|
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: 974.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 116 QPYKWLSYKEVADRAEFAGSALLHRGHSQSGDKYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASI 195
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 196 TTIICDIadkarlildcvsgrkhsvttivimesfdseltaqaqncGIDIISLKELEAIGKANHKTPIPPKPEDLALICFT 275
Cdd:cd05927 81 SIVFCDA--------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICYT 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 276 SGTTGNPKGAMLTHGNVVSNCSAFIKITEVHCMLNQTDIHISYLPLAHMFERVVEGVLLCHGAKIGYFQGDIRLLMDDLK 355
Cdd:cd05927 123 SGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDIK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 356 NLKPTIFPVVPRLLNRMFDKIFG--QANTPLKRWLLDFATSRKEAELKSGVVRKDSMWDKLIFSKVQASLGGRVRLMITG 433
Cdd:cd05927 203 ALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLTG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 434 AAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDVAEMNYFAA--NGEGEVCVKG 511
Cdd:cd05927 283 SAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAKdpNPRGEVCIRG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 512 PNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSDPVAQVFVHGDS 591
Cdd:cd05927 363 PNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGDS 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 592 LQACLVGVVVPDPDFLPGWAK-NRGIEGSFNDLCKSKEVKNAILEDMIQLGKEAGLKSFEQVRDIALHLEMFSVQNGLLT 670
Cdd:cd05927 443 LKSFLVAIVVPDPDVLKEWAAsKGGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLLT 522
|
570 580
....*....|....*....|...
gi 528467778 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: 713.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 88 DALTLYEFFLRGLRVSNNGPCLGSRKA--GQP--YKWLSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTIS 163
Cdd:PLN02736 42 EIGTLHDNFVYAVETFRDYKYLGTRIRvdGTVgeYKWMTYGEAGTARTAIGSGLVQHG-IPKGAC-VGLYFINRPEWLIV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 164 ELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIICdIADKARLILDCVSgRKHSVTTIVIMESFDSELTAQAQNCGID 243
Cdd:PLN02736 120 DHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCLS-EIPSVRLIVVVGGADEPLPSLPSGTGVE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 244 IISLKELEAIGKANHKTPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEvhcmLNQTDIHISYLPLAH 323
Cdd:PLN02736 198 IVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTK----FYPSDVHISYLPLAH 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 324 MFERVVEGVLLCHGAKIGYFQGDIRLLMDDLKNLKPTIFPVVPRLLNRMFDKIFG--QANTPLKRWLLDFATSRKEAELK 401
Cdd:PLN02736 274 IYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNavKESGGLKERLFNAAYNAKKQALE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 402 SGvvRKDS-MWDKLIFSKVQASLGGRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTEctAGCTMSL--PGDWTAGH 478
Cdd:PLN02736 354 NG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTE--TSCVISGmdEGDNLSGH 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 479 VGAPLPCNFVKLVDVAEMNYFAANG---EGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRK 555
Cdd:PLN02736 430 VGSPNPACEVKLVDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRK 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 556 KHIFKLAQGEYIAPEKIENIYIRSDPVAQVFVHGDSLQACLVGVVVPDPDFLPGWAKNRGIE-GSFNDLCKSKEVKNAIL 634
Cdd:PLN02736 510 KNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRVRAAVL 589
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528467778 635 EDMIQLGKEAGLKSFEQVRDIALHLEMFSVQNGLLTPTLKAKRTELKSRFREQIDQLYAKI 695
Cdd:PLN02736 590 ADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYAEL 650
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
86-694 |
1.57e-180 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 526.98 E-value: 1.57e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 86 YKDALTLYEFFLRGLRVSNNGPCLGSRKAGQpYKWLSYKEVADRAEFAGSALLHRGHsQSGDKyIGIFAQNRPEWTISEL 165
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVALREKEDGI-WQSLTWAEFAERVRALAAGLLALGV-KPGDR-VAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 166 ACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC---DIADKARLILDCVSgrkhSVTTIVIMEsfdseltAQAQNCGI 242
Cdd:COG1022 84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVedqEQLDKLLEVRDELP----SLRHIVVLD-------PRGLRDDP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 243 DIISLKELEAIGKAnHKTPI-------PPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEvhcmLNQTDIH 315
Cdd:COG1022 153 RLLSLDELLALGRE-VADPAelearraAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLP----LGPGDRT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 316 ISYLPLAHMFERVVEGVLLCHGAKIgYFQGDIRLLMDDLKNLKPTIFPVVPRLLNRMFDKIFGQAN--TPLKRWLLDFA- 392
Cdd:COG1022 228 LSFLPLAHVFERTVSYYALAAGATV-AFAESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEeaGGLKRKLFRWAl 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 393 -TSRKEAELK------SGVVR-KDSMWDKLIFSKVQASLGGRVRLMITGAAPVSPTVLTFLRAaLGCQFYEGYGQTECTA 464
Cdd:COG1022 307 aVGRRYARARlagkspSLLLRlKHALADKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 465 GCTMSLPGDWTAGHVGAPLPCNFVKLvdvAEmnyfaangEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWL 544
Cdd:COG1022 386 VITVNRPGDNRIGTVGPPLPGVEVKI---AE--------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELD 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 545 PNGTLKIIDRKKHIFKLAQGEYIAPEKIENIyIRSDP-VAQVFVHGDSlQACLVGVVVPDPDFLPGWAKNRGIE-GSFND 622
Cdd:COG1022 455 EDGFLRITGRKKDLIVTSGGKNVAPQPIENA-LKASPlIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGLPyTSYAE 532
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528467778 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 |
9.35e-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: 475.93 E-value: 9.35e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 116 QPYKWLSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASI 195
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALG-VEPGDR-VAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 196 TTIICDiadkarlildcvsgrkhsvttivimesfdseltaqaqncgidiislkeleaigkanhktpippKPEDLALICFT 275
Cdd:cd05907 79 KALFVE---------------------------------------------------------------DPDDLATIIYT 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 276 SGTTGNPKGAMLTHGNVVSNCSAFIKITEvhcmLNQTDIHISYLPLAHMFERV-VEGVLLCHGAKIGYFQgDIRLLMDDL 354
Cdd:cd05907 96 SGTTGRPKGVMLSHRNILSNALALAERLP----ATEGDRHLSFLPLAHVFERRaGLYVPLLAGARIYFAS-SAETLLDDL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 355 KNLKPTIFPVVPRLLNRMFDKIFGQANTPLKRWLLDFAtsrkeaelksgvvrkdsmwdklifskvqasLGGRVRLMITGA 434
Cdd:cd05907 171 SEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLA------------------------------VGGRLRFAASGG 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 435 APVSPTVLTFLRAaLGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDvaemnyfaangEGEVCVKGPNV 514
Cdd:cd05907 221 APLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPNV 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 515 FQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSDPVAQVFVHGDSlQA 594
Cdd:cd05907 289 MLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDG-RP 367
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 595 CLVGVVVPDPDFLPGWAKNRGIEG-SFNDLCKSKEVKNAILEDMIQLGkeAGLKSFEQVRDIALHLEMFSVQNGLLTPTL 673
Cdd:cd05907 368 FLVALIVPDPEALEAWAEEHGIAYtDVAELAANPAVRAEIEAAVEAAN--ARLSRYEQIKKFLLLPEPFTIENGELTPTL 445
|
....
gi 528467778 674 KAKR 677
Cdd:cd05907 446 KLKR 449
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
117-695 |
1.68e-159 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 475.07 E-value: 1.68e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 117 PYKWLSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASIT 196
Cdd:PLN02430 73 PYMWKTYKEVYEEVLQIGSALRASG-AEPGSR-VGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEID 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 197 TI-ICDIADKARLILDCVSGRKhsVTTIVIMESFDSELTAQAQNCGIDIISLKELEAIGKANHKTPIPPKPEDLALICFT 275
Cdd:PLN02430 151 FVfVQDKKIKELLEPDCKSAKR--LKAIVSFTSVTEEESDKASQIGVKTYSWIDFLHMGKENPSETNPPKPLDICTIMYT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 276 SGTTGNPKGAMLTHGNVvsncSAFIKITEVhCM------LNQTDIHISYLPLAHMFERVVEGVLLCHGAKIGYFQGDIRL 349
Cdd:PLN02430 229 SGTSGDPKGVVLTHEAV----ATFVRGVDL-FMeqfedkMTHDDVYLSFLPLAHILDRMIEEYFFRKGASVGYYHGDLNA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 350 LMDDLKNLKPTIFPVVPRLLNRMFDKIFG--QANTPLKRWLLDFATSRKEAELKSGVVRKDS--MWDKLIFSKVQASLGG 425
Cdd:PLN02430 304 LRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYKYKLAWMNRGYSHKKAspMADFLAFRKVKAKLGG 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 426 RVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTA-GHVGAPLPCNFVKLVDVAEMNY--FAAN 502
Cdd:PLN02430 384 RLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMCMlGTVGAPAVYNELRLEEVPEMGYdpLGEP 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 503 GEGEVCVKGPNVFQGYLKDPEQTSgAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSDPV 582
Cdd:PLN02430 464 PRGEICVRGKCLFSGYYKNPELTE-EVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIV 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 583 AQVFVHGDSLQACLVGVVVPDPDFLPGWAKNRGIEGSFNDLCKSKEVKNAILEDMIQLGKEAGLKSFEQVRDIALHLEMF 662
Cdd:PLN02430 543 EDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKEHILSELKSTAEKNKLRGFEYIKGVILETKPF 622
|
570 580 590
....*....|....*....|....*....|...
gi 528467778 663 SVQNGLLTPTLKAKRTELKSRFREQIDQLYAKI 695
Cdd:PLN02430 623 DVERDLVTATLKKRRNNLLKYYQVEIDEMYRKL 655
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
117-680 |
1.23e-158 |
|
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: 467.46 E-value: 1.23e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 117 PYKWLSYKEVADRAEFAGSALLHRGHsQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASIT 196
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLVELGL-KPGDK-VAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 197 TIICDiadkarlildcvsgrkhsvttivimesfdseltaqaqncgidiislkeleaigkanhktpipPKPEDLALICFTS 276
Cdd:cd17639 80 AIFTD--------------------------------------------------------------GKPDDLACIMYTS 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 277 GTTGNPKGAMLTHGNVVSNCSAFIKIteVHCMLNQTDIHISYLPLAHMFERVVEGVLLCHGAKIGYfqGDIRLLMD---- 352
Cdd:cd17639 98 GSTGNPKGVMLTHGNLVAGIAGLGDR--VPELLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDkskr 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 353 ----DLKNLKPTIFPVVPRLLNRMFDKIFGQANTP--LKRWLLDFATSRKEAELKSGvvrKDSM-WDKLIFSKVQASLGG 425
Cdd:cd17639 174 gckgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMggLKRTLFWTAYQSKLKALKEG---PGTPlLDELVFKKVRAALGG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 426 RVRLMITGAAPVSPTVLTFLrAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDVAEMNYFAANGE- 504
Cdd:cd17639 251 RLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDKPPp 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 505 -GEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSDPVA 583
Cdd:cd17639 330 rGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVN 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 584 QVFVHGDSLQACLVGVVVPDPDFLPGWA-KNRGIEGSFNDLCKSKEVKNAILEDMIQLGKEAGLKSFEQVRDIALHLEMF 662
Cdd:cd17639 410 NICVYADPDKSYPVAIVVPNEKHLTKLAeKHGVINSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEW 489
|
570
....*....|....*...
gi 528467778 663 SVQNGLLTPTLKAKRTEL 680
Cdd:cd17639 490 TPENGLVTAAQKLKRKEI 507
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
87-696 |
2.24e-154 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 462.00 E-value: 2.24e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 87 KDALTLYEFFLRGLRVSNNGPCLGSR-----KAGqPYKWLSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWT 161
Cdd:PLN02861 40 ADIDSPWQFFSDAVKKYPNNQMLGRRqvtdsKVG-PYVWLTYKEVYDAAIRIGSAIRSRG-VNPGDR-CGIYGSNCPEWI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 162 ISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIICDiADKARLILDCVSGRKHSVTTIVIMESFDSELTAQAQNCG 241
Cdd:PLN02861 117 IAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQ-ESKISSILSCLPKCSSNLKTIVSFGDVSSEQKEEAEELG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 242 IDIISLKELEAIGKANHKTPiPPKPEDLALICFTSGTTGNPKGAMLTHGNVVS---NCSAFIKITEVHCmlNQTDIHISY 318
Cdd:PLN02861 196 VSCFSWEEFSLMGSLDCELP-PKQKTDICTIMYTSGTTGEPKGVILTNRAIIAevlSTDHLLKVTDRVA--TEEDSYFSY 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 319 LPLAHMFERVVEGVLLCHGAKIGYFQGDIRLLMDDLKNLKPTIFPVVPRLLNRMFDKIFG--QANTPLKRWLLDFATSRK 396
Cdd:PLN02861 273 LPLAHVYDQVIETYCISKGASIGFWQGDIRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQkiSSGGMLRKKLFDFAYNYK 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 397 EAELKSGVVRKDS--MWDKLIFSKVQASLGGRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDW 474
Cdd:PLN02861 353 LGNLRKGLKQEEAspRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGCFTSIANVF 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 475 T-AGHVGAPLPCNFVKLVDVAEMNYFAANG--EGEVCVKGPNVFQGYLKDPEQTSGA-VDkaGWLHTGDIGKWLPNGTLK 550
Cdd:PLN02861 433 SmVGTVGVPMTTIEARLESVPEMGYDALSDvpRGEICLRGNTLFSGYHKRQDLTEEVlID--GWFHTGDIGEWQPNGAMK 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 551 IIDRKKHIFKLAQGEYIAPEKIENIYIRSDPVAQVFVHGDSLQACLVGVVVPDPDFLPGWAKNRGIEGSFNDLCKSKEVK 630
Cdd:PLN02861 511 IIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKAR 590
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528467778 631 NAILEDMIQLGKEAGLKSFEQVRDIALHLEMFSVQNGLLTPTLKAKRTELKSRFREQIDQLYAKIK 696
Cdd:PLN02861 591 KYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYSEAK 656
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
105-696 |
1.33e-148 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 447.54 E-value: 1.33e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 105 NGPCLGSR-----KAGQpYKWLSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYD 179
Cdd:PLN02614 60 NNPMLGRReivdgKPGK-YVWQTYQEVYDIVIKLGNSLRSVG-VKDEAK-CGIYGANSPEWIISMEACNAHGLYCVPLYD 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 180 TLGTEAISYVIDKASITTIICDIADKARLILDCVSGRKHsVTTIVIMESFDSELTAQAQNCGIDIISLKELEAIGKA-NH 258
Cdd:PLN02614 137 TLGAGAVEFIISHSEVSIVFVEEKKISELFKTCPNSTEY-MKTVVSFGGVSREQKEEAETFGLVIYAWDEFLKLGEGkQY 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 259 KTPIPpKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIK-ITEVHCMLNQTDIHISYLPLAHMFERVVEGVLLCHG 337
Cdd:PLN02614 216 DLPIK-KKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRlLKSANAALTVKDVYLSYLPLAHIFDRVIEECFIQHG 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 338 AKIGYFQGDIRLLMDDLKNLKPTIFPVVPRLLNRMFDKIFGQANTP--LKRWLLDFATSRKEAELKSGV--VRKDSMWDK 413
Cdd:PLN02614 295 AAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGgfLKKFVFDSAFSYKFGNMKKGQshVEASPLCDK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 414 LIFSKVQASLGGRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDW-TAGHVGAPLPCNFVKLVD 492
Cdd:PLN02614 375 LVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELdMLGTVGPPVPNVDIRLES 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 493 VAEMNY--FAANGEGEVCVKGPNVFQGYLKDpEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPE 570
Cdd:PLN02614 455 VPEMEYdaLASTPRGEICIRGKTLFSGYYKR-EDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVE 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 571 KIENIYIRSDPVAQVFVHGDSLQACLVGVVVPDPDFLPGWAKNRGIEGSFNDLCKSKEVKNAILEDMIQLGKEAGLKSFE 650
Cdd:PLN02614 534 NIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEFILGELVKMAKEKKMKGFE 613
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 528467778 651 QVRDIALHLEMFSVQNGLLTPTLKAKRTELKSRFREQIDQLYAKIK 696
Cdd:PLN02614 614 IIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYKTTN 659
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
62-693 |
1.65e-143 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 435.31 E-value: 1.65e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 62 VEVPGKE-YARRS--ILMDNDTHmtyyYKDALTLYEFFLRGLRVSNNGPCLGSRKA----------GQ--------PYKW 120
Cdd:PLN02387 31 VDVGGEPgYAIRNarFPELVETP----WEGATTLAALFEQSCKKYSDKRLLGTRKLisrefetssdGRkfeklhlgEYEW 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGHSQsgDKYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNK--EERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVIC 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 201 DIADKARLIldCVSGRKHSVTTIVIME-SFDSELTAQAQNCGIDIISLKELEAIGKANHKTPIPPKPEDLALICFTSGTT 279
Cdd:PLN02387 185 DSKQLKKLI--DISSQLETVKRVIYMDdEGVDSDSSLSGSSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGST 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 280 GNPKGAMLTHGNVVSNCSAFIKITEvhcMLNQTDIHISYLPLAHMFERVVEGVLLCHGAKIGYfqGDIRLLMD------- 352
Cdd:PLN02387 263 GLPKGVMMTHGNIVATVAGVMTVVP---KLGKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDtsnkikk 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 353 ----DLKNLKPTIFPVVPRLLNRMFDKIFGQANTP--LKRWLLDFATSRKEAELK------SGVVRkdSMWDKLIFSKVQ 420
Cdd:PLN02387 338 gtkgDASALKPTLMTAVPAILDRVRDGVRKKVDAKggLAKKLFDIAYKRRLAAIEgswfgaWGLEK--LLWDALVFKKIR 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 421 ASLGGRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDVAEMNYFA 500
Cdd:PLN02387 416 AVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLI 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 501 ANG---EGEVCVKGPNVFQGYLKDPEQTSGA--VDKAG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIE 573
Cdd:PLN02387 496 SDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVE 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 574 NIYIRSDPVAQVFVHGDSLQACLVGVVVPDPDFLPGWAKNRGIE-GSFNDLCKSKEVKNAILEDMIQLGKEAGLKSFEQV 652
Cdd:PLN02387 576 AALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIP 655
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 528467778 653 RDIALHLEMFSVQNGLLTPTLKAKRTELKSRFREQIDQLYA 693
Cdd:PLN02387 656 AKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
117-562 |
6.12e-125 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 377.81 E-value: 6.12e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 117 PYKWLSYKEVADRAEFAGSALLHRGHsQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASIT 196
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRALGV-GKGDR-VAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 197 TIICDIADKARLILDCVSGRKHSVTTIVImeSFDSELTAQAqncgidiisLKELEAIGKANHKTPIPPKPEDLALICFTS 276
Cdd:pfam00501 96 VLITDDALKLEELLEALGKLEVVKLVLVL--DRDPVLKEEP---------LPEEAKPADVPPPPPPPPDPDDLAYIIYTS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 277 GTTGNPKGAMLTHGNVVSNCSAFIKITEVHCMLNQTDIHISYLPLAHMFERVVE-GVLLCHGAKIGYFQGDIRL----LM 351
Cdd:pfam00501 165 GTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGlLGPLLAGATVVLPPGFPALdpaaLL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 352 DDLKNLKPTIFPVVPRLLNRMFDKIfgqantPLKRWLLdfatsrkeaelksgvvrkdsmwdklifskvqaslgGRVRLMI 431
Cdd:pfam00501 245 ELIERYKVTVLYGVPTLLNMLLEAG------APKRALL-----------------------------------SSLRLVL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 432 TGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDW---TAGHVGAPLPCNFVKLVDVAEMNYFAANGEGEVC 508
Cdd:pfam00501 284 SGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELC 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 528467778 509 VKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLA 562
Cdd:pfam00501 364 VRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
119-694 |
9.02e-108 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 342.34 E-value: 9.02e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 119 KWLSYKEVADRAEFAGSALLHRGHSQsGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTI 198
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLAELGLTK-GSN-VAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 199 ICDIADKARLILDCVSGRKHSvTTIVIMESFDSELTAQaqncGIDIISLKELEAIG---KANHKTPIPPKPEDLALICFT 275
Cdd:PTZ00216 198 VCNGKNVPNLLRLMKSGGMPN-TTIIYLDSLPASVDTE----GCRLVAWTDVVAKGhsaGSHHPLNIPENNDDLALIMYT 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 276 SGTTGNPKGAMLTHGNVVSNCSAF-IKITEVHCMLNQTDIHISYLPLAHMFERVVEGVLLCHGAKIGYfqGDIRLLMD-- 352
Cdd:PTZ00216 273 SGTTGDPKGVMHTHGSLTAGILALeDRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRTLTDtf 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 353 -----DLKNLKPTIFPVVPRLlnrmFDKIFG--QANTP----LKRWLLDFA-TSRKEAeLKSGvvrKDS-MWDKLIFSKV 419
Cdd:PTZ00216 351 arphgDLTEFRPVFLIGVPRI----FDTIKKavEAKLPpvgsLKRRVFDHAyQSRLRA-LKEG---KDTpYWNEKVFSAP 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 420 QASLGGRVRLMITGAAPVSPTVLTFLRAALGCqFYEGYGQTEcTAGC-TMSLPGDWTAGHVGAPLPCNFVKLVDVAEMNY 498
Cdd:PTZ00216 423 RAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTE-TVCCgGIQRTGDLEPNAVGQLLKGVEMKLLDTEEYKH 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 499 F-AANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYI 577
Cdd:PTZ00216 501 TdTPEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEALYG 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 578 rSDPVAQ-----VFVHGDslQACLVGVVVPDPDFLPGWAKNRGIEGSFNDLCKSKEVKNAILEDMIQLGKEAGLKSFEQV 652
Cdd:PTZ00216 581 -QNELVVpngvcVLVHPA--RSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFEIV 657
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 528467778 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 |
3.23e-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: 273.47 E-value: 3.23e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 116 QPYKWLSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPlydtlgteaisyvidKASI 195
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLG-VKAGEK-VALFADNSPRWLIADQGIMALGAVDVV---------------RGSD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 196 TTIicdiaDKARLILdcvsgrKHSVTTIVIMEsfdseltaqaqncgidiislkeleaigkaNHktpippkPEDLALICFT 275
Cdd:cd17640 64 SSV-----EELLYIL------NHSESVALVVE-----------------------------ND-------SDDLATIIYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 276 SGTTGNPKGAMLTHGNVVSNCSAFIKITEVHcmlnQTDIHISYLPLAHMFERVVEGVLLCHGAKIGYfqGDIRLLMDDLK 355
Cdd:cd17640 97 SGTTGNPKGVMLTHANLLHQIRSLSDIVPPQ----PGDRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDDLK 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 356 NLKPTIFPVVPRLLNRMFDKIFGQ--ANTPLKRWLLDFATSrkeaelksgvvrkdsmwdklifskvqaslGGRVRLMITG 433
Cdd:cd17640 171 RVKPHYIVSVPRLWESLYSGIQKQvsKSSPIKQFLFLFFLS-----------------------------GGIFKFGISG 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 434 AAPVSPTVLTFLRAaLGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDVAEMNYFAANGEGEVCVKGPN 513
Cdd:cd17640 222 GGALPPHVDTFFEA-IGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQ 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 514 VFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSDPVAQVFVHGDSlQ 593
Cdd:cd17640 301 VMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQD-Q 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 594 ACLVGVVVPDPDFLPGWAKNRGI---EGSFNDLCKSKEVKNAILEDMIQLGKEAGLKSFEQVRDIALhLEMFSVQNGLLT 670
Cdd:cd17640 380 KRLGALIVPNFEELEKWAKESGVklaNDRSQLLASKKVLKLYKNEIKDEISNRPGFKSFEQIAPFAL-LEEPFIENGEMT 458
|
....*..
gi 528467778 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 |
2.47e-80 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 264.72 E-value: 2.47e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:cd05932 7 FTWGEVADKARRLAAALRALG-LEPGSK-IALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 201 DiadkarlILDCVSGRKHSV--TTIVIMESFDSELTAQAQncgidiisLKELEAIGKANHKTPiPPKPEDLALICFTSGT 278
Cdd:cd05932 85 G-------KLDDWKAMAPGVpeGLISISLPPPSAANCQYQ--------WDDLIAQHPPLEERP-TRFPEQLATLIYTSGT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 279 TGNPKGAMLTHGNVVSNCSAFIKitevHCMLNQTDIHISYLPLAHMFERV-VEGVLLCHGAKIgYFQGDIRLLMDDLKNL 357
Cdd:cd05932 149 TGQPKGVMLTFGSFAWAAQAGIE----HIGTEENDRMLSYLPLAHVTERVfVEGGSLYGGVLV-AFAESLDTFVEDVQRA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 358 KPTIFPVVPRLL----NRMFDKIfgqantPLKRwlLDFAtsrkeaeLKSGVVrkdsmwDKLIFSKVQASLG-GRVRLMIT 432
Cdd:cd05932 224 RPTLFFSVPRLWtkfqQGVQDKI------PQQK--LNLL-------LKIPVV------NSLVKRKVLKGLGlDQCRLAGC 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 433 GAAPVSPTVLTFLRaALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDvaemnyfaangEGEVCVKGP 512
Cdd:cd05932 283 GSAPVPPALLEWYR-SLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEILVRSP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 513 NVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSDPVAQVFVHGDSL 592
Cdd:cd05932 351 ALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSGL 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 593 QACLVGVVVPDPDFLPGWAKNRG-IEGSFndlckskevkNAILEDMiqlgkEAGLKSFEQVRDIALHLEMFSVQNGLLTP 671
Cdd:cd05932 431 PAPLALVVLSEEARLRADAFARAeLEASL----------RAHLARV-----NSTLDSHEQLAGIVVVKDPWSIDNGILTP 495
|
570
....*....|...
gi 528467778 672 TLKAKRTELKSRF 684
Cdd:cd05932 496 TLKIKRNVLEKAY 508
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
121-677 |
1.13e-68 |
|
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: 232.33 E-value: 1.13e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:cd05914 8 LTYKDLADNIAKFALLLKING-VGTGDR-VALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 201 DiadkarlildcvsgrkhsvttivimesfdseltaqaqncgidiislkeleaigkanhktpippKPEDLALICFTSGTTG 280
Cdd:cd05914 86 S---------------------------------------------------------------DEDDVALINYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 281 NPKGAMLTHGNVVSNCSAFIKITevhcMLNQTDIHISYLPLAHMFERVVEGVL-LCHGAKIgYFQGDI---RLLMDDLKN 356
Cdd:cd05914 103 NSKGVMLTYRNIVSNVDGVKEVV----LLGKGDKILSILPLHHIYPLTFTLLLpLLNGAHV-VFLDKIpsaKIIALAFAQ 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 357 LKPTIfpVVPRLLNRMfdKIFGQANTPLKrwlldfatSRKEAELKSGVVRKDSMWDKLIFSKVQASLGGRVRLMITGAAP 436
Cdd:cd05914 178 VTPTL--GVPVPLVIE--KIFKMDIIPKL--------TLKKFKFKLAKKINNRKIRKLAFKKVHEAFGGNIKEFVIGGAK 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 437 VSPTVLTFLRAaLGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLpcnfvKLVDVAEMNYFAANGEGEVCVKGPNVFQ 516
Cdd:cd05914 246 INPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVI-----DGVEVRIDSPDPATGEGEIIVRGPNVMK 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 517 GYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSDPVA--QVFVHGDSLQA 594
Cdd:cd05914 320 GYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLesLVVVQEKKLVA 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 595 clvgVVVPDPDFLPGWAKnrgiegsfndlcKSKEVKNAILEDMI-QLGKEagLKSFEQVRDIALHLEMFSVqngllTPTL 673
Cdd:cd05914 400 ----LAYIDPDFLDVKAL------------KQRNIIDAIKWEVRdKVNQK--VPNYKKISKVKIVKEEFEK-----TPKG 456
|
....
gi 528467778 674 KAKR 677
Cdd:cd05914 457 KIKR 460
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
121-606 |
6.76e-68 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 229.70 E-value: 6.76e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:COG0318 25 LTYAELDARARRLAAALRALG-VGPGDR-VALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 201 diadkarlildcvsgrkhsvttivimesfdseltaqaqncgidiislkeleaigkanhktpippkpedlALICFTSGTTG 280
Cdd:COG0318 103 ---------------------------------------------------------------------ALILYTSGTTG 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 281 NPKGAMLTHGNVVSNCSAFIKITEvhcmLNQTDIHISYLPLAHMFERVVEGVL-LCHGAKI---GYFqgDIRLLMDDLKN 356
Cdd:COG0318 114 RPKGVMLTHRNLLANAAAIAAALG----LTPGDVVLVALPLFHVFGLTVGLLApLLAGATLvllPRF--DPERVLELIER 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 357 LKPTIFPVVPRLLNRMfdkifgqANTPlkrwlldfatsrkeaelksgvvrkdsMWDKLIFSkvqaslggRVRLMITGAAP 436
Cdd:COG0318 188 ERVTVLFGVPTMLARL-------LRHP--------------------------EFARYDLS--------SLRLVVSGGAP 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 437 VSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTA--GHVGAPLPCNFVKLVDvAEMNYFAANGEGEVCVKGPNV 514
Cdd:COG0318 227 LPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGRPLPGVEVRIVD-EDGRELPPGEVGEIVVRGPNV 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 515 FQGYLKDPEQTsGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSDPVAQVFVhgdslqa 594
Cdd:COG0318 306 MKGYWNDPEAT-AEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEVLAAHPGVAEAAV------- 376
|
490
....*....|..
gi 528467778 595 clvgVVVPDPDF 606
Cdd:COG0318 377 ----VGVPDEKW 384
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
113-692 |
2.96e-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: 231.86 E-value: 2.96e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 113 KAGQPYKWLSYKEVADRAEFAGSALLHRG----HSqsgdkyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISY 188
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLKLGlerfHG------VGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 189 VIDKASITTIICDIADKARLILDCVSGRKHSVTTIVIMESFDSELT-----AQAQNCGIDIiSLKELEAIGKANhktpip 263
Cdd:cd05933 75 VAETSEANILVVENQKQLQKILQIQDKLPHLKAIIQYKEPLKEKEPnlyswDEFMELGRSI-PDEQLDAIISSQ------ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 264 pKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEVHCMLNQTDIHISYLPLAHMFERVVEgVLLC--HGAKIG 341
Cdd:cd05933 148 -KPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILD-IWLPikVGGQVY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 342 YFQGDIR--LLMDDLKNLKPTIFPVVPRLLNRMFDKI--FGQANTPLKRWLLDFA------TSRKEAELKSGVVRKDSMW 411
Cdd:cd05933 226 FAQPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkaVGAKSGTLKRKIASWAkgvgleTNLKLMGGESPSPLFYRLA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 412 DKLIFSKVQASLG-GRVRLMITGAAPVSPTVLTFLrAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKL 490
Cdd:cd05933 306 KKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 491 VDVAemnyfaANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPE 570
Cdd:cd05933 385 HNPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPV 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 571 KIEN-IYIRSDPVAQVFVHGDSLQ--------ACLVGVVVPDP-DFLP----GWAKNRGIEGS-FNDLCKSKE--VKNAI 633
Cdd:cd05933 459 PIEDaVKKELPIISNAMLIGDKRKflsmlltlKCEVNPETGEPlDELTeeaiEFCRKLGSQATrVSEIAGGKDpkVYEAI 538
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 528467778 634 LEDMIQLGKEAgLKSFEQVRDIALHLEMFSVQNGLLTPTLKAKRTELKSRFREQIDQLY 692
Cdd:cd05933 539 EEGIKRVNKKA-ISNAQKIQKWVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
122-677 |
1.68e-66 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 229.23 E-value: 1.68e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 122 SYKEVADRAEFAGSALLHRGhSQSGDkYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC- 200
Cdd:cd17641 13 TWADYADRVRAFALGLLALG-VGRGD-VVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAe 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 201 --DIADKARLILDcvsgRKHSVTTIVIMES------FDSELtaqaqncgidiISLKELEAIGKANHKTPipP-------- 264
Cdd:cd17641 91 deEQVDKLLEIAD----RIPSVRYVIYCDPrgmrkyDDPRL-----------ISFEDVVALGRALDRRD--Pglyereva 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 265 --KPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEvhcmLNQTDIHISYLPLAHMFERV--VEGVLLChGAKI 340
Cdd:cd17641 154 agKGEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADP----LGPGDEYVSVLPLPWIGEQMysVGQALVC-GFIV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 341 GyFQGDIRLLMDDLKNLKPTIFPVVPRLLN--------RMFDkifgqaNTPLKRWLLDF--------ATSRKEAELKSGV 404
Cdd:cd17641 229 N-FPEEPETMMEDLREIGPTFVLLPPRVWEgiaadvraRMMD------ATPFKRFMFELgmklglraLDRGKRGRPVSLW 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 405 VRKDS-MWDKLIFSKVQASLG-GRVRLMITGAAPVSPTVLTFLRAaLGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAP 482
Cdd:cd17641 302 LRLASwLADALLFRPLRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 483 LPCNFVKLVDVaemnyfaangeGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLA 562
Cdd:cd17641 381 FPGTEVRIDEV-----------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTS 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 563 QGEYIAPEKIEN-----IYIRSdpvAQVFVHGDSLQACLVGVvvpDPDFLPGWAKNRGIE-GSFNDLCKSKEVKNAILED 636
Cdd:cd17641 450 DGTRFSPQFIENklkfsPYIAE---AVVLGAGRPYLTAFICI---DYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKE 523
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 528467778 637 MIQLGKEagLKSFEQVRDIALHLEMFSVQNGLLTPTLKAKR 677
Cdd:cd17641 524 VEKVNAS--LPEAQRIRRFLLLYKELDADDGELTRTRKVRR 562
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
121-670 |
1.14e-64 |
|
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: 224.64 E-value: 1.14e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGHSQSGDkYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:cd17632 68 ITYAELWERVGAVAAAHDPEQPVRPGD-FVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 201 DiADKARLILDCVSGRKhSVTTIVImesFD--SELTAQAQ----------NCGIDIISLKELEAIGKANHKTP---IPPK 265
Cdd:cd17632 147 S-AEHLDLAVEAVLEGG-TPPRLVV---FDhrPEVDAHRAalesarerlaAVGIPVTTLTLIAVRGRDLPPAPlfrPEPD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 266 PEDLALICFTSGTTGNPKGAMLTHGNVVS---NCSAFIKITEvhcmlnQTDIHISYLPLAHMFERVVEGVLLCHGAkIGY 342
Cdd:cd17632 222 DDPLALLIYTSGSTGTPKGAMYTERLVATfwlKVSSIQDIRP------PASITLNFMPMSHIAGRISLYGTLARGG-TAY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 343 FQG--DIRLLMDDLKNLKPTIFPVVPRLlnrmFDKIFGQANTPLKRWLLDFATSRKEAELKSGVVRKDSmwdklifskvq 420
Cdd:cd17632 295 FAAasDMSTLFDDLALVRPTELFLVPRV----CDMLFQRYQAELDRRSVAGADAETLAERVKAELRERV----------- 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 421 asLGGRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTEctAGCTMSLpgdwtaGHVGAPlPCNFVKLVDVAEMNYFA 500
Cdd:cd17632 360 --LGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE--AGAVILD------GVIVRP-PVLDYKLVDVPELGYFR 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 501 ANG---EGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYI 577
Cdd:cd17632 429 TDRphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFA 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 578 RSDPVAQVFVHGDSLQACLVGVVVPDPDFLPGWAknrgiegsfndlckSKEVKNAILEDMIQLGKEAGLKSFEQVRDIAL 657
Cdd:cd17632 509 ASPLVRQIFVYGNSERAYLLAVVVPTQDALAGED--------------TARLRAALAESLQRIAREAGLQSYEIPRDFLI 574
|
570
....*....|...
gi 528467778 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 |
1.12e-63 |
|
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: 214.84 E-value: 1.12e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 268 DLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKitevHCMLNQTDIHISYLPLAHMFERVVEGVLLCHGAKI---GYFq 344
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAA----SGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVvllPKF- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 345 gDIRLLMDDLKNLKPTIFPVVPRLLNRMFDkifgqantplkrwlldfATSRKEAELKSgvvrkdsmwdklifskvqaslg 424
Cdd:cd04433 76 -DPEAALELIEREKVTILLGVPTLLARLLK-----------------APESAGYDLSS---------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 425 grVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWT--AGHVGAPLPCNFVKLVDVAEmNYFAAN 502
Cdd:cd04433 116 --LRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDPDG-GELPPG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 503 GEGEVCVKGPNVFQGYLKDPEQTSgAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYIRSDPV 582
Cdd:cd04433 193 EIGELVVRGPSVMKGYWNNPEATA-AVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPGV 270
|
330 340
....*....|....*....|....*.
gi 528467778 583 AQVFVHG---DSLQACLVGVVVPDPD 605
Cdd:cd04433 271 AEAAVVGvpdPEWGERVVAVVVLRPG 296
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
121-605 |
5.32e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 207.45 E-value: 5.32e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALG-IGKGDR-VAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 201 --DIADKARLILDCVSgrkhSVTTIVIMEsfdselTAQAQNCGIDIISLKELEAIGkANHKTPIPPKPEDLALICFTSGT 278
Cdd:PRK07656 109 lgLFLGVDYSATTRLP----ALEHVVICE------TEEDDPHTEKMKTFTDFLAAG-DPAERAPEVDPDDVADILFTSGT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 279 TGNPKGAMLTHGNVVSNCSAFIKITEvhcmLNQTDIHISYLPLAHMFERVVeGVLLC--HGAKI---GYFqgDIRLLMDD 353
Cdd:PRK07656 178 TGRPKGAMLTHRQLLSNAADWAEYLG----LTEGDRYLAANPFFHVFGYKA-GVNAPlmRGATIlplPVF--DPDEVFRL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 354 LKNLKPTIFPVVPRLLNRMFDkifgqantplkrwlldfATSRKEAELKSgvvrkdsmwdklifskvqaslggrVRLMITG 433
Cdd:PRK07656 251 IETERITVLPGPPTMYNSLLQ-----------------HPDRSAEDLSS------------------------LRLAVTG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 434 AAPVSPTVLTFLRAALGCQ-FYEGYGQTECTAGCTMSLPGD---WTAGHVGAPLPCNFVKLVDvaEMNYFAANGE-GEVC 508
Cdd:PRK07656 290 AASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIAGVENKIVN--ELGEEVPVGEvGELL 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 509 VKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVFVH 588
Cdd:PRK07656 368 VRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IVGGFNVYPAEVEEVLYEHPAVAEAAVI 446
|
490
....*....|....*..
gi 528467778 589 GdslqaclvgvvVPDPD 605
Cdd:PRK07656 447 G-----------VPDER 452
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
121-605 |
2.40e-57 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 202.06 E-value: 2.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLG-LKKGDV-VGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 201 D--IADKARLILDCVSgrkhSVTTIVIMESFDSELTAQAQncgidiiSLKELEAIGKANHKTPIPPKPEDLALICFTSGT 278
Cdd:cd05911 89 DpdGLEKVKEAAKELG----PKDKIIVLDDKPDGVLSIED-------LLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 279 TGNPKGAMLTHGNVVSNCSaFIKITEVHCMLNQtDIHISYLPLAHMFervveGVLLCHGAKIgyfQG---------DIRL 349
Cdd:cd05911 158 TGLPKGVCLSHRNLIANLS-QVQTFLYGNDGSN-DVILGFLPLYHIY-----GLFTTLASLL---NGatviimpkfDSEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 350 LMDDLKNLKPTIFPVVPRLLNRMFdkifgqantplkrwlldfatsrkeaelKSGVVRKDSMwdklifskvqASLggrvRL 429
Cdd:cd05911 228 FLDLIEKYKITFLYLVPPIAAALA---------------------------KSPLLDKYDL----------SSL----RV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 430 MITGAAPVSPTVLTFLRAALG-CQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPcNF-VKLVDVAEMNYFAANGEGEV 507
Cdd:cd05911 267 ILSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLP-NVeAKIVDDDGKDSLGPNEPGEI 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 508 CVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDPVAQVfv 587
Cdd:cd05911 346 CVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAVLLEHPGVADA-- 422
|
490
....*....|....*...
gi 528467778 588 hgdslqaCLVGvvVPDPD 605
Cdd:cd05911 423 -------AVIG--IPDEV 431
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
119-605 |
3.54e-56 |
|
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: 198.56 E-value: 3.54e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 119 KWLSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLyDTLGTEAisyvidkasitti 198
Cdd:cd05936 23 RKLTYRELDALAEAFAAGLQNLG-VQPGDR-VALMLPNCPQFPIAYFGALKAGAVVVPL-NPLYTPR------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 199 icdiadkarlildcvsgrkhsvttivimesfdsELTAQAQNCG----IDIISLKELEAIGKANHKTPIPPkPEDLALICF 274
Cdd:cd05936 87 ---------------------------------ELEHILNDSGakalIVAVSFTDLLAAGAPLGERVALT-PEDVAVLQY 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 275 TSGTTGNPKGAMLTHGNVVSNCSAFIKITEVhcMLNQTDIHISYLPLAHMFERVVEGVL-LCHGAKIGYFQG-DIRLLMD 352
Cdd:cd05936 133 TSGTTGVPKGAMLTHRNLVANALQIKAWLED--LLEGDDVVLAALPLFHVFGLTVALLLpLALGATIVLIPRfRPIGVLK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 353 DLKNLKPTIFPVVPRLLNRMfdkifgqANTPlkrwllDFAtsrkeaelksgvvrkdsmwdKLIFSkvqaslggRVRLMIT 432
Cdd:cd05936 211 EIRKHRVTIFPGVPTMYIAL-------LNAP------EFK--------------------KRDFS--------SLRLCIS 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 433 GAAPVSPTVLTFLRAALGCQFYEGYGQTECT-AGCTMSLPGDWTAGHVGAPLPCNFVKLVDvaEMNYFAANGE-GEVCVK 510
Cdd:cd05936 250 GGAPLPVEVAERFEELTGVPIVEGYGLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVD--DDGEELPPGEvGELWVR 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 511 GPNVFQGYLKDPEQTSgAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVFVhgd 590
Cdd:cd05936 328 GPQVMKGYWNRPEETA-EAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGGFNVYPREVEEVLYEHPAVAEAAV--- 402
|
490
....*....|....*
gi 528467778 591 slqaclVGvvVPDPD 605
Cdd:cd05936 403 ------VG--VPDPY 409
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
82-604 |
9.96e-52 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 187.70 E-value: 9.96e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 82 MTYYYkdaLTLYEFFLRGLRVsnngpcLGSRKA----GQPYkwlSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNR 157
Cdd:PRK06187 1 MQDYP---LTIGRILRHGARK------HPDKEAvyfdGRRT---TYAELDERVNRLANALRALG-VKKGDR-VAVFDWNS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 158 PEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIcdiADKARL-ILDCVSGRKHSVTTIVIMESFDSEltaq 236
Cdd:PRK06187 67 HEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVL---VDSEFVpLLAAILPQLPTVRTVIVEGDGPAA---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 237 aqNCGIDIISLKELEAiGKANHKTPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSN---CSAFIKITEvhcmlnqTD 313
Cdd:PRK06187 140 --PLAPEVGEYEELLA-AASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHslaVCAWLKLSR-------DD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 314 IHISYLPLAHMFERVVEGVLLCHGAKI---GYFqgDIRLLMDDLKNLKPTIFPVVPRLLNRMFdkifgQANTPLKRWLld 390
Cdd:PRK06187 210 VYLVIVPMFHVHAWGLPYLALMAGAKQvipRRF--DPENLLDLIETERVTFFFAVPTIWQMLL-----KAPRAYFVDF-- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 391 fatsrkeaelksgvvrkdsmwdklifskvqaslgGRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSL 470
Cdd:PRK06187 281 ----------------------------------SSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVLP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 471 P-----GDWT-AGHVGAPLPCNFVKLVDvAEMNYFAANGE--GEVCVKGPNVFQGYLKDPEQTSGAVDKaGWLHTGDIGK 542
Cdd:PRK06187 327 PedqlpGQWTkRRSAGRPLPGVEARIVD-DDGDELPPDGGevGEIIVRGPWLMQGYWNRPEATAETIDG-GWLHTGDVGY 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528467778 543 WLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSDPVAQVFVhgdslqaclVGvvVPDP 604
Cdd:PRK06187 405 IDEDGYLYITDRIKDVIISG-GENIYPRELEDALYGHPAVAEVAV---------IG--VPDE 454
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
232-677 |
5.76e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 180.68 E-value: 5.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 232 ELTAQAQNCGIDIISLKELEAIGKANHKTpIPPKPEDLALICFTSGTTGNPKGAMLTHGNV------VSNCSAFIKITEV 305
Cdd:PTZ00342 270 DLKEKAKKLGISIILFDDMTKNKTTNYKI-QNEDPDFITSIVYTSGTSGKPKGVMLSNKNLyntvvpLCKHSIFKKYNPK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 306 HcmlnqtdiHISYLPLAHMFERVVEGVLLCHGAKIGYFQGDIRLLMDDLKNLKPTIFPVVPRLLNRMFDKIFGQAN--TP 383
Cdd:PTZ00342 349 T--------HLSYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINnlPP 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 384 LKRWLLDFATSRKEAELK---SGVVRKDSMWDKLIFSKVQASLggrvRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQT 460
Cdd:PTZ00342 421 LKRFLVKKILSLRKSNNNggfSKFLEGITHISSKIKDKVNPNL----EVILNGGGKLSPKIAEELSVLLNVNYYQGYGLT 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 461 ECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDVAEMnyFAANG---EGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHT 537
Cdd:PTZ00342 497 ETTGPIFVQHADDNNTESIGGPISPNTKYKVRTWET--YKATDtlpKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKT 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 538 GDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSDPVAQVFVHG-DSLQACLvGVVVPDPDFLPGWAKNRGI 616
Cdd:PTZ00342 575 GDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGdDSMDGPL-AIISVDKYLLFKCLKDDNM 653
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528467778 617 -------EGSFNDLCKSKEVKNAIL-----EDMIQLGKEAGLKSFEQVRDIALHLEMFSVQNgLLTPTLKAKR 677
Cdd:PTZ00342 654 lestginEKNYLEKLTDETINNNIYvdyvkGKMLEVYKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKR 725
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
121-604 |
1.05e-45 |
|
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: 168.56 E-value: 1.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIdkasittiic 200
Cdd:cd17631 21 LTYAELDERVNRLAHALRALG-VAKGDR-VAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYIL---------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 201 diadkarlildcvsgrKHSVTTIVImesfdseltaqaqncgidiislkeleaigkanhktpippkpEDLALICFTSGTTG 280
Cdd:cd17631 89 ----------------ADSGAKVLF-----------------------------------------DDLALLMYTSGTTG 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 281 NPKGAMLTHGNV---VSNCSAFIKITEvhcmlnqTDIHISYLPLahmfervvegvllCHGAKIGYFqgdirllmddlknl 357
Cdd:cd17631 112 RPKGAMLTHRNLlwnAVNALAALDLGP-------DDVLLVVAPL-------------FHIGGLGVF-------------- 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 358 kptifpVVPRLLNrmfdkifGQANTPLKRWLLD--FATSRKEAELKSGVVrkDSMWDKLI----FSKVQASlggRVRLMI 431
Cdd:cd17631 158 ------TLPTLLR-------GGTVVILRKFDPEtvLDLIERHRVTSFFLV--PTMIQALLqhprFATTDLS---SLRAVI 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 432 TGAAPVSPTVLTFLRAAlGCQFYEGYGQTECTAGCTMSLPGDW--TAGHVGAPLPCNFVKLVDvAEMNYFAANGEGEVCV 509
Cdd:cd17631 220 YGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHrrKLGSAGRPVFFVEVRIVD-PDGREVPPGEVGEIVV 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 510 KGPNVFQGYLKDPEQTSGAVDKaGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYIRSDPVAQVFVHG 589
Cdd:cd17631 298 RGPHVMAGYWNRPEATAAAFRD-GWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDVLYEHPAVAEVAVIG 375
|
490
....*....|....*
gi 528467778 590 dslqaclvgvvVPDP 604
Cdd:cd17631 376 -----------VPDE 379
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
121-606 |
6.86e-39 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 149.36 E-value: 6.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGHSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIc 200
Cdd:cd05941 12 ITYADLVARAARLANRLLALGKDLRGDR-VAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 201 diadkarlildcvsgrkhsvttivimesfdseltaqaqncgidiislkeleaigkanhktpippkpeDLALICFTSGTTG 280
Cdd:cd05941 90 -------------------------------------------------------------------DPALILYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 281 NPKGAMLTHGNVVSNCSAFIKITEvhcmLNQTDIHISYLPLAHmfervVEGV---LLC---HGAKI---GYFQGDIRLLM 351
Cdd:cd05941 103 RPKGVVLTHANLAANVRALVDAWR----WTEDDVLLHVLPLHH-----VHGLvnaLLCplfAGASVeflPKFDPKEVAIS 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 352 DDLKNLkpTIFPVVP----RLL---NRMFDkifgqantplkrwllDFATSRKEAElksgvvrkdsmwdklifskvqaslg 424
Cdd:cd05941 174 RLMPSI--TVFMGVPtiytRLLqyyEAHFT---------------DPQFARAAAA------------------------- 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 425 GRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTEctAGCTMSLP--GDWTAGHVGAPLPCNFVKLVDVAEMNYFAAN 502
Cdd:cd05941 212 ERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVDEETGEPLPRG 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 503 GEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKK-HIFKlAQGEYIAPEKIEniyirsdp 581
Cdd:cd05941 290 EVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEIE-------- 360
|
490 500
....*....|....*....|....*
gi 528467778 582 vAQVFVHGDSLQACLVGvvVPDPDF 606
Cdd:cd05941 361 -RVLLAHPGVSECAVIG--VPDPDW 382
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
266-606 |
2.81e-38 |
|
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: 145.50 E-value: 2.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 266 PEDLALICFTSGTTGNPKGAMLTHGNVVSNcSAFIKitevHCM-LNQTDIHISYLPLAHMFERVVeGVLLC--HGAKIGY 342
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNN-GYFIG----ERLgLTEQDRLCIPVPLFHCFGSVL-GVLACltHGATMVF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 343 ----FqgDIRLLMDDLKNLKPTIFPVVPRllnrMFdkifgqantplkrwlldfatsrkEAELKSGvvrkdsmwDKLIFSK 418
Cdd:cd05917 75 pspsF--DPLAVLEAIEKEKCTALHGVPT----MF-----------------------IAELEHP--------DFDKFDL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 419 vqaslgGRVRLMITGAAPVSPTVLTFLRAALGC-QFYEGYGQTECTAGCTMSLPGD---WTAGHVGAPLPCNFVKLVDVA 494
Cdd:cd05917 118 ------SSLRTGIMAGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDsieKRVNTVGRIMPHTEAKIVDPE 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 495 EMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIEN 574
Cdd:cd05917 192 GGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGENIYPREIEE 270
|
330 340 350
....*....|....*....|....*....|..
gi 528467778 575 IyirsdpvaqVFVHGDSLQACLVGvvVPDPDF 606
Cdd:cd05917 271 F---------LHTHPKVSDVQVVG--VPDERY 291
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
114-604 |
3.29e-38 |
|
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: 148.61 E-value: 3.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 114 AGQPYKWLSYKEVADRAE-FAGSalLHRGHSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDK 192
Cdd:cd05926 8 VPGSTPALTYADLAELVDdLARQ--LAALGIKKGDR-VAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 193 ASiTTIIcdIADKARLiLDCVSGRKHSVTTIVimesfdsELTAQAQNCgIDIISLKEL--EAIGKANHKTPIPPKPEDLA 270
Cdd:cd05926 85 LG-SKLV--LTPKGEL-GPASRAASKLGLAIL-------ELALDVGVL-IRAPSAESLsnLLADKKNAKSEGVPLPDDLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 271 LICFTSGTTGNPKGAMLTHGNVVSNCSAfikITEVHCmLNQTDIHISYLPLAHMFERVVeGVL--LCHGAKIgyfqgdir 348
Cdd:cd05926 153 LILHTSGTTGRPKGVPLTHRNLAASATN---ITNTYK-LTPDDRTLVVMPLFHVHGLVA-SLLstLAAGGSV-------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 349 lLM----------DDLKNLKPTIFPVVPRLLnrmfdKIfgqantplkrwLLDFATSRKEAELksgvvrkdsmwdklifsk 418
Cdd:cd05926 220 -VLpprfsastfwPDVRDYNATWYTAVPTIH-----QI-----------LLNRPEPNPESPP------------------ 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 419 vqaslgGRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAgcTMSL----PGDWTAGHVGAPlpcNFVKLVDVA 494
Cdd:cd05926 265 ------PKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAH--QMTSnplpPGPRKPGSVGKP---VGVEVRILD 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 495 EM-NYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIE 573
Cdd:cd05926 334 EDgEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVD 412
|
490 500 510
....*....|....*....|....*....|.
gi 528467778 574 NIYIRSDPVAQVFVHGdslqaclvgvvVPDP 604
Cdd:cd05926 413 GVLLSHPAVLEAVAFG-----------VPDE 432
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
265-605 |
2.62e-37 |
|
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: 146.23 E-value: 2.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 265 KPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEVhcMLNQTDIHISYLPLAHM--FERVVEGVLLChGAKI-- 340
Cdd:cd05904 156 KQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGS--NSDSEDVFLCVLPMFHIygLSSFALGLLRL-GATVvv 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 341 -GYFqgDIRLLMDDLKNLKPTIFPVVPrllnrmfdkifgqantPLkrwLLDFAtsrkeaelksgvvrKDSMWDKLIFSKV 419
Cdd:cd05904 233 mPRF--DLEELLAAIERYKVTHLPVVP----------------PI---VLALV--------------KSPIVDKYDLSSL 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 420 qaslggrvRLMITGAAPVSPTVLTFLRAAL-GCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAP---LPCNFVKLVDVAE 495
Cdd:cd05904 278 --------RQIMSGAAPLGKELIEAFRAKFpNVDLGQGYGMTESTGVVAMCFAPEKDRAKYGSVgrlVPNVEAKIVDPET 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 496 MNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 575
Cdd:cd05904 350 GESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEAL 428
|
330 340 350
....*....|....*....|....*....|
gi 528467778 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 |
2.70e-37 |
|
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: 145.94 E-value: 2.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 263 PPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEvhcmLNQTDIHISYLPLAHMFERVVEGVL-LCHGAKIG 341
Cdd:cd05909 143 PVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFD----PNPEDVVFGALPFFHSFGLTGCLWLpLLSGIKVV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 342 YFQgdirllmddlknlKPTIFPVVPRLlnrmfdkIFGQANTPLkrwlldFATSrkeaELKSGVVRKdsmWDKLIFSkvqa 421
Cdd:cd05909 219 FHP-------------NPLDYKKIPEL-------IYDKKATIL------LGTP----TFLRGYARA---AHPEDFS---- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 422 slggRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPG-DWTAGHVGAPLPCNFVKLVDVAEMNYFA 500
Cdd:cd05909 262 ----SLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVP 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 501 ANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKaGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSD 580
Cdd:cd05909 338 IGEGGLLLVRGPNVMLGYLNEPELTSFAFGD-GWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDILSEIL 415
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 528467778 581 P----VAQVFV----HGDSLQACLVGvVVPDPDFLPGWAKNRGIE 617
Cdd:cd05909 416 PedneVAVVSVpdgrKGEKIVLLTTT-TDTDPSSLNDILKNAGIS 459
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
232-614 |
3.56e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 147.07 E-value: 3.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 232 ELTAQAQNcgidIISLKEL--EAIGKANHKTPIP-PKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCS---AFIKitev 305
Cdd:PRK05605 185 ALTGPAPG----TVPWETLvdAAIGGDGSDVSHPrPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqgkAWVP---- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 306 hCMLNQTDIHISYLPLAHMFervveGVLLCH------GAKIGYFQG-DIRLLMDDLKNLKPTIFPVVPRLlnrmFDKIfg 378
Cdd:PRK05605 257 -GLGDGPERVLAALPMFHAY-----GLTLCLtlavsiGGELVLLPApDIDLILDAMKKHPPTWLPGVPPL----YEKI-- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 379 qantplkrwlldfatsRKEAElKSGVvrkdsmwdklifskvqaSLGGrVRLMITGAAPVSPTVLTFLRAALGCQFYEGYG 458
Cdd:PRK05605 325 ----------------AEAAE-ERGV-----------------DLSG-VRNAFSGAMALPVSTVELWEKLTGGLLVEGYG 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 459 QTECT---AGCTMSlpGDWTAGHVGAPLPCNFVKLVDVAEMNYFAANGE-GEVCVKGPNVFQGYLKDPEQTSgAVDKAGW 534
Cdd:PRK05605 370 LTETSpiiVGNPMS--DDRRPGYVGVPFPDTEVRIVDPEDPDETMPDGEeGELLVRGPQVFKGYWNRPEETA-KSFLDGW 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 535 LHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVFVHG-------DSLQACLV---GVVVpDP 604
Cdd:PRK05605 447 FRTGDVVVMEEDGFIRIVDRIKELI-ITGGFNVYPAEVEEVLREHPGVEDAAVVGlpredgsEEVVAAVVlepGAAL-DP 524
|
410
....*....|
gi 528467778 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 |
1.01e-36 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 142.97 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 123 YKEVADRAEfagsaLLHRGHSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIICDi 202
Cdd:TIGR01923 6 DCEAAHLAK-----ALKAQGIRSGSR-VALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 203 adkarlildcvsgrkhsvttivimESFDSEltaqaqncGIDIISLKELEAIGKANHKTPIPPKPEDLALICFTSGTTGNP 282
Cdd:TIGR01923 79 ------------------------SLLEEK--------DFQADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 283 KGAMLTHGN----VVSNCSAFiKITEVHCMLnqtdihiSYLPLAHmfervVEGV-----LLCHGAKIGYFQGDIRLLmDD 353
Cdd:TIGR01923 127 KAVPHTFRNhyasAVGSKENL-GFTEDDNWL-------LSLPLYH-----ISGLsilfrWLIEGATLRIVDKFNQLL-EM 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 354 LKNLKPTIFPVVPRLLNRMFDKifGQANTPLKRWLLdfatsrkeaelksgvvrkdsmwdklifskvqaslGGrvrlmitG 433
Cdd:TIGR01923 193 IANERVTHISLVPTQLNRLLDE--GGHNENLRKILL----------------------------------GG-------S 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 434 AAPVsptvlTFLRAAL--GCQFYEGYGQTE-CTAGCTMSLPGDWTAGHVGAPLPCNFVKL-VDVAEmnyfaanGEGEVCV 509
Cdd:TIGR01923 230 AIPA-----PLIEEAQqyGLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIkVDNKE-------GHGEIMV 297
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528467778 510 KGPNVFQGYLkDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVFV 587
Cdd:TIGR01923 298 KGANLMKGYL-YQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVV 373
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
245-605 |
3.74e-35 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 140.78 E-value: 3.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 245 ISLKELEAIGKANHKTPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNcsafikITEVHCMLNQT-------DIHIS 317
Cdd:PRK08751 186 IRFREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVAN------MQQAHQWLAGTgkleegcEVVIT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 318 YLPLAHMFERVVEGVLLCHGAKIGYFQGDIRLLMDDLKNLKPTIFPVVPRLlNRMFDKIFgqaNTPlkrwlldfatsrke 397
Cdd:PRK08751 260 ALPLYHIFALTANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGV-NTLFNGLL---NTP-------------- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 398 aelksgvvrkdsMWDKLIFSKVQASLGGrvrlmitGAApVSPTVLTFLRAALGCQFYEGYGQTECT-AGCTMSLPGDWTA 476
Cdd:PRK08751 322 ------------GFDQIDFSSLKMTLGG-------GMA-VQRSVAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYN 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 477 GHVGAPLPCNFVKLVDvaEMNYFAANGE-GEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRK 555
Cdd:PRK08751 382 GSIGLPIPSTDACIKD--DAGTVLAIGEiGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRK 459
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 528467778 556 KHIFkLAQGEYIAPEKIENIYIRSDPVAQVFVHG--DSLQACLVGVVVPDPD 605
Cdd:PRK08751 460 KDMI-LVSGFNVYPNEIEDVIAMMPGVLEVAAVGvpDEKSGEIVKVVIVKKD 510
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
172-608 |
4.58e-34 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 136.03 E-value: 4.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 172 LVAVPLYDTLGTEAISYVIDKASITTIICDiadkarlildcvsgrkhsvttivimESFDSELTAQAQNCGIDIISLKElE 251
Cdd:cd05922 47 LVFVPLNPTLKESVLRYLVADAGGRIVLAD-------------------------AGAADRLRDALPASPDPGTVLDA-D 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 252 AIGKANHKTP-IPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEVHcmlnQTDIHISYLPLAHMFervve 330
Cdd:cd05922 101 GIRAARASAPaHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGIT----ADDRALTVLPLSYDY----- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 331 G--VLLCH---GAKIgYFQGDIRL---LMDDLKNLKPTIFPVVP---RLLNRMfdkIFGQANTPLKRWLldfatsrkeae 399
Cdd:cd05922 172 GlsVLNTHllrGATL-VLTNDGVLddaFWEDLREHGATGLAGVPstyAMLTRL---GFDPAKLPSLRYL----------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 400 lksgvvrkdsmwdklifskvqASLGGRVRlmitgaapvsPTVLTFLRAAL-GCQFYEGYGQTECTAGCTMsLPGDWTA-- 476
Cdd:cd05922 237 ---------------------TQAGGRLP----------QETIARLRELLpGAQVYVMYGQTEATRRMTY-LPPERILek 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 477 -GHVGAPLP-CNFVKLVDVAEMnyfAANGE-GEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIID 553
Cdd:cd05922 285 pGSIGLAIPgGEFEILDDDGTP---TPPGEpGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVG 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528467778 554 RKKHIFKLAqGEYIAPEKIENIyIRSDPVAQVFV-------HGDSLQACLVGVVVPDPDFLP 608
Cdd:cd05922 362 RRDRMIKLF-GNRISPTEIEAA-ARSIGLIIEAAavglpdpLGEKLALFVTAPDKIDPKDVL 421
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
147-605 |
7.53e-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: 7.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 147 DKYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIICdiadkARLILDCVSGRKHSVTTIVIM 226
Cdd:cd17642 69 NDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFC-----SKKGLQKVLNVQKKLKIIKTI 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 227 ESFDSELTAQAQNCGIDIISLKELEAIGKANHKTPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEVH 306
Cdd:cd17642 144 IILDSKEDYKGYQCLYTFITQNLPPGFNEYDFKPPSFDRDEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGN 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 307 CMLNQTDIhISYLPLAHMFERVVEGVLLCHGAKIGY-FQGDIRLLMDDLKNLKPTIFPVVPRLLnrmfdkifgqantplk 385
Cdd:cd17642 224 QIIPDTAI-LTVIPFHHGFGMFTTLGYLICGFRVVLmYKFEEELFLRSLQDYKVQSALLVPTLF---------------- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 386 rwlldfatsrkeaelksGVVRKDSMWDKLIFSKVQAslggrvrlMITGAAPVSPTVLTFLRAALGCQFY-EGYGQTECTA 464
Cdd:cd17642 287 -----------------AFFAKSTLVDKYDLSNLHE--------IASGGAPLSKEVGEAVAKRFKLPGIrQGYGLTETTS 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 465 GCTMSLPGDWTAGHVGAPLPCNFVKLVDVAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWL 544
Cdd:cd17642 342 AILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYD 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528467778 545 PNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDPVAQVFVHGdslqaclvgvvVPDPD 605
Cdd:cd17642 422 EDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQHPKIFDAGVAG-----------IPDED 470
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
243-604 |
8.18e-34 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 136.72 E-value: 8.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 243 DIISLKELEAIGKanHKTPIPP--KPEDLALICFTSGTTGNPKGAMLTHGNVVSNC-------SAFIKitevhcmlNQTD 313
Cdd:PRK08974 182 DAISFRSALHKGR--RMQYVKPelVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqakaayGPLLH--------PGKE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 314 IHISYLPLAHMFERVVEGVLLCHgakigyfQGDIRLLMDDLKNLKPTifpvVPRLLNRMFDKIFGqANTPLKRWLldfat 393
Cdd:PRK08974 252 LVVTALPLYHIFALTVNCLLFIE-------LGGQNLLITNPRDIPGF----VKELKKYPFTAITG-VNTLFNALL----- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 394 srKEAELKsgvvrkdsmwdKLIFSkvqaslggRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECT---AGCTMSL 470
Cdd:PRK08974 315 --NNEEFQ-----------ELDFS--------SLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVNPYDL 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 471 PGdwTAGHVGAPLPCNFVKLVDvaEMNYFAANGE-GEVCVKGPNVFQGYLKDPEQTSgAVDKAGWLHTGDIGKWLPNGTL 549
Cdd:PRK08974 374 DY--YSGSIGLPVPSTEIKLVD--DDGNEVPPGEpGELWVKGPQVMLGYWQRPEATD-EVIKDGWLATGDIAVMDEEGFL 448
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 528467778 550 KIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVFV----HGDSLQACLVGVVVPDP 604
Cdd:PRK08974 449 RIVDRKKDMI-LVSGFNVYPNEIEDVVMLHPKVLEVAAvgvpSEVSGEAVKIFVVKKDP 506
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
268-589 |
1.26e-33 |
|
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: 131.85 E-value: 1.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 268 DLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEVhcmlNQTDIHISYLPLAHMFERVVeGVLLC--HGAKI---GY 342
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADL----TEDDRYLIINPFFHTFGYKA-GIVACllTGATVvpvAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 343 FqgDIRLLMDDLKNLKPTIFPVVPRLLNRMFDKifgqantplkrwlldfaTSRKEAELKSgvvrkdsmwdklifskvqas 422
Cdd:cd17638 76 F--DVDAILEAIERERITVLPGPPTLFQSLLDH-----------------PGRKKFDLSS-------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 423 lggrVRLMITGAAPVSPTVLTFLRAALGCQ-FYEGYGQTECTAGcTMSLPGD---WTAGHVGAPLPCNFVKLVDvaemny 498
Cdd:cd17638 117 ----LRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVA-TMCRPGDdaeTVATTCGRACPGFEVRIAD------ 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 499 faangEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIR 578
Cdd:cd17638 186 -----DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGALAE 259
|
330
....*....|.
gi 528467778 579 SDPVAQVFVHG 589
Cdd:cd17638 260 HPGVAQVAVIG 270
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
91-589 |
3.10e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 134.90 E-value: 3.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 91 TLYEFFLRGLRVSNNGPCLGSRKAGQPYkwlSYKEVADRAEFAGSALLHRGHsQSGDKyIGIFAQNRPEWTISELACYTY 170
Cdd:PRK12583 19 TIGDAFDATVARFPDREALVVRHQALRY---TWRQLADAVDRLARGLLALGV-QPGDR-VGIWAPNCAEWLLTQFATARI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 171 SLVAVPLYDTLGTEAISYVIDKASITTIICDIADKAR----LILDCVSGRKHSVTTIVIME---------SFDSE----- 232
Cdd:PRK12583 94 GAILVNINPAYRASELEYALGQSGVRWVICADAFKTSdyhaMLQELLPGLAEGQPGALACErlpelrgvvSLAPApppgf 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 233 LTAQAQNCGIDIISLKELEAIGKANHktpippkPEDLALICFTSGTTGNPKGAMLTHGNVVSNcsAFIKITEVHcmLNQT 312
Cdd:PRK12583 174 LAWHELQARGETVSREALAERQASLD-------RDDPINIQYTSGTTGFPKGATLSHHNILNN--GYFVAESLG--LTEH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 313 DIHISYLPLAHMFERVVeGVLLC--HGAKIGYFQG--DIRLLMDDLKNLKPTIFPVVPRllnrMFdkiFGQANTPlkrwl 388
Cdd:PRK12583 243 DRLCVPVPLYHCFGMVL-ANLGCmtVGACLVYPNEafDPLATLQAVEEERCTALYGVPT----MF---IAELDHP----- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 389 ldfatSRKEAELKSgvvrkdsmwdklifskvqaslggrVRLMITGAAPVSPTVLTFLRAALGC-QFYEGYGQTECTAGCT 467
Cdd:PRK12583 310 -----QRGNFDLSS------------------------LRTGIMAGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 468 MSLPGD---WTAGHVGAPLPCNFVKLVDvAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWL 544
Cdd:PRK12583 361 QTTAADdleRRVETVGRTQPHLEVKVVD-PDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMD 439
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 528467778 545 PNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVFVHG 589
Cdd:PRK12583 440 EQGYVRIVGRSKDMI-IRGGENIYPREIEEFLFTHPAVADVQVFG 483
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
121-603 |
4.72e-32 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 129.42 E-value: 4.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKAsittiic 200
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALG-VGPGDV-VAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRA------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 201 diadKARLIldcvsgrkhsvttiVIMESFdseltaqaqncgidiislkeleaiGKANHKtpipPKPEDLALICFTSGTTG 280
Cdd:cd05903 73 ----KAKVF--------------VVPERF------------------------RQFDPA----AMPDAVALLLFTSGTTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 281 NPKGAMLTHGNVVSNCSAFIKitevHCMLNQTDIHISYLPLAHMfervvEGVLlcHGAKIGYFQGDIRLLMDDLKNLKpt 360
Cdd:cd05903 107 EPKGVMHSHNTLSASIRQYAE----RLGLGPGDVFLVASPMAHQ-----TGFV--YGFTLPLLLGAPVVLQDIWDPDK-- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 361 ifpvVPRLLNRmfDKI-FGQANTPlkrwlldFATSRKEAELKSGVVRKdsmwdklifskvqaslggRVRLMITGAAPVSP 439
Cdd:cd05903 174 ----ALALMRE--HGVtFMMGATP-------FLTDLLNAVEEAGEPLS------------------RLRTFVCGGATVPR 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 440 TVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGD-WTAGHV-GAPLPCNFVKLVDvAEMNYFAANGEGEVCVKGPNVFQG 517
Cdd:cd05903 223 SLARRAAELLGAKVCSAYGSTECPGAVTSITPAPeDRRLYTdGRPLPGVEIKVVD-DTGATLAPGVEGELLSRGPSVFLG 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 518 YLKDPEQTSGAVDKaGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIyirsdpvaqVFVHGDSLQACLV 597
Cdd:cd05903 302 YLDRPDLTADAAPE-GWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDL---------LLGHPGVIEAAVV 370
|
....*.
gi 528467778 598 GvvVPD 603
Cdd:cd05903 371 A--LPD 374
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
122-604 |
1.98e-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: 1.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 122 SYKEVADRAEFAGSALLHRGhSQSGDkYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIICD 201
Cdd:cd05934 5 TYAELLRESARIAAALAALG-IRPGD-RVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 202 iadkarlildcvsgrkhsvttivimesfdseltaqaqncgidiislkeleaigkanhktpippkpedLALICFTSGTTGN 281
Cdd:cd05934 83 -------------------------------------------------------------------PASILYTSGTTGP 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 282 PKGAMLTHGNVVSNCSAFIKitevHCMLNQTDIHISYLPLAHMfERVVEGVL--LCHGAKI--------GYFQGDIRllm 351
Cdd:cd05934 96 PKGVVITHANLTFAGYYSAR----RFGLGEDDVYLTVLPLFHI-NAQAVSVLaaLSVGATLvllprfsaSRFWSDVR--- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 352 ddlkNLKPTIF---PVVPRLLnrmfdkifgqANTPlkrwlldfatsrkeaelksgvvrkDSMWDKlifskvqaslGGRVR 428
Cdd:cd05934 168 ----RYGATVTnylGAMLSYL----------LAQP------------------------PSPDDR----------AHRLR 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 429 LmiTGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDvaEMNYFAANGE-GEV 507
Cdd:cd05934 200 A--AYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVD--DDGQELPAGEpGEL 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 508 CVK---GPNVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYIRSDPVAQ 584
Cdd:cd05934 276 VIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVERAILRHPAVRE 353
|
490 500
....*....|....*....|
gi 528467778 585 VFVHGdslqaclvgvvVPDP 604
Cdd:cd05934 354 AAVVA-----------VPDE 362
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
245-603 |
6.50e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 127.96 E-value: 6.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 245 ISLKELEAIGKANHKTPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSN---CSAFIKITevhcmLNQ-TDIHISYLP 320
Cdd:PRK05677 185 VKFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANmlqCRALMGSN-----LNEgCEILIAPLP 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 321 LAHMFERVVE-GVLLCHGAKigyfqgdiRLLMDDlknlkPTIFPVVPRLLNRMFDKIFGQANTplkrwlLDFATSRKEAe 399
Cdd:PRK05677 260 LYHIYAFTFHcMAMMLIGNH--------NILISN-----PRDLPAMVKELGKWKFSGFVGLNT------LFVALCNNEA- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 400 lksgvvrkdsmWDKLIFSKVQASLGGRVRLMITGAapvsptvlTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHV 479
Cdd:PRK05677 320 -----------FRKLDFSALKLTLSGGMALQLATA--------ERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTI 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 480 GAPLPCNFVKLVDvAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIF 559
Cdd:PRK05677 381 GIPVPSTLCKVID-DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI 459
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 528467778 560 kLAQGEYIAPEKIENIyirsdpvaqVFVHGDSLQACLVGvvVPD 603
Cdd:PRK05677 460 -LVSGFNVYPNELEDV---------LAALPGVLQCAAIG--VPD 491
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
121-586 |
6.61e-31 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 128.00 E-value: 6.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAV---PLYDTlgtEAISYVIDKASITT 197
Cdd:PRK08315 44 WTYREFNEEVDALAKGLLALG-IEKGDR-VGIWAPNVPEWVLTQFATAKIGAILVtinPAYRL---SELEYALNQSGCKA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 198 IIC-------DIADKARLIL----DCVSGRKHSV------TTIVI-------MESFDsELTAQAQNcgidiISLKELEAI 253
Cdd:PRK08315 119 LIAadgfkdsDYVAMLYELApelaTCEPGQLQSArlpelrRVIFLgdekhpgMLNFD-ELLALGRA-----VDDAELAAR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 254 GKANHktpippkPEDLALICFTSGTTGNPKGAMLTHGNVVSNcsAFIkITEvhCM-LNQTD---IHIsylPLAHMFErVV 329
Cdd:PRK08315 193 QATLD-------PDDPINIQYTSGTTGFPKGATLTHRNILNN--GYF-IGE--AMkLTEEDrlcIPV---PLYHCFG-MV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 330 EGVLLC--HGAKIGY----FqgdirllmDDLKNLK-------------PTIFpvVPRLLNRMFDKifgqantplkrwlLD 390
Cdd:PRK08315 257 LGNLACvtHGATMVYpgegF--------DPLATLAaveeerctalygvPTMF--IAELDHPDFAR-------------FD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 391 FATsrkeaeLKSGV---------VRKdsmwdklifsKVQASLGgrvrlM--ITGAapvsptvltflraalgcqfyegYGQ 459
Cdd:PRK08315 314 LSS------LRTGImagspcpieVMK----------RVIDKMH-----MseVTIA----------------------YGM 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 460 TECTAGCTMSLPGD------WTaghVGAPLPCNFVKLVDvAEMNYFAANGE-GEVCVKGPNVFQGYLKDPEQTSGAVDKA 532
Cdd:PRK08315 351 TETSPVSTQTRTDDplekrvTT---VGRALPHLEVKIVD-PETGETVPRGEqGELCTRGYSVMKGYWNDPEKTAEAIDAD 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 528467778 533 GWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPV--AQVF 586
Cdd:PRK08315 427 GWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEFLYTHPKIqdVQVV 481
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
68-577 |
7.71e-31 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 127.40 E-value: 7.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 68 EYARRSILMDndthmtYYYKDALTLYEF-FLRGLRVSNNgPCLGSRKAGQPYkwlSYKEVADRAEFAGSALLHRGHSQsG 146
Cdd:PLN02246 7 EFIFRSKLPD------IYIPNHLPLHDYcFERLSEFSDR-PCLIDGATGRVY---TYADVELLSRRVAAGLHKLGIRQ-G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 147 DkYIGIFAQNRPEWTISELACYTYSLV---AVPLYdtlgTEAISYVIDKASITTIICDIA---DKARLILDcvsgrKHSV 220
Cdd:PLN02246 76 D-VVMLLLPNCPEFVLAFLGASRRGAVtttANPFY----TPAEIAKQAKASGAKLIITQScyvDKLKGLAE-----DDGV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 221 TTIVIMESFD-----SELTAQAQNcgidiiSLKELEAigkanhktpippKPEDLALICFTSGTTGNPKGAMLTHGNVVSN 295
Cdd:PLN02246 146 TVVTIDDPPEgclhfSELTQADEN------ELPEVEI------------SPDDVVALPYSSGTTGLPKGVMLTHKGLVTS 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 296 CSAFIKITEVHCMLNQTDIHISYLPLAHMFErvVEGVLLCH---GAKIGYFQG-DIRLLMDDLKNLKPTIFPVVPrllnr 371
Cdd:PLN02246 208 VAQQVDGENPNLYFHSDDVILCVLPMFHIYS--LNSVLLCGlrvGAAILIMPKfEIGALLELIQRHKVTIAPFVP----- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 372 mfdkifgqantPLkrwLLDFAtsrkeaelKSGVVRKDSMwdklifskvqASlggrVRLMITGAAPVSPTVLTFLRAAL-G 450
Cdd:PLN02246 281 -----------PI---VLAIA--------KSPVVEKYDL----------SS----IRMVLSGAAPLGKELEDAFRAKLpN 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 451 CQFYEGYGQTECTAGCTMSL-----PGDWTAGHVGAPLPCNFVKLVDVAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQT 525
Cdd:PLN02246 325 AVLGQGYGMTEAGPVLAMCLafakePFPVKSGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYLNDPEAT 404
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 528467778 526 SGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYI 577
Cdd:PLN02246 405 ANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAELEALLI 455
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
121-604 |
1.89e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 126.25 E-value: 1.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYdTLGTEA-ISYVIDKASITTII 199
Cdd:PRK06188 38 LTYGQLADRISRYIQAFEALG-LGTGDA-VALLSLNRPEVLMAIGAAQLAGLRRTALH-PLGSLDdHAYVLEDAGISTLI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 200 CD---IADKARLILDCVSGRKHSvttivimesfdseLTAQAQNCGIDIislkeLEAIGKANHKTPIPPK-PEDLALICFT 275
Cdd:PRK06188 115 VDpapFVERALALLARVPSLKHV-------------LTLGPVPDGVDL-----LAAAAKFGPAPLVAAAlPPDIAGLAYT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 276 SGTTGNPKGAMLTHGNVVsncsafikiTEVHCMLNQTDI--HISYL---PLAHMFERVVEGVLLcHGAKIGYFQG-DIRL 349
Cdd:PRK06188 177 GGTTGKPKGVMGTHRSIA---------TMAQIQLAEWEWpaDPRFLmctPLSHAGGAFFLPTLL-RGGTVIVLAKfDPAE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 350 LMDDLKNLKPTIFPVVPRLLNRmfdkifgqantplkrwLLDFATSRKeAELKSgvvrkdsmwdklifskvqaslggrVRL 429
Cdd:PRK06188 247 VLRAIEEQRITATFLVPTMIYA----------------LLDHPDLRT-RDLSS------------------------LET 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 430 MITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHV------GAPLPCNFVKLVDvAEMNYFAANG 503
Cdd:PRK06188 286 VYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLRVALLD-EDGREVAQGE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 504 EGEVCVKGPNVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIEniyirsDPVA 583
Cdd:PRK06188 365 VGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMI-VTGGFNVFPREVE------DVLA 436
|
490 500
....*....|....*....|.
gi 528467778 584 QvfvHGDSLQACLVGvvVPDP 604
Cdd:PRK06188 437 E---HPAVAQVAVIG--VPDE 452
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
268-605 |
2.51e-30 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 126.25 E-value: 2.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 268 DLALICFTSGTTGNPKGAMLTHGNVVSN-CSAFIKITEVhcMLNQTdIHISYLPLAHMFErvVEGV----LLCHGAKIGY 342
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTHRNLVANlCSSLFSVGPE--MIGQV-VTLGLIPFFHIYG--ITGIccatLRNKGKVVVM 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 343 FQGDIRLLMDDLKNLKPTIFPVVPRLLNRMFdkifgqantplkrwlldfatsrkeaelksgvvrKDSMWDKLIFSKVqas 422
Cdd:PLN02330 260 SRFELRTFLNALITQEVSFAPIVPPIILNLV---------------------------------KNPIVEEFDLSKL--- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 423 lggRVRLMITGAAPVSPTVLTFLRAAL-GCQFYEGYGQTECTagCTMSLPGDWTAGH-------VGAPLPCNFVKLVDVA 494
Cdd:PLN02330 304 ---KLQAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEHS--CITLTHGDPEKGHgiakknsVGFILPNLEVKFIDPD 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 495 EMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIEN 574
Cdd:PLN02330 379 TGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEA 457
|
330 340 350
....*....|....*....|....*....|.
gi 528467778 575 IYIRSDPVAQVfvhgdslqaclvgVVVPDPD 605
Cdd:PLN02330 458 ILLTHPSVEDA-------------AVVPLPD 475
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
121-605 |
2.97e-30 |
|
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: 124.18 E-value: 2.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGHSQsgDKYIGIFAQNRPEWTISELACytysLVA----VPLYDTLGTEAISYVIDKAsit 196
Cdd:cd05930 13 LTYAELDARANRLARYLRERGVGP--GDLVAVLLERSLEMVVAILAV----LKAgaayVPLDPSYPAERLAYILEDS--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 197 tiicdiadKARLILDCvsgrkhsvttivimesfdseltaqaqncgidiislkeleaigkanhktpippkPEDLALICFTS 276
Cdd:cd05930 84 --------GAKLVLTD-----------------------------------------------------PDDLAYVIYTS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 277 GTTGNPKGAMLTHGNVVSNCSAFIKITEVH---CMLNQT----DIHISYLPLAhmfervvegvlLCHGAKIgYF-----Q 344
Cdd:cd05930 103 GSTGKPKGVMVEHRGLVNLLLWMQEAYPLTpgdRVLQFTsfsfDVSVWEIFGA-----------LLAGATL-VVlpeevR 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 345 GDIRLLMDDLKNLKPTIFPVVPRLLNRMFDKIFGQANTPLkrwlldfatsrkeaelksgvvrkdsmwdklifskvqaslg 424
Cdd:cd05930 171 KDPEALADLLAEEGITVLHLTPSLLRLLLQELELAALPSL---------------------------------------- 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 425 grvRLMITGAAPVSPTVLT-FLRAALGCQFYEGYGQTECTAGCTM--SLPGDWTAGHV--GAPLPCNFVKLVDvAEMNYF 499
Cdd:cd05930 211 ---RLVLVGGEALPPDLVRrWRELLPGARLVNLYGPTEATVDATYyrVPPDDEEDGRVpiGRPIPNTRVYVLD-ENLRPV 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 500 AANGEGEVCVKGPNVFQGYLKDPEQTSGAV-----DKAGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIE 573
Cdd:cd05930 287 PPGVPGELYIGGAGLARGYLNRPELTAERFvpnpfGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIELGEIE 365
|
490 500 510
....*....|....*....|....*....|....*
gi 528467778 574 NIYIRSDPVAQVFV---HGDSLQACLVGVVVPDPD 605
Cdd:cd05930 366 AALLAHPGVREAAVvarEDGDGEKRLVAYVVPDEG 400
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
121-556 |
3.20e-30 |
|
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: 125.47 E-value: 3.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGhSQSGDKYIGIFAQNRPewTISEL-ACYTYSLVAVPLydtlgTEAISYVIDKASITTI- 198
Cdd:cd05906 40 QSYQDLLEDARRLAAGLRQLG-LRPGDSVILQFDDNED--FIPAFwACVLAGFVPAPL-----TVPPTYDEPNARLRKLr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 199 -ICDIADKARLIldcvsgrkhsvTTIVIMESFDsELTAQAQNCGIDIISLKELEAIGkANHKTPiPPKPEDLALICFTSG 277
Cdd:cd05906 112 hIWQLLGSPVVL-----------TDAELVAEFA-GLETLSGLPGIRVLSIEELLDTA-ADHDLP-QSRPDDLALLMLTSG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 278 TTGNPKGAMLTHGNVVSNCSAfikiTEVHCMLNQTDIHISYLPLAHmfervVEGVLLCHGAkigyfqgDIRLLMDDLKNL 357
Cdd:cd05906 178 STGFPKAVPLTHRNILARSAG----KIQHNGLTPQDVFLNWVPLDH-----VGGLVELHLR-------AVYLGCQQVHVP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 358 KPTIFPVVPRLLnRMFDKiFGQANTplkrWLLDFATSRKEAELKSgvvRKDSMWDkliFSkvqaslggRVRLMIT-GAAP 436
Cdd:cd05906 242 TEEILADPLRWL-DLIDR-YRVTIT----WAPNFAFALLNDLLEE---IEDGTWD---LS--------SLRYLVNaGEAV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 437 VSPTVLTFLR--AALGCQ---FYEGYGQTECTAGCTMSLP---GDWTAGH----VGAPLPCNFVKLVDvAEMNYFAANGE 504
Cdd:cd05906 302 VAKTIRRLLRllEPYGLPpdaIRPAFGMTETCSGVIYSRSfptYDHSQALefvsLGRPIPGVSMRIVD-DEGQLLPEGEV 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 528467778 505 GEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGkWLPNGTLKIIDRKK 556
Cdd:cd05906 381 GRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
262-604 |
5.30e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 125.15 E-value: 5.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 262 IPPKPE-DLALICFTSGTTGNPKGAMLTHGNVVSNcsAFIKITEVHCMLNQTDIHISYLPLAHMF-ERVVEGVLLCHGAK 339
Cdd:PRK06710 200 VPCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSN--TLMGVQWLYNCKEGEEVVLGVLPFFHVYgMTAVMNLSIMQGYK 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 340 IGYF-QGDIRLLMDDLKNLKPTIFPVVPRLLNRMFdkifgqaNTPLkrwlldfatsRKEAELKSgvvrkdsmwdklifsk 418
Cdd:PRK06710 278 MVLIpKFDMKMVFEAIKKHKVTLFPGAPTIYIALL-------NSPL----------LKEYDISS---------------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 419 vqaslggrVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTEcTAGCTMS--LPGDWTAGHVGAPLPCNFVKLVDVAEM 496
Cdd:PRK06710 325 --------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTE-SSPVTHSnfLWEKRVPGSIGVPWPDTEAMIMSLETG 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 497 NYFAANGEGEVCVKGPNVFQGYLKDPEQTSgAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 576
Cdd:PRK06710 396 EALPPGEIGEIVVKGPQIMKGYWNKPEETA-AVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREVEEVL 473
|
330 340
....*....|....*....|....*...
gi 528467778 577 IRSDPVAQVFVHGdslqaclvgvvVPDP 604
Cdd:PRK06710 474 YEHEKVQEVVTIG-----------VPDP 490
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
265-607 |
8.40e-30 |
|
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: 123.42 E-value: 8.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 265 KPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEvhcmLNQT-----------DIHI--SYLPLAHmfervveG 331
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALG----LTSEsrvlqfasytfDVSIleIFTTLAA-------G 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 332 VLLCHGAKigyfqgdiRLLMDDLknlkptifpvvPRLLNRMfdkifgQANTplkrwlldfatsrkeAELKSGVVRkdsmw 411
Cdd:cd05918 173 GCLCIPSE--------EDRLNDL-----------AGFINRL------RVTW---------------AFLTPSVAR----- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 412 dkLIFSKVQASLggrvRLMITGAAPVSPTVLTflRAALGCQFYEGYGQTECTAGCTMSLPG-DWTAGHVGAPLPCNFVkL 490
Cdd:cd05918 208 --LLDPEDVPSL----RTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRPLGATCW-V 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 491 VDVAEMNYFAANGE-GEVCVKGPNVFQGYLKDPEQTSGA-VDKAGWLH------------TGDIGKWLPNGTLKIIDRKK 556
Cdd:cd05918 279 VDPDNHDRLVPIGAvGELLIEGPILARGYLNDPEKTAAAfIEDPAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKD 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 528467778 557 HIFKLaQGEYIAPEKIENIYIRSDP-----VAQVFVH-GDSLQACLVGVVVPDPDFL 607
Cdd:cd05918 359 TQVKI-RGQRVELGEIEHHLRQSLPgakevVVEVVKPkDGSSSPQLVAFVVLDGSSS 414
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
245-604 |
2.27e-29 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 123.21 E-value: 2.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 245 ISLKELEAIGKANHKTPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNC--------SAFIKITEVHCMlnqtdIHI 316
Cdd:PRK07059 182 VRFNDALAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqmeawlqPAFEKKPRPDQL-----NFV 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 317 SYLPLAHMFERVVEGVLlchGAKIGyfqG---------DIRLLMDDLKNLKPTIFPVVPRLLNRMFdkifgqaNTPlkrw 387
Cdd:PRK07059 257 CALPLYHIFALTVCGLL---GMRTG---GrnilipnprDIPGFIKELKKYQVHIFPAVNTLYNALL-------NNP---- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 388 llDFatsrkeaelksgvvrkdsmwDKLIFSKVQASLGGrvrlmitGAApVSPTVLTFLRAALGCQFYEGYGQTEcTAGCT 467
Cdd:PRK07059 320 --DF--------------------DKLDFSKLIVANGG-------GMA-VQRPVAERWLEMTGCPITEGYGLSE-TSPVA 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 468 MSLPGDWTA--GHVGAPLPCNFVKLVDVAEMNyfAANGE-GEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWL 544
Cdd:PRK07059 369 TCNPVDATEfsGTIGLPLPSTEVSIRDDDGND--LPLGEpGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMD 446
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 545 PNGTLKIIDRKKHIFkLAQGEYIAPEKIENIyirsdpvaqVFVHGDSLQACLVGvvVPDP 604
Cdd:PRK07059 447 ERGYTKIVDRKKDMI-LVSGFNVYPNEIEEV---------VASHPGVLEVAAVG--VPDE 494
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
121-605 |
2.52e-29 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 123.30 E-value: 2.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADR-AEFAGsALLHRGhSQSGDKyIGIFAQNRPEWTISELACYtySL--VAVPLYDTLGTEAISYVIDKASITT 197
Cdd:COG0365 40 LTYAELRREvNRFAN-ALRALG-VKKGDR-VAIYLPNIPEAVIAMLACA--RIgaVHSPVFPGFGAEALADRIEDAEAKV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 198 IICD--------------IADKARLILDCVsgrkhsVTTIVI--------ME---SFDSELTAQAQNCgidiislkelea 252
Cdd:COG0365 115 LITAdgglrggkvidlkeKVDEALEELPSL------EHVIVVgrtgadvpMEgdlDWDELLAAASAEF------------ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 253 igkanhkTPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKItevHCMLNQTDIH-----------ISYL-- 319
Cdd:COG0365 177 -------EPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKY---VLDLKPGDVFwctadigwatgHSYIvy 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 320 -PLAHmfervveG--VLLCHGaKIGYFQGDIrlLMDDLKNLKPTIFPVVPRLLnRMFDKifgQANTPLKRWllDFATsrk 396
Cdd:COG0365 247 gPLLN-------GatVVLYEG-RPDFPDPGR--LWELIEKYGVTVFFTAPTAI-RALMK---AGDEPLKKY--DLSS--- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 397 eaelksgvvrkdsmwdklifskvqaslggrVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWT- 475
Cdd:COG0365 308 ------------------------------LRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGLPVk 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 476 AGHVGAPLPCNFVKLVDvAEMNYFAANGEGEVCVKG--PNVFQGYLKDPEQTSGAV--DKAGWLHTGDIGKWLPNGTLKI 551
Cdd:COG0365 358 PGSMGKPVPGYDVAVVD-EDGNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWI 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 528467778 552 IDRKKHIFKLAqGEYIAPEKIENIYIRSDPVAQVFVhgdslqaclVGvvVPDPD 605
Cdd:COG0365 437 LGRSDDVINVS-GHRIGTAEIESALVSHPAVAEAAV---------VG--VPDEI 478
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
245-583 |
3.01e-29 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 123.01 E-value: 3.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 245 ISLKELEAIGKANHKTPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNcsafikITEVHCMLNQ------------T 312
Cdd:PRK12492 185 VPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVAN------MLQVRACLSQlgpdgqplmkegQ 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 313 DIHISYLPLAHMFE-------RVVEG---VLLCHGAKIGYFqgdirllmddLKNLKPTIFPVVPRLlNRMFDKIFgqaNT 382
Cdd:PRK12492 259 EVMIAPLPLYHIYAftancmcMMVSGnhnVLITNPRDIPGF----------IKELGKWRFSALLGL-NTLFVALM---DH 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 383 PlkrwllDFAtsrkeaelksgvvrkdsmwdKLIFSKVQASLGGrvrlmitGAAPVSPTVLTFlRAALGCQFYEGYGQTEC 462
Cdd:PRK12492 325 P------GFK--------------------DLDFSALKLTNSG-------GTALVKATAERW-EQLTGCTIVEGYGLTET 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 463 TAGCTMSLPGDWTA-GHVGAPLPCNFVKLVDvAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIG 541
Cdd:PRK12492 371 SPVASTNPYGELARlGTVGIPVPGTALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIA 449
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 528467778 542 KWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVA 583
Cdd:PRK12492 450 VIDPDGFVRIVDRKKDLI-IVSGFNVYPNEIEDVVMAHPKVA 490
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
111-604 |
8.36e-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: 121.20 E-value: 8.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 111 SRKAGQPYKWLSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNrpewTISELACYtyslVAVPLydtLGT------- 183
Cdd:cd12119 16 SRTHEGEVHRYTYAEVAERARRLANALRRLG-VKPGDR-VATLAWN----THRHLELY----YAVPG---MGAvlhtinp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 184 ----EAISYVIDKASITTIICDIADKArlILDCVSGRKHSVTTIVIMESfDSELTAQAqncGIDIISLKELeaIGKANHK 259
Cdd:cd12119 83 rlfpEQIAYIINHAEDRVVFVDRDFLP--LLEAIAPRLPTVEHVVVMTD-DAAMPEPA---GVGVLAYEEL--LAAESPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 260 TPIPPKPE-DLALICFTSGTTGNPKGAMLTHGNVVsncsafikiteVHCM-LNQTD-IHIS----YLPLAHMFERVVEGV 332
Cdd:cd12119 155 YDWPDFDEnTAAAICYTSGTTGNPKGVVYSHRSLV-----------LHAMaALLTDgLGLSesdvVLPVVPMFHVNAWGL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 333 ----LLChGAKI----GYFQGDirLLMDDLKNLKPTIFPVVPRLLNRMFDkifgqantplkrWLldfatSRKEAELKSGV 404
Cdd:cd12119 224 pyaaAMV-GAKLvlpgPYLDPA--SLAELIEREGVTFAAGVPTVWQGLLD------------HL-----EANGRDLSSLR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 405 vrkdsmwdklifskvqaslggrvRLMITGAAPVSPTVLTFlrAALGCQFYEGYGQTECTAGCTMSLPgdwTAGHVGAP-- 482
Cdd:cd12119 284 -----------------------RVVIGGSAVPRSLIEAF--EERGVRVIHAWGMTETSPLGTVARP---PSEHSNLSed 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 483 ----------LPCNFV--KLVDvAEMNYFAANGE--GEVCVKGPNVFQGYLKDPEQTSgAVDKAGWLHTGDIGKWLPNGT 548
Cdd:cd12119 336 eqlalrakqgRPVPGVelRIVD-DDGRELPWDGKavGELQVRGPWVTKSYYKNDEESE-ALTEDGWLRTGDVATIDEDGY 413
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 528467778 549 LKIIDRKKHIFKLAqGEYIAPEKIENIYIRSDPVAQVFVhgdslqaclvgVVVPDP 604
Cdd:cd12119 414 LTITDRSKDVIKSG-GEWISSVELENAIMAHPAVAEAAV-----------IGVPHP 457
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
121-589 |
9.11e-29 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 120.74 E-value: 9.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGHSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:PRK06839 28 MTYKQLHEYVSKVAAYLIYELNVKKGER-IAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 201 DIADKAR-LILDCVSGRKHsvttivimesfdseltaqaqncgidIISLKELEAIGKANHKTPIPPKPEDLALICFTSGTT 279
Cdd:PRK06839 107 EKTFQNMaLSMQKVSYVQR-------------------------VISITSLKEIEDRKIDNFVEKNESASFIICYTSGTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 280 GNPKGAMLTHGNVVSNCsafikITEVHCM-LNQTDIHISYLPLAHMfervvegvllchgAKIGYFQgdirllmddlknlK 358
Cdd:PRK06839 162 GKPKGAVLTQENMFWNA-----LNNTFAIdLTMHDRSIVLLPLFHI-------------GGIGLFA-------------F 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 359 PTIFP----VVPRllnrMFDKifgqantplkrwllDFATSRKEAELKSGVVRKDSMWDKLIFSKVQASLG-GRVRLMITG 433
Cdd:PRK06839 211 PTLFAggviIVPR----KFEP--------------TKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNlQSVRWFYNG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 434 AAPVsPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDW--TAGHVGAPLPCNFVKLVDVAEmNYFAANGEGEVCVKG 511
Cdd:PRK06839 273 GAPC-PEELMREFIDRGFLFGQGFGMTETSPTVFMLSEEDArrKVGSIGKPVLFCDYELIDENK-NKVEVGEVGELLIRG 350
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528467778 512 PNVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVFVHG 589
Cdd:PRK06839 351 PNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQVINKLSDVYEVAVVG 426
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
173-603 |
2.14e-28 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 121.95 E-value: 2.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 173 VAVPLYDTLGTEAISYVIDKASITTIICDIADKARLILDCVSGRKHSVTTIVIMESFDSELTAQAQNCGIDIISLKELEA 252
Cdd:PRK08633 691 VPVNLNYTASEAALKSAIEQAQIKTVITSRKFLEKLKNKGFDLELPENVKVIYLEDLKAKISKVDKLTALLAARLLPARL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 253 IGKANHKTPippKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAfikITEVHCmLNQTDIHISYLPLAHMFERVVEGV 332
Cdd:PRK08633 771 LKRLYGPTF---KPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQ---ISDVFN-LRNDDVILSSLPFFHSFGLTVTLW 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 333 L-LCHGAKIGYFQG--DIRLLMDDLKNLKPTIfpvvprllnrmfdkIFGqanTPlkRWLLDFATSRKeaelksgvvrkds 409
Cdd:PRK08633 844 LpLLEGIKVVYHPDptDALGIAKLVAKHRATI--------------LLG---TP--TFLRLYLRNKK------------- 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 410 mWDKLIFskvqASLggrvRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLP-----GDWT-----AGHV 479
Cdd:PRK08633 892 -LHPLMF----ASL----RLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNLPdvlaaDFKRqtgskEGSV 962
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 480 GAPLPCNFVKLVDVAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAV---DKAGWLHTGDIGKWLPNGTLKIIDRKK 556
Cdd:PRK08633 963 GMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRYS 1042
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 528467778 557 HIFKLAqGEYIAPEKIEniyirsDPVAQVFvhGDSLQACLVgVVVPD 603
Cdd:PRK08633 1043 RFAKIG-GEMVPLGAVE------EELAKAL--GGEEVVFAV-TAVPD 1079
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
122-575 |
4.25e-28 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 119.08 E-value: 4.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 122 SYKEVADRAEFAGSALLHRGhSQSGDkyigIFAQNRPEW---TISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTI 198
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKG-IEPGD----RVAFQLPGWcefTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 199 ICDIADKAR----LILDCVSGRKHsVTTIVIMESFDSELTAqaqncgidiISLKELEAIGKAnHKTPIPPKPEDLALICF 274
Cdd:PRK06087 126 FAPTLFKQTrpvdLILPLQNQLPQ-LQQIVGVDKLAPATSS---------LSLSQIIADYEP-LTTAITTHGDELAAVLF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 275 TSGTTGNPKGAMLTHGNVVSNCSAFIKITEvhcmLNQTDIHISYLPLAHmfervVEGVLlcHGAKIGYFQGDIRLLMDDL 354
Cdd:PRK06087 195 TSGTEGLPKGVMLTHNNILASERAYCARLN----LTWQDVFMMPAPLGH-----ATGFL--HGVTAPFLIGARSVLLDIF 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 355 KNLKPTifpvvpRLLNRmfDKI-FGQANTPLKRWLLDfATSRKEAELKSgvvrkdsmwdklifskvqaslggrVRLMITG 433
Cdd:PRK06087 264 TPDACL------ALLEQ--QRCtCMLGATPFIYDLLN-LLEKQPADLSA------------------------LRFFLCG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 434 AAPVsPTVLTflRAAL--GCQFYEGYGQTECTAGCTMSL--PGDWTAGHVGAPLPCNFVKLVDVAEmNYFAANGEGEVCV 509
Cdd:PRK06087 311 GTTI-PKKVA--RECQqrGIKLLSVYGSTESSPHAVVNLddPLSRFMHTDGYAAAGVEIKVVDEAR-KTLPPGCEGEEAS 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528467778 510 KGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENI 575
Cdd:PRK06087 387 RGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDI 451
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
121-605 |
6.37e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 118.73 E-value: 6.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGHSqSGDKYIgIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:PRK07786 43 TTWRELDDRVAALAGALSRRGVG-FGDRVL-ILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 201 D--IADKARLILDCVSGRKhsvTTIVIMESFDSeltaqaqncgiDIISLKELEAIGKANHktPIPPKPEDL-ALICFTSG 277
Cdd:PRK07786 121 EaaLAPVATAVRDIVPLLS---TVVVAGGSSDD-----------SVLGYEDLLAEAGPAH--APVDIPNDSpALIMYTSG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 278 TTGNPKGAMLTHGNVVSNCSAFIKITEVHcmlNQTDIHISYLPLAHM--FERVVEGVLLchGAKIgyfqgdirllmddlk 355
Cdd:PRK07786 185 TTGRPKGAVLTHANLTGQAMTCLRTNGAD---INSDVGFVGVPLFHIagIGSMLPGLLL--GAPT--------------- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 356 nlkpTIFPVvprllnRMFDKifGQantplkrwLLDFAtsrkEAELKSGVVRKDSMWDKLIFSKVQASLGGRVRLMITGAA 435
Cdd:PRK07786 245 ----VIYPL------GAFDP--GQ--------LLDVL----EAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 436 PVSPTVLTFLRAAL-GCQFYEGYGQTECTAGCTMSLPGDWTA--GHVGAPLPCNFVKLVDvAEMNYFAANGEGEVCVKGP 512
Cdd:PRK07786 301 PASDTLLRQMAATFpEAQILAAFGQTEMSPVTCMLLGEDAIRklGSVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 513 NVFQGYLKDPEQTSGAVDkAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVFVHG--- 589
Cdd:PRK07786 380 TLMSGYWNNPEATAEAFA-GGWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPDIVEVAVIGrad 457
|
490
....*....|....*.
gi 528467778 590 DSLQACLVGVVVPDPD 605
Cdd:PRK07786 458 EKWGEVPVAVAAVRND 473
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
264-589 |
7.46e-28 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 116.68 E-value: 7.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 264 PKPEDLALICFTSGTTGNPKGAMLTHGN----VVSnCSAFIKITEVHCMLNQTDI-HISYLPLahMFERVVEG--VLLch 336
Cdd:cd05912 74 VKLDDIATIMYTSGTTGKPKGVQQTFGNhwwsAIG-SALNLGLTEDDNWLCALPLfHISGLSI--LMRSVIYGmtVYL-- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 337 gakigYFQGDIRLLMDDLKNLKPTIFPVVPRLLNRMFdKIFGQANTPlkrwlldfatsrkeaelksgvvrkdsmwdklif 416
Cdd:cd05912 149 -----VDKFDAEQVLHLINSGKVTIISVVPTMLQRLL-EILGEGYPN--------------------------------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 417 skvqaslggRVRLMITGAAPVSPTVLTFLRAaLGCQFYEGYGQTE-CTAGCTMSlPGDWTA--GHVGAPLPCNFVKLVDv 493
Cdd:cd05912 190 ---------NLRCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTEtCSQIVTLS-PEDALNkiGSAGKPLFPVELKIED- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 494 aemNYFAANGEGEVCVKGPNVFQGYLKdPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIE 573
Cdd:cd05912 258 ---DGQPPYEVGEILLKGPNVTKGYLN-RPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIE 332
|
330
....*....|....*.
gi 528467778 574 NIYIRSDPVAQVFVHG 589
Cdd:cd05912 333 EVLLSHPAIKEAGVVG 348
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
233-603 |
1.81e-27 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 115.87 E-value: 1.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 233 LTAQAQNCGIDIISLKE-LEAIGKANHKTPI--PPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSafikitEVHCML 309
Cdd:cd17653 68 LKAGAAYVPLDAKLPSArIQAILRTSGATLLltTDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVS------QPPARL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 310 NQT--DIHISYLPLAhmFERVVEGVL--LCHGAKIgYFQGDIRLLMDDLKNLkpTIFPVVPRLLnrmfdkifgqantplk 385
Cdd:cd17653 142 DVGpgSRVAQVLSIA--FDACIGEIFstLCNGGTL-VLADPSDPFAHVARTV--DALMSTPSIL---------------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 386 rwlldfatsrkeaelksGVVRKDSmwdkliFSkvqaslggRVRLMITGAAPVSPTVLTflRAALGCQFYEGYGQTECTAG 465
Cdd:cd17653 201 -----------------STLSPQD------FP--------NLKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTIS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 466 CTMS--LPGDWTagHVGAPLPCNFVKLVDvAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAV----DKAGWLH--T 537
Cdd:cd17653 248 STMTelLPGQPV--TIGKPIPNSTCYILD-ADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFvpdpFWPGSRMyrT 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528467778 538 GDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDPVAQ---VFVHGDSlqacLVGVVVPD 603
Cdd:cd17653 325 GDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEIEEVVLQSQPEVTqaaAIVVNGR----LVAFVTPE 388
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
119-589 |
1.86e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 116.60 E-value: 1.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 119 KWLSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTI 198
Cdd:PRK03640 26 KKVTFMELHEAVVSVAGKLAALG-VKKGDR-VALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 199 ICDiadkarlildcvsgrkhsvttivimESFDSELTAQAQncgidiISLKELEAiGKANHKTPIPPKPED-LALICFTSG 277
Cdd:PRK03640 104 ITD-------------------------DDFEAKLIPGIS------VKFAELMN-GPKEEAEIQEEFDLDeVATIMYTSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 278 TTGNPKGAMLTHGN----VVSncSAF-IKITEVHCMLNQTDI-HISYLPLahMFERVVEG---VLLCH--GAKIgyfqgd 346
Cdd:PRK03640 152 TTGKPKGVIQTYGNhwwsAVG--SALnLGLTEDDCWLAAVPIfHISGLSI--LMRSVIYGmrvVLVEKfdAEKI------ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 347 IRLLMDDlknlKPTIFPVVPRLLNRMFDKIfGQANTPlkrwlldfatsrkeaelksgvvrkdsmwdklifskvqaslgGR 426
Cdd:PRK03640 222 NKLLQTG----GVTIISVVSTMLQRLLERL-GEGTYP-----------------------------------------SS 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 427 VRLMITGAAPVSPTVLTFLRAAlGCQFYEGYGQTEcTAGCTMSLPGDWTA---GHVGAPL-PCNfVKLVDvaEMNYFAAN 502
Cdd:PRK03640 256 FRCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLfPCE-LKIEK--DGVVVPPF 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 503 GEGEVCVKGPNVFQGYLKDPEQTSgAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPV 582
Cdd:PRK03640 331 EEGEIVVKGPNVTKGYLNREDATR-ETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPGV 408
|
....*..
gi 528467778 583 AQVFVHG 589
Cdd:PRK03640 409 AEAGVVG 415
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
121-604 |
2.16e-27 |
|
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: 115.51 E-value: 2.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALlhRGHS-QSGDKYIGIFAqNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTII 199
Cdd:cd05972 1 WSFRELKRESAKAANVL--AKLGlRKGDRVAVLLP-RVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 200 CDiadkarlildcvsgrkhsvttivimesfdseltaqaqncgidiislkeleaigkanhktpippkPEDLALICFTSGTT 279
Cdd:cd05972 78 TD----------------------------------------------------------------AEDPALIYFTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 280 GNPKGAMLTHGNVVSNCSAFIKITEVHcmlnQTDIHIS--------------YLPLAHMFERVVegvllCHGAKIgyfqg 345
Cdd:cd05972 94 GLPKGVLHTHSYPLGHIPTAAYWLGLR----PDDIHWNiadpgwakgawssfFGPWLLGATVFV-----YEGPRF----- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 346 DIRLLMDDLKNLKPTIFPVVPrllnrmfdkifgqanTPLKRWLldfatsrkEAELKSGVvrkdsmwdkliFSkvqaslgg 425
Cdd:cd05972 160 DAERILELLERYGVTSFCGPP---------------TAYRMLI--------KQDLSSYK-----------FS-------- 197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 426 RVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDvAEMNYFAANGEG 505
Cdd:cd05972 198 HLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIID-DDGRELPPGEEG 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 506 EVCVKGPNV--FQGYLKDPEQTSgAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYIRSDPVA 583
Cdd:cd05972 277 DIAIKLPPPglFLGYVGDPEKTE-ASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVESALLEHPAVA 354
|
490 500
....*....|....*....|.
gi 528467778 584 QVFVhgdslqaclvgVVVPDP 604
Cdd:cd05972 355 EAAV-----------VGSPDP 364
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
121-606 |
2.90e-27 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 116.13 E-value: 2.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLyDTLGTEA-ISYVIDKASITTII 199
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALG-VKPGDR-VAVQVEKSPEALALYLATLRAGAVFLPL-NTAYTLAeLDYFIGDAEPALVV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 200 CDIADKA--RLIldcvsGRKHSVTTIvimesfdseLTAQAQNCGidiiSLKELeAIGKANHKTPIPPKPEDLALICFTSG 277
Cdd:PRK07514 106 CDPANFAwlSKI-----AAAAGAPHV---------ETLDADGTG----SLLEA-AAAAPDDFETVPRGADDLAAILYTSG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 278 TTGNPKGAMLTHGNVVSNCSAFIKITEVhcmlNQTDIHISYLPLAH---MFerVVEGVLLCHGAKIGYFQgdiRLLMDDL 354
Cdd:PRK07514 167 TTGRSKGAMLSHGNLLSNALTLVDYWRF----TPDDVLIHALPIFHthgLF--VATNVALLAGASMIFLP---KFDPDAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 355 KNLKP--TIFPVVPRLLNRMFDkifgqantplkrwlldfatsrkEAELKSGVVRkdsmwdklifskvqaslggRVRLMIT 432
Cdd:PRK07514 238 LALMPraTVMMGVPTFYTRLLQ----------------------EPRLTREAAA-------------------HMRLFIS 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 433 GAAPVSPTVLTFLRAALGCQFYEGYGQTEcTAGCTmSLP--GDWTAGHVGAPLPCNFVKLVDVAEMNYFAANGEGEVCVK 510
Cdd:PRK07514 277 GSAPLLAETHREFQERTGHAILERYGMTE-TNMNT-SNPydGERRAGTVGFPLPGVSLRVTDPETGAELPPGEIGMIEVK 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 511 GPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIfkLAQGEY-IAPEKIENiYIrsDPVAQVfvhg 589
Cdd:PRK07514 355 GPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDL--IISGGYnVYPKEVEG-EI--DELPGV---- 425
|
490
....*....|....*..
gi 528467778 590 dsLQACLVGvvVPDPDF 606
Cdd:PRK07514 426 --VESAVIG--VPHPDF 438
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
119-604 |
3.76e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 115.67 E-value: 3.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 119 KWlSYKEVaDRAEFAGSALLHRGHSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTI 198
Cdd:PRK09088 22 RW-TYAEL-DALVGRLAAVLRRRGCVDGER-LAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 199 ICDIADKArlildcvsGRkhsvttiVIMESFDSeLTAQAqncgidiislkelEAIGKANhKTPIPPkpEDLALICFTSGT 278
Cdd:PRK09088 99 LGDDAVAA--------GR-------TDVEDLAA-FIASA-------------DALEPAD-TPSIPP--ERVSLILFTSGT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 279 TGNPKGAMLTHGNVVSNCSAFIKITEVhcmlnqtDIHISYLPLAHMFERV-----VEGVLLcHGAKIGYFQGdirllmdd 353
Cdd:PRK09088 147 SGQPKGVMLSERNLQQTAHNFGVLGRV-------DAHSSFLCDAPMFHIIglitsVRPVLA-VGGSILVSNG-------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 354 lknLKPTifpvvpRLLNRMFDKIFGQANTplkrwlldFATSRKEAELksgvvRKDSMWDklifskvqASLGGRVRLMITG 433
Cdd:PRK09088 211 ---FEPK------RTLGRLGDPALGITHY--------FCVPQMAQAF-----RAQPGFD--------AAALRHLTALFTG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 434 AAP-VSPTVLTFLraALGCQFYEGYGQTEctAGCTMSLPGDWT-----AGHVGAPLPCNFVKLVDvAEMNYFAANGEGEV 507
Cdd:PRK09088 261 GAPhAAEDILGWL--DDGIPMVDGFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVVD-DQGNDCPAGVPGEL 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 508 CVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIEniyirsdpvAQVFV 587
Cdd:PRK09088 336 LLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIE---------AVLAD 405
|
490
....*....|....*..
gi 528467778 588 HGDSLQACLVGvvVPDP 604
Cdd:PRK09088 406 HPGIRECAVVG--MADA 420
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
121-604 |
4.64e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 115.80 E-value: 4.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:PRK08316 37 WTYAELDAAVNRVAAALLDLG-LKKGDR-VAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 201 DIADKARLilDCVSGRKHSVTTIVIMESFDSELTAqaqncgidiiSLKELEAIGKANHKTPIPPKP--EDLALICFTSGT 278
Cdd:PRK08316 115 DPALAPTA--EAALALLPVDTLILSLVLGGREAPG----------GWLDFADWAEAGSVAEPDVELadDDLAQILYTSGT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 279 TGNPKGAMLTHGNVVSNCSAFIkiteVHCMLNQTDIHISYLPLAHMFER-VVEGVLLCHGAKIGYFQG-DIRLLMDDLKN 356
Cdd:PRK08316 183 ESLPKGAMLTHRALIAEYVSCI----VAGDMSADDIPLHALPLYHCAQLdVFLGPYLYVGATNVILDApDPELILRTIEA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 357 LKPTIF---PVVprllnrmfdkIFGQANTPlkrwllDFATsrkeAELKSgvVRKDSMwdklifskvqaslggrvrlmitG 433
Cdd:PRK08316 259 ERITSFfapPTV----------WISLLRHP------DFDT----RDLSS--LRKGYY----------------------G 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 434 AAPVSPTVLTFLRAAL-GCQFYEGYGQTECTAGCTMSLPGDwTAGHVG-APLPCNFV--KLVDvAEMNYFAANGEGEVCV 509
Cdd:PRK08316 295 ASIMPVEVLKELRERLpGLRFYNCYGQTEIAPLATVLGPEE-HLRRPGsAGRPVLNVetRVVD-DDGNDVAPGEVGEIVH 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 510 KGPNVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSDPVAQVFVHG 589
Cdd:PRK08316 373 RSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEALYTHPAVAEVAVIG 450
|
490
....*....|....*
gi 528467778 590 dslqaclvgvvVPDP 604
Cdd:PRK08316 451 -----------LPDP 454
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
261-577 |
5.78e-27 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 116.09 E-value: 5.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 261 PIPP-KPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEVHCMLNQTD-IHISYLPLAHMF--ERVVEGVLLCH 336
Cdd:PLN02574 191 PKPViKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEYPGSDnVYLAALPMFHIYglSLFVVGLLSLG 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 337 GAKIGYFQGDIRLLMDDLKNLKPTIFPVVPRLLNRMFDKIFGQANTPLKrwlldfatsrkeaelksgvvrkdsmwdklif 416
Cdd:PLN02574 271 STIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLK------------------------------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 417 SKVQASlggrvrlmiTGAAPVS-PTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGH--VGAPLPCNFVKLVDV 493
Cdd:PLN02574 320 SLKQVS---------CGAAPLSgKFIQDFVQTLPHVDFIQGYGMTESTAVGTRGFNTEKLSKYssVGLLAPNMQAKVVDW 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 494 AEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIE 573
Cdd:PLN02574 391 STGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQIAPADLE 469
|
....
gi 528467778 574 NIYI 577
Cdd:PLN02574 470 AVLI 473
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
121-604 |
1.04e-26 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 113.34 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAE-FAGsaLLHRGHSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTII 199
Cdd:cd05935 2 LTYLELLEVVKkLAS--FLSNKGVRKGDR-VGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 200 CDiadkarlildcvsgrkhsvttivimesfdSELtaqaqncgidiislkeleaigkanhktpippkpEDLALICFTSGTT 279
Cdd:cd05935 79 VG-----------------------------SEL---------------------------------DDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 280 GNPKGAMLTHGNVVSNCSAFIKITevhcMLNQTDIHISYLPLAHM--FERVVEGVLLCHGAKIGYFQGDIRLLMDDLKNL 357
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQSAVWT----GLTPSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMARWDRETALELIEKY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 358 KPTIFPVVPRLLNrmfdkifgqantplkrwlldfatsrkeaELKSGVVRKDSMWDKLifskvqaslggrvRLMITGAAPV 437
Cdd:cd05935 173 KVTFWTNIPTMLV----------------------------DLLATPEFKTRDLSSL-------------KVLTGGGAPM 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 438 SPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDVAEMNYFAANGEGEVCVKGPNVFQG 517
Cdd:cd05935 212 PPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKG 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 518 YLKDPEQTSGA---VDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIyirsdpvaqVFVHGDSLQA 594
Cdd:cd05935 292 YWNRPEETEESfieIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAK---------LYKHPAI*EV 361
|
490
....*....|
gi 528467778 595 CLVGvvVPDP 604
Cdd:cd05935 362 CVIS--VPDE 369
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
122-587 |
2.06e-26 |
|
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: 112.36 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 122 SYKEVADRAE-FAGsALLHRGHSQSGDkYIGIFAQNRPEWTISELACytysLVA----VPLYDTLGTEAISYVIDKASIT 196
Cdd:TIGR01733 1 TYRELDERANrLAR-HLRAAGGVGPGD-RVAVLLERSAELVVAILAV----LKAgaayVPLDPAYPAERLAFILEDAGAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 197 TIICDIADKARLIldcvsgrkhSVTTIVIMESFDSELTAQAQNCGIDiislkeleaigkanhkTPIPPKPEDLALICFTS 276
Cdd:TIGR01733 75 LLLTDSALASRLA---------GLVLPVILLDPLELAALDDAPAPPP----------------PDAPSGPDDLAYVIYTS 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 277 GTTGNPKGAMLTHGNVVSNCSAFIKITEvhcmLNQTDIHISYLPLAhmFERVVEGVL--LCHGAKI-----GYFQGDIRL 349
Cdd:TIGR01733 130 GSTGRPKGVVVTHRSLVNLLAWLARRYG----LDPDDRVLQFASLS--FDASVEEIFgaLLAGATLvvppeDEERDDAAL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 350 LMDDLKNLKPTIFPVVPRLLNRMfdkifgqantplkrwlldfatsrkeaelksgvvrkdsmwdklifSKVQASLGGRVRL 429
Cdd:TIGR01733 204 LAALIAEHPVTVLNLTPSLLALL--------------------------------------------AAALPPALASLRL 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 430 MITGAAPVSPTVLTFLRAALG-CQFYEGYGQTECTAGCTM-SLPGDWTAGHV----GAPLPCNFVKLVDvAEMNYFAANG 503
Cdd:TIGR01733 240 VILGGEALTPALVDRWRARGPgARLINLYGPTETTVWSTAtLVDPDDAPRESpvpiGRPLANTRLYVLD-DDLRPVPVGV 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 504 EGEVCVKGPNVFQGYLKDPEQTS--------GAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 575
Cdd:TIGR01733 319 VGELYIGGPGVARGYLNRPELTAerfvpdpfAGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAA 397
|
490
....*....|..
gi 528467778 576 YIRSDPVAQVFV 587
Cdd:TIGR01733 398 LLRHPGVREAVV 409
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
264-604 |
3.78e-26 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 113.22 E-value: 3.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 264 PKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKitevHCMLNQTDIHISYLPLAHMfervvEGVLlcHGAKIGYF 343
Cdd:PRK13295 194 PGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAE----RLGLGADDVILMASPMAHQ-----TGFM--YGLMMPVM 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 344 QGDIRLLMDDLKNLkptifpvvprllnRMFDKI------FGQANTPlkrWLLDFATSRKEAelksgvvrkdsmwdklifS 417
Cdd:PRK13295 263 LGATAVLQDIWDPA-------------RAAELIrtegvtFTMASTP---FLTDLTRAVKES------------------G 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 418 KVQASLggrvRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAgCTMSLPGD---WTAGHVGAPLPCNFVKLVDvA 494
Cdd:PRK13295 309 RPVSSL----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA-VTLTKLDDpdeRASTTDGCPLPGVEVRVVD-A 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 495 EMNYFAANGEGEVCVKGPNVFQGYLKDPEQTsgAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIEN 574
Cdd:PRK13295 383 DGAPLPAGQIGRLQVRGCSNFGGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEA 459
|
330 340 350
....*....|....*....|....*....|...
gi 528467778 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 |
8.99e-26 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 111.23 E-value: 8.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 120 WLSYKEVADRAEFAGSALLHRGHSQsgDKYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTII 199
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGVGP--GDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 200 CDIADKARLILDCVsgrkhsvttivimesfdseltaqaqncgidiISLKELEAIGKANHKTPIPPKPEDLALICFTSGTT 279
Cdd:cd12116 90 TDDALPDRLPAGLP-------------------------------VLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 280 GNPKGAMLTHGNVVSNCSAFIK---ITEVHCMLNQT----DIHI--SYLPlahmfervvegvlLCHGAKI----GYFQGD 346
Cdd:cd12116 139 GRPKGVVVSHRNLVNFLHSMRErlgLGPGDRLLAVTtyafDISLleLLLP-------------LLAGARVviapRETQRD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 347 IRLLMDDLKNLKPTIFpvvprllnrmfdkifgQAnTPlkrwlldfATSRkeaelksgvVRKDSMWDKLifskvqaslgGR 426
Cdd:cd12116 206 PEALARLIEAHSITVM----------------QA-TP--------ATWR---------MLLDAGWQGR----------AG 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 427 VRLMITGAApvSPTVLTFLRAALGCQFYEGYGQTECT--AGCTMSLPGDwTAGHVGAPLPCNFVKLVDVAeMNYFAANGE 504
Cdd:cd12116 242 LTALCGGEA--LPPDLAARLLSRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLDAA-LRPVPPGVP 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 505 GEVCVKGPNVFQGYLKDPEQTSGAV--DKAG-----WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYI 577
Cdd:cd12116 318 GELYIGGDGVAQGYLGRPALTAERFvpDPFAgpgsrLYRTGDLVRRRADGRLEYLGRADGQVKI-RGHRIELGEIEAALA 396
|
490 500
....*....|....*....|....*...
gi 528467778 578 RSDPVAQ--VFVHGDSLQACLVGVVVPD 603
Cdd:cd12116 397 AHPGVAQaaVVVREDGGDRRLVAYVVLK 424
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
120-605 |
1.24e-25 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 111.56 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 120 WLSYKEVADRAEFAGSALLHRGhsQSGDkYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEA---ISYVIDKASIT 196
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAVG--KPGD-RVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 197 TIICDIADKARLILDCVSGRKHSVTTIVIMESFDSELTAQAQNCGIDiislkeleaigkanhktpippkPEDLALICFTS 276
Cdd:cd05931 101 VVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPD----------------------PDDIAYLQYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 277 GTTGNPKGAMLTHGNVVSNCSAFIKItevhCMLNQTDIHISYLPLAH-MfervveGVLLCHGAKIgYFQGDIrLLMDdlk 355
Cdd:cd05931 159 GSTGTPKGVVVTHRNLLANVRQIRRA----YGLDPGDVVVSWLPLYHdM------GLIGGLLTPL-YSGGPS-VLMS--- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 356 nlkPTIFpvvprlLNRmfdkifgqantPLkRWL-----------------LDFATSRKEAELKSGVvrkDsmwdkLifsk 418
Cdd:cd05931 224 ---PAAF------LRR-----------PL-RWLrlisryratisaapnfaYDLCVRRVRDEDLEGL---D-----L---- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 419 vqaslgGRVRLMITGAAPVSPTVLT-FLRAALGCQF-----YEGYGQTECTAGCTMSLPG----------DWTAGHV--- 479
Cdd:cd05931 271 ------SSWRVALNGAEPVRPATLRrFAEAFAPFGFrpeafRPSYGLAEATLFVSGGPPGtgpvvlrvdrDALAGRAvav 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 480 -------------GAPLPCNFVKLVDVAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQT------SGAVDKAGWLHTGDI 540
Cdd:cd05931 345 aaddpaarelvscGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATaetfgaLAATDEGGWLRTGDL 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528467778 541 GkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSDPVAQVfvhgdslqACLVGVVVPDPD 605
Cdd:cd05931 425 G-FLHDGELYITGRLKDLIIVR-GRNHYPQDIEATAEEAHPALRP--------GCVAAFSVPDDG 479
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
87-692 |
4.40e-25 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 111.87 E-value: 4.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 87 KDALTLYEFFLRGLRVSNNGPCLGSRK-AGQPyKWLSYKEVADRAEFAGSALLHRGhSQSGDkYIGIFAQNRPEWTISEL 165
Cdd:PTZ00297 424 AGVRSLGEMWERSVTRHSTFRCLGQTSeSGES-EWLTYGTVDARARELGSGLLALG-VRPGD-VIGVDCEASRNIVILEV 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 166 ACYTYSLVAVPLYDTLGTeaISYVIDKASITTIICDIADKArLILDCvsgRKHSVTTIVIMESF-DSELTAQAQNCGIDI 244
Cdd:PTZ00297 501 ACALYGFTTLPLVGKGST--MRTLIDEHKIKVVFADRNSVA-AILTC---RSRKLETVVYTHSFyDEDDHAVARDLNITL 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 245 ISLKELEAIGKAnhkTPIPPKPEDLALICFT-------SGTTGNPKGAMLTHGNVVSNCSAFIkITEVHCMLNQTDIHIS 317
Cdd:PTZ00297 575 IPYEFVEQKGRL---CPVPLKEHVTTDTVFTyvvdnttSASGDGLAVVRVTHADVLRDISTLV-MTGVLPSSFKKHLMVH 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 318 YLPLAHMFERVVEGVLLCHGAKIGyfQGDIRLLMDDLKNLKPTIFPVVPRLlnrmfdkiFGQANTPLKR----------W 387
Cdd:PTZ00297 651 FTPFAMLFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSL--------FSTSRLQLSRanerysavysW 720
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 388 LLDfatsrKEAELKSGVV---RKDSMWDKLIFSK-VQASLGGRVRLMITGAAPVSPTvltflraalgcqfyegYGQTECT 463
Cdd:PTZ00297 721 LFE-----RAFQLRSRLInihRRDSSLLRFIFFRaTQELLGGCVEKIVLCVSEESTS----------------FSLLEHI 779
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 464 AGCTMslpgdwtaghvgaplPCnfvklvdVAEMNYFaaNGEGEVCVKG---PNVfQGYLKDPEQTSGAVdKAGWL----- 535
Cdd:PTZ00297 780 SVCYV---------------PC-------LREVFFL--PSEGVFCVDGtpaPSL-QVDLEPFDEPSDGA-GIGQLvlakk 833
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 536 ----HTGDI-GKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSDPVAQVFVHGDSLQAcLVGVVVPDPDFLP-G 609
Cdd:PTZ00297 834 geprRTLPIaAQWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEfE 912
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 610 WAKNRGIEG--------SFNDLckSKEVKNAILEDMIQLGKEAGLKSFEQVRDIALHLEMFSVQNGLLTPTLKAKRTELK 681
Cdd:PTZ00297 913 WRQSHCMGEgggparqlGWTEL--VAYASSLLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVH 990
|
650
....*....|.
gi 528467778 682 SRFREQIDQLY 692
Cdd:PTZ00297 991 SYFSSVIERFY 1001
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
263-556 |
4.60e-25 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 110.43 E-value: 4.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 263 PPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNC---SAFIKITEvhcmlnqTDIHISYLPLAHMFERVVEGVL-LCHGA 338
Cdd:PRK07529 209 PIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAwlgALLLGLGP-------GDTVFCGLPLFHVNALLVTGLApLARGA 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 339 KI------GYfQGDirLLMDDLKNL----KPTIFPVVPRLLNrmfdkifgqantplkrwlldfatsrkeaelksgvvrkd 408
Cdd:PRK07529 282 HVvlatpqGY-RGP--GVIANFWKIveryRINFLSGVPTVYA-------------------------------------- 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 409 smwdklifSKVQASLGGR----VRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLP-GDWTAGHVGAPL 483
Cdd:PRK07529 321 --------ALLQVPVDGHdissLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPdGERRIGSVGLRL 392
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528467778 484 PCNFVKLVDV-AEMNYF---AANGEGEVCVKGPNVFQGYLkDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKK 556
Cdd:PRK07529 393 PYQRVRVVILdDAGRYLrdcAVDEVGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAK 468
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
268-606 |
5.77e-25 |
|
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: 106.59 E-value: 5.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 268 DLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIkitevHCM-LNQTDIHISYLPLAHmfervVEGV-----LLCHGAK-- 339
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLI-----HAMgLTEADVYLNMLPLFH-----IAGLnlalaTFHAGGAnv 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 340 -IGYFqgDIRLLMDDLKNLKPTIFPVVPRLLNRMFDKIFgqantplkrwlldfATSRKEAELKsGVVRKDSmwdklifsk 418
Cdd:cd17637 71 vMEKF--DPAEALELIEEEKVTLMGSFPPILSNLLDAAE--------------KSGVDLSSLR-HVLGLDA--------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 419 vqaslggrvrlmitgaapvsPTVLTFLRAALGCQFYEGYGQTECTAGCTMSlPGDWTAGHVGAPLPCNFVKLVDvaEMNY 498
Cdd:cd17637 125 --------------------PETIQRFEETTGATFWSLYGQTETSGLVTLS-PYRERPGSAGRPGPLVRVRIVD--DNDR 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 499 FAANGE-GEVCVKGPNVFQGYLKDPEQTSGAVDKaGWLHTGDIGKWLPNGTLKIIDRK--KHIFKlAQGEYIAPEKIENI 575
Cdd:cd17637 182 PVPAGEtGEIVVRGPLVFQGYWNLPELTAYTFRN-GWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKV 259
|
330 340 350
....*....|....*....|....*....|.
gi 528467778 576 YIRSDPVAQVFVHGdslqaclvgvvVPDPDF 606
Cdd:cd17637 260 ILEHPAIAEVCVIG-----------VPDPKW 279
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
121-604 |
1.04e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 108.89 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAE-FAGSaLLHRGHSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTII 199
Cdd:PRK08314 36 ISYRELLEEAErLAGY-LQQECGVRKGDR-VLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 200 C--DIADK----------ARLILDCVSGRKHSVTTIVIMESFDSELTAQAQNcGIDIISLKEleAIgkANHKTPIP--PK 265
Cdd:PRK08314 114 VgsELAPKvapavgnlrlRHVIVAQYSDYLPAEPEIAVPAWLRAEPPLQALA-PGGVVAWKE--AL--AAGLAPPPhtAG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 266 PEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIkiteVHCMLNQTDIHISYLPLAHmfervVEGVLLCHGAKIgyFQG 345
Cdd:PRK08314 189 PDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSV----LWSNSTPESVVLAVLPLFH-----VTGMVHSMNAPI--YAG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 346 DIRLLMddlknlkptifP-----VVPRLLNRMfdKIFGQANTPlkRWLLDFATSRK--EAELKSgvvrkdsmwdklifsk 418
Cdd:PRK08314 258 ATVVLM-----------PrwdreAAARLIERY--RVTHWTNIP--TMVVDFLASPGlaERDLSS---------------- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 419 vQASLGGrvrlmitGAAPVSPTVLTFLRAALGCQFYEGYGQTEcTAGCTMSLPGDWTA-GHVGAPLPCNFVKLVDVAEMN 497
Cdd:PRK08314 307 -LRYIGG-------GGAAMPEAVAERLKELTGLDYVEGYGLTE-TMAQTHSNPPDRPKlQCLGIPTFGVDARVIDPETLE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 498 YFAANGEGEVCVKGPNVFQGYLKDPEQTSGA---VDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIEN 574
Cdd:PRK08314 378 ELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMIN-ASGFKVWPAEVEN 456
|
490 500 510
....*....|....*....|....*....|
gi 528467778 575 IyirsdpvaqVFVHGDSLQACLVGvvVPDP 604
Cdd:PRK08314 457 L---------LYKHPAIQEACVIA--TPDP 475
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
107-694 |
3.18e-24 |
|
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: 107.52 E-value: 3.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 107 PCLGSRKAGQPYKWLSYKEVADRAEFAGSALLHRGhsQSGDKYIGIFAQNRPEWTISELACYTYSLVAVPL---YDTLGT 183
Cdd:cd05921 12 TWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLG--LSAERPLLILSGNSIEHALMALAAMYAGVPAAPVspaYSLMSQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 184 E--AISYVIDKASITTIICDIADKARLILDCVsgrKHSVTTIVIMesfdseltaQAQNCGIDIISLKEL---EAIGKANH 258
Cdd:cd05921 90 DlaKLKHLFELLKPGLVFAQDAAPFARALAAI---FPLGTPLVVS---------RNAVAGRGAISFAELaatPPTAAVDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 259 KTPiPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSN------CSAFIKiTEVHCMLNqtdihisYLPLAHMF-ERVVEG 331
Cdd:cd05921 158 AFA-AVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANqamleqTYPFFG-EEPPVLVD-------WLPWNHTFgGNHNFN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 332 VLLCHGAKI---------GYFQGDIRllmdDLKNLKPTIFPVVPrllnrmfdkifgqantplKRWlldfatsrkeaELKS 402
Cdd:cd05921 229 LVLYNGGTLyiddgkpmpGGFEETLR----NLREISPTVYFNVP------------------AGW-----------EMLV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 403 GVVRKDSMWDKLIFSkvqaslggRVRLMITGAAPVSPTVLTFLRAaLGCQ-------FYEGYGQTECTAGCTMSLPGDWT 475
Cdd:cd05921 276 AALEKDEALRRRFFK--------RLKLMFYAGAGLSQDVWDRLQA-LAVAtvgeripMMAGLGATETAPTATFTHWPTER 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 476 AGHVGAPLPCNFVKLVdvaemnyfAANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWL----PNGTLKI 551
Cdd:cd05921 347 SGLIGLPAPGTELKLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpddPAKGLVF 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 552 IDRKKHIFKLAQGEYIA--PEKIENIYIRSDPVAQVFVHGDSlQACLVGVVVPDPDFLPgwAKNRGIEGSFNDLCKSKEV 629
Cdd:cd05921 419 DGRVAEDFKLASGTWVSvgPLRARAVAACAPLVHDAVVAGED-RAEVGALVFPDLLACR--RLVGLQEASDAEVLRHAKV 495
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528467778 630 KNAILEDMIQLGKEAGLKSFEQVRdIALHLEMFSVQNGLLTPTLKAKRTELKSRFREQIDQLYAK 694
Cdd:cd05921 496 RAAFRDRLAALNGEATGSSSRIAR-ALLLDEPPSIDKGEITDKGYINQRAVLERRAALVERLYAD 559
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
121-608 |
2.45e-23 |
|
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: 106.09 E-value: 2.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAE-FAGsALLHRGHsQSGDKyIGIFAQNRPEWTISELA------CYtyslvaVPLYDTLGTEAISYVIDKA 193
Cdd:COG1020 502 LTYAELNARANrLAH-HLRALGV-GPGDL-VGVCLERSLEMVVALLAvlkagaAY------VPLDPAYPAERLAYMLEDA 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 194 sittiicdiadKARLILDcvsgrkhsvttivimesfDSELTAQAQNCGIDIISLKELEAIGKANHKTPIPPKPEDLALIC 273
Cdd:COG1020 573 -----------GARLVLT------------------QSALAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLAYVI 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 274 FTSGTTGNPKGAMLTHGNVVSNCSAFIKitevHCMLNQTDIHISYLPLAH------MFervvegVLLCHGAKIGYFQGDI 347
Cdd:COG1020 624 YTSGSTGRPKGVMVEHRALVNLLAWMQR----RYGLGPGDRVLQFASLSFdasvweIF------GALLSGATLVLAPPEA 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 348 RLLMDDLKNL----KPTIFPVVPrllnrmfdkifgqantplkrwlldfatsrkeaelksgvvrkdSMWDKLIfsKVQASL 423
Cdd:COG1020 694 RRDPAALAELlarhRVTVLNLTP------------------------------------------SLLRALL--DAAPEA 729
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 424 GGRVRLMITGAAPVSPTVLTFLRAAL-GCQFYEGYGQTECTAGCTMSL--PGDWTAGHV--GAPLPCNFVKLVDvaemny 498
Cdd:COG1020 730 LPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTVDSTYYEvtPPDADGGSVpiGRPIANTRVYVLD------ 803
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 499 faANGE-------GEVCVKGPNVFQGYLKDPEQTSGA-----VDKAG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQG 564
Cdd:COG1020 804 --AHLQpvpvgvpGELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNLEFLGRADDQVKI-RG 880
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 528467778 565 EYIAPEKIENIyIRSDP-VAQ--VFVHGDSLQA-CLVGVVVPDPDFLP 608
Cdd:COG1020 881 FRIELGEIEAA-LLQHPgVREavVVAREDAPGDkRLVAYVVPEAGAAA 927
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
258-605 |
5.34e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 102.76 E-value: 5.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 258 HKTPIPPkPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEvhcmLNQTDIHISYLPLAHMfervvegvllcHG 337
Cdd:PRK07787 120 HRYPEPD-PDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQ----WTADDVLVHGLPLFHV-----------HG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 338 akigyfqgdirLLMDDLKNLkptifpvvpRLLNRMfdkifgqantplkRWLLDFATSRKEAELKS------GVvrkDSMW 411
Cdd:PRK07787 184 -----------LVLGVLGPL---------RIGNRF-------------VHTGRPTPEAYAQALSEggtlyfGV---PTVW 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 412 DKLIFSKVQASLGGRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLV 491
Cdd:PRK07787 228 SRIAADPEAARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLV 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 492 DVaEMNYFAANGE--GEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDR------KKHIFKLAQ 563
Cdd:PRK07787 308 DE-DGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGGYRIGA 386
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 528467778 564 GEyiapekIENIYIRSDPVAQVFVHG---DSLQACLVGVVVPDPD 605
Cdd:PRK07787 387 GE------IETALLGHPGVREAAVVGvpdDDLGQRIVAYVVGADD 425
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
112-543 |
2.40e-22 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 101.88 E-value: 2.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 112 RKAGQPYKWLSYKEVADRAEFAGSALLHRGHSQsgDKYIGIFAQNRPEWTISELACYT-----------YSLVAVPL--- 177
Cdd:PRK08180 61 RGADGGWRRLTYAEALERVRAIAQALLDRGLSA--ERPLMILSGNSIEHALLALAAMYagvpyapvspaYSLVSQDFgkl 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 178 ---YDTLgTEAISYVIDKASITTIIcDIADKARLILDCVSGRKHSVTTIvimeSFDSELTAQaqncgidiislkELEAIG 254
Cdd:PRK08180 139 rhvLELL-TPGLVFADDGAAFARAL-AAVVPADVEVVAVRGAVPGRAAT----PFAALLATP------------PTAAVD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 255 KANHKTpippKPEDLALICFTSGTTGNPKGAMLTHGNVVSN------CSAFIKITEVhcmlnqtdIHISYLPLAHMFERV 328
Cdd:PRK08180 201 AAHAAV----GPDTIAKFLFTSGSTGLPKAVINTHRMLCANqqmlaqTFPFLAEEPP--------VLVDWLPWNHTFGGN 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 329 VE-GVLLCHGAKigyfqgdirLLMDD-----------LKNLK---PTIFPVVPR----LLNRMfdkifgqantplkrwll 389
Cdd:PRK08180 269 HNlGIVLYNGGT---------LYIDDgkptpggfdetLRNLReisPTVYFNVPKgwemLVPAL----------------- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 390 dfatsRKEAELKsgvvrkdsmwdklifskvqASLGGRVRLMITGAAPVSPTVLTFL----RAALGCQ--FYEGYGQTEcT 463
Cdd:PRK08180 323 -----ERDAALR-------------------RRFFSRLKLLFYAGAALSQDVWDRLdrvaEATCGERirMMTGLGMTE-T 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 464 AGCTMSL--PGDwTAGHVGAPLPCNFVKLVDVaemnyfaaNGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIG 541
Cdd:PRK08180 378 APSATFTtgPLS-RAGNIGLPAPGCEVKLVPV--------GGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAV 448
|
..
gi 528467778 542 KW 543
Cdd:PRK08180 449 RF 450
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
233-606 |
3.98e-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: 100.48 E-value: 3.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 233 LTAQAQNCGIDIISLKELEAIGKANHKT----PIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITevhcM 308
Cdd:cd17655 99 LTQSHLQPPIAFIGLIDLLDEDTIYHEEsenlEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVI----Y 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 309 LNQTDIHISYLPLAhmFERVVEGV---LLCHGAKIGYFQ---GDIRLLMDDLKNLKPTIFPVVPRLLNrmfdkifgqant 382
Cdd:cd17655 175 QGEHLRVALFASIS--FDASVTEIfasLLSGNTLYIVRKetvLDGQALTQYIRQNRITIIDLTPAHLK------------ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 383 plkrwLLDfatsrkeaelksgvvrkdsmwdklifsKVQASLGGRVRLMITGAAPVSPTVLTFL--RAALGCQFYEGYGQT 460
Cdd:cd17655 241 -----LLD---------------------------AADDSEGLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPT 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 461 ECTAGCTMSL--PGDWTAGHV--GAPLPCNFVKLVDvAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGA-VDK---- 531
Cdd:cd17655 289 ETTVDASIYQyePETDQQVSVpiGKPLGNTRIYILD-QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKfVDDpfvp 367
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528467778 532 AGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDPVAQ--VFVHGD-SLQACLVGVVVPDPDF 606
Cdd:cd17655 368 GERMYrTGDLARWLPDGNIEFLGRIDHQVKI-RGYRIELGEIEARLLQHPDIKEavVIARKDeQGQNYLCAYIVSEKEL 445
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
120-604 |
1.43e-21 |
|
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: 98.53 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 120 WLSYKEVADRAEFAGSALLHRGHSqSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTII 199
Cdd:cd12118 29 RYTWRQTYDRCRRLASALAALGIS-RGDT-VAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 200 CDiadkarlildcvsgrkhsvttivimESFDSEltaqaqncgidiislkELEAIGKANHKtPIPPKPE-DLALICFTSGT 278
Cdd:cd12118 107 VD-------------------------REFEYE----------------DLLAEGDPDFE-WIPPADEwDPIALNYTSGT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 279 TGNPKGAMLTH-GNVVSNCSAFIkitevhcmLNQTDIHISYLPLAHMFErvvegvllCHG-------AKIGyfqG----- 345
Cdd:cd12118 145 TGRPKGVVYHHrGAYLNALANIL--------EWEMKQHPVYLWTLPMFH--------CNGwcfpwtvAAVG---Gtnvcl 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 346 ---DIRLLMDDLKNLKPTIFPVVPRLLNRMfdkifgqANTPlkrwlldfatsrkeaelksgvvrkdsmwdklifSKVQAS 422
Cdd:cd12118 206 rkvDAKAIYDLIEKHKVTHFCGAPTVLNML-------ANAP---------------------------------PSDARP 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 423 LGGRVRLMITGAAPvsPTVLTFLRAALGCQFYEGYGQTEcTAG----CTM-----SLPGDWTA--------GHVGAplpc 485
Cdd:cd12118 246 LPHRVHVMTAGAPP--PAAVLAKMEELGFDVTHVYGLTE-TYGpatvCAWkpewdELPTEERArlkarqgvRYVGL---- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 486 NFVKLVDVAEMNYFAANGE--GEVCVKGPNVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQ 563
Cdd:cd12118 319 EEVDVLDPETMKPVPRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISG 396
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 528467778 564 GEYIAPEKIENIyirsdpvaqVFVHGDSLQACLVGvvVPDP 604
Cdd:cd12118 397 GENISSVEVEGV---------LYKHPAVLEAAVVA--RPDE 426
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
121-604 |
1.99e-21 |
|
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: 97.70 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEfAGSALLHRGHSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:cd05945 17 LTYRELKERAD-ALAAALASLGLDAGDP-VVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPALLIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 201 DiadkarlildcvsgrkhsvttivimesfdseltaqaqncgidiislkeleaigkanhktpippkPEDLALICFTSGTTG 280
Cdd:cd05945 95 D----------------------------------------------------------------GDDNAYIIFTSGSTG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 281 NPKGAMLTHGNVVS----NCSAFIKITEVHcMLNQTDIHisylplahmFERVVEGVL--LCHGAkigyfqgdirllmddl 354
Cdd:cd05945 111 RPKGVQISHDNLVSftnwMLSDFPLGPGDV-FLNQAPFS---------FDLSVMDLYpaLASGA---------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 355 knlkpTIFPVvPRLLnrmfdkifgqantplKRWLLDFATSRKEAELkSGVVRKDSMWDKLIFSK--VQASLGGRVRLMIT 432
Cdd:cd05945 165 -----TLVPV-PRDA---------------TADPKQLFRFLAEHGI-TVWVSTPSFAAMCLLSPtfTPESLPSLRHFLFC 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 433 GAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTM------------SLPgdwtaghVGAPLPCNFVKLVDvAEMNYFA 500
Cdd:cd05945 223 GEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYievtpevldgydRLP-------IGYAKPGAKLVILD-EDGRPVP 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 501 ANGEGEVCVKGPNVFQGYLKDPEQTSGA---VDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYI 577
Cdd:cd05945 295 PGEKGELVISGPSVSKGYLNNPEKTAAAffpDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIELEEIEAALR 373
|
490 500 510
....*....|....*....|....*....|.
gi 528467778 578 RSDPVAQVFV----HGDSLQAcLVGVVVPDP 604
Cdd:cd05945 374 QVPGVKEAVVvpkyKGEKVTE-LIAFVVPKP 403
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
266-589 |
5.92e-21 |
|
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: 95.24 E-value: 5.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 266 PEDLALICFTSGTTGNPKGAMLTHGNVVSNCsafiKITEVHCMLNQTDIHISYLPLAHMFERVVEGVLLCH-GAKIgyfq 344
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNA----WMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLAsGAHV---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 345 gdirLLMDDLKNLKPTIFPVVPRLLNRMfdkifgqantplkrwlldfatsrkEAELKSGVvrkDSMWDKLIFSKVQASLG 424
Cdd:cd05944 73 ----VLAGPAGYRNPGLFDNFWKLVERY------------------------RITSLSTV---PTVYAALLQVPVNADIS 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 425 GrVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLP-GDWTAGHVGAPLPCNFVKLVDV-AEMNYF--A 500
Cdd:cd05944 122 S-LRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKVLdGVGRLLrdC 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 501 ANGE-GEVCVKGPNVFQGYLKDpEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRS 579
Cdd:cd05944 201 APDEvGEICVAGPGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLRH 278
|
330
....*....|
gi 528467778 580 DPVAQVFVHG 589
Cdd:cd05944 279 PAVAFAGAVG 288
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
268-604 |
1.08e-20 |
|
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: 93.55 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 268 DLALICFTSGTTGNPKGAMLTHGNVVSNCSA---FIKIT-EVHCMLNqtdihisyLPLAHM--FERVVEGVLLchGAKIg 341
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGlhsRLGFGgGDSWLLS--------LPLYHVggLAILVRSLLA--GAEL- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 342 YFQGDIRLLMDDLKNLKPTIFPVVPRLLNRMFDKifGQANTPLKRwlldfatsrkeaelksgvvrkdsmwdklifskvqa 421
Cdd:cd17630 70 VLLERNQALAEDLAPPGVTHVSLVPTQLQRLLDS--GQGPAALKS----------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 422 slggrVRLMITGAAPVsPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDvaemnyfaa 501
Cdd:cd17630 113 -----LRAVLLGGAPI-PPELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVE--------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 502 ngEGEVCVKGPNVFQGYLKDPEQtsGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDP 581
Cdd:cd17630 178 --DGEIWVGGASLAMGYLRGQLV--PEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPA 252
|
330 340
....*....|....*....|....*.
gi 528467778 582 VAQVFVHG---DSLQACLVGVVVPDP 604
Cdd:cd17630 253 VRDAFVVGvpdEELGQRPVAVIVGRG 278
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
115-604 |
1.20e-20 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 95.19 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 115 GQPYKWlSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKAS 194
Cdd:cd05971 2 GTPEKV-TFKELKTASNRFANVLKEIG-LEKGDR-VGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 195 ITTIICDIADkarlildcvsgrkhsvttivimesfdseltaqaqncgidiislkeleaigkanhktpippkpeDLALICF 274
Cdd:cd05971 79 ASALVTDGSD---------------------------------------------------------------DPALIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 275 TSGTTGNPKGAMltHGNVVsncsafikitevhcMLNqtdiHISYLPLAH-MFERvvEGVLLCHGAKIGYFQGDIRLLMdd 353
Cdd:cd05971 96 TSGTTGPPKGAL--HAHRV--------------LLG----HLPGVQFPFnLFPR--DGDLYWTPADWAWIGGLLDVLL-- 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 354 lknlkPTIFPVVPRLLNRM--FDKifGQANTPLKRWLLDFATSRKEAeLKSGVVRKDSMWDKLIfskvqaslggRVRLMI 431
Cdd:cd05971 152 -----PSLYFGVPVLAHRMtkFDP--KAALDLMSRYGVTTAFLPPTA-LKMMRQQGEQLKHAQV----------KLRAIA 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 432 TGAAPVSPTVLTFLRAALGCQFYEGYGQTEC---TAGCTMSLPGDwtAGHVGAPLPCNFVKLVDvAEMNYFAANGEGEVC 508
Cdd:cd05971 214 TGGESLGEELLGWAREQFGVEVNEFYGQTECnlvIGNCSALFPIK--PGSMGKPIPGHRVAIVD-DNGTPLPPGEVGEIA 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 509 VKGPN--VFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRsdpvaqvf 586
Cdd:cd05971 291 VELPDpvAFLGYWNNPSATEKKM-AGDWLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAEIEECLLK-------- 360
|
490
....*....|....*...
gi 528467778 587 vHGDSLQACLVGvvVPDP 604
Cdd:cd05971 361 -HPAVLMAAVVG--IPDP 375
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
121-604 |
1.67e-20 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 96.96 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGHsqsGDKYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:PRK06814 659 LTYRKLLTGAFVLGRKLKKNTP---PGENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 201 DIA--DKARLildcvsgrkhsvttivimesfdSELTAQAQNcGIDIISLKELEA-----------IGKANHKTPIP-PKP 266
Cdd:PRK06814 736 SRAfiEKARL----------------------GPLIEALEF-GIRIIYLEDVRAqigladkikglLAGRFPLVYFCnRDP 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 267 EDLALICFTSGTTGNPKGAMLTHGNVVSNC---SAFIKitevhcmLNQTDIHISYLPLAHMFervvegvllchgakiGYF 343
Cdd:PRK06814 793 DDPAVILFTSGSEGTPKGVVLSHRNLLANRaqvAARID-------FSPEDKVFNALPVFHSF---------------GLT 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 344 QGdirLLMDDLKNLKPTIFP------VVPRLlnrmfdkIFGQANTPLkrwlldFATSrkeaELKSGVVRKDSMWDkliFs 417
Cdd:PRK06814 851 GG---LVLPLLSGVKVFLYPsplhyrIIPEL-------IYDTNATIL------FGTD----TFLNGYARYAHPYD---F- 906
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 418 kvqASLggrvRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDVAEMN 497
Cdd:PRK06814 907 ---RSL----RYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGID 979
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 498 yfaaNGeGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYI 577
Cdd:PRK06814 980 ----EG-GRLFVRGPNVMLGYLRAENPGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAVEELAA 1053
|
490 500
....*....|....*....|....*..
gi 528467778 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 |
2.27e-20 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 94.96 E-value: 2.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELA------CYtyslvaVPLYDTLGTEAISYVIDKAs 194
Cdd:cd12117 23 LTYAELNERANRLARRLRAAG-VGPGDV-VGVLAERSPELVVALLAvlkagaAY------VPLDPELPAERLAFMLADA- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 195 ittiicdiadKARLILDcvsgrkhsvttivimesfDSELTAQAQNCGIDIISLKELEAIGKANHKTPIppKPEDLALICF 274
Cdd:cd12117 94 ----------GAKVLLT------------------DRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPV--SPDDLAYVMY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 275 TSGTTGNPKGAMLTHGNVVSNC--SAFIKITEVHCMLNQTdihisylPL---AHMFErvVEGVLLcHGAkigyfqgdiRL 349
Cdd:cd12117 144 TSGSTGRPKGVAVTHRGVVRLVknTNYVTLGPDDRVLQTS-------PLafdASTFE--IWGALL-NGA---------RL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 350 LMDDlknlkptifPVVPRLLNRMFDKIFGQANTPLkrWLldfatsrkEAELKSGVVRKDSmwdklifskvqASLGGrVRL 429
Cdd:cd12117 205 VLAP---------KGTLLDPDALGALIAEEGVTVL--WL--------TAALFNQLADEDP-----------ECFAG-LRE 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 430 MITGAAPVSPT-VLTFLRAALGCQFYEGYGQTECT--AGCTMSLPGDWTAGHV--GAPLPCNFVKLVDVAEMnyFAANGE 504
Cdd:cd12117 254 LLTGGEVVSPPhVRRVLAACPGLRLVNGYGPTENTtfTTSHVVTELDEVAGSIpiGRPIANTRVYVLDEDGR--PVPPGV 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 505 -GEVCVKGPNVFQGYLKDPEQTSGAVDKAGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYI 577
Cdd:cd12117 332 pGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI-RGFRIELGEIEAALR 410
|
490 500 510
....*....|....*....|....*....|.
gi 528467778 578 RSDPVAQVFV---HGDSLQACLVGVVVPDPD 605
Cdd:cd12117 411 AHPGVREAVVvvrEDAGGDKRLVAYVVAEGA 441
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
258-584 |
2.38e-20 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 95.93 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 258 HKTPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNcsafikITEVHCMLNQT--DIHISYLPLAHMFERVVeGVL-- 333
Cdd:PRK08043 356 RLAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLLAN------VEQIKTIADFTpnDRFMSALPLFHSFGLTV-GLFtp 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 334 LCHGAKIGYFQgdirllmddlknlKPTIFPVVPRLL-NRMFDKIFGQAnTPLKRWL-----LDFAtsrkeaelksgvvrk 407
Cdd:PRK08043 429 LLTGAEVFLYP-------------SPLHYRIVPELVyDRNCTVLFGTS-TFLGNYArfanpYDFA--------------- 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 408 dsmwdklifskvqaslggRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNF 487
Cdd:PRK08043 480 ------------------RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMD 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 488 VKLVDVAEMnyfaANGeGEVCVKGPNVFQGYLK--DP--------EQTSGAVDkAGWLHTGDIGKWLPNGTLKIIDRKKH 557
Cdd:PRK08043 542 ARLLSVPGI----EQG-GRLQLKGPNIMNGYLRveKPgvlevptaENARGEME-RGWYDTGDIVRFDEQGFVQIQGRAKR 615
|
330 340
....*....|....*....|....*..
gi 528467778 558 IFKLAqGEYIAPEKIENIYIRSDPVAQ 584
Cdd:PRK08043 616 FAKIA-GEMVSLEMVEQLALGVSPDKQ 641
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
119-604 |
1.85e-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: 92.56 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 119 KWLSYKEVADRAEFAGSALLHRGhSQSGDkYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTI 198
Cdd:cd05970 46 RIFTFAELADYSDKTANFFKAMG-IGKGD-TVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 199 ICDIADKARLILDCVSGRKHSVTTIVIMESFDSEltaqaqncgiDIISLKELeaIGKANHKTPIP-----PKPEDLALIC 273
Cdd:cd05970 124 VAIAEDNIPEEIEKAAPECPSKPKLVWVGDPVPE----------GWIDFRKL--IKNASPDFERPtansyPCGEDILLVY 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 274 FTSGTTGNPKgaMLTHGNvvsncsafikitevhcmlnqtdihiSYlPLAHM-----FERVVEGVLLCHGAKIGYFQGdir 348
Cdd:cd05970 192 FSSGTTGMPK--MVEHDF-------------------------TY-PLGHIvtakyWQNVREGGLHLTVADTGWGKA--- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 349 llmddlknlkptifpvvprllnrMFDKIFGQANTPLKRWLLDFATSRKEAEL----KSGVVR---KDSMWDKLIFSKVQA 421
Cdd:cd05970 241 -----------------------VWGKIYGQWIAGAAVFVYDYDKFDPKALLeklsKYGVTTfcaPPTIYRFLIREDLSR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 422 SLGGRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAgCTMSLPG-DWTAGHVGAPLPCNFVKLVDvAEMNYFA 500
Cdd:cd05970 298 YDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTL-TIATFPWmEPKPGSMGKPAPGYEIDLID-REGRSCE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 501 ANGEGEVCV---KGPNV--FQGYLKDPEQTSgAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENI 575
Cdd:cd05970 376 AGEEGEIVIrtsKGKPVglFGGYYKDAEKTA-EVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVESA 453
|
490 500
....*....|....*....|....*....
gi 528467778 576 YIRSDPVAQVFVHGdslqaclvgvvVPDP 604
Cdd:cd05970 454 LIQHPAVLECAVTG-----------VPDP 471
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
121-597 |
2.00e-19 |
|
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: 92.19 E-value: 2.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITT-II 199
Cdd:cd05923 29 LTYSELRARIEAVAARLHARG-LRPGQR-VAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAaVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 200 CDIADKARLILDCVsGRkhsvttiVIMESfdseltaqaqncgiDIISLKELEAIGKAnhKTPIPPKPEDLALICFTSGTT 279
Cdd:cd05923 107 AVDAQVMDAIFQSG-VR-------VLALS--------------DLVGLGEPESAGPL--IEDPPREPEQPAFVFYTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 280 GNPKGAMLTHGNVVSNcSAFIkITEVHCMLNQTDIHISYLPLAHMfervvegvllchgakIGYFQgdirLLMDDLKnLKP 359
Cdd:cd05923 163 GLPKGAVIPQRAAESR-VLFM-STQAGLRHGRHNVVLGLMPLYHV---------------IGFFA----VLVAALA-LDG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 360 TIFPVvprllnRMFDKifGQAntpLKrWLldfatsrkEAELKSGVVRKDSMWDKLIFSKVQASLG-GRVRLMITGAAPVS 438
Cdd:cd05923 221 TYVVV------EEFDP--ADA---LK-LI--------EQERVTSLFATPTHLDALAAAAEFAGLKlSSLRHVTFAGATMP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 439 PTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPgdwTAGHVGAPLPCNFVKLVDV-AEMNYFAANG-EGEVCVK--GPNV 514
Cdd:cd05923 281 DAVLERVNQHLPGEKVNIYGTTEAMNSLYMRDA---RTGTEMRPGFFSEVRIVRIgGSPDEALANGeEGELIVAaaADAA 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 515 FQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVFV------- 587
Cdd:cd05923 358 FTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVigvader 435
|
490
....*....|
gi 528467778 588 HGDSLQACLV 597
Cdd:cd05923 436 WGQSVTACVV 445
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
222-573 |
4.78e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 91.21 E-value: 4.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 222 TIVIMESFDSELTAQAQNcGIDIISLKELEAIGKAnhkTPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAF-- 299
Cdd:PRK07768 111 AVVVGEPFLAAAPVLEEK-GIRVLTVADLLAADPI---DPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMfv 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 300 -IKITEVHcmlnqtDIHISYLPLAH-MfervvegvllchgAKIGYFQGDIRLLMDDLKnLKPTIFPVVPRLLNRMFDKIF 377
Cdd:PRK07768 187 aAEFDVET------DVMVSWLPLFHdM-------------GMVGFLTVPMYFGAELVK-VTPMDFLRDPLLWAELISKYR 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 378 GqANT--PlkrwllDFATSrkeaeLKSGVVRKDSMWDKLIFSKvqaslggrVRLMITGAAPVSP-TVLTFLRA------- 447
Cdd:PRK07768 247 G-TMTaaP------NFAYA-----LLARRLRRQAKPGAFDLSS--------LRFALNGAEPIDPaDVEDLLDAgarfglr 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 448 --ALGCqfyeGYGQTECTAGCTMSLPGD--------------------WTAGHV------GAPLPCNFVKLVDvAEMNYF 499
Cdd:PRK07768 307 peAILP----AYGMAEATLAVSFSPCGAglvvdevdadllaalrravpATKGNTrrlatlGPPLPGLEVRVVD-EDGQVL 381
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528467778 500 AANGEGEVCVKGPNVFQGYLkDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIE 573
Cdd:PRK07768 382 PPRGVGVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPTDIE 453
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
135-602 |
6.53e-19 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 90.72 E-value: 6.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 135 SALLHRGHSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLgteAISYVIDKASittiicdiADKARLILdcVS 214
Cdd:PRK05852 57 AGQLTRSGLLPGDR-VALRMGSNAEFVVALLAASRADLVVVPLDPAL---PIAEQRVRSQ--------AAGARVVL--ID 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 215 GRKHSVTTIVIMESFDSELTAQAQNCGIDIISLKELEAIGKANHKTPIPP--KPEDlALICFTSGTTGNPKGAMLTHGNV 292
Cdd:PRK05852 123 ADGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTPATSTPEglRPDD-AMIMFTGGTTGLPKMVPWTHANI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 293 VSNCSAFIKITEvhcmLNQTDIHISYLPLAHMfERVVEGVL--LCHGAKI-----GYFQGdiRLLMDDLKNLKPTIFPVV 365
Cdd:PRK05852 202 ASSVRAIITGYR----LSPRDATVAVMPLYHG-HGLIAALLatLASGGAVllparGRFSA--HTFWDDIKAVGATWYTAV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 366 PR----LLNRMFDKIFGQANTPLkrwlldfatsrkeaelksgvvrkdsmwdklifskvqaslggrvRLMITGAAPVSPTV 441
Cdd:PRK05852 275 PTihqiLLERAATEPSGRKPAAL-------------------------------------------RFIRSCSAPLTAET 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 442 LTFLRAALGCQFYEGYGQTECT----------AGCT----MS--LPGDWTA------GHVGAPLPCNFVklvdvaemnyf 499
Cdd:PRK05852 312 AQALQTEFAAPVVCAFGMTEAThqvtttqiegIGQTenpvVStgLVGRSTGaqirivGSDGLPLPAGAV----------- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 500 aangeGEVCVKGPNVFQGYLKDPEQTSGAVDKaGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRS 579
Cdd:PRK05852 381 -----GEVWLRGTTVVRGYLGDPTITAANFTD-GWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLASH 453
|
490 500
....*....|....*....|....*.
gi 528467778 580 DPVAQVFVHG--DSLQACLVG-VVVP 602
Cdd:PRK05852 454 PNVMEAAVFGvpDQLYGEAVAaVIVP 479
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
121-587 |
1.98e-18 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 88.29 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALlhRGHSQSGDKYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIdkasittiic 200
Cdd:cd05919 11 VTYGQLHDGANRLGSAL--RNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIA---------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 201 diadkarlildcvsgrKHSVTTIVIMESfdseltaqaqncgidiislkeleaigkanhktpippkpEDLALICFTSGTTG 280
Cdd:cd05919 79 ----------------RDCEARLVVTSA--------------------------------------DDIAYLLYSSGTTG 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 281 NPKGAMLTHGNVVSNCSAFIKitEVhCMLNQTDIHISylpLAHMFErvveGVLLCHGAKIGYFQGDIRLLMDD------- 353
Cdd:cd05919 105 PPKGVMHAHRDPLLFADAMAR--EA-LGLTPGDRVFS---SAKMFF----GYGLGNSLWFPLAVGASAVLNPGwptaerv 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 354 ---LKNLKPTIFPVVPRLLNRMfdkifgqantplkrwlldfatsrkeaeLKSGVVRKDSMWDklifskvqaslggrVRLM 430
Cdd:cd05919 175 latLARFRPTVLYGVPTFYANL---------------------------LDSCAGSPDALRS--------------LRLC 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 431 ITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDvAEMNYFAANGEGEVCVK 510
Cdd:cd05919 214 VSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD-EEGHTIPPGEEGDLLVR 292
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528467778 511 GPNVFQGYLKDPEqTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSDPVAQVFV 587
Cdd:cd05919 293 GPSAAVGYWNNPE-KSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVESLIIQHPAVAEAAV 367
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
266-603 |
1.28e-17 |
|
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: 85.98 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 266 PEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEVhcmlnqTDIHISYLPLAHMFERVVEGVL---LCHGAKIGY 342
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYEL------DSFPVRLLQMASFSFDVFAGDFarsLLNGGTLVI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 343 FQGDIRL----LMDDLKNLKPTIFPVVPRLLnrmfdkifgqantplkRWLLDFATSRKE--AELKSGVVRKDSMWDKLiF 416
Cdd:cd17650 166 CPDEVKLdpaaLYDLILKSRITLMESTPALI----------------RPVMAYVYRNGLdlSAMRLLIVGSDGCKAQD-F 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 417 SKVQASLGGRVRlmITGAAPVSptvltflRAALGCQFYEGYGQTECTAGCTmslPgdwtaghVGAPLPCNFVKLVDvAEM 496
Cdd:cd17650 229 KTLAARFGQGMR--IINSYGVT-------EATIDSTYYEEGRDPLGDSANV---P-------IGRPLPNTAMYVLD-ERL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 497 NYFAANGEGEVCVKGPNVFQGYLKDPEQTSGA------VDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPE 570
Cdd:cd17650 289 QPQPVGVAGELYIGGAGVARGYLNRPELTAERfvenpfAPGERMYRTGDLARWRADGNVELLGRVDHQVKI-RGFRIELG 367
|
330 340 350
....*....|....*....|....*....|....*.
gi 528467778 571 KIENIYIRSDPVAQVFV---HGDSLQACLVGVVVPD 603
Cdd:cd17650 368 EIESQLARHPAIDEAVVavrEDKGGEARLCAYVVAA 403
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
266-582 |
2.27e-17 |
|
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: 85.62 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 266 PEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEVhcmlNQTDIHISYLPLAHMFervveGVLLCHGAKIgyFQG 345
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEW----KTKDRILSWMPLTHDM-----GLIAFHLAPL--IAG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 346 DIRLLMddlknlkPT-IFPVVPRLLNRMFDK----IFGQANTPLKrWLLDFATSRKEAElksgvvrkdsmWDKlifskvq 420
Cdd:cd05908 174 MNQYLM-------PTrLFIRRPILWLKKASEhkatIVSSPNFGYK-YFLKTLKPEKAND-----------WDL------- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 421 aslgGRVRLMITGAAPVSPT---VLTFLRAALGCQ---FYEGYGQTECTAGCTMSLPGD--------------------- 473
Cdd:cd05908 228 ----SSIRMILNGAEPIDYElchEFLDHMSKYGLKrnaILPVYGLAEASVGASLPKAQSpfktitlgrrhvthgepepev 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 474 -------WTAGHVGAPLPCNFVKLVDvaEMNYFAANGE-GEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGkWLP 545
Cdd:cd05908 304 dkkdsecLTFVEVGKPIDETDIRICD--EDNKILPDGYiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIR 380
|
330 340 350
....*....|....*....|....*....|....*..
gi 528467778 546 NGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPV 582
Cdd:cd05908 381 NGRLVITGREKDII-FVNGQNVYPHDIERIAEELEGV 416
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
122-604 |
2.91e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 85.48 E-value: 2.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 122 SYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC- 200
Cdd:PRK07470 34 TWREIDARVDALAAALAARG-VRKGDR-ILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMICh 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 201 -DIADKARLILDCVSGRKHSvttIVIMESFDSEltaqaqncgidiislkELEAIGKANHKTPIPPKP---EDLALICFTS 276
Cdd:PRK07470 112 aDFPEHAAAVRAASPDLTHV---VAIGGARAGL----------------DYEALVARHLGARVANAAvdhDDPCWFFFTS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 277 GTTGNPKGAMLTHGNVvsncsAFIkITEVHCML----NQTDIHISYLPLAHMfervvEGV-LLC---HGAKigyfqgdir 348
Cdd:PRK07470 173 GTTGRPKAAVLTHGQM-----AFV-ITNHLADLmpgtTEQDASLVVAPLSHG-----AGIhQLCqvaRGAA--------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 349 llmddlknlkpTIFPVVPRllnrmFDkiFGQANTPLKRWLLD--FA--TSRKEAELKSGVVRKDsmwdklifskvQASLg 424
Cdd:PRK07470 233 -----------TVLLPSER-----FD--PAEVWALVERHRVTnlFTvpTILKMLVEHPAVDRYD-----------HSSL- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 425 grvRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTaGCTMSLP------GDWTAGHVGaplPCNF------VKLVD 492
Cdd:PRK07470 283 ---RYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVT-GNITVLPpalhdaEDGPDARIG---TCGFertgmeVQIQD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 493 vAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKI 572
Cdd:PRK07470 356 -DEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPREI 432
|
490 500 510
....*....|....*....|....*....|..
gi 528467778 573 ENiyirsdpvaQVFVHGDSLQACLVGvvVPDP 604
Cdd:PRK07470 433 EE---------KLLTHPAVSEVAVLG--VPDP 453
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
107-609 |
3.01e-17 |
|
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: 84.84 E-value: 3.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 107 PCLGSrkagqPYKWLSYKEVADRAEFAGSALLHRGHSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAI 186
Cdd:cd05958 2 TCLRS-----PEREWTYRDLLALANRIANVLVGELGIVPGNR-VLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 187 SYVIDKASITTIICDiadkarlildcvsgrkHSVTTIvimesfdseltaqaqncgidiislkeleaigkanhktpippkp 266
Cdd:cd05958 76 AYILDKARITVALCA----------------HALTAS------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 267 EDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFikitEVHCM-LNQTDIHISYLPLAHMFERvvEGVLL---CHGAKIGY 342
Cdd:cd05958 97 DDICILAFTSGTTGAPKATMHFHRDPLASADRY----AVNVLrLREDDRFVGSPPLAFTFGL--GGVLLfpfGVGASGVL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 343 FQGDI-RLLMDDLKNLKPTIFPVVPRLLNRMFDKifgqantplkrwlLDFAtsrkeaelksgvvrkdsmwdklifskvqA 421
Cdd:cd05958 171 LEEATpDLLLSAIARYKPTVLFTAPTAYRAMLAH-------------PDAA----------------------------G 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 422 SLGGRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDvAEMNYFAA 501
Cdd:cd05958 210 PDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD-DEGNPVPD 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 502 NGEGEVCVKGPNVFQgYLKDPEQTSGAVDkaGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSDP 581
Cdd:cd05958 289 GTIGRLAVRGPTGCR-YLADKRQRTYVQG--GWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQHPA 364
|
490 500 510
....*....|....*....|....*....|.
gi 528467778 582 VAQVFVHGDSLQACLVGV---VVPDPDFLPG 609
Cdd:cd05958 365 VAECAVVGHPDESRGVVVkafVVLRPGVIPG 395
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
266-589 |
3.87e-17 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 85.24 E-value: 3.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 266 PEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEvhcmLNQTDIHISYLPLAH-------MFERVVEGvllCHgA 338
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVG----YGEDDVYLHTAPLCHigglssaLAMLMVGA---CH-V 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 339 KIGYFqgDIRLLMDDLKNLKPTIFPVVPRLL------NRMfdKIFGQANTPLKRwLLDFATSRKEAELKSGVvrkdsmwd 412
Cdd:PLN02860 243 LLPKF--DAKAALQAIKQHNVTSMITVPAMMadlislTRK--SMTWKVFPSVRK-ILNGGGSLSSRLLPDAK-------- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 413 kLIFSkvqaslggRVRLMITGAAPVSPTVLTFLRaaLGCQFYEGYGQTECTAGCTMSLPGDWTAGH-VGAPLPcnFVKLv 491
Cdd:PLN02860 310 -KLFP--------NAKLFSAYGMTEACSSLTFMT--LHDPTLESPKQTLQTVNQTKSSSVHQPQGVcVGKPAP--HVEL- 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 492 dvaEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEK 571
Cdd:PLN02860 376 ---KIGLDESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIK-TGGENVYPEE 451
|
330
....*....|....*...
gi 528467778 572 IENIYIRSDPVAQVFVHG 589
Cdd:PLN02860 452 VEAVLSQHPGVASVVVVG 469
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
243-606 |
4.98e-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: 84.81 E-value: 4.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 243 DIISLKELEAigKANHKTPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSN--CSAFIkitevhCMLNQTDIHISYLP 320
Cdd:COG1021 162 EFTSLDALLA--APADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSvrASAEI------CGLDADTVYLAALP 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 321 LAHMFERVVEGVL--LCHGAKIgyfqgdirLLMDDLKnlkP-TIFP-----------VVPRLLNRMFDkifgqantplkr 386
Cdd:COG1021 234 AAHNFPLSSPGVLgvLYAGGTV--------VLAPDPS---PdTAFPlierervtvtaLVPPLALLWLD------------ 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 387 wlldfATSRKEAELKSgvvrkdsmwdklifskvqaslggrVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTEctaG- 465
Cdd:COG1021 291 -----AAERSRYDLSS------------------------LRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---Gl 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 466 -CTMSL--PGDWTAGHVGAPL-PCNFVKLVD-----VAEmnyfaanGE-GEVCVKGPNVFQGYLKDPEQTSGAVDKAGWL 535
Cdd:COG1021 339 vNYTRLddPEEVILTTQGRPIsPDDEVRIVDedgnpVPP-------GEvGELLTRGPYTIRGYYRAPEHNARAFTPDGFY 411
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528467778 536 HTGDIGKWLPNGTLKIIDRKK-HIFKlaQGEYIAPEKIENIYIRsdpvaqvfvHGDSLQACLVGvvVPDPDF 606
Cdd:COG1021 412 RTGDLVRRTPDGYLVVEGRAKdQINR--GGEKIAAEEVENLLLA---------HPAVHDAAVVA--MPDEYL 470
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
268-606 |
6.74e-17 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 83.92 E-value: 6.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 268 DLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKItevhCMLNQTDIHISYLPLAHMFERV---VEGVLLCHGAKIGYFQ 344
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEV----CGLDQDTVYLAVLPAAHNFPLAcpgVLGTLLAGGRVVLAPD 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 345 GDIRLLMDDLKNLKPTIFPVVPRLLnrmfdkifgqantplKRWLlDFATSRKeAELKSgvvrkdsmwdklifskvqaslg 424
Cdd:cd05920 216 PSPDAAFPLIEREGVTVTALVPALV---------------SLWL-DAAASRR-ADLSS---------------------- 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 425 grVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCT-MSLPGDWTAGHVGAPL-PCNFVKLVDvAEMNYFAAN 502
Cdd:cd05920 257 --LRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTrLDDPDEVIIHTQGRPMsPDDEIRVVD-EEGNPVPPG 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 503 GEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRsdpv 582
Cdd:cd05920 334 EEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVENLLLR---- 408
|
330 340
....*....|....*....|....
gi 528467778 583 aqvfvHgDSLQACLVgVVVPDPDF 606
Cdd:cd05920 409 -----H-PAVHDAAV-VAMPDELL 425
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
121-589 |
6.86e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 84.17 E-value: 6.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGHSQsGDkYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASittiic 200
Cdd:PRK06145 28 ISYAEFHQRILQAAGMLHARGIGQ-GD-VVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAG------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 201 diadkARLILdcvsgrkhsvttivIMESFDSELTAQAQNCGIDIISLKELEAIGKANhkTPIPP----KPEDLALICFTS 276
Cdd:PRK06145 100 -----AKLLL--------------VDEEFDAIVALETPKIVIDAAAQADSRRLAQGG--LEIPPqaavAPTDLVRLMYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 277 GTTGNPKGAMLTHGNVvsncsAFIKITEVHCM-LNQTDIHISYLPLAHMFERVVEGV-LLCHGakigyfqGDIRLLmddl 354
Cdd:PRK06145 159 GTTDRPKGVMHSYGNL-----HWKSIDHVIALgLTASERLLVVGPLYHVGAFDLPGIaVLWVG-------GTLRIH---- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 355 KNLKP-TIFPVVPRllnrmfDKIFGQantplkrWLLDFATSRkeaelksgvVRKDSMWDKLIFSKVQASLGGrvrlmitG 433
Cdd:PRK06145 223 REFDPeAVLAAIER------HRLTCA-------WMAPVMLSR---------VLTVPDRDRFDLDSLAWCIGG-------G 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 434 AAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTA--GHVGAPLPCNFVKLVDvAEMNYFAANGEGEVCVKG 511
Cdd:PRK06145 274 EKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREIEkiGSTGRALAHVEIRIAD-GAGRWLPPNMKGEICMRG 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528467778 512 PNVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVFVHG 589
Cdd:PRK06145 353 PKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERVIYELPEVAEAAVIG 428
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
107-694 |
8.40e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 84.33 E-value: 8.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 107 PCLGSRKAGQ-PYKWLSYKEVADRAEFAGSALLHRGHSQsgDKYIGIFAQNRPEWTISELACYTYSLVAVPL---YDTLG 182
Cdd:PRK12582 66 PWLAQREPGHgQWRKVTYGEAKRAVDALAQALLDLGLDP--GRPVMILSGNSIEHALMTLAAMQAGVPAAPVspaYSLMS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 183 TE--AISYVIDKASITTIICDIAD---KARLILDCVSgrkhsVTTIVIMESFDseltaqaqncGIDIISLKELEAigkan 257
Cdd:PRK12582 144 HDhaKLKHLFDLVKPRVVFAQSGApfaRALAALDLLD-----VTVVHVTGPGE----------GIASIAFADLAA----- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 258 hkTPIPPK---------PEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEvhcmLNQTD---IHISYLPLAHMF 325
Cdd:PRK12582 204 --TPPTAAvaaaiaaitPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRP----REPDPpppVSLDWMPWNHTM 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 326 ervvegvllchGAKIGyFQGDIR----LLMDDLKNLkPTIFPVVPRLLNRMFDKIFGqaNTPLKRWLLDFATSRKEAELK 401
Cdd:PRK12582 278 -----------GGNAN-FNGLLWgggtLYIDDGKPL-PGMFEETIRNLREISPTVYG--NVPAGYAMLAEAMEKDDALRR 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 402 SgvvrkdsmwdklIFSkvqaslggRVRLMITGAAPVSPTVLTFLRA----ALGCQ--FYEGYGQTEcTAGCTMSLpgDWT 475
Cdd:PRK12582 343 S------------FFK--------NLRLMAYGGATLSDDLYERMQAlavrTTGHRipFYTGYGATE-TAPTTTGT--HWD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 476 A---GHVGAPLPCNFVKLVDVAEmNYfaangegEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWL----PNGT 548
Cdd:PRK12582 400 TervGLIGLPLPGVELKLAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdpddPEKG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 549 LKIIDRKKHIFKLAQGEYIAPEKieniyIRSDPVAQV--FVHgDSLQACL----VGVVV-PDPDFLPGWAKNRGieGSFN 621
Cdd:PRK12582 472 LIFDGRVAEDFKLSTGTWVSVGT-----LRPDAVAACspVIH-DAVVAGQdrafIGLLAwPNPAACRQLAGDPD--AAPE 543
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528467778 622 DLCKSKEVKNAILEDMIQLGKEAGLKSfEQVRDIALHLEMFSVQNGLLTPtlKA---KRTELKSRfREQIDQLYAK 694
Cdd:PRK12582 544 DVVKHPAVLAILREGLSAHNAEAGGSS-SRIARALLMTEPPSIDAGEITD--KGyinQRAVLERR-AALVERLYAE 615
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
260-627 |
1.08e-16 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 83.57 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 260 TPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITevhCMLNQTDIHISYLPLAHMFErvvegvlLCHGAK 339
Cdd:cd05959 156 KPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNV---LGIREDDVCFSAAKLFFAYG-------LGNSLT 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 340 IGYFQGDIRLLM----------DDLKNLKPTIFPVVPRLLNRMFdkifgqantplkrwlldfatsrkeaelksgvvrKDS 409
Cdd:cd05959 226 FPLSVGATTVLMperptpaavfKRIRRYRPTVFFGVPTLYAAML---------------------------------AAP 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 410 MWDKLIFSkvqaslggRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVK 489
Cdd:cd05959 273 NLPSRDLS--------SLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVE 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 490 LVDVAEmNYFAANGEGEVCVKGPNVFQGYLKDPEQTSgAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAP 569
Cdd:cd05959 345 LRDEDG-GDVADGEPGELYVRGPSSATMYWNNRDKTR-DTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSP 421
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528467778 570 EKIENIYIRSDPVAQVFV----HGDSLQAcLVGVVVPDPDFLPGWAKNRGIEgsfnDLCKSK 627
Cdd:cd05959 422 FEVESALVQHPAVLEAAVvgveDEDGLTK-PKAFVVLRPGYEDSEALEEELK----EFVKDR 478
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
266-603 |
1.36e-16 |
|
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: 82.74 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 266 PEDLALICFTSGTTGNPKGAMLTHGNVVsncsAFIKITEVHCMLNQTDIHISYLPLAHMFErVVE--GVLLcHGAKIgyf 343
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHANVL----ALFAATQRWFGFNEDDVWTLFHSYAFDFS-VWEiwGALL-HGGRL--- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 344 qgdirLLMDDLKNLKPTIFPvvpRLLNRMFDKIFGQANTPLKRwLLDFATSRKEAELksgvvrkdsmwdklifskvqasl 423
Cdd:cd17643 163 -----VVVPYEVARSPEDFA---RLLRDEGVTVLNQTPSAFYQ-LVEAADRDGRDPL----------------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 424 ggRVRLMITGAAPVSPTVLTFLRAALGC---QFYEGYGQTECTAGCTM------SLPGDwTAGHVGAPLPCNFVKLVDvA 494
Cdd:cd17643 211 --ALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFrpldaaDLPAA-AASPIGRPLPGLRVYVLD-A 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 495 EMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSG-----AVDKAG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 567
Cdd:cd17643 287 DGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanPFGGPGsrMYRTGDLARRLPDGELEYLGRADEQVKI-RGFRI 365
|
330 340 350
....*....|....*....|....*....|....*....
gi 528467778 568 APEKIENIYIRSDPVAQVFV---HGDSLQACLVGVVVPD 603
Cdd:cd17643 366 ELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVAD 404
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
121-605 |
1.26e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 80.47 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:PRK06178 59 ITYAELDELSDRFAALLRQRG-VGAGDR-VAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 201 --DIADKARLILDCVSGRKHSVT----------TIVIMESFDSELTAQAqncgiDIISLkeLEAIGKANHKTPIP-PKPE 267
Cdd:PRK06178 137 ldQLAPVVEQVRAETSLRHVIVTsladvlpaepTLPLPDSLRAPRLAAA-----GAIDL--LPALRACTAPVPLPpPALD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 268 DLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEVhcmLNQTDIHISYLPlahMFervvegvllchgakigYFQGDi 347
Cdd:PRK06178 210 ALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVV---GGEDSVFLSFLP---EF----------------WIAGE- 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 348 rllmdDLKNLKPTIF--PVVprLLNRMFDKIFGQA-------NTPLkrwLLDFAT------SRKEAELKS-GVVRKDSMW 411
Cdd:PRK06178 267 -----NFGLLFPLFSgaTLV--LLARWDAVAFMAAveryrvtRTVM---LVDNAVelmdhpRFAEYDLSSlRQVRVVSFV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 412 DKLifskvqaslggrvrlmitgaapvSPTVLTFLRAALGCQFYEG-YGQTEC------TAGCT---MSLPGDWTagHVGA 481
Cdd:PRK06178 337 KKL-----------------------NPDYRQRWRALTGSVLAEAaWGMTEThtcdtfTAGFQdddFDLLSQPV--FVGL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 482 PLPCNFVKLVDVAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKL 561
Cdd:PRK06178 392 PVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 528467778 562 aQGEYIAPEKIENIYIRsdpvaqvfvHGDSLQACLVGvvVPDPD 605
Cdd:PRK06178 471 -NGMSVFPSEVEALLGQ---------HPAVLGSAVVG--RPDPD 502
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
246-602 |
1.42e-15 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 80.33 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 246 SLKELEAIGKANHKTPIPPKPEDLALICFTSGTTGNPKGAMLTHGnvvsncsafikitevhcmlnqtdihisylplahMF 325
Cdd:PRK09274 153 TLATLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHG---------------------------------MF 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 326 ERVVEgvLLCHGAKIGyfQGDIrllmdDLknlkPTiFPVV----PRLLNRMF--------------DKIFGQ-------- 379
Cdd:PRK09274 200 EAQIE--ALREDYGIE--PGEI-----DL----PT-FPLFalfgPALGMTSVipdmdptrpatvdpAKLFAAierygvtn 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 380 --ANTPLKRWLLDFATSRkeaelksgvvrkdsmwdklifskvQASLGGrVRLMITGAAPVSPTVLTFLRAAL--GCQFYE 455
Cdd:PRK09274 266 lfGSPALLERLGRYGEAN------------------------GIKLPS-LRRVISAGAPVPIAVIERFRAMLppDAEILT 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 456 GYGQTECTAGCTMS----LPGDWT-----AGH-VGAPLPCNFVKLVDV--------AEMNYFAANGEGEVCVKGPNVFQG 517
Cdd:PRK09274 321 PYGATEALPISSIEsreiLFATRAatdngAGIcVGRPVDGVEVRIIAIsdapipewDDALRLATGEIGEIVVAGPMVTRS 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 518 YLKDPEQTSGA--VDKAG--WLHTGDIGkWL-PNGTLKIIDRKKHIFKLAQGEYIapekieniyirSDPVAQVF-VHGDS 591
Cdd:PRK09274 401 YYNRPEATRLAkiPDGQGdvWHRMGDLG-YLdAQGRLWFCGRKAHRVETAGGTLY-----------TIPCERIFnTHPGV 468
|
410
....*....|.
gi 528467778 592 LQACLVGVVVP 602
Cdd:PRK09274 469 KRSALVGVGVP 479
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
121-603 |
1.96e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 80.77 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGhsQSGDKYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARG--VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLT 2106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 201 DIADKARLILdcvsgrkhsvTTIVIMESFDSELtaqaqncgidiislkELEaiGKANHKTPIPPKPEDLALICFTSGTTG 280
Cdd:PRK12316 2107 QRHLLERLPL----------PAGVARLPLDRDA---------------EWA--DYPDTAPAVQLAGENLAYVIYTSGSTG 2159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 281 NPKGAMLTHGNVVSNCSAFIKITEvhcmLNQTDIHISYLPLAhmFERVVEGVL--LCHGAkigyfqgdiRLLMDDLKNLK 358
Cdd:PRK12316 2160 LPKGVAVSHGALVAHCQAAGERYE----LSPADCELQFMSFS--FDGAHEQWFhpLLNGA---------RVLIRDDELWD 2224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 359 PtifpvvprllNRMFDKIFGQANTplkrwLLDFATsrkeaelksgvvrkdSMWDKLIfsKVQASLGGR--VRLMITGAAP 436
Cdd:PRK12316 2225 P----------EQLYDEMERHGVT-----ILDFPP---------------VYLQQLA--EHAERDGRPpaVRVYCFGGEA 2272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 437 VSPTVLTFLRAALGCQF-YEGYGQTEctagcTMSLPGDWTAGH----------VGAPLPCNFVKLVDvAEMNYFAANGEG 505
Cdd:PRK12316 2273 VPAASLRLAWEALRPVYlFNGYGPTE-----AVVTPLLWKCRPqdpcgaayvpIGRALGNRRAYILD-ADLNLLAPGMAG 2346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 506 EVCVKGPNVFQGYLKDPEQTS--------GAVdkAGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIY 576
Cdd:PRK12316 2347 ELYLGGEGLARGYLNRPGLTAerfvpdpfSAS--GERLYrTGDLARYRADGVVEYLGRIDHQVKI-RGFRIELGEIEARL 2423
|
490 500 510
....*....|....*....|....*....|
gi 528467778 577 IRSDPVAQVFV---HGDSLQAcLVGVVVPD 603
Cdd:PRK12316 2424 QAHPAVREAVVvaqDGASGKQ-LVAYVVPD 2452
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
121-605 |
2.16e-15 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 79.31 E-value: 2.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:cd17651 21 LTYAELDRRANRLAHRLRARG-VGPGDL-VALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 201 DIADKARLildcvSGRKHSVTtivimesfdseLTAQAQncgidiislkeLEAIGKANHktPIPPKPEDLALICFTSGTTG 280
Cdd:cd17651 99 HPALAGEL-----AVELVAVT-----------LLDQPG-----------AAAGADAEP--DPALDADDLAYVIYTSGSTG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 281 NPKGAMLTHGNVVSNCSAFIKITEVHcmlnQTDIHISYLPLAhmFERVVEGVL--LCHGAKIGYFQGDIRllMDdlknlk 358
Cdd:cd17651 150 RPKGVVMPHRSLANLVAWQARASSLG----PGARTLQFAGLG--FDVSVQEIFstLCAGATLVLPPEEVR--TD------ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 359 ptiFPVVPRLLNRM-FDKIFgqANTPLKRWLLdfatsrkEAELKSGVVrkdsmwdklifskvqaslGGRVRLMITG--AA 435
Cdd:cd17651 216 ---PPALAAWLDEQrISRVF--LPTVALRALA-------EHGRPLGVR------------------LAALRYLLTGgeQL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 436 PVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGD---WTA-GHVGAPLPCNFVKLVDvaemnyfaANGE------- 504
Cdd:cd17651 266 VLTEDLREFCAGLPGLRLHNHYGPTETHVVTALSLPGDpaaWPApPPIGRPIDNTRVYVLD--------AALRpvppgvp 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 505 GEVCVKGPNVFQGYLKDPEQT------SGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIR 578
Cdd:cd17651 338 GELYIGGAGLARGYLNRPELTaerfvpDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKI-RGFRIELGEIEAALAR 416
|
490 500 510
....*....|....*....|....*....|
gi 528467778 579 SDPVAQ--VFVHGD-SLQACLVGVVVPDPD 605
Cdd:cd17651 417 HPGVREavVLAREDrPGEKRLVAYVVGDPE 446
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
173-604 |
3.78e-15 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 78.57 E-value: 3.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 173 VAVPLYDTLGTEAISYVIDKASITTIICD-----IADKARLILDcvsgrkHSVTTIVIMESFDSELTaqaqncgiDIISL 247
Cdd:PRK08008 88 IMVPINARLLREESAWILQNSQASLLVTSaqfypMYRQIQQEDA------TPLRHICLTRVALPADD--------GVSSF 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 248 KELEAIGKANHKTPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVsncsaFIKI-TEVHCMLNQTDIHISYLPLAHM-F 325
Cdd:PRK08008 154 TQLKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLR-----FAGYySAWQCALRDDDVYLTVMPAFHIdC 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 326 ErvvegvllCHGAkigyfqgdirllMddlknlkpTIFPVVPRLLnrmfdkifgqantplkrwLLDFATSRKeaelksgvv 405
Cdd:PRK08008 229 Q--------CTAA------------M--------AAFSAGATFV------------------LLEKYSARA--------- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 406 rkdsMWDKLifSKVQASLGGRVRLMITG--AAPVSPT--------VLTFLRAA----------LGCQFYEGYGQTECTAG 465
Cdd:PRK08008 254 ----FWGQV--CKYRATITECIPMMIRTlmVQPPSANdrqhclreVMFYLNLSdqekdafeerFGVRLLTSYGMTETIVG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 466 CTMSLPGD---WTAghVGAPLPCNFVKLVDvaEMNYFAANGE-GEVCVKG---PNVFQGYLKDPEQTSGAVDKAGWLHTG 538
Cdd:PRK08008 328 IIGDRPGDkrrWPS--IGRPGFCYEAEIRD--DHNRPLPAGEiGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTG 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528467778 539 DIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIyIRSDPVAQvfvhgdslQACLVGvvVPDP 604
Cdd:PRK08008 404 DTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVELENI-IATHPKIQ--------DIVVVG--IKDS 457
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
121-603 |
4.61e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 79.82 E-value: 4.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALlhRGHSQSGDKYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASIttiic 200
Cdd:PRK12467 538 LSYAELNRQANRLAHVL--IAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGV----- 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 201 diadkaRLILDcvsgrkhsvttivimesfDSELTAQAQNC-GIDIISLKELEAI--GKANHKTPIPPKPEDLALICFTSG 277
Cdd:PRK12467 611 ------RLLLT------------------QSHLLAQLPVPaGLRSLCLDEPADLlcGYSGHNPEVALDPDNLAYVIYTSG 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 278 TTGNPKGAMLTHGNVVSncsaFIKITEVHCMLNQTDIHISYLPLAHMFERVVEGVLLCHGAKIgyfqgdirLLMDDLKNL 357
Cdd:PRK12467 667 STGQPKGVAISHGALAN----YVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATL--------HLLPPDCAR 734
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 358 KPTIFpvvprllnrmFDKIFGQANTplkrwLLDFATsrkeaelksgvvrkdSMWDKLIFSKVQASLGGRVRLMITGAA-P 436
Cdd:PRK12467 735 DAEAF----------AALMADQGVT-----VLKIVP---------------SHLQALLQASRVALPRPQRALVCGGEAlQ 784
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 437 VSPTVLTFlRAALGCQFYEGYGQTECTAGCTM----SLPGDWTAGHVGAPLPCNFVKLVDvAEMNYFAANGEGEVCVKGP 512
Cdd:PRK12467 785 VDLLARVR-ALGPGARLINHYGPTETTVGVSTyelsDEERDFGNVPIGQPLANLGLYILD-HYLNPVPVGVVGELYIGGA 862
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 513 NVFQGYLKDPEQTS-------GAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDPVAQV 585
Cdd:PRK12467 863 GLARGYHRRPALTAerfvpdpFGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKI-RGFRIELGEIEARLLAQPGVREA 941
|
490 500
....*....|....*....|....
gi 528467778 586 FV------HGDSLQACLVGVVVPD 603
Cdd:PRK12467 942 VVlaqpgdAGLQLVAYLVPAAVAD 965
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
439-606 |
5.57e-15 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 77.99 E-value: 5.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 439 PTVLTFLRAALGCQFYEGYGQTEctAGCTM------SLPGdwtaghVGAPLPCNFVKLVDvaemnyfaangeGEVCVKGP 512
Cdd:PRK09029 253 PVELTEQAEQQGIRCWCGYGLTE--MASTVcakradGLAG------VGSPLPGREVKLVD------------GEIWLRGA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 513 NVFQGYLKDPEQTSgAVDKAGWLHTGDIGKWLpNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVFVhgdsl 592
Cdd:PRK09029 313 SLALGYWRQGQLVP-LVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQVFV----- 384
|
170
....*....|....
gi 528467778 593 qaclvgVVVPDPDF 606
Cdd:PRK09029 385 ------VPVADAEF 392
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
115-604 |
6.30e-15 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 78.28 E-value: 6.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 115 GQPYKWlSYKEVADRAEFAGSALLHRGHSQSGDKYIGIFAQnRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKAS 194
Cdd:cd05928 37 GDEVKW-SFRELGSLSRKAANVLSGACGLQRGDRVAVILPR-VPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 195 ITTIICDiaDKARLILDCVSGRKHSVTT--IVIMESFDSELtaqaqncgidiiSLKELEAIGKANHkTPIPPKPEDLALI 272
Cdd:cd05928 115 AKCIVTS--DELAPEVDSVASECPSLKTklLVSEKSRDGWL------------NFKELLNEASTEH-HCVETGSQEPMAI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 273 CFTSGTTGNPKGAMLTHGN----VVSNCSAFIKITEVHCMLNQTDIHISYLPLAHMFERVVEG--VLLCHGAKIgyfqgD 346
Cdd:cd05928 180 YFTSGTTGSPKMAEHSHSSlglgLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGacVFVHHLPRF-----D 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 347 IRLLMDDLKNLKPTIFPVVPRLLnRMFdkifgqantplkrwlldfatsrkeaelksgvVRKDsmwdkliFSKVQASlggR 426
Cdd:cd05928 255 PLVILKTLSSYPITTFCGAPTVY-RML-------------------------------VQQD-------LSSYKFP---S 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 427 VRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDVaEMNYFAANGEGE 506
Cdd:cd05928 293 LQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDD-NGNVLPPGTEGD 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 507 VCVK-GPN----VFQGYLKDPEQTSgAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDP 581
Cdd:cd05928 372 IGIRvKPIrpfgLFSGYVDNPEKTA-ATIRGDFYLTGDRGIMDEDGYFWFMGRADDVI-NSSGYRIGPFEVESALIEHPA 449
|
490 500
....*....|....*....|...
gi 528467778 582 VAQVFVhgdslqaclvgVVVPDP 604
Cdd:cd05928 450 VVESAV-----------VSSPDP 461
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
267-575 |
1.05e-14 |
|
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: 76.15 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 267 EDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKitevhCMLNQT--DIHISYLPLAHMFERVVEGVLLCHGAKIGYFQ 344
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQK-----EGLNWVvgDVTYLPLPATHIGGLWWILTCLIHGGLCVTGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 345 GDIRL--LMDDLKNLKPTIFPVVPRLLNRMfdkifgqantplkrwLLDFATSRKEAElksgvvrkdsmwdklifskvqas 422
Cdd:cd17635 76 ENTTYksLFKILTTNAVTTTCLVPTLLSKL---------------VSELKSANATVP----------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 423 lggRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWT-AGHVGAPLPCNFVKLVDVAEMNYFAA 501
Cdd:cd17635 118 ---SLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLPTDDDSIeINAVGRPYPGVDVYLAATDGIAGPSA 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528467778 502 nGEGEVCVKGPNVFQGYLKDPEQTSgAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 575
Cdd:cd17635 195 -SFGTIWIKSPANMLGYWNNPERTA-EVLIDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERI 265
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
121-589 |
1.06e-14 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 77.52 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAefagSALLHRGHSQ---SGDKYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITT 197
Cdd:PRK05620 39 TTFAAIGARA----AALAHALHDElgiTGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 198 IICDIADK---ARLILDCvsgrkHSVTTIVIMESFDSELTAQAQNCGIDIISLkELEAIGKANHkTPIPPKPEDL-ALIC 273
Cdd:PRK05620 115 IVADPRLAeqlGEILKEC-----PCVRAVVFIGPSDADSAAAHMPEGIKVYSY-EALLDGRSTV-YDWPELDETTaAAIC 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 274 FTSGTTGNPKGAMLTHGNVVSNCSAfIKITEVHCMLNQTdihiSYL---PLAHmfervvegvLLCHGAKIGYFQGDIRLL 350
Cdd:PRK05620 188 YSTGTTGAPKGVVYSHRSLYLQSLS-LRTTDSLAVTHGE----SFLccvPIYH---------VLSWGVPLAAFMSGTPLV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 351 MDDLKNLKPTIFPVVPRLLNRmfdkifgQANtplkrwlldfatsrkeaelksGVvrkDSMWDKLIFSKVQASlGGRVRL- 429
Cdd:PRK05620 254 FPGPDLSAPTLAKIIATAMPR-------VAH---------------------GV---PTLWIQLMVHYLKNP-PERMSLq 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 430 -MITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHVGA---------PLPCNFvKLVDVAEMNYF 499
Cdd:PRK05620 302 eIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEARWayrvsqgrfPASLEY-RIVNDGQVMES 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 500 AANGEGEVCVKGPNVFQGYLKDPEQTSG---------AVDKA-------GWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQ 563
Cdd:PRK05620 381 TDRNEGEIQVRGNWVTASYYHSPTEEGGgaastfrgeDVEDAndrftadGWLRTGDVGSVTRDGFLTIHDRARDVIR-SG 459
|
490 500
....*....|....*....|....*.
gi 528467778 564 GEYIAPEKIENIYIRSDPVAQVFVHG 589
Cdd:PRK05620 460 GEWIYSAQLENYIMAAPEVVECAVIG 485
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
263-609 |
1.61e-14 |
|
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: 76.55 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 263 PPKPEDLALICFTSGTTGNPKGAMLTHGNVVSncsafikitEVHCM-----LNQTDIHISYLPLAhmFERVVEGVL--LC 335
Cdd:cd17646 134 PPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVN---------RLLWMqdeypLGPGDRVLQKTPLS--FDVSVWELFwpLV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 336 HGAKI------GYfqGDIRLLMDDLKNLKPTIFPVVPRLLnrmfdkifgqantplkRWLLDFATSRKEAELksgvvrkds 409
Cdd:cd17646 203 AGARLvvarpgGH--RDPAYLAALIREHGVTTCHFVPSML----------------RVFLAEPAAGSCASL--------- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 410 mwdklifskvqaslggrvRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCT-MSLPGDWTAGHV--GAPLPCN 486
Cdd:cd17646 256 ------------------RRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVThWPVRGPAETPSVpiGRPVPNT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 487 FVKLVDvAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAV-----DKAGWLH-TGDIGKWLPNGTLKIIDRKKHIFK 560
Cdd:cd17646 318 RLYVLD-DALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFvpdpfGPGSRMYrTGDLARWRPDGALEFLGRSDDQVK 396
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 528467778 561 LaQGEYIAPEKIENIYIRSDPVAQ--VFVHGD-SLQACLVGVVVPDPDFLPG 609
Cdd:cd17646 397 I-RGFRVEPGEIEAALAAHPAVTHavVVARAApAGAARLVGYVVPAAGAAGP 447
|
|
| 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 528467778 456 GYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLVDVA--EMnyfaANGE-GEVCVKGPNVFQGYLKDPEQTSgAVDKA 532
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDgrEV----PDGEvGEIVARGPTVMAGYWNRPEVNA-RRTRG 216
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528467778 533 GWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIyIRSDP-VAQVFVHGdslqaclvgvvVPDP 604
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSG-AENIYPAEVERC-LRQHPaVADAAVIG-----------VPDP 276
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
121-605 |
3.66e-14 |
|
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: 75.43 E-value: 3.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGHSQsgDKYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVGP--ESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 201 DiadkarlildcvsgrkhsvttivimesfdseltaqaqncgidiislkeleaigkanhktpippkPEDLALICFTSGTTG 280
Cdd:cd12115 103 D----------------------------------------------------------------PDDLAYVIYTSGSTG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 281 NPKGAMLTHGNVVsncsAFIKITEVHC-------MLNQTDIHISyLPLAHMFervvegVLLCHGAKIgyfqgdirllmdd 353
Cdd:cd12115 119 RPKGVAIEHRNAA----AFLQWAAAAFsaeelagVLASTSICFD-LSVFELF------GPLATGGKV------------- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 354 lknlkptifpvvpRLLNRMFDkifgqantplkrwLLDFAtSRKEAELKSGVvrkDSMWDKLIfskVQASLGGRVRLMITG 433
Cdd:cd12115 175 -------------VLADNVLA-------------LPDLP-AAAEVTLINTV---PSAAAELL---RHDALPASVRVVNLA 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 434 AAPVSPTVLTFLRAAL-GCQFYEGYGQTECTAGCTMSL--PGDWTAGHVGAPLPCNFVKLVDvAEMNYFAANGEGEVCVK 510
Cdd:cd12115 222 GEPLPRDLVQRLYARLqVERVVNLYGPSEDTTYSTVAPvpPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVPGELYIG 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 511 GPNVFQGYLKDPEQTS------GAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDPVAQ 584
Cdd:cd12115 301 GAGVARGYLGRPGLTAerflpdPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAALRSIPGVRE 379
|
490 500
....*....|....*....|....
gi 528467778 585 --VFVHGDSL-QACLVGVVVPDPD 605
Cdd:cd12115 380 avVVAIGDAAgERRLVAYIVAEPG 403
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
266-611 |
4.67e-14 |
|
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: 75.10 E-value: 4.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 266 PEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEVHcmlnQTDIHISYLPLAhmFERVVEGVL--LCHGAkigyf 343
Cdd:cd17649 93 PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLT----PGDRELQFASFN--FDGAHEQLLppLICGA----- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 344 qgdiRLLMDDLKNLKPtifpvvPRLLNRMFDKifGQANtplkrwLLDFATSrkeaelksgvvrkdsMWDKLI--FSKVQA 421
Cdd:cd17649 162 ----CVVLRPDELWAS------ADELAEMVRE--LGVT------VLDLPPA---------------YLQQLAeeADRTGD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 422 SLGGRVRLMITGAAPVSPTvltFLRAALGCQ--FYEGYGQTECTAGCTMSL--PGDWTAGH---VGAPLPCNFVKLVDvA 494
Cdd:cd17649 209 GRPPSLRLYIFGGEALSPE---LLRRWLKAPvrLFNAYGPTEATVTPLVWKceAGAARAGAsmpIGRPLGGRSAYILD-A 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 495 EMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSG-------AVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 567
Cdd:cd17649 285 DLNPVPVGVTGELYIGGEGLARGYLGRPELTAErfvpdpfGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKI-RGFRI 363
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 528467778 568 APEKIENIYIRSDPVAQVFV------HGDSLQACLVGVvvpDPDFLPGWA 611
Cdd:cd17649 364 ELGEIEAALLEHPGVREAAVvaldgaGGKQLVAYVVLR---AAAAQPELR 410
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
266-605 |
6.76e-14 |
|
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: 74.21 E-value: 6.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 266 PEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIK---ITEVHCMLNQT----DIHISYLPLAhmfervvegvlLCHGA 338
Cdd:cd17652 92 PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAafdVGPGSRVLQFAspsfDASVWELLMA-----------LLAGA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 339 kigyfqgdiRLLMDDLKNLKPtifpvvprllnrmfdkifGQantPLKRWLLDFATSrkEAELKSGVVRKDSmwdklifsk 418
Cdd:cd17652 161 ---------TLVLAPAEELLP------------------GE---PLADLLREHRIT--HVTLPPAALAALP--------- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 419 vQASLGGRVRLMITGAAPVSPTVLtflRAALGCQFYEGYGQTECTAGCTMSLP-GDWTAGHVGAPLPCNFVKLVDvAEMN 497
Cdd:cd17652 200 -PDDLPDLRTLVVAGEACPAELVD---RWAPGRRMINAYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYVLD-ARLR 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 498 YFAANGEGEVCVKGPNVFQGYLKDPEQTS--------GAvdKAGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIA 568
Cdd:cd17652 275 PVPPGVPGELYIAGAGLARGYLNRPGLTAerfvadpfGA--PGSRMYrTGDLARWRADGQLEFLGRADDQVKI-RGFRIE 351
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 528467778 569 PEKIENIYIRSDPVAQ--VFVHGDSL-QACLVGVVVPDPD 605
Cdd:cd17652 352 LGEVEAALTEHPGVAEavVVVRDDRPgDKRLVAYVVPAPG 391
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
121-573 |
7.70e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 75.59 E-value: 7.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALlhRGHSQSGDKYIGIFAQNrPEWTISELACYTYSLVAVPLYDTLGTEAISyvidKASITTIIC 200
Cdd:PRK05691 41 LSYRDLDLRARTIAAAL--QARASFGDRAVLLFPSG-PDYVAAFFGCLYAGVIAVPAYPPESARRHH----QERLLSIIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 201 DIadKARLILdcvsgrkhsvTTIVIMESFdSELTAQAQNCGIDIISLKELEAIGKANHKTPIPPkPEDLALICFTSGTTG 280
Cdd:PRK05691 114 DA--EPRLLL----------TVADLRDSL-LQMEELAAANAPELLCVDTLDPALAEAWQEPALQ-PDDIAFLQYTSGSTA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 281 NPKGAMLTHGNVVSN-----CSAFIKitevhcmLNQTDIHISYLPLAHmfervvegvllchgakigyfqgDIRLLmddlK 355
Cdd:PRK05691 180 LPKGVQVSHGNLVANeqlirHGFGID-------LNPDDVIVSWLPLYH----------------------DMGLI----G 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 356 NLKPTIFPVVPRLLnrMFDKIFgqANTPLkRWLLdfATSRKEAELKSGvvrKDSMWdKLIFSKV-QASLGG----RVRLM 430
Cdd:PRK05691 227 GLLQPIFSGVPCVL--MSPAYF--LERPL-RWLE--AISEYGGTISGG---PDFAY-RLCSERVsESALERldlsRWRVA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 431 ITGAAPVSPTVL-TFLRAALGC-----QFYEGYGQTECTAGCTMSLPG--------DWTA----------GHV----GAP 482
Cdd:PRK05691 296 YSGSEPIRQDSLeRFAEKFAACgfdpdSFFASYGLAEATLFVSGGRRGqgipalelDAEAlarnraepgtGSVlmscGRS 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 483 LPCNFVKLVDVAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGA-VDKAG--WLHTGDIGkWLPNGTLKIIDRKKHIF 559
Cdd:PRK05691 376 QPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfVEHDGrtWLRTGDLG-FLRDGELFVTGRLKDML 454
|
490
....*....|....
gi 528467778 560 kLAQGEYIAPEKIE 573
Cdd:PRK05691 455 -IVRGHNLYPQDIE 467
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
409-605 |
1.26e-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: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 409 SMWDKLIFSKVqASLGGRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSlPGD-WTAGHVGAPLPCNF 487
Cdd:cd05974 185 TVWRMLIQQDL-ASFDVKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNS-PGQpVKAGSMGRPLPGYR 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 488 VKLVDVAEmnyfAANGEGEVCV-----KGPNVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKlA 562
Cdd:cd05974 263 VALLDPDG----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-S 336
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 528467778 563 QGEYIAPEKIENIYIRSDPVAQvfvhgdslqaclvGVVVPDPD 605
Cdd:cd05974 337 SDYRISPFELESVLIEHPAVAE-------------AAVVPSPD 366
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
265-602 |
1.31e-13 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 73.62 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 265 KPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIK----ITEVHCMLNQTdihISylplahmFERVVEG--VLLCHGA 338
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKeygiTSSDRVLQFAS---IA-------FDVAAEEiyVTLLSGA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 339 KIgyfqgdirllmddlkNLKPtifpvvprllNRMFDKI--FGQANTPLKRWLLDFATSrkeaelksgvvrkdsMWDKLIF 416
Cdd:cd17644 174 TL---------------VLRP----------EEMRSSLedFVQYIQQWQLTVLSLPPA---------------YWHLLVL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 417 SKVQASLGG--RVRLMITGAAPVSPTVLTFLRAALG--CQFYEGYGQTECTAGCTMSLPGDWTAGH-----VGAPLPC-- 485
Cdd:cd17644 214 ELLLSTIDLpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIANtq 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 486 -----NFVKLVDVAEMnyfaangeGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLH--------TGDIGKWLPNGTLKII 552
Cdd:cd17644 294 vyildENLQPVPVGVP--------GELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYL 365
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 528467778 553 DRKKHIFKLaQGEYIAPEKIENIYIRSDPVAQ--VFVHGDSL-QACLVGVVVP 602
Cdd:cd17644 366 GRIDNQVKI-RGFRIELGEIEAVLSQHNDVKTavVIVREDQPgNKRLVAYIVP 417
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
266-577 |
1.57e-13 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 73.70 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 266 PEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEVhcmlNQTDIHISYLPLAHMFervveGVLLChgakiGYFQg 345
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSP----KEDDVMMSFLPPFHAY-----GFNSC-----TLFP- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 346 dirLLMDdlknlKPTIF---PVVPRLLNRMFDK----IFGqaNTPLkrwLLDF---ATSRKEAELKS-------GVVRKD 408
Cdd:PRK06334 247 ---LLSG-----VPVVFaynPLYPKKIVEMIDEakvtFLG--STPV---FFDYilkTAKKQESCLPSlrfvvigGDAFKD 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 409 SMWDKlifskvqaslggrvrlmitgaapvspTVLTFLRAALgcqfYEGYGQTECTAGCTMSL---PGDWTAghVGAPLPC 485
Cdd:PRK06334 314 SLYQE--------------------------ALKTFPHIQL----RQGYGTTECSPVITINTvnsPKHESC--VGMPIRG 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 486 NFVKLVDvAEMNYFAANGE-GEVCVKGPNVFQGYL-KDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAq 563
Cdd:PRK06334 362 MDVLIVS-EETKVPVSSGEtGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG- 439
|
330
....*....|....
gi 528467778 564 GEYIAPEKIENIYI 577
Cdd:PRK06334 440 AEMVSLEALESILM 453
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
120-587 |
2.27e-13 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 73.25 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 120 WLSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTII 199
Cdd:PRK06155 46 RWTYAEAARAAAAAAHALAAAG-VKRGDR-VALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 200 CDIADKARLilDCVSGRKHSVTTIVIMESFDSELTAQaqncGIDIISLKELEAIGkanhkTPIPPKPEDLALICFTSGTT 279
Cdd:PRK06155 124 VEAALLAAL--EAADPGDLPLPAVWLLDAPASVSVPA----GWSTAPLPPLDAPA-----PAAAVQPGDTAAILYTSGTT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 280 GNPKGAMLTHGNVV---SNCSAFIKITEvhcmlnqTDIHISYLPLAH------MFERVVEGVLLCHGAKI---GYFqgdi 347
Cdd:PRK06155 193 GPSKGVCCPHAQFYwwgRNSAEDLEIGA-------DDVLYTTLPLFHtnalnaFFQALLAGATYVLEPRFsasGFW---- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 348 rllmDDLKNLKPTIFpvvpRLLNRMFDKIFGQANTPLKRwlldfatsrkeaelksgvvrkdsmwdklifskvqaslGGRV 427
Cdd:PRK06155 262 ----PAVRRHGATVT----YLLGAMVSILLSQPARESDR-------------------------------------AHRV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 428 RLMITGAAPvsPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDwTAGHVGAPLPCNFVKLVDvaEMNYFAANGE-GE 506
Cdd:PRK06155 297 RVALGPGVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSMGRLAPGFEARVVD--EHDQELPDGEpGE 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 507 VCVKG--PNVF-QGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIyIRSDP-V 582
Cdd:PRK06155 372 LLLRAdePFAFaTGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIKDAIR-RRGENISSFEVEQV-LLSHPaV 448
|
....*
gi 528467778 583 AQVFV 587
Cdd:PRK06155 449 AAAAV 453
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
125-608 |
4.25e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 72.41 E-value: 4.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 125 EVADRA-EFAGSALLHRGHSQSGDK---------------YIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISY 188
Cdd:PRK07867 16 EDDDRGlYFEDSFTSWREHIRGSAAraaalrarldptrppHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALAR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 189 VIDKASITTIICDiaDKARLILDCVSGrkhSVTTIVIMESFDSELTAQAQNCGIDiislkeleaigkanhktPIPPKPED 268
Cdd:PRK07867 96 DIAHADCQLVLTE--SAHAELLDGLDP---GVRVINVDSPAWADELAAHRDAEPP-----------------FRVADPDD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 269 LALICFTSGTTGNPKGAMLTHGNVVSncsAFIKITEvHCMLNQTDIHISYLPLAHMfERVVEG--VLLCHGAKIGyfqgd 346
Cdd:PRK07867 154 LFMLIFTSGTSGDPKAVRCTHRKVAS---AGVMLAQ-RFGLGPDDVCYVSMPLFHS-NAVMAGwaVALAAGASIA----- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 347 IRL------LMDDLKNLKPTIFPVVPRLLNRMF--DKIFGQANTPLKrwlldfatsrkeaelksgvvrkdsmwdklifsk 418
Cdd:PRK07867 224 LRRkfsasgFLPDVRRYGATYANYVGKPLSYVLatPERPDDADNPLR--------------------------------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 419 vqaslggrvrlMITGAAPVSPTVLTFlRAALGCQFYEGYGQTE----------CTAGCTMSLPGDWTAGHVGAPLPCNFV 488
Cdd:PRK07867 271 -----------IVYGNEGAPGDIARF-ARRFGCVVVDGFGSTEggvaitrtpdTPPGALGPLPPGVAIVDPDTGTECPPA 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 489 KLVDVAEMNYFAANGEgEVCVKGPNVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIA 568
Cdd:PRK07867 339 EDADGRLLNADEAIGE-LVNTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLG 415
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 528467778 569 PEKIENIYIRSDPVAQVFVH-------GDSLQACLVGvvVPDPDFLP 608
Cdd:PRK07867 416 TAPIERILLRYPDATEVAVYavpdpvvGDQVMAALVL--APGAKFDP 460
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
420-604 |
5.85e-13 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 71.97 E-value: 5.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 420 QASLGGRVRLMITGAAPvsPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGD-WTAghvgapLPCN------------ 486
Cdd:PLN03102 296 LSPRSGPVHVLTGGSPP--PAALVKKVQRLGFQVMHAYGLTEATGPVLFCEWQDeWNR------LPENqqmelkarqgvs 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 487 FVKLVDVAEMN-----YFAANGE--GEVCVKGPNVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIF 559
Cdd:PLN03102 368 ILGLADVDVKNketqeSVPRDGKtmGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII 446
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 528467778 560 kLAQGEYIAPEKIENIyirsdpvaqVFVHGDSLQACLVGvvVPDP 604
Cdd:PLN03102 447 -ISGGENISSVEVENV---------LYKYPKVLETAVVA--MPHP 479
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
122-610 |
6.72e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 71.52 E-value: 6.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 122 SYKEVADRAEFAGSALLHRGhSQSGDkyigifaqnrpewTISELACYTYSLV----AVPL----YDTLGT----EAISYV 189
Cdd:PRK08162 45 TWAETYARCRRLASALARRG-IGRGD-------------TVAVLLPNIPAMVeahfGVPMagavLNTLNTrldaASIAFM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 190 IDKASITTIICD--IADKARLILDCVSGRKhsvttIVIMESFDSELTaqaqncGIDIISLKELEAI---GKANHkTPIPP 264
Cdd:PRK08162 111 LRHGEAKVLIVDteFAEVAREALALLPGPK-----PLVIDVDDPEYP------GGRFIGALDYEAFlasGDPDF-AWTLP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 265 KPE-DLALICFTSGTTGNPKGAMLTH-G---NVVSNCsafikiteVHCMLNQTDIHISYLPLAHmfervvegvllCHG-- 337
Cdd:PRK08162 179 ADEwDAIALNYTSGTTGNPKGVVYHHrGaylNALSNI--------LAWGMPKHPVYLWTLPMFH-----------CNGwc 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 338 ------AKIGYF----QGDIRLLMDDLKNLKPTIF---PVVPRLLnrmfdkifgqANTPlkrwlldfatsrkeAELKSGv 404
Cdd:PRK08162 240 fpwtvaARAGTNvclrKVDPKLIFDLIREHGVTHYcgaPIVLSAL----------INAP--------------AEWRAG- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 405 vrkdsmwdklifskvqasLGGRVRLMITGAAPvSPTVLTFLRAAlGCQFYEGYGQTEcTAG----CTM-----SLPGDWT 475
Cdd:PRK08162 295 ------------------IDHPVHAMVAGAAP-PAAVIAKMEEI-GFDLTHVYGLTE-TYGpatvCAWqpewdALPLDER 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 476 A---GHVGAPLPC-NFVKLVDVAEMNYFAANGE--GEVCVKGPNVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTL 549
Cdd:PRK08162 354 AqlkARQGVRYPLqEGVTVLDPDTMQPVPADGEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYI 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528467778 550 KIIDRKKHIFkLAQGEYIAPEKIENIYIRsdpvaqvfvHgdslQACLVGVVVPDPDflPGW 610
Cdd:PRK08162 433 KIKDRSKDII-ISGGENISSIEVEDVLYR---------H----PAVLVAAVVAKPD--PKW 477
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
121-605 |
7.36e-13 |
|
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: 71.15 E-value: 7.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGHsQSGDkYIGIFAQNRPEWTISEL------ACYtyslvaVPLYDTLGTEAISYVIDKAS 194
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGV-RPGD-LVAVTLPKGPEQVVAVLgilaagAAY------VPVDIDQPAARREAILADAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 195 ITTIICDiadkarlildcvsgrkhsvttivimesfdSELTAQAQNCGIDIISLKELEAIGKANhkTPIPPKPEDLALICF 274
Cdd:cd12114 85 ARLVLTD-----------------------------GPDAQLDVAVFDVLILDLDALAAPAPP--PPVDVAPDDLAYVIF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 275 TSGTTGNPKGAMLTHGNVVSNCSAFIK------------ITEVHCMLNQTDIhisylplahmFervveGVLlCHGAKIgy 342
Cdd:cd12114 134 TSGSTGTPKGVMISHRAALNTILDINRrfavgpddrvlaLSSLSFDLSVYDI----------F-----GAL-SAGATL-- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 343 fqgdirllmddlknlkptifpVVPRLlnrmfdkifGQANTPlKRWlldfatsrKEAELKSGVvrkdSMWDKlifskVQAS 422
Cdd:cd12114 196 ---------------------VLPDE---------ARRRDP-AHW--------AELIERHGV----TLWNS-----VPAL 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 423 LGgrvrlMITGAAPVSPTVLTFLRAAL-------------------GCQFYEGYGQTECTAGCTM----SLPGDWTAGHV 479
Cdd:cd12114 228 LE-----MLLDVLEAAQALLPSLRLVLlsgdwipldlparlralapDARLISLGGATEASIWSIYhpidEVPPDWRSIPY 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 480 GAPLPCNFVKLVDvaemnyfaANGE-------GEVCVKGPNVFQGYLKDPEQTSGA----VDKAGWLHTGDIGKWLPNGT 548
Cdd:cd12114 303 GRPLANQRYRVLD--------PRGRdcpdwvpGELWIGGRGVALGYLGDPELTAARfvthPDGERLYRTGDLGRYRPDGT 374
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 528467778 549 LKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDPVAQ--VFVHGDSLQACLVGVVVPDPD 605
Cdd:cd12114 375 LEFLGRRDGQVKV-RGYRIELGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPDND 432
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
121-604 |
1.40e-12 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 70.22 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAIsyvidkasittiic 200
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLG-VGKGDR-VFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAI-------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 201 diadKARLILdcvSGRKHSVTTIVIMESFDseltaqaqncgidiislkeleaigkanhktpippkPEDLALICFTSGTTG 280
Cdd:cd05969 65 ----RDRLEN---SEAKVLITTEELYERTD-----------------------------------PEDPTLLHYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 281 NPKGAMLTHGNVVsncsAFIKITEVHCMLNQTDIH-ISYLP--LAHMFERVVEGVLlcHGAKIGYFQG--DIRLLMDDLK 355
Cdd:cd05969 103 TPKGVLHVHDAMI----FYYFTGKYVLDLHPDDIYwCTADPgwVTGTVYGIWAPWL--NGVTNVVYEGrfDAESWYGIIE 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 356 NLKPTIFPVVPRLLnRMfdkifgqantpLKRWLLDFATSRKEAELksgvvrkdsmwdklifskvqaslggrvRLMITGAA 435
Cdd:cd05969 177 RVKVTVWYTAPTAI-RM-----------LMKEGDELARKYDLSSL---------------------------RFIHSVGE 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 436 PVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPG-DWTAGHVGAPLPCNFVKLVDvAEMNYFAANGEGEVCVKG--P 512
Cdd:cd05969 218 PLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYPCmPIKPGSMGKPLPGVKAAVVD-ENGNELPPGTKGILALKPgwP 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 513 NVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSDPVAQVFVHGdsl 592
Cdd:cd05969 297 SMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHRVGPFEVESALMEHPAVAEAGVIG--- 371
|
490
....*....|..
gi 528467778 593 qaclvgvvVPDP 604
Cdd:cd05969 372 --------KPDP 375
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
263-597 |
4.40e-12 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 69.10 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 263 PPKPE--DLALiCFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEvhcmLNQTDIHISYLPLAHMFERVVEGVLLCH-GAK 339
Cdd:PLN02479 190 PPADEwqSIAL-GYTSGTTASPKGVVLHHRGAYLMALSNALIWG----MNEGAVYLWTLPMFHCNGWCFTWTLAALcGTN 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 340 IGYFQGDIRLLMDDLKNLKPTIFPVVPRLLNRMFDKIFGQANTPLKRwlldfatsrkeaelksgvvrkdsmwdklifskv 419
Cdd:PLN02479 265 ICLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETILPLPR--------------------------------- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 420 qaslggRVRLMITGAAPvSPTVLtFLRAALGCQFYEGYGQTECTAGCTM--------SLPGDwTAGHVGAPLPCNFVKL- 490
Cdd:PLN02479 312 ------VVHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSETYGPSTVcawkpewdSLPPE-EQARLNARQGVRYIGLe 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 491 ----VDVAEMNYFAANGE--GEVCVKGPNVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQG 564
Cdd:PLN02479 383 gldvVDTKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGG 460
|
330 340 350
....*....|....*....|....*....|...
gi 528467778 565 EYIAPEKIENIyirsdpvaqVFVHGDSLQACLV 597
Cdd:PLN02479 461 ENISSLEVENV---------VYTHPAVLEASVV 484
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
245-585 |
5.62e-12 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 68.64 E-value: 5.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 245 ISLKELEAIGKANHKTPIPPKP-EDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEVHcmlNQTDIHISYLPLAH 323
Cdd:PRK05851 129 VTVHDLATAAHTNRSASLTPPDsGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLD---AATDVGCSWLPLYH 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 324 -MfervvegvllchgakigyfqGDIRLLMDDLKN----LKPT-IFPVVP-RLLNrmfdkifgqantplkrWLLDF-ATSR 395
Cdd:PRK05851 206 dM--------------------GLAFLLTAALAGaplwLAPTtAFSASPfRWLS----------------WLSDSrATLT 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 396 KEAELKSGVVRKDSmwdklifSKVQASLGGRVRLMITGAAPVSPTVLT-FLRAALGCQFYEG-----YGQTECTAGCTMS 469
Cdd:PRK05851 250 AAPNFAYNLIGKYA-------RRVSDVDLGALRVALNGGEPVDCDGFErFATAMAPFGFDAGaaapsYGLAESTCAVTVP 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 470 LPG-----------DWTAGH----VGAPLPCNFVKLVDVAEMNYFAANGEGEVCVKGPNVFQGYLKDPeqtsgAVDKAGW 534
Cdd:PRK05851 323 VPGiglrvdevttdDGSGARrhavLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQA-----PIDPDDW 397
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 528467778 535 LHTGDIGkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIyirsdpVAQV 585
Cdd:PRK05851 398 FPTGDLG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERV------AAQV 440
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
264-602 |
9.45e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 67.87 E-value: 9.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 264 PKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEVHcmlnQTDIHISYLPLAHMFervveGVLLCHGAKIGYF 343
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIR----PGEVDLATFPLFALF-----GPALGLTSVIPDM 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 344 ------QGDIRLLMDDLKNLKPTIFPVVPRLLNRmfdkifgqantpLKRWLLdfatsRKEAELKSgvvrkdsmwdklifs 417
Cdd:cd05910 153 dptrpaRADPQKLVGAIRQYGVSIVFGSPALLER------------VARYCA-----QHGITLPS--------------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 418 kvqaslggrVRLMITGAAPVSPTVLTFLRAAL--GCQFYEGYGQTECTAGCTM------SLPGDWTAGH----VGAPLPC 485
Cdd:cd05910 201 ---------LRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSIgsrellATTTAATSGGagtcVGRPIPG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 486 NFVKLVDVAEMNYFAANGE--------GEVCVKGPNVFQGYLKDPEQTSGA----VDKAGWLHTGDIGKWLPNGTLKIID 553
Cdd:cd05910 272 VRVRIIEIDDEPIAEWDDTlelprgeiGEITVTGPTVTPTYVNRPVATALAkiddNSEGFWHRMGDLGYLDDEGRLWFCG 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 528467778 554 RKKHIFKLAQGEYIapekieniyirSDPVAQVF-VHGDSLQACLVGVVVP 602
Cdd:cd05910 352 RKAHRVITTGGTLY-----------TEPVERVFnTHPGVRRSALVGVGKP 390
|
|
| 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 528467778 428 RLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTE----------------CTAGCTMSlPGD--WTAGHVGAPLPcnfvk 489
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAEglvnytrlddsderifTTQGRPMS-PDDevWVADADGNPLP----- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 490 lvdvaemnyfaaNGE-GEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHifklaQ----G 564
Cdd:PRK10946 377 ------------QGEvGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgG 439
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 528467778 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 528467778 434 AAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSlPGDWTA--GHVGAPLPCNfVKLVDvAEMNYFAANGEGEVCVKG 511
Cdd:cd05929 253 AAPCPPWVKEQWIDWGGPIIWEYYGGTEGQGLTIIN-GEEWLThpGSVGRAVLGK-VHILD-EDGNEVPPGEIGEVYFAN 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 512 PNVFQgYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRsdpvaqvfvHGDS 591
Cdd:cd05929 330 GPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIA---------HPKV 398
|
170
....*....|....
gi 528467778 592 LQACLVGvvVPDPD 605
Cdd:cd05929 399 LDAAVVG--VPDEE 410
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
263-604 |
1.33e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 64.38 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 263 PPKPEDLALICFT-SGTTGNPK------GAMLTHGNVVSncsafikiteVHCMLNQTDIHISYLPLAHMFErvVEGVLlc 335
Cdd:PRK06164 176 RAADPDAGALLFTtSGTTSGPKlvlhrqATLLRHARAIA----------RAYGYDPGAVLLAALPFCGVFG--FSTLL-- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 336 hgakiGYFQGDIRLLMDDLKNLKPTIfpvvpRLL-----------NRMFDKIFGQANTPLkrwllDFATSRkeaelksgv 404
Cdd:PRK06164 242 -----GALAGGAPLVCEPVFDAARTA-----RALrrhrvthtfgnDEMLRRILDTAGERA-----DFPSAR--------- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 405 vrkdsmwdklifskvqaslggrvRLMITGAAPVSPTVLTFLRAAlGCQFYEGYGQTECTA---GCTMSLPgdWTAGHVGA 481
Cdd:PRK06164 298 -----------------------LFGFASFAPALGELAALARAR-GVPLTGLYGSSEVQAlvaLQPATDP--VSVRIEGG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 482 PLPCN---FVKLVDVAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHI 558
Cdd:PRK06164 352 GRPASpeaRVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDS 431
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 528467778 559 FKLAqGEYIAPEKIENIYIRSDPVAQVFVHGDSL--QACLVGVVVPDP 604
Cdd:PRK06164 432 LRLG-GFLVNPAEIEHALEALPGVAAAQVVGATRdgKTVPVAFVIPTD 478
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
121-605 |
1.67e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 64.14 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPL---YdtlgTEA-ISYVIDKASIT 196
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQG-LGPGDH-VGIYARNRIEYVEAMLGAFKARAVPVNVnyrY----VEDeLRYLLDDSDAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 197 TIICD--IADKARLILDCVSGRKHsvtTIVIMESFDSELTAQAqncgidiISLKELEAIGKANHKtPIPPKPEDLALICf 274
Cdd:PRK07798 103 ALVYEreFAPRVAEVLPRLPKLRT---LVVVEDGSGNDLLPGA-------VDYEDALAAGSPERD-FGERSPDDLYLLY- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 275 TSGTTGNPKGAMLTHGNVvsncsafikiteVHCMLNQTDiHISYLPLAHMFERVVEGVL-----------LCHGAkigyf 343
Cdd:PRK07798 171 TGGTTGMPKGVMWRQEDI------------FRVLLGGRD-FATGEPIEDEEELAKRAAAgpgmrrfpappLMHGA----- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 344 qGDIRLLMdDLKNLKPTIFPVVPRL-------------LNRMFdkIFGQAntpLKRWLLDFATSRKEAELKSgvvrkdsm 410
Cdd:PRK07798 233 -GQWAAFA-ALFSGQTVVLLPDVRFdadevwrtierekVNVIT--IVGDA---MARPLLDALEARGPYDLSS-------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 411 wdklifskvqaslggrVRLMITGAAPVSPTVLTFLRAAL-GCQFYEGYGQTECTAGCT-MSLPGdwtAGHVGAPL--PCN 486
Cdd:PRK07798 298 ----------------LFAIASGGALFSPSVKEALLELLpNVVLTDSIGSSETGFGGSgTVAKG---AVHTGGPRftIGP 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 487 FVKLVDvaEMNYFAANGEGEVCV--KGPNVFQGYLKDPEQTSGA---VDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKL 561
Cdd:PRK07798 359 RTVVLD--EDGNPVEPGSGEIGWiaRRGHIPLGYYKDPEKTAETfptIDGVRYAIPGDRARVEADGTITLLGRGSVCINT 436
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 528467778 562 AqGEYIAPEKIENIyIRSDP-VAQVFVHG---DSLQACLVGVVVPDPD 605
Cdd:PRK07798 437 G-GEKVFPEEVEEA-LKAHPdVADALVVGvpdERWGQEVVAVVQLREG 482
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
266-613 |
1.94e-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: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 266 PEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEVhcmlNQTDIHISYLPLAhmFERVVEGVL--LCHGAKIGYF 343
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGV----TPADKSLVYASFS--FDASAWEIFphLTAGAALHVV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 344 QGDIRLLMDDLknlkptifpvvprllNRMFDKifgqantplKRWLLDFatsrkeaeLKSGVVRKDSMWDKLIFskvqasl 423
Cdd:cd17645 177 PSERRLDLDAL---------------NDYFNQ---------EGITISF--------LPTGAAEQFMQLDNQSL------- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 424 ggrvRLMITGAAPVSPTVLTflraalGCQFYEGYGQTECTAGCTMsLPGDWTAGHVGAPLPCNFVKLVDVAEMNYFAANG 503
Cdd:cd17645 218 ----RVLLTGGDKLKKIERK------GYKLVNNYGPTENTVVATS-FEIDKPYANIPIGKPIDNTRVYILDEALQLQPIG 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 504 -EGEVCVKGPNVFQGYLKDPEQTSGA------VDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIY 576
Cdd:cd17645 287 vAGELCIAGEGLARGYLNRPELTAEKfivhpfVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIEPFL 365
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 528467778 577 IRSDPVAQVFV----HGDSLQAcLVGVVVP----DPDFLPGWAKN 613
Cdd:cd17645 366 MNHPLIELAAVlakeDADGRKY-LVAYVTApeeiPHEELREWLKN 409
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
419-604 |
6.22e-10 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 61.77 E-value: 6.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 419 VQASLGGRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTEctagCTMSLPGDWTAGHV------GAPLPCNFVKLVD 492
Cdd:cd05973 199 VPARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTE----LGMVLANHHALEHPvhagsaGRAMPGWRVAVLD 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 493 VAeMNYFAANGEGEVCVKGPNV----FQGYLKDPEQTSgavdKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIA 568
Cdd:cd05973 275 DD-GDELGPGEPGRLAIDIANSplmwFRGYQLPDTPAI----DGGYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIG 348
|
170 180 190
....*....|....*....|....*....|....*.
gi 528467778 569 PEKIENIYIRSDPVAQVFVHGdslqaclvgvvVPDP 604
Cdd:cd05973 349 PFDVESALIEHPAVAEAAVIG-----------VPDP 373
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
266-608 |
6.76e-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: 62.03 E-value: 6.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 266 PEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEVHCmlnqTDIHISYLPLAHMFERVVEGVLLchgAKIGyfqG 345
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRD----NGDEAVLFFSNYVFDFFVEQMTL---ALLN---G 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 346 DIRLLMDDLKNLKPTIFpvvPRLLNRmfDKIFGQANTPLKRWLLDFAtsrkeaelksgvvRKDSMwdklifskvqaslgg 425
Cdd:cd17648 163 QKLVVPPDEMRFDPDRF---YAYINR--EKVTYLSGTPSVLQQYDLA-------------RLPHL--------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 426 rvRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTECTAGCTMSL--PGDWTAGHVGAPLPCNFVKLVDvAEMNYFAANG 503
Cdd:cd17648 210 --KRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRFfpGDQRFDKSLGRPVRNTKCYVLN-DAMKRVPVGA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 504 EGEVCVKGPNVFQGYLKDPEQTS---------GAVDKA----GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAP 569
Cdd:cd17648 287 VGELYLGGDGVARGYLNRPELTAerflpnpfqTEQERArgrnARLYkTGDLVRWLPSGELEYLGRNDFQVKI-RGQRIEP 365
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 528467778 570 EKIENIYIRSDPVAQVFV--------HGDSLQACLVGVVVPDPDFLP 608
Cdd:cd17648 366 GEVEAALASYPGVRECAVvakedasqAQSRIQKYLVGYYLPEPGHVP 412
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
121-603 |
6.78e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 63.05 E-value: 6.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGhsQSGDKYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASIttiic 200
Cdd:PRK12316 4577 LTYAELNRRANRLAHALIARG--VGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGA----- 4649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 201 diadkaRLILDcvsgRKHSVTTIVIMEsfdseltaqaqncGIDIISL-KELEAIGKANHKTPIPPKPEDLALICFTSGTT 279
Cdd:PRK12316 4650 ------ALLLT----QSHLLQRLPIPD-------------GLASLALdRDEDWEGFPAHDPAVRLHPDNLAYVIYTSGST 4706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 280 GNPKGAMLTHGNVVsncsAFIKITEVHCMLNQTDIHISYLPLAhmFERVVEGVL--LCHGAkigyfqgdiRLLMDDLKNL 357
Cdd:PRK12316 4707 GRPKGVAVSHGSLV----NHLHATGERYELTPDDRVLQFMSFS--FDGSHEGLYhpLINGA---------SVVIRDDSLW 4771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 358 KPtifpvvprllNRMFDKIFGQANTplkrwLLDFATsrkeaelksgvvrkdSMWDKLIFSKVQASLGGRVRLMITGAAPV 437
Cdd:PRK12316 4772 DP----------ERLYAEIHEHRVT-----VLVFPP---------------VYLQQLAEHAERDGEPPSLRVYCFGGEAV 4821
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 438 SPTVLT-FLRAALGCQFYEGYGQTECTA-----GCTMSLPGDWTAGHVGAPLPCNFVKLVDVaEMNYFAANGEGEVCVKG 511
Cdd:PRK12316 4822 AQASYDlAWRALKPVYLFNGYGPTETTVtvllwKARDGDACGAAYMPIGTPLGNRSGYVLDG-QLNPLPVGVAGELYLGG 4900
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 512 PNVFQGYLKDPEQTSGAV------DKAGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDPV-- 582
Cdd:PRK12316 4901 EGVARGYLERPALTAERFvpdpfgAPGGRLYrTGDLARYRADGVIDYLGRVDHQVKI-RGFRIELGEIEARLREHPAVre 4979
|
490 500
....*....|....*....|.
gi 528467778 583 AQVFVHGDSLQACLVGVVVPD 603
Cdd:PRK12316 4980 AVVIAQEGAVGKQLVGYVVPQ 5000
|
|
| 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 528467778 427 VRLMITGAAPVSPTVLtflRAAL---GCQFYEGYGQTEcTAGCTMSLPGDWTA--GHVGAPLPCNfVKLVDvAEMNYFAA 501
Cdd:PRK08276 264 LRVAIHAAAPCPVEVK---RAMIdwwGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGE-VRILD-EDGNELPP 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 502 NGEGEVCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGkWL-PNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSD 580
Cdd:PRK08276 338 GEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVG-YLdEDGYLYLTDRKSDMI-ISGGVNIYPQEIENLLVTHP 415
|
170 180
....*....|....*....|....*.
gi 528467778 581 PVAQVFVHGdslqaclvgvvVPDPDF 606
Cdd:PRK08276 416 KVADVAVFG-----------VPDEEM 430
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
260-606 |
3.28e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 59.70 E-value: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 260 TPIPPKPEDLALIcFTSGTTGNPKG--AMLTHGNVVSNcsafikitevhcmlnqtdihisyLPLAHMFERVV----EGVL 333
Cdd:PRK13391 148 TPIADESLGTDML-YSSGTTGRPKGikRPLPEQPPDTP-----------------------LPLTAFLQRLWgfrsDMVY 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 334 LC-----HGAKIGYFQGDIRL-----LMDD---------LKNLKPTIFPVVPRLLNRMfdkifgqantpLKrwlLDFATs 394
Cdd:PRK13391 204 LSpaplyHSAPQRAVMLVIRLggtviVMEHfdaeqylalIEEYGVTHTQLVPTMFSRM-----------LK---LPEEV- 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 395 RKEAELKSgvvrkdsmwdklifskvqaslggrVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTEcTAGCTMSLPGDW 474
Cdd:PRK13391 269 RDKYDLSS------------------------LEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATE-GLGFTACDSEEW 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 475 TA--GHVGAPLpcnFVKLVDVAEMNYFAANGE-GEVCVKGPNVFQgYLKDPEQTSGAVD-KAGWLHTGDIGKWLPNGTLK 550
Cdd:PRK13391 324 LAhpGTVGRAM---FGDLHILDDDGAELPPGEpGTIWFEGGRPFE-YLNDPAKTAEARHpDGTWSTVGDIGYVDEDGYLY 399
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 528467778 551 IIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVFVHGdslqaclvgvvVPDPDF 606
Cdd:PRK13391 400 LTDRAAFMI-ISGGVNIYPQEAENLLITHPKVADAAVFG-----------VPNEDL 443
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
121-573 |
3.48e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 60.02 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLY--DTLGTEAiSYVidkasitti 198
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALG-LKPGDR-VALIAETDGDFVEAFFACQYAGLVPVPLPlpMGFGGRE-SYI--------- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 199 icdiaDKARLILDcvSGRKHSVTTIVIMESFDSELTAQAQNC-GIDIISLKELEAIGKAnhkTPiPPKPEDLALICFTSG 277
Cdd:PRK09192 118 -----AQLRGMLA--SAQPAAIITPDELLPWVNEATHGNPLLhVLSHAWFKALPEADVA---LP-RPTPDDIAYLQYSSG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 278 TTGNPKGAMLTHGNVVSNCSAfikITEVHCMLNQTDIHISYLPLAH-MfervvegvllchgakigyfqGDIRLLMDDLKN 356
Cdd:PRK09192 187 STRFPRGVIITHRALMANLRA---ISHDGLKVRPGDRCVSWLPFYHdM--------------------GLVGFLLTPVAT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 357 ------LKPTIFPVVP----RLLNR-----MFDKIFGqantplkrwlLDFATSRkeAELKSGVVRKDSMWdklifskvqa 421
Cdd:PRK09192 244 qlsvdyLPTRDFARRPlqwlDLISRnrgtiSYSPPFG----------YELCARR--VNSKDLAELDLSCW---------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 422 slggrvRLMITGAAPVSPTVL-----TFlrAALGCQ---FYEGYGQTECTAGCTMSLPG--------DWTA----GHV-- 479
Cdd:PRK09192 302 ------RVAGIGADMIRPDVLhqfaeAF--APAGFDdkaFMPSYGLAEATLAVSFSPLGsgivveevDRDRleyqGKAva 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 480 --------------GAPLPCNFVKLVDVAEmNYFAANGEGEVCVKGPNVFQGYLKDPEqTSGAVDKAGWLHTGDIGkWLP 545
Cdd:PRK09192 374 pgaetrrvrtfvncGKALPGHEIEIRNEAG-MPLPERVVGHICVRGPSLMSGYFRDEE-SQDVLAADGWLDTGDLG-YLL 450
|
490 500
....*....|....*....|....*...
gi 528467778 546 NGTLKIIDRKKHIFkLAQGEYIAPEKIE 573
Cdd:PRK09192 451 DGYLYITGRAKDLI-IINGRNIWPQDIE 477
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
272-583 |
4.32e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 59.33 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 272 ICFTSGTTGNPKGAMLTHGNVVSNCSAfIKITEVHCmLNQTDihiSYLPLAHMFErvVEGVLLCH-----GAKIgYFQG- 345
Cdd:PRK07008 181 LCYTSGTTGNPKGALYSHRSTVLHAYG-AALPDAMG-LSARD---AVLPVVPMFH--VNAWGLPYsapltGAKL-VLPGp 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 346 --DIRLLMDDLKNLKPTIFPVVPR----LLNRMfdkifgqantplkrwlldfatsrKEAELKsgvvrkdsmwdkliFSKV 419
Cdd:PRK07008 253 dlDGKSLYELIEAERVTFSAGVPTvwlgLLNHM-----------------------REAGLR--------------FSTL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 420 QaslggrvRLMITGAApVSPTVLTFLRAALGCQFYEGYGQTECTA-GCTMSLpgdwTAGHVGAPLPCNFVKL-------- 490
Cdd:PRK07008 296 R-------RTVIGGSA-CPPAMIRTFEDEYGVEVIHAWGMTEMSPlGTLCKL----KWKHSQLPLDEQRKLLekqgrviy 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 491 -VDvaeMNYFAANGE---------GEVCVKGPNVFQGYLKDpeQTSGAVDkaGWLHTGDIGKWLPNGTLKIIDRKKHIFK 560
Cdd:PRK07008 364 gVD---MKIVGDDGRelpwdgkafGDLQVRGPWVIDRYFRG--DASPLVD--GWFPTGDVATIDADGFMQITDRSKDVIK 436
|
330 340
....*....|....*....|...
gi 528467778 561 lAQGEYIAPEKIENIYIRSDPVA 583
Cdd:PRK07008 437 -SGGEWISSIDIENVAVAHPAVA 458
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
101-609 |
4.41e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 59.66 E-value: 4.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 101 RVSNNGPCLGSRkaGQPYKWLSY-KEVADRAEFAGSAllhrgHSQSGDKYIGIFAQNRPEWTISELACYTYSLVAVPLYD 179
Cdd:PRK13388 12 RAGDDTIAVRYG--DRTWTWREVlAEAAARAAALIAL-----ADPDRPLHVGVLLGNTPEMLFWLAAAALGGYVLVGLNT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 180 TLGTEAISYVIDKASITTIICDIADKARLI-LDcVSGrkhsVTTIVIMESFDSELTAQAQncgidiiSLKELEAIGkanh 258
Cdd:PRK13388 85 TRRGAALAADIRRADCQLLVTDAEHRPLLDgLD-LPG----VRVLDVDTPAYAELVAAAG-------ALTPHREVD---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 259 ktpippkPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEVHCmlnqTDIHISYLPLAHMfERVVEG--VLLCH 336
Cdd:PRK13388 149 -------AMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTR----DDVCYVSMPLFHS-NAVMAGwaPAVAS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 337 GAKIGY--------FQGDIRLLmddlknlKPTIFPVVPRLL-------NRMFDkifgqANTPLKRWLLDFATSRKEAElk 401
Cdd:PRK13388 217 GAAVALpakfsasgFLDDVRRY-------GATYFNYVGKPLayilatpERPDD-----ADNPLRVAFGNEASPRDIAE-- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 402 sgvvrkdsmwdklifskvqaslggrvrlmitgaapvsptvltFLRAaLGCQFYEGYGQTEctAGCTMSLPGDWTAGHVGA 481
Cdd:PRK13388 283 ------------------------------------------FSRR-FGCQVEDGYGSSE--GAVIVVREPGTPPGSIGR 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 482 PLPCnfVKLVD--------VAEmnyFAANGE--------GE-VCVKGPNVFQGYLKDPEQTSGAVdKAGWLHTGDIGKWL 544
Cdd:PRK13388 318 GAPG--VAIYNpetltecaVAR---FDAHGAllnadeaiGElVNTAGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRD 391
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528467778 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 |
5.13e-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: 59.51 E-value: 5.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 122 SYKEV-ADRAEFAGsALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAI-SYVIDKASITTII 199
Cdd:cd17634 86 SYRELhREVCRFAG-TLLDLG-VKKGDR-VAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVaGRIIDSSSRLLIT 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 200 CD-------IADKARLILDCVSGRKHSVTTIVIMESFDSELTAQAqncGIDIiSLKELEAIGKANHKtPIPPKPEDLALI 272
Cdd:cd17634 163 ADggvragrSVPLKKNVDDALNPNVTSVEHVIVLKRTGSDIDWQE---GRDL-WWRDLIAKASPEHQ-PEAMNAEDPLFI 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 273 CFTSGTTGNPKGAMLTHGN-VVSNCSAFIKITEVHcmlnQTDIHISYLPLAHMFER--VVEGVLLChGAKIGYFQGdirl 349
Cdd:cd17634 238 LYTSGTTGKPKGVLHTTGGyLVYAATTMKYVFDYG----PGDIYWCTADVGWVTGHsyLLYGPLAC-GATTLLYEG---- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 350 lmddlKNLKPTifpvvPRLLNRMFDK----IFGQANTPLKrwlldfatsrkeAELKSGvvrkdsmwDKLIFSKVQASLgg 425
Cdd:cd17634 309 -----VPNWPT-----PARMWQVVDKhgvnILYTAPTAIR------------ALMAAG--------DDAIEGTDRSSL-- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 426 rvRLMITGAAPVSPTVLTFLRAALG---CQFYEGYGQTECTAGCTMSLPG--DWTAGHVGAPLPCNFVKLVDvAEMNYFA 500
Cdd:cd17634 357 --RILGSVGEPINPEAYEWYWKKIGkekCPVVDTWWQTETGGFMITPLPGaiELKAGSATRPVFGVQPAVVD-NEGHPQP 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 501 ANGEGEVCVKG--PNVFQGYLKDPE---QTSGAVDKAGWLHtGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 575
Cdd:cd17634 434 GGTEGNLVITDpwPGQTRTLFGDHErfeQTYFSTFKGMYFS-GDGARRDEDGYYWITGRSDDVINVA-GHRLGTAEIESV 511
|
490 500
....*....|....*....|....*....
gi 528467778 576 YIrSDPVAQvfvhgdslQACLVGvvVPDP 604
Cdd:cd17634 512 LV-AHPKVA--------EAAVVG--IPHA 529
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
121-603 |
2.54e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 57.66 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGhsQSGDKYIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERG--VGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLS 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 201 DIADKARLILDcvsgrkhsvttivimesfdseltAQAQNCGIDIISLkELEAIGKANHKTPIppKPEDLALICFTSGTTG 280
Cdd:PRK12316 615 QSHLGRKLPLA-----------------------AGVQVLDLDRPAA-WLEGYSEENPGTEL--NPENLAYVIYTSGSTG 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 281 NPKGAMLTHGNVVSncsafikitEVHCMLN--QTDIHisylplahmfERVVEGVLLCHGAKIGYFQGdirllmdDLKNLK 358
Cdd:PRK12316 669 KPKGAGNRHRALSN---------RLCWMQQayGLGVG----------DTVLQKTPFSFDVSVWEFFW-------PLMSGA 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 359 PTIfpVVPRLLNRMFDKIFGQANTPLKRwLLDFATSRKEAELKSGVVrkdsmwdklifskvqASLGGRVRLMITGAAPVS 438
Cdd:PRK12316 723 RLV--VAAPGDHRDPAKLVELINREGVD-TLHFVPSMLQAFLQDEDV---------------ASCTSLRRIVCSGEALPA 784
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 439 PTVLTFLRAALGCQFYEGYGQTECTAGCTMSLPGDWTAGHV--GAPLPCNFVKLVDvAEMNYFAANGEGEVCVKGPNVFQ 516
Cdd:PRK12316 785 DAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGGDSVpiGRPIANLACYILD-ANLEPVPVGVLGELYLAGRGLAR 863
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 517 GYLKDPEQT------SGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSDPVAQVFVHG- 589
Cdd:PRK12316 864 GYHGRPGLTaerfvpSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL-RGLRIELGEIEARLLEHPWVREAAVLAv 942
|
490
....*....|....
gi 528467778 590 DSLQacLVGVVVPD 603
Cdd:PRK12316 943 DGKQ--LVGYVVLE 954
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
266-603 |
3.76e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 57.09 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 266 PEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFikitEVHCMLNQTDIHISYLPLAhmFERVVEGVL--LCHGAKIGYF 343
Cdd:PRK12467 3236 GENLAYVIYTSGSTGKPKGVGVRHGALANHLCWI----AEAYELDANDRVLLFMSFS--FDGAQERFLwtLICGGCLVVR 3309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 344 QGDIRllmddlknlkptifpvvprllnrmfdkifgqanTPLKRW---------LLDFATSRKEAELKSGVVRKdsmwdkl 414
Cdd:PRK12467 3310 DNDLW---------------------------------DPEELWqaihahrisIACFPPAYLQQFAEDAGGAD------- 3349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 415 ifskvqaslGGRVRLMITGAAPVSPTVLTFLRAALG-CQFYEGYGQTECTAGCTMslpgdWTAGHVGAPLPCNFVKLVDV 493
Cdd:PRK12467 3350 ---------CASLDIYVFGGEAVPPAAFEQVKRKLKpRGLTNGYGPTEAVVTVTL-----WKCGGDAVCEAPYAPIGRPV 3415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 494 AEMNYFAANGE---------GEVCVKGPNVFQGY-----------LKDPEQTSGavdkaGWLH-TGDIGKWLPNGTLKII 552
Cdd:PRK12467 3416 AGRSIYVLDGQlnpvpvgvaGELYIGGVGLARGYhqrpsltaerfVADPFSGSG-----GRLYrTGDLARYRADGVIEYL 3490
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 528467778 553 DRKKHIFKLaQGEYIAPEKIENIYIRSDPVAQ-VFVHGDSLQAC-LVGVVVPD 603
Cdd:PRK12467 3491 GRIDHQVKI-RGFRIELGEIEARLLQHPSVREaVVLARDGAGGKqLVAYVVPA 3542
|
|
| 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 528467778 119 KWLSYKEVADRAEFAGSALLHRGHSQsGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTI 198
Cdd:cd05968 90 RTLTYGELLYEVKRLANGLRALGVGK-GDR-VGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKAL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 199 IcdIAD----KARLI-----LDCVSGRKHSVTTIVIMESFDSELTAQAQNcgiDIISLKELEAIGKANHKTpippKPEDL 269
Cdd:cd05968 168 I--TADgftrRGREVnlkeeADKACAQCPTVEKVVVVRHLGNDFTPAKGR---DLSYDEEKETAGDGAERT----ESEDP 238
|
170 180
....*....|....*....|.
gi 528467778 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 528467778 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRPEWTISELACYTYSLVAVPLYDTLGTEAISYVIDKASITTIIC 200
Cdd:PRK04319 74 YTYKELKELSNKFANVLKELG-VEKGDR-VFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLIT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 201 DIADKARLILDCVSGRKHSVttivimesfdseLTAQAQNCGIDIISLKELEAigKANHKTPIPP-KPEDLALICFTSGTT 279
Cdd:PRK04319 152 TPALLERKPADDLPSLKHVL------------LVGEDVEEGPGTLDFNALME--QASDEFDIEWtDREDGAILHYTSGST 217
|
170
....*....|....
gi 528467778 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 528467778 428 RLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTEcTAGCTMSLPGDWTA--GHVGAPLPCNFVKLVDvAEMNYFAANGEG 505
Cdd:PRK12406 274 RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE-SGAVTFATSEDALShpGTVGKAAPGAELRFVD-EDGRPLPQGEIG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 506 EVCVKGPNV--FQgYLKDPEQTSgAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVA 583
Cdd:PRK12406 352 EIYSRIAGNpdFT-YHNKPEKRA-EIDRGGFITSGDVGYLDADGYLFLCDRKRDMV-ISGGVNIYPAEIEAVLHAVPGVH 428
|
170 180
....*....|....*....|...
gi 528467778 584 QVFVHGdslqaclvgvvVPDPDF 606
Cdd:PRK12406 429 DCAVFG-----------IPDAEF 440
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
121-606 |
1.87e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 54.16 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 121 LSYKEVADRAEFAGSALLHRGhSQSGDKyIGIFAQNRpEWTISELACYTYSLVAVPLYDT-LGTEAISYVIDKASITTII 199
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALG-VRAGDG-VAVLARNH-RGFVLALYAAGKVGARIILLNTgFSGPQLAEVAAREGVKALV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 200 CD--IADKARLILDCVSGrkhsVTTIVIMESFDSELTAQAQncgidiiSLKELEAiGKANHKTPIPPKPEdlALICFTSG 277
Cdd:PRK07788 152 YDdeFTDLLSALPPDLGR----LRAWGGNPDDDEPSGSTDE-------TLDDLIA-GSSTAPLPKPPKPG--GIVILTSG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 278 TTGNPKGAMLTHGNVVSNCSAFIkiTEVHCMLNQTDIHISylPLAHMFERVVEGVLLCHGAKI---GYFqgDIRLLMDDL 354
Cdd:PRK07788 218 TTGTPKGAPRPEPSPLAPLAGLL--SRVPFRAGETTLLPA--PMFHATGWAHLTLAMALGSTVvlrRRF--DPEATLEDI 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 355 KNLKPTIFPVVPRLLNRMFDKifgqantpLKRWLLDFATSrkeaelksgvvrkdSMwdKLIFSkvqaslggrvrlmiTGA 434
Cdd:PRK07788 292 AKHKATALVVVPVMLSRILDL--------GPEVLAKYDTS--------------SL--KIIFV--------------SGS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 435 ApVSPTVLTFLRAALGCQFYEGYGQTECtAGCTMSLPGDWTA--GHVGAPLPCNFVKLVDvAEMNYFAANGEGEVCVKGP 512
Cdd:PRK07788 334 A-LSPELATRALEAFGPVLYNLYGSTEV-AFATIATPEDLAEapGTVGRPPKGVTVKILD-ENGNEVPRGVVGRIFVGNG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 513 NVFQGYlkdpeqTSGA----VDkaGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVFVH 588
Cdd:PRK07788 411 FPFEGY------TDGRdkqiID--GLLSSGDVGYFDEDGLLFVDGRDDDMI-VSGGENVFPAEVEDLLAGHPDVVEAAVI 481
|
490
....*....|....*...
gi 528467778 589 GdslqaclvgvvVPDPDF 606
Cdd:PRK07788 482 G-----------VDDEEF 488
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
264-615 |
2.52e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 54.40 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 264 PKPEDLALICFTSGTTGNPKGAMLTHGNVVsncsAFIKITEVHCMLNQTDIHISYLPLAhmFERVVEGVL--LCHGAKIG 341
Cdd:PRK12467 1715 LAPQNLAYVIYTSGSTGRPKGAGNRHGALV----NRLCATQEAYQLSAADVVLQFTSFA--FDVSVWELFwpLINGARLV 1788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 342 YFQGDIRL----LMDDLKNLKPTIFPVVPRLLNRmFDKIFGQANTPLKrwlldfatsrkeaelksgvvrkdsmwdklifs 417
Cdd:PRK12467 1789 IAPPGAHRdpeqLIQLIERQQVTTLHFVPSMLQQ-LLQMDEQVEHPLS-------------------------------- 1835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 418 kvqaslggrVRLMITGAAPVSPTVLTFLRAALG-CQFYEGYGQTECTAGCTMslpgdWTAGH----------VGAPLPCN 486
Cdd:PRK12467 1836 ---------LRRVVCGGEALEVEALRPWLERLPdTGLFNLYGPTETAVDVTH-----WTCRRkdlegrdsvpIGQPIANL 1901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 487 FVKLVDvAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQT------SGAVDKAGWLH-TGDIGKWLPNGTLKIIDRKKHIF 559
Cdd:PRK12467 1902 STYILD-ASLNPVPIGVAGELYLGGVGLARGYLNRPALTaerfvaDPFGTVGSRLYrTGDLARYRADGVIEYLGRIDHQV 1980
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 528467778 560 KLaQGEYIAPEKIENIYIRSDPVAQ--VFVHGDSLQACLVGVVVPDPDFLPGWAKNRG 615
Cdd:PRK12467 1981 KI-RGFRIELGEIEARLREQGGVREavVIAQDGANGKQLVAYVVPTDPGLVDDDEAQV 2037
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
241-638 |
2.80e-07 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 53.75 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 241 GIDIISLKELEAIGKAnhKTPIPP----KPEDLALICFTSGTTGNPKGAMLTHGNVVS----NCSAFIKITEVHcMLNQT 312
Cdd:PRK04813 115 GIPVITLDELKDIFAT--GNPYDFdhavKGDDNYYIIFTSGTTGKPKGVQISHDNLVSftnwMLEDFALPEGPQ-FLNQA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 313 ----DIHISYLPLAhmfervvegvlLCHGAKIGYFQGDI----RLLMDDLKNLKPTIFPVVPR-----LLNRMFDkifgQ 379
Cdd:PRK04813 192 pysfDLSVMDLYPT-----------LASGGTLVALPKDMtanfKQLFETLPQLPINVWVSTPSfadmcLLDPSFN----E 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 380 ANTP-LKRWLLDFAT-SRKEAElksgvvrkdsmwdKLI--FSKvqaslgGRVrlmitgaapvsptvltflraalgcqfYE 455
Cdd:PRK04813 257 EHLPnLTHFLFCGEElPHKTAK-------------KLLerFPS------ATI--------------------------YN 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 456 GYGQTECTAGCtmslpgdwTAGHVGA-------PLPCNFVK-----LVDVAEMNYFAANGEGEVCVKGPNVFQGYLKDPE 523
Cdd:PRK04813 292 TYGPTEATVAV--------TSIEITDemldqykRLPIGYAKpdsplLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 524 QTSGA---VDKAGWLHTGDIGKwLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI-----YIRSdPVAQVFVHGDSLQAc 595
Cdd:PRK04813 364 KTAEAfftFDGQPAYHTGDAGY-LEDGLLFYQGRIDFQIKLN-GYRIELEEIEQNlrqssYVES-AVVVPYNKDHKVQY- 439
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 528467778 596 LVGVVVPdpdflpgwaKNRGIEGSFnDLCKS--KEVKNAILEDMI 638
Cdd:PRK04813 440 LIAYVVP---------KEEDFEREF-ELTKAikKELKERLMEYMI 474
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
252-575 |
3.41e-07 |
|
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: 53.59 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 252 AIGKANHKtPIPPKPE-DLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEVHcmLNQTDIHISYLPLAHmfervVE 330
Cdd:cd05915 138 EEALGEEA-DPVRVPErAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTA--LSEKDVVLPVVPMFH-----VN 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 331 GvlLCHGAKIGYFQGDIRLLMDDLKNlkptifpvvprllNRMFDKIfgqantpLKRWLLDFATSRKEAELKSGVvrKDSm 410
Cdd:cd05915 210 A--WCLPYAATLVGAKQVLPGPRLDP-------------ASLVELF-------DGEGVTFTAGVPTVWLALADY--LES- 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 411 wdklifskVQASLGGRVRLMITGAAPvsPTVLTFLRAALGCQFYEGYGQTEC----TAGCTM----SLPGDWTAGHVGAP 482
Cdd:cd05915 265 --------TGHRLKTLRRLVVGGSAA--PRSLIARFERMGVEVRQGYGLTETspvvVQNFVKshleSLSEEEKLTLKAKT 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 483 LPCNFVKLVDVAEMNYFAANGEGE----VCVKGPNVFQGYLKDPEQTSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHI 558
Cdd:cd05915 335 GLPIPLVRLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDL 414
|
330
....*....|....*..
gi 528467778 559 FKLAqGEYIAPEKIENI 575
Cdd:cd05915 415 IKSG-GEWISSVDLENA 430
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
264-614 |
4.91e-07 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 52.35 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 264 PKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAfikiteVHCMLNQTDIHISYLPLAHmfervvegvllchgakIGYF 343
Cdd:PRK07824 32 PIDDDVALVVATSGTTGTPKGAMLTAAALTASADA------THDRLGGPGQWLLALPAHH----------------IAGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 344 QGDIRLLmddLKNLKPTIFPVvprllNRMFDkifgqantplkrwLLDFAtsRKEAELKSGvvRKDSMWDKLIFSKVQASL 423
Cdd:PRK07824 90 QVLVRSV---IAGSEPVELDV-----SAGFD-------------PTALP--RAVAELGGG--RRYTSLVPMQLAKALDDP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 424 GGRVRL-----MITGAAPVSPTVLTflRA-ALGCQFYEGYGQTECTAGCTMSlpgdwtaghvGAPLPCNFVKLVDvaemn 497
Cdd:PRK07824 145 AATAALaeldaVLVGGGPAPAPVLD--AAaAAGINVVRTYGMSETSGGCVYD----------GVPLDGVRVRVED----- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 498 yfaangeGEVCVKGPNVFQGYLKDPEQtsGAVDKAGWLHTGDIGKwLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYI 577
Cdd:PRK07824 208 -------GRIALGGPTLAKGYRNPVDP--DPFAEPGWFRTDDLGA-LDDGVLTVLGRADDAISTG-GLTVLPQVVEAALA 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 528467778 578 RSDPVAQVFVHG---DSLQACLVGVVVPDP--------------DFLPGWAKNR 614
Cdd:PRK07824 277 THPAVADCAVFGlpdDRLGQRVVAAVVGDGgpaptlealrahvaRTLDRTAAPR 330
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
270-597 |
5.73e-07 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 52.73 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 270 ALICFTSGTTGNPKGAMLTHGNVVS----NCSAFIKITEVHCMLNQTDIHISY-------LPLAHMFERVVEGVLLchGA 338
Cdd:PRK06060 148 AYATYTSGTTGPPKAAIHRHADPLTfvdaMCRKALRLTPEDTGLCSARMYFAYglgnsvwFPLATGGSAVINSAPV--TP 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 339 KIGYFQGdirllmddlKNLKPTIFPVVPRLLNRMFDkifgqANTPlkrwlldfatsrkeaelksgvvrkDSMWDklifsk 418
Cdd:PRK06060 226 EAAAILS---------ARFGPSVLYGVPNFFARVID-----SCSP------------------------DSFRS------ 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 419 vqaslggrVRLMITGAAPVSPTVLTFLRAALG-CQFYEGYGQTECTAGCTMSLPGDWTAGHVGAPLPCNFVKLV--DVAE 495
Cdd:PRK06060 262 --------LRCVVSAGEALELGLAERLMEFFGgIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVapDGTT 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 496 MnyfAANGEGEVCVKGPNVFQGYLKDPEQTsgaVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIfKLAQGEYIAPEKIENI 575
Cdd:PRK06060 334 A---GPGVEGDLWVRGPAIAKGYWNRPDSP---VANEGWLDTRDRVCIDSDGWVTYRCRADDT-EVIGGVNVDPREVERL 406
|
330 340
....*....|....*....|....*....
gi 528467778 576 YIRSDPVAQVFVHG-------DSLQACLV 597
Cdd:PRK06060 407 IIEDEAVAEAAVVAvrestgaSTLQAFLV 435
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
270-589 |
5.90e-07 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 52.83 E-value: 5.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 270 ALICFTSGTTGNPKGAMLTH-GNVVsncsafikitevHCML-NQTDIhisylplahmfervvegvllchgakIGYFQGDi 347
Cdd:PRK06018 180 AGMCYTSGTTGDPKGVLYSHrSNVL------------HALMaNNGDA-------------------------LGTSAAD- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 348 rllmddlknlkpTIFPVVPrllnrMFdkifgQANTplkrWLLDFATSRKEAELKSGVVRKD--SMWDKLIFSKVQASLG- 424
Cdd:PRK06018 222 ------------TMLPVVP-----LF-----HANS----WGIAFSAPSMGTKLVMPGAKLDgaSVYELLDTEKVTFTAGv 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 425 GRVRLM-------------------ITGAAPVSPTVLTFLRaaLGCQFYEGYGQTECTAGCTMS--------LPGD---- 473
Cdd:PRK06018 276 PTVWLMllqymekeglklphlkmvvCGGSAMPRSMIKAFED--MGVEVRHAWGMTEMSPLGTLAalkppfskLPGDarld 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 474 WTAGHVGAPLPCNfVKLVDVAEmNYFAANGE--GEVCVKGPNVFQGYLK-DPEQtsgaVDKAGWLHTGDIGKWLPNGTLK 550
Cdd:PRK06018 354 VLQKQGYPPFGVE-MKITDDAG-KELPWDGKtfGRLKVRGPAVAAAYYRvDGEI----LDDDGFFDTGDVATIDAYGYMR 427
|
330 340 350
....*....|....*....|....*....|....*....
gi 528467778 551 IIDRKKHIFKlAQGEYIAPEKIENIYIRSDPVAQVFVHG 589
Cdd:PRK06018 428 ITDRSKDVIK-SGGEWISSIDLENLAVGHPKVAEAAVIG 465
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
270-605 |
9.71e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 51.93 E-value: 9.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 270 ALICFTSGTTGNPKGAM--LTHGNVVSNCSAFIKITEVHCMLNQTDIHISYLPLAHMFE-RVVEGVLLCHGAKIGYFQGD 346
Cdd:PRK13390 151 AVMLYSSGTTGFPKGIQpdLPGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHAAPlRWCSMVHALGGTVVLAKRFD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 347 IRLLMDDLKNLKPTIFPVVPRLLNRMFDkifgqantplkrwlLDfATSRKEAELKSgvvrkdsmwdklifskvqaslggr 426
Cdd:PRK13390 231 AQATLGHVERYRITVTQMVPTMFVRLLK--------------LD-ADVRTRYDVSS------------------------ 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 427 VRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTEcTAGCTMSLPGDWTA--GHVGAPLPCNFVKLVDvaEMNYFAANGE 504
Cdd:PRK13390 272 LRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGRSVLGDLHICDD--DGNELPAGRI 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 505 GEVCVKGPNVFQGYLKDPEQTSGAVDKAG--WLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPV 582
Cdd:PRK13390 349 GTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQETENALTMHPAV 427
|
330 340
....*....|....*....|...
gi 528467778 583 AQVFVHGdslqaclvgvvVPDPD 605
Cdd:PRK13390 428 HDVAVIG-----------VPDPE 439
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
267-591 |
1.47e-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: 51.32 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 267 EDLALICFTSGTTGNPKGAMLTHGNVVSncsaFIKITEVHCMLNQTDihiSYLPLAHM-FERVVEGVL--LCHGAKIGYF 343
Cdd:cd17656 128 DDLLYIIYTSGTTGKPKGVQLEHKNMVN----LLHFEREKTNINFSD---KVLQFATCsFDVCYQEIFstLLSGGTLYII 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 344 QGDIRLLMDDLKNLKPT------IFPVVprLLNRMFDkifgqantpLKRWLLDFATSRKEaelksgvvrkdsmwdkLIFS 417
Cdd:cd17656 201 REETKRDVEQLFDLVKRhnievvFLPVA--FLKFIFS---------EREFINRFPTCVKH----------------IITA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 418 KVQaslggrvrLMITgaapvSPTVLTFLRAalGCQFYEGYG--QTECTAGCTMSLPGDWTA-GHVGAPLPCNFVKLVDvA 494
Cdd:cd17656 254 GEQ--------LVIT-----NEFKEMLHEH--NVHLHNHYGpsETHVVTTYTINPEAEIPElPPIGKPISNTWIYILD-Q 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 495 EMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSgavDK---------AGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGE 565
Cdd:cd17656 318 EQQLQPQGIVGELYISGASVARGYLNRQELTA---EKffpdpfdpnERMYRTGDLARYLPDGNIEFLGRADHQVKI-RGY 393
|
330 340
....*....|....*....|....*...
gi 528467778 566 YIAPEKIENIYIRSDPVAQ--VFVHGDS 591
Cdd:cd17656 394 RIELGEIEAQLLNHPGVSEavVLDKADD 421
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
263-324 |
1.48e-06 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 51.52 E-value: 1.48e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528467778 263 PPKPEDLALICFTSGTTGNPKGAMLTHGNVVSnCSAFIKITEVHcmlnQTDIHISYLPLAHM 324
Cdd:cd05938 140 HVTIKSPALYIYTSGTTGLPKAARISHLRVLQ-CSGFLSLCGVT----ADDVIYITLPLYHS 196
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
427-574 |
2.28e-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: 50.10 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 427 VRLMITGAAPVSPTVLTFLRAAL-GCQFYEGYGQTEcTAGCTMSLPGD-WTAGHVGAPLPCNFVKLVDvaemnyfAANGE 504
Cdd:cd17633 112 IKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSE-LSFITYNFNQEsRPPNSVGRPFPNVEIEIRN-------ADGGE 183
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528467778 505 -GEVCVKGPNVFQGYLKdpeqtSGAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIEN 574
Cdd:cd17633 184 iGKIFVKSEMVFSGYVR-----GGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIES 248
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
425-598 |
9.98e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 49.40 E-value: 9.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 425 GRVRLMITGAAPVSPTVLTFLRAAL-GCQFYEGYGQTE---------CTAGCTMSLPgdwtaghVGAPLPCNFVKLVDvA 494
Cdd:PRK05691 1388 TSLRRLFSGGEALPAELRNRVLQRLpQVQLHNRYGPTEtainvthwqCQAEDGERSP-------IGRPLGNVLCRVLD-A 1459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 495 EMNYFAANGEGEVCVKGPNVFQGYLKDPEQTS-------GAVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 567
Cdd:PRK05691 1460 ELNLLPPGVAGELCIGGAGLARGYLGRPALTAerfvpdpLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKL-RGFRV 1538
|
170 180 190
....*....|....*....|....*....|...
gi 528467778 568 APEKIENIYIRSDPVAQ--VFVHGDSLQACLVG 598
Cdd:PRK05691 1539 EPEEIQARLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
457-605 |
1.07e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 48.89 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 457 YGQTEctAGCTMS-LP--GDWTAGHVGAPLPCNF------VKLVDvAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSG 527
Cdd:PRK10252 749 YGPTE--AAVDVSwYPafGEELAAVRGSSVPIGYpvwntgLRILD-ARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTAS 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 528 ------AVDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIyIRSDP-VAQVFVH-----------G 589
Cdd:PRK10252 826 rfiadpFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKI-RGQRIELGEIDRA-MQALPdVEQAVTHacvinqaaatgG 903
|
170
....*....|....*.
gi 528467778 590 DSLQacLVGVVVPDPD 605
Cdd:PRK10252 904 DARQ--LVGYLVSQSG 917
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
264-606 |
1.07e-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: 45.07 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 264 PKPEDLALICfTSGTTGNPKGAMLTHGnvvsncsafikitevhcmlnqtDIHISYLPLAHMFERVVEGVLLCHGAKIgyf 343
Cdd:cd05924 1 RSADDLYILY-TGGTTGMPKGVMWRQE----------------------DIFRMLMGGADFGTGEFTPSEDAHKAAA--- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 344 qgdirllmddlKNLKPTIFPVVP-----RLLNRMFDKIFGQAnTPLKRWLLDFATSRKEAE---LKSGVVRKDSMWDKLI 415
Cdd:cd05924 55 -----------AAAGTVMFPAPPlmhgtGSWTAFGGLLGGQT-VVLPDDRFDPEEVWRTIEkhkVTSMTIVGDAMARPLI 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 416 --FSKVQASLGGRVRLMITGAAPVSPTVLT-FLRAALGCQFYEGYGQTECTAGCT-MSLPGDWTAGHVGAPLPCNFVKLV 491
Cdd:cd05924 123 daLRDAGPYDLSSLFAISSGGALLSPEVKQgLLELVPNITLVDAFGSSETGFTGSgHSAGSGPETGPFTRANPDTVVLDD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 492 DVAEMNYfAANGEGEVCVKGpNVFQGYLKDPEQTSGA---VDKAGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIA 568
Cdd:cd05924 203 DGRVVPP-GSGGVGWIARRG-HIPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTG-GEKVF 279
|
330 340 350
....*....|....*....|....*....|....*....
gi 528467778 569 PEKIENIyIRSDP-VAQVFVHGdslqaclvgvvVPDPDF 606
Cdd:cd05924 280 PEEVEEA-LKSHPaVYDVLVVG-----------RPDERW 306
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
267-323 |
1.76e-04 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 44.87 E-value: 1.76e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 528467778 267 EDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEvhcmLNQTDIHISYLPLAH 323
Cdd:PRK08279 199 KDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLR----LTPDDVLYCCLPLYH 251
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
256-556 |
2.00e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 44.55 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 256 ANHKTPIPPKP-EDLALICFTSGTTGNPKGAMLTHGNVVSNC----SAFIKITEVHCMLNQTdiHISYLPLAH-Mfervv 329
Cdd:PRK05850 148 SPRGSDARPRDlPSTAYLQYTSGSTRTPAGVMVSHRNVIANFeqlmSDYFGDTGGVPPPDTT--VVSWLPFYHdM----- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 330 eGVLLchGAKIGYFQGDIRLLMddlknlKPTIFpvvprlLNRmfdkifgqantPlKRWLLDFATSRKEA--------ELk 401
Cdd:PRK05850 221 -GLVL--GVCAPILGGCPAVLT------SPVAF------LQR-----------P-ARWMQLLASNPHAFsaapnfafEL- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 402 sgVVRKDSMWDklifskvQASLG-GRVRLMITGAAPVSP-TVLTFLR--AALGcqFYE-----GYGQTECTAGCTMSLPG 472
Cdd:PRK05850 273 --AVRKTSDDD-------MAGLDlGGVLGIISGSERVHPaTLKRFADrfAPFN--LREtairpSYGLAEATVYVATREPG 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 473 D-----------WTAGHV-------GAPL------PCNFVKLVDVAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQT--- 525
Cdd:PRK05850 342 QppesvrfdyekLSAGHAkrcetggGTPLvsygspRSPTVRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETert 421
|
330 340 350
....*....|....*....|....*....|....*....
gi 528467778 526 --------SGAVDKAGWLHTGDIGkWLPNGTLKIIDRKK 556
Cdd:PRK05850 422 fgatlvdpSPGTPEGPWLRTGDLG-FISEGELFIVGRIK 459
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
262-606 |
2.46e-04 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 44.36 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 262 IPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEvhcMLNQTDIHISylplAHMF------ERVVEGVLLC 335
Cdd:PRK13382 191 PEPTGRKGRVILLTSGTTGTPKGARRSGPGGIGTLKAILDRTP---WRAEEPTVIV----APMFhawgfsQLVLAASLAC 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 336 HGAKIGYFQGDIRLLMDDlKNlKPTIFPVVPRllnrMFDKIFgqantplkrwlldfatsrkeaELKSGVVRKDSmwdkli 415
Cdd:PRK13382 264 TIVTRRRFDPEATLDLID-RH-RATGLAVVPV----MFDRIM---------------------DLPAEVRNRYS------ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 416 fskvqaslGGRVRLMITGAAPVSPTVLTFLRAALGCQFYEGYGQTEctAG-CTMSLPGDWTAG--HVGAPLPCNFVKLVD 492
Cdd:PRK13382 311 --------GRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATE--AGmIATATPADLRAApdTAGRPAEGTEIRILD 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 493 vAEMNYFAaNGE-GEVCVKGPNVFQGYlkdpeqTSGAvDK---AGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIA 568
Cdd:PRK13382 381 -QDFREVP-TGEvGTIFVRNDTQFDGY------TSGS-TKdfhDGFMASGDVGYLDENGRLFVVGRDDEMI-VSGGENVY 450
|
330 340 350
....*....|....*....|....*....|....*...
gi 528467778 569 PEKIENIYIRSDPVAQVFVHGdslqaclvgvvVPDPDF 606
Cdd:PRK13382 451 PIEVEKTLATHPDVAEAAVIG-----------VDDEQY 477
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
260-323 |
1.13e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 42.02 E-value: 1.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528467778 260 TPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIKITEvhcmLNQTDIHISYLPLAH 323
Cdd:PRK07769 173 VPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALE----GQEGDRGVSWLPFFH 232
|
|
| 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 528467778 266 PEDLALICFTSGTTGNPKGAMLTHGNVVSNCSAFIK 301
Cdd:PRK05691 2332 PQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIE 2367
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
249-597 |
1.68e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.08 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 249 ELEAIGKANHKTPIPPKPEDLALICFTSGTTGNPKGAMLTHGNVVSNCSA---FIKITEvHCMLNQT-----DIHISYLP 320
Cdd:PRK05691 3851 EVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSkvpYLALSE-ADVIAQTasqsfDISVWQFL 3929
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 321 LAHMFervvegvllchGAKIGYFQGDI----RLLMDDLKNLKPTIFPVVPRLLNRMfdkifgqantplkrwlldfatsrk 396
Cdd:PRK05691 3930 AAPLF-----------GARVEIVPNAIahdpQGLLAHVQAQGITVLESVPSLIQGM------------------------ 3974
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 397 eaelksgvvrkdsmwdkliFSKVQASLGGrVRLMI-TGAAPVSPTVLTFLRAALGCQFYEGYGQTECT---------AGC 466
Cdd:PRK05691 3975 -------------------LAEDRQALDG-LRWMLpTGEAMPPELARQWLQRYPQIGLVNAYGPAECSddvaffrvdLAS 4034
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467778 467 TMS--LPgdwtaghVGAPLPCNFVKLVDVAeMNYFAANGEGEVCVKGPNVFQGYLKDPEQTS--------GAVDKAGWlH 536
Cdd:PRK05691 4035 TRGsyLP-------IGSPTDNNRLYLLDEA-LELVPLGAVGELCVAGTGVGRGYVGDPLRTAlafvphpfGAPGERLY-R 4105
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528467778 537 TGDIGKWLPNGTLKIIDRKKHI-----FKLAQGEyIAPEKIENIYIRSDPVA-QVFVHGDSLQACLV 597
Cdd:PRK05691 4106 TGDLARRRSDGVLEYVGRIDHQvkirgYRIELGE-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 528467778 452 QFYEGYGQTECTAgCTMSLPGDWTAGHVGAPLPCNFVKL-VDVAEMNYFAANGEGEVCVKGPNVFQGYLKDPEQTSgAVD 530
Cdd:PRK07638 281 KLYEFYGASELSF-VTALVDEESERRPNSVGRPFHNVQVrICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLAR-ELN 358
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528467778 531 KAGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSDPVAQVFVHGdslqaclvgvvVPDP 604
Cdd:PRK07638 359 ADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIESVLHEHPAVDEIVVIG-----------VPDS 420
|
|
| |
