKASV-LIENVEkgftpslkvVILMDPFDDDLKQRGEksgieilslydaENLGkehfrkpVPPSPEDLSIICFTSGT 264
Cdd:PRK12467 1678 QSHLQARLpLPDGLR---------SLVLDQEDDWLEGYSD------------SNPA-------VNLAPQNLAYVIYTSGS 1729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 265 TGDPKGAMITHQNIVsnasAFLKCVEHTFEPTPDDVTISYLPLAhmFERVVQTVVY--CCGARVgffqgnirLLADDMNT 342
Cdd:PRK12467 1730 TGRPKGAGNRHGALV----NRLCATQEAYQLSAADVVLQFTSFA--FDVSVWELFWplINGARL--------VIAPPGAH 1795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 343 LKPtlfptvprvlNRIYDKVQNEAKTPLKKfllnlaVASKFKElqkgiirrdsfwdkliFAKIQASLGG--RVRIIVTG- 419
Cdd:PRK12467 1796 RDP----------EQLIQLIERQQVTTLHF------VPSMLQQ----------------LLQMDEQVEHplSLRRVVCGg 1843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 420 -AAPISA--PVMTFFRAAmgcQVYEAYGQTECTAGCTFtspgdWTSGHvGAPLTCNYVKL-EDVADMDYFSVNNE----- 490
Cdd:PRK12467 1844 eALEVEAlrPWLERLPDT---GLFNLYGPTETAVDVTH-----WTCRR-KDLEGRDSVPIgQPIANLSTYILDASlnpvp 1914
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622967304 491 ----GEICIKGTNVFKGYLKDPEKTQEAL------DSDGWLH-TGDIGRWLPNGTLKIIDR 540
Cdd:PRK12467 1915 igvaGELYLGGVGLARGYLNRPALTAERFvadpfgTVGSRLYrTGDLARYRADGVIEYLGR 1975
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
247-563 |
3.09e-12 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 69.54 E-value: 3.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 247 PVPPSPEDLSIICFTSGTTGDPKGAMITHQNIVSNASAflkcVEHTFEPTPDDVTISYLPLAHMFERvvqtvvyCCGarv 326
Cdd:PRK09274 168 MADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEA----LREDYGIEPGEIDLPTFPLFALFGP-------ALG--- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 327 gffqgnirlladdMNTLKPTLFPTVPRVLN--RIYDKVQNEAKTplkkfllNLAVASkfkelqkgiirrdSFWDKLIFAK 404
Cdd:PRK09274 234 -------------MTSVIPDMDPTRPATVDpaKLFAAIERYGVT-------NLFGSP-------------ALLERLGRYG 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 405 IQ--ASLGGRVRIIVTGaAPISAPVMTFFRAAM--GCQVYEAYGQTEC------------TAGCTFTSPGDwtsGH-VGA 467
Cdd:PRK09274 281 EAngIKLPSLRRVISAG-APVPIAVIERFRAMLppDAEILTPYGATEAlpissiesreilFATRAATDNGA---GIcVGR 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 468 PLTCNYVKLEDVAD--MDYFS------VNNEGEICIKGTNVFKGYLKDPEKTQEA--LDSDG--WLHTGDIGRWLPNGTL 535
Cdd:PRK09274 357 PVDGVEVRIIAISDapIPEWDdalrlaTGEIGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLGYLDAQGRL 436
|
330 340
....*....|....*....|....*...
gi 1622967304 536 KIIDRKKNIFKLAQGEYIaPEKIENIYN 563
Cdd:PRK09274 437 WFCGRKAHRVETAGGTLY-TIPCERIFN 463
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
106-570 |
3.33e-12 |
|
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: 69.20 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVIC 185
Cdd:cd17652 13 LTYAELNARANRLARLLAARGVG--PERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 dtpqkasvlienvekgftpslkvvilmdpfdddlkqrgeksgieilslydaenlgkehfrkpvppSPEDLSIICFTSGTT 265
Cdd:cd17652 91 -----------------------------------------------------------------TPDNLAYVIYTSGST 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 266 GDPKGAMITHQNIVSNASAFlkcVEHtFEPTPDDVTISYLPLAhmFERVVQTVV--YCCGARVgffqgnirLLADDmntl 343
Cdd:cd17652 106 GRPKGVVVTHRGLANLAAAQ---IAA-FDVGPGSRVLQFASPS--FDASVWELLmaLLAGATL--------VLAPA---- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 344 kPTLFPTVPrvlnrIYDKVQNEAKTPLkkfLLNLAVASKFKElqkgiirrdsfwdklifakiqASLGGRVRIIVTGAAPi 423
Cdd:cd17652 168 -EELLPGEP-----LADLLREHRITHV---TLPPAALAALPP---------------------DDLPDLRTLVVAGEAC- 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 424 SAPVMTffRAAMGCQVYEAYGQTECTAGCTFTSP-GDWTSGHVGAPL--TCNYV---KLEDVAdmdyfsVNNEGEICIKG 497
Cdd:cd17652 217 PAELVD--RWAPGRRMINAYGPTETTVCATMAGPlPGGGVPPIGRPVpgTRVYVldaRLRPVP------PGVPGELYIAG 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 498 TNVFKGYLKDPEKTQEALDSD------GWLH-TGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIENIYNRSRPVLQ 570
Cdd:cd17652 289 AGLARGYLNRPGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKI-RGFRIELGEVEAALTEHPGVAE 367
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
106-559 |
5.34e-12 |
|
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: 68.55 E-value: 5.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLlhKGYKSSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVIC 185
Cdd:cd17649 13 LSYAELDARANRLAHRL--RALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLLLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 DTPQKASVLIenvekgftpslkvvilmdpfdddlkqrgeksgieilslydaenlgkehfrkpvppspedlsiicFTSGTT 265
Cdd:cd17649 91 HHPRQLAYVI----------------------------------------------------------------YTSGST 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 266 GDPKGAMITHQNIVSNASAFLKCvehtFEPTPDDVTISYLPL----AHmfERVVQTVVycCGARVgffqgnirLLADdmn 341
Cdd:cd17649 107 GTPKGVAVSHGPLAAHCQATAER----YGLTPGDRELQFASFnfdgAH--EQLLPPLI--CGACV--------VLRP--- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 342 tlkPTLFPTVprvlNRIYDKVQNEAKTplkkfLLNLAVAskfkelqkgiirrdsFWDKLI--FAKIQASLGGRVRIIVTG 419
Cdd:cd17649 168 ---DELWASA----DELAEMVRELGVT-----VLDLPPA---------------YLQQLAeeADRTGDGRPPSLRLYIFG 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 420 AAPISApvmTFFRAAMGCQVY--EAYGQTECTAGCTF--TSPGD---WTSGHVGAPLTCNYVKLEDvADMDYFSVNNEGE 492
Cdd:cd17649 221 GEALSP---ELLRRWLKAPVRlfNAYGPTEATVTPLVwkCEAGAaraGASMPIGRPLGGRSAYILD-ADLNPVPVGVTGE 296
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622967304 493 ICIKGTNVFKGYLKDPEKTQEAL--DSDG-----WLHTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIE 559
Cdd:cd17649 297 LYIGGEGLARGYLGRPELTAERFvpDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-RGFRIELGEIE 369
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
250-563 |
1.04e-11 |
|
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: 67.49 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 250 PSPEDLSIICFTSGTTGDPKGAMITHQNIVSNASAflkcVEHTFEPTPDDVTISYLPLAHMFervvqtvvyccGARVGff 329
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDA----LRQLYGIRPGEVDLATFPLFALF-----------GPALG-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 330 qgnirlladdMNTLKPTLFPTVPRVLNriydkvQNEAKTPLKKFLLNLAVASkfkelqKGIIRRDSFWDklifAKIQASL 409
Cdd:cd05910 145 ----------LTSVIPDMDPTRPARAD------PQKLVGAIRQYGVSIVFGS------PALLERVARYC----AQHGITL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 410 GGRVRIIVTGaAPISAPVMTFFRAAM--GCQVYEAYGQTECTAGCT------FTSPGDWTSGH----VGAPLTCNYVKLE 477
Cdd:cd05910 199 PSLRRVLSAG-APVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrelLATTTAATSGGagtcVGRPIPGVRVRII 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 478 DVADMDYFSVNNE--------GEICIKGTNVFKGYLKDPEKTQEALDSDG----WLHTGDIGRWLPNGTLKIIDRKKNIF 545
Cdd:cd05910 278 EIDDEPIAEWDDTlelprgeiGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHRV 357
|
330
....*....|....*...
gi 1622967304 546 KLAQGEYIApEKIENIYN 563
Cdd:cd05910 358 ITTGGTLYT-EPVERVFN 374
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
106-561 |
1.75e-11 |
|
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: 66.77 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVIC 185
Cdd:cd05973 1 LTFGELRALSARFANALQELGVG--PGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 DTPQKASVlienvekgftpslkvvilmdpfdddlkqrgeksgieilslydaenlgkehfrkpvppsPEDLSIICFTSGTT 265
Cdd:cd05973 79 DAANRHKL----------------------------------------------------------DSDPFVMMFTSGTT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 266 GDPKGAMIThqniVSNASAFLKCVEHTFEPTPDDVtisylplahmfervvqtvvYCCGARVGFFQGNIRLLADDMNTLKP 345
Cdd:cd05973 101 GLPKGVPVP----LRALAAFGAYLRDAVDLRPEDS-------------------FWNAADPGWAYGLYYAITGPLALGHP 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 346 TLF-------PTVPRVLNRIydKVQNEAKTPLKKFLLNLAVASkfkelqkgiirrdsfwdklifakIQASLGGRVRIIVT 418
Cdd:cd05973 158 TILleggfsvESTWRVIERL--GVTNLAGSPTAYRLLMAAGAE-----------------------VPARPKGRLRRVSS 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 419 GAAPISAPVMTFFRAAMGCQVYEAYGQTEC-TAGCTFTSPGDWT-SGHVGAPLTCNYVKLEDvADMDYFSVNNEGEICIK 496
Cdd:cd05973 213 AGEPLTPEVIRWFDAALGVPIHDHYGQTELgMVLANHHALEHPVhAGSAGRAMPGWRVAVLD-DDGDELGPGEPGRLAID 291
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622967304 497 GTNV----FKGYLKDPEKTQealdSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENI 561
Cdd:cd05973 292 IANSplmwFRGYQLPDTPAI----DGGYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFDVESA 355
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
421-562 |
2.44e-11 |
|
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: 65.40 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 421 APISAPVMTFFRAAMGcqvyeaYGQTECTAGCTFTSPGDWTSGHVGAPLTCNYVKLEDVADMDyFSVNNEGEICIKGTNV 500
Cdd:cd17636 127 DMATVDTSPWGRKPGG------YGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDGRE-VPDGEVGEIVARGPTV 199
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622967304 501 FKGYLKDPEKTQEALdSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqgeyiapekIENIY 562
Cdd:cd17636 200 MAGYWNRPEVNARRT-RGGWHHTNDLGRREPDGSLSFVGPKTRMIKSG---------AENIY 251
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
107-561 |
2.96e-11 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 66.31 E-value: 2.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 107 SYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEwiisELACYTYSMVAVPLYDTLGP----EAIVYIVNKADIAM 182
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIK--LGDRVATIAWNTWR----HLEAWYGIMGIGAICHTVNPrlfpEQIAWIINHAEDRV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 183 VICDTpqkasVLIENVEK--GFTPSLK-VVILMDpfDDDLKQRGEKSGI---EILSLYDAENLGKEHfrkpvppsPEDLS 256
Cdd:PRK06018 115 VITDL-----TFVPILEKiaDKLPSVErYVVLTD--AAHMPQTTLKNAVayeEWIAEADGDFAWKTF--------DENTA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 257 I-ICFTSGTTGDPKGAMITHQnivSNasaflkcVEHTF-EPTPDDVTIS----YLPLAHMFERVVQTVVYCC-------- 322
Cdd:PRK06018 180 AgMCYTSGTTGDPKGVLYSHR---SN-------VLHALmANNGDALGTSaadtMLPVVPLFHANSWGIAFSApsmgtklv 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 323 --GARVGffQGNIRLLADdmnTLKPTLFPTVPRVLNRIYDKVQNEAKTplkkfLLNLavaskfkelqkgiirrdsfwdkl 400
Cdd:PRK06018 250 mpGAKLD--GASVYELLD---TEKVTFTAGVPTVWLMLLQYMEKEGLK-----LPHL----------------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 401 ifakiqaslggrvRIIVTGAAPISAPVMTFFRAaMGCQVYEAYGQTEctagctfTSPgdwtSGHVGApLTCNYVKLEDVA 480
Cdd:PRK06018 297 -------------KMVVCGGSAMPRSMIKAFED-MGVEVRHAWGMTE-------MSP----LGTLAA-LKPPFSKLPGDA 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 481 DMDY--------FSV--------NNE--------GEICIKGTNVFKGYLKdpeKTQEALDSDGWLHTGDIGRWLPNGTLK 536
Cdd:PRK06018 351 RLDVlqkqgyppFGVemkitddaGKElpwdgktfGRLKVRGPAVAAAYYR---VDGEILDDDGFFDTGDVATIDAYGYMR 427
|
490 500
....*....|....*....|....*
gi 1622967304 537 IIDRKKNIFKlAQGEYIAPEKIENI 561
Cdd:PRK06018 428 ITDRSKDVIK-SGGEWISSIDLENL 451
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
235-561 |
4.66e-11 |
|
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: 65.53 E-value: 4.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 235 DAENLGKEHFrKPVPPSPE-DLSIICFTSGTTGDPKGAMITHQNIVSNASAFLKCVEHTFEPTPddVTISYLPLAHmfer 313
Cdd:cd05915 135 LAYEEALGEE-ADPVRVPErAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKD--VVLPVVPMFH---- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 314 vvqTVVYCCGARVGFFQGNIRLLADDMNtlKPTLFPTVprvlnrIYDKVQNEAKTPLkkfLLNLAVASkfkelqkgiirR 393
Cdd:cd05915 208 ---VNAWCLPYAATLVGAKQVLPGPRLD--PASLVELF------DGEGVTFTAGVPT---VWLALADY-----------L 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 394 DSfwdklifakIQASLGGRVRIIVTGAAP----ISAPVMTFFRAAMGCQVYEAYG-QTECTAGCTFTSPGDWTSGHVGAP 468
Cdd:cd05915 263 ES---------TGHRLKTLRRLVVGGSAAprslIARFERMGVEVRQGYGLTETSPvVVQNFVKSHLESLSEEEKLTLKAK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 469 LTCN-YVKLEDVADMDYFSVNNEGE----ICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKN 543
Cdd:cd05915 334 TGLPiPLVRLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKD 413
|
330
....*....|....*...
gi 1622967304 544 IFKLAqGEYIAPEKIENI 561
Cdd:cd05915 414 LIKSG-GEWISSVDLENA 430
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
413-561 |
5.26e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 65.48 E-value: 5.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 413 VRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTEcTAGCTFTSPGDWTS--GHVGAPLTCNYVKLEDvaDMDYFSVNNE 490
Cdd:PRK13391 277 LEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATE-GLGFTACDSEEWLAhpGTVGRAMFGDLHILDD--DGAELPPGEP 353
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622967304 491 GEICIKGTNVFKgYLKDPEKTQEALDSDG-WLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENI 561
Cdd:PRK13391 354 GTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMI-ISGGVNIYPQEAENL 423
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
261-560 |
8.27e-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: 64.66 E-value: 8.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 261 TSGTTGDPKGAMITHQNIVSNASAflkCVEhTFEPTPDDVTISYLPLAHMFervvqtVVYCCGARVGFFQGNIRLLADDM 340
Cdd:cd05920 147 SGGTTGTPKLIPRTHNDYAYNVRA---SAE-VCGLDQDTVYLAVLPAAHNF------PLACPGVLGTLLAGGRVVLAPDP 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 341 NTLKptLFPTVPRvlnriyDKVQNEAKTPlkkfllnlAVASKFkeLQKGIIRRDSFwdklifakiqASLggrvRIIVTGA 420
Cdd:cd05920 217 SPDA--AFPLIER------EGVTVTALVP--------ALVSLW--LDAAASRRADL----------SSL----RLLQVGG 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 421 APISAPVMTFFRAAMGCQVYEAYGQTECTAGCT-FTSPGDWTSGHVGAPLtCNYVKLEdVADMDYFSV--NNEGEICIKG 497
Cdd:cd05920 265 ARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTrLDDPDEVIIHTQGRPM-SPDDEIR-VVDEEGNPVppGEEGELLTRG 342
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622967304 498 TNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIEN 560
Cdd:cd05920 343 PYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVEN 404
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
249-568 |
9.60e-11 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 64.79 E-value: 9.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 249 PPSPEDLSIICFTSGTTGDPKGAMITHQNIVSNASAFlkcVEHTFEPTPDDVTISYLPLAH-MFERVVQTvvyccgarvG 327
Cdd:PRK05851 148 PPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGL---NARVGLDAATDVGCSWLPLYHdMGLAFLLT---------A 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 328 FFQGNIRLLAddmntlkPT-LFPTVP-RVLNRIYDKVQNEAKTPlkkfllNLAVaskfkelqkGII----RRDSFWDKli 401
Cdd:PRK05851 216 ALAGAPLWLA-------PTtAFSASPfRWLSWLSDSRATLTAAP------NFAY---------NLIgkyaRRVSDVDL-- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 402 fakiqaslgGRVRIIVTGAAPISAPVMTFFRAAMG------CQVYEAYGQTECTAGCTFTSPG-----------DWTSGH 464
Cdd:PRK05851 272 ---------GALRVALNGGEPVDCDGFERFATAMApfgfdaGAAAPSYGLAESTCAVTVPVPGiglrvdevttdDGSGAR 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 465 ----VGAPLTCNYVKL---EDVADMDYFSVnneGEICIKGTNVFKGYLKdpektQEALDSDGWLHTGDIGrWLPNGTLKI 537
Cdd:PRK05851 343 rhavLGNPIPGMEVRIspgDGAAGVAGREI---GEIEIRGASMMSGYLG-----QAPIDPDDWFPTGDLG-YLVDGGLVV 413
|
330 340 350
....*....|....*....|....*....|.
gi 1622967304 538 IDRKKNIFKLAqGEYIAPEKIENIYNRSRPV 568
Cdd:PRK05851 414 CGRAKELITVA-GRNIFPTEIERVAAQVRGV 443
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
106-575 |
1.04e-10 |
|
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: 64.45 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADiamvic 185
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVG--KGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSE------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 dtpqkASVLIEnvekgfTPSLKvvilmdpfdddlkqrgEKSgieilslydaenlgkehfrkpvppSPEDLSIICFTSGTT 265
Cdd:cd05969 73 -----AKVLIT------TEELY----------------ERT------------------------DPEDPTLLHYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 266 GDPKGAMITHQNIVSNASAflkcVEHTFEPTPDDV-----------TISY---LPLAHMfervVQTVVYCCGARVGFFQG 331
Cdd:cd05969 102 GTPKGVLHVHDAMIFYYFT----GKYVLDLHPDDIywctadpgwvtGTVYgiwAPWLNG----VTNVVYEGRFDAESWYG 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 332 NIRlladdmnTLKPTLFPTVPRVLNRiydkvqneaktpLKKflLNLAVASKFKElqkgiirrdsfwdklifakiqASLgg 411
Cdd:cd05969 174 IIE-------RVKVTVWYTAPTAIRM------------LMK--EGDELARKYDL---------------------SSL-- 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 412 rvRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTSPG-DWTSGHVGAPLTCNYVKLEDvADMDYFSVNNE 490
Cdd:cd05969 210 --RFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYPCmPIKPGSMGKPLPGVKAAVVD-ENGNELPPGTK 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 491 GEICIKG--TNVFKGYLKDPEKTQEALdSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENIYNRSRPV 568
Cdd:cd05969 287 GILALKPgwPSMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHRVGPFEVESALMEHPAV 364
|
....*..
gi 1622967304 569 LQIFVHG 575
Cdd:cd05969 365 AEAGVIG 371
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
414-560 |
1.55e-10 |
|
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: 64.01 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 414 RIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTEctaG-CTFTSPGD--WTSGH-VGAPLtCNY--VKL-----EDVADM 482
Cdd:COG1021 303 RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---GlVNYTRLDDpeEVILTtQGRPI-SPDdeVRIvdedgNPVPPG 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 483 DyfsvnnEGEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNifklaQ----GEYIAPEKI 558
Cdd:COG1021 379 E------VGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKD-----QinrgGEKIAAEEV 447
|
..
gi 1622967304 559 EN 560
Cdd:COG1021 448 EN 449
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
397-561 |
1.68e-10 |
|
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: 63.74 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 397 WDKLIFAKIqASLGGRVRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCTfTSPGD-WTSGHVGAPLTCNYVK 475
Cdd:cd05974 187 WRMLIQQDL-ASFDVKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVG-NSPGQpVKAGSMGRPLPGYRVA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 476 LEDVADmdyfSVNNEGEICI-----KGTNVFKGYLKDPEKTQEALdSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKlAQG 550
Cdd:cd05974 265 LLDPDG----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SSD 338
|
170
....*....|.
gi 1622967304 551 EYIAPEKIENI 561
Cdd:cd05974 339 YRISPFELESV 349
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
166-561 |
1.90e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 63.96 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 166 LGPEAIVYIVNKADIAMVICDT---PqkasvLIENVEkGFTPSLKVVILMDpfDDDlkqRGEKSGIEILS---LYDAENL 239
Cdd:PRK07008 98 LFPEQIAYIVNHAEDRYVLFDLtflP-----LVDALA-PQCPNVKGWVAMT--DAA---HLPAGSTPLLCyetLVGAQDG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 240 GKEHfrkpvPPSPEDL-SIICFTSGTTGDPKGAMITHQNIVSNASAflkcvehtfEPTPDDVTIS----YLPLAHMFERV 314
Cdd:PRK07008 167 DYDW-----PRFDENQaSSLCYTSGTTGNPKGALYSHRSTVLHAYG---------AALPDAMGLSardaVLPVVPMFHVN 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 315 VQTVVYCC---GARVGF----FQGniRLLADDMNTLKPTLFPTVPRVLNRIYDKVQneaktplkkfllnlAVASKFKELQ 387
Cdd:PRK07008 233 AWGLPYSApltGAKLVLpgpdLDG--KSLYELIEAERVTFSAGVPTVWLGLLNHMR--------------EAGLRFSTLR 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 388 KGIIrrdsfwdklifakiqaslGGrvriivtGAAPisaPVM-TFFRAAMGCQVYEAYGQTECTAGCTFTSPgdwTSGHVG 466
Cdd:PRK07008 297 RTVI------------------GG-------SACP---PAMiRTFEDEYGVEVIHAWGMTEMSPLGTLCKL---KWKHSQ 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 467 APLTCNYVKLED----VADMDYFSVNNEG-----------EICIKGTNVFKGYLKdpeKTQEALDsDGWLHTGDIGRWLP 531
Cdd:PRK07008 346 LPLDEQRKLLEKqgrvIYGVDMKIVGDDGrelpwdgkafgDLQVRGPWVIDRYFR---GDASPLV-DGWFPTGDVATIDA 421
|
410 420 430
....*....|....*....|....*....|
gi 1622967304 532 NGTLKIIDRKKNIFKlAQGEYIAPEKIENI 561
Cdd:PRK07008 422 DGFMQITDRSKDVIK-SGGEWISSIDIENV 450
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
414-575 |
2.04e-10 |
|
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: 63.55 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 414 RIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTECTaGCTFTSPGDWTS--GHVGAPLTCNyVKLEDvADMDYFSVNNEG 491
Cdd:cd05929 247 KRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEGQ-GLTIINGEEWLThpGSVGRAVLGK-VHILD-EDGNEVPPGEIG 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 492 EICIKGTNVFKgYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENIYNRSRPVLQI 571
Cdd:cd05929 324 EVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIAHPKVLDA 401
|
....
gi 1622967304 572 FVHG 575
Cdd:cd05929 402 AVVG 405
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
242-570 |
2.07e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 64.42 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 242 EHFRKPVPPsPEDLSIICFTSGTTGDPKGAMITHQNIVSNASaflkCVEHTF--EPTPDDVTISYLPLAH---MFERVVQ 316
Cdd:PRK05691 156 EAWQEPALQ-PDDIAFLQYTSGSTALPKGVQVSHGNLVANEQ----LIRHGFgiDLNPDDVIVSWLPLYHdmgLIGGLLQ 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 317 TVvyccgarvgfFQGNIRLLaddmntLKPTLFPTVP-RVLNRI------------------YDKVQNEAKTPLKkfLLNL 377
Cdd:PRK05691 231 PI----------FSGVPCVL------MSPAYFLERPlRWLEAIseyggtisggpdfayrlcSERVSESALERLD--LSRW 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 378 AVASKFKElqkgIIRRDS---FWDKliFA-------KIQASLG-GRVRIIVTGAAPISA-PVMTFFRAAMGCQVYEAyGQ 445
Cdd:PRK05691 293 RVAYSGSE----PIRQDSlerFAEK--FAacgfdpdSFFASYGlAEATLFVSGGRRGQGiPALELDAEALARNRAEP-GT 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 446 TECTAGCTFTSPGDwtsghvgAPLTCNYVKLEDVADmdyfsvNNEGEICIKGTNVFKGYLKDPEKTQEA---LDSDGWLH 522
Cdd:PRK05691 366 GSVLMSCGRSQPGH-------AVLIVDPQSLEVLGD------NRVGEIWASGPSIAHGYWRNPEASAKTfveHDGRTWLR 432
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1622967304 523 TGDIGrWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENIYNRSRPVLQ 570
Cdd:PRK05691 433 TGDLG-FLRDGELFVTGRLKDML-IVRGHNLYPQDIEKTVEREVEVVR 478
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
106-559 |
3.53e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 63.82 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYksSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADiAMVIC 185
Cdd:PRK12316 3083 LSYAELNRRANRLAHRLIERGV--GPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSG-AQLLL 3159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 DTPQKASVLIENVEkgftpslkvVILMDPFDDDlkqrgeksgieilslYDAENLgkehfrkPVPPSPEDLSIICFTSGTT 265
Cdd:PRK12316 3160 SQSHLRLPLAQGVQ---------VLDLDRGDEN---------------YAEANP-------AIRTMPENLAYVIYTSGST 3208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 266 GDPKGAMITHQNIvsnaSAFLKCVEHTFEPTPDDVTISYLPLAHMFERVVQTVVYCCGARVgffqgnirLLADDMNTLKP 345
Cdd:PRK12316 3209 GKPKGVGIRHSAL----SNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARV--------VLAGPEDWRDP 3276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 346 TLFPTVprvlnriydkvqneaktpLKKFLLNLAVASKfkelqkgiirrdSFWDKLIFAKIQASLGGRVRIIVTGAApisA 425
Cdd:PRK12316 3277 ALLVEL------------------INSEGVDVLHAYP------------SMLQAFLEEEDAHRCTSLKRIVCGGEA---L 3323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 426 PVMTFFRAAMGCQVYEAYGQTECTAGCTFTSPGDWTSGH--VGAPLTCNYVKLEDVAdMDYFSVNNEGEICIKGTNVFKG 503
Cdd:PRK12316 3324 PADLQQQVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILDGS-LEPVPVGALGELYLGGEGLARG 3402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622967304 504 YLKDPEKTQEALDSDGW------LHTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIE 559
Cdd:PRK12316 3403 YHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQVKI-RGFRIELGEIE 3463
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
106-540 |
6.50e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 62.25 E-value: 6.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACyTYSMVAVPLYDT-LGPEAIVYIVNKADIAMVI 184
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVR--AGDGVAVLARNHRGFVLALYAA-GKVGARIILLNTgFSGPQLAEVAAREGVKALV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 185 CD---TPQ---------KASVLIENVEKGFTPSLKVVILmdpfdDDLKQRGEKSgieilslydaenlgkehfRKPVPPSP 252
Cdd:PRK07788 152 YDdefTDLlsalppdlgRLRAWGGNPDDDEPSGSTDETL-----DDLIAGSSTA------------------PLPKPPKP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 253 EdlSIICFTSGTTGDPKGAMITHQNIVSNASAFLKCVehtfePTPDDVTISyLPlAHMFervvQTVVYCCgARVGFFQGN 332
Cdd:PRK07788 209 G--GIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRV-----PFRAGETTL-LP-APMF----HATGWAH-LTLAMALGS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 333 ---IRLLADDMNTL------KPTLFPTVPRVLNRIYDkvqneaktplkkfllnlavaskfkELQKGIIRRDSfwdklifa 403
Cdd:PRK07788 275 tvvLRRRFDPEATLediakhKATALVVVPVMLSRILD------------------------LGPEVLAKYDT-------- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 404 kiqASLggrvRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTECtAGCTFTSPGDWT--SGHVG-APLTCNyVKLEDVA 480
Cdd:PRK07788 323 ---SSL----KIIFVSGSALSPELATRALEAFGPVLYNLYGSTEV-AFATIATPEDLAeaPGTVGrPPKGVT-VKILDEN 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 481 DMDyFSVNNEGEICIKGTNVFKGYLKDPEKTQEaldsDGWLHTGDIGRWLPNGTLKIIDR 540
Cdd:PRK07788 394 GNE-VPRGVVGRIFVGNGFPFEGYTDGRDKQII----DGLLSSGDVGYFDEDGLLFVDGR 448
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
417-560 |
9.61e-10 |
|
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: 61.71 E-value: 9.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 417 VTGAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTSPGDWTSGHVGAPLTCNYVKLEDVaDMDYFSVNNEGEICI- 495
Cdd:cd05928 297 VTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDD-NGNVLPPGTEGDIGIr 375
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622967304 496 ----KGTNVFKGYLKDPEKTQEALDSDGWLhTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIEN 560
Cdd:cd05928 376 vkpiRPFGLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYRIGPFEVES 442
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
104-540 |
9.62e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 62.28 E-value: 9.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 104 RWLSYKQVSDRAEYLGSCLLHKGYksSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMV 183
Cdd:PRK12316 4575 EKLTYAELNRRANRLAHALIARGV--GPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALL 4652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 184 ICDTPQKASVLIEnveKGFTpSLkvvilmdpfddDLKQRGEKSGieilslYDAENlgkehfrKPVPPSPEDLSIICFTSG 263
Cdd:PRK12316 4653 LTQSHLLQRLPIP---DGLA-SL-----------ALDRDEDWEG------FPAHD-------PAVRLHPDNLAYVIYTSG 4704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 264 TTGDPKGAMITHQNIVsnasAFLKCVEHTFEPTPDDVTISYLPLAhmFERVVQTV--VYCCGARVgffqgnirLLADDMN 341
Cdd:PRK12316 4705 STGRPKGVAVSHGSLV----NHLHATGERYELTPDDRVLQFMSFS--FDGSHEGLyhPLINGASV--------VIRDDSL 4770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 342 TLKPTLFptvpRVLNRIYDKVQNeaktplkkfllnlAVASKFKELQKGiirrdsfwdklifAKIQASLGGRVRIIVTGAA 421
Cdd:PRK12316 4771 WDPERLY----AEIHEHRVTVLV-------------FPPVYLQQLAEH-------------AERDGEPPSLRVYCFGGEA 4820
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 422 PISAPVMTFFRAAMGCQVYEAYGQTECTAGCT-FTSPGDWTSG----HVGAPL--TCNYVkLEDVADMdyFSVNNEGEIC 494
Cdd:PRK12316 4821 VAQASYDLAWRALKPVYLFNGYGPTETTVTVLlWKARDGDACGaaymPIGTPLgnRSGYV-LDGQLNP--LPVGVAGELY 4897
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1622967304 495 IKGTNVFKGYLKDPEKTQEALDSD------GWLH-TGDIGRWLPNGTLKIIDR 540
Cdd:PRK12316 4898 LGGEGVARGYLERPALTAERFVPDpfgapgGRLYrTGDLARYRADGVIDYLGR 4950
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
98-535 |
1.22e-09 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 61.06 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 98 KPNQP-YRWL----SYKQVSDRAEYLGSCLLHKGY-KSSPdqfVGIFAQNRPEWIISELAC----YTYsmvaVPLYDTLG 167
Cdd:PRK04813 15 QPDFPaYDYLgeklTYGQLKEDSDALAAFIDSLKLpDKSP---IIVFGHMSPEMLATFLGAvkagHAY----IPVDVSSP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 168 PEAIVYIVNKADIAMVICDTPqkasvliENVEKGFTPSLKVVILMDPFDDDLKqrgeksgieilslYDAENLGKEHfrkp 247
Cdd:PRK04813 88 AERIEMIIEVAKPSLIIATEE-------LPLEILGIPVITLDELKDIFATGNP-------------YDFDHAVKGD---- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 248 vppspeDLSIICFTSGTTGDPKGAMITHQNIVSnasaFLKCVEHTFePTPDDVTIsylpLAHM---FERVVQTvVYCCGA 324
Cdd:PRK04813 144 ------DNYYIIFTSGTTGKPKGVQISHDNLVS----FTNWMLEDF-ALPEGPQF----LNQApysFDLSVMD-LYPTLA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 325 RvGffqGNIRLLADDMnTLKP-TLFPTVPR-VLNR-----------IYDKVQNEAKTP-LKKFL-----LNLAVASKFKE 385
Cdd:PRK04813 208 S-G---GTLVALPKDM-TANFkQLFETLPQlPINVwvstpsfadmcLLDPSFNEEHLPnLTHFLfcgeeLPHKTAKKLLE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 386 lqkgiiRrdsfwdklifakiqaslggrvriivtgaapisapvmtfFRAAmgcQVYEAYGQTECTAGCtftspgdwTSGHV 465
Cdd:PRK04813 283 ------R--------------------------------------FPSA---TIYNTYGPTEATVAV--------TSIEI 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 466 GA-------PLTCNYVKledvADMDYFSVN---------NEGEICIKGTNVFKGYLKDPEKTQEAL-DSDGW--LHTGDI 526
Cdd:PRK04813 308 TDemldqykRLPIGYAK----PDSPLLIIDeegtklpdgEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDA 383
|
....*....
gi 1622967304 527 GRwLPNGTL 535
Cdd:PRK04813 384 GY-LEDGLL 391
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
135-275 |
1.88e-09 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 60.68 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 135 VGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADiAMVICDTPQkasvLIENVEKGFTPSLKVVILMDp 214
Cdd:PRK04319 101 VFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSE-AKVLITTPA----LLERKPADDLPSLKHVLLVG- 174
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622967304 215 fDDDlkqrgeKSGIEILSLYDAENLGKEHFRkPVPPSPEDLSIICFTSGTTGDPKG------AMITH 275
Cdd:PRK04319 175 -EDV------EEGPGTLDFNALMEQASDEFD-IEWTDREDGAILHYTSGSTGKPKGvlhvhnAMLQH 233
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
104-559 |
2.41e-09 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 60.10 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 104 RWLSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKAdiamv 183
Cdd:PRK12406 10 RRRSFDELAQRAARAAGGLAALGVR--PGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDS----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 184 icdtpqKASVLI------ENVEKGFTPSLKVVILMDPfdddlkqrgeksgIEILSLYdaeNLGKEHFRKPV--------- 248
Cdd:PRK12406 83 ------GARVLIahadllHGLASALPAGVTVLSVPTP-------------PEIAAAY---RISPALLTPPAgaidwegwl 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 249 --------PPSPEDLSIIcFTSGTTGDPKG----AMITHQnivsnASAFLKCVEHTFEPTPDDVTISYLPLAHmfervvq 316
Cdd:PRK12406 141 aqqepydgPPVPQPQSMI-YTSGTTGHPKGvrraAPTPEQ-----AAAAEQMRALIYGLKPGIRALLTGPLYH------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 317 TVVYCCGARVGFFQGNI----RLLADDMNTL----KPTLFPTVPRVLNRIYDkvqneaktplkkflLNLAVASKFKelqk 388
Cdd:PRK12406 208 SAPNAYGLRAGRLGGVLvlqpRFDPEELLQLierhRITHMHMVPTMFIRLLK--------------LPEEVRAKYD---- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 389 giirrdsfwdklifakiQASLggrvRIIVTGAAPISAPVmtffRAAM----GCQVYEAYGQTEcTAGCTFTSPGDWTS-- 462
Cdd:PRK12406 270 -----------------VSSL----RHVIHAAAPCPADV----KRAMiewwGPVIYEYYGSTE-SGAVTFATSEDALShp 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 463 GHVGAPLTCNYVKLEDvADMDYFSVNNEGEIC--IKGTNVFKgYLKDPEKTQEaLDSDGWLHTGDIGRWLPNGTLKIIDR 540
Cdd:PRK12406 324 GTVGKAAPGAELRFVD-EDGRPLPQGEIGEIYsrIAGNPDFT-YHNKPEKRAE-IDRGGFITSGDVGYLDADGYLFLCDR 400
|
490
....*....|....*....
gi 1622967304 541 KKNIFkLAQGEYIAPEKIE 559
Cdd:PRK12406 401 KRDMV-ISGGVNIYPAEIE 418
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
71-559 |
3.97e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 60.36 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 71 FSDATTMYEVFQRGLAISDNGPCLGYRKPNqpyrwLSYKQVSDRAEYLGSCLLHKGYksSPDQFVGIFAQNRPEWIISEL 150
Cdd:PRK12316 507 YPLQRGVHRLFEEQVERTPEAPALAFGEET-----LDYAELNRRANRLAHALIERGV--GPDVLVGVAMERSIEMVVALL 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 151 ACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVICDtpqkaSVLIENVEkgFTPSLKVVILMDPfdddlkqrgeksgIEI 230
Cdd:PRK12316 580 AILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQ-----SHLGRKLP--LAAGVQVLDLDRP-------------AAW 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 231 LSLYDAENLGKEhfrkpvpPSPEDLSIICFTSGTTGDPKGAMITHQNIVSNASAF-----LKCVEHTFEPTPDDVTIS-- 303
Cdd:PRK12316 640 LEGYSEENPGTE-------LNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMqqaygLGVGDTVLQKTPFSFDVSvw 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 304 --YLPLAHmfervvqtvvyccGAR-VGFFQGNIR---LLADDMNTLKPTLFPTVPRVLNRIYDKVQNEAKTPLKkfllnl 377
Cdd:PRK12316 713 efFWPLMS-------------GARlVVAAPGDHRdpaKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLR------ 773
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 378 avaskfkelqkgiirrdsfwdklifakiqaslggrvRIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTSP 457
Cdd:PRK12316 774 ------------------------------------RIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTC 817
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 458 GDWTSGHV--GAPLTCNYVKLEDvADMDYFSVNNEGEICIKGTNVFKGYLKDPEKTQEAL------DSDGWLHTGDIGRW 529
Cdd:PRK12316 818 VEEGGDSVpiGRPIANLACYILD-ANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFvpspfvAGERMYRTGDLARY 896
|
490 500 510
....*....|....*....|....*....|
gi 1622967304 530 LPNGTLKIIDRKKNIFKLaQGEYIAPEKIE 559
Cdd:PRK12316 897 RADGVIEYAGRIDHQVKL-RGLRIELGEIE 925
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
258-577 |
5.42e-09 |
|
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: 58.19 E-value: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 258 ICFTSGTTGDPKGAMITHQNIVsnasAFLKCVEHTFEPTPDDVTISYLPLAH-MFERVVQTVVYCCGARVGFFQGNIRLL 336
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERSWI----ESFVCNEDLFNISGEDAILAPGPLSHsLFLYGAISALYLGGTFIGQRKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 337 ADDMNTLKPTLFPTVPRVLNRIYDKVQNEAKtplkkfllnlaVASKFKELQKgiirrdsfWDKLIFAKIQAslggrvrii 416
Cdd:cd17633 81 IRKINQYNATVIYLVPTMLQALARTLEPESK-----------IKSIFSSGQK--------LFESTKKKLKN--------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 417 vtgAAPISapvmtffraamgcQVYEAYGQTEcTAGCTFTSPGD-WTSGHVGAPLTCNYVKLEDVADmdyfsvNNEGEICI 495
Cdd:cd17633 133 ---IFPKA-------------NLIEFYGTSE-LSFITYNFNQEsRPPNSVGRPFPNVEIEIRNADG------GEIGKIFV 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 496 KGTNVFKGYLKDPEktqeaLDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENIYNRSRPVLQIFVHG 575
Cdd:cd17633 190 KSEMVFSGYVRGGF-----SNPDGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIEEAIVVG 263
|
..
gi 1622967304 576 ES 577
Cdd:cd17633 264 IP 265
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
79-275 |
9.17e-09 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 58.66 E-value: 9.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 79 EVFQRGLAISDNGPCLGYRKPNQPYRWLSYKQVSDRAEYLGSCLLHKGYKSSpDQfVGIFAQNRPEWIISELACYTYSMV 158
Cdd:cd05968 65 QLLDKWLADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGLRALGVGKG-DR-VGIYLPMIPEIVPAFLAVARIGGI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 159 AVPLYDTLGPEAIVYIVNKADIAMVICD--TPQKASV--LIENVEKGFT--PSL-KVVILMDPFDDDLKQRGEKsgieil 231
Cdd:cd05968 143 VVPIFSGFGKEAAATRLQDAEAKALITAdgFTRRGREvnLKEEADKACAqcPTVeKVVVVRHLGNDFTPAKGRD------ 216
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622967304 232 SLYDAENlgKEHFRKPVPPSPEDLSIICFTSGTTGDPKGAMITH 275
Cdd:cd05968 217 LSYDEEK--ETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVH 258
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
104-540 |
1.16e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 58.63 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 104 RWLSYKQVSDRAEYLGSCLLHKGykSSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMV 183
Cdd:PRK12467 3119 QQLSYAELNRRANRLAHRLIAIG--VGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLL 3196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 184 IcdtpQKASVLienvekgftpslkvvilmdpfdddlKQRGEKSGIEILSLyDAENLGKEHFRKPVPPS-PEDLSIICFTS 262
Cdd:PRK12467 3197 L----TQAHLL-------------------------EQLPAPAGDTALTL-DRLDLNGYSENNPSTRVmGENLAYVIYTS 3246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 263 GTTGDPKGAMITHQNIVSNasafLKCVEHTFEPTPDDVTISYLPLAhmFERVVQTV--VYCCGARVGFFQGNIRlladDM 340
Cdd:PRK12467 3247 GSTGKPKGVGVRHGALANH----LCWIAEAYELDANDRVLLFMSFS--FDGAQERFlwTLICGGCLVVRDNDLW----DP 3316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 341 NTLKptlfptvpRVLNRIYDKVQNEAKTPLKKFLLnlavaskfkelqkgiirrdsfwdkliFAKIQAslGGRVRIIVTG- 419
Cdd:PRK12467 3317 EELW--------QAIHAHRISIACFPPAYLQQFAE--------------------------DAGGAD--CASLDIYVFGg 3360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 420 -AAPISApVMTFFRAAMGCQVYEAYGQTECTAGCT-FTSPGDWTSGHVGAP-------LTCnYV---KLEDVAdmdyfsV 487
Cdd:PRK12467 3361 eAVPPAA-FEQVKRKLKPRGLTNGYGPTEAVVTVTlWKCGGDAVCEAPYAPigrpvagRSI-YVldgQLNPVP------V 3432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 488 NNEGEICIKGTNVFKGYLKDPEKTQEAL------DSDGWLH-TGDIGRWLPNGTLKIIDR 540
Cdd:PRK12467 3433 GVAGELYIGGVGLARGYHQRPSLTAERFvadpfsGSGGRLYrTGDLARYRADGVIEYLGR 3492
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
106-573 |
1.46e-08 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. 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: 341309 [Multi-domain] Cd Length: 449 Bit Score: 57.48 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGykSSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIamvic 185
Cdd:cd17654 17 VSYADLAEKISNLSNFLRKKF--QTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHV----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 dtpqkaSVLIENvekgftpslkvvilmdpfdddlkqrgEKSGIEILSLYDAenlgKEHFRKPvppSPEDLSIICFTSGTT 265
Cdd:cd17654 90 ------SYLLQN--------------------------KELDNAPLSFTPE----HRHFNIR---TDECLAYVIHTSGTT 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 266 GDPKGAMITHQNIVSNASAFLKcvehTFEPTPDDVTISYLPLahMFERVVQTVVyccgarVGFFQGNIRLLADDMNTLKP 345
Cdd:cd17654 131 GTPKIVAVPHKCILPNIQHFRS----LFNITSEDILFLTSPL--TFDPSVVEIF------LSLSSGATLLIVPTSVKVLP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 346 TLFPTVPRVLNRIydkvQNEAKTP--LKKFLLnlavaskfKELQKGIIRRDSfwdklifakiqaSLggrvRIIVTG--AA 421
Cdd:cd17654 199 SKLADILFKRHRI----TVLQATPtlFRRFGS--------QSIKSTVLSATS------------SL----RVLALGgePF 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 422 PISAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTSPGDWTSG-HVGAPL--TCNYVKledvaDMDYFSVnnEGEICIKGT 498
Cdd:cd17654 251 PSLVILSSWRGKGNRTRIFNIYGITEVSCWALAYKVPEEDSPvQLGSPLlgTVIEVR-----DQNGSEG--TGQVFLGGL 323
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622967304 499 NVfKGYLKDPEKTQEALdsdgWLHTGDIGRwLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENIYNRSRPVLQIFV 573
Cdd:cd17654 324 NR-VCILDDEVTVPKGT----MRATGDFVT-VKDGELFFLGRKDSQIKRR-GKRINLDLIQQVIESCLGVESCAV 391
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
260-575 |
2.25e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 57.10 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 260 FTSGTTGDPKGAMITHQNIVSNasafLKCVEHTFEPTPDD-VTIS-YLPLAHMFERVVQTVvyccgarvgFFQGNIRLLa 337
Cdd:PRK07638 150 FTSGSTGKPKAFLRAQQSWLHS----FDCNVHDFHMKREDsVLIAgTLVHSLFLYGAISTL---------YVGQTVHLM- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 338 ddmntlkPTLFPtvprvlNRIYDKVQNEaktplkkfllNLAVASKFKELQKGiirrdsfwdkliFAKIQASLGGRVRIIV 417
Cdd:PRK07638 216 -------RKFIP------NQVLDKLETE----------NISVMYTVPTMLES------------LYKENRVIENKMKIIS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 418 TGA---APISAPVMTFFRAAmgcQVYEAYGQTECTAgCTFTSPGDWT--SGHVGAPltCNYVKLEDV-ADMDYFSVNNEG 491
Cdd:PRK07638 261 SGAkweAEAKEKIKNIFPYA---KLYEFYGASELSF-VTALVDEESErrPNSVGRP--FHNVQVRICnEAGEEVQKGEIG 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 492 EICIKGTNVFKGYLKDPEKTQEaLDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENIYNRSRPVLQI 571
Cdd:PRK07638 335 TVYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIESVLHEHPAVDEI 412
|
....
gi 1622967304 572 FVHG 575
Cdd:PRK07638 413 VVIG 416
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
413-560 |
3.71e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 56.45 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 413 VRIIVTGAAPISAPVmtffRAAM----GCQVYEAYGQTEcTAGCTFTSPGDWTS--GHVGAPLTCNyVKLEDvADMDYFS 486
Cdd:PRK08276 264 LRVAIHAAAPCPVEV----KRAMidwwGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGE-VRILD-EDGNELP 336
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622967304 487 VNNEGEICIK-GTNVFKgYLKDPEKTQEALDSDGWLHTGDIGrWL-PNGTLKIIDRKKNIFkLAQGEYIAPEKIEN 560
Cdd:PRK08276 337 PGEIGTVYFEmDGYPFE-YHNDPEKTAAARNPHGWVTVGDVG-YLdEDGYLYLTDRKSDMI-ISGGVNIYPQEIEN 409
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
413-561 |
1.79e-07 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 54.24 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 413 VRIIVTGAAPISAPVMTFFRAAmGCQVYEAYG--QTECTAGCTFTSPGDWT---SGHVGAPL--TCNYVKLEDVAD---M 482
Cdd:PRK05857 288 LRLVGYGGSRAIAADVRFIEAT-GVRTAQVYGlsETGCTALCLPTDDGSIVkieAGAVGRPYpgVDVYLAATDGIGptaP 366
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622967304 483 DYFSVNNEGEICIKGTNVFKGYLKDPEKTQEALdSDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENI 561
Cdd:PRK05857 367 GAGPSASFGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGGVNIAPDEVDRI 443
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
106-560 |
1.92e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 54.24 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYKssPDQFVGIFAQNRPEWIIselacYTYSMVAVPLYDTlgpeAIVYIVNKADIAMVIC 185
Cdd:PRK13390 25 VSYRQLDDDSAALARVLYDAGLR--TGDVVALLSDNSPEALV-----VLWAALRSGLYIT----AINHHLTAPEADYIVG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 DTPQKASVlienvekgftPSLKVVILMDPFDDDLKQRGEKSG-IEILSLYDAENLGKEhfrkpvPPSPEDL--SIICFTS 262
Cdd:PRK13390 94 DSGARVLV----------ASAALDGLAAKVGADLPLRLSFGGeIDGFGSFEAALAGAG------PRLTEQPcgAVMLYSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 263 GTTGDPKGAM--ITHQNIVSNASAFLKCVEHTFEPTPDDVTISYLPLAHMFERVVQTVVYCCGARVGFFQgniRLLADD- 339
Cdd:PRK13390 158 GTTGFPKGIQpdLPGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHAAPLRWCSMVHALGGTVVLAK---RFDAQAt 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 340 ---MNTLKPTLFPTVPRVLNRIYdKVQNEAKTplkkfllnlavaskfkelqkgiiRRDSfwdklifakiqASLggrvRII 416
Cdd:PRK13390 235 lghVERYRITVTQMVPTMFVRLL-KLDADVRT-----------------------RYDV-----------SSL----RAV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 417 VTGAAPISAPVMTFFRAAMGCQVYEAYGQTEcTAGCTFTSPGDWTS--GHVG-APLTCNYVKLEDVADMDyfsvnnEGEI 493
Cdd:PRK13390 276 IHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGrSVLGDLHICDDDGNELP------AGRI 348
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622967304 494 cikGTNVFK------GYLKDPEKTQEALDSDG--WLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIEN 560
Cdd:PRK13390 349 ---GTVYFErdrlpfRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQETEN 419
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
414-560 |
7.30e-07 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 52.30 E-value: 7.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 414 RIIVTGAAPISAPVMTFFRAAMGCQVYEAYGQTEctagctftspgdwtsGHVgapltcNYVKLED--------------- 478
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAE---------------GLV------NYTRLDDsderifttqgrpmsp 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 479 -----VADMDYFSV--NNEGEICIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNifklaQ-- 549
Cdd:PRK10946 362 ddevwVADADGNPLpqGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----Qin 436
|
170
....*....|...
gi 1622967304 550 --GEYIAPEKIEN 560
Cdd:PRK10946 437 rgGEKIAAEEIEN 449
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
254-575 |
9.00e-07 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 51.97 E-value: 9.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 254 DLSIICFTSGTTGDPKGAMITHQNIVsNASAFlkcVEHTFEPTPDDVTISYLPLAHmfeRVVQTVVYCCGARVGffqGNI 333
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAW-RGGAF---FAGSGGALPSDVLYTCLPLYH---STALIVGWSACLASG---ATL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 334 RL--------LADDMNTLKPTLFPTVPRVLnriydkvqneaktplkKFLLNlavaSKFKELQKGiirrdsfwdklifAKI 405
Cdd:cd05940 152 VIrkkfsasnFWDDIRKYQATIFQYIGELC----------------RYLLN----QPPKPTERK-------------HKV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 406 QASLGGRVRiivtgaAPISAPVMTFFRAAmgcQVYEAYGQTECTAGCTFTSPGDWTSGHVGAPLTCNY----VKLeDVAD 481
Cdd:cd05940 199 RMIFGNGLR------PDIWEEFKERFGVP---RIAEFYAATEGNSGFINFFGKPGAIGRNPSLLRKVAplalVKY-DLES 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 482 MDyfSVNNEGEICIK--------------GTNVFKGYLkDPEKTQEAL------DSDGWLHTGDIGRWLPNGTLKIIDRK 541
Cdd:cd05940 269 GE--PIRDAEGRCIKvprgepgllisrinPLEPFDGYT-DPAATEKKIlrdvfkKGDAWFNTGDLMRLDGEGFWYFVDRL 345
|
330 340 350
....*....|....*....|....*....|....
gi 1622967304 542 KNIFKLaQGEYIAPEKIENIYNRSRPVLQIFVHG 575
Cdd:cd05940 346 GDTFRW-KGENVSTTEVAAVLGAFPGVEEANVYG 378
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
246-310 |
1.00e-06 |
|
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: 51.91 E-value: 1.00e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622967304 246 KPVPPSPE------DLSIICFTSGTTGDPKGAMITHQNIVSnASAFLkcveHTFEPTPDDVTISYLPLAHM 310
Cdd:cd05938 131 EPVPASLRahvtikSPALYIYTSGTTGLPKAARISHLRVLQ-CSGFL----SLCGVTADDVIYITLPLYHS 196
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
104-561 |
1.46e-06 |
|
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: 51.42 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 104 RWLSYKQVSDRAEYLGSCLLHKGYKSSpdQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMV 183
Cdd:cd17634 83 RTISYRELHREVCRFAGTLLDLGVKKG--DRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 184 ICDT----PQKASVLIENVEKGFT---PSLKVVILMDPFDDDLKQRGEKSgieilSLYDAENLGKEHFRKPVPPSPEDLS 256
Cdd:cd17634 161 ITADggvrAGRSVPLKKNVDDALNpnvTSVEHVIVLKRTGSDIDWQEGRD-----LWWRDLIAKASPEHQPEAMNAEDPL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 257 IICFTSGTTGDPKGAMITHQNIVSNASAFLKcveHTFEPTPDDVTISYLPLAHMFERvvQTVVY---CCGARVGFFQGni 333
Cdd:cd17634 236 FILYTSGTTGKPKGVLHTTGGYLVYAATTMK---YVFDYGPGDIYWCTADVGWVTGH--SYLLYgplACGATTLLYEG-- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 334 rlladdmntlKPTlFPTVprvlNRIYDKVQNEAKTPLkkFLLNLAVASKFKELQKGIIRRDsfwdklifakiQASLggrv 413
Cdd:cd17634 309 ----------VPN-WPTP----ARMWQVVDKHGVNIL--YTAPTAIRALMAAGDDAIEGTD-----------RSSL---- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 414 RIIVTGAAPISAPVMTFFRAAMG---CQVYEAYGQTECTAGCTFTSPG--DWTSGHVGAPLTCNYVKLEDvADMDYFSVN 488
Cdd:cd17634 357 RILGSVGEPINPEAYEWYWKKIGkekCPVVDTWWQTETGGFMITPLPGaiELKAGSATRPVFGVQPAVVD-NEGHPQPGG 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 489 NEGEICIK-----GTnvfKGYLKDPEKTQEALDS--DGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIENI 561
Cdd:cd17634 436 TEGNLVITdpwpgQT---RTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVA-GHRLGTAEIESV 511
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
107-575 |
2.29e-06 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 50.51 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 107 SYKQVSDRAEYLGScLLHKGYKSSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVICD 186
Cdd:cd05937 7 TYSETYDLVLRYAH-WLHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVIVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 187 tpqkasvlienvekgftpslkvvilmdpfdddlkqrgeksgieilslydaenlgkehfrkpvppsPEDLSIICFTSGTTG 266
Cdd:cd05937 86 -----------------------------------------------------------------PDDPAILIYTSGTTG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 267 DPKGAMITHQNIVSNASAFlkcvEHTFEPTPDDVTISYLPLAHmfervvqtvvyccgaRVGFFQGNIRLLaddMNtlkpt 346
Cdd:cd05937 101 LPKAAAISWRRTLVTSNLL----SHDLNLKNGDRTYTCMPLYH---------------GTAAFLGACNCL---MS----- 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 347 lfptvprvlnriydkvqneAKTplkkfllnLAVASKFKELQkgiirrdsFWDklifakiQASLGGRVRIIVTG------- 419
Cdd:cd05937 154 -------------------GGT--------LALSRKFSASQ--------FWK-------DVRDSGATIIQYVGelcryll 191
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 420 AAPIS-----------------APVMTFFRAAMGC-QVYEAYGQTECTAGCTFTSPGDWTSGHVGAPLTCNYVKLEDV-- 479
Cdd:cd05937 192 STPPSpydrdhkvrvawgnglrPDIWERFRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKFENQvv 271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 480 -------ADMDYFS----------VNNEGEIC--IKGTNV--FKGYLKDPEKTQEAL------DSDGWLHTGDIGRWLPN 532
Cdd:cd05937 272 lvkmdpeTDDPIRDpktgfcvrapVGEPGEMLgrVPFKNReaFQGYLHNEDATESKLvrdvfrKGDIYFRTGDLLRQDAD 351
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1622967304 533 GTLKIIDRKKNIFKLaQGEYIAPEKIENIYNRSRPVLQIFVHG 575
Cdd:cd05937 352 GRWYFLDRLGDTFRW-KSENVSTTEVADVLGAHPDIAEANVYG 393
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
250-544 |
2.50e-06 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 50.04 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 250 PSPEDLSIICFTSGTTGDPKGAMITHQNIVSNASAflkcvEHTFEPTPDDVTISyLPLAHM--FERVVQTVV-----YCC 322
Cdd:PRK07824 32 PIDDDVALVVATSGTTGTPKGAMLTAAALTASADA-----THDRLGGPGQWLLA-LPAHHIagLQVLVRSVIagsepVEL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 323 GARVGFfqgNIRLLADDMNTLKPtlfptvprvlNRIYDKVqneAKTPLKKFLLNLAVASKFKELqkgiirrDSfwdklif 402
Cdd:PRK07824 106 DVSAGF---DPTALPRAVAELGG----------GRRYTSL---VPMQLAKALDDPAATAALAEL-------DA------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 403 akiqaslggrvriIVTGAAPISAPVMTFFRAAmGCQVYEAYGQTECTAGCTFTspgdwtsghvGAPLTCNYVKLEDvadm 482
Cdd:PRK07824 156 -------------VLVGGGPAPAPVLDAAAAA-GINVVRTYGMSETSGGCVYD----------GVPLDGVRVRVED---- 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622967304 483 dyfsvnneGEICIKGTNVFKGYLKDPEktQEALDSDGWLHTGDIGRwLPNGTLKIIDRKKNI 544
Cdd:PRK07824 208 --------GRIALGGPTLAKGYRNPVD--PDPFAEPGWFRTDDLGA-LDDGVLTVLGRADDA 258
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
106-575 |
7.30e-06 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 48.99 E-value: 7.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYKSsPDQfVGIFAQNRPEWIISELAcytysmvavplYDTLGPEAIVYIVNKADIAMVIC 185
Cdd:PRK13382 69 LTWRELDERSDALAAALQALPIGE-PRV-VGIMCRNHRGFVEALLA-----------ANRIGADILLLNTSFAGPALAEV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 DTPQKASVLIENVEkgFTPSLkvvilmdpfDDDLKQRGEKSGIEILSLYDA----ENLGKEHFRKPVPPSPEDLSIICFT 261
Cdd:PRK13382 136 VTREGVDTVIYDEE--FSATV---------DRALADCPQATRIVAWTDEDHdltvEVLIAAHAGQRPEPTGRKGRVILLT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 262 SGTTGDPKGAMITHQNIVSNASAFLkcvehtfEPTP---DDVTISYLPLAHMFervvqtvvyccgarvGFfqGNIRLLAD 338
Cdd:PRK13382 205 SGTTGTPKGARRSGPGGIGTLKAIL-------DRTPwraEEPTVIVAPMFHAW---------------GF--SQLVLAAS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 339 DMNTLkptlfptvprVLNRIYDKvqnEAktplkkfllNLAVASKFKElqKGIIRRDSFWDKL--IFAKIQASLGGR-VRI 415
Cdd:PRK13382 261 LACTI----------VTRRRFDP---EA---------TLDLIDRHRA--TGLAVVPVMFDRImdLPAEVRNRYSGRsLRF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 416 IVTGAAPISAPVMTFFRAAMGCQVYEAYGQTECTAGCTFTsPGDWTSG--HVGAPLTCNYVKLEDvADMDYFSVNNEGEI 493
Cdd:PRK13382 317 AAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIATAT-PADLRAApdTAGRPAEGTEIRILD-QDFREVPTGEVGTI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 494 CIKGTNVFKGYlkDPEKTQEAldSDGWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIENIYNRSRPVLQIFV 573
Cdd:PRK13382 395 FVRNDTQFDGY--TSGSTKDF--HDGFMASGDVGYLDENGRLFVVGRDDEMI-VSGGENVYPIEVEKTLATHPDVAEAAV 469
|
..
gi 1622967304 574 HG 575
Cdd:PRK13382 470 IG 471
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
246-300 |
1.41e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 48.50 E-value: 1.41e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622967304 246 KPVPPS-PEDLSIICFTSGTTGDPKGAMITHQNIVSNasafLKCVEHTFEPTPDDV 300
Cdd:PRK10252 590 APLQLSqPHHTAYIIFTSGSTGRPKGVMVGQTAIVNR----LLWMQNHYPLTADDV 641
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
252-540 |
1.49e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 48.63 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 252 PEDLSIICFTSGTTGDPKGAMITHQNIVSNasaflkcvehtfeptpddvTISYLPLAHMFER--VVQTVVYCCGARVGFF 329
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEQRGMLNN-------------------QLSKVPYLALSEAdvIAQTASQSFDISVWQF 3928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 330 qgnirlladdmntLKPTLFPTvpRVlnriyDKVQNE-AKTPlkKFLLNLAVASKFKELQK--GIIRRdsfwdklIFAKIQ 406
Cdd:PRK05691 3929 -------------LAAPLFGA--RV-----EIVPNAiAHDP--QGLLAHVQAQGITVLESvpSLIQG-------MLAEDR 3979
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 407 ASLGGRVRIIVTGAApisapvMTFFRAAMGCQVY------EAYGQTECTAGCTFTsPGDWTSGH-----VGAPLTCNYVK 475
Cdd:PRK05691 3980 QALDGLRWMLPTGEA------MPPELARQWLQRYpqiglvNAYGPAECSDDVAFF-RVDLASTRgsylpIGSPTDNNRLY 4052
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622967304 476 LEDvADMDYFSVNNEGEICIKGTNVFKGYLKDPEKTQEAL-------DSDGWLHTGDIGRWLPNGTLKIIDR 540
Cdd:PRK05691 4053 LLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFvphpfgaPGERLYRTGDLARRRSDGVLEYVGR 4123
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
443-560 |
5.25e-05 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 46.14 E-value: 5.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 443 YGQTEcTAG--CTFTsPGDWTSG--HVGAPLTCNYVKLEDvadmdyfsvNNEGEICIKGTNVFKGYLkdpektQEALDSD 518
Cdd:PRK07445 261 YGMTE-TASqiATLK-PDDFLAGnnSSGQVLPHAQITIPA---------NQTGNITIQAQSLALGYY------PQILDSQ 323
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1622967304 519 GWLHTGDIGRWLPNGTLKIIDRKKNIFkLAQGEYIAPEKIEN 560
Cdd:PRK07445 324 GIFETDDLGYLDAQGYLHILGRNSQKI-ITGGENVYPAEVEA 364
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
106-559 |
7.36e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 46.31 E-value: 7.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 106 LSYKQVSDRAEYLGSCLLHKGYksSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYIVNKADIAMVIc 185
Cdd:PRK05691 1157 LDYAELHAQANRLAHYLRDKGV--GPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLL- 1233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 186 dtpqKASVLIENVekgftPSLKVVILMDPfdDDLKQRGEKSGIEILSLYDaenlgkehfrkpvppspEDLSIICFTSGTT 265
Cdd:PRK05691 1234 ----TQSHLLERL-----PQAEGVSAIAL--DSLHLDSWPSQAPGLHLHG-----------------DNLAYVIYTSGST 1285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 266 GDPKGAMITHQNIVSNasafLKCVEHTFEPTPDDVTISYLPLAhmFErvvqTVVYCC------GARVgffqgnirLLADD 339
Cdd:PRK05691 1286 GQPKGVGNTHAALAER----LQWMQATYALDDSDVLMQKAPIS--FD----VSVWECfwplitGCRL--------VLAGP 1347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 340 MNTLKPtlfptvprvlNRIYDKVQNEAKTPLKkFLLNLavaskfkeLQkgiirrdsfwdkLIFAKIQASLGGRVRIIVTG 419
Cdd:PRK05691 1348 GEHRDP----------QRIAELVQQYGVTTLH-FVPPL--------LQ------------LFIDEPLAAACTSLRRLFSG 1396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 420 AAPISAPVMTFFRAAM-GCQVYEAYGQTE---------CTAGCTFTSPgdwtsghVGAPLTCNYVKLEDvADMDYFSVNN 489
Cdd:PRK05691 1397 GEALPAELRNRVLQRLpQVQLHNRYGPTEtainvthwqCQAEDGERSP-------IGRPLGNVLCRVLD-AELNLLPPGV 1468
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622967304 490 EGEICIKGTNVFKGYLKDPEKTQE-----ALDSDG--WLHTGDIGRWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIE 559
Cdd:PRK05691 1469 AGELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL-RGFRVEPEEIQ 1544
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
260-309 |
1.02e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 45.32 E-value: 1.02e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1622967304 260 FTSGTTGDPKGAMITHQNIVSN----ASAFLkcVEHTFEPTPDDVTISYLPLAH 309
Cdd:PRK05850 167 YTSGSTRTPAGVMVSHRNVIANfeqlMSDYF--GDTGGVPPPDTTVVSWLPFYH 218
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
104-309 |
5.35e-04 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports 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 FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 43.18 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 104 RWLSYKQVSDRAEYLGSCLLHKGYKSSpdQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVYivnkadiamv 183
Cdd:cd05939 2 RHWTFRELNEYSNKVANFFQAQGYRSG--DVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLH---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 184 iCDTPQKASVLIENvekgftpslkvviLMDPFDDDLKQRgeksgieilslydaenlgkehfrkpvPPSPEDL---SIICF 260
Cdd:cd05939 70 -CITVSKAKALIFN-------------LLDPLLTQSSTE--------------------------PPSQDDVnfrDKLFY 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622967304 261 --TSGTTGDPKGAMITHQNIVSNASAflkcVEHTFEPTPDDVTISYLPLAH 309
Cdd:cd05939 110 iyTSGTTGLPKAAVIVHSRYYRIAAG----AYYAFGMRPEDVVYDCLPLYH 156
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
246-544 |
5.83e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 43.18 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 246 KPVPPSPEDLSIICFTSGTTGDPKGAMITHQNIVSNASAFLKCVehtfEPTPDDVTISYLPLAHMFERVVQTVVYCCGAR 325
Cdd:PRK07769 173 VPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDAL----EGQEGDRGVSWLPFFHDMGLITVLLPALLGHY 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 326 VGFfqgnirlladdmntLKPTLFPTVP-RVLNRIYDKVQNEAKTplkkfllnLAVASKFK-EL--QKGIIRRDSF-WDKl 400
Cdd:PRK07769 249 ITF--------------MSPAAFVRRPgRWIRELARKPGGTGGT--------FSAAPNFAfEHaaARGLPKDGEPpLDL- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 401 ifakiqaslgGRVRIIVTGAAPISAPVMTFFRAAMG------CQVYEAYGQTECTAGCTfTSPGD------------WTS 462
Cdd:PRK07769 306 ----------SNVKGLLNGSEPVSPASMRKFNEAFApyglppTAIKPSYGMAEATLFVS-TTPMDeeptviyvdrdeLNA 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 463 GHV-----GAP-----LTCNYVKLEDVADMdyfsVNNE----------GEICIKGTNVFKGYLKDPEKTQE--------- 513
Cdd:PRK07769 375 GRFvevpaDAPnavaqVSAGKVGVSEWAVI----VDPEtaselpdgqiGEIWLHGNNIGTGYWGKPEETAAtfqnilksr 450
|
330 340 350
....*....|....*....|....*....|....*....
gi 1622967304 514 --------ALDSDGWLHTGDIGRWLpNGTLKIIDRKKNI 544
Cdd:PRK07769 451 lseshaegAPDDALWVRTGDYGVYF-DGELYITGRVKDL 488
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
253-309 |
8.99e-04 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 42.55 E-value: 8.99e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622967304 253 EDLSIICFTSGTTGDPKGAMITHQNIVSNASAFlkcvEHTFEPTPDDVTISYLPLAH 309
Cdd:PRK08279 199 KDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGF----GGLLRLTPDDVLYCCLPLYH 251
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
414-559 |
1.10e-03 |
|
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: 41.98 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 414 RIIVTGAAPISAPVMTFFRAAM-GCQVYEAYGQTECTAGCTFTSPGdwtSGHVGAPLTcNYVKLEDVADMDYFSV----N 488
Cdd:cd05924 137 FAISSGGALLSPEVKQGLLELVpNITLVDAFGSSETGFTGSGHSAG---SGPETGPFT-RANPDTVVLDDDGRVVppgsG 212
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622967304 489 NEGEICIKGtNVFKGYLKDPEKTQEA---LDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAqGEYIAPEKIE 559
Cdd:cd05924 213 GVGWIARRG-HIPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTG-GEKVFPEEVE 284
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
236-575 |
4.30e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 40.40 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 236 AENLGKEHFRKPV-PPSPEDLSIICFTSGTTGDPKGAMITHQNIVSNASAFLKcvehTFEPTPDDVTISYLPLAHMfERV 314
Cdd:PRK13388 132 AELVAAAGALTPHrEVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTE----RFGLTRDDVCYVSMPLFHS-NAV 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 315 VQ--TVVYCCGARV---------GFFqgnirllaDDMNTLKPTLFPTVPRVLNRIYDKVQ--NEAKTPLkkfllnlavas 381
Cdd:PRK13388 207 MAgwAPAVASGAAValpakfsasGFL--------DDVRRYGATYFNYVGKPLAYILATPErpDDADNPL----------- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 382 kfkelqkgiirrdsfwdklifakiQASLGgrvriivTGAAP--ISApvmtfFRAAMGCQVYEAYGQTEctAGCTFTSPGD 459
Cdd:PRK13388 268 ------------------------RVAFG-------NEASPrdIAE-----FSRRFGCQVEDGYGSSE--GAVIVVREPG 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967304 460 WTSGHVGAP------LTCNYVKLEDVADMD-YFSVNNE----GEICIK-GTNVFKGYLKDPEKTQEALdSDGWLHTGDIG 527
Cdd:PRK13388 310 TPPGSIGRGapgvaiYNPETLTECAVARFDaHGALLNAdeaiGELVNTaGAGFFEGYYNNPEATAERM-RHGMYWSGDLA 388
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1622967304 528 RWLPNGTLKIIDRKKNIFKLaQGEYIAPEKIENIYNRSRPVLQIFVHG 575
Cdd:PRK13388 389 YRDADGWIYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYA 435
|
|
| |
