|
Name |
Accession |
Description |
Interval |
E-value |
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
116-693 |
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: 968.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 116 QPYKWLSYKEVADRAEFAGSALLHRGHSQSGDKYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASI 195
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 196 TTIICDIadkarlildcvsgrkhsvttivimesfdseltaqaqncGIDIISLKELEAIGKANHKTPIPPKPEDLALICFT 275
Cdd:cd05927 81 SIVFCDA--------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICYT 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 276 SGTTGNPKGAMLTHGNVVSNCSAFIKITEESLKLCPQDVLISFLPLAHMFERVVEGVLLCHGAKIGYFQGDIRLLMDDLK 355
Cdd:cd05927 123 SGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDIK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 356 NLKPTIFPVVPRLLNRMFDKIFG--QANTPLKRWLLDFATSRKEAELKSGVVRKDSMWDKLIFSKVQASLGGRVRLMITG 433
Cdd:cd05927 203 ALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLTG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 434 AAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDVAEMNYFAA--NGEGEVCVKG 511
Cdd:cd05927 283 SAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAKdpNPRGEVCIRG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 512 PNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSDPVAQVFVHGDS 591
Cdd:cd05927 363 PNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGDS 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 592 LQACLVGVVVPDPDFLPGWAK-NRGIEGSFNDLCKSKEVKNAILEDMIQLGKEAGLKSFEQVRDIALHLEMFSVQNGLLT 670
Cdd:cd05927 443 LKSFLVAIVVPDPDVLKEWAAsKGGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLLT 522
|
570 580
....*....|....*....|...
gi 528467780 671 PTLKAKRTELKSRFREQIDQLYA 693
Cdd:cd05927 523 PTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
88-695 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 714.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 88 DALTLYEFFLRGLRVSNNGPCLGSRKA--GQP--YKWLSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTIS 163
Cdd:PLN02736 42 EIGTLHDNFVYAVETFRDYKYLGTRIRvdGTVgeYKWMTYGEAGTARTAIGSGLVQHG-IPKGAC-VGLYFINRPEWLIV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 164 ELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIICdIADKARLILDCVSgRKHSVTTIVIMESFDSELTAQAQNCGID 243
Cdd:PLN02736 120 DHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCLS-EIPSVRLIVVVGGADEPLPSLPSGTGVE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 244 IISLKELEAIGKANHKTPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAfikiTEESLKLCPQDVLISFLPLAH 323
Cdd:PLN02736 198 IVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAG----SSLSTKFYPSDVHISYLPLAH 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 324 MFERVVEGVLLCHGAKIGYFQGDIRLLMDDLKNLKPTIFPVVPRLLNRMFDKIFG--QANTPLKRWLLDFATSRKEAELK 401
Cdd:PLN02736 274 IYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNavKESGGLKERLFNAAYNAKKQALE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 402 SGvvRKDS-MWDKLIFSKVQASLGGRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTEctAGCTMSL--PGDWTAGH 478
Cdd:PLN02736 354 NG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTE--TSCVISGmdEGDNLSGH 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 479 VGAPLPCNFVKLVDVAEMNYFAANG---EGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRK 555
Cdd:PLN02736 430 VGSPNPACEVKLVDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRK 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 556 KHIFKLAQGEYIAPEKIENIYIRSDPVAQVFVHGDSLQACLVGVVVPDPDFLPGWAKNRGIE-GSFNDLCKSKEVKNAIL 634
Cdd:PLN02736 510 KNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRVRAAVL 589
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528467780 635 EDMIQLGKEAGLKSFEQVRDIALHLEMFSVQNGLLTPTLKAKRTELKSRFREQIDQLYAKI 695
Cdd:PLN02736 590 ADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYAEL 650
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
86-694 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 530.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 86 YKDALTLYEFFLRGLRVSNNGPCLGSRKAGQpYKWLSYKEVADRAEFAGSALLHRGHsQSGDKyIGIFAQNRPEWTISEL 165
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVALREKEDGI-WQSLTWAEFAERVRALAAGLLALGV-KPGDR-VAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 166 ACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC---DIADKARLILDCVSgrkhSVTTIVIMEsfdseltAQAQNCGI 242
Cdd:COG1022 84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVedqEQLDKLLEVRDELP----SLRHIVVLD-------PRGLRDDP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 243 DIISLKELEAIGKAnHKTPI-------PPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIkiteESLKLCPQDVL 315
Cdd:COG1022 153 RLLSLDELLALGRE-VADPAelearraAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALL----ERLPLGPGDRT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 316 ISFLPLAHMFERVVEGVLLCHGAKIgYFQGDIRLLMDDLKNLKPTIFPVVPRLLNRMFDKIFGQAN--TPLKRWLLDFA- 392
Cdd:COG1022 228 LSFLPLAHVFERTVSYYALAAGATV-AFAESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEeaGGLKRKLFRWAl 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 393 -TSRKEAELK------SGVVR-KDSMWDKLIFSKVQASLGGRVRLMITGAAPVSPTVLTFLRAaLGCQFYEGYGQTECTA 464
Cdd:COG1022 307 aVGRRYARARlagkspSLLLRlKHALADKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 465 GCTMSLPGDWTAGHVGAPLPCNFVKLvdvAEmnyfaangEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWL 544
Cdd:COG1022 386 VITVNRPGDNRIGTVGPPLPGVEVKI---AE--------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELD 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 545 PNGTLKIIDRKKHIFKLAQGEYIAPEKIENIyIRSDP-VAQVFVHGDSlQACLVGVVVPDPDFLPGWAKNRGIE-GSFND 622
Cdd:COG1022 455 EDGFLRITGRKKDLIVTSGGKNVAPQPIENA-LKASPlIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGLPyTSYAE 532
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528467780 623 LCKSKEVKNAILEDMIQLgkEAGLKSFEQVRDIALHLEMFSVQNGLLTPTLKAKRTELKSRFREQIDQLYAK 694
Cdd:COG1022 533 LAQDPEVRALIQEEVDRA--NAGLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYAG 602
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
116-677 |
2.96e-163 |
|
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: 477.09 E-value: 2.96e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 116 QPYKWLSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASI 195
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALG-VEPGDR-VAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 196 TTIICDiadkarlildcvsgrkhsvttivimesfdseltaqaqncgidiislkeleaigkanhktpippKPEDLALICFT 275
Cdd:cd05907 79 KALFVE---------------------------------------------------------------DPDDLATIIYT 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 276 SGTTGNPKGAMLTHGNVVSNCSAFIKITEESlklcPQDVLISFLPLAHMFERV-VEGVLLCHGAKIGYFQgDIRLLMDDL 354
Cdd:cd05907 96 SGTTGRPKGVMLSHRNILSNALALAERLPAT----EGDRHLSFLPLAHVFERRaGLYVPLLAGARIYFAS-SAETLLDDL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 355 KNLKPTIFPVVPRLLNRMFDKIFGQANTPLKRWLLDFAtsrkeaelksgvvrkdsmwdklifskvqasLGGRVRLMITGA 434
Cdd:cd05907 171 SEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLA------------------------------VGGRLRFAASGG 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 435 APVSPTVLTFLRAaLGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDvaemnyfaangEGEVCVKGPNV 514
Cdd:cd05907 221 APLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPNV 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 515 FQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSDPVAQVFVHGDSlQA 594
Cdd:cd05907 289 MLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDG-RP 367
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 595 CLVGVVVPDPDFLPGWAKNRGIEG-SFNDLCKSKEVKNAILEDMIQLGkeAGLKSFEQVRDIALHLEMFSVQNGLLTPTL 673
Cdd:cd05907 368 FLVALIVPDPEALEAWAEEHGIAYtDVAELAANPAVRAEIEAAVEAAN--ARLSRYEQIKKFLLLPEPFTIENGELTPTL 445
|
....
gi 528467780 674 KAKR 677
Cdd:cd05907 446 KLKR 449
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
117-695 |
2.15e-161 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 480.08 E-value: 2.15e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 117 PYKWLSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASIT 196
Cdd:PLN02430 73 PYMWKTYKEVYEEVLQIGSALRASG-AEPGSR-VGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEID 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 197 TI-ICDIADKARLILDCVSGRKhsVTTIVIMESFDSELTAQAQNCGIDIISLKELEAIGKANHKTPIPPKPEDLALICFT 275
Cdd:PLN02430 151 FVfVQDKKIKELLEPDCKSAKR--LKAIVSFTSVTEEESDKASQIGVKTYSWIDFLHMGKENPSETNPPKPLDICTIMYT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 276 SGTTGNPKGAMLTHGNV---VSNCSAFIKITEEslKLCPQDVLISFLPLAHMFERVVEGVLLCHGAKIGYFQGDIRLLMD 352
Cdd:PLN02430 229 SGTSGDPKGVVLTHEAVatfVRGVDLFMEQFED--KMTHDDVYLSFLPLAHILDRMIEEYFFRKGASVGYYHGDLNALRD 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 353 DLKNLKPTIFPVVPRLLNRMFDKIFG--QANTPLKRWLLDFATSRKEAELKSGVVRKDS--MWDKLIFSKVQASLGGRVR 428
Cdd:PLN02430 307 DLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYKYKLAWMNRGYSHKKAspMADFLAFRKVKAKLGGRLR 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 429 LMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTA-GHVGAPLPCNFVKLVDVAEMNY--FAANGEG 505
Cdd:PLN02430 387 LLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMCMlGTVGAPAVYNELRLEEVPEMGYdpLGEPPRG 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 506 EVCVKGPNVFQGYLKDPEQTSgAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSDPVAQV 585
Cdd:PLN02430 467 EICVRGKCLFSGYYKNPELTE-EVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDI 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 586 FVHGDSLQACLVGVVVPDPDFLPGWAKNRGIEGSFNDLCKSKEVKNAILEDMIQLGKEAGLKSFEQVRDIALHLEMFSVQ 665
Cdd:PLN02430 546 WVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKEHILSELKSTAEKNKLRGFEYIKGVILETKPFDVE 625
|
570 580 590
....*....|....*....|....*....|
gi 528467780 666 NGLLTPTLKAKRTELKSRFREQIDQLYAKI 695
Cdd:PLN02430 626 RDLVTATLKKRRNNLLKYYQVEIDEMYRKL 655
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
117-680 |
4.21e-160 |
|
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: 471.31 E-value: 4.21e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 117 PYKWLSYKEVADRAEFAGSALLHRGHsQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASIT 196
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLVELGL-KPGDK-VAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 197 TIICDiadkarlildcvsgrkhsvttivimesfdseltaqaqncgidiislkeleaigkanhktpipPKPEDLALICFTS 276
Cdd:cd17639 80 AIFTD--------------------------------------------------------------GKPDDLACIMYTS 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 277 GTTGNPKGAMLTHGNVVSNCSAFIKITEESLklCPQDVLISFLPLAHMFERVVEGVLLCHGAKIGYfqGDIRLLMD---- 352
Cdd:cd17639 98 GSTGNPKGVMLTHGNLVAGIAGLGDRVPELL--GPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDkskr 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 353 ----DLKNLKPTIFPVVPRLLNRMFDKIFGQANTP--LKRWLLDFATSRKEAELKSGvvrKDSM-WDKLIFSKVQASLGG 425
Cdd:cd17639 174 gckgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMggLKRTLFWTAYQSKLKALKEG---PGTPlLDELVFKKVRAALGG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 426 RVRLMITGAAPVSPTVLTFLrAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDVAEMNYFAANGE- 504
Cdd:cd17639 251 RLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDKPPp 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 505 -GEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSDPVA 583
Cdd:cd17639 330 rGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVN 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 584 QVFVHGDSLQACLVGVVVPDPDFLPGWA-KNRGIEGSFNDLCKSKEVKNAILEDMIQLGKEAGLKSFEQVRDIALHLEMF 662
Cdd:cd17639 410 NICVYADPDKSYPVAIVVPNEKHLTKLAeKHGVINSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEW 489
|
570
....*....|....*...
gi 528467780 663 SVQNGLLTPTLKAKRTEL 680
Cdd:cd17639 490 TPENGLVTAAQKLKRKEI 507
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
87-696 |
1.56e-155 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 465.09 E-value: 1.56e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 87 KDALTLYEFFLRGLRVSNNGPCLGSR-----KAGqPYKWLSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWT 161
Cdd:PLN02861 40 ADIDSPWQFFSDAVKKYPNNQMLGRRqvtdsKVG-PYVWLTYKEVYDAAIRIGSAIRSRG-VNPGDR-CGIYGSNCPEWI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 162 ISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIICDiADKARLILDCVSGRKHSVTTIVIMESFDSELTAQAQNCG 241
Cdd:PLN02861 117 IAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQ-ESKISSILSCLPKCSSNLKTIVSFGDVSSEQKEEAEELG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 242 IDIISLKELEAIGKANHKTPiPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEESLKLCPQ-DVLISFLP 320
Cdd:PLN02861 196 VSCFSWEEFSLMGSLDCELP-PKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKVTDRVATEeDSYFSYLP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 321 LAHMFERVVEGVLLCHGAKIGYFQGDIRLLMDDLKNLKPTIFPVVPRLLNRMFDKIFG--QANTPLKRWLLDFATSRKEA 398
Cdd:PLN02861 275 LAHVYDQVIETYCISKGASIGFWQGDIRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQkiSSGGMLRKKLFDFAYNYKLG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 399 ELKSGVVRKDS--MWDKLIFSKVQASLGGRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWT- 475
Cdd:PLN02861 355 NLRKGLKQEEAspRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGCFTSIANVFSm 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 476 AGHVGAPLPCNFVKLVDVAEMNYFAANG--EGEVCVKGPNVFQGYLKDPEQTSGA-VDkaGWLHTGDIGKWLPNGTLKII 552
Cdd:PLN02861 435 VGTVGVPMTTIEARLESVPEMGYDALSDvpRGEICLRGNTLFSGYHKRQDLTEEVlID--GWFHTGDIGEWQPNGAMKII 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 553 DRKKHIFKLAQGEYIAPEKIENIYIRSDPVAQVFVHGDSLQACLVGVVVPDPDFLPGWAKNRGIEGSFNDLCKSKEVKNA 632
Cdd:PLN02861 513 DRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKY 592
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528467780 633 ILEDMIQLGKEAGLKSFEQVRDIALHLEMFSVQNGLLTPTLKAKRTELKSRFREQIDQLYAKIK 696
Cdd:PLN02861 593 ILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYSEAK 656
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
105-696 |
4.57e-147 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 443.69 E-value: 4.57e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 105 NGPCLGSR-----KAGQpYKWLSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYD 179
Cdd:PLN02614 60 NNPMLGRReivdgKPGK-YVWQTYQEVYDIVIKLGNSLRSVG-VKDEAK-CGIYGANSPEWIISMEACNAHGLYCVPLYD 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 180 TLGTEAISYVIDKASITTIICDIADKARLILDCVSGRKHsVTTIVIMESFDSELTAQAQNCGIDIISLKELEAIGKA-NH 258
Cdd:PLN02614 137 TLGAGAVEFIISHSEVSIVFVEEKKISELFKTCPNSTEY-MKTVVSFGGVSREQKEEAETFGLVIYAWDEFLKLGEGkQY 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 259 KTPIPpKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSA---FIKITEESLKLcpQDVLISFLPLAHMFERVVEGVLLC 335
Cdd:PLN02614 216 DLPIK-KKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGvirLLKSANAALTV--KDVYLSYLPLAHIFDRVIEECFIQ 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 336 HGAKIGYFQGDIRLLMDDLKNLKPTIFPVVPRLLNRMFDKIFGQANTP--LKRWLLDFATSRKEAELKSGV--VRKDSMW 411
Cdd:PLN02614 293 HGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGgfLKKFVFDSAFSYKFGNMKKGQshVEASPLC 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 412 DKLIFSKVQASLGGRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDW-TAGHVGAPLPCNFVKL 490
Cdd:PLN02614 373 DKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELdMLGTVGPPVPNVDIRL 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 491 VDVAEMNY--FAANGEGEVCVKGPNVFQGYLKDpEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIA 568
Cdd:PLN02614 453 ESVPEMEYdaLASTPRGEICIRGKTLFSGYYKR-EDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVA 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 569 PEKIENIYIRSDPVAQVFVHGDSLQACLVGVVVPDPDFLPGWAKNRGIEGSFNDLCKSKEVKNAILEDMIQLGKEAGLKS 648
Cdd:PLN02614 532 VENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEFILGELVKMAKEKKMKG 611
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 528467780 649 FEQVRDIALHLEMFSVQNGLLTPTLKAKRTELKSRFREQIDQLYAKIK 696
Cdd:PLN02614 612 FEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYKTTN 659
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
62-693 |
4.94e-143 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 434.16 E-value: 4.94e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 62 VEVPGKE-YARRS--ILMDNDTHmtyyYKDALTLYEFFLRGLRVSNNGPCLGSRKA----------GQ--------PYKW 120
Cdd:PLN02387 31 VDVGGEPgYAIRNarFPELVETP----WEGATTLAALFEQSCKKYSDKRLLGTRKLisrefetssdGRkfeklhlgEYEW 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGHSQsgDKYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNK--EERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVIC 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 DIADKARLIldCVSGRKHSVTTIVIME-SFDSELTAQAQNCGIDIISLKELEAIGKANHKTPIPPKPEDLALICFTSGTT 279
Cdd:PLN02387 185 DSKQLKKLI--DISSQLETVKRVIYMDdEGVDSDSSLSGSSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGST 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 280 GNPKGAMLTHGNVVSNCSAFIKITEeslKLCPQDVLISFLPLAHMFERVVEGVLLCHGAKIGYfqGDIRLLMD------- 352
Cdd:PLN02387 263 GLPKGVMMTHGNIVATVAGVMTVVP---KLGKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDtsnkikk 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 353 ----DLKNLKPTIFPVVPRLLNRMFDKIFGQANTP--LKRWLLDFATSRKEAELK------SGVVRkdSMWDKLIFSKVQ 420
Cdd:PLN02387 338 gtkgDASALKPTLMTAVPAILDRVRDGVRKKVDAKggLAKKLFDIAYKRRLAAIEgswfgaWGLEK--LLWDALVFKKIR 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 421 ASLGGRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDVAEMNYFA 500
Cdd:PLN02387 416 AVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLI 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 501 ANG---EGEVCVKGPNVFQGYLKDPEQTSGA--VDKAG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIE 573
Cdd:PLN02387 496 SDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVE 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 574 NIYIRSDPVAQVFVHGDSLQACLVGVVVPDPDFLPGWAKNRGIE-GSFNDLCKSKEVKNAILEDMIQLGKEAGLKSFEQV 652
Cdd:PLN02387 576 AALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIP 655
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 528467780 653 RDIALHLEMFSVQNGLLTPTLKAKRTELKSRFREQIDQLYA 693
Cdd:PLN02387 656 AKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
117-562 |
4.95e-129 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 388.21 E-value: 4.95e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 117 PYKWLSYKEVADRAEFAGSALLHRGHsQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASIT 196
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRALGV-GKGDR-VAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 197 TIICDIADKARLILDCVSGRKHSVTTIVImeSFDSELTAQAqncgidiisLKELEAIGKANHKTPIPPKPEDLALICFTS 276
Cdd:pfam00501 96 VLITDDALKLEELLEALGKLEVVKLVLVL--DRDPVLKEEP---------LPEEAKPADVPPPPPPPPDPDDLAYIIYTS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 277 GTTGNPKGAMLTHGNVVSNCSAFIKITEESLKLCPQDVLISFLPLAHMFERVVE-GVLLCHGAKIGYFQGDIRL----LM 351
Cdd:pfam00501 165 GTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGlLGPLLAGATVVLPPGFPALdpaaLL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 352 DDLKNLKPTIFPVVPRLLNRMFDKIfgqantPLKRWLLdfatsrkeaelksgvvrkdsmwdklifskvqaslgGRVRLMI 431
Cdd:pfam00501 245 ELIERYKVTVLYGVPTLLNMLLEAG------APKRALL-----------------------------------SSLRLVL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 432 TGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDW---TAGHVGAPLPCNFVKLVDVAEMNYFAANGEGEVC 508
Cdd:pfam00501 284 SGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELC 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 528467780 509 VKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLA 562
Cdd:pfam00501 364 VRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
119-694 |
6.51e-107 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 340.42 E-value: 6.51e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 119 KWLSYKEVADRAEFAGSALLHRGHSQsGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTI 198
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLAELGLTK-GSN-VAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 199 ICDIADKARLILDCVSGRKHSvTTIVIMESFDSELTAQaqncGIDIISLKELEAIG---KANHKTPIPPKPEDLALICFT 275
Cdd:PTZ00216 198 VCNGKNVPNLLRLMKSGGMPN-TTIIYLDSLPASVDTE----GCRLVAWTDVVAKGhsaGSHHPLNIPENNDDLALIMYT 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 276 SGTTGNPKGAMLTHGNVVSNCSAF-IKITEESLKLCPQDVLISFLPLAHMFERVVEGVLLCHGAKIGYfqGDIRLLMD-- 352
Cdd:PTZ00216 273 SGTTGDPKGVMHTHGSLTAGILALeDRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRTLTDtf 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 353 -----DLKNLKPTIFPVVPRLlnrmFDKIFG--QANTP----LKRWLLDFA-TSRKEAeLKSGvvrKDS-MWDKLIFSKV 419
Cdd:PTZ00216 351 arphgDLTEFRPVFLIGVPRI----FDTIKKavEAKLPpvgsLKRRVFDHAyQSRLRA-LKEG---KDTpYWNEKVFSAP 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 420 QASLGGRVRLMITGAAPVSPTVLTFLRAALGCqFYEGYGQTEcTAGC-TMSLPGDWTAGHVGAPLPCNFVKLVDVAEMNY 498
Cdd:PTZ00216 423 RAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTE-TVCCgGIQRTGDLEPNAVGQLLKGVEMKLLDTEEYKH 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 499 F-AANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYI 577
Cdd:PTZ00216 501 TdTPEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEALYG 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 578 rSDPVAQ-----VFVHGDslQACLVGVVVPDPDFLPGWAKNRGIEGSFNDLCKSKEVKNAILEDMIQLGKEAGLKSFEQV 652
Cdd:PTZ00216 581 -QNELVVpngvcVLVHPA--RSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFEIV 657
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 528467780 653 RDIALHLEMFSVQNGLLTPTLKAKRTELKSRFREQIDQLYAK 694
Cdd:PTZ00216 658 RHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELFAD 699
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
116-677 |
1.81e-84 |
|
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: 274.24 E-value: 1.81e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 116 QPYKWLSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPlydtlgteaisyvidKASI 195
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLG-VKAGEK-VALFADNSPRWLIADQGIMALGAVDVV---------------RGSD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 196 TTIicdiaDKARLILdcvsgrKHSVTTIVIMEsfdseltaqaqncgidiislkeleaigkaNHktpippkPEDLALICFT 275
Cdd:cd17640 64 SSV-----EELLYIL------NHSESVALVVE-----------------------------ND-------SDDLATIIYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 276 SGTTGNPKGAMLTHGNVVSNCSAFIKITEESlklcPQDVLISFLPLAHMFERVVEGVLLCHGAKIGYfqGDIRLLMDDLK 355
Cdd:cd17640 97 SGTTGNPKGVMLTHANLLHQIRSLSDIVPPQ----PGDRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDDLK 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 356 NLKPTIFPVVPRLLNRMFDKIFGQ--ANTPLKRWLLDFATSrkeaelksgvvrkdsmwdklifskvqaslGGRVRLMITG 433
Cdd:cd17640 171 RVKPHYIVSVPRLWESLYSGIQKQvsKSSPIKQFLFLFFLS-----------------------------GGIFKFGISG 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 434 AAPVSPTVLTFLRAaLGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDVAEMNYFAANGEGEVCVKGPN 513
Cdd:cd17640 222 GGALPPHVDTFFEA-IGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQ 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 514 VFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSDPVAQVFVHGDSlQ 593
Cdd:cd17640 301 VMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQD-Q 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 594 ACLVGVVVPDPDFLPGWAKNRGI---EGSFNDLCKSKEVKNAILEDMIQLGKEAGLKSFEQVRDIALhLEMFSVQNGLLT 670
Cdd:cd17640 380 KRLGALIVPNFEELEKWAKESGVklaNDRSQLLASKKVLKLYKNEIKDEISNRPGFKSFEQIAPFAL-LEEPFIENGEMT 458
|
....*..
gi 528467780 671 PTLKAKR 677
Cdd:cd17640 459 QTMKIKR 465
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
121-684 |
1.29e-81 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 268.18 E-value: 1.29e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:cd05932 7 FTWGEVADKARRLAAALRALG-LEPGSK-IALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 DiadkarlILDCVSGRKHSV--TTIVIMESFDSELTAQAQncgidiisLKELEAIGKANHKTPiPPKPEDLALICFTSGT 278
Cdd:cd05932 85 G-------KLDDWKAMAPGVpeGLISISLPPPSAANCQYQ--------WDDLIAQHPPLEERP-TRFPEQLATLIYTSGT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 279 TGNPKGAMLTHGNVVSNCSAFIkiteESLKLCPQDVLISFLPLAHMFERV-VEGVLLCHGAKIgYFQGDIRLLMDDLKNL 357
Cdd:cd05932 149 TGQPKGVMLTFGSFAWAAQAGI----EHIGTEENDRMLSYLPLAHVTERVfVEGGSLYGGVLV-AFAESLDTFVEDVQRA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 358 KPTIFPVVPRLL----NRMFDKIfgqantPLKRwlLDFAtsrkeaeLKSGVVrkdsmwDKLIFSKVQASLG-GRVRLMIT 432
Cdd:cd05932 224 RPTLFFSVPRLWtkfqQGVQDKI------PQQK--LNLL-------LKIPVV------NSLVKRKVLKGLGlDQCRLAGC 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 433 GAAPVSPTVLTFLRaALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDvaemnyfaangEGEVCVKGP 512
Cdd:cd05932 283 GSAPVPPALLEWYR-SLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEILVRSP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 513 NVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSDPVAQVFVHGDSL 592
Cdd:cd05932 351 ALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSGL 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 593 QACLVGVVVPDPDFLPGWAKNRG-IEGSFndlckskevkNAILEDMiqlgkEAGLKSFEQVRDIALHLEMFSVQNGLLTP 671
Cdd:cd05932 431 PAPLALVVLSEEARLRADAFARAeLEASL----------RAHLARV-----NSTLDSHEQLAGIVVVKDPWSIDNGILTP 495
|
570
....*....|...
gi 528467780 672 TLKAKRTELKSRF 684
Cdd:cd05932 496 TLKIKRNVLEKAY 508
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
121-606 |
1.00e-70 |
|
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: 237.40 E-value: 1.00e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:COG0318 25 LTYAELDARARRLAAALRALG-VGPGDR-VALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 diadkarlildcvsgrkhsvttivimesfdseltaqaqncgidiislkeleaigkanhktpippkpedlALICFTSGTTG 280
Cdd:COG0318 103 ---------------------------------------------------------------------ALILYTSGTTG 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 281 NPKGAMLTHGNVVSNCSAFIkiteESLKLCPQDVLISFLPLAHMFERVVEGVL-LCHGAKI---GYFqgDIRLLMDDLKN 356
Cdd:COG0318 114 RPKGVMLTHRNLLANAAAIA----AALGLTPGDVVLVALPLFHVFGLTVGLLApLLAGATLvllPRF--DPERVLELIER 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 357 LKPTIFPVVPRLLNRMfdkifgqANTPlkrwlldfatsrkeaelksgvvrkdsMWDKLIFSkvqaslggRVRLMITGAAP 436
Cdd:COG0318 188 ERVTVLFGVPTMLARL-------LRHP--------------------------EFARYDLS--------SLRLVVSGGAP 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 437 VSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTA--GHVGAPLPCNFVKLVDvAEMNYFAANGEGEVCVKGPNV 514
Cdd:COG0318 227 LPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGRPLPGVEVRIVD-EDGRELPPGEVGEIVVRGPNV 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 515 FQGYLKDPEQTsGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSDPVAQVFVhgdslqa 594
Cdd:COG0318 306 MKGYWNDPEAT-AEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEVLAAHPGVAEAAV------- 376
|
490
....*....|..
gi 528467780 595 clvgVVVPDPDF 606
Cdd:COG0318 377 ----VGVPDEKW 384
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
121-677 |
6.84e-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: 6.84e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:cd05914 8 LTYKDLADNIAKFALLLKING-VGTGDR-VALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 DiadkarlildcvsgrkhsvttivimesfdseltaqaqncgidiislkeleaigkanhktpippKPEDLALICFTSGTTG 280
Cdd:cd05914 86 S---------------------------------------------------------------DEDDVALINYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 281 NPKGAMLTHGNVVSNCSAFIKIteesLKLCPQDVLISFLPLAHMFERVVEGVL-LCHGAKIgYFQGDI---RLLMDDLKN 356
Cdd:cd05914 103 NSKGVMLTYRNIVSNVDGVKEV----VLLGKGDKILSILPLHHIYPLTFTLLLpLLNGAHV-VFLDKIpsaKIIALAFAQ 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 357 LKPTIfpVVPRLLNRMfdKIFGQANTPLKrwlldfatSRKEAELKSGVVRKDSMWDKLIFSKVQASLGGRVRLMITGAAP 436
Cdd:cd05914 178 VTPTL--GVPVPLVIE--KIFKMDIIPKL--------TLKKFKFKLAKKINNRKIRKLAFKKVHEAFGGNIKEFVIGGAK 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 437 VSPTVLTFLRAaLGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLpcnfvKLVDVAEMNYFAANGEGEVCVKGPNVFQ 516
Cdd:cd05914 246 INPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVI-----DGVEVRIDSPDPATGEGEIIVRGPNVMK 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 517 GYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSDPVA--QVFVHGDSLQA 594
Cdd:cd05914 320 GYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLesLVVVQEKKLVA 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 595 clvgVVVPDPDFLPGWAKnrgiegsfndlcKSKEVKNAILEDMI-QLGKEagLKSFEQVRDIALHLEMFSVqngllTPTL 673
Cdd:cd05914 400 ----LAYIDPDFLDVKAL------------KQRNIIDAIKWEVRdKVNQK--VPNYKKISKVKIVKEEFEK-----TPKG 456
|
....
gi 528467780 674 KAKR 677
Cdd:cd05914 457 KIKR 460
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
122-677 |
5.28e-67 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 230.77 E-value: 5.28e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 122 SYKEVADRAEFAGSALLHRGhSQSGDkYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC- 200
Cdd:cd17641 13 TWADYADRVRAFALGLLALG-VGRGD-VVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAe 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 --DIADKARLILDcvsgRKHSVTTIVIMES------FDSELtaqaqncgidiISLKELEAIGKANHKTPipP-------- 264
Cdd:cd17641 91 deEQVDKLLEIAD----RIPSVRYVIYCDPrgmrkyDDPRL-----------ISFEDVVALGRALDRRD--Pglyereva 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 265 --KPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEESlklcPQDVLISFLPLAHMFERV--VEGVLLChGAKI 340
Cdd:cd17641 154 agKGEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLG----PGDEYVSVLPLPWIGEQMysVGQALVC-GFIV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 341 GyFQGDIRLLMDDLKNLKPTIFPVVPRLLN--------RMFDkifgqaNTPLKRWLLDF--------ATSRKEAELKSGV 404
Cdd:cd17641 229 N-FPEEPETMMEDLREIGPTFVLLPPRVWEgiaadvraRMMD------ATPFKRFMFELgmklglraLDRGKRGRPVSLW 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 405 VRKDS-MWDKLIFSKVQASLG-GRVRLMITGAAPVSPTVLTFLRAaLGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAP 482
Cdd:cd17641 302 LRLASwLADALLFRPLRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 483 LPCNFVKLVDVaemnyfaangeGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLA 562
Cdd:cd17641 381 FPGTEVRIDEV-----------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTS 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 563 QGEYIAPEKIEN-----IYIRSdpvAQVFVHGDSLQACLVGVvvpDPDFLPGWAKNRGIE-GSFNDLCKSKEVKNAILED 636
Cdd:cd17641 450 DGTRFSPQFIENklkfsPYIAE---AVVLGAGRPYLTAFICI---DYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKE 523
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 528467780 637 MIQLGKEagLKSFEQVRDIALHLEMFSVQNGLLTPTLKAKR 677
Cdd:cd17641 524 VEKVNAS--LPEAQRIRRFLLLYKELDADDGELTRTRKVRR 562
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
113-692 |
8.32e-67 |
|
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: 230.71 E-value: 8.32e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 113 KAGQPYKWLSYKEVADRAEFAGSALLHRG----HSqsgdkyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISY 188
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLKLGlerfHG------VGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 189 VIDKASITTIICDIADKARLILDCVSGRKHSVTTIVIMESFDSELT-----AQAQNCGIDIiSLKELEAIGKANhktpip 263
Cdd:cd05933 75 VAETSEANILVVENQKQLQKILQIQDKLPHLKAIIQYKEPLKEKEPnlyswDEFMELGRSI-PDEQLDAIISSQ------ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 264 pKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKiteeSLKLCP----QDVLISFLPLAHMFERVVEgVLLC--HG 337
Cdd:cd05933 148 -KPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQ----HMDLRPatvgQESVVSYLPLSHIAAQILD-IWLPikVG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 338 AKIGYFQGDIR--LLMDDLKNLKPTIFPVVPRLLNRMFDKI--FGQANTPLKRWLLDFA------TSRKEAELKSGVVRK 407
Cdd:cd05933 222 GQVYFAQPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkaVGAKSGTLKRKIASWAkgvgleTNLKLMGGESPSPLF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 408 DSMWDKLIFSKVQASLG-GRVRLMITGAAPVSPTVLTFLrAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCN 486
Cdd:cd05933 302 YRLAKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGC 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 487 FVKLVDVAemnyfaANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEY 566
Cdd:cd05933 381 KTKIHNPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGEN 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 567 IAPEKIEN-IYIRSDPVAQVFVHGDSLQ--------ACLVGVVVPDP-DFLP----GWAKNRGIEGS-FNDLCKSKE--V 629
Cdd:cd05933 455 VPPVPIEDaVKKELPIISNAMLIGDKRKflsmlltlKCEVNPETGEPlDELTeeaiEFCRKLGSQATrVSEIAGGKDpkV 534
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528467780 630 KNAILEDMIQLGKEAgLKSFEQVRDIALHLEMFSVQNGLLTPTLKAKRTELKSRFREQIDQLY 692
Cdd:cd05933 535 YEAIEEGIKRVNKKA-ISNAQKIQKWVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
121-670 |
7.18e-65 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 225.41 E-value: 7.18e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGHSQSGDkYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:cd17632 68 ITYAELWERVGAVAAAHDPEQPVRPGD-FVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 DiADKARLILDCVSGRKhSVTTIVImesFD--SELTAQAQ----------NCGIDIISLKELEAIGKANHKTP---IPPK 265
Cdd:cd17632 147 S-AEHLDLAVEAVLEGG-TPPRLVV---FDhrPEVDAHRAalesarerlaAVGIPVTTLTLIAVRGRDLPPAPlfrPEPD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 266 PEDLALICFTSGTTGNPKGAMLTHGNVVS---NCSAFIKITEeslklcPQDVLISFLPLAHMFERVVEGVLLCHGAkIGY 342
Cdd:cd17632 222 DDPLALLIYTSGSTGTPKGAMYTERLVATfwlKVSSIQDIRP------PASITLNFMPMSHIAGRISLYGTLARGG-TAY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 343 FQG--DIRLLMDDLKNLKPTIFPVVPRLlnrmFDKIFGQANTPLKRWLLDFATSRKEAELKSGVVRKDSmwdklifskvq 420
Cdd:cd17632 295 FAAasDMSTLFDDLALVRPTELFLVPRV----CDMLFQRYQAELDRRSVAGADAETLAERVKAELRERV----------- 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 421 asLGGRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTEctAGCTMSLpgdwtaGHVGAPlPCNFVKLVDVAEMNYFA 500
Cdd:cd17632 360 --LGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE--AGAVILD------GVIVRP-PVLDYKLVDVPELGYFR 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 501 ANG---EGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYI 577
Cdd:cd17632 429 TDRphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFA 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 578 RSDPVAQVFVHGDSLQACLVGVVVPDPDFLPGWAknrgiegsfndlckSKEVKNAILEDMIQLGKEAGLKSFEQVRDIAL 657
Cdd:cd17632 509 ASPLVRQIFVYGNSERAYLLAVVVPTQDALAGED--------------TARLRAALAESLQRIAREAGLQSYEIPRDFLI 574
|
570
....*....|...
gi 528467780 658 HLEMFSVQNGLLT 670
Cdd:cd17632 575 ETEPFTIANGLLS 587
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
268-605 |
7.42e-65 |
|
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: 217.92 E-value: 7.42e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 268 DLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKiteeSLKLCPQDVLISFLPLAHMFERVVEGVLLCHGAKI---GYFq 344
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAA----SGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVvllPKF- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 345 gDIRLLMDDLKNLKPTIFPVVPRLLNRMFDkifgqantplkrwlldfATSRKEAELKSgvvrkdsmwdklifskvqaslg 424
Cdd:cd04433 76 -DPEAALELIEREKVTILLGVPTLLARLLK-----------------APESAGYDLSS---------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 425 grVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWT--AGHVGAPLPCNFVKLVDVAEmNYFAAN 502
Cdd:cd04433 116 --LRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDPDG-GELPPG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 503 GEGEVCVKGPNVFQGYLKDPEQTSgAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYIRSDPV 582
Cdd:cd04433 193 EIGELVVRGPSVMKGYWNNPEATA-AVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPGV 270
|
330 340
....*....|....*....|....*.
gi 528467780 583 AQVFVHG---DSLQACLVGVVVPDPD 605
Cdd:cd04433 271 AEAAVVGvpdPEWGERVVAVVVLRPG 296
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
121-605 |
1.32e-60 |
|
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: 210.92 E-value: 1.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLG-LKKGDV-VGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 D--IADKARLILDCVSgrkhSVTTIVIMESFDSELTAQAQncgidiiSLKELEAIGKANHKTPIPPKPEDLALICFTSGT 278
Cdd:cd05911 89 DpdGLEKVKEAAKELG----PKDKIIVLDDKPDGVLSIED-------LLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 279 TGNPKGAMLTHGNVVSNCSAFIKITEESLklCPQDVLISFLPLAHMFervveGVLLCHGAKIgyfQG---------DIRL 349
Cdd:cd05911 158 TGLPKGVCLSHRNLIANLSQVQTFLYGND--GSNDVILGFLPLYHIY-----GLFTTLASLL---NGatviimpkfDSEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 350 LMDDLKNLKPTIFPVVPRLLNRMFdkifgqantplkrwlldfatsrkeaelKSGVVRKDSMwdklifskvqASLggrvRL 429
Cdd:cd05911 228 FLDLIEKYKITFLYLVPPIAAALA---------------------------KSPLLDKYDL----------SSL----RV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 430 MITGAAPVSPTVLTFLRAALG-CQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPcNF-VKLVDVAEMNYFAANGEGEV 507
Cdd:cd05911 267 ILSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLP-NVeAKIVDDDGKDSLGPNEPGEI 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 508 CVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDPVAQVfv 587
Cdd:cd05911 346 CVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAVLLEHPGVADA-- 422
|
490
....*....|....*...
gi 528467780 588 hgdslqaCLVGvvVPDPD 605
Cdd:cd05911 423 -------AVIG--IPDEV 431
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
121-605 |
2.83e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 208.22 E-value: 2.83e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALG-IGKGDR-VAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 --DIADKARLILDCVSgrkhSVTTIVIMEsfdselTAQAQNCGIDIISLKELEAIGkANHKTPIPPKPEDLALICFTSGT 278
Cdd:PRK07656 109 lgLFLGVDYSATTRLP----ALEHVVICE------TEEDDPHTEKMKTFTDFLAAG-DPAERAPEVDPDDVADILFTSGT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 279 TGNPKGAMLTHGNVVSNCSAFIKIteesLKLCPQDVLISFLPLAHMFERVVeGVLLC--HGAKI---GYFqgDIRLLMDD 353
Cdd:PRK07656 178 TGRPKGAMLTHRQLLSNAADWAEY----LGLTEGDRYLAANPFFHVFGYKA-GVNAPlmRGATIlplPVF--DPDEVFRL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 354 LKNLKPTIFPVVPRLLNRMFDkifgqantplkrwlldfATSRKEAELKSgvvrkdsmwdklifskvqaslggrVRLMITG 433
Cdd:PRK07656 251 IETERITVLPGPPTMYNSLLQ-----------------HPDRSAEDLSS------------------------LRLAVTG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 434 AAPVSPTVLTFLRAALGCQ-FYEGYGQTECTAGCTMSLPGD---WTAGHVGAPLPCNFVKLVDvaEMNYFAANGE-GEVC 508
Cdd:PRK07656 290 AASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIAGVENKIVN--ELGEEVPVGEvGELL 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 509 VKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVFVH 588
Cdd:PRK07656 368 VRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IVGGFNVYPAEVEEVLYEHPAVAEAAVI 446
|
490
....*....|....*..
gi 528467780 589 GdslqaclvgvvVPDPD 605
Cdd:PRK07656 447 G-----------VPDER 452
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
119-605 |
3.10e-58 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 203.95 E-value: 3.10e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 119 KWLSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLyDTLGTEAisyvidkasitti 198
Cdd:cd05936 23 RKLTYRELDALAEAFAAGLQNLG-VQPGDR-VALMLPNCPQFPIAYFGALKAGAVVVPL-NPLYTPR------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 199 icdiadkarlildcvsgrkhsvttivimesfdsELTAQAQNCG----IDIISLKELEAIGKANHKTPIPPkPEDLALICF 274
Cdd:cd05936 87 ---------------------------------ELEHILNDSGakalIVAVSFTDLLAAGAPLGERVALT-PEDVAVLQY 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 275 TSGTTGNPKGAMLTHGNVVSNCSAFIKITEESLKlcPQDVLISFLPLAHMFERVVEGVL-LCHGAKIGYFQG-DIRLLMD 352
Cdd:cd05936 133 TSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLE--GDDVVLAALPLFHVFGLTVALLLpLALGATIVLIPRfRPIGVLK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 353 DLKNLKPTIFPVVPRLLNRMfdkifgqANTPlkrwllDFAtsrkeaelksgvvrkdsmwdKLIFSkvqaslggRVRLMIT 432
Cdd:cd05936 211 EIRKHRVTIFPGVPTMYIAL-------LNAP------EFK--------------------KRDFS--------SLRLCIS 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 433 GAAPVSPTVLTFLRAALGCQFYEGYGQTECT-AGCTMSLPGDWTAGHVGAPLPCNFVKLVDvaEMNYFAANGE-GEVCVK 510
Cdd:cd05936 250 GGAPLPVEVAERFEELTGVPIVEGYGLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVD--DDGEELPPGEvGELWVR 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 511 GPNVFQGYLKDPEQTSgAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVFVhgd 590
Cdd:cd05936 328 GPQVMKGYWNRPEETA-EAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGGFNVYPREVEEVLYEHPAVAEAAV--- 402
|
490
....*....|....*
gi 528467780 591 slqaclVGvvVPDPD 605
Cdd:cd05936 403 ------VG--VPDPY 409
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
82-604 |
5.35e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 191.17 E-value: 5.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 82 MTYYYkdaLTLYEFFLRGLRVsnngpcLGSRKA----GQPYkwlSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNR 157
Cdd:PRK06187 1 MQDYP---LTIGRILRHGARK------HPDKEAvyfdGRRT---TYAELDERVNRLANALRALG-VKKGDR-VAVFDWNS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 158 PEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIcdiADKARL-ILDCVSGRKHSVTTIVIMESFDSEltaq 236
Cdd:PRK06187 67 HEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVL---VDSEFVpLLAAILPQLPTVRTVIVEGDGPAA---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 237 aqNCGIDIISLKELEAiGKANHKTPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNcsafIKITEESLKLCPQDVLI 316
Cdd:PRK06187 140 --PLAPEVGEYEELLA-AASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLH----SLAVCAWLKLSRDDVYL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 317 SFLPLAHMFERVVEGVLLCHGAKI---GYFqgDIRLLMDDLKNLKPTIFPVVPRLLNRMFdkifgQANTPLKRWLldfat 393
Cdd:PRK06187 213 VIVPMFHVHAWGLPYLALMAGAKQvipRRF--DPENLLDLIETERVTFFFAVPTIWQMLL-----KAPRAYFVDF----- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 394 srkeaelksgvvrkdsmwdklifskvqaslgGRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLP-- 471
Cdd:PRK06187 281 -------------------------------SSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVLPPed 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 472 ---GDWT-AGHVGAPLPCNFVKLVDvAEMNYFAANGE--GEVCVKGPNVFQGYLKDPEQTSGAVDKaGWLHTGDIGKWLP 545
Cdd:PRK06187 330 qlpGQWTkRRSAGRPLPGVEARIVD-DDGDELPPDGGevGEIIVRGPWLMQGYWNRPEATAETIDG-GWLHTGDVGYIDE 407
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 528467780 546 NGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSDPVAQVFVhgdslqaclVGvvVPDP 604
Cdd:PRK06187 408 DGYLYITDRIKDVIISG-GENIYPRELEDALYGHPAVAEVAV---------IG--VPDE 454
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
121-604 |
1.20e-46 |
|
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: 171.25 E-value: 1.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIdkasittiic 200
Cdd:cd17631 21 LTYAELDERVNRLAHALRALG-VAKGDR-VAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYIL---------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 diadkarlildcvsgrKHSVTTIVImesfdseltaqaqncgidiislkeleaigkanhktpippkpEDLALICFTSGTTG 280
Cdd:cd17631 89 ----------------ADSGAKVLF-----------------------------------------DDLALLMYTSGTTG 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 281 NPKGAMLTHGNVVSNCSAFIKiteeSLKLCPQDVLISFLPLahmfervvegvllCHGAKIGYFqgdirllmddlknlkpt 360
Cdd:cd17631 112 RPKGAMLTHRNLLWNAVNALA----ALDLGPDDVLLVVAPL-------------FHIGGLGVF----------------- 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 361 ifpVVPRLLNrmfdkifGQANTPLKRWLLD--FATSRKEAELKSGVVrkDSMWDKLI----FSKVQASlggRVRLMITGA 434
Cdd:cd17631 158 ---TLPTLLR-------GGTVVILRKFDPEtvLDLIERHRVTSFFLV--PTMIQALLqhprFATTDLS---SLRAVIYGG 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 435 APVSPTVLTFLRAAlGCQFYEGYGQTECTAGCTMSLPGDW--TAGHVGAPLPCNFVKLVDvAEMNYFAANGEGEVCVKGP 512
Cdd:cd17631 223 APMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHrrKLGSAGRPVFFVEVRIVD-PDGREVPPGEVGEIVVRGP 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 513 NVFQGYLKDPEQTSGAVDKaGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYIRSDPVAQVFVHGdsl 592
Cdd:cd17631 301 HVMAGYWNRPEATAAAFRD-GWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDVLYEHPAVAEVAVIG--- 375
|
490
....*....|..
gi 528467780 593 qaclvgvvVPDP 604
Cdd:cd17631 376 --------VPDE 379
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
232-677 |
8.09e-46 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 174.52 E-value: 8.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 232 ELTAQAQNCGIDIISLKELEAIGKANHKTpIPPKPEDLALICFTSGTTGNPKGAMLTHGNV------VSNCSAFikitee 305
Cdd:PTZ00342 270 DLKEKAKKLGISIILFDDMTKNKTTNYKI-QNEDPDFITSIVYTSGTSGKPKGVMLSNKNLyntvvpLCKHSIF------ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 306 sLKLCPQDVLiSFLPLAHMFERVVEGVLLCHGAKIGYFQGDIRLLMDDLKNLKPTIFPVVPRLLNRMFDKIFGQAN--TP 383
Cdd:PTZ00342 343 -KKYNPKTHL-SYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINnlPP 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 384 LKRWLLDFATSRKEAELK---SGVVRKDSMWDKLIFSKVQASLggrvRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQT 460
Cdd:PTZ00342 421 LKRFLVKKILSLRKSNNNggfSKFLEGITHISSKIKDKVNPNL----EVILNGGGKLSPKIAEELSVLLNVNYYQGYGLT 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 461 ECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDVAEMnyFAANG---EGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHT 537
Cdd:PTZ00342 497 ETTGPIFVQHADDNNTESIGGPISPNTKYKVRTWET--YKATDtlpKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKT 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 538 GDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSDPVAQVFVHG-DSLQACLvGVVVPDPDFLPGWAKNRGI 616
Cdd:PTZ00342 575 GDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGdDSMDGPL-AIISVDKYLLFKCLKDDNM 653
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528467780 617 -------EGSFNDLCKSKEVKNAIL-----EDMIQLGKEAGLKSFEQVRDIALHLEMFSVQNgLLTPTLKAKR 677
Cdd:PTZ00342 654 lestginEKNYLEKLTDETINNNIYvdyvkGKMLEVYKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKR 725
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
266-606 |
1.06e-41 |
|
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: 155.13 E-value: 1.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 266 PEDLALICFTSGTTGNPKGAMLTHGNVVSNcsAFIkiTEESLKLCPQDVLISFLPLAHMFERVVeGVLLC--HGAKIGY- 342
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNN--GYF--IGERLGLTEQDRLCIPVPLFHCFGSVL-GVLACltHGATMVFp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 343 ---FqgDIRLLMDDLKNLKPTIFPVVPRllnrMFdkifgqantplkrwlldfatsrkEAELKSGvvrkdsmwDKLIFSKv 419
Cdd:cd05917 76 spsF--DPLAVLEAIEKEKCTALHGVPT----MF-----------------------IAELEHP--------DFDKFDL- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 420 qaslgGRVRLMITGAAPVSPTVLTFLRAALGC-QFYEGYGQTECTAGCTMSLPGD---WTAGHVGAPLPCNFVKLVDVAE 495
Cdd:cd05917 118 -----SSLRTGIMAGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDsieKRVNTVGRIMPHTEAKIVDPEG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 496 MNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENI 575
Cdd:cd05917 193 GIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGENIYPREIEEF 271
|
330 340 350
....*....|....*....|....*....|.
gi 528467780 576 yirsdpvaqVFVHGDSLQACLVGvvVPDPDF 606
Cdd:cd05917 272 ---------LHTHPKVSDVQVVG--VPDERY 291
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
121-606 |
3.85e-41 |
|
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: 155.91 E-value: 3.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGHSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIc 200
Cdd:cd05941 12 ITYADLVARAARLANRLLALGKDLRGDR-VAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 diadkarlildcvsgrkhsvttivimesfdseltaqaqncgidiislkeleaigkanhktpippkpeDLALICFTSGTTG 280
Cdd:cd05941 90 -------------------------------------------------------------------DPALILYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 281 NPKGAMLTHGNVVSNCSAFIkiteESLKLCPQDVLISFLPLAHmfervVEGV---LLC---HGAKI---GYFQGDIRLLM 351
Cdd:cd05941 103 RPKGVVLTHANLAANVRALV----DAWRWTEDDVLLHVLPLHH-----VHGLvnaLLCplfAGASVeflPKFDPKEVAIS 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 352 DDLKNLkpTIFPVVP----RLL---NRMFDkifgqantplkrwllDFATSRKEAElksgvvrkdsmwdklifskvqaslg 424
Cdd:cd05941 174 RLMPSI--TVFMGVPtiytRLLqyyEAHFT---------------DPQFARAAAA------------------------- 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 425 GRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTEctAGCTMSLP--GDWTAGHVGAPLPCNFVKLVDVAEMNYFAAN 502
Cdd:cd05941 212 ERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVDEETGEPLPRG 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 503 GEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKK-HIFKlAQGEYIAPEKIEniyirsdp 581
Cdd:cd05941 290 EVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEIE-------- 360
|
490 500
....*....|....*....|....*
gi 528467780 582 vAQVFVHGDSLQACLVGvvVPDPDF 606
Cdd:cd05941 361 -RVLLAHPGVSECAVIG--VPDPDW 382
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
265-605 |
1.04e-40 |
|
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: 156.24 E-value: 1.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 265 KPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEESLklCPQDVLISFLPLAHM--FERVVEGVLLChGAKI-- 340
Cdd:cd05904 156 KQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNS--DSEDVFLCVLPMFHIygLSSFALGLLRL-GATVvv 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 341 -GYFqgDIRLLMDDLKNLKPTIFPVVPrllnrmfdkifgqantPLkrwLLDFAtsrkeaelksgvvrKDSMWDKLIFSKV 419
Cdd:cd05904 233 mPRF--DLEELLAAIERYKVTHLPVVP----------------PI---VLALV--------------KSPIVDKYDLSSL 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 420 qaslggrvRLMITGAAPVSPTVLTFLRAAL-GCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAP---LPCNFVKLVDVAE 495
Cdd:cd05904 278 --------RQIMSGAAPLGKELIEAFRAKFpNVDLGQGYGMTESTGVVAMCFAPEKDRAKYGSVgrlVPNVEAKIVDPET 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 496 MNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 575
Cdd:cd05904 350 GESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEAL 428
|
330 340 350
....*....|....*....|....*....|
gi 528467780 576 YIrsdpvaqvfVHGDSLQAclvgVVVPDPD 605
Cdd:cd05904 429 LL---------SHPEILDA----AVIPYPD 445
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
263-617 |
2.15e-39 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 152.10 E-value: 2.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 263 PPKPEDLALICFTSGTTGNPKGAMLTHGNVVSN---CSAFIKITeeslklcPQDVLISFLPLAHMFERVVEGVL-LCHGA 338
Cdd:cd05909 143 PVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANveqITAIFDPN-------PEDVVFGALPFFHSFGLTGCLWLpLLSGI 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 339 KIGYFQgdirllmddlknlKPTIFPVVPRLlnrmfdkIFGQANTPLkrwlldFATSrkeaELKSGVVRKdsmWDKLIFSk 418
Cdd:cd05909 216 KVVFHP-------------NPLDYKKIPEL-------IYDKKATIL------LGTP----TFLRGYARA---AHPEDFS- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 419 vqaslggRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPG-DWTAGHVGAPLPCNFVKLVDVAEMN 497
Cdd:cd05909 262 -------SLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHE 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 498 YFAANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKaGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYI 577
Cdd:cd05909 335 EVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGD-GWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDILS 412
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 528467780 578 RSDP----VAQVFV----HGDSLQACLVGvVVPDPDFLPGWAKNRGIE 617
Cdd:cd05909 413 EILPedneVAVVSVpdgrKGEKIVLLTTT-TDTDPSSLNDILKNAGIS 459
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
114-604 |
6.55e-39 |
|
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: 150.54 E-value: 6.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 114 AGQPYKWLSYKEVADRAE-FAGSalLHRGHSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDK 192
Cdd:cd05926 8 VPGSTPALTYADLAELVDdLARQ--LAALGIKKGDR-VAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 193 ASiTTIIcdIADKARLiLDCVSGRKHSVTTIVimesfdsELTAQAQNCgIDIISLKEL--EAIGKANHKTPIPPKPEDLA 270
Cdd:cd05926 85 LG-SKLV--LTPKGEL-GPASRAASKLGLAIL-------ELALDVGVL-IRAPSAESLsnLLADKKNAKSEGVPLPDDLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 271 LICFTSGTTGNPKGAMLTHGNVVSNCSAFIKiteeSLKLCPQDVLISFLPLAHMFERVVeGVL--LCHGAKIgyfqgdir 348
Cdd:cd05926 153 LILHTSGTTGRPKGVPLTHRNLAASATNITN----TYKLTPDDRTLVVMPLFHVHGLVA-SLLstLAAGGSV-------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 349 lLM----------DDLKNLKPTIFPVVPRLLnrmfdKIfgqantplkrwLLDFATSRKEAELksgvvrkdsmwdklifsk 418
Cdd:cd05926 220 -VLpprfsastfwPDVRDYNATWYTAVPTIH-----QI-----------LLNRPEPNPESPP------------------ 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 419 vqaslgGRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAgcTMSL----PGDWTAGHVGAPlpcNFVKLVDVA 494
Cdd:cd05926 265 ------PKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAH--QMTSnplpPGPRKPGSVGKP---VGVEVRILD 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 495 EM-NYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIE 573
Cdd:cd05926 334 EDgEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVD 412
|
490 500 510
....*....|....*....|....*....|.
gi 528467780 574 NIYIRSDPVAQVFVHGdslqaclvgvvVPDP 604
Cdd:cd05926 413 GVLLSHPAVLEAVAFG-----------VPDE 432
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
232-614 |
2.19e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 150.54 E-value: 2.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 232 ELTAQAQNcgidIISLKEL--EAIGKANHKTPIP-PKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCS---AFIKITEE 305
Cdd:PRK05605 185 ALTGPAPG----TVPWETLvdAAIGGDGSDVSHPrPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqgkAWVPGLGD 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 306 SlklcpQDVLISFLPLAHMFervveGVLLCH------GAKIGYFQG-DIRLLMDDLKNLKPTIFPVVPRLlnrmFDKIfg 378
Cdd:PRK05605 261 G-----PERVLAALPMFHAY-----GLTLCLtlavsiGGELVLLPApDIDLILDAMKKHPPTWLPGVPPL----YEKI-- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 379 qantplkrwlldfatsRKEAElKSGVvrkdsmwdklifskvqaSLGGrVRLMITGAAPVSPTVLTFLRAALGCQFYEGYG 458
Cdd:PRK05605 325 ----------------AEAAE-ERGV-----------------DLSG-VRNAFSGAMALPVSTVELWEKLTGGLLVEGYG 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 459 QTECT---AGCTMSlpGDWTAGHVGAPLPCNFVKLVDVAEMNYFAANGE-GEVCVKGPNVFQGYLKDPEQTSgAVDKAGW 534
Cdd:PRK05605 370 LTETSpiiVGNPMS--DDRRPGYVGVPFPDTEVRIVDPEDPDETMPDGEeGELLVRGPQVFKGYWNRPEETA-KSFLDGW 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 535 LHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVFVHG-------DSLQACLV---GVVVpDP 604
Cdd:PRK05605 447 FRTGDVVVMEEDGFIRIVDRIKELI-ITGGFNVYPAEVEEVLREHPGVEDAAVVGlpredgsEEVVAAVVlepGAAL-DP 524
|
410
....*....|
gi 528467780 605 DFLPGWAKNR 614
Cdd:PRK05605 525 EGLRAYCREH 534
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
123-587 |
3.20e-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: 147.60 E-value: 3.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 123 YKEVADRAEfagsaLLHRGHSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIICDi 202
Cdd:TIGR01923 6 DCEAAHLAK-----ALKAQGIRSGSR-VALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 203 adkarlildcvsgrkhsvttivimESFDSEltaqaqncGIDIISLKELEAIGKANHKTPIPPKPEDLALICFTSGTTGNP 282
Cdd:TIGR01923 79 ------------------------SLLEEK--------DFQADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 283 KGAMLTHGNVVSNCSAfikiTEESLKLCPQDVLISFLPLAHmfervVEGV-----LLCHGAKIGYFQGDIRLLmDDLKNL 357
Cdd:TIGR01923 127 KAVPHTFRNHYASAVG----SKENLGFTEDDNWLLSLPLYH-----ISGLsilfrWLIEGATLRIVDKFNQLL-EMIANE 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 358 KPTIFPVVPRLLNRMFDKifGQANTPLKRWLLdfatsrkeaelksgvvrkdsmwdklifskvqaslGGrvrlmitGAAPV 437
Cdd:TIGR01923 197 RVTHISLVPTQLNRLLDE--GGHNENLRKILL----------------------------------GG-------SAIPA 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 438 sptvlTFLRAAL--GCQFYEGYGQTE-CTAGCTMSLPGDWTAGHVGAPLPCNFVKL-VDVAEmnyfaanGEGEVCVKGPN 513
Cdd:TIGR01923 234 -----PLIEEAQqyGLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIkVDNKE-------GHGEIMVKGAN 301
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528467780 514 VFQGYLkDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVFV 587
Cdd:TIGR01923 302 LMKGYL-YQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVV 373
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
245-605 |
1.29e-36 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 145.02 E-value: 1.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 245 ISLKELEAIGKANHKTPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEESLKLCP-QDVLISFLPLAH 323
Cdd:PRK08751 186 IRFREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKLEEgCEVVITALPLYH 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 324 MFERVVEGVLLCHGAKIGYFQGDIRLLMDDLKNLKPTIFPVVPRLlNRMFDKIFgqaNTPlkrwlldfatsrkeaelksg 403
Cdd:PRK08751 266 IFALTANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGV-NTLFNGLL---NTP-------------------- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 404 vvrkdsMWDKLIFSKVQASLGGrvrlmitGAApVSPTVLTFLRAALGCQFYEGYGQTECT-AGCTMSLPGDWTAGHVGAP 482
Cdd:PRK08751 322 ------GFDQIDFSSLKMTLGG-------GMA-VQRSVAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLP 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 483 LPCNFVKLVDvaEMNYFAANGE-GEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkL 561
Cdd:PRK08751 388 IPSTDACIKD--DAGTVLAIGEiGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-L 464
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 528467780 562 AQGEYIAPEKIENIYIRSDPVAQVFVHG--DSLQACLVGVVVPDPD 605
Cdd:PRK08751 465 VSGFNVYPNEIEDVIAMMPGVLEVAAVGvpDEKSGEIVKVVIVKKD 510
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
91-589 |
3.65e-36 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 143.76 E-value: 3.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 91 TLYEFFLRGLRVSNNGPCLGSRKAGQPYkwlSYKEVADRAEFAGSALLHRGHsQSGDKyIGIFAQNRPEWTISELACYTY 170
Cdd:PRK12583 19 TIGDAFDATVARFPDREALVVRHQALRY---TWRQLADAVDRLARGLLALGV-QPGDR-VGIWAPNCAEWLLTQFATARI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 171 SLVAVPLYDTLGTEAISYVIDKASITTIICDIADKAR----LILDCVSGRKHSVTTIVIME---------SFDSE----- 232
Cdd:PRK12583 94 GAILVNINPAYRASELEYALGQSGVRWVICADAFKTSdyhaMLQELLPGLAEGQPGALACErlpelrgvvSLAPApppgf 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 233 LTAQAQNCGIDIISLKELEAIGKANHktpippkPEDLALICFTSGTTGNPKGAMLTHGNVVSNCsafiKITEESLKLCPQ 312
Cdd:PRK12583 174 LAWHELQARGETVSREALAERQASLD-------RDDPINIQYTSGTTGFPKGATLSHHNILNNG----YFVAESLGLTEH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 313 DVLISFLPLAHMFERVVeGVLLC--HGAKIGYFQG--DIRLLMDDLKNLKPTIFPVVPRllnrMFdkiFGQANTPlkrwl 388
Cdd:PRK12583 243 DRLCVPVPLYHCFGMVL-ANLGCmtVGACLVYPNEafDPLATLQAVEEERCTALYGVPT----MF---IAELDHP----- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 389 ldfatSRKEAELKSgvvrkdsmwdklifskvqaslggrVRLMITGAAPVSPTVLTFLRAALGC-QFYEGYGQTECTAGCT 467
Cdd:PRK12583 310 -----QRGNFDLSS------------------------LRTGIMAGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 468 MSLPGD---WTAGHVGAPLPCNFVKLVDvAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWL 544
Cdd:PRK12583 361 QTTAADdleRRVETVGRTQPHLEVKVVD-PDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMD 439
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 528467780 545 PNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVFVHG 589
Cdd:PRK12583 440 EQGYVRIVGRSKDMI-IRGGENIYPREIEEFLFTHPAVADVQVFG 483
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
172-608 |
8.02e-36 |
|
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: 141.04 E-value: 8.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 172 LVAVPLYDTLGTEAISYVIDKASITTIICDiadkarlildcvsgrkhsvttivimESFDSELTAQAQNCGIDIISLKElE 251
Cdd:cd05922 47 LVFVPLNPTLKESVLRYLVADAGGRIVLAD-------------------------AGAADRLRDALPASPDPGTVLDA-D 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 252 AIGKANHKTP-IPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIkiteESLKLCPQDVLISFLPLAHMFervve 330
Cdd:cd05922 101 GIRAARASAPaHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIA----EYLGITADDRALTVLPLSYDY----- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 331 G--VLLCH---GAKIgYFQGDIRL---LMDDLKNLKPTIFPVVP---RLLNRMfdkIFGQANTPLKRWLldfatsrkeae 399
Cdd:cd05922 172 GlsVLNTHllrGATL-VLTNDGVLddaFWEDLREHGATGLAGVPstyAMLTRL---GFDPAKLPSLRYL----------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 400 lksgvvrkdsmwdklifskvqASLGGRVRlmitgaapvsPTVLTFLRAAL-GCQFYEGYGQTECTAGCTMsLPGDWTA-- 476
Cdd:cd05922 237 ---------------------TQAGGRLP----------QETIARLRELLpGAQVYVMYGQTEATRRMTY-LPPERILek 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 477 -GHVGAPLP-CNFVKLVDVAEMnyfAANGE-GEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIID 553
Cdd:cd05922 285 pGSIGLAIPgGEFEILDDDGTP---TPPGEpGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVG 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528467780 554 RKKHIFKLAqGEYIAPEKIENIyIRSDPVAQVFV-------HGDSLQACLVGVVVPDPDFLP 608
Cdd:cd05922 362 RRDRMIKLF-GNRISPTEIEAA-ARSIGLIIEAAavglpdpLGEKLALFVTAPDKIDPKDVL 421
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
268-589 |
2.73e-34 |
|
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: 133.78 E-value: 2.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 268 DLALICFTSGTTGNPKGAMLTHGNVVSNCSAF---IKITEESLKLCPQdvlisflPLAHMFERVVeGVLLC--HGAKI-- 340
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWadcADLTEDDRYLIIN-------PFFHTFGYKA-GIVACllTGATVvp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 341 -GYFqgDIRLLMDDLKNLKPTIFPVVPRLLNRMFDKifgqantplkrwlldfaTSRKEAELKSgvvrkdsmwdklifskv 419
Cdd:cd17638 73 vAVF--DVDAILEAIERERITVLPGPPTLFQSLLDH-----------------PGRKKFDLSS----------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 420 qaslggrVRLMITGAAPVSPTVLTFLRAALGCQ-FYEGYGQTECTAGcTMSLPGD---WTAGHVGAPLPCNFVKLVDvae 495
Cdd:cd17638 117 -------LRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVA-TMCRPGDdaeTVATTCGRACPGFEVRIAD--- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 496 mnyfaangEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENI 575
Cdd:cd17638 186 --------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGA 256
|
330
....*....|....
gi 528467780 576 YIRSDPVAQVFVHG 589
Cdd:cd17638 257 LAEHPGVAQVAVIG 270
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
243-604 |
2.98e-34 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 137.88 E-value: 2.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 243 DIISLKELEAIGKanHKTPIPP--KPEDLALICFTSGTTGNPKGAMLTHGNVVSNC-------SAFIKITEEslklcpqd 313
Cdd:PRK08974 182 DAISFRSALHKGR--RMQYVKPelVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqakaayGPLLHPGKE-------- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 314 VLISFLPLAHMFERVVEGVLLCHgakigyfQGDIRLLMDDLKNLKPTifpvVPRLLNRMFDKIFGqANTPLKRWLldfat 393
Cdd:PRK08974 252 LVVTALPLYHIFALTVNCLLFIE-------LGGQNLLITNPRDIPGF----VKELKKYPFTAITG-VNTLFNALL----- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 394 srKEAELKsgvvrkdsmwdKLIFSkvqaslggRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECT---AGCTMSL 470
Cdd:PRK08974 315 --NNEEFQ-----------ELDFS--------SLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVNPYDL 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 471 PGdwTAGHVGAPLPCNFVKLVDvaEMNYFAANGE-GEVCVKGPNVFQGYLKDPEQTSgAVDKAGWLHTGDIGKWLPNGTL 549
Cdd:PRK08974 374 DY--YSGSIGLPVPSTEIKLVD--DDGNEVPPGEpGELWVKGPQVMLGYWQRPEATD-EVIKDGWLATGDIAVMDEEGFL 448
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 528467780 550 KIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVFV----HGDSLQACLVGVVVPDP 604
Cdd:PRK08974 449 RIVDRKKDMI-LVSGFNVYPNEIEDVVMLHPKVLEVAAvgvpSEVSGEAVKIFVVKKDP 506
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
121-586 |
7.53e-34 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 136.86 E-value: 7.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAV---PLYDTlgtEAISYVIDKASITT 197
Cdd:PRK08315 44 WTYREFNEEVDALAKGLLALG-IEKGDR-VGIWAPNVPEWVLTQFATAKIGAILVtinPAYRL---SELEYALNQSGCKA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 198 IIC-------DIADKARLIL----DCVSGRKHSV------TTIVI-------MESFDsELTAQAQNcgidiISLKELEAI 253
Cdd:PRK08315 119 LIAadgfkdsDYVAMLYELApelaTCEPGQLQSArlpelrRVIFLgdekhpgMLNFD-ELLALGRA-----VDDAELAAR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 254 GKANHktpippkPEDLALICFTSGTTGNPKGAMLTHGNVVSNcSAFIKiteESLKLCPQDVLISFLPLAHMFErVVEGVL 333
Cdd:PRK08315 193 QATLD-------PDDPINIQYTSGTTGFPKGATLTHRNILNN-GYFIG---EAMKLTEEDRLCIPVPLYHCFG-MVLGNL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 334 LC--HGAKIGY----FqgdirllmDDLKNLK-------------PTIFpvVPRLLNRMFDKifgqantplkrwlLDFATs 394
Cdd:PRK08315 261 ACvtHGATMVYpgegF--------DPLATLAaveeerctalygvPTMF--IAELDHPDFAR-------------FDLSS- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 395 rkeaeLKSGV---------VRKdsmwdklifsKVQASLGgrvrlM--ITGAapvsptvltflraalgcqfyegYGQTECT 463
Cdd:PRK08315 317 -----LRTGImagspcpieVMK----------RVIDKMH-----MseVTIA----------------------YGMTETS 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 464 AGCTMSLPGD------WTaghVGAPLPCNFVKLVDvAEMNYFAANGE-GEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLH 536
Cdd:PRK08315 355 PVSTQTRTDDplekrvTT---VGRALPHLEVKIVD-PETGETVPRGEqGELCTRGYSVMKGYWNDPEKTAEAIDADGWMH 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 528467780 537 TGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPV--AQVF 586
Cdd:PRK08315 431 TGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEFLYTHPKIqdVQVV 481
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
147-605 |
7.89e-34 |
|
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: 136.50 E-value: 7.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 147 DKYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIICdiadkARLILDCVSGRKHSVTTIVIM 226
Cdd:cd17642 69 NDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFC-----SKKGLQKVLNVQKKLKIIKTI 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 227 ESFDSELTAQAQNCGIDIISLKELEAIGKANHKTPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEES 306
Cdd:cd17642 144 IILDSKEDYKGYQCLYTFITQNLPPGFNEYDFKPPSFDRDEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGN 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 307 lKLCPQDVLISFLPLAHMFERVVEGVLLCHGAKIGY-FQGDIRLLMDDLKNLKPTIFPVVPRLLnrmfdkifgqantplk 385
Cdd:cd17642 224 -QIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLmYKFEEELFLRSLQDYKVQSALLVPTLF---------------- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 386 rwlldfatsrkeaelksGVVRKDSMWDKLIFSKVQAslggrvrlMITGAAPVSPTVLTFLRAALGCQFY-EGYGQTECTA 464
Cdd:cd17642 287 -----------------AFFAKSTLVDKYDLSNLHE--------IASGGAPLSKEVGEAVAKRFKLPGIrQGYGLTETTS 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 465 GCTMSLPGDWTAGHVGAPLPCNFVKLVDVAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWL 544
Cdd:cd17642 342 AILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYD 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528467780 545 PNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDPVAQVFVHGdslqaclvgvvVPDPD 605
Cdd:cd17642 422 EDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQHPKIFDAGVAG-----------IPDED 470
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
121-603 |
1.99e-33 |
|
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: 133.66 E-value: 1.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKAsittiic 200
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALG-VGPGDV-VAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRA------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 diadKARLIldcvsgrkhsvttiVIMESFdseltaqaqncgidiislkeleaiGKANHKtpipPKPEDLALICFTSGTTG 280
Cdd:cd05903 73 ----KAKVF--------------VVPERF------------------------RQFDPA----AMPDAVALLLFTSGTTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 281 NPKGAMLTHGNVVSNCSAFIkiteESLKLCPQDVLISFLPLAHMfervvEGVLlcHGAKIGYFQGDIRLLMDDLKNLKpt 360
Cdd:cd05903 107 EPKGVMHSHNTLSASIRQYA----ERLGLGPGDVFLVASPMAHQ-----TGFV--YGFTLPLLLGAPVVLQDIWDPDK-- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 361 ifpvVPRLLNRmfDKI-FGQANTPlkrwlldFATSRKEAELKSGVVRKdsmwdklifskvqaslggRVRLMITGAAPVSP 439
Cdd:cd05903 174 ----ALALMRE--HGVtFMMGATP-------FLTDLLNAVEEAGEPLS------------------RLRTFVCGGATVPR 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 440 TVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGD-WTAGHV-GAPLPCNFVKLVDvAEMNYFAANGEGEVCVKGPNVFQG 517
Cdd:cd05903 223 SLARRAAELLGAKVCSAYGSTECPGAVTSITPAPeDRRLYTdGRPLPGVEIKVVD-DTGATLAPGVEGELLSRGPSVFLG 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 518 YLKDPEQTSGAVDKaGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIyirsdpvaqVFVHGDSLQACLV 597
Cdd:cd05903 302 YLDRPDLTADAAPE-GWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDL---------LLGHPGVIEAAVV 370
|
....*.
gi 528467780 598 GvvVPD 603
Cdd:cd05903 371 A--LPD 374
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
68-577 |
2.68e-33 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 134.72 E-value: 2.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 68 EYARRSILMDndthmtYYYKDALTLYEF-FLRGLRVSNNgPCLGSRKAGQPYkwlSYKEVADRAEFAGSALLHRGHSQsG 146
Cdd:PLN02246 7 EFIFRSKLPD------IYIPNHLPLHDYcFERLSEFSDR-PCLIDGATGRVY---TYADVELLSRRVAAGLHKLGIRQ-G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 147 DkYIGIFAQNRPEWTISELACYTYSLV---AVPLYdtlgTEAISYVIDKASITTIICDIA---DKARLILDcvsgrKHSV 220
Cdd:PLN02246 76 D-VVMLLLPNCPEFVLAFLGASRRGAVtttANPFY----TPAEIAKQAKASGAKLIITQScyvDKLKGLAE-----DDGV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 221 TTIVIMESFD-----SELTAQAQNcgidiiSLKELEAigkanhktpippKPEDLALICFTSGTTGNPKGAMLTHGNVVSN 295
Cdd:PLN02246 146 TVVTIDDPPEgclhfSELTQADEN------ELPEVEI------------SPDDVVALPYSSGTTGLPKGVMLTHKGLVTS 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 296 CSAFIKITEESLKLCPQDVLISFLPLAHMFErvVEGVLLCH---GAKIGYFQG-DIRLLMDDLKNLKPTIFPVVPrllnr 371
Cdd:PLN02246 208 VAQQVDGENPNLYFHSDDVILCVLPMFHIYS--LNSVLLCGlrvGAAILIMPKfEIGALLELIQRHKVTIAPFVP----- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 372 mfdkifgqantPLkrwLLDFAtsrkeaelKSGVVRKDSMwdklifskvqASlggrVRLMITGAAPVSPTVLTFLRAAL-G 450
Cdd:PLN02246 281 -----------PI---VLAIA--------KSPVVEKYDL----------SS----IRMVLSGAAPLGKELEDAFRAKLpN 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 451 CQFYEGYGQTECTAGCTMSL-----PGDWTAGHVGAPLPCNFVKLVDVAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQT 525
Cdd:PLN02246 325 AVLGQGYGMTEAGPVLAMCLafakePFPVKSGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYLNDPEAT 404
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 528467780 526 SGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYI 577
Cdd:PLN02246 405 ANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAELEALLI 455
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
268-605 |
9.97e-32 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 130.48 E-value: 9.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 268 DLALICFTSGTTGNPKGAMLTHGNVVSN-CSAFIKITEEslkLCPQDVLISFLPLAHMFErvVEGV----LLCHGAKIGY 342
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTHRNLVANlCSSLFSVGPE---MIGQVVTLGLIPFFHIYG--ITGIccatLRNKGKVVVM 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 343 FQGDIRLLMDDLKNLKPTIFPVVPRLLNRMFdkifgqantplkrwlldfatsrkeaelksgvvrKDSMWDKLIFSKVqas 422
Cdd:PLN02330 260 SRFELRTFLNALITQEVSFAPIVPPIILNLV---------------------------------KNPIVEEFDLSKL--- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 423 lggRVRLMITGAAPVSPTVLTFLRAAL-GCQFYEGYGQTECTagCTMSLPGDWTAGH-------VGAPLPCNFVKLVDVA 494
Cdd:PLN02330 304 ---KLQAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEHS--CITLTHGDPEKGHgiakknsVGFILPNLEVKFIDPD 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 495 EMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIEN 574
Cdd:PLN02330 379 TGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEA 457
|
330 340 350
....*....|....*....|....*....|.
gi 528467780 575 IYIRSDPVAQVfvhgdslqaclvgVVVPDPD 605
Cdd:PLN02330 458 ILLTHPSVEDA-------------AVVPLPD 475
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
245-603 |
1.67e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 129.88 E-value: 1.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 245 ISLKELEAIGKANHKTPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSN---CSAFIKITEESLKlcpqDVLISFLPL 321
Cdd:PRK05677 185 VKFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANmlqCRALMGSNLNEGC----EILIAPLPL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 322 AHMFERVVE-GVLLCHGAKigyfqgdiRLLMDDlknlkPTIFPVVPRLLNRMFDKIFGQANTplkrwlLDFATSRKEAel 400
Cdd:PRK05677 261 YHIYAFTFHcMAMMLIGNH--------NILISN-----PRDLPAMVKELGKWKFSGFVGLNT------LFVALCNNEA-- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 401 ksgvvrkdsmWDKLIFSKVQASLGGRVRLMITGAapvsptvlTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVG 480
Cdd:PRK05677 320 ----------FRKLDFSALKLTLSGGMALQLATA--------ERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIG 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 481 APLPCNFVKLVDvAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFk 560
Cdd:PRK05677 382 IPVPSTLCKVID-DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI- 459
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 528467780 561 LAQGEYIAPEKIENIyirsdpvaqVFVHGDSLQACLVGvvVPD 603
Cdd:PRK05677 460 LVSGFNVYPNELEDV---------LAALPGVLQCAAIG--VPD 491
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
122-604 |
2.06e-31 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 127.41 E-value: 2.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 122 SYKEVADRAEFAGSALLHRGhSQSGDkYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIICD 201
Cdd:cd05934 5 TYAELLRESARIAAALAALG-IRPGD-RVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 202 iadkarlildcvsgrkhsvttivimesfdseltaqaqncgidiislkeleaigkanhktpippkpedLALICFTSGTTGN 281
Cdd:cd05934 83 -------------------------------------------------------------------PASILYTSGTTGP 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 282 PKGAMLTHGNVVSNCSAFIkiteESLKLCPQDVLISFLPLAHMfERVVEGVL--LCHGAKI--------GYFQGDIRllm 351
Cdd:cd05934 96 PKGVVITHANLTFAGYYSA----RRFGLGEDDVYLTVLPLFHI-NAQAVSVLaaLSVGATLvllprfsaSRFWSDVR--- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 352 ddlkNLKPTIF---PVVPRLLnrmfdkifgqANTPlkrwlldfatsrkeaelksgvvrkDSMWDKlifskvqaslGGRVR 428
Cdd:cd05934 168 ----RYGATVTnylGAMLSYL----------LAQP------------------------PSPDDR----------AHRLR 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 429 LmiTGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDvaEMNYFAANGE-GEV 507
Cdd:cd05934 200 A--AYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVD--DDGQELPAGEpGEL 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 508 CVK---GPNVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYIRSDPVAQ 584
Cdd:cd05934 276 VIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVERAILRHPAVRE 353
|
490 500
....*....|....*....|
gi 528467780 585 VFVHGdslqaclvgvvVPDP 604
Cdd:cd05934 354 AAVVA-----------VPDE 362
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
121-605 |
3.24e-31 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 127.26 E-value: 3.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGHSQsgDKYIGIFAQNRPEWTISELACytysLVA----VPLYDTLGTEAISYVIDKAsit 196
Cdd:cd05930 13 LTYAELDARANRLARYLRERGVGP--GDLVAVLLERSLEMVVAILAV----LKAgaayVPLDPSYPAERLAYILEDS--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 197 tiicdiadKARLILDCvsgrkhsvttivimesfdseltaqaqncgidiislkeleaigkanhktpippkPEDLALICFTS 276
Cdd:cd05930 84 --------GAKLVLTD-----------------------------------------------------PDDLAYVIYTS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 277 GTTGNPKGAMLTHGNVVSNCSAFIkiteESLKLCPQDVLISFLPLAH------MFervvegVLLCHGAKIgYF-----QG 345
Cdd:cd05930 103 GSTGKPKGVMVEHRGLVNLLLWMQ----EAYPLTPGDRVLQFTSFSFdvsvweIF------GALLAGATL-VVlpeevRK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 346 DIRLLMDDLKNLKPTIFPVVPRLLNRMFDKIFGQANTPLkrwlldfatsrkeaelksgvvrkdsmwdklifskvqaslgg 425
Cdd:cd05930 172 DPEALADLLAEEGITVLHLTPSLLRLLLQELELAALPSL----------------------------------------- 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 426 rvRLMITGAAPVSPTVLT-FLRAALGCQFYEGYGQTECTAGCTM--SLPGDWTAGHV--GAPLPCNFVKLVDvAEMNYFA 500
Cdd:cd05930 211 --RLVLVGGEALPPDLVRrWRELLPGARLVNLYGPTEATVDATYyrVPPDDEEDGRVpiGRPIPNTRVYVLD-ENLRPVP 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 501 ANGEGEVCVKGPNVFQGYLKDPEQTSGAV-----DKAGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEN 574
Cdd:cd05930 288 PGVPGELYIGGAGLARGYLNRPELTAERFvpnpfGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIELGEIEA 366
|
490 500 510
....*....|....*....|....*....|....
gi 528467780 575 IYIRSDPVAQVFV---HGDSLQACLVGVVVPDPD 605
Cdd:cd05930 367 ALLAHPGVREAAVvarEDGDGEKRLVAYVVPDEG 400
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
121-604 |
3.93e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 128.18 E-value: 3.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYdTLGTEA-ISYVIDKASITTII 199
Cdd:PRK06188 38 LTYGQLADRISRYIQAFEALG-LGTGDA-VALLSLNRPEVLMAIGAAQLAGLRRTALH-PLGSLDdHAYVLEDAGISTLI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 200 CD---IADKARLILDCVSGRKHSvttivimesfdseLTAQAQNCGIDIislkeLEAIGKANHKTPIPPK-PEDLALICFT 275
Cdd:PRK06188 115 VDpapFVERALALLARVPSLKHV-------------LTLGPVPDGVDL-----LAAAAKFGPAPLVAAAlPPDIAGLAYT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 276 SGTTGNPKGAMLTHGNVVSncSAFIKITEESLklcPQDvlISFL---PLAHMFERVVEGVLLcHGAKIGYFQG-DIRLLM 351
Cdd:PRK06188 177 GGTTGKPKGVMGTHRSIAT--MAQIQLAEWEW---PAD--PRFLmctPLSHAGGAFFLPTLL-RGGTVIVLAKfDPAEVL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 352 DDLKNLKPTIFPVVPRLLNRmfdkifgqantplkrwLLDFATSRKeAELKSgvvrkdsmwdklifskvqaslggrVRLMI 431
Cdd:PRK06188 249 RAIEEQRITATFLVPTMIYA----------------LLDHPDLRT-RDLSS------------------------LETVY 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 432 TGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHV------GAPLPCNFVKLVDvAEMNYFAANGEG 505
Cdd:PRK06188 288 YGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLRVALLD-EDGREVAQGEVG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 506 EVCVKGPNVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIEniyirsDPVAQv 585
Cdd:PRK06188 367 EICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMI-VTGGFNVFPREVE------DVLAE- 437
|
490
....*....|....*....
gi 528467780 586 fvHGDSLQACLVGvvVPDP 604
Cdd:PRK06188 438 --HPAVAQVAVIG--VPDE 452
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
121-606 |
1.73e-30 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 126.14 E-value: 1.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLyDTLGTEA-ISYVIDKASITTII 199
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALG-VKPGDR-VAVQVEKSPEALALYLATLRAGAVFLPL-NTAYTLAeLDYFIGDAEPALVV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 200 CDIADKA--RLIldcvsGRKHSVTTIvimesfdseLTAQAQNCGidiiSLKELeAIGKANHKTPIPPKPEDLALICFTSG 277
Cdd:PRK07514 106 CDPANFAwlSKI-----AAAAGAPHV---------ETLDADGTG----SLLEA-AAAAPDDFETVPRGADDLAAILYTSG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 278 TTGNPKGAMLTHGNVVSNCsafikiteESLKLC----PQDVLISFLPLAH---MFerVVEGVLLCHGAKIGYFQgdiRLL 350
Cdd:PRK07514 167 TTGRSKGAMLSHGNLLSNA--------LTLVDYwrftPDDVLIHALPIFHthgLF--VATNVALLAGASMIFLP---KFD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 351 MDDLKNLKP--TIFPVVPRLLNRMFDkifgqantplkrwlldfatsrkEAELKSGVVRkdsmwdklifskvqaslggRVR 428
Cdd:PRK07514 234 PDAVLALMPraTVMMGVPTFYTRLLQ----------------------EPRLTREAAA-------------------HMR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 429 LMITGAAPVSPTVLTFLRAALGCQFYEGYGQTEcTAGCTmSLP--GDWTAGHVGAPLPCNFVKLVDVAEMNYFAANGEGE 506
Cdd:PRK07514 273 LFISGSAPLLAETHREFQERTGHAILERYGMTE-TNMNT-SNPydGERRAGTVGFPLPGVSLRVTDPETGAELPPGEIGM 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 507 VCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIfkLAQGEY-IAPEKIENiYIrsDPVAQV 585
Cdd:PRK07514 351 IEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDL--IISGGYnVYPKEVEG-EI--DELPGV 425
|
490 500
....*....|....*....|.
gi 528467780 586 fvhgdsLQACLVGvvVPDPDF 606
Cdd:PRK07514 426 ------VESAVIG--VPHPDF 438
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
262-604 |
3.93e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 125.53 E-value: 3.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 262 IPPKPE-DLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEESLKlcPQDVLISFLPLAHMF-ERVVEGVLLCHGAK 339
Cdd:PRK06710 200 VPCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKE--GEEVVLGVLPFFHVYgMTAVMNLSIMQGYK 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 340 IGYF-QGDIRLLMDDLKNLKPTIFPVVPRLLNRMFdkifgqaNTPLkrwlldfatsRKEAELKSgvvrkdsmwdklifsk 418
Cdd:PRK06710 278 MVLIpKFDMKMVFEAIKKHKVTLFPGAPTIYIALL-------NSPL----------LKEYDISS---------------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 419 vqaslggrVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTEcTAGCTMS--LPGDWTAGHVGAPLPCNFVKLVDVAEM 496
Cdd:PRK06710 325 --------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTE-SSPVTHSnfLWEKRVPGSIGVPWPDTEAMIMSLETG 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 497 NYFAANGEGEVCVKGPNVFQGYLKDPEQTSgAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 576
Cdd:PRK06710 396 EALPPGEIGEIVVKGPQIMKGYWNKPEETA-AVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREVEEVL 473
|
330 340
....*....|....*....|....*...
gi 528467780 577 IRSDPVAQVFVHGdslqaclvgvvVPDP 604
Cdd:PRK06710 474 YEHEKVQEVVTIG-----------VPDP 490
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
245-583 |
4.68e-30 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 125.32 E-value: 4.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 245 ISLKELEAIGKANHKTPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNC----SAFIKITEESLKLCP--QDVLISF 318
Cdd:PRK12492 185 VPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMlqvrACLSQLGPDGQPLMKegQEVMIAP 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 319 LPLAHMFE-------RVVEG---VLLCHGAKIGYFqgdirllmddLKNLKPTIFPVVPRLlNRMFDKIFgqaNTPlkrwl 388
Cdd:PRK12492 265 LPLYHIYAftancmcMMVSGnhnVLITNPRDIPGF----------IKELGKWRFSALLGL-NTLFVALM---DHP----- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 389 lDFAtsrkeaelksgvvrkdsmwdKLIFSKVQASLGGrvrlmitGAAPVSPTVLTFlRAALGCQFYEGYGQTECTAGCTM 468
Cdd:PRK12492 326 -GFK--------------------DLDFSALKLTNSG-------GTALVKATAERW-EQLTGCTIVEGYGLTETSPVAST 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 469 SLPGDWTA-GHVGAPLPCNFVKLVDvAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNG 547
Cdd:PRK12492 377 NPYGELARlGTVGIPVPGTALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDG 455
|
330 340 350
....*....|....*....|....*....|....*.
gi 528467780 548 TLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVA 583
Cdd:PRK12492 456 FVRIVDRKKDLI-IVSGFNVYPNEIEDVVMAHPKVA 490
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
233-603 |
7.58e-30 |
|
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: 122.80 E-value: 7.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 233 LTAQAQNCGIDIISLKE-LEAIGKANHKTPI--PPKPEDLALICFTSGTTGNPKGAMLTHGNVVSncsaFIKITEESLKL 309
Cdd:cd17653 68 LKAGAAYVPLDAKLPSArIQAILRTSGATLLltTDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLN----YVSQPPARLDV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 310 CPQDVLISFLPLAhmFERVVEGVL--LCHGAKIgYFQGDIRLLMDDLKNLkpTIFPVVPRLLnrmfdkifgqantplkrw 387
Cdd:cd17653 144 GPGSRVAQVLSIA--FDACIGEIFstLCNGGTL-VLADPSDPFAHVARTV--DALMSTPSIL------------------ 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 388 lldfatsrkeaelksGVVRKDSmwdkliFSkvqaslggRVRLMITGAAPVSPTVLTflRAALGCQFYEGYGQTECTAGCT 467
Cdd:cd17653 201 ---------------STLSPQD------FP--------NLKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISST 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 468 MS--LPGDWTagHVGAPLPCNFVKLVDvAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAV----DKAGWLH--TGD 539
Cdd:cd17653 250 MTelLPGQPV--TIGKPIPNSTCYILD-ADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFvpdpFWPGSRMyrTGD 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528467780 540 IGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDPVAQ---VFVHGDSlqacLVGVVVPD 603
Cdd:cd17653 327 YGRWTEDGGLEFLGREDNQVKV-RGFRINLEEIEEVVLQSQPEVTqaaAIVVNGR----LVAFVTPE 388
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
121-589 |
1.36e-29 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 123.05 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGHSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:PRK06839 28 MTYKQLHEYVSKVAAYLIYELNVKKGER-IAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 DIADKAR-LILDCVSGRKHSVTtivimesfdseltaqaqncgidIISLKELEAIGKANHktpIPPKPEDLALICFTSGTT 279
Cdd:PRK06839 107 EKTFQNMaLSMQKVSYVQRVIS----------------------ITSLKEIEDRKIDNF---VEKNESASFIICYTSGTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 280 GNPKGAMLTHGNV----VSNCSAfikiteesLKLCPQDVLISFLPLAHMfervvegvllchgAKIGYFQgdirllmddlk 355
Cdd:PRK06839 162 GKPKGAVLTQENMfwnaLNNTFA--------IDLTMHDRSIVLLPLFHI-------------GGIGLFA----------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 356 nlKPTIFP----VVPRllnrMFDKifgqantplkrwllDFATSRKEAELKSGVVRKDSMWDKLIFSKVQASLG-GRVRLM 430
Cdd:PRK06839 210 --FPTLFAggviIVPR----KFEP--------------TKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNlQSVRWF 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 431 ITGAAPVsPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDW--TAGHVGAPLPCNFVKLVDVAEmNYFAANGEGEVC 508
Cdd:PRK06839 270 YNGGAPC-PEELMREFIDRGFLFGQGFGMTETSPTVFMLSEEDArrKVGSIGKPVLFCDYELIDENK-NKVEVGEVGELL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 509 VKGPNVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVFVH 588
Cdd:PRK06839 348 IRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQVINKLSDVYEVAVV 425
|
.
gi 528467780 589 G 589
Cdd:PRK06839 426 G 426
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
265-607 |
1.49e-29 |
|
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: 122.65 E-value: 1.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 265 KPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKIteesLKLCPQD-VL--------IS----FLPLAHmfervveG 331
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRA----LGLTSESrVLqfasytfdVSileiFTTLAA-------G 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 332 VLLCHGAKigyfqgdiRLLMDDLknlkptifpvvPRLLNRMfdkifgQANTplkrwlldfatsrkeAELKSGVVRkdsmw 411
Cdd:cd05918 173 GCLCIPSE--------EDRLNDL-----------AGFINRL------RVTW---------------AFLTPSVAR----- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 412 dkLIFSKVQASLggrvRLMITGAAPVSPTVLTflRAALGCQFYEGYGQTECTAGCTMSLPG-DWTAGHVGAPLPCNFVkL 490
Cdd:cd05918 208 --LLDPEDVPSL----RTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRPLGATCW-V 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 491 VDVAEMNYFAANGE-GEVCVKGPNVFQGYLKDPEQTSGA-VDKAGWLH------------TGDIGKWLPNGTLKIIDRKK 556
Cdd:cd05918 279 VDPDNHDRLVPIGAvGELLIEGPILARGYLNDPEKTAAAfIEDPAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKD 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 528467780 557 HIFKLaQGEYIAPEKIENIYIRSDP-----VAQVFVH-GDSLQACLVGVVVPDPDFL 607
Cdd:cd05918 359 TQVKI-RGQRVELGEIEHHLRQSLPgakevVVEVVKPkDGSSSPQLVAFVVLDGSSS 414
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
245-604 |
1.70e-29 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 123.59 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 245 ISLKELEAIGKANHKTPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNC--------SAFIKITEESlklcpQDVLI 316
Cdd:PRK07059 182 VRFNDALAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqmeawlqPAFEKKPRPD-----QLNFV 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 317 SFLPLAHMFERVVEGVLlchGAKIGyfqG---------DIRLLMDDLKNLKPTIFPVVPRLLNRMFdkifgqaNTPlkrw 387
Cdd:PRK07059 257 CALPLYHIFALTVCGLL---GMRTG---GrnilipnprDIPGFIKELKKYQVHIFPAVNTLYNALL-------NNP---- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 388 llDFatsrkeaelksgvvrkdsmwDKLIFSKVQASLGGrvrlmitGAApVSPTVLTFLRAALGCQFYEGYGQTEcTAGCT 467
Cdd:PRK07059 320 --DF--------------------DKLDFSKLIVANGG-------GMA-VQRPVAERWLEMTGCPITEGYGLSE-TSPVA 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 468 MSLPGDWTA--GHVGAPLPCNFVKLVDVAEMNyfAANGE-GEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWL 544
Cdd:PRK07059 369 TCNPVDATEfsGTIGLPLPSTEVSIRDDDGND--LPLGEpGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMD 446
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 545 PNGTLKIIDRKKHIFkLAQGEYIAPEKIENIyirsdpvaqVFVHGDSLQACLVGvvVPDP 604
Cdd:PRK07059 447 ERGYTKIVDRKKDMI-LVSGFNVYPNEIEEV---------VASHPGVLEVAAVG--VPDE 494
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
111-604 |
2.97e-29 |
|
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: 122.35 E-value: 2.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 111 SRKAGQPYKWLSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNrpewTISELACYtyslVAVPLydtLGT------- 183
Cdd:cd12119 16 SRTHEGEVHRYTYAEVAERARRLANALRRLG-VKPGDR-VATLAWN----THRHLELY----YAVPG---MGAvlhtinp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 184 ----EAISYVIDKASITTIICDIADKArlILDCVSGRKHSVTTIVIMESfDSELTAQAqncGIDIISLKELeaIGKANHK 259
Cdd:cd12119 83 rlfpEQIAYIINHAEDRVVFVDRDFLP--LLEAIAPRLPTVEHVVVMTD-DAAMPEPA---GVGVLAYEEL--LAAESPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 260 TPIPPKPE-DLALICFTSGTTGNPKGAMLTHGNVVSNcsAFIKITEESLKLCPQDVlisFLPLAHMFERVVEGV----LL 334
Cdd:cd12119 155 YDWPDFDEnTAAAICYTSGTTGNPKGVVYSHRSLVLH--AMAALLTDGLGLSESDV---VLPVVPMFHVNAWGLpyaaAM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 335 ChGAKI----GYFQGDirLLMDDLKNLKPTIFPVVPRLLNRMFDkifgqantplkrWLldfatSRKEAELKSGVvrkdsm 410
Cdd:cd12119 230 V-GAKLvlpgPYLDPA--SLAELIEREGVTFAAGVPTVWQGLLD------------HL-----EANGRDLSSLR------ 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 411 wdklifskvqaslggrvRLMITGAAPVSPTVLTFlrAALGCQFYEGYGQTECTAGCTMSLPgdwTAGHVGAP-------- 482
Cdd:cd12119 284 -----------------RVVIGGSAVPRSLIEAF--EERGVRVIHAWGMTETSPLGTVARP---PSEHSNLSedeqlalr 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 483 ----LPCNFV--KLVDvAEMNYFAANGE--GEVCVKGPNVFQGYLKDPEQTSgAVDKAGWLHTGDIGKWLPNGTLKIIDR 554
Cdd:cd12119 342 akqgRPVPGVelRIVD-DDGRELPWDGKavGELQVRGPWVTKSYYKNDEESE-ALTEDGWLRTGDVATIDEDGYLTITDR 419
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 528467780 555 KKHIFKLAqGEYIAPEKIENIYIRSDPVAQVFVhgdslqaclvgVVVPDP 604
Cdd:cd12119 420 SKDVIKSG-GEWISSVELENAIMAHPAVAEAAV-----------IGVPHP 457
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
264-589 |
3.24e-29 |
|
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: 120.53 E-value: 3.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 264 PKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAfikiTEESLKLCPQDVLISFLPLAH------MFERVVEG--VLLc 335
Cdd:cd05912 74 VKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIG----SALNLGLTEDDNWLCALPLFHisglsiLMRSVIYGmtVYL- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 336 hgakigYFQGDIRLLMDDLKNLKPTIFPVVPRLLNRMFdKIFGQANTPlkrwlldfatsrkeaelksgvvrkdsmwdkli 415
Cdd:cd05912 149 ------VDKFDAEQVLHLINSGKVTIISVVPTMLQRLL-EILGEGYPN-------------------------------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 416 fskvqaslggRVRLMITGAAPVSPTVLTFLRAaLGCQFYEGYGQTE-CTAGCTMSlPGDWTA--GHVGAPLPCNFVKLVD 492
Cdd:cd05912 190 ----------NLRCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTEtCSQIVTLS-PEDALNkiGSAGKPLFPVELKIED 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 493 vaemNYFAANGEGEVCVKGPNVFQGYLKdPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKI 572
Cdd:cd05912 258 ----DGQPPYEVGEILLKGPNVTKGYLN-RPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEI 331
|
330
....*....|....*..
gi 528467780 573 ENIYIRSDPVAQVFVHG 589
Cdd:cd05912 332 EEVLLSHPAIKEAGVVG 348
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
121-556 |
3.76e-29 |
|
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: 122.39 E-value: 3.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGhSQSGDKYIGIFAQNRPewTISEL-ACYTYSLVAVPLydtlgTEAISYVIDKASITTI- 198
Cdd:cd05906 40 QSYQDLLEDARRLAAGLRQLG-LRPGDSVILQFDDNED--FIPAFwACVLAGFVPAPL-----TVPPTYDEPNARLRKLr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 199 -ICDIADKARLIldcvsgrkhsvTTIVIMESFDsELTAQAQNCGIDIISLKELEAIGkANHKTPiPPKPEDLALICFTSG 277
Cdd:cd05906 112 hIWQLLGSPVVL-----------TDAELVAEFA-GLETLSGLPGIRVLSIEELLDTA-ADHDLP-QSRPDDLALLMLTSG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 278 TTGNPKGAMLTHGNVVSNCSAFIKITEeslkLCPQDVLISFLPLAHmfervVEGVLLCHGAkigyfqgDIRLLMDDLKNL 357
Cdd:cd05906 178 STGFPKAVPLTHRNILARSAGKIQHNG----LTPQDVFLNWVPLDH-----VGGLVELHLR-------AVYLGCQQVHVP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 358 KPTIFPVVPRLLnRMFDKiFGQANTplkrWLLDFATSRKEAELKSgvvRKDSMWDkliFSkvqaslggRVRLMIT-GAAP 436
Cdd:cd05906 242 TEEILADPLRWL-DLIDR-YRVTIT----WAPNFAFALLNDLLEE---IEDGTWD---LS--------SLRYLVNaGEAV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 437 VSPTVLTFLR--AALGCQ---FYEGYGQTECTAGCTMSLP---GDWTAGH----VGAPLPCNFVKLVDvAEMNYFAANGE 504
Cdd:cd05906 302 VAKTIRRLLRllEPYGLPpdaIRPAFGMTETCSGVIYSRSfptYDHSQALefvsLGRPIPGVSMRIVD-DEGQLLPEGEV 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 528467780 505 GEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGkWLPNGTLKIIDRKK 556
Cdd:cd05906 381 GRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
121-605 |
6.06e-29 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 122.14 E-value: 6.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADR-AEFAGsALLHRGhSQSGDKyIGIFAQNRPEWTISELACYtySL--VAVPLYDTLGTEAISYVIDKASITT 197
Cdd:COG0365 40 LTYAELRREvNRFAN-ALRALG-VKKGDR-VAIYLPNIPEAVIAMLACA--RIgaVHSPVFPGFGAEALADRIEDAEAKV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 198 IICD--------------IADKARLILDCVsgrkhsVTTIVI--------ME---SFDSELTAQAQNCgidiislkelea 252
Cdd:COG0365 115 LITAdgglrggkvidlkeKVDEALEELPSL------EHVIVVgrtgadvpMEgdlDWDELLAAASAEF------------ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 253 igkanhkTPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITeesLKLCPQDVLISFLPLAHMFER--VVE 330
Cdd:COG0365 177 -------EPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYV---LDLKPGDVFWCTADIGWATGHsyIVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 331 GVLLcHGAKIGYFQG-----DIRLLMDDLKNLKPTIFPVVPRLLnRMFDKifgQANTPLKRWllDFATsrkeaelksgvv 405
Cdd:COG0365 247 GPLL-NGATVVLYEGrpdfpDPGRLWELIEKYGVTVFFTAPTAI-RALMK---AGDEPLKKY--DLSS------------ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 406 rkdsmwdklifskvqaslggrVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWT-AGHVGAPLP 484
Cdd:COG0365 308 ---------------------LRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGLPVkPGSMGKPVP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 485 CNFVKLVDvAEMNYFAANGEGEVCVKG--PNVFQGYLKDPEQTSGAV--DKAGWLHTGDIGKWLPNGTLKIIDRKKHIFK 560
Cdd:COG0365 367 GYDVAVVD-EDGNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVIN 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 528467780 561 LAqGEYIAPEKIENIYIRSDPVAQVFVhgdslqaclVGvvVPDPD 605
Cdd:COG0365 446 VS-GHRIGTAEIESALVSHPAVAEAAV---------VG--VPDEI 478
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
122-587 |
1.08e-28 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 118.91 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 122 SYKEVADRAE-FAGsALLHRGHSQSGDkYIGIFAQNRPEWTISELACytysLVA----VPLYDTLGTEAISYVIDKASIT 196
Cdd:TIGR01733 1 TYRELDERANrLAR-HLRAAGGVGPGD-RVAVLLERSAELVVAILAV----LKAgaayVPLDPAYPAERLAFILEDAGAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 197 TIICDIADKARLIldcvsgrkhSVTTIVIMESFDSELTAQAQNCGIDiislkeleaigkanhkTPIPPKPEDLALICFTS 276
Cdd:TIGR01733 75 LLLTDSALASRLA---------GLVLPVILLDPLELAALDDAPAPPP----------------PDAPSGPDDLAYVIYTS 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 277 GTTGNPKGAMLTHGNVVSNCSAFIKITEeslkLCPQDVLISFLPLAhmFERVVEGVL--LCHGAKI-----GYFQGDIRL 349
Cdd:TIGR01733 130 GSTGRPKGVVVTHRSLVNLLAWLARRYG----LDPDDRVLQFASLS--FDASVEEIFgaLLAGATLvvppeDEERDDAAL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 350 LMDDLKNLKPTIFPVVPRLLNRMfdkifgqantplkrwlldfatsrkeaelksgvvrkdsmwdklifSKVQASLGGRVRL 429
Cdd:TIGR01733 204 LAALIAEHPVTVLNLTPSLLALL--------------------------------------------AAALPPALASLRL 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 430 MITGAAPVSPTVLTFLRAALG-CQFYEGYGQTECTAGCTM-SLPGDWTAGHV----GAPLPCNFVKLVDvAEMNYFAANG 503
Cdd:TIGR01733 240 VILGGEALTPALVDRWRARGPgARLINLYGPTETTVWSTAtLVDPDDAPRESpvpiGRPLANTRLYVLD-DDLRPVPVGV 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 504 EGEVCVKGPNVFQGYLKDPEQTS--------GAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 575
Cdd:TIGR01733 319 VGELYIGGPGVARGYLNRPELTAerfvpdpfAGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAA 397
|
490
....*....|..
gi 528467780 576 YIRSDPVAQVFV 587
Cdd:TIGR01733 398 LLRHPGVREAVV 409
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
173-603 |
1.43e-28 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 122.73 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 173 VAVPLYDTLGTEAISYVIDKASITTIICDIADKARLILDCVSGRKHSVTTIVIMESFDSELTAQAQNCGIDIISLKELEA 252
Cdd:PRK08633 691 VPVNLNYTASEAALKSAIEQAQIKTVITSRKFLEKLKNKGFDLELPENVKVIYLEDLKAKISKVDKLTALLAARLLPARL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 253 IGKANHKTPippKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKIteesLKLCPQDVLISFLPLAHMFERVVEGV 332
Cdd:PRK08633 771 LKRLYGPTF---KPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDV----FNLRNDDVILSSLPFFHSFGLTVTLW 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 333 L-LCHGAKIGYFQG--DIRLLMDDLKNLKPTIfpvvprllnrmfdkIFGqanTPlkRWLLDFATSRKeaelksgvvrkds 409
Cdd:PRK08633 844 LpLLEGIKVVYHPDptDALGIAKLVAKHRATI--------------LLG---TP--TFLRLYLRNKK------------- 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 410 mWDKLIFskvqASLggrvRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLP-----GDWT-----AGHV 479
Cdd:PRK08633 892 -LHPLMF----ASL----RLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNLPdvlaaDFKRqtgskEGSV 962
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 480 GAPLPCNFVKLVDVAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAV---DKAGWLHTGDIGKWLPNGTLKIIDRKK 556
Cdd:PRK08633 963 GMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRYS 1042
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 528467780 557 HIFKLAqGEYIAPEKIEniyirsDPVAQVFvhGDSLQACLVgVVVPD 603
Cdd:PRK08633 1043 RFAKIG-GEMVPLGAVE------EELAKAL--GGEEVVFAV-TAVPD 1079
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
122-575 |
1.46e-28 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 120.62 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 122 SYKEVADRAEFAGSALLHRGhSQSGDkyigIFAQNRPEW---TISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTI 198
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKG-IEPGD----RVAFQLPGWcefTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 199 ICDIADKAR----LILDCVSGRKHsVTTIVIMESFDSELTAqaqncgidiISLKELEAIGKAnHKTPIPPKPEDLALICF 274
Cdd:PRK06087 126 FAPTLFKQTrpvdLILPLQNQLPQ-LQQIVGVDKLAPATSS---------LSLSQIIADYEP-LTTAITTHGDELAAVLF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 275 TSGTTGNPKGAMLTHGNVVSNCSAFIKiteeSLKLCPQDVLISFLPLAHmfervVEGVLlcHGAKIGYFQGDIRLLMDDL 354
Cdd:PRK06087 195 TSGTEGLPKGVMLTHNNILASERAYCA----RLNLTWQDVFMMPAPLGH-----ATGFL--HGVTAPFLIGARSVLLDIF 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 355 KNLKPTifpvvpRLLNRmfDKI-FGQANTPLKRWLLDfATSRKEAELKSgvvrkdsmwdklifskvqaslggrVRLMITG 433
Cdd:PRK06087 264 TPDACL------ALLEQ--QRCtCMLGATPFIYDLLN-LLEKQPADLSA------------------------LRFFLCG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 434 AAPVsPTVLTflRAAL--GCQFYEGYGQTECTAGCTMSL--PGDWTAGHVGAPLPCNFVKLVDVAEmNYFAANGEGEVCV 509
Cdd:PRK06087 311 GTTI-PKKVA--RECQqrGIKLLSVYGSTESSPHAVVNLddPLSRFMHTDGYAAAGVEIKVVDEAR-KTLPPGCEGEEAS 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528467780 510 KGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENI 575
Cdd:PRK06087 387 RGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDI 451
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
121-604 |
1.56e-28 |
|
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: 118.98 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALlhRGHS-QSGDKYIGIFAqNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTII 199
Cdd:cd05972 1 WSFRELKRESAKAANVL--AKLGlRKGDRVAVLLP-RVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 200 CDiadkarlildcvsgrkhsvttivimesfdseltaqaqncgidiislkeleaigkanhktpippkPEDLALICFTSGTT 279
Cdd:cd05972 78 TD----------------------------------------------------------------AEDPALIYFTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 280 GNPKGAMLTHG---NVVSNCSAFIKITEESLKLCPQD------VLISFL-PLAHMFERVVegvllCHGAKIgyfqgDIRL 349
Cdd:cd05972 94 GLPKGVLHTHSyplGHIPTAAYWLGLRPDDIHWNIADpgwakgAWSSFFgPWLLGATVFV-----YEGPRF-----DAER 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 350 LMDDLKNLKPTIFPVVPrllnrmfdkifgqanTPLKRWLldfatsrkEAELKSGVvrkdsmwdkliFSkvqaslggRVRL 429
Cdd:cd05972 164 ILELLERYGVTSFCGPP---------------TAYRMLI--------KQDLSSYK-----------FS--------HLRL 201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 430 MITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDvAEMNYFAANGEGEVCV 509
Cdd:cd05972 202 VVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIID-DDGRELPPGEEGDIAI 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 510 KGPNV--FQGYLKDPEQTSgAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYIRSDPVAQVFV 587
Cdd:cd05972 281 KLPPPglFLGYVGDPEKTE-ASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVESALLEHPAVAEAAV 358
|
490
....*....|....*..
gi 528467780 588 hgdslqaclvgVVVPDP 604
Cdd:cd05972 359 -----------VGSPDP 364
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
264-604 |
4.66e-28 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 119.00 E-value: 4.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 264 PKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIkiteESLKLCPQDVLISFLPLAHMfervvEGVLlcHGAKIGYF 343
Cdd:PRK13295 194 PGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYA----ERLGLGADDVILMASPMAHQ-----TGFM--YGLMMPVM 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 344 QGDIRLLMDDLKNLkptifpvvprllnRMFDKI------FGQANTPlkrWLLDFATSRKEAelksgvvrkdsmwdklifS 417
Cdd:PRK13295 263 LGATAVLQDIWDPA-------------RAAELIrtegvtFTMASTP---FLTDLTRAVKES------------------G 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 418 KVQASLggrvRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAgCTMSLPGD---WTAGHVGAPLPCNFVKLVDvA 494
Cdd:PRK13295 309 RPVSSL----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA-VTLTKLDDpdeRASTTDGCPLPGVEVRVVD-A 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 495 EMNYFAANGEGEVCVKGPNVFQGYLKDPEQTsgAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIEN 574
Cdd:PRK13295 383 DGAPLPAGQIGRLQVRGCSNFGGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEA 459
|
330 340 350
....*....|....*....|....*....|...
gi 528467780 575 IYIRSDPVAQVFVHG---DSLQACLVGVVVPDP 604
Cdd:PRK13295 460 LLYRHPAIAQVAIVAypdERLGERACAFVVPRP 492
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
120-603 |
5.21e-28 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 118.16 E-value: 5.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 120 WLSYKEVADRAEFAGSALLHRGHSQsgDKYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTII 199
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGVGP--GDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 200 CDIADKARLILDCVsgrkhsvttivimesfdseltaqaqncgidiISLKELEAIGKANHKTPIPPKPEDLALICFTSGTT 279
Cdd:cd12116 90 TDDALPDRLPAGLP-------------------------------VLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 280 GNPKGAMLTHGNVVSncsaFIKITEESLKLCPQDVLISFLPLAhmFE-RVVEGVL-LCHGAKI----GYFQGDIRLLMDD 353
Cdd:cd12116 139 GRPKGVVVSHRNLVN----FLHSMRERLGLGPGDRLLAVTTYA--FDiSLLELLLpLLAGARVviapRETQRDPEALARL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 354 LKNLKPTIFpvvprllnrmfdkifgQAnTPlkrwlldfATSRkeaelksgvVRKDSMWDKLifskvqaslgGRVRLMITG 433
Cdd:cd12116 213 IEAHSITVM----------------QA-TP--------ATWR---------MLLDAGWQGR----------AGLTALCGG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 434 AApvSPTVLTFLRAALGCQFYEGYGQTECT--AGCTMSLPGDwTAGHVGAPLPCNFVKLVDVAeMNYFAANGEGEVCVKG 511
Cdd:cd12116 249 EA--LPPDLAARLLSRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLDAA-LRPVPPGVPGELYIGG 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 512 PNVFQGYLKDPEQTSGAV--DKAG-----WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDPVAQ 584
Cdd:cd12116 325 DGVAQGYLGRPALTAERFvpDPFAgpgsrLYRTGDLVRRRADGRLEYLGRADGQVKI-RGHRIELGEIEAALAAHPGVAQ 403
|
490 500
....*....|....*....|.
gi 528467780 585 --VFVHGDSLQACLVGVVVPD 603
Cdd:cd12116 404 aaVVVREDGGDRRLVAYVVLK 424
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
121-605 |
1.17e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 117.96 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGHSqSGDKYIgIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:PRK07786 43 TTWRELDDRVAALAGALSRRGVG-FGDRVL-ILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 D--IADKARLILDCVSGRKhsvTTIVIMESFDSeltaqaqncgiDIISLKELEAIGKANHktPIPPKPEDL-ALICFTSG 277
Cdd:PRK07786 121 EaaLAPVATAVRDIVPLLS---TVVVAGGSSDD-----------SVLGYEDLLAEAGPAH--APVDIPNDSpALIMYTSG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 278 TTGNPKGAMLTHGNVVSNCSAFIKITEESLklcPQDVLISFLPLAHM--FERVVEGVLLchGAKIgyfqgdirllmddlk 355
Cdd:PRK07786 185 TTGRPKGAVLTHANLTGQAMTCLRTNGADI---NSDVGFVGVPLFHIagIGSMLPGLLL--GAPT--------------- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 356 nlkpTIFPVvprllnRMFDKifGQantplkrwLLDFAtsrkEAELKSGVVRKDSMWDKLIFSKVQASLGGRVRLMITGAA 435
Cdd:PRK07786 245 ----VIYPL------GAFDP--GQ--------LLDVL----EAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 436 PVSPTVLTFLRAAL-GCQFYEGYGQTECTAGCTMSLPGDWTA--GHVGAPLPCNFVKLVDvAEMNYFAANGEGEVCVKGP 512
Cdd:PRK07786 301 PASDTLLRQMAATFpEAQILAAFGQTEMSPVTCMLLGEDAIRklGSVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 513 NVFQGYLKDPEQTSGAVDkAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVFVHG--- 589
Cdd:PRK07786 380 TLMSGYWNNPEATAEAFA-GGWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPDIVEVAVIGrad 457
|
490
....*....|....*.
gi 528467780 590 DSLQACLVGVVVPDPD 605
Cdd:PRK07786 458 EKWGEVPVAVAAVRND 473
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
261-577 |
1.43e-27 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 117.64 E-value: 1.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 261 PIPP-KPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKItEESLKLCP--QDVLISFLPLAHMF--ERVVEGVLLC 335
Cdd:PLN02574 191 PKPViKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRF-EASQYEYPgsDNVYLAALPMFHIYglSLFVVGLLSL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 336 HGAKIGYFQGDIRLLMDDLKNLKPTIFPVVPRLLNRMFDKIFGQANTPLKrwlldfatsrkeaelksgvvrkdsmwdkli 415
Cdd:PLN02574 270 GSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLK------------------------------ 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 416 fSKVQASlggrvrlmiTGAAPVS-PTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGH--VGAPLPCNFVKLVD 492
Cdd:PLN02574 320 -SLKQVS---------CGAAPLSgKFIQDFVQTLPHVDFIQGYGMTESTAVGTRGFNTEKLSKYssVGLLAPNMQAKVVD 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 493 VAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKI 572
Cdd:PLN02574 390 WSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQIAPADL 468
|
....*
gi 528467780 573 ENIYI 577
Cdd:PLN02574 469 EAVLI 473
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
121-604 |
1.52e-27 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 116.04 E-value: 1.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAE-FAGsaLLHRGHSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTII 199
Cdd:cd05935 2 LTYLELLEVVKkLAS--FLSNKGVRKGDR-VGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 200 CDiadkarlildcvsgrkhsvttivimesfdSELtaqaqncgidiislkeleaigkanhktpippkpEDLALICFTSGTT 279
Cdd:cd05935 79 VG-----------------------------SEL---------------------------------DDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 280 GNPKGAMLTHGNVVSNCSAFIKITeeslKLCPQDVLISFLPLAHM--FERVVEGVLLCHGAKIGYFQGDIRLLMDDLKNL 357
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQSAVWT----GLTPSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMARWDRETALELIEKY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 358 KPTIFPVVPRLLNrmfdkifgqantplkrwlldfatsrkeaELKSGVVRKDSMWDKLifskvqaslggrvRLMITGAAPV 437
Cdd:cd05935 173 KVTFWTNIPTMLV----------------------------DLLATPEFKTRDLSSL-------------KVLTGGGAPM 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 438 SPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDVAEMNYFAANGEGEVCVKGPNVFQG 517
Cdd:cd05935 212 PPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKG 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 518 YLKDPEQTSGA---VDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIyirsdpvaqVFVHGDSLQA 594
Cdd:cd05935 292 YWNRPEETEESfieIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAK---------LYKHPAI*EV 361
|
490
....*....|
gi 528467780 595 CLVGvvVPDP 604
Cdd:cd05935 362 CVIS--VPDE 369
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
119-589 |
2.63e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 116.22 E-value: 2.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 119 KWLSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTI 198
Cdd:PRK03640 26 KKVTFMELHEAVVSVAGKLAALG-VKKGDR-VALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 199 ICDiadkarlildcvsgrkhsvttivimESFDSELTAQAQncgidiISLKELEAiGKANHKTPIPPKPED-LALICFTSG 277
Cdd:PRK03640 104 ITD-------------------------DDFEAKLIPGIS------VKFAELMN-GPKEEAEIQEEFDLDeVATIMYTSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 278 TTGNPKGAMLTHGN----VVSncSAF-IKITEESLKLCPqdvlisfLPLAH------MFERVVEG---VLLCH--GAKIg 341
Cdd:PRK03640 152 TTGKPKGVIQTYGNhwwsAVG--SALnLGLTEDDCWLAA-------VPIFHisglsiLMRSVIYGmrvVLVEKfdAEKI- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 342 yfqgdIRLLMDDlknlKPTIFPVVPRLLNRMFDKIfGQANTPlkrwlldfatsrkeaelksgvvrkdsmwdklifskvqa 421
Cdd:PRK03640 222 -----NKLLQTG----GVTIISVVSTMLQRLLERL-GEGTYP-------------------------------------- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 422 slgGRVRLMITGAAPVSPTVLTFLRAAlGCQFYEGYGQTEcTAGCTMSLPGDWTA---GHVGAPL-PCNfVKLVDvaEMN 497
Cdd:PRK03640 254 ---SSFRCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLfPCE-LKIEK--DGV 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 498 YFAANGEGEVCVKGPNVFQGYLKDPEQTSgAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYI 577
Cdd:PRK03640 326 VVPPFEEGEIVVKGPNVTKGYLNREDATR-ETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLL 403
|
490
....*....|..
gi 528467780 578 RSDPVAQVFVHG 589
Cdd:PRK03640 404 SHPGVAEAGVVG 415
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
120-605 |
2.68e-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: 116.95 E-value: 2.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 120 WLSYKEVADRAEFAGSALLHRGhsQSGDkYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEA---ISYVIDKASIT 196
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAVG--KPGD-RVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 197 TIICDIADKARLILDCVSGRKHSVTTIVIMESFDSELTAQAQNCGIDiislkeleaigkanhktpippkPEDLALICFTS 276
Cdd:cd05931 101 VVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPD----------------------PDDIAYLQYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 277 GTTGNPKGAMLTHGNVVSNCSAFIKiteeSLKLCPQDVLISFLPLAH-MfervveGVLLCHGAKIgYFQGDIrLLMDdlk 355
Cdd:cd05931 159 GSTGTPKGVVVTHRNLLANVRQIRR----AYGLDPGDVVVSWLPLYHdM------GLIGGLLTPL-YSGGPS-VLMS--- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 356 nlkPTIFpvvprlLNRmfdkifgqantPLkRWL-----------------LDFATSRKEAELKSGVvrkDsmwdkLifsk 418
Cdd:cd05931 224 ---PAAF------LRR-----------PL-RWLrlisryratisaapnfaYDLCVRRVRDEDLEGL---D-----L---- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 419 vqaslgGRVRLMITGAAPVSPTVLT-FLRAALGCQF-----YEGYGQTECTAGCTMSLPG----------DWTAGHV--- 479
Cdd:cd05931 271 ------SSWRVALNGAEPVRPATLRrFAEAFAPFGFrpeafRPSYGLAEATLFVSGGPPGtgpvvlrvdrDALAGRAvav 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 480 -------------GAPLPCNFVKLVDVAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQT------SGAVDKAGWLHTGDI 540
Cdd:cd05931 345 aaddpaarelvscGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATaetfgaLAATDEGGWLRTGDL 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528467780 541 GkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSDPVAQVfvhgdslqACLVGVVVPDPD 605
Cdd:cd05931 425 G-FLHDGELYITGRLKDLIIVR-GRNHYPQDIEATAEEAHPALRP--------GCVAAFSVPDDG 479
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
263-556 |
2.87e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 117.36 E-value: 2.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 263 PPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNC---SAFIKITEESLKLCPqdvlisfLPLAHMFERVVEGVL-LCHGA 338
Cdd:PRK07529 209 PIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAwlgALLLGLGPGDTVFCG-------LPLFHVNALLVTGLApLARGA 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 339 KI------GYfQGDirLLMDDLKNL----KPTIFPVVPRLLNrmfdkifgqantplkrwlldfatsrkeaelksgvvrkd 408
Cdd:PRK07529 282 HVvlatpqGY-RGP--GVIANFWKIveryRINFLSGVPTVYA-------------------------------------- 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 409 smwdklifSKVQASLGGR----VRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLP-GDWTAGHVGAPL 483
Cdd:PRK07529 321 --------ALLQVPVDGHdissLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPdGERRIGSVGLRL 392
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528467780 484 PCNFVKLVDV-AEMNYF---AANGEGEVCVKGPNVFQGYLkDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKK 556
Cdd:PRK07529 393 PYQRVRVVILdDAGRYLrdcAVDEVGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAK 468
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
119-604 |
4.73e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 115.29 E-value: 4.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 119 KWlSYKEVaDRAEFAGSALLHRGHSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTI 198
Cdd:PRK09088 22 RW-TYAEL-DALVGRLAAVLRRRGCVDGER-LAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 199 ICDIADKArlildcvsGRkhsvttiVIMESFDSeLTAQAqncgidiislkelEAIGKANhKTPIPPkpEDLALICFTSGT 278
Cdd:PRK09088 99 LGDDAVAA--------GR-------TDVEDLAA-FIASA-------------DALEPAD-TPSIPP--ERVSLILFTSGT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 279 TGNPKGAMLTHGN---VVSNCSAFIKITEESLKLCPQdvlisflPLAHMFERV--VEGVLLcHGAKIGYFQGdirllmdd 353
Cdd:PRK09088 147 SGQPKGVMLSERNlqqTAHNFGVLGRVDAHSSFLCDA-------PMFHIIGLItsVRPVLA-VGGSILVSNG-------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 354 lknLKPTifpvvpRLLNRMFDKIFGQANTplkrwlldFATSRKEAELksgvvRKDSMWDklifskvqASLGGRVRLMITG 433
Cdd:PRK09088 211 ---FEPK------RTLGRLGDPALGITHY--------FCVPQMAQAF-----RAQPGFD--------AAALRHLTALFTG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 434 AAP-VSPTVLTFLraALGCQFYEGYGQTEctAGCTMSLPGDWT-----AGHVGAPLPCNFVKLVDvAEMNYFAANGEGEV 507
Cdd:PRK09088 261 GAPhAAEDILGWL--DDGIPMVDGFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVVD-DQGNDCPAGVPGEL 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 508 CVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIEniyirsdpvAQVFV 587
Cdd:PRK09088 336 LLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIE---------AVLAD 405
|
490
....*....|....*..
gi 528467780 588 HGDSLQACLVGvvVPDP 604
Cdd:PRK09088 406 HPGIRECAVVG--MADA 420
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
258-605 |
1.29e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 113.93 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 258 HKTPIPPkPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFikitEESLKLCPQDVLISFLPLAHMfervvegvllcHG 337
Cdd:PRK07787 120 HRYPEPD-PDAPALIVYTSGTTGPPKGVVLSRRAIAADLDAL----AEAWQWTADDVLVHGLPLFHV-----------HG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 338 akigyfqgdirLLMDDLKNLkptifpvvpRLLNRMfdkifgqantplkRWLLDFATSRKEAELKS------GVvrkDSMW 411
Cdd:PRK07787 184 -----------LVLGVLGPL---------RIGNRF-------------VHTGRPTPEAYAQALSEggtlyfGV---PTVW 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 412 DKLIFSKVQASLGGRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLV 491
Cdd:PRK07787 228 SRIAADPEAARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLV 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 492 DVaEMNYFAANGE--GEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDR------KKHIFKLAQ 563
Cdd:PRK07787 308 DE-DGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGGYRIGA 386
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 528467780 564 GEyiapekIENIYIRSDPVAQVFVHG---DSLQACLVGVVVPDPD 605
Cdd:PRK07787 387 GE------IETALLGHPGVREAAVVGvpdDDLGQRIVAYVVGADD 425
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
121-604 |
1.74e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 113.87 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:PRK08316 37 WTYAELDAAVNRVAAALLDLG-LKKGDR-VAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 DIADKARLilDCVSGRKHSVTTIVIMESFDSELTAqaqncgidiiSLKELEAIGKANHKTPIPPKP--EDLALICFTSGT 278
Cdd:PRK08316 115 DPALAPTA--EAALALLPVDTLILSLVLGGREAPG----------GWLDFADWAEAGSVAEPDVELadDDLAQILYTSGT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 279 TGNPKGAMLTHGNVVSN-CSAFIkiteeSLKLCPQDVLISFLPLAHMFER-VVEGVLLCHGAKIGYFQG-DIRLLMDDLK 355
Cdd:PRK08316 183 ESLPKGAMLTHRALIAEyVSCIV-----AGDMSADDIPLHALPLYHCAQLdVFLGPYLYVGATNVILDApDPELILRTIE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 356 NLKPTIF---PVVprllnrmfdkIFGQANTPlkrwllDFATsrkeAELKSgvVRKDSMwdklifskvqaslggrvrlmit 432
Cdd:PRK08316 258 AERITSFfapPTV----------WISLLRHP------DFDT----RDLSS--LRKGYY---------------------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 433 GAAPVSPTVLTFLRAAL-GCQFYEGYGQTECTAGCTMSLPGDwTAGHVG-APLPCNFV--KLVDvAEMNYFAANGEGEVC 508
Cdd:PRK08316 294 GASIMPVEVLKELRERLpGLRFYNCYGQTEIAPLATVLGPEE-HLRRPGsAGRPVLNVetRVVD-DDGNDVAPGEVGEIV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 509 VKGPNVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSDPVAQVFVH 588
Cdd:PRK08316 372 HRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEALYTHPAVAEVAVI 449
|
490
....*....|....*.
gi 528467780 589 GdslqaclvgvvVPDP 604
Cdd:PRK08316 450 G-----------LPDP 454
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
121-608 |
1.35e-25 |
|
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: 113.41 E-value: 1.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAE-FAGsALLHRGHsQSGDKyIGIFAQNRPEWTISELA------CYtyslvaVPLYDTLGTEAISYVIDKA 193
Cdd:COG1020 502 LTYAELNARANrLAH-HLRALGV-GPGDL-VGVCLERSLEMVVALLAvlkagaAY------VPLDPAYPAERLAYMLEDA 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 194 sittiicdiadKARLILDcvsgrkhsvttivimesfDSELTAQAQNCGIDIISLKELEAIGKANHKTPIPPKPEDLALIC 273
Cdd:COG1020 573 -----------GARLVLT------------------QSALAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLAYVI 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 274 FTSGTTGNPKGAMLTHGNVVSNCSAFIkiteESLKLCPQDVLISFLPLAH------MFervvegVLLCHGAKIGYFQGDI 347
Cdd:COG1020 624 YTSGSTGRPKGVMVEHRALVNLLAWMQ----RRYGLGPGDRVLQFASLSFdasvweIF------GALLSGATLVLAPPEA 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 348 RLLMDDLKNL----KPTIFPVVPrllnrmfdkifgqantplkrwlldfatsrkeaelksgvvrkdSMWDKLIfsKVQASL 423
Cdd:COG1020 694 RRDPAALAELlarhRVTVLNLTP------------------------------------------SLLRALL--DAAPEA 729
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 424 GGRVRLMITGAAPVSPTVLTFLRAAL-GCQFYEGYGQTECTAGCTMSL--PGDWTAGHV--GAPLPCNFVKLVDvaemny 498
Cdd:COG1020 730 LPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTVDSTYYEvtPPDADGGSVpiGRPIANTRVYVLD------ 803
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 499 faANGE-------GEVCVKGPNVFQGYLKDPEQTSGA-----VDKAG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQG 564
Cdd:COG1020 804 --AHLQpvpvgvpGELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNLEFLGRADDQVKI-RG 880
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 528467780 565 EYIAPEKIENIyIRSDP-VAQ--VFVHGDSLQA-CLVGVVVPDPDFLP 608
Cdd:COG1020 881 FRIELGEIEAA-LLQHPgVREavVVAREDAPGDkRLVAYVVPEAGAAA 927
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
87-692 |
2.31e-25 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 112.64 E-value: 2.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 87 KDALTLYEFFLRGLRVSNNGPCLGSRK-AGQPyKWLSYKEVADRAEFAGSALLHRGhSQSGDkYIGIFAQNRPEWTISEL 165
Cdd:PTZ00297 424 AGVRSLGEMWERSVTRHSTFRCLGQTSeSGES-EWLTYGTVDARARELGSGLLALG-VRPGD-VIGVDCEASRNIVILEV 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 166 ACYTYSLVAVPLYDTLGTeaISYVIDKASITTIICDIADKArLILDCvsgRKHSVTTIVIMESF-DSELTAQAQNCGIDI 244
Cdd:PTZ00297 501 ACALYGFTTLPLVGKGST--MRTLIDEHKIKVVFADRNSVA-AILTC---RSRKLETVVYTHSFyDEDDHAVARDLNITL 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 245 ISLKELEAIGKAnhkTPIPPKPEDLALICFT-------SGTTGNPKGAMLTHGNVVSNCSAFI--KITEESLKlcpQDVL 315
Cdd:PTZ00297 575 IPYEFVEQKGRL---CPVPLKEHVTTDTVFTyvvdnttSASGDGLAVVRVTHADVLRDISTLVmtGVLPSSFK---KHLM 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 316 ISFLPLAHMFERVVEGVLLCHGAKIGyfQGDIRLLMDDLKNLKPTIFPVVPRLlnrmfdkiFGQANTPLKR--------- 386
Cdd:PTZ00297 649 VHFTPFAMLFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSL--------FSTSRLQLSRanerysavy 718
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 387 -WLLDfatsrKEAELKSGVV---RKDSMWDKLIFSK-VQASLGGRVRLMITGAAPVSPTvltflraalgcqfyegYGQTE 461
Cdd:PTZ00297 719 sWLFE-----RAFQLRSRLInihRRDSSLLRFIFFRaTQELLGGCVEKIVLCVSEESTS----------------FSLLE 777
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 462 CTAGCTMslpgdwtaghvgaplPCnfvklvdVAEMNYFaaNGEGEVCVKG---PNVfQGYLKDPEQTSGAVdKAGWL--- 535
Cdd:PTZ00297 778 HISVCYV---------------PC-------LREVFFL--PSEGVFCVDGtpaPSL-QVDLEPFDEPSDGA-GIGQLvla 831
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 536 ------HTGDI-GKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSDPVAQVFVHGDSLQAcLVGVVVPDPDFLP 608
Cdd:PTZ00297 832 kkgeprRTLPIaAQWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVE 910
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 609 -GWAKNRGIEG--------SFNDLckSKEVKNAILEDMIQLGKEAGLKSFEQVRDIALHLEMFSVQNGLLTPTLKAKRTE 679
Cdd:PTZ00297 911 fEWRQSHCMGEgggparqlGWTEL--VAYASSLLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDA 988
|
650
....*....|...
gi 528467780 680 LKSRFREQIDQLY 692
Cdd:PTZ00297 989 VHSYFSSVIERFY 1001
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
107-694 |
3.38e-25 |
|
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: 110.60 E-value: 3.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 107 PCLGSRKAGQPYKWLSYKEVADRAEFAGSALLHRGhsQSGDKYIGIFAQNRPEWTISELACYTYSLVAVPL---YDTLGT 183
Cdd:cd05921 12 TWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLG--LSAERPLLILSGNSIEHALMALAAMYAGVPAAPVspaYSLMSQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 184 E--AISYVIDKASITTIICDIADKARLILDCVsgrKHSVTTIVIMesfdseltaQAQNCGIDIISLKEL---EAIGKANH 258
Cdd:cd05921 90 DlaKLKHLFELLKPGLVFAQDAAPFARALAAI---FPLGTPLVVS---------RNAVAGRGAISFAELaatPPTAAVDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 259 KTPiPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSA----FIKITEESLklcpqdVLISFLPLAHMF-ERVVEGVL 333
Cdd:cd05921 158 AFA-AVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMleqtYPFFGEEPP------VLVDWLPWNHTFgGNHNFNLV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 334 LCHGAKI---------GYFQGDIRllmdDLKNLKPTIFPVVPrllnrmfdkifgqantplKRWlldfatsrkeaELKSGV 404
Cdd:cd05921 231 LYNGGTLyiddgkpmpGGFEETLR----NLREISPTVYFNVP------------------AGW-----------EMLVAA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 405 VRKDSMWDKLIFSkvqaslggRVRLMITGAAPVSPTVLTFLRAaLGCQ-------FYEGYGQTECTAGCTMSLPGDWTAG 477
Cdd:cd05921 278 LEKDEALRRRFFK--------RLKLMFYAGAGLSQDVWDRLQA-LAVAtvgeripMMAGLGATETAPTATFTHWPTERSG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 478 HVGAPLPCNFVKLVdvaemnyfAANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWL----PNGTLKIID 553
Cdd:cd05921 349 LIGLPAPGTELKLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpddPAKGLVFDG 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 554 RKKHIFKLAQGEYIA--PEKIENIYIRSDPVAQVFVHGDSlQACLVGVVVPDPDFLPgwAKNRGIEGSFNDLCKSKEVKN 631
Cdd:cd05921 421 RVAEDFKLASGTWVSvgPLRARAVAACAPLVHDAVVAGED-RAEVGALVFPDLLACR--RLVGLQEASDAEVLRHAKVRA 497
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528467780 632 AILEDMIQLGKEAGLKSFEQVRdIALHLEMFSVQNGLLTPTLKAKRTELKSRFREQIDQLYAK 694
Cdd:cd05921 498 AFRDRLAALNGEATGSSSRIAR-ALLLDEPPSIDKGEITDKGYINQRAVLERRAALVERLYAD 559
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
121-604 |
4.41e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 110.05 E-value: 4.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAE-FAGSaLLHRGHSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTII 199
Cdd:PRK08314 36 ISYRELLEEAErLAGY-LQQECGVRKGDR-VLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 200 C--DIADK----------ARLILDCVSGRKHSVTTIVIMESFDSELTAQAQNcGIDIISLKEleAIgkANHKTPIP--PK 265
Cdd:PRK08314 114 VgsELAPKvapavgnlrlRHVIVAQYSDYLPAEPEIAVPAWLRAEPPLQALA-PGGVVAWKE--AL--AAGLAPPPhtAG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 266 PEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITeeslKLCPQDVLISFLPLAHmfervVEGVLLCHGAKIgyFQG 345
Cdd:PRK08314 189 PDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWS----NSTPESVVLAVLPLFH-----VTGMVHSMNAPI--YAG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 346 DIRLLMddlknlkptifP-----VVPRLLNRMfdKIFGQANTPlkRWLLDFATSRK--EAELKSgvvrkdsmwdklifsk 418
Cdd:PRK08314 258 ATVVLM-----------PrwdreAAARLIERY--RVTHWTNIP--TMVVDFLASPGlaERDLSS---------------- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 419 vQASLGGrvrlmitGAAPVSPTVLTFLRAALGCQFYEGYGQTEcTAGCTMSLPGDWTA-GHVGAPLPCNFVKLVDVAEMN 497
Cdd:PRK08314 307 -LRYIGG-------GGAAMPEAVAERLKELTGLDYVEGYGLTE-TMAQTHSNPPDRPKlQCLGIPTFGVDARVIDPETLE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 498 YFAANGEGEVCVKGPNVFQGYLKDPEQTSGA---VDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIEN 574
Cdd:PRK08314 378 ELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMIN-ASGFKVWPAEVEN 456
|
490 500 510
....*....|....*....|....*....|
gi 528467780 575 IyirsdpvaqVFVHGDSLQACLVGvvVPDP 604
Cdd:PRK08314 457 L---------LYKHPAIQEACVIA--TPDP 475
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
112-543 |
1.38e-24 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 108.81 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 112 RKAGQPYKWLSYKEVADRAEFAGSALLHRGHSQsgDKYIGIFAQNRPEWTISELACYT-----------YSLVAVPL--- 177
Cdd:PRK08180 61 RGADGGWRRLTYAEALERVRAIAQALLDRGLSA--ERPLMILSGNSIEHALLALAAMYagvpyapvspaYSLVSQDFgkl 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 178 ---YDTLgTEAISYVIDKASITTIIcDIADKARLILDCVSGRKHSVTTIvimeSFDSELTAQaqncgidiislkELEAIG 254
Cdd:PRK08180 139 rhvLELL-TPGLVFADDGAAFARAL-AAVVPADVEVVAVRGAVPGRAAT----PFAALLATP------------PTAAVD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 255 KANHKTpippKPEDLALICFTSGTTGNPKGAMLTHGNVVSN------CSAFikiteesLKLCPQdVLISFLPLAHMFERV 328
Cdd:PRK08180 201 AAHAAV----GPDTIAKFLFTSGSTGLPKAVINTHRMLCANqqmlaqTFPF-------LAEEPP-VLVDWLPWNHTFGGN 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 329 VE-GVLLCHGAKigyfqgdirLLMDD-----------LKNLK---PTIFPVVPR----LLNRMfdkifgqantplkrwll 389
Cdd:PRK08180 269 HNlGIVLYNGGT---------LYIDDgkptpggfdetLRNLReisPTVYFNVPKgwemLVPAL----------------- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 390 dfatsRKEAELKsgvvrkdsmwdklifskvqASLGGRVRLMITGAAPVSPTVLTFL----RAALGCQ--FYEGYGQTEcT 463
Cdd:PRK08180 323 -----ERDAALR-------------------RRFFSRLKLLFYAGAALSQDVWDRLdrvaEATCGERirMMTGLGMTE-T 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 464 AGCTMSL--PGDwTAGHVGAPLPCNFVKLVDVaemnyfaaNGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIG 541
Cdd:PRK08180 378 APSATFTtgPLS-RAGNIGLPAPGCEVKLVPV--------GGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAV 448
|
..
gi 528467780 542 KW 543
Cdd:PRK08180 449 RF 450
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
268-606 |
4.86e-24 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 103.89 E-value: 4.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 268 DLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIkiteESLKLCPQDVLISFLPLAHmfervVEGV-----LLCHGAK--- 339
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLI----HAMGLTEADVYLNMLPLFH-----IAGLnlalaTFHAGGAnvv 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 340 IGYFqgDIRLLMDDLKNLKPTIFPVVPRLLNRMFDKIFgqantplkrwlldfATSRKEAELKsGVVRKDSmwdklifskv 419
Cdd:cd17637 72 MEKF--DPAEALELIEEEKVTLMGSFPPILSNLLDAAE--------------KSGVDLSSLR-HVLGLDA---------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 420 qaslggrvrlmitgaapvsPTVLTFLRAALGCQFYEGYGQTECTAGCTMSlPGDWTAGHVGAPLPCNFVKLVDvaEMNYF 499
Cdd:cd17637 125 -------------------PETIQRFEETTGATFWSLYGQTETSGLVTLS-PYRERPGSAGRPGPLVRVRIVD--DNDRP 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 500 AANGE-GEVCVKGPNVFQGYLKDPEQTSGAVDKaGWLHTGDIGKWLPNGTLKIIDRK--KHIFKlAQGEYIAPEKIENIY 576
Cdd:cd17637 183 VPAGEtGEIVVRGPLVFQGYWNLPELTAYTFRN-GWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKVI 260
|
330 340 350
....*....|....*....|....*....|
gi 528467780 577 IRSDPVAQVFVHGdslqaclvgvvVPDPDF 606
Cdd:cd17637 261 LEHPAIAEVCVIG-----------VPDPKW 279
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
268-604 |
2.64e-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: 101.25 E-value: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 268 DLALICFTSGTTGNPKGAMLTHGNVVSNCSAfikiTEESLKLCPQDVLISFLPLAHM--FERVVEGVLLchGAKIgYFQG 345
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAG----LHSRLGFGGGDSWLLSLPLYHVggLAILVRSLLA--GAEL-VLLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 346 DIRLLMDDLKNLKPTIFPVVPRLLNRMFDKifGQANTPLKRwlldfatsrkeaelksgvvrkdsmwdklifskvqaslgg 425
Cdd:cd17630 74 RNQALAEDLAPPGVTHVSLVPTQLQRLLDS--GQGPAALKS--------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 426 rVRLMITGAAPVsPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDvaemnyfaangEG 505
Cdd:cd17630 113 -LRAVLLGGAPI-PPELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVE-----------DG 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 506 EVCVKGPNVFQGYLKDPEQtsGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQV 585
Cdd:cd17630 180 EIWVGGASLAMGYLRGQLV--PEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAVRDA 256
|
330 340
....*....|....*....|..
gi 528467780 586 FVHG---DSLQACLVGVVVPDP 604
Cdd:cd17630 257 FVVGvpdEELGQRPVAVIVGRG 278
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
266-589 |
5.96e-23 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 101.02 E-value: 5.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 266 PEDLALICFTSGTTGNPKGAMLTHGNVVSNCsafiKITEESLKLCPQDVLISFLPLAHMFERVVEGVLLCH-GAKIgyfq 344
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNA----WMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLAsGAHV---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 345 gdirLLMDDLKNLKPTIFPVVPRLLNRMfdkifgqantplkrwlldfatsrkEAELKSGVvrkDSMWDKLIFSKVQASLG 424
Cdd:cd05944 73 ----VLAGPAGYRNPGLFDNFWKLVERY------------------------RITSLSTV---PTVYAALLQVPVNADIS 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 425 GrVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLP-GDWTAGHVGAPLPCNFVKLVDV-AEMNYF--A 500
Cdd:cd05944 122 S-LRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKVLdGVGRLLrdC 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 501 ANGE-GEVCVKGPNVFQGYLKDpEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRS 579
Cdd:cd05944 201 APDEvGEICVAGPGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLRH 278
|
330
....*....|
gi 528467780 580 DPVAQVFVHG 589
Cdd:cd05944 279 PAVAFAGAVG 288
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
121-604 |
1.34e-22 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 101.17 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEfAGSALLHRGHSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:cd05945 17 LTYRELKERAD-ALAAALASLGLDAGDP-VVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPALLIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 DiadkarlildcvsgrkhsvttivimesfdseltaqaqncgidiislkeleaigkanhktpippkPEDLALICFTSGTTG 280
Cdd:cd05945 95 D----------------------------------------------------------------GDDNAYIIFTSGSTG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 281 NPKGAMLTHGNVVSncsaFIKITEESLKLCPQDVLISFLPLAhmFERVVEGVL--LCHGAkigyfqgdirllmddlknlk 358
Cdd:cd05945 111 RPKGVQISHDNLVS----FTNWMLSDFPLGPGDVFLNQAPFS--FDLSVMDLYpaLASGA-------------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 359 pTIFPVvPRLLnrmfdkifgqantplKRWLLDFATSRKEAELkSGVVRKDSMWDKLIFSK--VQASLGGRVRLMITGAAP 436
Cdd:cd05945 165 -TLVPV-PRDA---------------TADPKQLFRFLAEHGI-TVWVSTPSFAAMCLLSPtfTPESLPSLRHFLFCGEVL 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 437 VSPTVLTFLRAALGCQFYEGYGQTECTAGCTM------------SLPgdwtaghVGAPLPCNFVKLVDvAEMNYFAANGE 504
Cdd:cd05945 227 PHKTARALQQRFPDARIYNTYGPTEATVAVTYievtpevldgydRLP-------IGYAKPGAKLVILD-EDGRPVPPGEK 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 505 GEVCVKGPNVFQGYLKDPEQTSGA---VDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDP 581
Cdd:cd05945 299 GELVISGPSVSKGYLNNPEKTAAAffpDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIELEEIEAALRQVPG 377
|
490 500
....*....|....*....|....*..
gi 528467780 582 VAQVFV----HGDSLQAcLVGVVVPDP 604
Cdd:cd05945 378 VKEAVVvpkyKGEKVTE-LIAFVVPKP 403
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
120-604 |
2.49e-22 |
|
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: 100.84 E-value: 2.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 120 WLSYKEVADRAEFAGSALLHRGHSqSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTII 199
Cdd:cd12118 29 RYTWRQTYDRCRRLASALAALGIS-RGDT-VAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 200 CDiadkarlildcvsgrkhsvttivimESFDSEltaqaqncgidiislkELEAIGKANHKtPIPPKPE-DLALICFTSGT 278
Cdd:cd12118 107 VD-------------------------REFEYE----------------DLLAEGDPDFE-WIPPADEwDPIALNYTSGT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 279 TGNPKGAMLTHGNVVSNcsAFIKITEESLKLCPqdVLISFLPLAH---------MFerVVEGVLLCHgAKIgyfqgDIRL 349
Cdd:cd12118 145 TGRPKGVVYHHRGAYLN--ALANILEWEMKQHP--VYLWTLPMFHcngwcfpwtVA--AVGGTNVCL-RKV-----DAKA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 350 LMDDLKNLKPTIFPVVPRLLNRMfdkifgqANTPlkrwlldfatsrkeaelksgvvrkdsmwdklifSKVQASLGGRVRL 429
Cdd:cd12118 213 IYDLIEKHKVTHFCGAPTVLNML-------ANAP---------------------------------PSDARPLPHRVHV 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 430 MITGAAPvsPTVLTFLRAALGCQFYEGYGQTEcTAG----CTM-----SLPGDWTA--------GHVGAplpcNFVKLVD 492
Cdd:cd12118 253 MTAGAPP--PAAVLAKMEELGFDVTHVYGLTE-TYGpatvCAWkpewdELPTEERArlkarqgvRYVGL----EEVDVLD 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 493 VAEMNYFAANGE--GEVCVKGPNVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPE 570
Cdd:cd12118 326 PETMKPVPRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENISSV 403
|
490 500 510
....*....|....*....|....*....|....
gi 528467780 571 KIENIyirsdpvaqVFVHGDSLQACLVGvvVPDP 604
Cdd:cd12118 404 EVEGV---------LYKHPAVLEAAVVA--RPDE 426
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
121-587 |
3.80e-22 |
|
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: 99.84 E-value: 3.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALlhRGHSQSGDKYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIdkasittiic 200
Cdd:cd05919 11 VTYGQLHDGANRLGSAL--RNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIA---------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 diadkarlildcvsgrKHSVTTIVIMESfdseltaqaqncgidiislkeleaigkanhktpippkpEDLALICFTSGTTG 280
Cdd:cd05919 79 ----------------RDCEARLVVTSA--------------------------------------DDIAYLLYSSGTTG 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 281 NPKGAMLTHGNVVSNCSAFIKiteESLKLCPQDVLISflpLAHMFErvveGVLLCHGAKIGYFQGDIRLLMDD------- 353
Cdd:cd05919 105 PPKGVMHAHRDPLLFADAMAR---EALGLTPGDRVFS---SAKMFF----GYGLGNSLWFPLAVGASAVLNPGwptaerv 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 354 ---LKNLKPTIFPVVPRLLNRMfdkifgqantplkrwlldfatsrkeaeLKSGVVRKDSMWDklifskvqaslggrVRLM 430
Cdd:cd05919 175 latLARFRPTVLYGVPTFYANL---------------------------LDSCAGSPDALRS--------------LRLC 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 431 ITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDvAEMNYFAANGEGEVCVK 510
Cdd:cd05919 214 VSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD-EEGHTIPPGEEGDLLVR 292
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528467780 511 GPNVFQGYLKDPEqTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSDPVAQVFV 587
Cdd:cd05919 293 GPSAAVGYWNNPE-KSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVESLIIQHPAVAEAAV 367
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
233-606 |
6.07e-22 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 99.71 E-value: 6.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 233 LTAQAQNCGIDIISLKELEAIGKANHKT----PIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFikitEESLK 308
Cdd:cd17655 99 LTQSHLQPPIAFIGLIDLLDEDTIYHEEsenlEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWA----NKVIY 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 309 LCPQDVLISFLPLAhmFERVVEGV---LLCHGAKIGYFQ---GDIRLLMDDLKNLKPTIFPVVPRLLNrmfdkifgqant 382
Cdd:cd17655 175 QGEHLRVALFASIS--FDASVTEIfasLLSGNTLYIVRKetvLDGQALTQYIRQNRITIIDLTPAHLK------------ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 383 plkrwLLDfatsrkeaelksgvvrkdsmwdklifsKVQASLGGRVRLMITGAAPVSPTVLTFL--RAALGCQFYEGYGQT 460
Cdd:cd17655 241 -----LLD---------------------------AADDSEGLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPT 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 461 ECTAGCTMSL--PGDWTAGHV--GAPLPCNFVKLVDvAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGA-VDK---- 531
Cdd:cd17655 289 ETTVDASIYQyePETDQQVSVpiGKPLGNTRIYILD-QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKfVDDpfvp 367
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528467780 532 AGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDPVAQ--VFVHGD-SLQACLVGVVVPDPDF 606
Cdd:cd17655 368 GERMYrTGDLARWLPDGNIEFLGRIDHQVKI-RGYRIELGEIEARLLQHPDIKEavVIARKDeQGQNYLCAYIVSEKEL 445
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
258-584 |
7.95e-22 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 100.55 E-value: 7.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 258 HKTPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEeslkLCPQDVLISFLPLAHMFERVVeGVL--LC 335
Cdd:PRK08043 356 RLAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIAD----FTPNDRFMSALPLFHSFGLTV-GLFtpLL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 336 HGAKIGYFQgdirllmddlknlKPTIFPVVPRLL-NRMFDKIFGQAnTPLKRWL-----LDFAtsrkeaelksgvvrkds 409
Cdd:PRK08043 431 TGAEVFLYP-------------SPLHYRIVPELVyDRNCTVLFGTS-TFLGNYArfanpYDFA----------------- 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 410 mwdklifskvqaslggRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVK 489
Cdd:PRK08043 480 ----------------RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDAR 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 490 LVDVAEMnyfaANGeGEVCVKGPNVFQGYLK--DP--------EQTSGAVDkAGWLHTGDIGKWLPNGTLKIIDRKKHIF 559
Cdd:PRK08043 544 LLSVPGI----EQG-GRLQLKGPNIMNGYLRveKPgvlevptaENARGEME-RGWYDTGDIVRFDEQGFVQIQGRAKRFA 617
|
330 340
....*....|....*....|....*
gi 528467780 560 KLAqGEYIAPEKIENIYIRSDPVAQ 584
Cdd:PRK08043 618 KIA-GEMVSLEMVEQLALGVSPDKQ 641
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
115-604 |
1.37e-21 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 98.27 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 115 GQPYKWlSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKAS 194
Cdd:cd05971 2 GTPEKV-TFKELKTASNRFANVLKEIG-LEKGDR-VGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 195 ITTIICDIADkarlildcvsgrkhsvttivimesfdseltaqaqncgidiislkeleaigkanhktpippkpeDLALICF 274
Cdd:cd05971 79 ASALVTDGSD---------------------------------------------------------------DPALIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 275 TSGTTGNPKGAMLTHGNVVSNcsafIKITEESLKLCPQ------------------DVLISFL----P-LAHMFERVveg 331
Cdd:cd05971 96 TSGTTGPPKGALHAHRVLLGH----LPGVQFPFNLFPRdgdlywtpadwawiggllDVLLPSLyfgvPvLAHRMTKF--- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 332 vllchgakigyfqgDIRLLMDDLKNLKPTIFPVVPRLLnrmfdKIFGQANTPLKRWLLdfatsrkeaelksgvvrkdsmw 411
Cdd:cd05971 169 --------------DPKAALDLMSRYGVTTAFLPPTAL-----KMMRQQGEQLKHAQV---------------------- 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 412 dklifskvqaslggRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTEC---TAGCTMSLPGDwtAGHVGAPLPCNFV 488
Cdd:cd05971 208 --------------KLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECnlvIGNCSALFPIK--PGSMGKPIPGHRV 271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 489 KLVDvAEMNYFAANGEGEVCVKGPN--VFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEY 566
Cdd:cd05971 272 AIVD-DNGTPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKM-AGDWLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYR 348
|
490 500 510
....*....|....*....|....*....|....*...
gi 528467780 567 IAPEKIENIYIRsdpvaqvfvHGDSLQACLVGvvVPDP 604
Cdd:cd05971 349 IGPAEIEECLLK---------HPAVLMAAVVG--IPDP 375
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
121-604 |
2.14e-21 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 99.65 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGHsqsGDKYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:PRK06814 659 LTYRKLLTGAFVLGRKLKKNTP---PGENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 DIA--DKARLildcvsgrkhsvttivimesfdSELTAQAQNcGIDIISLKELEA-----------IGKANHKTPIP-PKP 266
Cdd:PRK06814 736 SRAfiEKARL----------------------GPLIEALEF-GIRIIYLEDVRAqigladkikglLAGRFPLVYFCnRDP 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 267 EDLALICFTSGTTGNPKGAMLTHGNVVSNC---SAFIKITeeslklcPQDVLISFLPLAHMFervvegvllchgakiGYF 343
Cdd:PRK06814 793 DDPAVILFTSGSEGTPKGVVLSHRNLLANRaqvAARIDFS-------PEDKVFNALPVFHSF---------------GLT 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 344 QGdirLLMDDLKNLKPTIFP------VVPRLlnrmfdkIFGQANTPLkrwlldFATSrkeaELKSGVVRKDSMWDkliFs 417
Cdd:PRK06814 851 GG---LVLPLLSGVKVFLYPsplhyrIIPEL-------IYDTNATIL------FGTD----TFLNGYARYAHPYD---F- 906
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 418 kvqASLggrvRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDVAEMN 497
Cdd:PRK06814 907 ---RSL----RYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGID 979
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 498 yfaaNGeGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYI 577
Cdd:PRK06814 980 ----EG-GRLFVRGPNVMLGYLRAENPGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAVEELAA 1053
|
490 500
....*....|....*....|....*..
gi 528467780 578 RSDPvaqvfvhgDSLQAClvgVVVPDP 604
Cdd:PRK06814 1054 ELWP--------DALHAA---VSIPDA 1069
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
121-605 |
2.24e-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: 98.04 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELA------CYtyslvaVPLYDTLGTEAISYVIDKAs 194
Cdd:cd12117 23 LTYAELNERANRLARRLRAAG-VGPGDV-VGVLAERSPELVVALLAvlkagaAY------VPLDPELPAERLAFMLADA- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 195 ittiicdiadKARLILDcvsgrkhsvttivimesfDSELTAQAQNCGIDIISLKELEAIGKANHKTPIppKPEDLALICF 274
Cdd:cd12117 94 ----------GAKVLLT------------------DRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPV--SPDDLAYVMY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 275 TSGTTGNPKGAMLTHGNVVSNC--SAFIKITeeslklcPQDVLISFLPL---AHMFErvVEGVLLcHGAkigyfqgdiRL 349
Cdd:cd12117 144 TSGSTGRPKGVAVTHRGVVRLVknTNYVTLG-------PDDRVLQTSPLafdASTFE--IWGALL-NGA---------RL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 350 LMDDlknlkptifPVVPRLLNRMFDKIFGQANTPLkrWLldfatsrkEAELKSGVVRKDSmwdklifskvqASLGGrVRL 429
Cdd:cd12117 205 VLAP---------KGTLLDPDALGALIAEEGVTVL--WL--------TAALFNQLADEDP-----------ECFAG-LRE 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 430 MITGAAPVSPT-VLTFLRAALGCQFYEGYGQTECT--AGCTMSLPGDWTAGHV--GAPLPCNFVKLVDVAEMnyFAANGE 504
Cdd:cd12117 254 LLTGGEVVSPPhVRRVLAACPGLRLVNGYGPTENTtfTTSHVVTELDEVAGSIpiGRPIANTRVYVLDEDGR--PVPPGV 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 505 -GEVCVKGPNVFQGYLKDPEQTSGAVDKAGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYI 577
Cdd:cd12117 332 pGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI-RGFRIELGEIEAALR 410
|
490 500 510
....*....|....*....|....*....|.
gi 528467780 578 RSDPVAQVFV---HGDSLQACLVGVVVPDPD 605
Cdd:cd12117 411 AHPGVREAVVvvrEDAGGDKRLVAYVVAEGA 441
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
121-597 |
3.79e-21 |
|
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: 97.19 E-value: 3.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITT-II 199
Cdd:cd05923 29 LTYSELRARIEAVAARLHARG-LRPGQR-VAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAaVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 200 CDIADKARLILDCVsGRkhsvttiVIMESfdseltaqaqncgiDIISLKELEAIGKAnhKTPIPPKPEDLALICFTSGTT 279
Cdd:cd05923 107 AVDAQVMDAIFQSG-VR-------VLALS--------------DLVGLGEPESAGPL--IEDPPREPEQPAFVFYTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 280 GNPKGAMLTHGNVVSNcSAFIkITEESLKLCPQDVLISFLPLAHMfervvegvllchgakIGYFQgdirLLMDDLKnLKP 359
Cdd:cd05923 163 GLPKGAVIPQRAAESR-VLFM-STQAGLRHGRHNVVLGLMPLYHV---------------IGFFA----VLVAALA-LDG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 360 TIFPVvprllnRMFDKifGQAntpLKrWLldfatsrkEAELKSGVVRKDSMWDKLIFSKVQASLG-GRVRLMITGAAPVS 438
Cdd:cd05923 221 TYVVV------EEFDP--ADA---LK-LI--------EQERVTSLFATPTHLDALAAAAEFAGLKlSSLRHVTFAGATMP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 439 PTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPgdwTAGHVGAPLPCNFVKLVDV-AEMNYFAANG-EGEVCVK--GPNV 514
Cdd:cd05923 281 DAVLERVNQHLPGEKVNIYGTTEAMNSLYMRDA---RTGTEMRPGFFSEVRIVRIgGSPDEALANGeEGELIVAaaADAA 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 515 FQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVFV------- 587
Cdd:cd05923 358 FTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVigvader 435
|
490
....*....|
gi 528467780 588 HGDSLQACLV 597
Cdd:cd05923 436 WGQSVTACVV 445
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
135-602 |
5.47e-21 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 97.26 E-value: 5.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 135 SALLHRGHSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLgteAISYVIDKASittiicdiADKARLILdcVS 214
Cdd:PRK05852 57 AGQLTRSGLLPGDR-VALRMGSNAEFVVALLAASRADLVVVPLDPAL---PIAEQRVRSQ--------AAGARVVL--ID 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 215 GRKHSVTTIVIMESFDSELTAQAQNCGIDIISLKELEAIGKANHKTPIPP--KPEDlALICFTSGTTGNPKGAMLTHGNV 292
Cdd:PRK05852 123 ADGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTPATSTPEglRPDD-AMIMFTGGTTGLPKMVPWTHANI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 293 VSNCSAFIKiteeSLKLCPQDVLISFLPLAHMfERVVEGVL--LCHGAKI-----GYFQGdiRLLMDDLKNLKPTIFPVV 365
Cdd:PRK05852 202 ASSVRAIIT----GYRLSPRDATVAVMPLYHG-HGLIAALLatLASGGAVllparGRFSA--HTFWDDIKAVGATWYTAV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 366 PR----LLNRMFDKIFGQANTPLkrwlldfatsrkeaelksgvvrkdsmwdklifskvqaslggrvRLMITGAAPVSPTV 441
Cdd:PRK05852 275 PTihqiLLERAATEPSGRKPAAL-------------------------------------------RFIRSCSAPLTAET 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 442 LTFLRAALGCQFYEGYGQTECT----------AGCT----MS--LPGDWTA------GHVGAPLPCNFVklvdvaemnyf 499
Cdd:PRK05852 312 AQALQTEFAAPVVCAFGMTEAThqvtttqiegIGQTenpvVStgLVGRSTGaqirivGSDGLPLPAGAV----------- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 500 aangeGEVCVKGPNVFQGYLKDPEQTSGAVDKaGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRS 579
Cdd:PRK05852 381 -----GEVWLRGTTVVRGYLGDPTITAANFTD-GWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLASH 453
|
490 500
....*....|....*....|....*.
gi 528467780 580 DPVAQVFVHG--DSLQACLVG-VVVP 602
Cdd:PRK05852 454 PNVMEAAVFGvpDQLYGEAVAaVIVP 479
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
222-573 |
4.68e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 94.29 E-value: 4.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 222 TIVIMESFDSELTAQAQNcGIDIISLKELEAIGKAnhkTPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAF-- 299
Cdd:PRK07768 111 AVVVGEPFLAAAPVLEEK-GIRVLTVADLLAADPI---DPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMfv 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 300 -IKITEESlklcpqDVLISFLPLAH-MfervvegvllchgAKIGYFQGDIRLLMDDLKnLKPTIFPVVPRLLNRMFDKIF 377
Cdd:PRK07768 187 aAEFDVET------DVMVSWLPLFHdM-------------GMVGFLTVPMYFGAELVK-VTPMDFLRDPLLWAELISKYR 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 378 GqANT--PlkrwllDFATSrkeaeLKSGVVRKDSMWDKLIFSKvqaslggrVRLMITGAAPVSP-TVLTFLRA------- 447
Cdd:PRK07768 247 G-TMTaaP------NFAYA-----LLARRLRRQAKPGAFDLSS--------LRFALNGAEPIDPaDVEDLLDAgarfglr 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 448 --ALGCqfyeGYGQTECTAGCTMSLPGD--------------------WTAGHV------GAPLPCNFVKLVDvAEMNYF 499
Cdd:PRK07768 307 peAILP----AYGMAEATLAVSFSPCGAglvvdevdadllaalrravpATKGNTrrlatlGPPLPGLEVRVVD-EDGQVL 381
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528467780 500 AANGEGEVCVKGPNVFQGYLkDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIE 573
Cdd:PRK07768 382 PPRGVGVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPTDIE 453
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
266-603 |
5.68e-20 |
|
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: 93.14 E-value: 5.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 266 PEDLALICFTSGTTGNPKGAMLTHGNVVsncsAFIKITEESLKLCPQDVLISFLPLAHMFErVVE--GVLLcHGAKIgyf 343
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHANVL----ALFAATQRWFGFNEDDVWTLFHSYAFDFS-VWEiwGALL-HGGRL--- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 344 qgdirLLMDDLKNLKPTIFPvvpRLLNRMFDKIFGQANTPLKRwLLDFATSRKEAELksgvvrkdsmwdklifskvqasl 423
Cdd:cd17643 163 -----VVVPYEVARSPEDFA---RLLRDEGVTVLNQTPSAFYQ-LVEAADRDGRDPL----------------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 424 ggRVRLMITGAAPVSPTVLTFLRAALGC---QFYEGYGQTECTAGCTM------SLPGDwTAGHVGAPLPCNFVKLVDvA 494
Cdd:cd17643 211 --ALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFrpldaaDLPAA-AASPIGRPLPGLRVYVLD-A 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 495 EMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSG-----AVDKAG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 567
Cdd:cd17643 287 DGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanPFGGPGsrMYRTGDLARRLPDGELEYLGRADEQVKI-RGFRI 365
|
330 340 350
....*....|....*....|....*....|....*....
gi 528467780 568 APEKIENIYIRSDPVAQVFV---HGDSLQACLVGVVVPD 603
Cdd:cd17643 366 ELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVAD 404
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
119-604 |
1.91e-19 |
|
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: 92.17 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 119 KWLSYKEVADRAEFAGSALLHRGhSQSGDkYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTI 198
Cdd:cd05970 46 RIFTFAELADYSDKTANFFKAMG-IGKGD-TVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 199 ICDIADKARLILDCVSGRKHSVTTIVIMESFDSEltaqaqncgiDIISLKELeaIGKANHKTPIP-----PKPEDLALIC 273
Cdd:cd05970 124 VAIAEDNIPEEIEKAAPECPSKPKLVWVGDPVPE----------GWIDFRKL--IKNASPDFERPtansyPCGEDILLVY 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 274 FTSGTTGNPKgaMLTHGNVvsncsafikiteeslklcpqdvlisfLPLAHM-----FERVVEGVLLCHGAKIGYFQGdir 348
Cdd:cd05970 192 FSSGTTGMPK--MVEHDFT--------------------------YPLGHIvtakyWQNVREGGLHLTVADTGWGKA--- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 349 llmddlknlkptifpvvprllnrMFDKIFGQANTPLKRWLLDFATSRKEAEL----KSGVVR---KDSMWDKLIFSKVQA 421
Cdd:cd05970 241 -----------------------VWGKIYGQWIAGAAVFVYDYDKFDPKALLeklsKYGVTTfcaPPTIYRFLIREDLSR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 422 SLGGRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAgCTMSLPG-DWTAGHVGAPLPCNFVKLVDvAEMNYFA 500
Cdd:cd05970 298 YDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTL-TIATFPWmEPKPGSMGKPAPGYEIDLID-REGRSCE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 501 ANGEGEVCV---KGPNV--FQGYLKDPEQTSgAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENI 575
Cdd:cd05970 376 AGEEGEIVIrtsKGKPVglFGGYYKDAEKTA-EVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVESA 453
|
490 500
....*....|....*....|....*....
gi 528467780 576 YIRSDPVAQVFVHGdslqaclvgvvVPDP 604
Cdd:cd05970 454 LIQHPAVLECAVTG-----------VPDP 471
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
121-603 |
5.52e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 92.53 E-value: 5.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALlhRGHSQSGDKYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASIttiic 200
Cdd:PRK12467 538 LSYAELNRQANRLAHVL--IAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGV----- 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 diadkaRLILDcvsgrkhsvttivimesfDSELTAQAQNC-GIDIISLKELEAI--GKANHKTPIPPKPEDLALICFTSG 277
Cdd:PRK12467 611 ------RLLLT------------------QSHLLAQLPVPaGLRSLCLDEPADLlcGYSGHNPEVALDPDNLAYVIYTSG 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 278 TTGNPKGAMLTHGNVVSncsaFIKITEESLKLCPQDVLISFLPLAHMFERVVEGVLLCHGAKIgyfqgdirLLMDDLKNL 357
Cdd:PRK12467 667 STGQPKGVAISHGALAN----YVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATL--------HLLPPDCAR 734
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 358 KPTIFpvvprllnrmFDKIFGQANTplkrwLLDFATsrkeaelksgvvrkdSMWDKLIFSKVQASLGGRVRLMITGAA-P 436
Cdd:PRK12467 735 DAEAF----------AALMADQGVT-----VLKIVP---------------SHLQALLQASRVALPRPQRALVCGGEAlQ 784
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 437 VSPTVLTFlRAALGCQFYEGYGQTECTAGCTM----SLPGDWTAGHVGAPLPCNFVKLVDvAEMNYFAANGEGEVCVKGP 512
Cdd:PRK12467 785 VDLLARVR-ALGPGARLINHYGPTETTVGVSTyelsDEERDFGNVPIGQPLANLGLYILD-HYLNPVPVGVVGELYIGGA 862
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 513 NVFQGYLKDPEQTS-------GAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDPVAQV 585
Cdd:PRK12467 863 GLARGYHRRPALTAerfvpdpFGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKI-RGFRIELGEIEARLLAQPGVREA 941
|
490 500
....*....|....*....|....
gi 528467780 586 FV------HGDSLQACLVGVVVPD 603
Cdd:PRK12467 942 VVlaqpgdAGLQLVAYLVPAAVAD 965
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
266-582 |
1.32e-18 |
|
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: 89.47 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 266 PEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEESLKlcpqDVLISFLPLAHMFervveGVLLCHGAKIgyFQG 345
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTK----DRILSWMPLTHDM-----GLIAFHLAPL--IAG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 346 DIRLLMddlknlkPT-IFPVVPRLLNRMFDK----IFGQANTPLKrWLLDFATSRKEAElksgvvrkdsmWDKlifskvq 420
Cdd:cd05908 174 MNQYLM-------PTrLFIRRPILWLKKASEhkatIVSSPNFGYK-YFLKTLKPEKAND-----------WDL------- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 421 aslgGRVRLMITGAAPVSPT---VLTFLRAALGCQ---FYEGYGQTECTAGCTMSLPGD--------------------- 473
Cdd:cd05908 228 ----SSIRMILNGAEPIDYElchEFLDHMSKYGLKrnaILPVYGLAEASVGASLPKAQSpfktitlgrrhvthgepepev 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 474 -------WTAGHVGAPLPCNFVKLVDvaEMNYFAANGE-GEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGkWLP 545
Cdd:cd05908 304 dkkdsecLTFVEVGKPIDETDIRICD--EDNKILPDGYiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIR 380
|
330 340 350
....*....|....*....|....*....|....*..
gi 528467780 546 NGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPV 582
Cdd:cd05908 381 NGRLVITGREKDII-FVNGQNVYPHDIERIAEELEGV 416
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
107-694 |
1.75e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 89.72 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 107 PCLGSRKAGQ-PYKWLSYKEVADRAEFAGSALLHRGHSQsgDKYIGIFAQNRPEWTISELACYTYSLVAVPL---YDTLG 182
Cdd:PRK12582 66 PWLAQREPGHgQWRKVTYGEAKRAVDALAQALLDLGLDP--GRPVMILSGNSIEHALMTLAAMQAGVPAAPVspaYSLMS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 183 TE--AISYVIDKASITTIICDIAD---KARLILDCVSgrkhsVTTIVIMESFDseltaqaqncGIDIISLKELEAigkan 257
Cdd:PRK12582 144 HDhaKLKHLFDLVKPRVVFAQSGApfaRALAALDLLD-----VTVVHVTGPGE----------GIASIAFADLAA----- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 258 hkTPIPPK---------PEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEESLKLCPQDVLiSFLPLAHMFerv 328
Cdd:PRK12582 204 --TPPTAAvaaaiaaitPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPVSL-DWMPWNHTM--- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 329 vegvllchGAKIGyFQGDIR----LLMDDLKNLkPTIFPVVPRLLNRMFDKIFGqaNTPLKRWLLDFATSRKEAELKSgv 404
Cdd:PRK12582 278 --------GGNAN-FNGLLWgggtLYIDDGKPL-PGMFEETIRNLREISPTVYG--NVPAGYAMLAEAMEKDDALRRS-- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 405 vrkdsmwdklIFSkvqaslggRVRLMITGAAPVSPTVLTFLRA----ALGCQ--FYEGYGQTEcTAGCTMSLpgDWTA-- 476
Cdd:PRK12582 344 ----------FFK--------NLRLMAYGGATLSDDLYERMQAlavrTTGHRipFYTGYGATE-TAPTTTGT--HWDTer 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 477 -GHVGAPLPCNFVKLVDVAEmNYfaangegEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWL----PNGTLKI 551
Cdd:PRK12582 403 vGLIGLPLPGVELKLAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdpddPEKGLIF 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 552 IDRKKHIFKLAQGEYIAPEKieniyIRSDPVAQV--FVHgDSLQACL----VGVVV-PDPDFLPGWAKNRGieGSFNDLC 624
Cdd:PRK12582 475 DGRVAEDFKLSTGTWVSVGT-----LRPDAVAACspVIH-DAVVAGQdrafIGLLAwPNPAACRQLAGDPD--AAPEDVV 546
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528467780 625 KSKEVKNAILEDMIQLGKEAGLKSfEQVRDIALHLEMFSVQNGLLTPtlKA---KRTELKSRfREQIDQLYAK 694
Cdd:PRK12582 547 KHPAVLAILREGLSAHNAEAGGSS-SRIARALLMTEPPSIDAGEITD--KGyinQRAVLERR-AALVERLYAE 615
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
107-609 |
2.00e-18 |
|
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: 88.30 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 107 PCLGSrkagqPYKWLSYKEVADRAEFAGSALLHRGHSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAI 186
Cdd:cd05958 2 TCLRS-----PEREWTYRDLLALANRIANVLVGELGIVPGNR-VLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 187 SYVIDKASITTIICDiadkarlildcvsgrkHSVTTIvimesfdseltaqaqncgidiislkeleaigkanhktpippkp 266
Cdd:cd05958 76 AYILDKARITVALCA----------------HALTAS------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 267 EDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFikiTEESLKLCPQDVLISFLPLAHMFERvvEGVLL---CHGAKIGYF 343
Cdd:cd05958 97 DDICILAFTSGTTGAPKATMHFHRDPLASADRY---AVNVLRLREDDRFVGSPPLAFTFGL--GGVLLfpfGVGASGVLL 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 344 QGDI-RLLMDDLKNLKPTIFPVVPRLLNRMFDKifgqantplkrwlLDFAtsrkeaelksgvvrkdsmwdklifskvqAS 422
Cdd:cd05958 172 EEATpDLLLSAIARYKPTVLFTAPTAYRAMLAH-------------PDAA----------------------------GP 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 423 LGGRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDvAEMNYFAAN 502
Cdd:cd05958 211 DLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD-DEGNPVPDG 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 503 GEGEVCVKGPNVFQgYLKDPEQTSGAVDkaGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSDPV 582
Cdd:cd05958 290 TIGRLAVRGPTGCR-YLADKRQRTYVQG--GWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQHPAV 365
|
490 500 510
....*....|....*....|....*....|
gi 528467780 583 AQVFVHGDSLQACLVGV---VVPDPDFLPG 609
Cdd:cd05958 366 AECAVVGHPDESRGVVVkafVVLRPGVIPG 395
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
121-589 |
2.93e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 88.40 E-value: 2.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGHSQsGDkYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASittiic 200
Cdd:PRK06145 28 ISYAEFHQRILQAAGMLHARGIGQ-GD-VVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAG------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 diadkARLILdcvsgrkhsvttivIMESFDSELTAQAQNCGIDIISLKELEAIGKANhkTPIPP----KPEDLALICFTS 276
Cdd:PRK06145 100 -----AKLLL--------------VDEEFDAIVALETPKIVIDAAAQADSRRLAQGG--LEIPPqaavAPTDLVRLMYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 277 GTTGNPKGAMLTHGNVVSNCSAFIKiteeSLKLCPQDVLISFLPLAHMFERVVEGV-LLCHGakigyfqGDIRLLmddlK 355
Cdd:PRK06145 159 GTTDRPKGVMHSYGNLHWKSIDHVI----ALGLTASERLLVVGPLYHVGAFDLPGIaVLWVG-------GTLRIH----R 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 356 NLKP-TIFPVVPRllnrmfDKIFGQantplkrWLLDFATSRkeaelksgvVRKDSMWDKLIFSKVQASLGGrvrlmitGA 434
Cdd:PRK06145 224 EFDPeAVLAAIER------HRLTCA-------WMAPVMLSR---------VLTVPDRDRFDLDSLAWCIGG-------GE 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 435 APVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTA--GHVGAPLPCNFVKLVDvAEMNYFAANGEGEVCVKGP 512
Cdd:PRK06145 275 KTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREIEkiGSTGRALAHVEIRIAD-GAGRWLPPNMKGEICMRGP 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528467780 513 NVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVFVHG 589
Cdd:PRK06145 354 KVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERVIYELPEVAEAAVIG 428
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
122-604 |
6.45e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 87.40 E-value: 6.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 122 SYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC- 200
Cdd:PRK07470 34 TWREIDARVDALAAALAARG-VRKGDR-ILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMICh 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 -DIADKARLILDCVSGRKHSvttIVIMESFDSEltaqaqncgidiislkELEAIGKANHKTPIPPKP---EDLALICFTS 276
Cdd:PRK07470 112 aDFPEHAAAVRAASPDLTHV---VAIGGARAGL----------------DYEALVARHLGARVANAAvdhDDPCWFFFTS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 277 GTTGNPKGAMLTHGNVvsncsAFIkITEESLKLCP----QDVLISFLPLAHMfervvEGV-LLC---HGAKigyfqgdir 348
Cdd:PRK07470 173 GTTGRPKAAVLTHGQM-----AFV-ITNHLADLMPgtteQDASLVVAPLSHG-----AGIhQLCqvaRGAA--------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 349 llmddlknlkpTIFPVVPRllnrmFDkiFGQANTPLKRWLLD--FA--TSRKEAELKSGVVRKDsmwdklifskvQASLg 424
Cdd:PRK07470 233 -----------TVLLPSER-----FD--PAEVWALVERHRVTnlFTvpTILKMLVEHPAVDRYD-----------HSSL- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 425 grvRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTaGCTMSLP------GDWTAGHVGaplPCNF------VKLVD 492
Cdd:PRK07470 283 ---RYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVT-GNITVLPpalhdaEDGPDARIG---TCGFertgmeVQIQD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 493 vAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKI 572
Cdd:PRK07470 356 -DEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPREI 432
|
490 500 510
....*....|....*....|....*....|..
gi 528467780 573 ENiyirsdpvaQVFVHGDSLQACLVGvvVPDP 604
Cdd:PRK07470 433 EE---------KLLTHPAVSEVAVLG--VPDP 453
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
266-603 |
8.64e-18 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 86.75 E-value: 8.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 266 PEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEesLKLCPQDVL----ISFLPLAHMFERVvegvlLCHGAKIG 341
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYE--LDSFPVRLLqmasFSFDVFAGDFARS-----LLNGGTLV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 342 YFQGDIRL----LMDDLKNLKPTIFPVVPRLLnrmfdkifgqantplkRWLLDFATSRKE--AELKSGVVRKDSMWDKLi 415
Cdd:cd17650 165 ICPDEVKLdpaaLYDLILKSRITLMESTPALI----------------RPVMAYVYRNGLdlSAMRLLIVGSDGCKAQD- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 416 FSKVQASLGGRVRlmITGAAPVSptvltflRAALGCQFYEGYGQTECTAGCTmslPgdwtaghVGAPLPCNFVKLVDvAE 495
Cdd:cd17650 228 FKTLAARFGQGMR--IINSYGVT-------EATIDSTYYEEGRDPLGDSANV---P-------IGRPLPNTAMYVLD-ER 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 496 MNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGA------VDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAP 569
Cdd:cd17650 288 LQPQPVGVAGELYIGGAGVARGYLNRPELTAERfvenpfAPGERMYRTGDLARWRADGNVELLGRVDHQVKI-RGFRIEL 366
|
330 340 350
....*....|....*....|....*....|....*..
gi 528467780 570 EKIENIYIRSDPVAQVFV---HGDSLQACLVGVVVPD 603
Cdd:cd17650 367 GEIESQLARHPAIDEAVVavrEDKGGEARLCAYVVAA 403
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
260-627 |
9.70e-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: 86.65 E-value: 9.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 260 TPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITeesLKLCPQDVLISFLPLAHMFErvvegvlLCHGAK 339
Cdd:cd05959 156 KPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNV---LGIREDDVCFSAAKLFFAYG-------LGNSLT 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 340 IGYFQGDIRLLM----------DDLKNLKPTIFPVVPRLLNRMFdkifgqantplkrwlldfatsrkeaelksgvvrKDS 409
Cdd:cd05959 226 FPLSVGATTVLMperptpaavfKRIRRYRPTVFFGVPTLYAAML---------------------------------AAP 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 410 MWDKLIFSkvqaslggRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVK 489
Cdd:cd05959 273 NLPSRDLS--------SLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVE 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 490 LVDVAEmNYFAANGEGEVCVKGPNVFQGYLKDPEQTSgAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAP 569
Cdd:cd05959 345 LRDEDG-GDVADGEPGELYVRGPSSATMYWNNRDKTR-DTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSP 421
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528467780 570 EKIENIYIRSDPVAQVFV----HGDSLQAcLVGVVVPDPDFLPGWAKNRGIEgsfnDLCKSK 627
Cdd:cd05959 422 FEVESALVQHPAVLEAAVvgveDEDGLTK-PKAFVVLRPGYEDSEALEEELK----EFVKDR 478
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
266-611 |
1.11e-17 |
|
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: 86.27 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 266 PEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAfikiTEESLKLCPQDVLISFLPLAhmFERVVEGVL--LCHGAkigyf 343
Cdd:cd17649 93 PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQA----TAERYGLTPGDRELQFASFN--FDGAHEQLLppLICGA----- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 344 qgdiRLLMDDLKNLKPtifpvvPRLLNRMFDKifGQANtplkrwLLDFATsrkeaelksgvvrkdSMWDKLI--FSKVQA 421
Cdd:cd17649 162 ----CVVLRPDELWAS------ADELAEMVRE--LGVT------VLDLPP---------------AYLQQLAeeADRTGD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 422 SLGGRVRLMITGAAPVSPtvlTFLRAALGC--QFYEGYGQTECTAGCTMSL--PGDWTAGH---VGAPLPCNFVKLVDvA 494
Cdd:cd17649 209 GRPPSLRLYIFGGEALSP---ELLRRWLKApvRLFNAYGPTEATVTPLVWKceAGAARAGAsmpIGRPLGGRSAYILD-A 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 495 EMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSG-------AVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 567
Cdd:cd17649 285 DLNPVPVGVTGELYIGGEGLARGYLGRPELTAErfvpdpfGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKI-RGFRI 363
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 528467780 568 APEKIENIYIRSDPVAQVFV------HGDSLQACLVGVvvpDPDFLPGWA 611
Cdd:cd17649 364 ELGEIEAALLEHPGVREAAVvaldgaGGKQLVAYVVLR---AAAAQPELR 410
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
121-603 |
1.49e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 87.71 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGhsQSGDKYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARG--VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLT 2106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 DIADKARLILdcvsgrkhsvTTIVIMESFDSELtaqaqncgidiislkELEaiGKANHKTPIPPKPEDLALICFTSGTTG 280
Cdd:PRK12316 2107 QRHLLERLPL----------PAGVARLPLDRDA---------------EWA--DYPDTAPAVQLAGENLAYVIYTSGSTG 2159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 281 NPKGAMLTHGNVVSNCSAfikiTEESLKLCPQDVLISFLPLAhmFERVVEGVL--LCHGAkigyfqgdiRLLMDDLKNLK 358
Cdd:PRK12316 2160 LPKGVAVSHGALVAHCQA----AGERYELSPADCELQFMSFS--FDGAHEQWFhpLLNGA---------RVLIRDDELWD 2224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 359 PtifpvvprllNRMFDKIFGQANTplkrwLLDFATsrkeaelksgvvrkdSMWDKLIfsKVQASLGGR--VRLMITGAAP 436
Cdd:PRK12316 2225 P----------EQLYDEMERHGVT-----ILDFPP---------------VYLQQLA--EHAERDGRPpaVRVYCFGGEA 2272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 437 VSPTVLTFLRAALGCQF-YEGYGQTEctagcTMSLPGDWTAGH----------VGAPLPCNFVKLVDvAEMNYFAANGEG 505
Cdd:PRK12316 2273 VPAASLRLAWEALRPVYlFNGYGPTE-----AVVTPLLWKCRPqdpcgaayvpIGRALGNRRAYILD-ADLNLLAPGMAG 2346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 506 EVCVKGPNVFQGYLKDPEQTS--------GAVdkAGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIY 576
Cdd:PRK12316 2347 ELYLGGEGLARGYLNRPGLTAerfvpdpfSAS--GERLYrTGDLARYRADGVVEYLGRIDHQVKI-RGFRIELGEIEARL 2423
|
490 500 510
....*....|....*....|....*....|
gi 528467780 577 IRSDPVAQVFV---HGDSLQAcLVGVVVPD 603
Cdd:PRK12316 2424 QAHPAVREAVVvaqDGASGKQ-LVAYVVPD 2452
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
267-575 |
2.07e-17 |
|
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: 84.23 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 267 EDLALICFTSGTTGNPKGAMLTHGNVVSncsAFIKITEESLKLCPQDVLISFLPLAHMFERVVEGVLLCHGAKIGYFQGD 346
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFA---VPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 347 IRL--LMDDLKNLKPTIFPVVPRLLNRMfdkifgqantplkrwLLDFATSRKEAElksgvvrkdsmwdklifskvqaslg 424
Cdd:cd17635 78 TTYksLFKILTTNAVTTTCLVPTLLSKL---------------VSELKSANATVP------------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 425 gRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWT-AGHVGAPLPCNFVKLVDVAEMNYFAAnG 503
Cdd:cd17635 118 -SLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLPTDDDSIeINAVGRPYPGVDVYLAATDGIAGPSA-S 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528467780 504 EGEVCVKGPNVFQGYLKDPEQTSgAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 575
Cdd:cd17635 196 FGTIWIKSPANMLGYWNNPERTA-EVLIDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERI 265
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
266-589 |
2.25e-17 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 86.01 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 266 PEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKIteesLKLCPQDVLISFLPLAH-------MFERVVEGvllCHgA 338
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAI----VGYGEDDVYLHTAPLCHigglssaLAMLMVGA---CH-V 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 339 KIGYFqgDIRLLMDDLKNLKPTIFPVVPRLL------NRMfdKIFGQANTPLKRwLLDFATSRKEAELKSGVvrkdsmwd 412
Cdd:PLN02860 243 LLPKF--DAKAALQAIKQHNVTSMITVPAMMadlislTRK--SMTWKVFPSVRK-ILNGGGSLSSRLLPDAK-------- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 413 kLIFSkvqaslggRVRLMITGAAPVSPTVLTFLRaaLGCQFYEGYGQTECTAGCTMSLPGDWTAGH-VGAPLPcnFVKLv 491
Cdd:PLN02860 310 -KLFP--------NAKLFSAYGMTEACSSLTFMT--LHDPTLESPKQTLQTVNQTKSSSVHQPQGVcVGKPAP--HVEL- 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 492 dvaEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEK 571
Cdd:PLN02860 376 ---KIGLDESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIK-TGGENVYPEE 451
|
330
....*....|....*...
gi 528467780 572 IENIYIRSDPVAQVFVHG 589
Cdd:PLN02860 452 VEAVLSQHPGVASVVVVG 469
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
243-606 |
3.02e-17 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 85.58 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 243 DIISLKELEAigKANHKTPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVsnCSAfikitEESLKLC---PQDVLISFL 319
Cdd:COG1021 162 EFTSLDALLA--APADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYL--YSV-----RASAEICgldADTVYLAAL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 320 PLAHMFERVVEGVL--LCHGAKIgyfqgdirLLMDDLKnlkP-TIFP-----------VVPRLLNRMFDkifgqantplk 385
Cdd:COG1021 233 PAAHNFPLSSPGVLgvLYAGGTV--------VLAPDPS---PdTAFPlierervtvtaLVPPLALLWLD----------- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 386 rwlldfATSRKEAELKSgvvrkdsmwdklifskvqaslggrVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTEctaG 465
Cdd:COG1021 291 ------AAERSRYDLSS------------------------LRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---G 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 466 --CTMSL--PGDWTAGHVGAPL-PCNFVKLVD-----VAEmnyfaanGE-GEVCVKGPNVFQGYLKDPEQTSGAVDKAGW 534
Cdd:COG1021 338 lvNYTRLddPEEVILTTQGRPIsPDDEVRIVDedgnpVPP-------GEvGELLTRGPYTIRGYYRAPEHNARAFTPDGF 410
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528467780 535 LHTGDIGKWLPNGTLKIIDRKK-HIFKlaQGEYIAPEKIENIYIRsdpvaqvfvHGDSLQACLVGvvVPDPDF 606
Cdd:COG1021 411 YRTGDLVRRTPDGYLVVEGRAKdQINR--GGEKIAAEEVENLLLA---------HPAVHDAAVVA--MPDEYL 470
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
121-605 |
3.22e-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: 85.09 E-value: 3.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:cd17651 21 LTYAELDRRANRLAHRLRARG-VGPGDL-VALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 DIADKARLildcvSGRKHSVTtivimesfdseLTAQAQncgidiislkeLEAIGKANHktPIPPKPEDLALICFTSGTTG 280
Cdd:cd17651 99 HPALAGEL-----AVELVAVT-----------LLDQPG-----------AAAGADAEP--DPALDADDLAYVIYTSGSTG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 281 NPKGAMLTHGNVVSncsaFIKITEESLKLCPQDVLISFLPLAhmFERVVEGVL--LCHGAKIGYFQGDIRllMDdlknlk 358
Cdd:cd17651 150 RPKGVVMPHRSLAN----LVAWQARASSLGPGARTLQFAGLG--FDVSVQEIFstLCAGATLVLPPEEVR--TD------ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 359 ptiFPVVPRLLNRM-FDKIFgqANTPLKRWLLdfatsrkEAELKSGVVrkdsmwdklifskvqaslGGRVRLMITG--AA 435
Cdd:cd17651 216 ---PPALAAWLDEQrISRVF--LPTVALRALA-------EHGRPLGVR------------------LAALRYLLTGgeQL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 436 PVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGD---WTA-GHVGAPLPCNFVKLVDvaemnyfaANGE------- 504
Cdd:cd17651 266 VLTEDLREFCAGLPGLRLHNHYGPTETHVVTALSLPGDpaaWPApPPIGRPIDNTRVYVLD--------AALRpvppgvp 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 505 GEVCVKGPNVFQGYLKDPEQT------SGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIR 578
Cdd:cd17651 338 GELYIGGAGLARGYLNRPELTaerfvpDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKI-RGFRIELGEIEAALAR 416
|
490 500 510
....*....|....*....|....*....|
gi 528467780 579 SDPVAQ--VFVHGD-SLQACLVGVVVPDPD 605
Cdd:cd17651 417 HPGVREavVLAREDrPGEKRLVAYVVGDPE 446
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
246-602 |
7.27e-17 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 84.18 E-value: 7.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 246 SLKELEAIGKANHKTPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVsncsAFIKITEESLKLCPQDVLISFLPLAHMF 325
Cdd:PRK09274 153 TLATLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFE----AQIEALREDYGIEPGEIDLPTFPLFALF 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 326 ervveGVLLCHGAKIGYF------QGDIRLLMDDLKNLKPTIFPVVPRLLNRmfdkifgqantplkrwLLDFATSRkeae 399
Cdd:PRK09274 229 -----GPALGMTSVIPDMdptrpaTVDPAKLFAAIERYGVTNLFGSPALLER----------------LGRYGEAN---- 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 400 lksgvvrkdsmwdklifskvQASLGGrVRLMITGAAPVSPTVLTFLRAAL--GCQFYEGYGQTECTAGCTMS----LPGD 473
Cdd:PRK09274 284 --------------------GIKLPS-LRRVISAGAPVPIAVIERFRAMLppDAEILTPYGATEALPISSIEsreiLFAT 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 474 WT-----AGH-VGAPLPCNFVKLVDV--------AEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGA--VDKAG--WL 535
Cdd:PRK09274 343 RAatdngAGIcVGRPVDGVEVRIIAIsdapipewDDALRLATGEIGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWH 422
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528467780 536 HTGDIGkWL-PNGTLKIIDRKKHIFKLAQGEYIapekieniyirSDPVAQVF-VHGDSLQACLVGVVVP 602
Cdd:PRK09274 423 RMGDLG-YLdAQGRLWFCGRKAHRVETAGGTLY-----------TIPCERIFnTHPGVKRSALVGVGVP 479
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
121-605 |
1.20e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 83.55 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:PRK06178 59 ITYAELDELSDRFAALLRQRG-VGAGDR-VAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 --DIADKARLILDCVSGRKHSVT----------TIVIMESFDSELTAQAqncgiDIISLkeLEAIGKANHKTPIP-PKPE 267
Cdd:PRK06178 137 ldQLAPVVEQVRAETSLRHVIVTsladvlpaepTLPLPDSLRAPRLAAA-----GAIDL--LPALRACTAPVPLPpPALD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 268 DLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITeesLKLCPQDVLISFLPlahMFervvegvllchgakigYFQGDi 347
Cdd:PRK06178 210 ALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVA---VVGGEDSVFLSFLP---EF----------------WIAGE- 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 348 rllmdDLKNLKPTIF--PVVprLLNRMFDKIFGQA-------NTPLkrwLLDFAT------SRKEAELKS-GVVRKDSMW 411
Cdd:PRK06178 267 -----NFGLLFPLFSgaTLV--LLARWDAVAFMAAveryrvtRTVM---LVDNAVelmdhpRFAEYDLSSlRQVRVVSFV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 412 DKLifskvqaslggrvrlmitgaapvSPTVLTFLRAALGCQFYEG-YGQTEC------TAGCT---MSLPGDWTagHVGA 481
Cdd:PRK06178 337 KKL-----------------------NPDYRQRWRALTGSVLAEAaWGMTEThtcdtfTAGFQdddFDLLSQPV--FVGL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 482 PLPCNFVKLVDVAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKL 561
Cdd:PRK06178 392 PVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 528467780 562 aQGEYIAPEKIENIYIRsdpvaqvfvHGDSLQACLVGvvVPDPD 605
Cdd:PRK06178 471 -NGMSVFPSEVEALLGQ---------HPAVLGSAVVG--RPDPD 502
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
268-606 |
2.37e-16 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 82.38 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 268 DLALICFTSGTTGNPKGAMLTHGNVVSNCSAfikiTEESLKLCPQDVLISFLPLAHMFERV---VEGVLLCHGAKIGYFQ 344
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTHNDYAYNVRA----SAEVCGLDQDTVYLAVLPAAHNFPLAcpgVLGTLLAGGRVVLAPD 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 345 GDIRLLMDDLKNLKPTIFPVVPRLLnrmfdkifgqantplKRWLlDFATSRKeAELKSgvvrkdsmwdklifskvqaslg 424
Cdd:cd05920 216 PSPDAAFPLIEREGVTVTALVPALV---------------SLWL-DAAASRR-ADLSS---------------------- 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 425 grVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCT-MSLPGDWTAGHVGAPL-PCNFVKLVDvAEMNYFAAN 502
Cdd:cd05920 257 --LRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTrLDDPDEVIIHTQGRPMsPDDEIRVVD-EEGNPVPPG 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 503 GEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRsdpv 582
Cdd:cd05920 334 EEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVENLLLR---- 408
|
330 340
....*....|....*....|....
gi 528467780 583 aqvfvHgDSLQACLVgVVVPDPDF 606
Cdd:cd05920 409 -----H-PAVHDAAV-VAMPDELL 425
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
263-609 |
5.35e-16 |
|
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: 81.17 E-value: 5.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 263 PPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNcsafIKITEESLKLCPQDVLISFLPLAhmFERVVEGVL--LCHGAKI 340
Cdd:cd17646 134 PPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNR----LLWMQDEYPLGPGDRVLQKTPLS--FDVSVWELFwpLVAGARL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 341 ------GYfqGDIRLLMDDLKNLKPTIFPVVPRLLnrmfdkifgqantplkRWLLDFATSRKEAELksgvvrkdsmwdkl 414
Cdd:cd17646 208 vvarpgGH--RDPAYLAALIREHGVTTCHFVPSML----------------RVFLAEPAAGSCASL-------------- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 415 ifskvqaslggrvRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCT-MSLPGDWTAGHV--GAPLPCNFVKLV 491
Cdd:cd17646 256 -------------RRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVThWPVRGPAETPSVpiGRPVPNTRLYVL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 492 DvAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAV-----DKAGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGE 565
Cdd:cd17646 323 D-DALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFvpdpfGPGSRMYrTGDLARWRPDGALEFLGRSDDQVKI-RGF 400
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 528467780 566 YIAPEKIENIYIRSDPVAQ--VFVHGD-SLQACLVGVVVPDPDFLPG 609
Cdd:cd17646 401 RVEPGEIEAALAAHPAVTHavVVARAApAGAARLVGYVVPAAGAAGP 447
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
120-587 |
9.59e-16 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 80.57 E-value: 9.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 120 WLSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTII 199
Cdd:PRK06155 46 RWTYAEAARAAAAAAHALAAAG-VKRGDR-VALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 200 CDIADKARLilDCVSGRKHSVTTIVIMESFDSELTAQaqncGIDIISLKELEAIGkanhkTPIPPKPEDLALICFTSGTT 279
Cdd:PRK06155 124 VEAALLAAL--EAADPGDLPLPAVWLLDAPASVSVPA----GWSTAPLPPLDAPA-----PAAAVQPGDTAAILYTSGTT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 280 GNPKGAMLTHGNVvsncsaFI--KITEESLKLCPQDVLISFLPLAH------MFERVVEGVLLCHGAKI---GYFqgdir 348
Cdd:PRK06155 193 GPSKGVCCPHAQF------YWwgRNSAEDLEIGADDVLYTTLPLFHtnalnaFFQALLAGATYVLEPRFsasGFW----- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 349 llmDDLKNLKPTIFpvvpRLLNRMFDKIFGQANTPLKRwlldfatsrkeaelksgvvrkdsmwdklifskvqaslGGRVR 428
Cdd:PRK06155 262 ---PAVRRHGATVT----YLLGAMVSILLSQPARESDR-------------------------------------AHRVR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 429 LMITGAAPvsPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDwTAGHVGAPLPCNFVKLVDvaEMNYFAANGE-GEV 507
Cdd:PRK06155 298 VALGPGVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSMGRLAPGFEARVVD--EHDQELPDGEpGEL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 508 CVKG--PNVF-QGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIyIRSDP-VA 583
Cdd:PRK06155 373 LLRAdePFAFaTGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIKDAIR-RRGENISSFEVEQV-LLSHPaVA 449
|
....
gi 528467780 584 QVFV 587
Cdd:PRK06155 450 AAAV 453
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
230-606 |
1.05e-15 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 80.30 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 230 DSELTAQAQNCGIDII-SLKELEAIGKANHKT--------PIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSN----C 296
Cdd:PRK09029 89 QPLLEELLPSLTLDFAlVLEGENTFSALTSLHlqlvegahAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASaegvL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 297 SAFikiteeslKLCPQDV-LISfLPLAHmfervVEGV------LLChGAkigyfqgdiRLLMDDLKNLKPTIFPV----- 364
Cdd:PRK09029 169 SLM--------PFTAQDSwLLS-LPLFH-----VSGQgivwrwLYA-GA---------TLVVRDKQPLEQALAGCthasl 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 365 VPRLLNRMFDKifGQANTPLKRWLLdfatsrkeaelksgvvrkdsmwdklifskvqaslGGRvrlMItgaapvsPTVLTF 444
Cdd:PRK09029 225 VPTQLWRLLDN--RSEPLSLKAVLL----------------------------------GGA---AI-------PVELTE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 445 LRAALGCQFYEGYGQTEctAGCTM------SLPGdwtaghVGAPLPCNFVKLVDvaemnyfaangeGEVCVKGPNVFQGY 518
Cdd:PRK09029 259 QAEQQGIRCWCGYGLTE--MASTVcakradGLAG------VGSPLPGREVKLVD------------GEIWLRGASLALGY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 519 LKDPEQTSgAVDKAGWLHTGDIGKWLpNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVFVhgdslqaclvg 598
Cdd:PRK09029 319 WRQGQLVP-LVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQVFV----------- 384
|
....*...
gi 528467780 599 VVVPDPDF 606
Cdd:PRK09029 385 VPVADAEF 392
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
121-589 |
2.50e-15 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 79.44 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAefagSALLHRGHSQ---SGDKYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITT 197
Cdd:PRK05620 39 TTFAAIGARA----AALAHALHDElgiTGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 198 IICDIADK---ARLILDCvsgrkHSVTTIVIMESFDSELTAQAQNCGIDIISLkELEAIGKANHkTPIPPKPEDL-ALIC 273
Cdd:PRK05620 115 IVADPRLAeqlGEILKEC-----PCVRAVVFIGPSDADSAAAHMPEGIKVYSY-EALLDGRSTV-YDWPELDETTaAAIC 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 274 FTSGTTGNPKGAMLTHGnvvsncSAFIkiteESLKLCPQDVL-----ISFL---PLAHmfervvegvLLCHGAKIGYFQG 345
Cdd:PRK05620 188 YSTGTTGAPKGVVYSHR------SLYL----QSLSLRTTDSLavthgESFLccvPIYH---------VLSWGVPLAAFMS 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 346 DIRLLMDDLKNLKPTIFPVVPRLLNRmfdkifgQANtplkrwlldfatsrkeaelksGVvrkDSMWDKLIFSKVQASlGG 425
Cdd:PRK05620 249 GTPLVFPGPDLSAPTLAKIIATAMPR-------VAH---------------------GV---PTLWIQLMVHYLKNP-PE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 426 RVRL--MITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGA---------PLPCNFvKLVDVA 494
Cdd:PRK05620 297 RMSLqeIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEARWayrvsqgrfPASLEY-RIVNDG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 495 EMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSG---------AVDKA-------GWLHTGDIGKWLPNGTLKIIDRKKHI 558
Cdd:PRK05620 376 QVMESTDRNEGEIQVRGNWVTASYYHSPTEEGGgaastfrgeDVEDAndrftadGWLRTGDVGSVTRDGFLTIHDRARDV 455
|
490 500 510
....*....|....*....|....*....|.
gi 528467780 559 FKlAQGEYIAPEKIENIYIRSDPVAQVFVHG 589
Cdd:PRK05620 456 IR-SGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
121-605 |
3.34e-15 |
|
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: 78.51 E-value: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGHSQsgDKYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVGP--ESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 DiadkarlildcvsgrkhsvttivimesfdseltaqaqncgidiislkeleaigkanhktpippkPEDLALICFTSGTTG 280
Cdd:cd12115 103 D----------------------------------------------------------------PDDLAYVIYTSGSTG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 281 NPKGAMLTHGNVVsncsAFIKITEESlklCPQDVL--------ISF-LPLAHMFervvegVLLCHGAKIgyfqgdirllm 351
Cdd:cd12115 119 RPKGVAIEHRNAA----AFLQWAAAA---FSAEELagvlastsICFdLSVFELF------GPLATGGKV----------- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 352 ddlknlkptifpvvpRLLNRMFDkifgqantplkrwLLDFAtSRKEAELKSGVvrkDSMWDKLIfskVQASLGGRVRLMI 431
Cdd:cd12115 175 ---------------VLADNVLA-------------LPDLP-AAAEVTLINTV---PSAAAELL---RHDALPASVRVVN 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 432 TGAAPVSPTVLTFLRAAL-GCQFYEGYGQTECTAGCTMSL--PGDWTAGHVGAPLPCNFVKLVDvAEMNYFAANGEGEVC 508
Cdd:cd12115 220 LAGEPLPRDLVQRLYARLqVERVVNLYGPSEDTTYSTVAPvpPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVPGELY 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 509 VKGPNVFQGYLKDPEQTS------GAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDPV 582
Cdd:cd12115 299 IGGAGVARGYLGRPGLTAerflpdPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAALRSIPGV 377
|
490 500
....*....|....*....|....*.
gi 528467780 583 AQ--VFVHGDSL-QACLVGVVVPDPD 605
Cdd:cd12115 378 REavVVAIGDAAgERRLVAYIVAEPG 403
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
121-573 |
3.37e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 80.21 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALlhRGHSQSGDKYIGIFAQNrPEWTISELACYTYSLVAVPLYDTLGTEAISyvidKASITTIIC 200
Cdd:PRK05691 41 LSYRDLDLRARTIAAAL--QARASFGDRAVLLFPSG-PDYVAAFFGCLYAGVIAVPAYPPESARRHH----QERLLSIIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 DIadKARLILdcvsgrkhsvTTIVIMESFdSELTAQAQNCGIDIISLKELEAIGKANHKTPIPPkPEDLALICFTSGTTG 280
Cdd:PRK05691 114 DA--EPRLLL----------TVADLRDSL-LQMEELAAANAPELLCVDTLDPALAEAWQEPALQ-PDDIAFLQYTSGSTA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 281 NPKGAMLTHGNVVSNcsafikiteESL-------KLCPQDVLISFLPLAHmfervvegvllchgakigyfqgDIRLlmdd 353
Cdd:PRK05691 180 LPKGVQVSHGNLVAN---------EQLirhgfgiDLNPDDVIVSWLPLYH----------------------DMGL---- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 354 LKNLKPTIFPVVPRLLnrMFDKIFgqANTPLkRWLLdfATSRKEAELKSGvvrKDSMWdKLIFSKV-QASLGG----RVR 428
Cdd:PRK05691 225 IGGLLQPIFSGVPCVL--MSPAYF--LERPL-RWLE--AISEYGGTISGG---PDFAY-RLCSERVsESALERldlsRWR 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 429 LMITGAAPVSPTVL-TFLRAALGC-----QFYEGYGQTECTAGCTMSLPG--------DWTA----------GHV----G 480
Cdd:PRK05691 294 VAYSGSEPIRQDSLeRFAEKFAACgfdpdSFFASYGLAEATLFVSGGRRGqgipalelDAEAlarnraepgtGSVlmscG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 481 APLPCNFVKLVDVAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGA-VDKAG--WLHTGDIGkWLPNGTLKIIDRKKH 557
Cdd:PRK05691 374 RSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfVEHDGrtWLRTGDLG-FLRDGELFVTGRLKD 452
|
490
....*....|....*.
gi 528467780 558 IFkLAQGEYIAPEKIE 573
Cdd:PRK05691 453 ML-IVRGHNLYPQDIE 467
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
266-605 |
3.38e-15 |
|
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: 78.45 E-value: 3.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 266 PEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIkiteESLKLCPQDVLISFLPLAhmFERVVEGVL--LCHGAkigyf 343
Cdd:cd17652 92 PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQI----AAFDVGPGSRVLQFASPS--FDASVWELLmaLLAGA----- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 344 qgdiRLLMDDLKNLKPtifpvvprllnrmfdkifGQantPLKRWLLDFATSrkEAELKSGVVRKDSmwdklifskvQASL 423
Cdd:cd17652 161 ----TLVLAPAEELLP------------------GE---PLADLLREHRIT--HVTLPPAALAALP----------PDDL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 424 GGRVRLMITGAAPVSPTVLtflRAALGCQFYEGYGQTECTAGCTMSLP-GDWTAGHVGAPLPCNFVKLVDvAEMNYFAAN 502
Cdd:cd17652 204 PDLRTLVVAGEACPAELVD---RWAPGRRMINAYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYVLD-ARLRPVPPG 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 503 GEGEVCVKGPNVFQGYLKDPEQTS--------GAvdKAGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIE 573
Cdd:cd17652 280 VPGELYIAGAGLARGYLNRPGLTAerfvadpfGA--PGSRMYrTGDLARWRADGQLEFLGRADDQVKI-RGFRIELGEVE 356
|
330 340 350
....*....|....*....|....*....|....*
gi 528467780 574 NIYIRSDPVAQ--VFVHGDSL-QACLVGVVVPDPD 605
Cdd:cd17652 357 AALTEHPGVAEavVVVRDDRPgDKRLVAYVVPAPG 391
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
121-605 |
5.47e-15 |
|
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: 78.08 E-value: 5.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGHsQSGDkYIGIFAQNRPEWTISEL------ACYtyslvaVPLYDTLGTEAISYVIDKAS 194
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGV-RPGD-LVAVTLPKGPEQVVAVLgilaagAAY------VPVDIDQPAARREAILADAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 195 ITTIICDiadkarlildcvsgrkhsvttivimesfdSELTAQAQNCGIDIISLKELEAIGKANhkTPIPPKPEDLALICF 274
Cdd:cd12114 85 ARLVLTD-----------------------------GPDAQLDVAVFDVLILDLDALAAPAPP--PPVDVAPDDLAYVIF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 275 TSGTTGNPKGAMLTHGNVVSNCSAfikiTEESLKLCPQDVLISFLPLAhmFERVVEGV--LLCHGAKIgyfqgdirllmd 352
Cdd:cd12114 134 TSGSTGTPKGVMISHRAALNTILD----INRRFAVGPDDRVLALSSLS--FDLSVYDIfgALSAGATL------------ 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 353 dlknlkptifpVVPRLlnrmfdkifGQANTPlKRWlldfatsrKEAELKSGVvrkdSMWDKlifskVQASLGgrvrlMIT 432
Cdd:cd12114 196 -----------VLPDE---------ARRRDP-AHW--------AELIERHGV----TLWNS-----VPALLE-----MLL 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 433 GAAPVSPTVLTFLRAAL-------------------GCQFYEGYGQTECTAGCTM----SLPGDWTAGHVGAPLPCNFVK 489
Cdd:cd12114 233 DVLEAAQALLPSLRLVLlsgdwipldlparlralapDARLISLGGATEASIWSIYhpidEVPPDWRSIPYGRPLANQRYR 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 490 LVDvaemnyfaANGE-------GEVCVKGPNVFQGYLKDPEQTSGA----VDKAGWLHTGDIGKWLPNGTLKIIDRKKHI 558
Cdd:cd12114 313 VLD--------PRGRdcpdwvpGELWIGGRGVALGYLGDPELTAARfvthPDGERLYRTGDLGRYRPDGTLEFLGRRDGQ 384
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 528467780 559 FKLaQGEYIAPEKIENIYIRSDPVAQ--VFVHGDSLQACLVGVVVPDPD 605
Cdd:cd12114 385 VKV-RGYRIELGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPDND 432
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
265-602 |
6.27e-15 |
|
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: 77.86 E-value: 6.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 265 KPEDLALICFTSGTTGNPKGAMLTHGNVVSncsaFIKITEESLKLCPQDVLISFLPLAhmFERVVEG--VLLCHGAKIgy 342
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMIEHQSLVN----LSHGLIKEYGITSSDRVLQFASIA--FDVAAEEiyVTLLSGATL-- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 343 fqgdirllmddlkNLKPtifpvvprllNRMFDKI--FGQANTPLKRWLLDFATSrkeaelksgvvrkdsMWDKLIFSKVQ 420
Cdd:cd17644 176 -------------VLRP----------EEMRSSLedFVQYIQQWQLTVLSLPPA---------------YWHLLVLELLL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 421 ASLGG--RVRLMITGAAPVSPTVLTFLRAALG--CQFYEGYGQTECTAGCTMSLPGDWTAGH-----VGAPLPC------ 485
Cdd:cd17644 218 STIDLpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIANtqvyil 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 486 -NFVKLVDVAEMnyfaangeGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLH--------TGDIGKWLPNGTLKIIDRKK 556
Cdd:cd17644 298 dENLQPVPVGVP--------GELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRID 369
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 528467780 557 HIFKLaQGEYIAPEKIENIYIRSDPVAQ--VFVHGDSL-QACLVGVVVP 602
Cdd:cd17644 370 NQVKI-RGFRIELGEIEAVLSQHNDVKTavVIVREDQPgNKRLVAYIVP 417
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
115-604 |
1.56e-14 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 76.74 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 115 GQPYKWlSYKEVADRAEFAGSALLHRGHSQSGDKYIGIFAQnRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKAS 194
Cdd:cd05928 37 GDEVKW-SFRELGSLSRKAANVLSGACGLQRGDRVAVILPR-VPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 195 ITTIICDiaDKARLILDCVSGRKHSVTT--IVIMESFDSELtaqaqncgidiiSLKELEAIGKANHkTPIPPKPEDLALI 272
Cdd:cd05928 115 AKCIVTS--DELAPEVDSVASECPSLKTklLVSEKSRDGWL------------NFKELLNEASTEH-HCVETGSQEPMAI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 273 CFTSGTTGNPKgaMLTHgnvvSNCSAFIKITEES---LKLCPQDVLISF-------LPLAHMFERVVEG--VLLCHGAKI 340
Cdd:cd05928 180 YFTSGTTGSPK--MAEH----SHSSLGLGLKVNGrywLDLTASDIMWNTsdtgwikSAWSSLFEPWIQGacVFVHHLPRF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 341 gyfqgDIRLLMDDLKNLKPTIFPVVPRLLnRMFdkifgqantplkrwlldfatsrkeaelksgvVRKDsmwdkliFSKVQ 420
Cdd:cd05928 254 -----DPLVILKTLSSYPITTFCGAPTVY-RML-------------------------------VQQD-------LSSYK 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 421 ASlggRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDVaEMNYFA 500
Cdd:cd05928 290 FP---SLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDD-NGNVLP 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 501 ANGEGEVCVK-GPN----VFQGYLKDPEQTSgAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENI 575
Cdd:cd05928 366 PGTEGDIGIRvKPIrpfgLFSGYVDNPEKTA-ATIRGDFYLTGDRGIMDEDGYFWFMGRADDVI-NSSGYRIGPFEVESA 443
|
490 500
....*....|....*....|....*....
gi 528467780 576 YIRSDPVAQVFVhgdslqaclvgVVVPDP 604
Cdd:cd05928 444 LIEHPAVVESAV-----------VSSPDP 461
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
266-577 |
1.93e-14 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 76.39 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 266 PEDLALICFTSGTTGNPKGAMLTHGNVVSN---CSAFIKITEeslklcpQDVLISFLPLAHMFervveGVLLChgakiGY 342
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANqraCLKFFSPKE-------DDVMMSFLPPFHAY-----GFNSC-----TL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 343 FQgdirLLMDdlknlKPTIF---PVVPRLLNRMFDK----IFGqaNTPLkrwLLDF---ATSRKEAELKS-------GVV 405
Cdd:PRK06334 245 FP----LLSG-----VPVVFaynPLYPKKIVEMIDEakvtFLG--STPV---FFDYilkTAKKQESCLPSlrfvvigGDA 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 406 RKDSMWDKlifskvqaslggrvrlmitgaapvspTVLTFLRAALgcqfYEGYGQTECTAGCTMSL---PGDWTAghVGAP 482
Cdd:PRK06334 311 FKDSLYQE--------------------------ALKTFPHIQL----RQGYGTTECSPVITINTvnsPKHESC--VGMP 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 483 LPCNFVKLVDvAEMNYFAANGE-GEVCVKGPNVFQGYL-KDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFK 560
Cdd:PRK06334 359 IRGMDVLIVS-EETKVPVSSGEtGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVK 437
|
330
....*....|....*..
gi 528467780 561 LAqGEYIAPEKIENIYI 577
Cdd:PRK06334 438 IG-AEMVSLEALESILM 453
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
456-604 |
2.38e-14 |
|
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: 74.65 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 456 GYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDVA--EMnyfaANGE-GEVCVKGPNVFQGYLKDPEQTSgAVDKA 532
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDgrEV----PDGEvGEIVARGPTVMAGYWNRPEVNA-RRTRG 216
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528467780 533 GWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIyIRSDP-VAQVFVHGdslqaclvgvvVPDP 604
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSG-AENIYPAEVERC-LRQHPaVADAAVIG-----------VPDP 276
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
121-604 |
2.70e-14 |
|
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: 75.62 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAIsyvidkasittiic 200
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLG-VGKGDR-VFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAI-------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 diadKARLILdcvSGRKHSVTTIVIMESFDseltaqaqncgidiislkeleaigkanhktpippkPEDLALICFTSGTTG 280
Cdd:cd05969 65 ----RDRLEN---SEAKVLITTEELYERTD-----------------------------------PEDPTLLHYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 281 NPKGAMLTHGNVVsncsAFIKITEESLKLCPQDVLIS--------------FLPLAHMFERVVEGvllchgakiGYFqgD 346
Cdd:cd05969 103 TPKGVLHVHDAMI----FYYFTGKYVLDLHPDDIYWCtadpgwvtgtvygiWAPWLNGVTNVVYE---------GRF--D 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 347 IRLLMDDLKNLKPTIFPVVPRLLnRMfdkifgqantpLKRWLLDFATSRKEAELksgvvrkdsmwdklifskvqaslggr 426
Cdd:cd05969 168 AESWYGIIERVKVTVWYTAPTAI-RM-----------LMKEGDELARKYDLSSL-------------------------- 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 427 vRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPG-DWTAGHVGAPLPCNFVKLVDvAEMNYFAANGEG 505
Cdd:cd05969 210 -RFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYPCmPIKPGSMGKPLPGVKAAVVD-ENGNELPPGTKG 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 506 EVCVKG--PNVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSDPVA 583
Cdd:cd05969 288 ILALKPgwPSMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHRVGPFEVESALMEHPAVA 365
|
490 500
....*....|....*....|.
gi 528467780 584 QVFVHGdslqaclvgvvVPDP 604
Cdd:cd05969 366 EAGVIG-----------KPDP 375
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
173-604 |
4.93e-14 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 75.10 E-value: 4.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 173 VAVPLYDTLGTEAISYVIDKASITTIICD-----IADKARLILDcvsgrkHSVTTIVIMESFDSELTaqaqncgiDIISL 247
Cdd:PRK08008 88 IMVPINARLLREESAWILQNSQASLLVTSaqfypMYRQIQQEDA------TPLRHICLTRVALPADD--------GVSSF 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 248 KELEAIGKANHKTPIPPKPEDLALICFTSGTTGNPKGAMLTHGNvvsncsafikiteeslklcpqdvlisfLPLAhmfer 327
Cdd:PRK08008 154 TQLKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYN---------------------------LRFA----- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 328 vvegvllchgakiGYF---QGDIRllMDDlknlkptifpvvpRLLnrmfdkifgqanTPLKRWLLDFATSRKEAELKSG- 403
Cdd:PRK08008 202 -------------GYYsawQCALR--DDD-------------VYL------------TVMPAFHIDCQCTAAMAAFSAGa 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 404 ---VVRKDS---MWDKLifSKVQASLGGRVRLMITG--AAPVSPT--------VLTFLRAA----------LGCQFYEGY 457
Cdd:PRK08008 242 tfvLLEKYSaraFWGQV--CKYRATITECIPMMIRTlmVQPPSANdrqhclreVMFYLNLSdqekdafeerFGVRLLTSY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 458 GQTECTAGCTMSLPGD---WTAghVGAPLPCNFVKLVDvaEMNYFAANGE-GEVCVKG---PNVFQGYLKDPEQTSGAVD 530
Cdd:PRK08008 320 GMTETIVGIIGDRPGDkrrWPS--IGRPGFCYEAEIRD--DHNRPLPAGEiGEICIKGvpgKTIFKEYYLDPKATAKVLE 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528467780 531 KAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIyIRSDPVAQvfvhgdslQACLVGvvVPDP 604
Cdd:PRK08008 396 ADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVELENI-IATHPKIQ--------DIVVVG--IKDS 457
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
125-608 |
5.56e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 75.10 E-value: 5.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 125 EVADRA-EFAGSALLHRGHSQSGDK---------------YIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISY 188
Cdd:PRK07867 16 EDDDRGlYFEDSFTSWREHIRGSAAraaalrarldptrppHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALAR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 189 VIDKASITTIICDiaDKARLILDCVSGrkhSVTTIVIMESFDSELTAQAQNCGIDiislkeleaigkanhktPIPPKPED 268
Cdd:PRK07867 96 DIAHADCQLVLTE--SAHAELLDGLDP---GVRVINVDSPAWADELAAHRDAEPP-----------------FRVADPDD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 269 LALICFTSGTTGNPKGAMLTHGNVVSNCSAFIkiteESLKLCPQDVLISFLPLAHMfERVVEG--VLLCHGAKIGyfqgd 346
Cdd:PRK07867 154 LFMLIFTSGTSGDPKAVRCTHRKVASAGVMLA----QRFGLGPDDVCYVSMPLFHS-NAVMAGwaVALAAGASIA----- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 347 IRL------LMDDLKNLKPTIFPVVPRLLNRMF--DKIFGQANTPLKrwlldfatsrkeaelksgvvrkdsmwdklifsk 418
Cdd:PRK07867 224 LRRkfsasgFLPDVRRYGATYANYVGKPLSYVLatPERPDDADNPLR--------------------------------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 419 vqaslggrvrlMITGAAPVSPTVLTFlRAALGCQFYEGYGQTE----------CTAGCTMSLPGDWTAGHVGAPLPCNFV 488
Cdd:PRK07867 271 -----------IVYGNEGAPGDIARF-ARRFGCVVVDGFGSTEggvaitrtpdTPPGALGPLPPGVAIVDPDTGTECPPA 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 489 KLVDVAEMNYFAANGEgEVCVKGPNVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIA 568
Cdd:PRK07867 339 EDADGRLLNADEAIGE-LVNTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLG 415
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 528467780 569 PEKIENIYIRSDPVAQVFVH-------GDSLQACLVGvvVPDPDFLP 608
Cdd:PRK07867 416 TAPIERILLRYPDATEVAVYavpdpvvGDQVMAALVL--APGAKFDP 460
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
409-605 |
1.43e-13 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 73.37 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 409 SMWDKLIFSKVqASLGGRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSlPGD-WTAGHVGAPLPCNF 487
Cdd:cd05974 185 TVWRMLIQQDL-ASFDVKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNS-PGQpVKAGSMGRPLPGYR 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 488 VKLVDVAEmnyfAANGEGEVCV-----KGPNVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKlA 562
Cdd:cd05974 263 VALLDPDG----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-S 336
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 528467780 563 QGEYIAPEKIENIYIRSDPVAQvfvhgdslqaclvGVVVPDPD 605
Cdd:cd05974 337 SDYRISPFELESVLIEHPAVAE-------------AAVVPSPD 366
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
264-602 |
1.84e-13 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 73.26 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 264 PKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFikitEESLKLCPQDVLISFLPLAHMFervveGVLLCHGAKIGYF 343
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDAL----RQLYGIRPGEVDLATFPLFALF-----GPALGLTSVIPDM 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 344 ------QGDIRLLMDDLKNLKPTIFPVVPRLLNRmfdkifgqantpLKRWLLdfatsRKEAELKSgvvrkdsmwdklifs 417
Cdd:cd05910 153 dptrpaRADPQKLVGAIRQYGVSIVFGSPALLER------------VARYCA-----QHGITLPS--------------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 418 kvqaslggrVRLMITGAAPVSPTVLTFLRAAL--GCQFYEGYGQTECTAGCTM------SLPGDWTAGH----VGAPLPC 485
Cdd:cd05910 201 ---------LRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSIgsrellATTTAATSGGagtcVGRPIPG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 486 NFVKLVDVAEMNYFAANGE--------GEVCVKGPNVFQGYLKDPEQTSGA----VDKAGWLHTGDIGKWLPNGTLKIID 553
Cdd:cd05910 272 VRVRIIEIDDEPIAEWDDTlelprgeiGEITVTGPTVTPTYVNRPVATALAkiddNSEGFWHRMGDLGYLDDEGRLWFCG 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 528467780 554 RKKHIFKLAQGEYIapekieniyirSDPVAQVF-VHGDSLQACLVGVVVP 602
Cdd:cd05910 352 RKAHRVITTGGTLY-----------TEPVERVFnTHPGVRRSALVGVGKP 390
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
274-604 |
5.75e-13 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 71.97 E-value: 5.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 274 FTSGTTGNPKGAMLTH-GNVVSNCSAFIKIteeSLKLCPqdVLISFLPLAHmfervvegvllCHGAKIGY---FQGDIRL 349
Cdd:PLN03102 193 YTSGTTADPKGVVISHrGAYLSTLSAIIGW---EMGTCP--VYLWTLPMFH-----------CNGWTFTWgtaARGGTSV 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 350 LMDDLKnlKPTIFPvvprllNRMFDKIFGQANTP-LKRWLLDfaTSRKEAELKSGVVRkdsmwdklifskvqaslggrvr 428
Cdd:PLN03102 257 CMRHVT--APEIYK------NIEMHNVTHMCCVPtVFNILLK--GNSLDLSPRSGPVH---------------------- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 429 lMITGAAPvSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGD-WTAghvgapLPCN------------FVKLVDVAE 495
Cdd:PLN03102 305 -VLTGGSP-PPAALVKKVQRLGFQVMHAYGLTEATGPVLFCEWQDeWNR------LPENqqmelkarqgvsILGLADVDV 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 496 MN-----YFAANGE--GEVCVKGPNVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIA 568
Cdd:PLN03102 377 KNketqeSVPRDGKtmGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGENIS 454
|
330 340 350
....*....|....*....|....*....|....*.
gi 528467780 569 PEKIENIyirsdpvaqVFVHGDSLQACLVGvvVPDP 604
Cdd:PLN03102 455 SVEVENV---------LYKYPKVLETAVVA--MPHP 479
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
122-610 |
6.21e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 71.90 E-value: 6.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 122 SYKEVADRAEFAGSALLHRGhSQSGDkyigifaqnrpewTISELACYTYSLV----AVPL----YDTLGT----EAISYV 189
Cdd:PRK08162 45 TWAETYARCRRLASALARRG-IGRGD-------------TVAVLLPNIPAMVeahfGVPMagavLNTLNTrldaASIAFM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 190 IDKASITTIICD--IADKARLILDCVSGRKhsvttIVIMESFDSELTaqaqncGIDIISLKELEAI---GKANHkTPIPP 264
Cdd:PRK08162 111 LRHGEAKVLIVDteFAEVAREALALLPGPK-----PLVIDVDDPEYP------GGRFIGALDYEAFlasGDPDF-AWTLP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 265 KPE-DLALICFTSGTTGNPKGAMLTH-G---NVVSNcsafikITEESLKlcPQDVLISFLPLAHmfervvegvllCHG-- 337
Cdd:PRK08162 179 ADEwDAIALNYTSGTTGNPKGVVYHHrGaylNALSN------ILAWGMP--KHPVYLWTLPMFH-----------CNGwc 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 338 ------AKIGYF----QGDIRLLMDDLKNLKPTIF---PVVPRLLnrmfdkifgqANTPlkrwlldfatsrkeAELKSGv 404
Cdd:PRK08162 240 fpwtvaARAGTNvclrKVDPKLIFDLIREHGVTHYcgaPIVLSAL----------INAP--------------AEWRAG- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 405 vrkdsmwdklifskvqasLGGRVRLMITGAAPvSPTVLTFLRAAlGCQFYEGYGQTEcTAG----CTM-----SLPGDWT 475
Cdd:PRK08162 295 ------------------IDHPVHAMVAGAAP-PAAVIAKMEEI-GFDLTHVYGLTE-TYGpatvCAWqpewdALPLDER 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 476 A---GHVGAPLPC-NFVKLVDVAEMNYFAANGE--GEVCVKGPNVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTL 549
Cdd:PRK08162 354 AqlkARQGVRYPLqEGVTVLDPDTMQPVPADGEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYI 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528467780 550 KIIDRKKHIFkLAQGEYIAPEKIENIYIRsdpvaqvfvHgdslQACLVGVVVPDPDflPGW 610
Cdd:PRK08162 433 KIKDRSKDII-ISGGENISSIEVEDVLYR---------H----PAVLVAAVVAKPD--PKW 477
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
121-573 |
2.34e-12 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 70.03 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLY--DTLGTEAiSYVidkasitti 198
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALG-LKPGDR-VALIAETDGDFVEAFFACQYAGLVPVPLPlpMGFGGRE-SYI--------- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 199 icdiaDKARLILDcvSGRKHSVTTIVIMESFDSELTAQAQNC-GIDIISLKELEAIGKAnhkTPiPPKPEDLALICFTSG 277
Cdd:PRK09192 118 -----AQLRGMLA--SAQPAAIITPDELLPWVNEATHGNPLLhVLSHAWFKALPEADVA---LP-RPTPDDIAYLQYSSG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 278 TTGNPKGAMLTHGNVVSNCSAfikITEESLKLCPQDVLISFLPLAH-MfervvegvllchgakigyfqGDIRLLMDDLKN 356
Cdd:PRK09192 187 STRFPRGVIITHRALMANLRA---ISHDGLKVRPGDRCVSWLPFYHdM--------------------GLVGFLLTPVAT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 357 ------LKPTIFPVVP----RLLNR-----MFDKIFGqantplkrwlLDFATSRkeAELKSGVVRKDSMWdklifskvqa 421
Cdd:PRK09192 244 qlsvdyLPTRDFARRPlqwlDLISRnrgtiSYSPPFG----------YELCARR--VNSKDLAELDLSCW---------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 422 slggrvRLMITGAAPVSPTVL-----TFlrAALGCQ---FYEGYGQTECTAGCTMSLPG--------DWTA----GHV-- 479
Cdd:PRK09192 302 ------RVAGIGADMIRPDVLhqfaeAF--APAGFDdkaFMPSYGLAEATLAVSFSPLGsgivveevDRDRleyqGKAva 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 480 --------------GAPLPCNFVKLVDVAEmNYFAANGEGEVCVKGPNVFQGYLKDPEqTSGAVDKAGWLHTGDIGkWLP 545
Cdd:PRK09192 374 pgaetrrvrtfvncGKALPGHEIEIRNEAG-MPLPERVVGHICVRGPSLMSGYFRDEE-SQDVLAADGWLDTGDLG-YLL 450
|
490 500
....*....|....*....|....*...
gi 528467780 546 NGTLKIIDRKKHIFkLAQGEYIAPEKIE 573
Cdd:PRK09192 451 DGYLYITGRAKDLI-IINGRNIWPQDIE 477
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
263-604 |
2.55e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 69.77 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 263 PPKPEDLALICFT-SGTTGNPK------GAMLTHGNVVSncsafikiteESLKLCPQDVLISFLPLAHMFErvVEGVLlc 335
Cdd:PRK06164 176 RAADPDAGALLFTtSGTTSGPKlvlhrqATLLRHARAIA----------RAYGYDPGAVLLAALPFCGVFG--FSTLL-- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 336 hgakiGYFQGDIRLLMDDLKNLKPTIfpvvpRLL-----------NRMFDKIFGQANTPLkrwllDFATSRkeaelksgv 404
Cdd:PRK06164 242 -----GALAGGAPLVCEPVFDAARTA-----RALrrhrvthtfgnDEMLRRILDTAGERA-----DFPSAR--------- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 405 vrkdsmwdklifskvqaslggrvRLMITGAAPVSPTVLTFLRAAlGCQFYEGYGQTECTA---GCTMSLPgdWTAGHVGA 481
Cdd:PRK06164 298 -----------------------LFGFASFAPALGELAALARAR-GVPLTGLYGSSEVQAlvaLQPATDP--VSVRIEGG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 482 PLPCN---FVKLVDVAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHI 558
Cdd:PRK06164 352 GRPASpeaRVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDS 431
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 528467780 559 FKLAqGEYIAPEKIENIYIRSDPVAQVFVHGDSL--QACLVGVVVPDP 604
Cdd:PRK06164 432 LRLG-GFLVNPAEIEHALEALPGVAAAQVVGATRdgKTVPVAFVIPTD 478
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
121-603 |
2.62e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 70.76 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGhsQSGDKYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASIttiic 200
Cdd:PRK12316 4577 LTYAELNRRANRLAHALIARG--VGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGA----- 4649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 diadkaRLILDcvsgRKHSVTTIVIMEsfdseltaqaqncGIDIISL-KELEAIGKANHKTPIPPKPEDLALICFTSGTT 279
Cdd:PRK12316 4650 ------ALLLT----QSHLLQRLPIPD-------------GLASLALdRDEDWEGFPAHDPAVRLHPDNLAYVIYTSGST 4706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 280 GNPKGAMLTHGNVVsncsAFIKITEESLKLCPQDVLISFLPLAhmFERVVEGVL--LCHGAkigyfqgdiRLLMDDLKNL 357
Cdd:PRK12316 4707 GRPKGVAVSHGSLV----NHLHATGERYELTPDDRVLQFMSFS--FDGSHEGLYhpLINGA---------SVVIRDDSLW 4771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 358 KPtifpvvprllNRMFDKIFGQANTplkrwLLDFATsrkeaelksgvvrkdSMWDKLIFSKVQASLGGRVRLMITGAAPV 437
Cdd:PRK12316 4772 DP----------ERLYAEIHEHRVT-----VLVFPP---------------VYLQQLAEHAERDGEPPSLRVYCFGGEAV 4821
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 438 SPTVLT-FLRAALGCQFYEGYGQTECTA-----GCTMSLPGDWTAGHVGAPLPCNFVKLVDVaEMNYFAANGEGEVCVKG 511
Cdd:PRK12316 4822 AQASYDlAWRALKPVYLFNGYGPTETTVtvllwKARDGDACGAAYMPIGTPLGNRSGYVLDG-QLNPLPVGVAGELYLGG 4900
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 512 PNVFQGYLKDPEQTSGAV------DKAGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDPV-- 582
Cdd:PRK12316 4901 EGVARGYLERPALTAERFvpdpfgAPGGRLYrTGDLARYRADGVIDYLGRVDHQVKI-RGFRIELGEIEARLREHPAVre 4979
|
490 500
....*....|....*....|.
gi 528467780 583 AQVFVHGDSLQACLVGVVVPD 603
Cdd:PRK12316 4980 AVVIAQEGAVGKQLVGYVVPQ 5000
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
245-585 |
6.29e-12 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 68.64 E-value: 6.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 245 ISLKELEAIGKANHKTPIPPKP-EDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEESlklCPQDVLISFLPLAH 323
Cdd:PRK05851 129 VTVHDLATAAHTNRSASLTPPDsGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLD---AATDVGCSWLPLYH 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 324 -MfervvegvllchgakigyfqGDIRLLMDDLKN----LKPT-IFPVVP-RLLNrmfdkifgqantplkrWLLDF-ATSR 395
Cdd:PRK05851 206 dM--------------------GLAFLLTAALAGaplwLAPTtAFSASPfRWLS----------------WLSDSrATLT 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 396 KEAELKSGVVRKDSmwdklifSKVQASLGGRVRLMITGAAPVSPTVLT-FLRAALGCQFYEG-----YGQTECTAGCTMS 469
Cdd:PRK05851 250 AAPNFAYNLIGKYA-------RRVSDVDLGALRVALNGGEPVDCDGFErFATAMAPFGFDAGaaapsYGLAESTCAVTVP 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 470 LPG-----------DWTAGH----VGAPLPCNFVKLVDVAEMNYFAANGEGEVCVKGPNVFQGYLKDPeqtsgAVDKAGW 534
Cdd:PRK05851 323 VPGiglrvdevttdDGSGARrhavLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQA-----PIDPDDW 397
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 528467780 535 LHTGDIGkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIyirsdpVAQV 585
Cdd:PRK05851 398 FPTGDLG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERV------AAQV 440
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
121-604 |
9.34e-12 |
|
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: 67.54 E-value: 9.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGHSqSGDKYIGIFAQNrPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:cd05973 1 LTFGELRALSARFANALQELGVG-PGDVVAGLLPRT-PELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 DIADKARLildcvsgrkhsvttivimesfdseltaqaqncgidiislkeleaigkanhktpippkPEDLALICFTSGTTG 280
Cdd:cd05973 79 DAANRHKL---------------------------------------------------------DSDPFVMMFTSGTTG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 281 NPKGAMLThgnvVSNCSAFIKITEESLKLCPQDVL--ISFLPLAHMFERVVEGVLLCHGAKIGYFQG-DIRLLMDDLKNL 357
Cdd:cd05973 102 LPKGVPVP----LRALAAFGAYLRDAVDLRPEDSFwnAADPGWAYGLYYAITGPLALGHPTILLEGGfSVESTWRVIERL 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 358 KPTIF---PVVPRLLnrmfdkifgqantplkrwlldfatsrkeaeLKSGVvrkdsmwdklifsKVQASLGGRVRLMITGA 434
Cdd:cd05973 178 GVTNLagsPTAYRLL------------------------------MAAGA-------------EVPARPKGRLRRVSSAG 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 435 APVSPTVLTFLRAALGCQFYEGYGQTEctagCTMSLPGDWTAGHV------GAPLPCNFVKLVDVAeMNYFAANGEGEVC 508
Cdd:cd05973 215 EPLTPEVIRWFDAALGVPIHDHYGQTE----LGMVLANHHALEHPvhagsaGRAMPGWRVAVLDDD-GDELGPGEPGRLA 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 509 VKGPNV----FQGYLKDPEQTSgavdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSDPVAQ 584
Cdd:cd05973 290 IDIANSplmwFRGYQLPDTPAI----DGGYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFDVESALIEHPAVAE 364
|
490 500
....*....|....*....|
gi 528467780 585 VFVHGdslqaclvgvvVPDP 604
Cdd:cd05973 365 AAVIG-----------VPDP 373
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
427-597 |
1.27e-11 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 67.56 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 427 VRLMITGAAPvSPTVLtFLRAALGCQFYEGYGQTECTAGCTM--------SLPGDwTAGHVGAPLPCNFVKL-----VDV 493
Cdd:PLN02479 313 VHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSETYGPSTVcawkpewdSLPPE-EQARLNARQGVRYIGLegldvVDT 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 494 AEMNYFAANGE--GEVCVKGPNVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEK 571
Cdd:PLN02479 390 KTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGGENISSLE 467
|
170 180
....*....|....*....|....*.
gi 528467780 572 IENIyirsdpvaqVFVHGDSLQACLV 597
Cdd:PLN02479 468 VENV---------VYTHPAVLEASVV 484
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
121-605 |
1.35e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 67.60 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPL---YdtlgTEA-ISYVIDKASIT 196
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQG-LGPGDH-VGIYARNRIEYVEAMLGAFKARAVPVNVnyrY----VEDeLRYLLDDSDAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 197 TIICD--IADKARLILDCVSGRKHsvtTIVIMESFDSELTAQAqncgidiISLKELEAIGKANHKtPIPPKPEDLALICf 274
Cdd:PRK07798 103 ALVYEreFAPRVAEVLPRLPKLRT---LVVVEDGSGNDLLPGA-------VDYEDALAAGSPERD-FGERSPDDLYLLY- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 275 TSGTTGNPKGAMLTH--------GNVVSNCSAFIKITEESLKLCPQDVLISFLPLAHMFervvegvllcHGAkigyfqGD 346
Cdd:PRK07798 171 TGGTTGMPKGVMWRQedifrvllGGRDFATGEPIEDEEELAKRAAAGPGMRRFPAPPLM----------HGA------GQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 347 IRLLMdDLKNLKPTIFPVVPRL-------------LNRMFdkIFGQAntpLKRWLLDFATSRKEAELKSgvvrkdsmwdk 413
Cdd:PRK07798 235 WAAFA-ALFSGQTVVLLPDVRFdadevwrtierekVNVIT--IVGDA---MARPLLDALEARGPYDLSS----------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 414 lifskvqaslggrVRLMITGAAPVSPTVLTFLRAAL-GCQFYEGYGQTECTAGCT-MSLPGdwtAGHVGAPL--PCNFVK 489
Cdd:PRK07798 298 -------------LFAIASGGALFSPSVKEALLELLpNVVLTDSIGSSETGFGGSgTVAKG---AVHTGGPRftIGPRTV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 490 LVDvaEMNYFAANGEGEVCV--KGPNVFQGYLKDPEQTSGA---VDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqG 564
Cdd:PRK07798 362 VLD--EDGNPVEPGSGEIGWiaRRGHIPLGYYKDPEKTAETfptIDGVRYAIPGDRARVEADGTITLLGRGSVCINTG-G 438
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 528467780 565 EYIAPEKIENIyIRSDP-VAQVFVHG---DSLQACLVGVVVPDPD 605
Cdd:PRK07798 439 EKVFPEEVEEA-LKAHPdVADALVVGvpdERWGQEVVAVVQLREG 482
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
428-604 |
1.64e-11 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 67.32 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 428 RLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTE----------------CTAGCTMSlPGD--WTAGHVGAPLPcnfvk 489
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAEglvnytrlddsderifTTQGRPMS-PDDevWVADADGNPLP----- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 490 lvdvaemnyfaaNGE-GEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHifklaQ----G 564
Cdd:PRK10946 377 ------------QGEvGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgG 439
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 528467780 565 EYIAPEKIENIYIRsdpvaqvfvHGDSLQACLVGvvVPDP 604
Cdd:PRK10946 440 EKIAAEEIENLLLR---------HPAVIHAALVS--MEDE 468
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
434-605 |
2.59e-11 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 66.25 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 434 AAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSlPGDWTA--GHVGAPLPCNfVKLVDvAEMNYFAANGEGEVCVKG 511
Cdd:cd05929 253 AAPCPPWVKEQWIDWGGPIIWEYYGGTEGQGLTIIN-GEEWLThpGSVGRAVLGK-VHILD-EDGNEVPPGEIGEVYFAN 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 512 PNVFQgYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRsdpvaqvfvHGDS 591
Cdd:cd05929 330 GPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIA---------HPKV 398
|
170
....*....|....
gi 528467780 592 LQACLVGvvVPDPD 605
Cdd:cd05929 399 LDAAVVG--VPDEE 410
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
272-583 |
4.37e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 65.88 E-value: 4.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 272 ICFTSGTTGNPKGAMLTHGNVVSNcsAFIKITEESLKLCPQDVLisfLPLAHMFErvVEGVLLCH-----GAKIgYFQG- 345
Cdd:PRK07008 181 LCYTSGTTGNPKGALYSHRSTVLH--AYGAALPDAMGLSARDAV---LPVVPMFH--VNAWGLPYsapltGAKL-VLPGp 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 346 --DIRLLMDDLKNLKPTIFPVVPR----LLNRMfdkifgqantplkrwlldfatsrKEAELKsgvvrkdsmwdkliFSKV 419
Cdd:PRK07008 253 dlDGKSLYELIEAERVTFSAGVPTvwlgLLNHM-----------------------REAGLR--------------FSTL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 420 QaslggrvRLMITGAApVSPTVLTFLRAALGCQFYEGYGQTECTA-GCTMSLpgdwTAGHVGAPLPCNFVKL-------- 490
Cdd:PRK07008 296 R-------RTVIGGSA-CPPAMIRTFEDEYGVEVIHAWGMTEMSPlGTLCKL----KWKHSQLPLDEQRKLLekqgrviy 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 491 -VDvaeMNYFAANGE---------GEVCVKGPNVFQGYLKDpeQTSGAVDkaGWLHTGDIGKWLPNGTLKIIDRKKHIFK 560
Cdd:PRK07008 364 gVD---MKIVGDDGRelpwdgkafGDLQVRGPWVIDRYFRG--DASPLVD--GWFPTGDVATIDADGFMQITDRSKDVIK 436
|
330 340
....*....|....*....|...
gi 528467780 561 lAQGEYIAPEKIENIYIRSDPVA 583
Cdd:PRK07008 437 -SGGEWISSIDIENVAVAHPAVA 458
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
264-615 |
4.39e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 66.72 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 264 PKPEDLALICFTSGTTGNPKGAMLTHGNVVsncsAFIKITEESLKLCPQDVLISFLPLAhmFERVVEGVL--LCHGAKIG 341
Cdd:PRK12467 1715 LAPQNLAYVIYTSGSTGRPKGAGNRHGALV----NRLCATQEAYQLSAADVVLQFTSFA--FDVSVWELFwpLINGARLV 1788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 342 YFQGDIRL----LMDDLKNLKPTIFPVVPRLLNRmFDKIFGQANTPLKrwlldfatsrkeaelksgvvrkdsmwdklifs 417
Cdd:PRK12467 1789 IAPPGAHRdpeqLIQLIERQQVTTLHFVPSMLQQ-LLQMDEQVEHPLS-------------------------------- 1835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 418 kvqaslggrVRLMITGAAPVSPTVLTFLRAALG-CQFYEGYGQTECTAGCTMslpgdWTAGH----------VGAPLPCN 486
Cdd:PRK12467 1836 ---------LRRVVCGGEALEVEALRPWLERLPdTGLFNLYGPTETAVDVTH-----WTCRRkdlegrdsvpIGQPIANL 1901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 487 FVKLVDvAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQT------SGAVDKAGWLH-TGDIGKWLPNGTLKIIDRKKHIF 559
Cdd:PRK12467 1902 STYILD-ASLNPVPIGVAGELYLGGVGLARGYLNRPALTaerfvaDPFGTVGSRLYrTGDLARYRADGVIEYLGRIDHQV 1980
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 528467780 560 KLaQGEYIAPEKIENIYIRSDPVAQ--VFVHGDSLQACLVGVVVPDPDFLPGWAKNRG 615
Cdd:PRK12467 1981 KI-RGFRIELGEIEARLREQGGVREavVIAQDGANGKQLVAYVVPTDPGLVDDDEAQV 2037
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
260-606 |
1.83e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 63.94 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 260 TPIPPKPEDLALIcFTSGTTGNPKG--AMLTHGNVVSN------CSAFIKITEESLKLCPQdvlisflPLAHMFERVVEG 331
Cdd:PRK13391 148 TPIADESLGTDML-YSSGTTGRPKGikRPLPEQPPDTPlpltafLQRLWGFRSDMVYLSPA-------PLYHSAPQRAVM 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 332 VLLCHGAKIgyfqgdirLLMDD---------LKNLKPTIFPVVPRLLNRMfdkifgqantpLKrwlLDFATsRKEAELKS 402
Cdd:PRK13391 220 LVIRLGGTV--------IVMEHfdaeqylalIEEYGVTHTQLVPTMFSRM-----------LK---LPEEV-RDKYDLSS 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 403 gvvrkdsmwdklifskvqaslggrVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTEcTAGCTMSLPGDWTA--GHVG 480
Cdd:PRK13391 277 ------------------------LEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATE-GLGFTACDSEEWLAhpGTVG 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 481 APLpcnFVKLVDVAEMNYFAANGE-GEVCVKGPNVFQgYLKDPEQTSGAVD-KAGWLHTGDIGKWLPNGTLKIIDRKKHI 558
Cdd:PRK13391 332 RAM---FGDLHILDDDGAELPPGEpGTIWFEGGRPFE-YLNDPAKTAEARHpDGTWSTVGDIGYVDEDGYLYLTDRAAFM 407
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 528467780 559 FkLAQGEYIAPEKIENIYIRSDPVAQVFVHGdslqaclvgvvVPDPDF 606
Cdd:PRK13391 408 I-ISGGVNIYPQEAENLLITHPKVADAAVFG-----------VPNEDL 443
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
266-613 |
2.27e-10 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 63.34 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 266 PEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFikitEESLKLCPQD---VLISFLPLAHMFERVVEgvlLCHGAKIGY 342
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWH----RPYFGVTPADkslVYASFSFDASAWEIFPH---LTAGAALHV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 343 FQGDIRLLMDDLknlkptifpvvprllNRMFDKifgqantplKRWLLDFatsrkeaeLKSGVVRKDSMWDKLIFskvqas 422
Cdd:cd17645 176 VPSERRLDLDAL---------------NDYFNQ---------EGITISF--------LPTGAAEQFMQLDNQSL------ 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 423 lggrvRLMITGAAPVSPTVLTflraalGCQFYEGYGQTECTAGCTMsLPGDWTAGHVGAPLPCNFVKLVDVAEMNYFAAN 502
Cdd:cd17645 218 -----RVLLTGGDKLKKIERK------GYKLVNNYGPTENTVVATS-FEIDKPYANIPIGKPIDNTRVYILDEALQLQPI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 503 G-EGEVCVKGPNVFQGYLKDPEQTSGA------VDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 575
Cdd:cd17645 286 GvAGELCIAGEGLARGYLNRPELTAEKfivhpfVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIEPF 364
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 528467780 576 YIRSDPVAQVFV----HGDSLQAcLVGVVVP----DPDFLPGWAKN 613
Cdd:cd17645 365 LMNHPLIELAAVlakeDADGRKY-LVAYVTApeeiPHEELREWLKN 409
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
266-608 |
2.75e-10 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 63.19 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 266 PEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEESlklCPQDVLISFLPlAHMFERVVEGVLLchgAKIGyfqG 345
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGR---DNGDEAVLFFS-NYVFDFFVEQMTL---ALLN---G 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 346 DIRLLMDDLKNLKPTIFpvvPRLLNRmfDKIFGQANTPLKRWLLDFAtsrkeaelksgvvRKDSMwdklifskvqaslgg 425
Cdd:cd17648 163 QKLVVPPDEMRFDPDRF---YAYINR--EKVTYLSGTPSVLQQYDLA-------------RLPHL--------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 426 rvRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSL--PGDWTAGHVGAPLPCNFVKLVDvAEMNYFAANG 503
Cdd:cd17648 210 --KRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRFfpGDQRFDKSLGRPVRNTKCYVLN-DAMKRVPVGA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 504 EGEVCVKGPNVFQGYLKDPEQTS---------GAVDKA----GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAP 569
Cdd:cd17648 287 VGELYLGGDGVARGYLNRPELTAerflpnpfqTEQERArgrnARLYkTGDLVRWLPSGELEYLGRNDFQVKI-RGQRIEP 365
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 528467780 570 EKIENIYIRSDPVAQVFV--------HGDSLQACLVGVVVPDPDFLP 608
Cdd:cd17648 366 GEVEAALASYPGVRECAVvakedasqAQSRIQKYLVGYYLPEPGHVP 412
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
121-603 |
6.07e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 63.05 E-value: 6.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGhsQSGDKYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKAsittiic 200
Cdd:PRK12316 3083 LSYAELNRRANRLAHRLIERG--VGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDS------- 3153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 diadKARLILDcvsgrkhsvttivimesfdSELTAQAQNCGIDIISLkELEAIGKANHKTPIPPKPEDLALICFTSGTTG 280
Cdd:PRK12316 3154 ----GAQLLLS-------------------QSHLRLPLAQGVQVLDL-DRGDENYAEANPAIRTMPENLAYVIYTSGSTG 3209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 281 NPKGAMLTHGNVvsncSAFIKITEESLKLCPQDVLISFLPLAHMFERVVEGVLLCHGAKIgyFQGDIRLLMDdlknlkpt 360
Cdd:PRK12316 3210 KPKGVGIRHSAL----SNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARV--VLAGPEDWRD-------- 3275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 361 ifpvvPRLLNRMFDKifGQANTPLKRWlldfatsrkeaelksgvvrkdSMWDKLIFSKVQASLGGrVRLMITGAAPVSPT 440
Cdd:PRK12316 3276 -----PALLVELINS--EGVDVLHAYP---------------------SMLQAFLEEEDAHRCTS-LKRIVCGGEALPAD 3326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 441 VLTflRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGH--VGAPLPCNFVKLVDVAeMNYFAANGEGEVCVKGPNVFQGY 518
Cdd:PRK12316 3327 LQQ--QVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILDGS-LEPVPVGALGELYLGGEGLARGY 3403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 519 LKDPEQT------SGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDPVAQVFVHGDSL 592
Cdd:PRK12316 3404 HNRPGLTaerfvpDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKI-RGFRIELGEIEARLLEHPWVREAVVLAVDG 3482
|
490
....*....|.
gi 528467780 593 QAcLVGVVVPD 603
Cdd:PRK12316 3483 RQ-LVAYVVPE 3492
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
101-609 |
6.68e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 61.97 E-value: 6.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 101 RVSNNGPCLGSRkaGQPYKWLSY-KEVADRAEFAGSAllhrgHSQSGDKYIGIFAQNRPEWTISELACYTYSLVAVPLYD 179
Cdd:PRK13388 12 RAGDDTIAVRYG--DRTWTWREVlAEAAARAAALIAL-----ADPDRPLHVGVLLGNTPEMLFWLAAAALGGYVLVGLNT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 180 TLGTEAISYVIDKASITTIICDIADKARLI-LDcVSGrkhsVTTIVIMESFDSELTAQAQncgidiiSLKELEAIGkanh 258
Cdd:PRK13388 85 TRRGAALAADIRRADCQLLVTDAEHRPLLDgLD-LPG----VRVLDVDTPAYAELVAAAG-------ALTPHREVD---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 259 ktpippkPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIkiteESLKLCPQDVLISFLPLAHMfERVVEG--VLLCH 336
Cdd:PRK13388 149 -------AMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALT----ERFGLTRDDVCYVSMPLFHS-NAVMAGwaPAVAS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 337 GAKIGY--------FQGDIRLLmddlknlKPTIFPVVPRLL-------NRMFDkifgqANTPLKRWLLDFATSRKEAElk 401
Cdd:PRK13388 217 GAAVALpakfsasgFLDDVRRY-------GATYFNYVGKPLayilatpERPDD-----ADNPLRVAFGNEASPRDIAE-- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 402 sgvvrkdsmwdklifskvqaslggrvrlmitgaapvsptvltFLRAaLGCQFYEGYGQTEctAGCTMSLPGDWTAGHVGA 481
Cdd:PRK13388 283 ------------------------------------------FSRR-FGCQVEDGYGSSE--GAVIVVREPGTPPGSIGR 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 482 PLPCnfVKLVD--------VAEmnyFAANGE--------GE-VCVKGPNVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWL 544
Cdd:PRK13388 318 GAPG--VAIYNpetltecaVAR---FDAHGAllnadeaiGElVNTAGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRD 391
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528467780 545 PNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDPVAQVFVH-------GDSLQACLvgVVVPDPDFLPG 609
Cdd:PRK13388 392 ADGWIYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYavpdervGDQVMAAL--VLRDGATFDPD 460
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
122-604 |
1.09e-09 |
|
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: 61.44 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 122 SYKEV-ADRAEFAGsALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAI-SYVIDKASITTII 199
Cdd:cd17634 86 SYRELhREVCRFAG-TLLDLG-VKKGDR-VAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVaGRIIDSSSRLLIT 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 200 CD-------IADKARLILDCVSGRKHSVTTIVIMESFDSELTAQAqncGIDIiSLKELEAIGKANHKtPIPPKPEDLALI 272
Cdd:cd17634 163 ADggvragrSVPLKKNVDDALNPNVTSVEHVIVLKRTGSDIDWQE---GRDL-WWRDLIAKASPEHQ-PEAMNAEDPLFI 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 273 CFTSGTTGNPKGAMLTHGnvvsncsAFIKITEESLKLC----PQDVLISFLPLAHMFER--VVEGVLLChGAKIGYFQGd 346
Cdd:cd17634 238 LYTSGTTGKPKGVLHTTG-------GYLVYAATTMKYVfdygPGDIYWCTADVGWVTGHsyLLYGPLAC-GATTLLYEG- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 347 irllmddlKNLKPTifpvvPRLLNRMFDK----IFGQANTPLKrwlldfatsrkeAELKSGvvrkdsmwDKLIFSKVQAS 422
Cdd:cd17634 309 --------VPNWPT-----PARMWQVVDKhgvnILYTAPTAIR------------ALMAAG--------DDAIEGTDRSS 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 423 LggrvRLMITGAAPVSPTVLTFLRAALG---CQFYEGYGQTECTAGCTMSLPG--DWTAGHVGAPLPCNFVKLVDvAEMN 497
Cdd:cd17634 356 L----RILGSVGEPINPEAYEWYWKKIGkekCPVVDTWWQTETGGFMITPLPGaiELKAGSATRPVFGVQPAVVD-NEGH 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 498 YFAANGEGEVCVKG--PNVFQGYLKDPE---QTSGAVDKAGWLHtGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKI 572
Cdd:cd17634 431 PQPGGTEGNLVITDpwPGQTRTLFGDHErfeQTYFSTFKGMYFS-GDGARRDEDGYYWITGRSDDVINVA-GHRLGTAEI 508
|
490 500 510
....*....|....*....|....*....|..
gi 528467780 573 ENIYIrSDPVAQvfvhgdslQACLVGvvVPDP 604
Cdd:cd17634 509 ESVLV-AHPKVA--------EAAVVG--IPHA 529
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
427-606 |
1.47e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 61.07 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 427 VRLMITGAAPVSPTVLtflRAAL---GCQFYEGYGQTEcTAGCTMSLPGDWTA--GHVGAPLPCNfVKLVDvAEMNYFAA 501
Cdd:PRK08276 264 LRVAIHAAAPCPVEVK---RAMIdwwGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGE-VRILD-EDGNELPP 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 502 NGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGkWL-PNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSD 580
Cdd:PRK08276 338 GEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVG-YLdEDGYLYLTDRKSDMI-ISGGVNIYPQEIENLLVTHP 415
|
170 180
....*....|....*....|....*.
gi 528467780 581 PVAQVFVHGdslqaclvgvvVPDPDF 606
Cdd:PRK08276 416 KVADVAVFG-----------VPDEEM 430
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
121-603 |
3.87e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 60.36 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGhsQSGDKYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERG--VGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLS 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 DIADKARLILDcvsgrkhsvttivimesfdseltAQAQNCGIDIISLkELEAIGKANHKTPIppKPEDLALICFTSGTTG 280
Cdd:PRK12316 615 QSHLGRKLPLA-----------------------AGVQVLDLDRPAA-WLEGYSEENPGTEL--NPENLAYVIYTSGSTG 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 281 NPKGAMLTHGNVVsncsAFIKITEESLKLCPQDVLISFLPLAhmFERVVEGVL--LCHGAkigyfqgdiRLLmddlknlk 358
Cdd:PRK12316 669 KPKGAGNRHRALS----NRLCWMQQAYGLGVGDTVLQKTPFS--FDVSVWEFFwpLMSGA---------RLV-------- 725
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 359 ptifpVVPRLLNRMFDKIFGQANTPLKRwLLDFATSRKEAELKSGVVrkdsmwdklifskvqASLGGRVRLMITGAAPVS 438
Cdd:PRK12316 726 -----VAAPGDHRDPAKLVELINREGVD-TLHFVPSMLQAFLQDEDV---------------ASCTSLRRIVCSGEALPA 784
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 439 PTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHV--GAPLPCNFVKLVDvAEMNYFAANGEGEVCVKGPNVFQ 516
Cdd:PRK12316 785 DAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGGDSVpiGRPIANLACYILD-ANLEPVPVGVLGELYLAGRGLAR 863
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 517 GYLKDPEQT------SGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDPVAQVFVHG- 589
Cdd:PRK12316 864 GYHGRPGLTaerfvpSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL-RGLRIELGEIEARLLEHPWVREAAVLAv 942
|
490
....*....|....
gi 528467780 590 DSLQacLVGVVVPD 603
Cdd:PRK12316 943 DGKQ--LVGYVVLE 954
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
266-603 |
4.28e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 60.17 E-value: 4.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 266 PEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFikitEESLKLCPQDVLISFLPLAhmFERVVEGVL--LCHGAKIGYF 343
Cdd:PRK12467 3236 GENLAYVIYTSGSTGKPKGVGVRHGALANHLCWI----AEAYELDANDRVLLFMSFS--FDGAQERFLwtLICGGCLVVR 3309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 344 QGDIRllmddlknlkptifpvvprllnrmfdkifgqanTPLKRW---------LLDFATSRKEAELKSGVVRKdsmwdkl 414
Cdd:PRK12467 3310 DNDLW---------------------------------DPEELWqaihahrisIACFPPAYLQQFAEDAGGAD------- 3349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 415 ifskvqaslGGRVRLMITGAAPVSPTVLTFLRAALG-CQFYEGYGQTECTAGCTMslpgdWTAGHVGAPLPCNFVKLVDV 493
Cdd:PRK12467 3350 ---------CASLDIYVFGGEAVPPAAFEQVKRKLKpRGLTNGYGPTEAVVTVTL-----WKCGGDAVCEAPYAPIGRPV 3415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 494 AEMNYFAANGE---------GEVCVKGPNVFQGY-----------LKDPEQTSGavdkaGWLH-TGDIGKWLPNGTLKII 552
Cdd:PRK12467 3416 AGRSIYVLDGQlnpvpvgvaGELYIGGVGLARGYhqrpsltaerfVADPFSGSG-----GRLYrTGDLARYRADGVIEYL 3490
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 528467780 553 DRKKHIFKLaQGEYIAPEKIENIYIRSDPVAQ-VFVHGDSLQAC-LVGVVVPD 603
Cdd:PRK12467 3491 GRIDHQVKI-RGFRIELGEIEARLLQHPSVREaVVLARDGAGGKqLVAYVVPA 3542
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
252-575 |
2.21e-08 |
|
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: 57.06 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 252 AIGKANHKtPIPPKPE-DLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEESLKlcPQDVLISFLPLAHmfervVE 330
Cdd:cd05915 138 EEALGEEA-DPVRVPErAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALS--EKDVVLPVVPMFH-----VN 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 331 GvlLCHGAKIGYFQGDIRLLMDDLKNlkptifpvvprllNRMFDKIfgqantpLKRWLLDFATSRKEAELKSGVvrKDSm 410
Cdd:cd05915 210 A--WCLPYAATLVGAKQVLPGPRLDP-------------ASLVELF-------DGEGVTFTAGVPTVWLALADY--LES- 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 411 wdklifskVQASLGGRVRLMITGAAPvsPTVLTFLRAALGCQFYEGYGQTEC----TAGCTM----SLPGDWTAGHVGAP 482
Cdd:cd05915 265 --------TGHRLKTLRRLVVGGSAA--PRSLIARFERMGVEVRQGYGLTETspvvVQNFVKshleSLSEEEKLTLKAKT 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 483 LPCNFVKLVDVAEMNYFAANGEGE----VCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHI 558
Cdd:cd05915 335 GLPIPLVRLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDL 414
|
330
....*....|....*..
gi 528467780 559 FKLAqGEYIAPEKIENI 575
Cdd:cd05915 415 IKSG-GEWISSVDLENA 430
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
270-597 |
2.57e-08 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 57.35 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 270 ALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKiteESLKLCPQDVLIS--------------FLPLAHMFERVVEGVLLc 335
Cdd:PRK06060 148 AYATYTSGTTGPPKAAIHRHADPLTFVDAMCR---KALRLTPEDTGLCsarmyfayglgnsvWFPLATGGSAVINSAPV- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 336 hGAKIGYFQGdirllmddlKNLKPTIFPVVPRLLNRMFDkifgqANTPlkrwlldfatsrkeaelksgvvrkDSMWDkli 415
Cdd:PRK06060 224 -TPEAAAILS---------ARFGPSVLYGVPNFFARVID-----SCSP------------------------DSFRS--- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 416 fskvqaslggrVRLMITGAAPVSPTVLTFLRAALG-CQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLV--D 492
Cdd:PRK06060 262 -----------LRCVVSAGEALELGLAERLMEFFGgIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVapD 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 493 VAEMnyfAANGEGEVCVKGPNVFQGYLKDPEQTsgaVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIfKLAQGEYIAPEKI 572
Cdd:PRK06060 331 GTTA---GPGVEGDLWVRGPAIAKGYWNRPDSP---VANEGWLDTRDRVCIDSDGWVTYRCRADDT-EVIGGVNVDPREV 403
|
330 340 350
....*....|....*....|....*....|..
gi 528467780 573 ENIYIRSDPVAQVFVHG-------DSLQACLV 597
Cdd:PRK06060 404 ERLIIEDEAVAEAAVVAvrestgaSTLQAFLV 435
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
121-606 |
3.18e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 56.86 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRpEWTISELACYTYSLVAVPLYDT-LGTEAISYVIDKASITTII 199
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALG-VRAGDG-VAVLARNH-RGFVLALYAAGKVGARIILLNTgFSGPQLAEVAAREGVKALV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 200 CD--IADKARLILDCVSGrkhsVTTIVIMESFDSELTAQAQncgidiiSLKELEAiGKANHKTPIPPKPEdlALICFTSG 277
Cdd:PRK07788 152 YDdeFTDLLSALPPDLGR----LRAWGGNPDDDEPSGSTDE-------TLDDLIA-GSSTAPLPKPPKPG--GIVILTSG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 278 TTGNPKGAmlthgnvvsncsafikiteeslklcPQDVLISFLPLAHMFERV---VEGVLLC-----HG-----AKIGYFQ 344
Cdd:PRK07788 218 TTGTPKGA-------------------------PRPEPSPLAPLAGLLSRVpfrAGETTLLpapmfHAtgwahLTLAMAL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 345 G---------DIRLLMDDLKNLKPTIFPVVPRLLNRMFDKifgqantpLKRWLLDFATSrkeaelksgvvrkdSMwdKLI 415
Cdd:PRK07788 273 GstvvlrrrfDPEATLEDIAKHKATALVVVPVMLSRILDL--------GPEVLAKYDTS--------------SL--KII 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 416 FSkvqaslggrvrlmiTGAApVSPTVLTFLRAALGCQFYEGYGQTECtAGCTMSLPGDWTA--GHVGAPLPCNFVKLVDv 493
Cdd:PRK07788 329 FV--------------SGSA-LSPELATRALEAFGPVLYNLYGSTEV-AFATIATPEDLAEapGTVGRPPKGVTVKILD- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 494 AEMNYFAANGEGEVCVKGPNVFQGYlkdpeqTSGA----VDkaGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAP 569
Cdd:PRK07788 392 ENGNEVPRGVVGRIFVGNGFPFEGY------TDGRdkqiID--GLLSSGDVGYFDEDGLLFVDGRDDDMI-VSGGENVFP 462
|
490 500 510
....*....|....*....|....*....|....*..
gi 528467780 570 EKIENIYIRSDPVAQVFVHGdslqaclvgvvVPDPDF 606
Cdd:PRK07788 463 AEVEDLLAGHPDVVEAAVIG-----------VDDEEF 488
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
119-290 |
6.45e-08 |
|
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: 55.96 E-value: 6.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 119 KWLSYKEVADRAEFAGSALLHRGHSQsGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTI 198
Cdd:cd05968 90 RTLTYGELLYEVKRLANGLRALGVGK-GDR-VGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKAL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 199 IcdIAD----KARLI-----LDCVSGRKHSVTTIVIMESFDSELTAQAQNcgiDIISLKELEAIGKANHKTpippKPEDL 269
Cdd:cd05968 168 I--TADgftrRGREVnlkeeADKACAQCPTVEKVVVVRHLGNDFTPAKGR---DLSYDEEKETAGDGAERT----ESEDP 238
|
170 180
....*....|....*....|.
gi 528467780 270 ALICFTSGTTGNPKGAMLTHG 290
Cdd:cd05968 239 LMIIYTSGTTGKPKGTVHVHA 259
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
121-293 |
1.14e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 54.90 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:PRK04319 74 YTYKELKELSNKFANVLKELG-VEKGDR-VFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLIT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 201 DIADKARLILDCVSGRKHSVttivimesfdseLTAQAQNCGIDIISLKELEAigKANHKTPIPP-KPEDLALICFTSGTT 279
Cdd:PRK04319 152 TPALLERKPADDLPSLKHVL------------LVGEDVEEGPGTLDFNALME--QASDEFDIEWtDREDGAILHYTSGST 217
|
170
....*....|....
gi 528467780 280 GNPKGAMLTHGNVV 293
Cdd:PRK04319 218 GKPKGVLHVHNAML 231
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
428-606 |
1.16e-07 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 54.70 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 428 RLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTEcTAGCTMSLPGDWTA--GHVGAPLPCNFVKLVDvAEMNYFAANGEG 505
Cdd:PRK12406 274 RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE-SGAVTFATSEDALShpGTVGKAAPGAELRFVD-EDGRPLPQGEIG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 506 EVCVKGPNV--FQgYLKDPEQTSgAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVA 583
Cdd:PRK12406 352 EIYSRIAGNpdFT-YHNKPEKRA-EIDRGGFITSGDVGYLDADGYLFLCDRKRDMV-ISGGVNIYPAEIEAVLHAVPGVH 428
|
170 180
....*....|....*....|...
gi 528467780 584 QVFVHGdslqaclvgvvVPDPDF 606
Cdd:PRK12406 429 DCAVFG-----------IPDAEF 440
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
270-589 |
1.95e-07 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 54.37 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 270 ALICFTSGTTGNPKGAMLTH-GNVVSncsAFIKITEESLKLCPQDVLISFLPLAHM------FERVVEGV-LLCHGAKIg 341
Cdd:PRK06018 180 AGMCYTSGTTGDPKGVLYSHrSNVLH---ALMANNGDALGTSAADTMLPVVPLFHAnswgiaFSAPSMGTkLVMPGAKL- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 342 yfqgDIRLLMDDLKNLKPTIFPVVPRLlnrmfdkifgqantplkrWLLDFATSRKEaelksgvvrkdsmwdklifskvQA 421
Cdd:PRK06018 256 ----DGASVYELLDTEKVTFTAGVPTV------------------WLMLLQYMEKE----------------------GL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 422 SLGGRVRLMITGAAPVSPTVLTFLRaaLGCQFYEGYGQTECTAGCTMS--------LPGD----WTAGHVGAPLPCNfVK 489
Cdd:PRK06018 292 KLPHLKMVVCGGSAMPRSMIKAFED--MGVEVRHAWGMTEMSPLGTLAalkppfskLPGDarldVLQKQGYPPFGVE-MK 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 490 LVDVAEmNYFAANGE--GEVCVKGPNVFQGYLK-DPEQtsgaVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEY 566
Cdd:PRK06018 369 ITDDAG-KELPWDGKtfGRLKVRGPAVAAAYYRvDGEI----LDDDGFFDTGDVATIDAYGYMRITDRSKDVIK-SGGEW 442
|
330 340
....*....|....*....|...
gi 528467780 567 IAPEKIENIYIRSDPVAQVFVHG 589
Cdd:PRK06018 443 ISSIDLENLAVGHPKVAEAAVIG 465
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
264-614 |
3.21e-07 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 53.13 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 264 PKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAfikiTEESLKLCPQDVLIsfLPLAHmfervvegvllchgakIGYF 343
Cdd:PRK07824 32 PIDDDVALVVATSGTTGTPKGAMLTAAALTASADA----THDRLGGPGQWLLA--LPAHH----------------IAGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 344 QGDIRLLmddLKNLKPTIFPVvprllNRMFDkifgqantplkrwLLDFAtsRKEAELKSGvvRKDSMWDKLIFSKVQASL 423
Cdd:PRK07824 90 QVLVRSV---IAGSEPVELDV-----SAGFD-------------PTALP--RAVAELGGG--RRYTSLVPMQLAKALDDP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 424 GGRVRL-----MITGAAPVSPTVLTflRA-ALGCQFYEGYGQTECTAGCTMSlpgdwtaghvGAPLPCNFVKLVDvaemn 497
Cdd:PRK07824 145 AATAALaeldaVLVGGGPAPAPVLD--AAaAAGINVVRTYGMSETSGGCVYD----------GVPLDGVRVRVED----- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 498 yfaangeGEVCVKGPNVFQGYLKDPEQtsGAVDKAGWLHTGDIGKwLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYI 577
Cdd:PRK07824 208 -------GRIALGGPTLAKGYRNPVDP--DPFAEPGWFRTDDLGA-LDDGVLTVLGRADDAISTG-GLTVLPQVVEAALA 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 528467780 578 RSDPVAQVFVHG---DSLQACLVGVVVPDP--------------DFLPGWAKNR 614
Cdd:PRK07824 277 THPAVADCAVFGlpdDRLGQRVVAAVVGDGgpaptlealrahvaRTLDRTAAPR 330
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
263-324 |
8.52e-07 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 52.29 E-value: 8.52e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528467780 263 PPKPEDLALICFTSGTTGNPKGAMLTHGNVVSnCSAFIKITeeslKLCPQDVLISFLPLAHM 324
Cdd:cd05938 140 HVTIKSPALYIYTSGTTGLPKAARISHLRVLQ-CSGFLSLC----GVTADDVIYITLPLYHS 196
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
267-591 |
1.07e-06 |
|
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: 51.71 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 267 EDLALICFTSGTTGNPKGAMLTHGNVVsNCSAFIKitEESLKLCPQDVL----ISFlplAHMFERVVEGvlLCHGAKIGY 342
Cdd:cd17656 128 DDLLYIIYTSGTTGKPKGVQLEHKNMV-NLLHFER--EKTNINFSDKVLqfatCSF---DVCYQEIFST--LLSGGTLYI 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 343 FQGDIRLLMDDLKNLKPT------IFPVVprLLNRMFDkifgqantpLKRWLLDFATSRKEaelksgvvrkdsmwdkLIF 416
Cdd:cd17656 200 IREETKRDVEQLFDLVKRhnievvFLPVA--FLKFIFS---------EREFINRFPTCVKH----------------IIT 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 417 SKVQaslggrvrLMITgaapvSPTVLTFLRAalGCQFYEGYG--QTECTAGCTMSLPGDWTA-GHVGAPLPCNFVKLVDv 493
Cdd:cd17656 253 AGEQ--------LVIT-----NEFKEMLHEH--NVHLHNHYGpsETHVVTTYTINPEAEIPElPPIGKPISNTWIYILD- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 494 AEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSgavDK---------AGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQG 564
Cdd:cd17656 317 QEQQLQPQGIVGELYISGASVARGYLNRQELTA---EKffpdpfdpnERMYRTGDLARYLPDGNIEFLGRADHQVKI-RG 392
|
330 340
....*....|....*....|....*....
gi 528467780 565 EYIAPEKIENIYIRSDPVAQ--VFVHGDS 591
Cdd:cd17656 393 YRIELGEIEAQLLNHPGVSEavVLDKADD 421
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
272-574 |
1.10e-06 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 51.25 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 272 ICFTSGTTGNPKGAMLTHGNVVsncsAFIKITEESLKLCPQDVLISFLPLAH-MFERVVEGVLLCHGAKIGYFQGDIRLL 350
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERSWI----ESFVCNEDLFNISGEDAILAPGPLSHsLFLYGAISALYLGGTFIGQRKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 351 MDDLKNLKPTIFPVVPRLLNRMFdkifgqantplkrwlldfATSRKEAELKSgVVRKDSMWDKLIFSKVQAslggrvrlm 430
Cdd:cd17633 81 IRKINQYNATVIYLVPTMLQALA------------------RTLEPESKIKS-IFSSGQKLFESTKKKLKN--------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 431 itgAAPVSptvltflraalgcQFYEGYGQTEcTAGCTMSLPGD-WTAGHVGAPLPCNFVKLVDvaemnyfAANGE-GEVC 508
Cdd:cd17633 133 ---IFPKA-------------NLIEFYGTSE-LSFITYNFNQEsRPPNSVGRPFPNVEIEIRN-------ADGGEiGKIF 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528467780 509 VKGPNVFQGYLKdpeqtSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIEN 574
Cdd:cd17633 189 VKSEMVFSGYVR-----GGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIES 248
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
241-294 |
1.55e-06 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 51.43 E-value: 1.55e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 528467780 241 GIDIISLKELEAIGKAnhKTPIPP----KPEDLALICFTSGTTGNPKGAMLTHGNVVS 294
Cdd:PRK04813 115 GIPVITLDELKDIFAT--GNPYDFdhavKGDDNYYIIFTSGTTGKPKGVQISHDNLVS 170
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
268-605 |
2.21e-06 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 50.82 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 268 DLALICFTSGTTGNPKGAMLTHGNVVSNCSAFikitEESLKLCPQDVLISFLPLAHmfervVEGVLLC------HGAKI- 340
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFF----AGSGGALPSDVLYTCLPLYH-----STALIVGwsaclaSGATLv 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 341 -------GYFQGDIRllmddlKNlKPTIFPVVPRLLnrmfdkifgqantplkRWLLdfATSRKEAELKSGVVR------K 407
Cdd:cd05940 153 irkkfsaSNFWDDIR------KY-QATIFQYIGELC----------------RYLL--NQPPKPTERKHKVRMifgnglR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 408 DSMWDKLIfskvqaslggrVRLMItgaapvsPTVLTFlraalgcqfyegYGQTECTAGCTMSLPGDWTAGHVGAPLPCNF 487
Cdd:cd05940 208 PDIWEEFK-----------ERFGV-------PRIAEF------------YAATEGNSGFINFFGKPGAIGRNPSLLRKVA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 488 -VKLVDVAEMNYFAANGEGEVCVKGP--------------NVFQGYLKDPEQTSGA---VDKAG--WLHTGDIGKWLPNG 547
Cdd:cd05940 258 pLALVKYDLESGEPIRDAEGRCIKVPrgepgllisrinplEPFDGYTDPAATEKKIlrdVFKKGdaWFNTGDLMRLDGEG 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 528467780 548 TLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDPVAQVFVHgdslqaclvGVVVPDPD 605
Cdd:cd05940 338 FWYFVDRLGDTFRW-KGENVSTTEVAAVLGAFPGVEEANVY---------GVQVPGTD 385
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
267-323 |
3.10e-06 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 50.26 E-value: 3.10e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 528467780 267 EDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIkiteESLKLCPQDVLISFLPLAH 323
Cdd:PRK08279 199 KDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFG----GLLRLTPDDVLYCCLPLYH 251
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
241-598 |
4.03e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 50.55 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 241 GIDIISLKELEAIGKANHKTPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNcsafIKITEESLKLCPQDVLISFLP 320
Cdd:PRK05691 1247 GVSAIALDSLHLDSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAER----LQWMQATYALDDSDVLMQKAP 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 321 LA------HMFERVVEG---VLLCHGAkigyfQGDIRLLMDDLKNLKPTIFPVVPRLLNRMFDKIFGQANTPLKRWLldf 391
Cdd:PRK05691 1323 ISfdvsvwECFWPLITGcrlVLAGPGE-----HRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRLF--- 1394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 392 atSRKEAelksgvvrkdsmwdklifskVQASLGGRVRLMItgaapvsPTVltflraalgcQFYEGYGQTE---------C 462
Cdd:PRK05691 1395 --SGGEA--------------------LPAELRNRVLQRL-------PQV----------QLHNRYGPTEtainvthwqC 1435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 463 TAGCTMSLPgdwtaghVGAPLPCNFVKLVDvAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTS-------GAVDKAGWL 535
Cdd:PRK05691 1436 QAEDGERSP-------IGRPLGNVLCRVLD-AELNLLPPGVAGELCIGGAGLARGYLGRPALTAerfvpdpLGEDGARLY 1507
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528467780 536 HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDPVAQ--VFVHGDSLQACLVG 598
Cdd:PRK05691 1508 RTGDRARWNADGALEYLGRLDQQVKL-RGFRVEPEEIQARLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
270-605 |
4.68e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 49.62 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 270 ALICFTSGTTGNPKGAM--LTHGNVVSNCSAFIKITEESLKLCPQDVLISFLPLAHMFE-RVVEGVLLCHGAKIGYFQGD 346
Cdd:PRK13390 151 AVMLYSSGTTGFPKGIQpdLPGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHAAPlRWCSMVHALGGTVVLAKRFD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 347 IRLLMDDLKNLKPTIFPVVPRLLNRMFDkifgqantplkrwlLDfATSRKEAELKSgvvrkdsmwdklifskvqaslggr 426
Cdd:PRK13390 231 AQATLGHVERYRITVTQMVPTMFVRLLK--------------LD-ADVRTRYDVSS------------------------ 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 427 VRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTEcTAGCTMSLPGDWTA--GHVGAPLPCNFVKLVDvaEMNYFAANGE 504
Cdd:PRK13390 272 LRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGRSVLGDLHICDD--DGNELPAGRI 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 505 GEVCVKGPNVFQGYLKDPEQTSGAVDKAG--WLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPV 582
Cdd:PRK13390 349 GTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQETENALTMHPAV 427
|
330 340
....*....|....*....|...
gi 528467780 583 AQVFVHGdslqaclvgvvVPDPD 605
Cdd:PRK13390 428 HDVAVIG-----------VPDPE 439
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
266-632 |
6.15e-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: 49.35 E-value: 6.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 266 PEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKIteesLKLCPQDVLISFLPLAH-------MFERVVEGVLLCHGA 338
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHD----LNLKNGDRTYTCMPLYHgtaaflgACNCLMSGGTLALSR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 339 KIgyfqgDIRLLMDDLKNLKPTIFPVVPRLLnrmfdkifgqantplkRWLLDFATSRKEAELKSGVV-----RKDsMWDK 413
Cdd:cd05937 162 KF-----SASQFWKDVRDSGATIIQYVGELC----------------RYLLSTPPSPYDRDHKVRVAwgnglRPD-IWER 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 414 LifskvqaslggRVRLMItgaapvsPTVLTFlraalgcqfyegYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDV 493
Cdd:cd05937 220 F-----------RERFNV-------PEIGEF------------YAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKFENQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 494 ---------AEMNYF---------AANGE-GEVCVKGPNV----FQGYLKDPEQTSGA----VDKAG--WLHTGDIGKWL 544
Cdd:cd05937 270 vvlvkmdpeTDDPIRdpktgfcvrAPVGEpGEMLGRVPFKnreaFQGYLHNEDATESKlvrdVFRKGdiYFRTGDLLRQD 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 545 PNGTLKIIDRKKHIFKLaqgeyiapeKIENiyIRSDPVAQVF-VHGDSLQACLVGVVVPDPDflpGWAKNRGIEGSFNDL 623
Cdd:cd05937 350 ADGRWYFLDRLGDTFRW---------KSEN--VSTTEVADVLgAHPDIAEANVYGVKVPGHD---GRAGCAAITLEESSA 415
|
....*....
gi 528467780 624 CKSKEVKNA 632
Cdd:cd05937 416 VPTEFTKSL 424
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
263-605 |
6.68e-06 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 49.66 E-value: 6.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 263 PPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNcsafIKITEESLKLCPQDVLIS-------------FLP--------- 320
Cdd:PRK10252 594 LSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNR----LLWMQNHYPLTADDVVLQktpcsfdvsvwefFWPfiagaklvm 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 321 -----------LAHMFERvvEGVLLCHgakigyfqgdirllmddlknlkptifpVVPRLLnrmfdKIFGQANTPlkrwll 389
Cdd:PRK10252 670 aepeahrdplaMQQFFAE--YGVTTTH---------------------------FVPSML-----AAFVASLTP------ 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 390 dfatsrkEAELKSgvvrkdsmwdklifskvQASLGgrvRLMITGAApvsptvltfLRAALgCQFYEG---------YGQT 460
Cdd:PRK10252 710 -------EGARQS-----------------CASLR---QVFCSGEA---------LPADL-CREWQQltgaplhnlYGPT 752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 461 EctAGCTMS-LP--GDWTAGHVGAPLPCNF------VKLVDvAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSG---- 527
Cdd:PRK10252 753 E--AAVDVSwYPafGEELAAVRGSSVPIGYpvwntgLRILD-ARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASrfia 829
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 528 --AVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIyIRSDP-VAQVFVH-----------GDSLQ 593
Cdd:PRK10252 830 dpFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKI-RGQRIELGEIDRA-MQALPdVEQAVTHacvinqaaatgGDARQ 907
|
410
....*....|..
gi 528467780 594 acLVGVVVPDPD 605
Cdd:PRK10252 908 --LVGYLVSQSG 917
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
482-638 |
2.78e-05 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 47.20 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 482 PLPCNFVK-----LVDVAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGA---VDKAGWLHTGDIGKwLPNGTLKIID 553
Cdd:PRK04813 317 RLPIGYAKpdsplLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAfftFDGQPAYHTGDAGY-LEDGLLFYQG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 554 RKKHIFKLAqGEYIAPEKIENI-----YIRSdPVAQVFVHGDSLQAcLVGVVVPdpdflpgwaKNRGIEGSFnDLCKS-- 626
Cdd:PRK04813 396 RIDFQIKLN-GYRIELEEIEQNlrqssYVES-AVVVPYNKDHKVQY-LIAYVVP---------KEEDFEREF-ELTKAik 462
|
170
....*....|..
gi 528467780 627 KEVKNAILEDMI 638
Cdd:PRK04813 463 KELKERLMEYMI 474
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
256-556 |
2.86e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 47.24 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 256 ANHKTPIPPKP-EDLALICFTSGTTGNPKGAMLTHGNVVSNC----SAFIKITEeslKLCPQD-VLISFLPLAH-Mferv 328
Cdd:PRK05850 148 SPRGSDARPRDlPSTAYLQYTSGSTRTPAGVMVSHRNVIANFeqlmSDYFGDTG---GVPPPDtTVVSWLPFYHdM---- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 329 veGVLLchGAKIGYFQGDIRLLMddlknlKPTIFpvvprlLNRmfdkifgqantPlKRWLLDFATSRKEA--------EL 400
Cdd:PRK05850 221 --GLVL--GVCAPILGGCPAVLT------SPVAF------LQR-----------P-ARWMQLLASNPHAFsaapnfafEL 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 401 ksgVVRKDSMWDklifskvQASLG-GRVRLMITGAAPVSP-TVLTFLR--AALGcqFYE-----GYGQTECTAGCTMSLP 471
Cdd:PRK05850 273 ---AVRKTSDDD-------MAGLDlGGVLGIISGSERVHPaTLKRFADrfAPFN--LREtairpSYGLAEATVYVATREP 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 472 GD-----------WTAGHV-------GAPL------PCNFVKLVDVAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQT-- 525
Cdd:PRK05850 341 GQppesvrfdyekLSAGHAkrcetggGTPLvsygspRSPTVRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETer 420
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 528467780 526 ---------SGAVDKAGWLHTGDIGkWLPNGTLKIIDRKK 556
Cdd:PRK05850 421 tfgatlvdpSPGTPEGPWLRTGDLG-FISEGELFIVGRIK 459
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
262-606 |
1.80e-04 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 44.75 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 262 IPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITeeslklcPQDVLISFLPLAHMF------ERVVEGVLLC 335
Cdd:PRK13382 191 PEPTGRKGRVILLTSGTTGTPKGARRSGPGGIGTLKAILDRT-------PWRAEEPTVIVAPMFhawgfsQLVLAASLAC 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 336 HGAKIGYFQGDIRLLMDDlKNlKPTIFPVVPRllnrMFDKIFgqantplkrwlldfatsrkeaELKSGVVRKDSmwdkli 415
Cdd:PRK13382 264 TIVTRRRFDPEATLDLID-RH-RATGLAVVPV----MFDRIM---------------------DLPAEVRNRYS------ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 416 fskvqaslGGRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTEctAG-CTMSLPGDWTAG--HVGAPLPCNFVKLVD 492
Cdd:PRK13382 311 --------GRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATE--AGmIATATPADLRAApdTAGRPAEGTEIRILD 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 493 vAEMNYFAaNGE-GEVCVKGPNVFQGYlkdpeqTSGAvDK---AGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIA 568
Cdd:PRK13382 381 -QDFREVP-TGEvGTIFVRNDTQFDGY------TSGS-TKdfhDGFMASGDVGYLDENGRLFVVGRDDEMI-VSGGENVY 450
|
330 340 350
....*....|....*....|....*....|....*...
gi 528467780 569 PEKIENIYIRSDPVAQVFVHGdslqaclvgvvVPDPDF 606
Cdd:PRK13382 451 PIEVEKTLATHPDVAEAAVIG-----------VDDEQY 477
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
264-606 |
2.05e-04 |
|
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: 44.30 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 264 PKPEDLALICfTSGTTGNPKGAMLTHGNVVSncsafikiteeslklcpqdvlISFLPLAHMFERVVEGVLLCHGAkigyf 343
Cdd:cd05924 1 RSADDLYILY-TGGTTGMPKGVMWRQEDIFR---------------------MLMGGADFGTGEFTPSEDAHKAA----- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 344 qgdirllmddLKNLKPTIFPVVP-----RLLNRMFDKIFGQAnTPLKRWLLDFATSRKEAE---LKSGVVRKDSMWDKLI 415
Cdd:cd05924 54 ----------AAAAGTVMFPAPPlmhgtGSWTAFGGLLGGQT-VVLPDDRFDPEEVWRTIEkhkVTSMTIVGDAMARPLI 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 416 --FSKVQASLGGRVRLMITGAAPVSPTVLT-FLRAALGCQFYEGYGQTECTAGCT-MSLPGDWTAGHVGAPLPCNFVKLV 491
Cdd:cd05924 123 daLRDAGPYDLSSLFAISSGGALLSPEVKQgLLELVPNITLVDAFGSSETGFTGSgHSAGSGPETGPFTRANPDTVVLDD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 492 DVAEMNYfAANGEGEVCVKGpNVFQGYLKDPEQTSGA---VDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIA 568
Cdd:cd05924 203 DGRVVPP-GSGGVGWIARRG-HIPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTG-GEKVF 279
|
330 340 350
....*....|....*....|....*....|....*....
gi 528467780 569 PEKIENIyIRSDP-VAQVFVHGdslqaclvgvvVPDPDF 606
Cdd:cd05924 280 PEEVEEA-LKSHPaVYDVLVVG-----------RPDERW 306
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
266-301 |
1.35e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.46 E-value: 1.35e-03
10 20 30
....*....|....*....|....*....|....*.
gi 528467780 266 PEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIK 301
Cdd:PRK05691 2332 PQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIE 2367
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
260-323 |
1.58e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 41.64 E-value: 1.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528467780 260 TPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIkiteESLKLCPQDVLISFLPLAH 323
Cdd:PRK07769 173 VPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVI----DALEGQEGDRGVSWLPFFH 232
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
249-597 |
1.71e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.08 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 249 ELEAIGKANHKTPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNcsAFIKITeeSLKLCPQDVL---------IS-- 317
Cdd:PRK05691 3851 EVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNN--QLSKVP--YLALSEADVIaqtasqsfdISvw 3926
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 318 -FLPlAHMFervvegvllchGAKIGYFQGDI----RLLMDDLKNLKPTIFPVVPRLLNRMfdkifgqantplkrwlldfa 392
Cdd:PRK05691 3927 qFLA-APLF-----------GARVEIVPNAIahdpQGLLAHVQAQGITVLESVPSLIQGM-------------------- 3974
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 393 tsrkeaelksgvvrkdsmwdkliFSKVQASLGGrVRLMI-TGAAPVSPTVLTFLRAALGCQFYEGYGQTECT-------- 463
Cdd:PRK05691 3975 -----------------------LAEDRQALDG-LRWMLpTGEAMPPELARQWLQRYPQIGLVNAYGPAECSddvaffrv 4030
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 464 -AGCTMS--LPgdwtaghVGAPLPCNFVKLVDVAeMNYFAANGEGEVCVKGPNVFQGYLKDPEQTS--------GAVDKA 532
Cdd:PRK05691 4031 dLASTRGsyLP-------IGSPTDNNRLYLLDEA-LELVPLGAVGELCVAGTGVGRGYVGDPLRTAlafvphpfGAPGER 4102
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528467780 533 GWlHTGDIGKWLPNGTLKIIDRKKHI-----FKLAQGEyIAPEKIENIYIRSDPVA-QVFVHGDSLQACLV 597
Cdd:PRK05691 4103 LY-RTGDLARRRSDGVLEYVGRIDHQvkirgYRIELGE-IEARLHEQAEVREAAVAvQEGVNGKHLVGYLV 4171
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
452-604 |
2.66e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 40.92 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 452 QFYEGYGQTECTAgCTMSLPGDWTAGHVGAPLPCNFVKL-VDVAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSgAVD 530
Cdd:PRK07638 281 KLYEFYGASELSF-VTALVDEESERRPNSVGRPFHNVQVrICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLAR-ELN 358
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528467780 531 KAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVFVHGdslqaclvgvvVPDP 604
Cdd:PRK07638 359 ADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIESVLHEHPAVDEIVVIG-----------VPDS 420
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
257-323 |
7.31e-03 |
|
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: 39.33 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467780 257 NHKTPI-------PPKPEDLAL---ICF--TSGTTGNPKGAMLTHgnvvsncSAFIKITE---ESLKLCPQDVLISFLPL 321
Cdd:cd05939 82 NLLDPLltqsstePPSQDDVNFrdkLFYiyTSGTTGLPKAAVIVH-------SRYYRIAAgayYAFGMRPEDVVYDCLPL 154
|
..
gi 528467780 322 AH 323
Cdd:cd05939 155 YH 156
|
|
| |
