|
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 ... |
111-688 |
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: 794.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 111 EWEWISYDQAFETSDHASQAIRKLGIEIGEESKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDDMHYITNLCEIS 190
Cdd:cd05927 2 PYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 191 LMFVDAeiktkqlirdksylsslkyivqfnecsddikemarenDFRLWSFNEFVEMGKKQKHrPHVPPTPETLATISFTS 270
Cdd:cd05927 82 IVFCDA-------------------------------------GVKVYSLEEFEKLGKKNKV-PPPPPKPEDLATICYTS 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 271 GTTGRPKGVMLTHLNMCSATMSCEEFENEA---GVQDAYLSYLPLAHIYERLCLLSNFMIGSRIGFSRGDPKLLVDDVQA 347
Cdd:cd05927 124 GTTGNPKGVMLTHGNIVSNVAGVFKILEILnkiNPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDIKA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 348 LAPRSFATVPRVIDKIHKAVMKQVQDK-PLKKMILNAAIAYKLYHYKMtGKATRKTWVDKYVLHKIQMLLGPNIRQLILG 426
Cdd:cd05927 204 LKPTVFPGVPRVLNRIYDKIFNKVQAKgPLKRKLFNFALNYKLAELRS-GVVRASPFWDKLVFNKIKQALGGNVRLMLTG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 427 AAKSDVSAMRFARGAFGVEVLEGYGQTETSGPTTLQLVGDTRIGCVGPPMACAMIKLIDVPELGYSVDKN--GGEVLVKG 504
Cdd:cd05927 283 SAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAKDPnpRGEVCIRG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 505 HNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMPQGKFVAPDLTESLYTSSSFVQQIYVHGDM 584
Cdd:cd05927 363 PNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGDS 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 585 EKPWLVAIVVPDPEYLASYALTKHNInGKTYEQLCNIPILADDVLRQFVELTEEDKRPRYEGVYGVHLTPVAFSAENGLT 664
Cdd:cd05927 443 LKSFLVAIVVPDPDVLKEWAASKGGG-TGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLL 521
|
570 580
....*....|....*....|....
gi 17541856 665 TPTLKNKRNAIAQFFKAEIDGMYK 688
Cdd:cd05927 522 TPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
103-689 |
8.24e-165 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 486.92 E-value: 8.24e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 103 RVMKDGklEWEWISYDQAFETSDHASQAIRKLGIEIGEesKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDDMHY 182
Cdd:COG1022 31 REKEDG--IWQSLTWAEFAERVRALAAGLLALGVKPGD--RVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVAY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 183 ITNLCEISLMFV-DAEIKTKQL-IRDKsyLSSLKYIVQFNEcsddikeMARENDFRLWSFNEFVEMGKKQKHRPHVP--- 257
Cdd:COG1022 107 ILNDSGAKVLFVeDQEQLDKLLeVRDE--LPSLRHIVVLDP-------RGLRDDPRLLSLDELLALGREVADPAELEarr 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 258 --PTPETLATISFTSGTTGRPKGVMLTHLNMCSATMSCEEFENeAGVQDAYLSYLPLAHIYERLCLLSNFMIGSRIGFSR 335
Cdd:COG1022 178 aaVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLP-LGPGDRTLSFLPLAHVFERTVSYYALAAGATVAFAE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 336 gDPKLLVDDVQALAPRSFATVPRVIDKIHKAVMKQVQDKP-LKKMILNAA--IAYKLYHYKMTGKATR-----KTWV-DK 406
Cdd:COG1022 257 -SPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGgLKRKLFRWAlaVGRRYARARLAGKSPSlllrlKHALaDK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 407 YVLHKIQMLLGPNIRQLILGAAKSDVSAMRFARGAfGVEVLEGYGQTETSGPTTLQLVGDTRIGCVGPPMACAMIKLIDv 486
Cdd:COG1022 336 LVFSKLREALGGRLRFAVSGGAALGPELARFFRAL-GIPVLEGYGLTETSPVITVNRPGDNRIGTVGPPLPGVEVKIAE- 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 487 pelgysvDkngGEVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMPQGKFVAPDLTE 566
Cdd:COG1022 414 -------D---GEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIVTSGGKNVAPQPIE 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 567 SLYTSSSFVQQIYVHGDmEKPWLVAIVVPDPEYLASYAlTKHNINGKTYEQLCNIPILADDVLRQFVELTEEdkRPRYEG 646
Cdd:COG1022 484 NALKASPLIEQAVVVGD-GRPFLAALIVPDFEALGEWA-EENGLPYTSYAELAQDPEVRALIQEEVDRANAG--LSRAEQ 559
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 17541856 647 VYGVHLTPVAFSAENGLTTPTLKNKRNAIAQFFKAEIDGMYKK 689
Cdd:COG1022 560 IKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYAG 602
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
100-690 |
1.86e-153 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 459.56 E-value: 1.86e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 100 LGKRVMKDGKL-EWEWISYDQAFETSDHASQAIRKLGIEigEESKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITND 178
Cdd:PLN02736 63 LGTRIRVDGTVgEYKWMTYGEAGTARTAIGSGLVQHGIP--KGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 179 DMHYITNLCEISLMFVDAEiKTKQLIRDKSYLSSLKYIVQFNECSDDIKEMARENDFRLWSFNEFVEMGKKQkHRPHVPP 258
Cdd:PLN02736 141 AVKFIVNHAEVAAIFCVPQ-TLNTLLSCLSEIPSVRLIVVVGGADEPLPSLPSGTGVEIVTYSKLLAQGRSS-PQPFRPP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 259 TPETLATISFTSGTTGRPKGVMLTHLNM-CSATMSCeeFENEAGVQDAYLSYLPLAHIYERLCLLSNFMIGSRIGFSRGD 337
Cdd:PLN02736 219 KPEDVATICYTSGTTGTPKGVVLTHGNLiANVAGSS--LSTKFYPSDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGD 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 338 PKLLVDDVQALAPRSFATVPRVIDKIHKAVMKQVQDK-PLKKMILNAAIAYKlYHYKMTGKATRKTWvDKYVLHKIQMLL 416
Cdd:PLN02736 297 NLKLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESgGLKERLFNAAYNAK-KQALENGKNPSPMW-DRLVFNKIKAKL 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 417 GPNIRQLILGAAKSDVSAMRFARGAFGVEVLEGYGQTETSGPTTLQLVGDTRIGCVGPPMACAMIKLIDVPELGY-SVDK 495
Cdd:PLN02736 375 GGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNYtSEDQ 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 496 N--GGEVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMPQGKFVAPDLTESLYTSSS 573
Cdd:PLN02736 455 PypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCK 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 574 FVQQIYVHGDMEKPWLVAIVVPDPEYLASYAlTKHNINGKTYEQLCNIPILADDVLRQFVELTEEDKRPRYEGVYGVHLT 653
Cdd:PLN02736 535 FVAQCFVYGDSLNSSLVAVVVVDPEVLKAWA-ASEGIKYEDLKQLCNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLV 613
|
570 580 590
....*....|....*....|....*....|....*..
gi 17541856 654 PVAFSAENGLTTPTLKNKRNAIAQFFKAEIDGMYKKI 690
Cdd:PLN02736 614 PEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYAEL 650
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
96-691 |
2.31e-137 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 418.45 E-value: 2.31e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 96 GKEMLGKRVMKDGKL-EWEWISYDQAFETSDHASQAIRKLGIEIGeeSKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDT 174
Cdd:PLN02430 57 DNKMLGWRRIVDGKVgPYMWKTYKEVYEEVLQIGSALRASGAEPG--SRVGIYGSNCPQWIVAMEACAAHSLICVPLYDT 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 175 ITNDDMHYITNLCEISLMFVDaEIKTKQLIR-DKSYLSSLKYIVQFNECSDDIKEMARENDFRLWSFNEFVEMGKKQKHR 253
Cdd:PLN02430 135 LGPGAVDYIVDHAEIDFVFVQ-DKKIKELLEpDCKSAKRLKAIVSFTSVTEEESDKASQIGVKTYSWIDFLHMGKENPSE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 254 PHvPPTPETLATISFTSGTTGRPKGVMLTHLNMCSATMSC----EEFENEAGVQDAYLSYLPLAHIYERLCLLSNFMIGS 329
Cdd:PLN02430 214 TN-PPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVdlfmEQFEDKMTHDDVYLSFLPLAHILDRMIEEYFFRKGA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 330 RIGFSRGDPKLLVDDVQALAPRSFATVPRVIDKIHKAVMKQVQD-KPLKKMILNAAIAYKLYHykMTGKATRKT---WVD 405
Cdd:PLN02430 293 SVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKALQElNPRRRLIFNALYKYKLAW--MNRGYSHKKaspMAD 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 406 KYVLHKIQMLLGPNIRQLILGAAKSDVSAMRFARGAFGVEVLEGYGQTETSGPTTLQLVGD-TRIGCVGPPMACAMIKLI 484
Cdd:PLN02430 371 FLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEmCMLGTVGAPAVYNELRLE 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 485 DVPELGYSV--DKNGGEVLVKGHNVTSGYYKNPEATASSFtEDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMPQGKFVAP 562
Cdd:PLN02430 451 EVPEMGYDPlgEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVAL 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 563 DLTESLYTSSSFVQQIYVHGDMEKPWLVAIVVPDPEYLASYAltKHNINGKTYEQLCNIPILADDVLRQFVELTEEDKRP 642
Cdd:PLN02430 530 EYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWA--KDNGFTGSFEELCSLPELKEHILSELKSTAEKNKLR 607
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 17541856 643 RYEGVYGVHLTPVAFSAENGLTTPTLKNKRNAIAQFFKAEIDGMYKKIE 691
Cdd:PLN02430 608 GFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMYRKLA 656
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
111-675 |
1.31e-126 |
|
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: 383.48 E-value: 1.31e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 111 EWEWISYDQAFETSDHASQAIRKLGIEIGEesKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDDMHYITNLCEIS 190
Cdd:cd05907 2 VWQPITWAEFAEEVRALAKGLIALGVEPGD--RVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 191 LMFVDaeiktkqlirdksylsslkyivqfnecsddikemarendfrlwsfnefvemgkkqkhrphvppTPETLATISFTS 270
Cdd:cd05907 80 ALFVE---------------------------------------------------------------DPDDLATIIYTS 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 271 GTTGRPKGVMLTHLNMCSATMSCEEFEnEAGVQDAYLSYLPLAHIYERLCLLSNFMI-GSRIGFSRgDPKLLVDDVQALA 349
Cdd:cd05907 97 GTTGRPKGVMLSHRNILSNALALAERL-PATEGDRHLSFLPLAHVFERRAGLYVPLLaGARIYFAS-SAETLLDDLSEVR 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 350 PRSFATVPRVIDKIHKAVmKQVQDKPLKKMILNAAIayklyhykmtgkatrktwvdkyvlhkiqmllGPNIRQLILGAAK 429
Cdd:cd05907 175 PTVFLAVPRVWEKVYAAI-KVKAVPGLKRKLFDLAV-------------------------------GGRLRFAASGGAP 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 430 SDVSAMRFARGAfGVEVLEGYGQTETSGPTTLQLVGDTRIGCVGPPMACAMIKLIDVpelgysvdkngGEVLVKGHNVTS 509
Cdd:cd05907 223 LPAELLHFFRAL-GIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIADD-----------GEILVRGPNVML 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 510 GYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMPQGKFVAPDLTESLYTSSSFVQQIYVHGDmEKPWL 589
Cdd:cd05907 291 GYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGD-GRPFL 369
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 590 VAIVVPDPEYLASYAlTKHNINGKTYEQLCNIPILADDVLRQFVELTEEdkRPRYEGVYGVHLTPVAFSAENGLTTPTLK 669
Cdd:cd05907 370 VALIVPDPEALEAWA-EEHGIAYTDVAELAANPAVRAEIEAAVEAANAR--LSRYEQIKKFLLLPEPFTIENGELTPTLK 446
|
....*.
gi 17541856 670 NKRNAI 675
Cdd:cd05907 447 LKRPVI 452
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
111-675 |
9.21e-123 |
|
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: 375.40 E-value: 9.21e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 111 EWEWISYDQAFETSDHASQAIRKLGIEigEESKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDDMHYITNLCEIS 190
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLVELGLK--PGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 191 LMFVDaeiktkqlirdksylsslkyivqfnecsddikemarendfrlwsfnefvemgkkqkhrphvpPTPETLATISFTS 270
Cdd:cd17639 80 AIFTD--------------------------------------------------------------GKPDDLACIMYTS 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 271 GTTGRPKGVMLTHLNMCSATMSCEEFENEA-GVQDAYLSYLPLAHIYERLCLLSNFMIGSRIGFsrGDPKLLVD------ 343
Cdd:cd17639 98 GSTGNPKGVMLTHGNLVAGIAGLGDRVPELlGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDkskrgc 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 344 --DVQALAPRSFATVPRVIDKIHKAVMKQVQDKP-LKKMILNAAIAYKLYHYKMtGKATrkTWVDKYVLHKIQMLLGPNI 420
Cdd:cd17639 176 kgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGgLKRTLFWTAYQSKLKALKE-GPGT--PLLDELVFKKVRAALGGRL 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 421 RQLILGAAKSDVSAMRFARgAFGVEVLEGYGQTETSGPTTLQLVGDTRIGCVGPPMACAMIKLIDVPELGYSVDK--NGG 498
Cdd:cd17639 253 RYMLSGGAPLSADTQEFLN-IVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDKppPRG 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 499 EVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMPQGKFVAPDLTESLYTSSSFVQQI 578
Cdd:cd17639 332 EILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVNNI 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 579 YVHGDMEKPWLVAIVVPDPEYLASYAlTKHNINGKTYEQLCNIPILADDVLRQFVELTEEDKRPRYEGVYGVHLTPVAFS 658
Cdd:cd17639 412 CVYADPDKSYPVAIVVPNEKHLTKLA-EKHGVINSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEWT 490
|
570
....*....|....*..
gi 17541856 659 AENGLTTPTLKNKRNAI 675
Cdd:cd17639 491 PENGLVTAAQKLKRKEI 507
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
98-688 |
1.66e-115 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 361.47 E-value: 1.66e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 98 EMLGKRVMKDGKL-EWEWISYDQAFETSDHASQAIRKLGIEIGEesKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTIT 176
Cdd:PLN02861 60 QMLGRRQVTDSKVgPYVWLTYKEVYDAAIRIGSAIRSRGVNPGD--RCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 177 NDDMHYITNLCEISLMFVDAEIKTKQLIRDKSYLSSLKYIVQFNECSDDIKEMARENDFRLWSFNEFVEMGKKQKHRPhv 256
Cdd:PLN02861 138 ANAVEFIINHAEVSIAFVQESKISSILSCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLDCELP-- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 257 PPTPETLATISFTSGTTGRPKGVMLTHLNMCSATMSCEEF----ENEAGVQDAYLSYLPLAHIYERLclLSNFMI--GSR 330
Cdd:PLN02861 216 PKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLlkvtDRVATEEDSYFSYLPLAHVYDQV--IETYCIskGAS 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 331 IGFSRGDPKLLVDDVQALAPRSFATVPRVIDKIHKAVMKQVQDK-PLKKMILNAAIAYKL-YHYKMTGKATRKTWVDKYV 408
Cdd:PLN02861 294 IGFWQGDIRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQKISSGgMLRKKLFDFAYNYKLgNLRKGLKQEEASPRLDRLV 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 409 LHKIQMLLGPNIRQLILGAAKSDVSAMRFARGAFGVEVLEGYGQTETSGPTTLQLVGD-TRIGCVGPPMACAMIKLIDVP 487
Cdd:PLN02861 374 FDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGCFTSIANVfSMVGTVGVPMTTIEARLESVP 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 488 ELGYSVDKN--GGEVLVKGHNVTSGYYKNPEATASSFTeDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMPQGKFVAPDLT 565
Cdd:PLN02861 454 EMGYDALSDvpRGEICLRGNTLFSGYHKRQDLTEEVLI-DGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENL 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 566 ESLYTSSSFVQQIYVHGDMEKPWLVAIVVPDPEYLASYAlTKHNINGKtYEQLCNIPILADDVLRQFVELTEEDKRPRYE 645
Cdd:PLN02861 533 ENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWA-ANNNKTGD-FKSLCKNLKARKYILDELNSTGKKLQLRGFE 610
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 17541856 646 GVYGVHLTPVAFSAENGLTTPTLKNKRNAIAQFFKAEIDGMYK 688
Cdd:PLN02861 611 MLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYS 653
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
99-693 |
2.88e-115 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 361.26 E-value: 2.88e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 99 MLGKRVMKDGKL-EWEWISYDQAFETSDHASQAIRKLGIEigEESKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITN 177
Cdd:PLN02614 63 MLGRREIVDGKPgKYVWQTYQEVYDIVIKLGNSLRSVGVK--DEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 178 DDMHYITNLCEISLMFVDaEIKTKQLIrdKSYLSSLKY---IVQFNECSDDIKEMARENDFRLWSFNEFVEMGKKQKHRP 254
Cdd:PLN02614 141 GAVEFIISHSEVSIVFVE-EKKISELF--KTCPNSTEYmktVVSFGGVSREQKEEAETFGLVIYAWDEFLKLGEGKQYDL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 255 HVPpTPETLATISFTSGTTGRPKGVMLTHLNMCSATMSCEEF---ENEA-GVQDAYLSYLPLAHIYERLCLLSNFMIGSR 330
Cdd:PLN02614 218 PIK-KKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLlksANAAlTVKDVYLSYLPLAHIFDRVIEECFIQHGAA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 331 IGFSRGDPKLLVDDVQALAPRSFATVPRVIDKIHKAVMKQVQDKP-LKKMILNAAIAYKL-YHYKMTGKATRKTWVDKYV 408
Cdd:PLN02614 297 IGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGfLKKFVFDSAFSYKFgNMKKGQSHVEASPLCDKLV 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 409 LHKIQMLLGPNIRQLILGAAKSDVSAMRFARGAFGVEVLEGYGQTETSGPTTLQLVGDT-RIGCVGPPMACAMIKLIDVP 487
Cdd:PLN02614 377 FNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELdMLGTVGPPVPNVDIRLESVP 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 488 ELGYSV--DKNGGEVLVKGHNVTSGYYKNPEATASSFTeDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMPQGKFVAPDLT 565
Cdd:PLN02614 457 EMEYDAlaSTPRGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENI 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 566 ESLYTSSSFVQQIYVHGDMEKPWLVAIVVPDPEYLASYAlTKHNINGKtYEQLCNIPILADDVLRQFVELTEEDKRPRYE 645
Cdd:PLN02614 536 ENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWA-AENGVSGD-YNALCQNEKAKEFILGELVKMAKEKKMKGFE 613
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 17541856 646 GVYGVHLTPVAFSAENGLTTPTLKNKRNAIAQFFKAEIDGMYKKIETS 693
Cdd:PLN02614 614 IIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYKTTNEK 661
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
111-553 |
8.46e-105 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 325.81 E-value: 8.46e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 111 EWEWISYDQAFETSDHASQAIRKLGIEIGEesKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDDMHYITNLCEIS 190
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRALGVGKGD--RVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 191 LMFVDAEIKTKQLIRDKSYLSSLKYIVqfneCSDDikemareNDFRLWSFNEFVEMGKKQKHRPHVPPTPETLATISFTS 270
Cdd:pfam00501 96 VLITDDALKLEELLEALGKLEVVKLVL----VLDR-------DPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYTS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 271 GTTGRPKGVMLTHLNMCSATMSCEEFENEA---GVQDAYLSYLPLAHIYER-LCLLSNFMIGSRIGFSRG----DPKLLV 342
Cdd:pfam00501 165 GTTGKPKGVMLTHRNLVANVLSIKRVRPRGfglGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGfpalDPAALL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 343 DDVQALAPRSFATVPRVIDkihkavmkqvqdkplkkMILNAAiayklyhykmtgkatrktwvdkyvlhKIQMLLGPNIRQ 422
Cdd:pfam00501 245 ELIERYKVTVLYGVPTLLN-----------------MLLEAG--------------------------APKRALLSSLRL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 423 LILGAAKSDVSAMRFARGAFGVEVLEGYGQTETSGPTTLQLVGDTR---IGCVGPPMACAMIKLIDVPELGYSVDKNGGE 499
Cdd:pfam00501 282 VLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEDlrsLGSVGRPLPGTEVKIVDDETGEPVPPGEPGE 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 17541856 500 VLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFK 553
Cdd:pfam00501 362 LCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIK 415
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
111-687 |
3.87e-96 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 312.05 E-value: 3.87e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 111 EWEWISYDQAFE-TSDHASQAIRklgIEIGEESKIGIYSNNRPEWILSEMAI--HNFSNVSVplYDTITNDDMHYITNLC 187
Cdd:PLN02387 103 EYEWITYGQVFErVCNFASGLVA---LGHNKEERVAIFADTRAEWLIALQGCfrQNITVVTI--YASLGEEALCHSLNET 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 188 EISLMFVDAEiKTKQLIRDKSYLSSLKYIVQFNECSDDIKEMAREN-DFRLWSFNEFVEMGKKQKHRPHVPpTPETLATI 266
Cdd:PLN02387 178 EVTTVICDSK-QLKKLIDISSQLETVKRVIYMDDEGVDSDSSLSGSsNWTVSSFSEVEKLGKENPVDPDLP-SPNDIAVI 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 267 SFTSGTTGRPKGVMLTHLNMCSATMSCEEFENEAGVQDAYLSYLPLAHIYERLCLLSNFMIGSRIGFsrGDPKLLVD--- 343
Cdd:PLN02387 256 MYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDtsn 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 344 --------DVQALAPRSFATVPRVIDKIHKAVMKQVQDKplkkmilnAAIAYKLYH--YKMTGKATRKTWV--------- 404
Cdd:PLN02387 334 kikkgtkgDASALKPTLMTAVPAILDRVRDGVRKKVDAK--------GGLAKKLFDiaYKRRLAAIEGSWFgawglekll 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 405 -DKYVLHKIQMLLGPNIRQLILGAAKSDVSAMRFARGAFGVEVLEGYGQTETSGPTTLQLVGDTRIGCVGPPMACAMIKL 483
Cdd:PLN02387 406 wDALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKL 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 484 IDVPELGYSV-DKNG--GEVLVKGHNVTSGYYKNPEATASSFTEDG----YMKTGDIGRFTAEGSLQIIDRRKNVFKMPQ 556
Cdd:PLN02387 486 VSWEEGGYLIsDKPMprGEIVIGGPSVTLGYFKNQEKTDEVYKVDErgmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQH 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 557 GKFVAPDLTESLYTSSSFVQQIYVHGDMEKPWLVAIVVPDPEYLASYAlTKHNINGKTYEQLCNIPILADDVLRQFVELT 636
Cdd:PLN02387 566 GEYVSLGKVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWA-KKAGIDYSNFAELCEKEEAVKEVQQSLSKAA 644
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 17541856 637 EEDKRPRYEGVYGVHLTPVAFSAENGLTTPTLKNKRNAIAQFFKAEIDGMY 687
Cdd:PLN02387 645 KAARLEKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLY 695
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
115-675 |
2.15e-75 |
|
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: 250.35 E-value: 2.15e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 115 ISYDQAFETSDHASQAIRKLGIEIGEesKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDDMHYITNLCEISLMFV 194
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGE--KVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 195 daeiktkqlirdksylsslkyivqfnecsddikemarENDfrlwsfnefvemgkkqkhrphvpptPETLATISFTSGTTG 274
Cdd:cd17640 84 -------------------------------------END-------------------------SDDLATIIYTSGTTG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 275 RPKGVMLTHLNMCSATMSCEEFEnEAGVQDAYLSYLPLAHIYERLCLLSNFMIGSRIGFSrgDPKLLVDDVQALAPRSFA 354
Cdd:cd17640 102 NPKGVMLTHANLLHQIRSLSDIV-PPQPGDRFLSILPIWHSYERSAEYFIFACGCSQAYT--SIRTLKDDLKRVKPHYIV 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 355 TVPRVIDKIHKAVMKQVQDKP-LKKMILNAAiayklyhykmtgkatrktwvdkyvlhkiqmLLGPNIRQLILGAAKSDVS 433
Cdd:cd17640 179 SVPRLWESLYSGIQKQVSKSSpIKQFLFLFF------------------------------LSGGIFKFGISGGGALPPH 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 434 AMRFARgAFGVEVLEGYGQTETSGPTTLQLVGDTRIGCVGPPMACAMIKLIDvpELGYSVDKNG--GEVLVKGHNVTSGY 511
Cdd:cd17640 229 VDTFFE-AIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVD--PEGNVVLPPGekGIVWVRGPQVMKGY 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 512 YKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMPQGKFVAPDLTESLYTSSSFVQQIYVHGDMEKpWLVA 591
Cdd:cd17640 306 YKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQK-RLGA 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 592 IVVPDPEYLASYAltkHNINGKTYEQLcnIPILADDVLRQFVE---LTEEDKRPRY---EGVYGVHLTPVAFSaENGLTT 665
Cdd:cd17640 385 LIVPNFEELEKWA---KESGVKLANDR--SQLLASKKVLKLYKneiKDEISNRPGFksfEQIAPFALLEEPFI-ENGEMT 458
|
570
....*....|
gi 17541856 666 PTLKNKRNAI 675
Cdd:cd17640 459 QTMKIKRNVV 468
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
112-677 |
1.45e-73 |
|
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: 248.49 E-value: 1.45e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 112 WEWISYDQAFETSDHASQAIRKLGIEIGEesKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDDMHYITNLCEISL 191
Cdd:cd17641 9 WQEFTWADYADRVRAFALGLLALGVGRGD--VVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 192 MFVDAEIKTKQLIRDKSYLSSLKYIVQFNEcsddiKEMARENDFRLWSFNEFVEMGKKQKHR-PHV------PPTPETLA 264
Cdd:cd17641 87 VIAEDEEQVDKLLEIADRIPSVRYVIYCDP-----RGMRKYDDPRLISFEDVVALGRALDRRdPGLyerevaAGKGEDVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 265 TISFTSGTTGRPKGVMLTHLNMCSATMSCEEFEnEAGVQDAYLSYLPLAHIYERLCLLSNFMI-GSRIGFSRgDPKLLVD 343
Cdd:cd17641 162 VLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAAD-PLGPGDEYVSVLPLPWIGEQMYSVGQALVcGFIVNFPE-EPETMME 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 344 DVQALAPRSFATVPRVIDKIHKAVMKQVQDK-PLKKMILNAAI--AYKLYHYKMTGKATRKTWVDKYVLHKiQMLLGPNI 420
Cdd:cd17641 240 DLREIGPTFVLLPPRVWEGIAADVRARMMDAtPFKRFMFELGMklGLRALDRGKRGRPVSLWLRLASWLAD-ALLFRPLR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 421 RQLILGAAKSDVSA--------MRFARgAFGVEVLEGYGQTETSGPTTLQLVGDTRIGCVGPPMACAMIKLIDVpelgys 492
Cdd:cd17641 319 DRLGFSRLRSAATGgaalgpdtFRFFH-AIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEV------ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 493 vdkngGEVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMPQGKFVAPDLTESLYTSS 572
Cdd:cd17641 392 -----GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKFS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 573 SFVQQIYVHGDmEKPWLVAIVVPDPEYLASYAlTKHNINGKTYEQLCNIP----ILADDVLRQFVELTEEDKRPRYEgvy 648
Cdd:cd17641 467 PYIAEAVVLGA-GRPYLTAFICIDYAIVGKWA-EQRGIAFTTYTDLASRPevyeLIRKEVEKVNASLPEAQRIRRFL--- 541
|
570 580
....*....|....*....|....*....
gi 17541856 649 gvhLTPVAFSAENGLTTPTLKNKRNAIAQ 677
Cdd:cd17641 542 ---LLYKELDADDGELTRTRKVRRGVIAE 567
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
116-675 |
4.32e-70 |
|
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: 237.37 E-value: 4.32e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 116 SYDQAFETSDHASQAIRKLGIEIGeeSKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDDMHYITNLCEISLMFV- 194
Cdd:cd05932 8 TWGEVADKARRLAAALRALGLEPG--SKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 195 --DAEIKTKQLIRDKSYLSSLKYivqfnecsddikeMARENDFRLWSfnEFVEMGKKQKHRPhvPPTPETLATISFTSGT 272
Cdd:cd05932 86 klDDWKAMAPGVPEGLISISLPP-------------PSAANCQYQWD--DLIAQHPPLEERP--TRFPEQLATLIYTSGT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 273 TGRPKGVMLTHLNMcsaTMSCEEFENEAGV--QDAYLSYLPLAHIYERLCL-LSNFMIGSRIGFSRG-DPklLVDDVQAL 348
Cdd:cd05932 149 TGQPKGVMLTFGSF---AWAAQAGIEHIGTeeNDRMLSYLPLAHVTERVFVeGGSLYGGVLVAFAESlDT--FVEDVQRA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 349 APRSFATVPRVIDKIHKAVMKQVqdkPLKKMILNAAIAYklyhykmtgkatrktwVDKYVLHKIQMLLGPN-IRQLILGA 427
Cdd:cd05932 224 RPTLFFSVPRLWTKFQQGVQDKI---PQQKLNLLLKIPV----------------VNSLVKRKVLKGLGLDqCRLAGCGS 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 428 AKSDVSAMRFARgAFGVEVLEGYGQTETSGPTTLQLVGDTRIGCVGPPMACAMIKLIDvpelgysvdknGGEVLVKGHNV 507
Cdd:cd05932 285 APVPPALLEWYR-SLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEILVRSPAL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 508 TSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMPQGKFVAPDLTESLYTSSSFVQQIYVHG-DMEK 586
Cdd:cd05932 353 MMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGsGLPA 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 587 PwlVAIVVPDPE-YLASYALTKhningKTYEQlcnipiladdVLRQFVELTEEDKRPrYEGVYGVHLTPVAFSAENGLTT 665
Cdd:cd05932 433 P--LALVVLSEEaRLRADAFAR-----AELEA----------SLRAHLARVNSTLDS-HEQLAGIVVVKDPWSIDNGILT 494
|
570
....*....|
gi 17541856 666 PTLKNKRNAI 675
Cdd:cd05932 495 PTLKIKRNVL 504
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
115-689 |
2.30e-69 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 240.26 E-value: 2.30e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 115 ISYDQAFETSDHASQAIRKLGIEigEESKIGIYSNNRPEWILSEMAIHNFSNVSVPLYdtitnddmhyiTNLCEISLMFV 194
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLT--KGSNVAIYEETRWEWLASIYGIWSQSMVAATVY-----------ANLGEDALAYA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 195 DAEIKTKQLIRDKSYLSSLKYIVQFNE-------CSDDIKEMARENDFRLWSFNEFVEMGKKQKHRpHVPPTPE---TLA 264
Cdd:PTZ00216 189 LRETECKAIVCNGKNVPNLLRLMKSGGmpnttiiYLDSLPASVDTEGCRLVAWTDVVAKGHSAGSH-HPLNIPEnndDLA 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 265 TISFTSGTTGRPKGVMLTHLNMCSATMSCEEFENE----AGVQDAYLSYLPLAHIYERLCLLSNFMIGSRIGFsrGDPKL 340
Cdd:PTZ00216 268 LIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLNDligpPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRT 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 341 LVD-------DVQALAPRSFATVPRVIDKIHKAV-MKQVQDKPLKKMILNAAIAYKLYHYKmTGKATrKTWVDKyVLHKI 412
Cdd:PTZ00216 346 LTDtfarphgDLTEFRPVFLIGVPRIFDTIKKAVeAKLPPVGSLKRRVFDHAYQSRLRALK-EGKDT-PYWNEK-VFSAP 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 413 QMLLGPNIRQLILGAAKSDVSAMRFARGAFGVeVLEGYGQTETSGPTTLQLVGDTRIGCVGPPMACAMIKLIDVPELGYS 492
Cdd:PTZ00216 423 RAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDTEEYKHT 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 493 vDKNG--GEVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMPQGKFVAPDLTESLYT 570
Cdd:PTZ00216 502 -DTPEprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEALYG 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 571 SSSFVQQ----IYVHGDmeKPWLVAIVVPDPEYLASYAlTKHNINGkTYEQLCNIPILADDVLRQFVELTEEDKRPRYEG 646
Cdd:PTZ00216 581 QNELVVPngvcVLVHPA--RSYICALVLTDEAKAMAFA-KEHGIEG-EYPAILKDPEFQKKATESLQETARAAGRKSFEI 656
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 17541856 647 VYGVHLTPVAFSAENGLTTPTLKNKRNAIAQFFKAEIDGMYKK 689
Cdd:PTZ00216 657 VRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELFAD 699
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
108-687 |
2.46e-56 |
|
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: 202.20 E-value: 2.46e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 108 GKLEWEWISYDQAFETSDHASQAIRKLGIEigEESKIGIYSNNRPEWILSEM-AIHNfSNVSVPLYDTITNDDMHYITNL 186
Cdd:cd05933 2 RGDKWHTLTYKEYYEACRQAAKAFLKLGLE--RFHGVGILGFNSPEWFIAAVgAIFA-GGIAVGIYTTNSPEACQYVAET 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 187 CEISLMFVDAEIKTKQLIRDKSYLSSLKYIVQFNEcsdDIKEmARENdfrLWSFNEFVEMGK----KQKHRPHVPPTPET 262
Cdd:cd05933 79 SEANILVVENQKQLQKILQIQDKLPHLKAIIQYKE---PLKE-KEPN---LYSWDEFMELGRsipdEQLDAIISSQKPNQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 263 LATISFTSGTTGRPKGVMLTHLNMC----SATMSCEEFENEAGvQDAYLSYLPLAHIYER-----LCLLsnfmIGSRIGF 333
Cdd:cd05933 152 CCTLIYTSGTTGMPKGVMLSHDNITwtakAASQHMDLRPATVG-QESVVSYLPLSHIAAQildiwLPIK----VGGQVYF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 334 SRGDP--KLLVDDVQALAPRSFATVPRVIDKIH-KAVMKQVQDKPLKKMILNAAIAYKLYHY--KMTGKA---TRKTWVD 405
Cdd:cd05933 227 AQPDAlkGTLVKTLREVRPTAFMGVPRVWEKIQeKMKAVGAKSGTLKRKIASWAKGVGLETNlkLMGGESpspLFYRLAK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 406 KYVLHKIQMLLG-PNIRQLILGAAKSDVSAMRFARGaFGVEVLEGYGQTETSGPTTLQLVGDTRIGCVGPPMACAMIKLI 484
Cdd:cd05933 307 KLVFKKVRKALGlDRCQKFFTGAAPISRETLEFFLS-LNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIH 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 485 DVpelgysvDKNG-GEVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMPQGKFVAPD 563
Cdd:cd05933 386 NP-------DADGiGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPV 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 564 LTESLY-TSSSFVQQIYVHGDMEKpwlvaivvpdpeYLASYALTKHNINGKTYEQLCNIPILADDVLRQFVE----LTE- 637
Cdd:cd05933 459 PIEDAVkKELPIISNAMLIGDKRK------------FLSMLLTLKCEVNPETGEPLDELTEEAIEFCRKLGSqatrVSEi 526
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 638 -EDKRPRY-----EGVYGVH--------------LTPVAFSAENGLTTPTLKNKRNAIAQFFKAEIDGMY 687
Cdd:cd05933 527 aGGKDPKVyeaieEGIKRVNkkaisnaqkiqkwvILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
253-665 |
1.52e-54 |
|
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: 196.91 E-value: 1.52e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 253 RPHVPPTPETLATISFTSGTTGRPKGVMLTHLNMcsATMSCEEFENEAGVQDA--YLSYLPLAHIYERLCLLSNFMIGSR 330
Cdd:cd17632 215 LFRPEPDDDPLALLIYTSGSTGTPKGAMYTERLV--ATFWLKVSSIQDIRPPAsiTLNFMPMSHIAGRISLYGTLARGGT 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 331 IGF-SRGDPKLLVDDVQALAPRSFATVPRVIDKIHKAVMKQVQDKplkkmilNAAIAYKLyhykmTGKATRKTWVDkyvl 409
Cdd:cd17632 293 AYFaAASDMSTLFDDLALVRPTELFLVPRVCDMLFQRYQAELDRR-------SVAGADAE-----TLAERVKAELR---- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 410 hkiQMLLGPNIRQLILGAAKsdVSA-MR-FARGAFGVEVLEGYGQTETSGpttlqLVGDTRIgcVGPPMAcaMIKLIDVP 487
Cdd:cd17632 357 ---ERVLGGRLLAAVCGSAP--LSAeMKaFMESLLDLDLHDGYGSTEAGA-----VILDGVI--VRPPVL--DYKLVDVP 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 488 ELGY-SVDKN--GGEVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMPQGKFVAPDL 564
Cdd:cd17632 423 ELGYfRTDRPhpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVAR 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 565 TESLYTSSSFVQQIYVHGDMEKPWLVAIVVPDPEYLAsyaltkhninGKTYEQLcnIPILADDVLRQfveLTEEDKRPrY 644
Cdd:cd17632 503 LEAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDALA----------GEDTARL--RAALAESLQRI---AREAGLQS-Y 566
|
410 420
....*....|....*....|.
gi 17541856 645 EGVYGVHLTPVAFSAENGLTT 665
Cdd:cd17632 567 EIPRDFLIETEPFTIANGLLS 587
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
115-610 |
7.49e-54 |
|
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: 192.27 E-value: 7.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 115 ISYDQAFETSDHASQAIRKLGIEIGEesKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDDMHYITNLCEISLMFv 194
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGD--RVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 195 daeiktkqlirdksylsslkyivqfneCSDdikemarendfrlwsfnefvemgkkqkhrphvpptPETLATISFTSGTTG 274
Cdd:cd05914 85 ---------------------------VSD-----------------------------------EDDVALINYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 275 RPKGVMLTHLNMCSATMSCEEFEnEAGVQDAYLSYLPLAHIYErLC--LLSNFMIGSRIGFSRGDPKLLVDDVQALAPRS 352
Cdd:cd05914 103 NSKGVMLTYRNIVSNVDGVKEVV-LLGKGDKILSILPLHHIYP-LTftLLLPLLNGAHVVFLDKIPSAKIIALAFAQVTP 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 353 FATVPRVIDKIHKAVMKQVQDKPLKKMILN-AAIAYKLYHYKMTGKAtrktwvdkyvLHKIqmlLGPNIRQLILGAAKSD 431
Cdd:cd05914 181 TLGVPVPLVIEKIFKMDIIPKLTLKKFKFKlAKKINNRKIRKLAFKK----------VHEA---FGGNIKEFVIGGAKIN 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 432 VSAMRFARGAfGVEVLEGYGQTETSGPTTLQLVGDTRIGCVGPPmacamIKLIDVPELGYSVDKNGGEVLVKGHNVTSGY 511
Cdd:cd05914 248 PDVEEFLRTI-GFPYTIGYGMTETAPIISYSPPNRIRLGSAGKV-----IDGVEVRIDSPDPATGEGEIIVRGPNVMKGY 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 512 YKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMPQGKFVAPDLTESLYTSSSFV--QQIYV-HGDmekpw 588
Cdd:cd05914 322 YKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVleSLVVVqEKK----- 396
|
490 500
....*....|....*....|..
gi 17541856 589 LVAIVVPDPEYLASYALTKHNI 610
Cdd:cd05914 397 LVALAYIDPDFLDVKALKQRNI 418
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
111-553 |
4.93e-53 |
|
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: 189.64 E-value: 4.93e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 111 EWEWISYDQAFETSDHASQAIRKLGIEIGEesKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDDMHYITNLCEIS 190
Cdd:COG0318 21 GGRRLTYAELDARARRLAAALRALGVGPGD--RVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGAR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 191 LMFVdaeiktkqlirdksylsslkyivqfnecsddikemarendfrlwsfnefvemgkkqkhrphvpptpetlATISFTS 270
Cdd:COG0318 99 ALVT---------------------------------------------------------------------ALILYTS 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 271 GTTGRPKGVMLTHLNMCSATMSCEEfENEAGVQDAYLSYLPLAHIY-ERLCLLSNFMIGSRIGFSRG-DPKLLVDDVQAL 348
Cdd:COG0318 110 GTTGRPKGVMLTHRNLLANAAAIAA-ALGLTPGDVVLVALPLFHVFgLTVGLLAPLLAGATLVLLPRfDPERVLELIERE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 349 APRSFATVPRVIdkihkavmkqvqdkplkKMILNAAIAyklyhykmtgkatrktwvDKYVLhkiqmllgPNIRQLILGAA 428
Cdd:COG0318 189 RVTVLFGVPTML-----------------ARLLRHPEF------------------ARYDL--------SSLRLVVSGGA 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 429 KSDVSAMRFARGAFGVEVLEGYGQTETSGPTTL--QLVGDTRIGCVGPPMACAMIKLIDvpELGYSVDKNG-GEVLVKGH 505
Cdd:COG0318 226 PLPPELLERFEERFGVRIVEGYGLTETSPVVTVnpEDPGERRPGSVGRPLPGVEVRIVD--EDGRELPPGEvGEIVVRGP 303
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 17541856 506 NVTSGYYKNPEATASSFtEDGYMKTGDIGRFTAEGSLQIIDRRKNVFK 553
Cdd:COG0318 304 NVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMII 350
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
210-691 |
3.61e-52 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 193.01 E-value: 3.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 210 LSSLKYIVQFNECSDDIKEMARENDFRLWSFNEfveMGKKQKHRPHVPPT-PETLATISFTSGTTGRPKGVMLTHLNMCS 288
Cdd:PTZ00342 255 LGPLEYDKEKLEKIKDLKEKAKKLGISIILFDD---MTKNKTTNYKIQNEdPDFITSIVYTSGTSGKPKGVMLSNKNLYN 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 289 ATMS---CEEFENEAgvQDAYLSYLPLAHIYERLCLLSNFMIGSRIGFSRGDPKLLVDDVQALAPRSFATVPRVIDKIHK 365
Cdd:PTZ00342 332 TVVPlckHSIFKKYN--PKTHLSYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYT 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 366 AVMKQVQDKP-LKKMILNAAIAYKlyhykmtgKATRKTWVDKY------VLHKIQMLLGPNIRQLILGAAKSDVSAMRFA 438
Cdd:PTZ00342 410 NIMTEINNLPpLKRFLVKKILSLR--------KSNNNGGFSKFlegithISSKIKDKVNPNLEVILNGGGKLSPKIAEEL 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 439 RGAFGVEVLEGYGQTETSGPTTLQLVGDTRIGCVGPPMAcamiklidvPELGYSV------DKNG----GEVLVKGHNVT 508
Cdd:PTZ00342 482 SVLLNVNYYQGYGLTETTGPIFVQHADDNNTESIGGPIS---------PNTKYKVrtwetyKATDtlpkGELLIKSDSIF 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 509 SGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMPQGKFVAPDLTESLYTSSSFVQQIYVHGD--MEK 586
Cdd:PTZ00342 553 SGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGDdsMDG 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 587 PwlVAIVVPDPEYLASY-----ALTKHNINGKTY-----EQLCNIPILADDVLRQFVELTEEDKRPRYEGVYGVHLTPVA 656
Cdd:PTZ00342 633 P--LAIISVDKYLLFKClkddnMLESTGINEKNYlekltDETINNNIYVDYVKGKMLEVYKKTNLNRYNIINDIYLTSKV 710
|
490 500 510
....*....|....*....|....*....|....*
gi 17541856 657 FSAENGLtTPTLKNKRNAIAQFFKAEIDGMYKKIE 691
Cdd:PTZ00342 711 WDTNNYL-TPTFKVKRFYVFKDYAFFIDQVKKIYK 744
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
262-599 |
3.00e-49 |
|
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: 175.94 E-value: 3.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 262 TLATISFTSGTTGRPKGVMLTHLNMCSATMSCEEFENEaGVQDAYLSYLPLAHIYERLCLLSNFMIGSRIGFSRG-DPKL 340
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGL-TEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKfDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 341 LVDDVQALAPRSFATVPRVIDKIhkavmkqvqDKPLKKmilnaaiayklyhykmtgkatrktwvDKYVLhkiqmllgPNI 420
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARL---------LKAPES--------------------------AGYDL--------SSL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 421 RQLILGAAKSDVSAMRFARGAFGVEVLEGYGQTETSGPTTLQLVGD--TRIGCVGPPMACAMIKLIDvPELGYSVDKNGG 498
Cdd:cd04433 117 RALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDdaRKPGSVGRPVPGVEVRIVD-PDGGELPPGEIG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 499 EVLVKGHNVTSGYYKNPEATASsFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFKmPQGKFVAPDLTESLytsssfvqqI 578
Cdd:cd04433 196 ELVVRGPSVMKGYWNNPEATAA-VDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAV---------L 264
|
330 340
....*....|....*....|..
gi 17541856 579 YVHGDMEKpwlVAIV-VPDPEY 599
Cdd:cd04433 265 LGHPGVAE---AAVVgVPDPEW 283
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
115-562 |
1.66e-48 |
|
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: 177.79 E-value: 1.66e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 115 ISYDQAFETSDHASQAIRKLGIEIGEesKIGIYSNNRPEWILSEMAIHN----FSNVSvPLYdtitNDDmhyitnlcEIS 190
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGD--VVGIISPNSTYYPPVFLGCLFaggiFSAAN-PIY----TAD--------ELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 191 LMFVDAeiKTKQLIRDKSYLSSLKYIVQFNECSDDIKEMARENDFRL----WSFNEFVEMGKKQKHRPHVPPTpeTLATI 266
Cdd:cd05911 76 HQLKIS--KPKVIFTDPDGLEKVKEAAKELGPKDKIIVLDDKPDGVLsiedLLSPTLGEEDEDLPPPLKDGKD--DTAAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 267 SFTSGTTGRPKGVMLTHLNMCSATMSCEEFENE-AGVQDAYLSYLPLAHIYERLCLLSNFMIG-SRIGFSRGDPKLLVDD 344
Cdd:cd05911 152 LYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGnDGSNDVILGFLPLYHIYGLFTTLASLLNGaTVIIMPKFDSELFLDL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 345 VQALAPRSFATVPRVIdkihkavmkqvqdkplkKMILNAAIayklyhykmtgkatrktwVDKYVLhkiqmllgPNIRQLI 424
Cdd:cd05911 232 IEKYKITFLYLVPPIA-----------------AALAKSPL------------------LDKYDL--------SSLRVIL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 425 LGAA---KSDVSamRFARGAFGVEVLEGYGQTETSGPTTLQLVGDTRIGCVGPPMACAMIKLIDvPELGYSVDKNG-GEV 500
Cdd:cd05911 269 SGGAplsKELQE--LLAKRFPNATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVD-DDGKDSLGPNEpGEI 345
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17541856 501 LVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMpQGKFVAP 562
Cdd:cd05911 346 CVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAP 406
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
115-552 |
6.97e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 170.86 E-value: 6.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 115 ISYDQAFETSDHASQAIRKLGIEIGEesKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDDMHYITNLCEISLMFV 194
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGKGD--RVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 195 -DAEIKTKQLIRDKsyLSSLKYIVQFNECSDDikemarENDFRLWSFNEFVEMGKKQKHRPHVppTPETLATISFTSGTT 273
Cdd:PRK07656 109 lGLFLGVDYSATTR--LPALEHVVICETEEDD------PHTEKMKTFTDFLAAGDPAERAPEV--DPDDVADILFTSGTT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 274 GRPKGVMLTHLNMCSATmscEEFENEAGVQ--DAYLSYLPLAHIY-ERLCLLSNFMIGSRIGFSrgdPKLLVDDVQALAP 350
Cdd:PRK07656 179 GRPKGAMLTHRQLLSNA---ADWAEYLGLTegDRYLAANPFFHVFgYKAGVNAPLMRGATILPL---PVFDPDEVFRLIE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 351 RSFATV-PRVidkihkavmkqvqdkPlkkmilnaaiayKLYHYkMTGKATRktwvDKYVLHkiqmllgpNIRQLILGAAK 429
Cdd:PRK07656 253 TERITVlPGP---------------P------------TMYNS-LLQHPDR----SAEDLS--------SLRLAVTGAAS 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 430 SDVSAMRFARGAFGVE-VLEGYGQTETSGPTTLQLVGDTRI---GCVGPPMACAMIKLIDvpELGYSVDKNG-GEVLVKG 504
Cdd:PRK07656 293 MPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDDRKtvaGTIGTAIAGVENKIVN--ELGEEVPVGEvGELLVRG 370
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 17541856 505 HNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVF 552
Cdd:PRK07656 371 PNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF 418
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
113-551 |
7.49e-44 |
|
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: 164.27 E-value: 7.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 113 EWISYDQAFETSDHASQAIRKLGIEIGEesKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDDMHYITNLCEISLM 192
Cdd:cd05936 23 RKLTYRELDALAEAFAAGLQNLGVQPGD--RVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 193 FVDAeiktkqlirdksylsslkyivqfnecsddikemarendfrlwSFNEFVEmgKKQKHRPHVPPTPETLATISFTSGT 272
Cdd:cd05936 101 IVAV------------------------------------------SFTDLLA--AGAPLGERVALTPEDVAVLQYTSGT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 273 TGRPKGVMLTHLNMCSATMSCEEFENEAGV-QDAYLSYLPLAHIYerlCLLSNFMIGSRIGFS-----RGDPKLLVDDVQ 346
Cdd:cd05936 137 TGVPKGAMLTHRNLVANALQIKAWLEDLLEgDDVVLAALPLFHVF---GLTVALLLPLALGATivlipRFRPIGVLKEIR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 347 ALAPRSFATVPrvidkihkavmkqvqdkPLKKMILNAAIayklyhykmtgkatrktwVDKYVLhkiqmllgPNIRQLILG 426
Cdd:cd05936 214 KHRVTIFPGVP-----------------TMYIALLNAPE------------------FKKRDF--------SSLRLCISG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 427 AAKSDVSAMRFARGAFGVEVLEGYGQTETSGPTTL-QLVGDTRIGCVGPPMACAMIKLID-----VPElgYSVdkngGEV 500
Cdd:cd05936 251 GAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVnPLDGPRKPGSIGIPLPGTEVKIVDddgeeLPP--GEV----GEL 324
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 17541856 501 LVKGHNVTSGYYKNPEATASSFTeDGYMKTGDIGRFTAEGSLQIIDRRKNV 551
Cdd:cd05936 325 WVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDM 374
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
115-553 |
1.50e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 161.51 E-value: 1.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 115 ISYDQAFETSDHASQAIRKLGIEIGEesKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDDMHYITNLCEISLMFV 194
Cdd:PRK06187 32 TTYAELDERVNRLANALRALGVKKGD--RVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 195 DAEIkTKQLIRDKSYLSSLKYIVQFNECsddikEMARENDFRLwsfnEFVEMGKKQ-KHRPHVPPTPETLATISFTSGTT 273
Cdd:PRK06187 110 DSEF-VPLLAAILPQLPTVRTVIVEGDG-----PAAPLAPEVG----EYEELLAAAsDTFDFPDIDENDAAAMLYTSGTT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 274 GRPKGVMLTHLNMCSATMSCEEFeNEAGVQDAYLSYLPLAHIYERLCLLSNFMIGSRI---GfsRGDPKLLVDDVQALAP 350
Cdd:PRK06187 180 GHPKGVVLSHRNLFLHSLAVCAW-LKLSRDDVYLVIVPMFHVHAWGLPYLALMAGAKQvipR--RFDPENLLDLIETERV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 351 RSFATVPrvidkihkAVMKqvqdkplkkMILNAAIAYKlyhykmtgkatrkTWVdkyvlhkiqmllgPNIRQLILGAAKS 430
Cdd:PRK06187 257 TFFFAVP--------TIWQ---------MLLKAPRAYF-------------VDF-------------SSLRLVIYGGAAL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 431 DVSAMRFARGAFGVEVLEGYGQTETSG------PTTLQLVGDTRIGCVGPPMACAMIKLID-----VPELGYSVdkngGE 499
Cdd:PRK06187 294 PPALLREFKEKFGIDLVQGYGMTETSPvvsvlpPEDQLPGQWTKRRSAGRPLPGVEARIVDddgdeLPPDGGEV----GE 369
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 17541856 500 VLVKGHNVTSGYYKNPEATASSFtEDGYMKTGDIGRFTAEGSLQIIDRRKNVFK 553
Cdd:PRK06187 370 IIVRGPWLMQGYWNRPEATAETI-DGGWLHTGDVGYIDEDGYLYITDRIKDVII 422
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
263-551 |
9.24e-37 |
|
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: 143.13 E-value: 9.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 263 LATISFTSGTTGRPKGVMLTHLNMCSATMSCEeFENEAGVQDAYLSYLPLAHIYERLC-LLSNFMIGSRIGFSRG-DPKL 340
Cdd:cd17631 100 LALLMYTSGTTGRPKGAMLTHRNLLWNAVNAL-AALDLGPDDVLLVVAPLFHIGGLGVfTLPTLLRGGTVVILRKfDPET 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 341 LVDDVQALAPRSFATVPRVIDkihkavmkqvqdkplkkMILNAAIAyklyhykmtgkatrktwvDKYVLhkiqmllgPNI 420
Cdd:cd17631 179 VLDLIERHRVTSFFLVPTMIQ-----------------ALLQHPRF------------------ATTDL--------SSL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 421 RQLILGAAKSDVSAMRfARGAFGVEVLEGYGQTETSGPTTLQLVGD--TRIGCVGPPMACAMIKLIDvpELGYSVDKNG- 497
Cdd:cd17631 216 RAVIYGGAPMPERLLR-ALQARGVKFVQGYGMTETSPGVTFLSPEDhrRKLGSAGRPVFFVEVRIVD--PDGREVPPGEv 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17541856 498 GEVLVKGHNVTSGYYKNPEATASSFtEDGYMKTGDIGRFTAEGSLQIIDRRKNV 551
Cdd:cd17631 293 GEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDM 345
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
113-551 |
4.83e-36 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 142.45 E-value: 4.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 113 EWISYDQAFETSDHASQAIRKLGIEIGEesKIGIYSNNRPEWILSEMAIHNFSNVSVPLydtitNddmhyiTNLC--EIS 190
Cdd:cd05926 13 PALTYADLAELVDDLARQLAALGIKKGD--RVAIALPNGLEFVVAFLAAARAGAVVAPL-----N------PAYKkaEFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 191 LMFVDAeiKTKQLIRDKSYLSS-----LKYIVQFNECSDDIKEMARENDFRLWSFNEFVemGKKQKHRPHvpPTPETLAT 265
Cdd:cd05926 80 FYLADL--GSKLVLTPKGELGPasraaSKLGLAILELALDVGVLIRAPSAESLSNLLAD--KKNAKSEGV--PLPDDLAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 266 ISFTSGTTGRPKGVMLTHLNMC-SATMSCEEFENEAGvqDAYLSYLPLAHIYERLC-LLSNFMIGSRI----GFSrgdPK 339
Cdd:cd05926 154 ILHTSGTTGRPKGVPLTHRNLAaSATNITNTYKLTPD--DRTLVVMPLFHVHGLVAsLLSTLAAGGSVvlppRFS---AS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 340 LLVDDVQALAPRSFATVPrvidKIHKAVMKQVQDKPLKKMilnaaiayklyhykmtgkatrktwvdkyvlhkiqmllgPN 419
Cdd:cd05926 229 TFWPDVRDYNATWYTAVP----TIHQILLNRPEPNPESPP--------------------------------------PK 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 420 IRQLILGAAKSDVSAMRFARGAFGVEVLEGYGQTETSGP-TTLQLVGDTR-IGCVGPPMAcamIKLIDVPELGySVDKNG 497
Cdd:cd05926 267 LRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQmTSNPLPPGPRkPGSVGKPVG---VEVRILDEDG-EILPPG 342
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 17541856 498 --GEVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNV 551
Cdd:cd05926 343 vvGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKEL 398
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
253-562 |
4.35e-34 |
|
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: 136.60 E-value: 4.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 253 RPHVPPTPETLATISFTSGTTGRPKGVMLTHLNMCSATMSCEEFENEAG-VQDAYLSYLPLAHIYErlclLSNFMIGS-R 330
Cdd:cd05904 150 PPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSdSEDVFLCVLPMFHIYG----LSSFALGLlR 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 331 IG-----FSRGDPKLLVDDVQALAPRSFATVPRVIDKIHKAVMkqvqdkplkkmilnaaiayklyhykmtgkatrktwVD 405
Cdd:cd05904 226 LGatvvvMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPI-----------------------------------VD 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 406 KYVLhkiqmllgPNIRQLILGAAKSDVSAM-RFARGAFGVEVLEGYGQTETSGPTTLQLV---GDTRIGCVG--PPMACA 479
Cdd:cd05904 271 KYDL--------SSLRQIMSGAAPLGKELIeAFRAKFPNVDLGQGYGMTESTGVVAMCFApekDRAKYGSVGrlVPNVEA 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 480 MIklIDvPELGYSVDKN-GGEVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMpQGK 558
Cdd:cd05904 343 KI--VD-PETGESLPPNqTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGF 418
|
....
gi 17541856 559 FVAP 562
Cdd:cd05904 419 QVAP 422
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
254-551 |
1.28e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 133.20 E-value: 1.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 254 PHVPPTPETLATISFTSGTTGRPKGVMLTHLNMCSATMSCEEFENEAGVQD-AYLSYLPLAHIYE-RLCLLSNFMIGSRI 331
Cdd:PRK05605 212 SHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVPGLGDGPeRVLAALPMFHAYGlTLCLTLAVSIGGEL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 332 G-FSRGDPKLLVDDVQALAPRSFATVPRVIDKIHKAVMKQvqDKPLKkmilnaaiayklyhykmtgkatrktwvdkyvlh 410
Cdd:PRK05605 292 VlLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEER--GVDLS--------------------------------- 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 411 kiqmllgpNIRQLILGAAKSDVSAMRFARGAFGVEVLEGYGQTETSGPTTLQLVGDTR-IGCVGPPMACAMIKLIDVPEL 489
Cdd:PRK05605 337 --------GVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPIIVGNPMSDDRrPGYVGVPFPDTEVRIVDPEDP 408
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17541856 490 GYSV-DKNGGEVLVKGHNVTSGYYKNPEATASSFtEDGYMKTGDIGRFTAEGSLQIIDRRKNV 551
Cdd:PRK05605 409 DETMpDGEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKEL 470
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
115-600 |
4.92e-30 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 123.17 E-value: 4.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 115 ISYDQAFETSDHASQAIRKLGIEIGEesKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDDMHYITNLCEISLMFV 194
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRPGD--RVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 195 DaeiktkqlirdksylsslkyivqfnecsddikemarendfrlwsfnefvemgkkqkhrphvpptpetLATISFTSGTTG 274
Cdd:cd05934 82 D-------------------------------------------------------------------PASILYTSGTTG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 275 RPKGVMLTHLNMCsatMSCEEFENEAGV--QDAYLSYLPLAHIyERLC--LLSNFMIGSRIG----FSrgdPKLLVDDVQ 346
Cdd:cd05934 95 PPKGVVITHANLT---FAGYYSARRFGLgeDDVYLTVLPLFHI-NAQAvsVLAALSVGATLVllprFS---ASRFWSDVR 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 347 alapRSFATVPRVIDKIHKAVMKQ---VQDKPlkkmilnaaiayklyhykmtgkatrktwvdkyvlHKIQmllgpnirqL 423
Cdd:cd05934 168 ----RYGATVTNYLGAMLSYLLAQppsPDDRA----------------------------------HRLR---------A 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 424 ILGAAKSDVSAMRFARgAFGVEVLEGYGQTETSGPTTLQLVGDTRIGCVGPPMACAMIKLidvpelgysVDKNG------ 497
Cdd:cd05934 201 AYGAPNPPELHEEFEE-RFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRI---------VDDDGqelpag 270
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 498 --GEVLVK---GHNVTSGYYKNPEATASSFtEDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMpQGKFVAPDLTESLYTSS 572
Cdd:cd05934 271 epGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIRR-RGENISSAEVERAILRH 348
|
490 500 510
....*....|....*....|....*....|..
gi 17541856 573 SFVQQIYVHG----DMEKPWLVAIVVPDPEYL 600
Cdd:cd05934 349 PAVREAAVVAvpdeVGEDEVKAVVVLRPGETL 380
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
115-598 |
9.41e-30 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 124.18 E-value: 9.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 115 ISYDQAFETSDHASQAIRKLGIeiGEESKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDDMHYITNLCEISLMFV 194
Cdd:cd17642 45 YSYAEYLEMSVRLAEALKKYGL--KQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFC 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 195 dAEIKTKQLIRDKSYLSSLKYIVQFNEcSDDIKEMARENDFR----LWSFNEFvemgkkqKHRPHVPPTPETLATISFTS 270
Cdd:cd17642 123 -SKKGLQKVLNVQKKLKIIKTIIILDS-KEDYKGYQCLYTFItqnlPPGFNEY-------DFKPPSFDRDEQVALIMNSS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 271 GTTGRPKGVMLTHLNMCSATMSCEE--FENEAGVQDAYLSYLPLAHIYERLCLLSNFMIGSRIGF-SRGDPKLLVDDVQA 347
Cdd:cd17642 194 GSTGLPKGVQLTHKNIVARFSHARDpiFGNQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLmYKFEEELFLRSLQD 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 348 LAPRSFATVPRVIDKIHKAvmkqvqdkplkkmilnaaiayklyhykmtgkatrkTWVDKYVLhkiqmllgPNIRQLILGA 427
Cdd:cd17642 274 YKVQSALLVPTLFAFFAKS-----------------------------------TLVDKYDL--------SNLHEIASGG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 428 A--KSDVSAMRFARgaFGVE-VLEGYGQTETSGPTTLQLVGDTRIGCVGPPMACAMIKLIDvPELGYSVDKNG-GEVLVK 503
Cdd:cd17642 311 AplSKEVGEAVAKR--FKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVD-LDTGKTLGPNErGELCVK 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 504 GHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMpQGKFVAPDLTESLYTSSSFVQQIYVHGd 583
Cdd:cd17642 388 GPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQHPKIFDAGVAG- 465
|
490
....*....|....*
gi 17541856 584 mekpwlvaivVPDPE 598
Cdd:cd17642 466 ----------IPDED 470
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
115-608 |
3.90e-29 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 121.61 E-value: 3.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 115 ISYDQAFETSDHASQAIRKLGIEIGEesKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDdmhyitnlcEISLMFV 194
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLAALGVKKGD--RVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSRE---------ELLWQLD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 195 DAEIKTkqLIRDKSYLSSLkYIVQFNECSDDIKEMARENDFR-LWSFNEfvemgkkqkhrphvpptpetLATISFTSGTT 273
Cdd:PRK03640 97 DAEVKC--LITDDDFEAKL-IPGISVKFAELMNGPKEEAEIQeEFDLDE--------------------VATIMYTSGTT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 274 GRPKGVMLTHLN-MCSATMSCEEFeneaGV--QDAYLSYLPLAHIYERLCLLSNFMIGSRIgfsrgdpkLLVDDVQAlap 350
Cdd:PRK03640 154 GKPKGVIQTYGNhWWSAVGSALNL----GLteDDCWLAAVPIFHISGLSILMRSVIYGMRV--------VLVEKFDA--- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 351 rsfatvprviDKIHKAVMKQ------VQDKPLKKMIlnAAIAYKLYHykmtgkatrktwvdkyvlhkiqmllgPNIRQLI 424
Cdd:PRK03640 219 ----------EKINKLLQTGgvtiisVVSTMLQRLL--ERLGEGTYP--------------------------SSFRCML 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 425 LGAAKSDVSAMRFARgAFGVEVLEGYGQTETSGpttlQLV------GDTRIGCVGPPMACAMIKLIDVPELGYSVDKngG 498
Cdd:PRK03640 261 LGGGPAPKPLLEQCK-EKGIPVYQSYGMTETAS----QIVtlspedALTKLGSAGKPLFPCELKIEKDGVVVPPFEE--G 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 499 EVLVKGHNVTSGYYKNPEATASSFtEDGYMKTGDIGRFTAEGSLQIIDRR--------KNVFkmpqgkfvaPDLTESLYT 570
Cdd:PRK03640 334 EIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRsdliisggENIY---------PAEIEEVLL 403
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 17541856 571 SSSFVQQIYVHGDMEKPW---LVAIVVPD------------PEYLASYALTKH 608
Cdd:PRK03640 404 SHPGVAEAGVVGVPDDKWgqvPVAFVVKSgevteeelrhfcEEKLAKYKVPKR 456
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
263-598 |
4.76e-28 |
|
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: 117.78 E-value: 4.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 263 LATISFTSGTTGRPKGVMLTH---LNMCSATMSCEEFENEagvqDAYLSYLPLAHIYER-LCLLSNFMIGSRIGF-SRGD 337
Cdd:cd05941 91 PALILYTSGTTGRPKGVVLTHanlAANVRALVDAWRWTED----DVLLHVLPLHHVHGLvNALLCPLFAGASVEFlPKFD 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 338 PKLlVDDVQALAPRS-FATVPRVIDKIHKAVMKQVQDKPLKkmilnaaiayklyhykmTGKATRKtwvdkyvlhkiqmll 416
Cdd:cd05941 167 PKE-VAISRLMPSITvFMGVPTIYTRLLQYYEAHFTDPQFA-----------------RAAAAER--------------- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 417 gpnIRQLILGAAKSDVSAMRFARGAFGVEVLEGYGQTETSGPTTLQLVGDTRIGCVGPPMACAMIKLIDvPELGYSVDKN 496
Cdd:cd05941 214 ---LRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGERRPGTVGMPLPGVQARIVD-EETGEPLPRG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 497 G-GEVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDrRKNVFKMPQGKF-VAPDLTESLYTSSSF 574
Cdd:cd05941 290 EvGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILG-RSSVDIIKSGGYkVSALEIERVLLAHPG 368
|
330 340
....*....|....*....|....*..
gi 17541856 575 VQQIYVHGDMEKPW---LVAIVVPDPE 598
Cdd:cd05941 369 VSECAVIGVPDPDWgerVVAVVVLRAG 395
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
240-596 |
1.03e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 115.25 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 240 FNEFVEMGKKQKHRPhVPPTPETLATISFTSGTTGRPKGVMLTHLNMCSATMSCEEFE----NEAgvQDAYLSYLPLAHI 315
Cdd:PRK05677 187 FNDALAKGAGQPVTE-ANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMgsnlNEG--CEILIAPLPLYHI 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 316 YErlcllsnFMIGSRIGFSRGDPKLLVDDvqalaPRSFatvPRVIdkihkavmkqvqdKPLKKmilnaaiayklyhYKMT 395
Cdd:PRK05677 264 YA-------FTFHCMAMMLIGNHNILISN-----PRDL---PAMV-------------KELGK-------------WKFS 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 396 GkatrktwvdkYV-LHKIQMLLGPN--IRQLILGAAKSDVS---AMRFA-----RGAFGVEVLEGYGQTETSGPTTLQLV 464
Cdd:PRK05677 303 G----------FVgLNTLFVALCNNeaFRKLDFSALKLTLSggmALQLAtaerwKEVTGCAICEGYGMTETSPVVSVNPS 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 465 GDTRIGCVGPPMACAMIKLID-----VPeLGYSvdkngGEVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAE 539
Cdd:PRK05677 373 QAIQVGTIGIPVPSTLCKVIDddgneLP-LGEV-----GELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQED 446
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 17541856 540 GSLQIIDRRKNVFkMPQGKFVAPDLTESLYTSSSFVQQIyvhgdmekpwlVAIVVPD 596
Cdd:PRK05677 447 GYMRIVDRKKDMI-LVSGFNVYPNELEDVLAALPGVLQC-----------AAIGVPD 491
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
256-549 |
2.15e-26 |
|
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: 113.58 E-value: 2.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 256 VPPTPETLATISFTSGTTGRPKGVMLTHLNMCSATMSCEEFEnEAGVQDAYLSYLPLAHIYE-RLCLLSNFMIGSRIgfs 334
Cdd:cd05909 142 APVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIF-DPNPEDVVFGALPFFHSFGlTGCLWLPLLSGIKV--- 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 335 rgdpkllvddVQALAPRSFATVPRVIDKIhkavmkqvqdkplKKMILNAAIAYklyhykMTGKATRKtwvdkyvlHKIQM 414
Cdd:cd05909 218 ----------VFHPNPLDYKKIPELIYDK-------------KATILLGTPTF------LRGYARAA--------HPEDF 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 415 llgPNIRQLILGAAKSDVSAMRFARGAFGVEVLEGYGQTETSGPTTLQLVG-DTRIGCVGPPMACAMIKLIDVPELGYSV 493
Cdd:cd05909 261 ---SSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVP 337
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17541856 494 DKNGGEVLVKGHNVTSGYYKNPEATASSFtEDGYMKTGDIGRFTAEGSLQIIDRRK 549
Cdd:cd05909 338 IGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLS 392
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
261-608 |
3.83e-26 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 111.67 E-value: 3.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 261 ETLATISFTSGTTGRPKGVMLT---HLNmcSATMSCEEFeneaGV--QDAYLSYLPLAHIYERLCLLSNFMIGSRIgfsr 335
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTfgnHWW--SAIGSALNL----GLteDDNWLCALPLFHISGLSILMRSVIYGMTV---- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 336 gdpkLLVDDVQAlaprsfatvprviDKIHKAVMkqvqdkplkkmilnaaiayklyhykmTGKATRKTWVDKYVLHKIQML 415
Cdd:cd05912 147 ----YLVDKFDA-------------EQVLHLIN--------------------------SGKVTIISVVPTMLQRLLEIL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 416 LG---PNIRQLILGAAKSDVSAMRFARgAFGVEVLEGYGQTETSGpttlQLV------GDTRIGCVGPPMACAMIKLIDV 486
Cdd:cd05912 184 GEgypNNLRCILLGGGPAPKPLLEQCK-EKGIPVYQSYGMTETCS----QIVtlspedALNKIGSAGKPLFPVELKIEDD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 487 PELGYSVdkngGEVLVKGHNVTSGYYKNPEATASSFtEDGYMKTGDIGRFTAEGSLQIIDRRKNVFkMPQGKFVAPDLTE 566
Cdd:cd05912 259 GQPPYEV----GEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIE 332
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 17541856 567 SLYTSSSFVQQIYVHGDMEKPW---LVAIVVPDP------------EYLASYALTKH 608
Cdd:cd05912 333 EVLLSHPAIKEAGVVGIPDDKWgqvPVAFVVSERpiseeeliaycsEKLAKYKVPKK 389
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
115-599 |
3.49e-25 |
|
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: 109.11 E-value: 3.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 115 ISYDQAFETSDHASQAIRKLGIEIGEesKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDDMHYITNLCEISLMFV 194
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGD--RVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 195 DAEIktkqlirdksylsslkyivqfnecsddikemarendfrlwsfnefvemgkkqkhrphvpptpETLATISFTSGTTG 274
Cdd:cd05935 80 GSEL--------------------------------------------------------------DDLALIPYTSGTTG 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 275 RPKGVMLTHLNMcSATMSCEEFENEAGVQDAYLSYLPLAHIYERLCLLSNFMI--GSRIGFSRGDPKLLVDDVQAL-APR 351
Cdd:cd05935 98 LPKGCMHTHFSA-AANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYvgGTYVLMARWDRETALELIEKYkVTF 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 352 SFATVPRVIDkihkaVMKQVQDKplkkmilnaaiayklyhykmtgkatrktwvdKYVLHKIQMLLGPnirqlilGAAKSD 431
Cdd:cd05935 177 WTNIPTMLVD-----LLATPEFK-------------------------------TRDLSSLKVLTGG-------GAPMPP 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 432 VSAMRFaRGAFGVEVLEGYGQTETSGPTTLQLVGDTRIGCVGPPMACAMIKLIDvPELGYSVDKN-GGEVLVKGHNVTSG 510
Cdd:cd05935 214 AVAEKL-LKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVID-IETGRELPPNeVGEIVVRGPQIFKG 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 511 YYKNPEATASSFTEDG---YMKTGDIGRFTAEGSLQIIDRRKNVFKMpQGKFVAPDLTESLYTSSSFVQQIYVHG--DME 585
Cdd:cd05935 292 YWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINV-SGFKVWPAEVEAKLYKHPAI*EVCVISvpDER 370
|
490
....*....|....*
gi 17541856 586 KPWLV-AIVVPDPEY 599
Cdd:cd05935 371 VGEEVkAFIVLRPEY 385
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
113-597 |
6.46e-25 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 109.18 E-value: 6.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 113 EWISYDQAFETSDHASQAIR-KLGIEIGEesKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDDMHYITNLCEISL 191
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIyELNVKKGE--RIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 192 MFVDAEIK-TKQLIRDKSYLSSLKYIVQFNECSDdikemARENDFrlwsfnefvemgkkqkhrphVPPTPETLATISFTS 270
Cdd:PRK06839 104 LFVEKTFQnMALSMQKVSYVQRVISITSLKEIED-----RKIDNF--------------------VEKNESASFIICYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 271 GTTGRPKGVMLTHLNMCSATMScEEFENEAGVQDAYLSYLPLAHIYE-RLCLLSNFMIGSRIgfsrgdpkllvddvqala 349
Cdd:PRK06839 159 GTTGKPKGAVLTQENMFWNALN-NTFAIDLTMHDRSIVLLPLFHIGGiGLFAFPTLFAGGVI------------------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 350 prsfaTVPRVIDKihkavmkqvqDKPLKkMILNaaiayklyhykmtgkatrktwvdkyvlHKIQMLLG-PNIRQLILGA- 427
Cdd:PRK06839 220 -----IVPRKFEP----------TKALS-MIEK---------------------------HKVTVVMGvPTIHQALINCs 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 428 --AKSDVSAMR-FARG----------AF---GVEVLEGYGQTETSgPTTLQLVGDT---RIGCVGPPMACAMIKLIDvpE 488
Cdd:PRK06839 257 kfETTNLQSVRwFYNGgapcpeelmrEFidrGFLFGQGFGMTETS-PTVFMLSEEDarrKVGSIGKPVLFCDYELID--E 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 489 LGYSVDKNG-GEVLVKGHNVTSGYYKNPEATASSFtEDGYMKTGDIGRFTAEGSLQIIDRRKNVFkMPQGKFVAPDLTES 567
Cdd:PRK06839 334 NKNKVEVGEvGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQ 411
|
490 500 510
....*....|....*....|....*....|...
gi 17541856 568 LYTSSSFVQQIYVHGDMEKPW---LVAIVVPDP 597
Cdd:PRK06839 412 VINKLSDVYEVAVVGRQHVKWgeiPIAFIVKKS 444
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
126-605 |
3.35e-24 |
|
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: 106.37 E-value: 3.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 126 HASQAIRKLGIEIGEESKIGIYSNNRPEWILSE--MAIHNFSNVSVPLYDTITNDDMHYITNLCEISLMFVDAEIKTkql 203
Cdd:cd05922 5 AAASALLEAGGVRGERVVLILPNRFTYIELSFAvaYAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAAD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 204 iRDKSYLSSlkyivqfneCSDDIkEMARENDFRlwsfnefvemgKKQKHRPHVPPTPETLATISFTSGTTGRPKGVMLTH 283
Cdd:cd05922 82 -RLRDALPA---------SPDPG-TVLDADGIR-----------AARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 284 LNMCSATMSCEEFENEAGvQDAYLSYLPLAHIYERLCLLSNFMIGSRIGFSRGD--PKLLVDDVQALAPRSFATVPrvid 361
Cdd:cd05922 140 QNLLANARSIAEYLGITA-DDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGvlDDAFWEDLREHGATGLAGVP---- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 362 kihkavmkqvqdkplkkmilnaaiayklYHYKMTGKATRKTwvDKYvlhkiqmllgPNIRQLI-LGAAKSDVSAMRFARG 440
Cdd:cd05922 215 ----------------------------STYAMLTRLGFDP--AKL----------PSLRYLTqAGGRLPQETIARLREL 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 441 AFGVEVLEGYGQTE-TSGPTTL--QLVGDtRIGCVGPPMACAMIKLIDVPELGYSVdKNGGEVLVKGHNVTSGYYKNPEA 517
Cdd:cd05922 255 LPGAQVYVMYGQTEaTRRMTYLppERILE-KPGSIGLAIPGGEFEILDDDGTPTPP-GEPGEIVHRGPNVMKGYWNDPPY 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 518 TASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMpQGKFVAPDLTESLYTSSSFVQQIYVHGD----MEKpwLVAIV 593
Cdd:cd05922 333 RRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKL-FGNRISPTEIEAAARSIGLIIEAAAVGLpdplGEK--LALFV 409
|
490
....*....|..
gi 17541856 594 VPDPEYLASYAL 605
Cdd:cd05922 410 TAPDKIDPKDVL 421
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
256-549 |
9.80e-24 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 105.34 E-value: 9.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 256 VPPTPETLATISFTSGTTGRPKGVMLTHLNMCS-ATMSCEEFENEAGvqDAYLSYLPLAHIYErLCLLSN--FMIGSRIG 332
Cdd:PRK07514 151 VPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSnALTLVDYWRFTPD--DVLIHALPIFHTHG-LFVATNvaLLAGASMI 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 333 FSrgdPKLLVDDVQALAPRsfATVprvidkihkavmkqvqdkplkkmilnaaiayklyhykMTGKATRktwvdkYVlhki 412
Cdd:PRK07514 228 FL---PKFDPDAVLALMPR--ATV-------------------------------------MMGVPTF------YT---- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 413 QMLLGP--------NIRQLILGAAKSDVSAMRFARGAFGVEVLEGYGQTETSGPTTLQLVGDTRIGCVGPPMACAMIKLI 484
Cdd:PRK07514 256 RLLQEPrltreaaaHMRLFISGSAPLLAETHREFQERTGHAILERYGMTETNMNTSNPYDGERRAGTVGFPLPGVSLRVT 335
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17541856 485 DvPELGYSVDKNG-GEVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRK 549
Cdd:PRK07514 336 D-PETGAELPPGEiGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGK 400
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
116-553 |
1.37e-23 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 105.15 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 116 SYDQAFETSDHASQAIRKLGIEIGEesKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDDMHYITNLCEISLMFVD 195
Cdd:PRK08008 39 SYLELNEEINRTANLFYSLGIRKGD--KVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 196 AEIKT--KQLIRDKSYlsSLKYIVqfnecsddikeMARENDFRLWSFNEFVEMGKKQ--KHRPHVPPTPETLATISFTSG 271
Cdd:PRK08008 117 AQFYPmyRQIQQEDAT--PLRHIC-----------LTRVALPADDGVSSFTQLKAQQpaTLCYAPPLSTDDTAEILFTSG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 272 TTGRPKGVMLTHLNMCSATMScEEFENEAGVQDAYLSYLPLAHI-YERLCLLSNFMIGSRIgfsrgdpkLLVDDVQAlap 350
Cdd:PRK08008 184 TTSRPKGVVITHYNLRFAGYY-SAWQCALRDDDVYLTVMPAFHIdCQCTAAMAAFSAGATF--------VLLEKYSA--- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 351 RSFatvprvidkihkavMKQVQDkplkkmilnaaiayklyhYKMTgkatrktwvdkyVLHKIQMLL--------GPN--- 419
Cdd:PRK08008 252 RAF--------------WGQVCK------------------YRAT------------ITECIPMMIrtlmvqppSANdrq 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 420 --IRQLILGAAKSDVSAMRFARgAFGVEVLEGYGQTETsgptTLQLVGDT-----RIGCVGPPMACAMIKLIDvpELGYS 492
Cdd:PRK08008 288 hcLREVMFYLNLSDQEKDAFEE-RFGVRLLTSYGMTET----IVGIIGDRpgdkrRWPSIGRPGFCYEAEIRD--DHNRP 360
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17541856 493 VDKNG-GEVLVKG---HNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFK 553
Cdd:PRK08008 361 LPAGEiGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIK 425
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
99-604 |
5.22e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 103.97 E-value: 5.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 99 MLGKRVMKDGklEWEWISYDQAFETSDHASQAIRKLGIeiGEESKIGIYSNNRPEWILSEMAIHN----FSNVSvPLYDT 174
Cdd:PRK12582 67 WLAQREPGHG--QWRKVTYGEAKRAVDALAQALLDLGL--DPGRPVMILSGNSIEHALMTLAAMQagvpAAPVS-PAYSL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 175 ITND--DMHYITNLCEISLMFV-DAEIKTKQLIRDKsyLSSLKYIVQFNECsDDIKEMArendfrlwsfneFVEMGKKqk 251
Cdd:PRK12582 142 MSHDhaKLKHLFDLVKPRVVFAqSGAPFARALAALD--LLDVTVVHVTGPG-EGIASIA------------FADLAAT-- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 252 hrphvPPT-----------PETLATISFTSGTTGRPKGVMLTHLNMCSAT---MSCEEFENEAGVQDaYLSYLPLAHIYE 317
Cdd:PRK12582 205 -----PPTaavaaaiaaitPDTVAKYLFTSGSTGMPKAVINTQRMMCANIamqEQLRPREPDPPPPV-SLDWMPWNHTMG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 318 RLCLLSNFMIGS---RIGFSRGDPKLLVDDVQAL---APRSFATVPRVIDKIHKAvMKQvqDKPL-----KKMilnAAIA 386
Cdd:PRK12582 279 GNANFNGLLWGGgtlYIDDGKPLPGMFEETIRNLreiSPTVYGNVPAGYAMLAEA-MEK--DDALrrsffKNL---RLMA 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 387 YklyhykmtGKATrktwVDKYVLHKIQMLLGPNIRQLILgaaksdvsamrfargafgveVLEGYGQTETSgPTTLQLVGD 466
Cdd:PRK12582 353 Y--------GGAT----LSDDLYERMQALAVRTTGHRIP--------------------FYTGYGATETA-PTTTGTHWD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 467 T-RIGCVGPPMACAMIKLIDVPelgysvDKNggEVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFT-----AEG 540
Cdd:PRK12582 400 TeRVGLIGLPLPGVELKLAPVG------DKY--EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdpddpEKG 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17541856 541 sLQIIDRRKNVFKMPQGKFV--APDLTESLYTSSSFVQQIYVHGdMEKPWLVAIVVPDPEYLASYA 604
Cdd:PRK12582 472 -LIFDGRVAEDFKLSTGTWVsvGTLRPDAVAACSPVIHDAVVAG-QDRAFIGLLAWPNPAACRQLA 535
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
263-552 |
6.18e-23 |
|
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: 100.27 E-value: 6.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 263 LATISFTSGTTGRPKGVMLTHLNMCSATMS-CEEFENEAGvqDAYLSYLPLAHIYerlcllsNFMIGSRIGFSRGdpkll 341
Cdd:cd17638 2 VSDIMFTSGTTGRSKGVMCAHRQTLRAAAAwADCADLTED--DRYLIINPFFHTF-------GYKAGIVACLLTG----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 342 vddvQALAPRSFATVPRVIDKIHKAVMKQVQDKPlkkmilnaaiayKLYHyKMTGKATRKtwvdKYVLhkiqmllgPNIR 421
Cdd:cd17638 68 ----ATVVPVAVFDVDAILEAIERERITVLPGPP------------TLFQ-SLLDHPGRK----KFDL--------SSLR 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 422 QLILGAAKSDVSAMRFARGAFGVE-VLEGYGQTEtSGPTTLQLVGD---TRIGCVGPPMACAMIKLIDvpelgysvdknG 497
Cdd:cd17638 119 AAVTGAATVPVELVRRMRSELGFEtVLTAYGLTE-AGVATMCRPGDdaeTVATTCGRACPGFEVRIAD-----------D 186
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 17541856 498 GEVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVF 552
Cdd:cd17638 187 GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY 241
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
239-550 |
6.23e-23 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 103.56 E-value: 6.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 239 SFNEFVEMGKKQKHRPhVPPTPETLATISFTSGTTGRPKGVMLTHLNMCSATMsceefENEAGVQDAYLSY--------- 309
Cdd:PRK07059 183 RFNDALAEGARQTFKP-VKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVL-----QMEAWLQPAFEKKprpdqlnfv 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 310 --LPLAHIYerlCLLSNFMIGSRIGfsrgdpkllvdDVQALAPRsfatvPRVIDKIHKAVMK-QVQDKPLKKMILNAaia 386
Cdd:PRK07059 257 caLPLYHIF---ALTVCGLLGMRTG-----------GRNILIPN-----PRDIPGFIKELKKyQVHIFPAVNTLYNA--- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 387 yklyhykmtgkatrktwvdkyvlhkiqMLLGPNIRQLilgaaksDVSAMRFARGA---------------FGVEVLEGYG 451
Cdd:PRK07059 315 ---------------------------LLNNPDFDKL-------DFSKLIVANGGgmavqrpvaerwlemTGCPITEGYG 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 452 QTETSGPTTLQLVGDTRI-GCVGPPMACAMIKLIDvpELGYSVdKNG--GEVLVKGHNVTSGYYKNPEATASSFTEDGYM 528
Cdd:PRK07059 361 LSETSPVATCNPVDATEFsGTIGLPLPSTEVSIRD--DDGNDL-PLGepGEICIRGPQVMAGYWNRPDETAKVMTADGFF 437
|
330 340
....*....|....*....|..
gi 17541856 529 KTGDIGRFTAEGSLQIIDRRKN 550
Cdd:PRK07059 438 RTGDVGVMDERGYTKIVDRKKD 459
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
132-549 |
1.26e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 102.35 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 132 RKLGIEIGEesKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDDM-HYITNlCEISLMFVDAEI--KTKQLIRDks 208
Cdd:PRK08314 54 QECGVRKGD--RVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELaHYVTD-SGARVAIVGSELapKVAPAVGN-- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 209 ylSSLKYIV--QFnecSDDIK-----------------EMARENDFRLWSfnefvEMGKKQKHRPHVPPTPETLATISFT 269
Cdd:PRK08314 129 --LRLRHVIvaQY---SDYLPaepeiavpawlraepplQALAPGGVVAWK-----EALAAGLAPPPHTAGPDDLAVLPYT 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 270 SGTTGRPKGVMLTHLN-MCSATMSCeeFENEAGVQDAYLSYLPLAHIYERL-CLLSNFMIGSRIgfsrgdpkllvddvqA 347
Cdd:PRK08314 199 SGTTGVPKGCMHTHRTvMANAVGSV--LWSNSTPESVVLAVLPLFHVTGMVhSMNAPIYAGATV---------------V 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 348 LAPR-SFATVPRVIDkihkavmkqvqdkplkkmilnaaiayklyHYKMTGKATRKTWVdkyvlhkIQMLLGPNIRQLIL- 425
Cdd:PRK08314 262 LMPRwDREAAARLIE-----------------------------RYRVTHWTNIPTMV-------VDFLASPGLAERDLs 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 426 --------GAAKSDVSAMRFaRGAFGVEVLEGYGQTETSGPTTLQLVGDTRIGCVGPPMACAMIKLIDvPELGYSVDKNG 497
Cdd:PRK08314 306 slryigggGAAMPEAVAERL-KELTGLDYVEGYGLTETMAQTHSNPPDRPKLQCLGIPTFGVDARVID-PETLEELPPGE 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 17541856 498 -GEVLVKGHNVTSGYYKNPEATASSFTE-DG--YMKTGDIGRFTAEGSLQIIDRRK 549
Cdd:PRK08314 384 vGEIVVHGPQVFKGYWNRPEATAEAFIEiDGkrFFRTGDLGRMDEEGYFFITDRLK 439
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
256-551 |
1.58e-22 |
|
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: 101.98 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 256 VPPTPETLATISFTSGTTGRPKGVMLTH---LNMCSATMSceefENEAGVQDAYLSYLPLAHIyerlcllsnfmiGSRIG 332
Cdd:cd05906 162 PQSRPDDLALLMLTSGSTGFPKAVPLTHrniLARSAGKIQ----HNGLTPQDVFLNWVPLDHV------------GGLVE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 333 FSRGDPKLLVDDVQALAPRSFATVPRVIDKIHKavmkqvqdkplkkmilnaaiayklyhYKMTgkatrKTWVDKYVLHKI 412
Cdd:cd05906 226 LHLRAVYLGCQQVHVPTEEILADPLRWLDLIDR--------------------------YRVT-----ITWAPNFAFALL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 413 QMLL--GP-------NIRQLI-LGAAKSDVSAMRFAR--GAFGVE---VLEGYGQTETS-------GPTTLQLVGDTRIG 470
Cdd:cd05906 275 NDLLeeIEdgtwdlsSLRYLVnAGEAVVAKTIRRLLRllEPYGLPpdaIRPAFGMTETCsgviysrSFPTYDHSQALEFV 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 471 CVGPPMACAMIKLIDvpELGYSVDKNG-GEVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGrFTAEGSLQIIDRRK 549
Cdd:cd05906 355 SLGRPIPGVSMRIVD--DEGQLLPEGEvGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
..
gi 17541856 550 NV 551
Cdd:cd05906 432 DT 433
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
220-551 |
1.67e-22 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 102.21 E-value: 1.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 220 NECSDDIKEMAreNDFRL---WSFNEFVEMGKKQKHRPhVPPTPETLATISFTSGTTGRPKGVMLTHLNMCsATM----S 292
Cdd:PRK12492 166 NTVVDKVKKMV--PAYHLpqaVPFKQALRQGRGLSLKP-VPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLV-ANMlqvrA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 293 CEEFENEAGV------QDAYLSYLPLAHIYER----LCLLSNfmigsrigfsrGDPKLLVddvqalaprsfaTVPRVIDk 362
Cdd:PRK12492 242 CLSQLGPDGQplmkegQEVMIAPLPLYHIYAFtancMCMMVS-----------GNHNVLI------------TNPRDIP- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 363 ihkAVMKQVQDKPLKKMI-LNAAIAYKLYHykmtgkatrktwvdkyvlhkiqmllgPNIRQLILGAAKSDVS-------- 433
Cdd:PRK12492 298 ---GFIKELGKWRFSALLgLNTLFVALMDH--------------------------PGFKDLDFSALKLTNSggtalvka 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 434 -AMRFArGAFGVEVLEGYGQTETSGPTTLQLVGD-TRIGCVGPPMACAMIKLIDVPELGYSVDKNGgEVLVKGHNVTSGY 511
Cdd:PRK12492 349 tAERWE-QLTGCTIVEGYGLTETSPVASTNPYGElARLGTVGIPVPGTALKVIDDDGNELPLGERG-ELCIKGPQVMKGY 426
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 17541856 512 YKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNV 551
Cdd:PRK12492 427 WQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDL 466
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
106-608 |
1.86e-22 |
|
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: 102.12 E-value: 1.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 106 KDGKLEWEWISYDQAFETSDHASQAIRKLGIeigeeskigiySNNRPEWILSEMAIHN-------------FSNVSvPLY 172
Cdd:cd05921 17 REGNGGWRRVTYAEALRQVRAIAQGLLDLGL-----------SAERPLLILSGNSIEHalmalaamyagvpAAPVS-PAY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 173 DTITND--DMHYITNLCEISLMFV-DAEIKTKQLirDKSYLSSLKYIVQFNECSDDikemareNDFRLWSFNEFVEMGKK 249
Cdd:cd05921 85 SLMSQDlaKLKHLFELLKPGLVFAqDAAPFARAL--AAIFPLGTPLVVSRNAVAGR-------GAISFAELAATPPTAAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 250 QKHRPHVppTPETLATISFTSGTTGRPKGVMLTHLNMCS-ATMSCEEFENEAGVQDAYLSYLPLAHIYerlcllsnfmiG 328
Cdd:cd05921 156 DAAFAAV--GPDTVAKFLFTSGSTGLPKAVINTQRMLCAnQAMLEQTYPFFGEEPPVLVDWLPWNHTF-----------G 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 329 SRIGFS---RGDPKLLVDDVQALaPRSFATVPRVIDKIHKAVMkqvqdkplkkmiLNAAIAYKLYHYKMTG-KATRKTWV 404
Cdd:cd05921 223 GNHNFNlvlYNGGTLYIDDGKPM-PGGFEETLRNLREISPTVY------------FNVPAGWEMLVAALEKdEALRRRFF 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 405 DKYvlhKIQMLLGPNIRQLILGAaksdVSAMRFARGAFGVEVLEGYGQTETsGPTTLQLVGDT-RIGCVGPPMACAMIKL 483
Cdd:cd05921 290 KRL---KLMFYAGAGLSQDVWDR----LQALAVATVGERIPMMAGLGATET-APTATFTHWPTeRSGLIGLPAPGTELKL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 484 idVPelgysvdkNGG--EVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQ---IIDRR-KNVFKMPQG 557
Cdd:cd05921 362 --VP--------SGGkyEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLADPDDPAkglVFDGRvAEDFKLASG 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 17541856 558 KFVA--PDLTESLYTSSSFVQQIYVHGDmEKPWLVAIVVPDPEYLASYALTKH 608
Cdd:cd05921 432 TWVSvgPLRARAVAACAPLVHDAVVAGE-DRAEVGALVFPDLLACRRLVGLQE 483
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
254-571 |
3.31e-22 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 100.83 E-value: 3.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 254 PHVPPTPETLATISFTSGTTGRPKGVMLTHLNMCSATMSCEEFENEA---GVQDAYLSYLPLAHIYerlCLLSNFMIGSR 330
Cdd:PLN02246 172 PEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNlyfHSDDVILCVLPMFHIY---SLNSVLLCGLR 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 331 IG-----FSRGDPKLLVDDVQalapRSFATVPRVIDKIHKAVMKqvqdkplkkmilNAAiayklyhykmtgkatrktwVD 405
Cdd:PLN02246 249 VGaailiMPKFEIGALLELIQ----RHKVTIAPFVPPIVLAIAK------------SPV-------------------VE 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 406 KYVLHKIQMLLGpnirqlilGAAK-----SDVSAMRFARGAFGvevlEGYGQTEtSGPTTLQLVG------DTRIGCVGP 474
Cdd:PLN02246 294 KYDLSSIRMVLS--------GAAPlgkelEDAFRAKLPNAVLG----QGYGMTE-AGPVLAMCLAfakepfPVKSGSCGT 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 475 PMACAMIKLIDvPELGYSVDKN-GGEVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFK 553
Cdd:PLN02246 361 VVRNAELKIVD-PETGASLPRNqPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIK 439
|
330
....*....|....*...
gi 17541856 554 MpQGKFVAPDLTESLYTS 571
Cdd:PLN02246 440 Y-KGFQVAPAELEALLIS 456
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
177-553 |
3.79e-22 |
|
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: 100.78 E-value: 3.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 177 NDDMHYITNLCEISLMFVDAEI-KTKQLIRDKsyLSSLKYIVQFnecsDDIKEMARENDFRLWSFNEFVEMGKKQKHRPH 255
Cdd:cd12119 86 PEQIAYIINHAEDRVVFVDRDFlPLLEAIAPR--LPTVEHVVVM----TDDAAMPEPAGVGVLAYEELLAAESPEYDWPD 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 256 VPPTpeTLATISFTSGTTGRPKGVMLTH-------LNMCSA-TMSCEEfeneagvQDAYLSYLPLAHI------Yerlcl 321
Cdd:cd12119 160 FDEN--TAAAICYTSGTTGNPKGVVYSHrslvlhaMAALLTdGLGLSE-------SDVVLPVVPMFHVnawglpY----- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 322 lSNFMIGSRIGFS--RGDPKLLVDDVQALAPRSFATVPRVIdkihkavmkqvqdkplkKMILNaaiayklyHYKMTGkat 399
Cdd:cd12119 226 -AAAMVGAKLVLPgpYLDPASLAELIEREGVTFAAGVPTVW-----------------QGLLD--------HLEANG--- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 400 rktwvdkYVLhkiqmllgPNIRQLILGAAKSDVSAMRFARgAFGVEVLEGYGQTETS--------GPTTLQLVGDTRIGC 471
Cdd:cd12119 277 -------RDL--------SSLRRVVIGGSAVPRSLIEAFE-ERGVRVIHAWGMTETSplgtvarpPSEHSNLSEDEQLAL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 472 V---GPPMACAMIKLIDvpELGYSVDKNG---GEVLVKGHNVTSGYYKNPEATASsFTEDGYMKTGDIGRFTAEGSLQII 545
Cdd:cd12119 341 RakqGRPVPGVELRIVD--DDGRELPWDGkavGELQVRGPWVTKSYYKNDEESEA-LTEDGWLRTGDVATIDEDGYLTIT 417
|
....*...
gi 17541856 546 DRRKNVFK 553
Cdd:cd12119 418 DRSKDVIK 425
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
266-599 |
4.41e-22 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 98.11 E-value: 4.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 266 ISFTSGTTGRPKGVMLTHLNMCSATMSCEEFENeAGVQDAYLSYLPLAHIYERLCLLSNFMIGSR-IGFSRGDPKLLVDD 344
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMG-LTEADVYLNMLPLFHIAGLNLALATFHAGGAnVVMEKFDPAEALEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 345 VQALAPRSFATVPrvidkihkavmkqvqdkPLKKMILNAAIayklyhykmtgkatrKTWVDKYVLHKIQMLLGPNIRQLI 424
Cdd:cd17637 84 IEEEKVTLMGSFP-----------------PILSNLLDAAE---------------KSGVDLSSLRHVLGLDAPETIQRF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 425 LGaaksdVSAMRFargafgvevLEGYGQTETSGPTTLQLVGDtRIGCVGPPMACAMIKLID-----VPeLGYSvdkngGE 499
Cdd:cd17637 132 EE-----TTGATF---------WSLYGQTETSGLVTLSPYRE-RPGSAGRPGPLVRVRIVDdndrpVP-AGET-----GE 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 500 VLVKGHNVTSGYYKNPEATASSFtEDGYMKTGDIGRFTAEGSLQIIDRR--KNVFKmPQGKFVAPDLTESLytsssfvqq 577
Cdd:cd17637 191 IVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKV--------- 259
|
330 340
....*....|....*....|..
gi 17541856 578 IYVHGDMEKpwLVAIVVPDPEY 599
Cdd:cd17637 260 ILEHPAIAE--VCVIGVPDPKW 279
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
257-547 |
5.86e-22 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 101.54 E-value: 5.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 257 PPTPETLATISFTSGTTGRPKGVMLTHLNMCSATMSCEEFENeAGVQDAYLSYLPLAH-----IYERLCLLSNFmigsri 331
Cdd:PRK08633 778 TFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFN-LRNDDVILSSLPFFHsfgltVTLWLPLLEGI------ 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 332 gfsrgdpkllvddvqalaprSFATVPRVID--KIHKAVMKQvqdkplkkmilNAAIayklyhykMTGKAT-RKTWVDKYV 408
Cdd:PRK08633 851 --------------------KVVYHPDPTDalGIAKLVAKH-----------RATI--------LLGTPTfLRLYLRNKK 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 409 LHKIQMllgPNIRQLILGAAK-----SDVSAMRFargafGVEVLEGYGQTETSGPTTLQL----VGD------TRIGCVG 473
Cdd:PRK08633 892 LHPLMF---ASLRLVVAGAEKlkpevADAFEEKF-----GIRILEGYGATETSPVASVNLpdvlAADfkrqtgSKEGSVG 963
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17541856 474 PPMACAMIKLIDvPELGYSVDKN-GGEVLVKGHNVTSGYYKNPEATASSFTE---DGYMKTGDIGRFTAEGSLQIIDR 547
Cdd:PRK08633 964 MPLPGVAVRIVD-PETFEELPPGeDGLILIGGPQVMKGYLGDPEKTAEVIKDidgIGWYVTGDKGHLDEDGFLTITDR 1040
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
116-599 |
9.41e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 99.85 E-value: 9.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 116 SYDQAFETSDHASQAIRKLGIEIGEesKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDDMHYITNLCEISLMFVD 195
Cdd:PRK12583 47 TWRQLADAVDRLARGLLALGVQPGD--RVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 196 AEIKTKqlirdkSYLSSLKYIV---QFNECSDDIKE----------MARENDFRLWSFNEFVEMGKKQkhrphvppTPET 262
Cdd:PRK12583 125 DAFKTS------DYHAMLQELLpglAEGQPGALACErlpelrgvvsLAPAPPPGFLAWHELQARGETV--------SREA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 263 LAT------------ISFTSGTTGRPKGVMLTHLNMCS-ATMSCEEFEneAGVQDAYLSYLPLAHIYErlCLLSNF---- 325
Cdd:PRK12583 191 LAErqasldrddpinIQYTSGTTGFPKGATLSHHNILNnGYFVAESLG--LTEHDRLCVPVPLYHCFG--MVLANLgcmt 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 326 ----MIGSRIGFsrgDPKLLVDDVQALAPRSFATVPRVIdkihkavMKQVqDKPLKKmilnaaiayklyHYKMTgkatrk 401
Cdd:PRK12583 267 vgacLVYPNEAF---DPLATLQAVEEERCTALYGVPTMF-------IAEL-DHPQRG------------NFDLS------ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 402 twvdkyvlhkiqmllgpNIRQLILGAAKSDVSAMRFARGAFGV-EVLEGYGQTETSGPTTLQLVGDT---RIGCVGPPMA 477
Cdd:PRK12583 318 -----------------SLRTGIMAGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSLQTTAADDlerRVETVGRTQP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 478 CAMIKLIDVpeLGYSVDKNG-GEVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFkMPQ 556
Cdd:PRK12583 381 HLEVKVVDP--DGATVPRGEiGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMI-IRG 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 17541856 557 GKFVAP-DLTESLYTSSSfVQQIYVHGdmekpwlvaivVPDPEY 599
Cdd:PRK12583 458 GENIYPrEIEEFLFTHPA-VADVQVFG-----------VPDEKY 489
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
260-550 |
1.27e-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: 341241 [Multi-domain] Cd Length: 349 Bit Score: 96.96 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 260 PETLATISFTSGTTGRPKGVMLTHLNmcsatmsceefeneagvqdaylsylplahiyerlcLLSN-FMIGSRIGFSRGDp 338
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHN-----------------------------------IVNNgYFIGERLGLTEQD- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 339 KL-----------LVDDVQALAPRSFATVPRVIDKIHKAVMKQVQDKplKKMILNAA----IAyKLYHYKMtgkatrktw 403
Cdd:cd05917 45 RLcipvplfhcfgSVLGVLACLTHGATMVFPSPSFDPLAVLEAIEKE--KCTALHGVptmfIA-ELEHPDF--------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 404 vDKYVLHkiqmllgpNIRQLILGAAKSDVSAMRFARGAFGV-EVLEGYGQTETSGPTTLQLVGDT---RIGCVGPPMACA 479
Cdd:cd05917 113 -DKFDLS--------SLRTGIMAGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDSiekRVNTVGRIMPHT 183
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17541856 480 MIKLID-----VPELGysvdkNGGEVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKN 550
Cdd:cd05917 184 EAKIVDpeggiVPPVG-----VPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKD 254
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
243-551 |
4.30e-21 |
|
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: 96.68 E-value: 4.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 243 FVEMGKKQKHRPHvpPTPETLATISFTSGTTGRPKGVMLTHLN-MCSATMSCEEFenEAGVQDAYLSYLPLAHIyerlcl 321
Cdd:cd05903 77 FVVPERFRQFDPA--AMPDAVALLLFTSGTTGEPKGVMHSHNTlSASIRQYAERL--GLGPGDVFLVASPMAHQ------ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 322 lSNFMIGSRIGFSRGDPKLLVDDVQAlaprsfATVPRVIDKIHKAVMKQ----VQDkplkkmILNAAiayklyhyKMTGK 397
Cdd:cd05903 147 -TGFVYGFTLPLLLGAPVVLQDIWDP------DKALALMREHGVTFMMGatpfLTD------LLNAV--------EEAGE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 398 ATrktwvdkyvlhkiqmllgPNIRQLILGAAKSDVSAMRFARGAFGVEVLEGYGQTETSGPTT-LQLVGDTRIGCV-GPP 475
Cdd:cd05903 206 PL------------------SRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTsITPAPEDRRLYTdGRP 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17541856 476 MACAMIKLIDvpELGYSVDKNG-GEVLVKGHNVTSGYYKNPEATASSFtEDGYMKTGDIGRFTAEGSLQIIDRRKNV 551
Cdd:cd05903 268 LPGVEIKVVD--DTGATLAPGVeGELLSRGPSVFLGYLDRPDLTADAA-PEGWFRTGDLARLDEDGYLRITGRSKDI 341
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
263-580 |
5.67e-21 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 97.36 E-value: 5.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 263 LATISFTSGTTGRPKGVMLTH----LNMCSATMSCEEfenEAGVQDAYLSYLPLAHIY--ERLCLLSNFMIGSRIGFSRG 336
Cdd:PLN02330 186 LCALPFSSGTTGISKGVMLTHrnlvANLCSSLFSVGP---EMIGQVVTLGLIPFFHIYgiTGICCATLRNKGKVVVMSRF 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 337 DPKLLVDdvqALAPR--SFA-TVPRVIDKIHKAVMkqVQDKPLKKMILNAAiayklyhykMTGKATrktwvdkyvlhkiq 413
Cdd:PLN02330 263 ELRTFLN---ALITQevSFApIVPPIILNLVKNPI--VEEFDLSKLKLQAI---------MTAAAP-------------- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 414 mlLGPNIrqliLGAaksdvsamrFARGAFGVEVLEGYGQTETSGPTTLQlvGDTRIG-------CVGPPMACAMIKLIDv 486
Cdd:PLN02330 315 --LAPEL----LTA---------FEAKFPGVQVQEAYGLTEHSCITLTH--GDPEKGhgiakknSVGFILPNLEVKFID- 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 487 PELGYSVDKN-GGEVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMpQGKFVAPDLT 565
Cdd:PLN02330 377 PDTGRSLPKNtPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAEL 455
|
330
....*....|....*
gi 17541856 566 ESLYTSSSFVQQIYV 580
Cdd:PLN02330 456 EAILLTHPSVEDAAV 470
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
115-547 |
6.49e-21 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 97.10 E-value: 6.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 115 ISYDQAFETSDHASQAIRKLGIEIGEesKIGIYSNNRPEWILSeM-------AIHnfSNVSvPLYdtiTNDDMHYITNLC 187
Cdd:COG0365 40 LTYAELRREVNRFANALRALGVKKGD--RVAIYLPNIPEAVIA-MlacarigAVH--SPVF-PGF---GAEALADRIEDA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 188 EISLMFVDAE-------IKTKQLIRD-KSYLSSLKYIVQFNECSDDIkemARENDFrlwSFNEFVEmgkkqKHRPHVPPT 259
Cdd:COG0365 111 EAKVLITADGglrggkvIDLKEKVDEaLEELPSLEHVIVVGRTGADV---PMEGDL---DWDELLA-----AASAEFEPE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 260 P---ETLATISFTSGTTGRPKGVMLTH---LNMCSATMsceefENEAGVQDA----------------YLSYLPLAH--- 314
Cdd:COG0365 180 PtdaDDPLFILYTSGTTGKPKGVVHTHggyLVHAATTA-----KYVLDLKPGdvfwctadigwatghsYIVYGPLLNgat 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 315 --IYERlcllsnfmigsRIGFSrgDPKLLVDDVQALAPRSFATVPRVIdkihKAVMKQVQDkplkkmilnaaiayklyhy 392
Cdd:COG0365 255 vvLYEG-----------RPDFP--DPGRLWELIEKYGVTVFFTAPTAI----RALMKAGDE------------------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 393 kmtgkatrktWVDKYVLHKIQML------LGPnirqlilgaaksdvSAMRFARGAFGVEVLEGYGQTETSGP-TTLQLVG 465
Cdd:COG0365 299 ----------PLKKYDLSSLRLLgsagepLNP--------------EVWEWWYEAVGVPIVDGWGQTETGGIfISNLPGL 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 466 DTRIGCVGPPMACAMIKLIDvpELGYSVDKN-GGEVLVKGHN--VTSGYYKNPEATASSF--TEDGYMKTGDIGRFTAEG 540
Cdd:COG0365 355 PVKPGSMGKPVPGYDVAVVD--EDGNPVPPGeEGELVIKGPWpgMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDG 432
|
....*..
gi 17541856 541 SLQIIDR 547
Cdd:COG0365 433 YFWILGR 439
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
239-550 |
1.28e-20 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 96.28 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 239 SFNEFVEMGKKQKH-RPHVppTPETLATISFTSGTTGRPKGVMLTHLNMCSATMSC----EEFENEAgvQDAYLSYLPLA 313
Cdd:PRK08974 185 SFRSALHKGRRMQYvKPEL--VPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAkaayGPLLHPG--KELVVTALPLY 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 314 HIYERL--CLLsnFMigsrigfSRGDPKLLVddvqalaprsfaTVPRVIDkihkAVMKQvqdkpLKKMILNAaiayklyh 391
Cdd:PRK08974 261 HIFALTvnCLL--FI-------ELGGQNLLI------------TNPRDIP----GFVKE-----LKKYPFTA-------- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 392 ykMTGKATR-KTWVDKYVLHKIqmllgpNIRQLIL----GAAKSDVSAMRFARgAFGVEVLEGYGQTETSgP----TTLQ 462
Cdd:PRK08974 303 --ITGVNTLfNALLNNEEFQEL------DFSSLKLsvggGMAVQQAVAERWVK-LTGQYLLEGYGLTECS-PlvsvNPYD 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 463 LVGDTriGCVGPPMACAMIKLID----VPELGYSvdkngGEVLVKGHNVTSGYYKNPEATASSFtEDGYMKTGDIGRFTA 538
Cdd:PRK08974 373 LDYYS--GSIGLPVPSTEIKLVDddgnEVPPGEP-----GELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDE 444
|
330
....*....|..
gi 17541856 539 EGSLQIIDRRKN 550
Cdd:PRK08974 445 EGFLRIVDRKKD 456
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
257-596 |
1.32e-20 |
|
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: 95.07 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 257 PPTPETLATISFTSGTTGRPKGVMLTHLNMCSAtMSCEEFENEAGVQDAYLSYLPLAHIYERLCLLSNFMIGSRIgfsrg 336
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLNY-VSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTL----- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 337 dpkLLVDDvqalaPRSFATVPRVIDKIHkavmkqvqdkplkkmilnaaiayklyhykMTGKATRKTWVDKYvlhkiqmll 416
Cdd:cd17653 175 ---VLADP-----SDPFAHVARTVDALM-----------------------------STPSILSTLSPQDF--------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 417 gPNIRQLILGAakSDVSAMRFARGAFGVEVLEGYGQTETS-GPTTLQLVGDTRIgCVGPPMACAMIKLIDvPELGYSVDK 495
Cdd:cd17653 209 -PNLKTIFLGG--EAVPPSLLDRWSPGRRLYNAYGPTECTiSSTMTELLPGQPV-TIGKPIPNSTCYILD-ADLQPVPEG 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 496 NGGEVLVKGHNVTSGYYKNPEATASSFTEDGY------MKTGDIGRFTAEGSLQIIDRRKNVFKMpQGKFVA-PDLTESL 568
Cdd:cd17653 284 VVGEICISGVQVARGYLGNPALTASKFVPDPFwpgsrmYRTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINlEEIEEVV 362
|
330 340 350
....*....|....*....|....*....|
gi 17541856 569 YTSSSFVQQIY--VHGDMekpwLVAIVVPD 596
Cdd:cd17653 363 LQSQPEVTQAAaiVVNGR----LVAFVTPE 388
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
260-551 |
1.38e-20 |
|
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: 95.63 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 260 PETLATISFTSGTTGRPKGVMLTHLNMCSATMSCEEfENEAGVQDAYLSYLPLAH-----IYERLCLLSN---FMIGSRI 331
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILN-STEWKTKDRILSWMPLTHdmgliAFHLAPLIAGmnqYLMPTRL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 332 GFSRgdPKLLVDDVQalapRSFATVPRVIDKIHKAVMKQVQDKPLK-------KMILNAA--IAYKLYHYKMTGKAtrkt 402
Cdd:cd05908 184 FIRR--PILWLKKAS----EHKATIVSSPNFGYKYFLKTLKPEKANdwdlssiRMILNGAepIDYELCHEFLDHMS---- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 403 wvdKYVLHKIQMLLGPNIRQLILGAAKSDVSAMRF--ARGAFGVEVLEGYGQTETSGPTTLQLVGdtrigcVGPPMACAM 480
Cdd:cd05908 254 ---KYGLKRNAILPVYGLAEASVGASLPKAQSPFKtiTLGRRHVTHGEPEPEVDKKDSECLTFVE------VGKPIDETD 324
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17541856 481 IKLID----VPELGYSvdkngGEVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGrFTAEGSLQIIDRRKNV 551
Cdd:cd05908 325 IRICDednkILPDGYI-----GHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIRNGRLVITGREKDI 393
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
263-679 |
1.41e-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: 93.16 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 263 LATISFTSGTTGRPKGVMLTHLNM-CSATMSCEEFEneAGVQDAYLSYLPLAHIYERLCLLSNFMIGSRIGFSRGDPKLL 341
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAANLlASAAGLHSRLG--FGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 342 VDdVQALAPRSFATVPRvidkihkavmkQVQdkplkkmilnaaiayKLYHYKMTgkatrKTWVDKyvLHKIqmLLGpnir 421
Cdd:cd17630 80 ED-LAPPGVTHVSLVPT-----------QLQ---------------RLLDSGQG-----PAALKS--LRAV--LLG---- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 422 qlilGAAKSDVSAMRFArgAFGVEVLEGYGQTETSGPTTLQLVGDTRIGCVGPPMACAMIKLIDvpelgysvdknGGEVL 501
Cdd:cd17630 120 ----GAPIPPELLERAA--DRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVE-----------DGEIW 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 502 VKGHNVTSGYYKNPEAtaSSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFkMPQGKFVAPDLTESLYTSSSFVQQIYVH 581
Cdd:cd17630 183 VGGASLAMGYLRGQLV--PEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAVRDAFVV 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 582 GDMEKPW---LVAIVVPDPEylasyaltkhningktyeqlcnipiLADDVLRQFVelteEDKRPRYEgvygvhlTPVAFS 658
Cdd:cd17630 260 GVPDEELgqrPVAVIVGRGP-------------------------ADPAELRAWL----KDKLARFK-------LPKRIY 303
|
410 420
....*....|....*....|..
gi 17541856 659 AENGLT-TPTLKNKRNAIAQFF 679
Cdd:cd17630 304 PVPELPrTGGGKVDRRALRAWL 325
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
256-609 |
1.71e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 95.87 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 256 VPPTPET-LATISFTSGTTGRPKGVMLTHLNMCSAT-MSCEEFENEAGVQDAYLSYLPLAHIYERLCLLS-NFMIGSR-I 331
Cdd:PRK06710 200 VPCDPENdLALLQYTGGTTGFPKGVMLTHKNLVSNTlMGVQWLYNCKEGEEVVLGVLPFFHVYGMTAVMNlSIMQGYKmV 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 332 GFSRGDPKLLVDDVQALAPRSFATVPrvidKIHKAVMkqvqDKPLKKmilnaaiayklyHYKMTgkatrktwvdkyvlhk 411
Cdd:PRK06710 280 LIPKFDMKMVFEAIKKHKVTLFPGAP----TIYIALL----NSPLLK------------EYDIS---------------- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 412 iqmllgpNIRQLILGAAKSDVSAMRFARGAFGVEVLEGYGQTETSGPTTLQLVGDTRI-GCVGPPMACAMIKLIDVpELG 490
Cdd:PRK06710 324 -------SIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVpGSIGVPWPDTEAMIMSL-ETG 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 491 YSVDKNG-GEVLVKGHNVTSGYYKNPEATASSFtEDGYMKTGDIGRFTAEGSLQIIDRRKNVFkMPQGKFVAPDLTESLY 569
Cdd:PRK06710 396 EALPPGEiGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREVEEVL 473
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 17541856 570 TSSSFVQQIyvhgdmekpwlVAIVVPDP---EYLASYALTKHN 609
Cdd:PRK06710 474 YEHEKVQEV-----------VTIGVPDPyrgETVKAFVVLKEG 505
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
150-550 |
2.01e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 95.61 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 150 NRPEWILSEMAIHNFSNVSVPLYDTITNDDMHYITNLCEISLMFVDAEIK-TKQLIRDKSylSSLKYIVQFNECSDD--- 225
Cdd:PRK07786 76 NRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALApVATAVRDIV--PLLSTVVVAGGSSDDsvl 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 226 -IKEMARENDfrlwsfnefvemgkkqkhrPHVPPT--PE-TLATISFTSGTTGRPKGVMLTHLNMCSATMSCEeFENEAG 301
Cdd:PRK07786 154 gYEDLLAEAG-------------------PAHAPVdiPNdSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCL-RTNGAD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 302 V-QDAYLSYLPLAHIYERLCLLSNFMIGSRI------GFsrgDPKLLVDDVQALAPRSFATVPRVIDKIHKAvmKQVQDK 374
Cdd:PRK07786 214 InSDVGFVGVPLFHIAGIGSMLPGLLLGAPTviyplgAF---DPGQLLDVLEAEKVTGIFLVPAQWQAVCAE--QQARPR 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 375 PLKkmilnaaiayklyhykmtgkatrktwvdkyvlhkiqmllgpnIRQLILGAAKSDVSAMRFARGAF-GVEVLEGYGQT 453
Cdd:PRK07786 289 DLA------------------------------------------LRVLSWGAAPASDTLLRQMAATFpEAQILAAFGQT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 454 ETSgPTTLQLVGD---TRIGCVGPPMACAMIKLID-----VP--ELGysvdknggEVLVKGHNVTSGYYKNPEATASSFt 523
Cdd:PRK07786 327 EMS-PVTCMLLGEdaiRKLGSVGKVIPTVAARVVDenmndVPvgEVG--------EIVYRAPTLMSGYWNNPEATAEAF- 396
|
410 420
....*....|....*....|....*..
gi 17541856 524 EDGYMKTGDIGRFTAEGSLQIIDRRKN 550
Cdd:PRK07786 397 AGGWFHSGDLVRQDEEGYVWVVDRKKD 423
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
127-551 |
2.77e-20 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 94.67 E-value: 2.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 127 ASqAIRKLGIeiGEESKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDDMHYITNLCEISLMFVDAEiktkqlird 206
Cdd:cd12118 43 AS-ALAALGI--SRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVDRE--------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 207 ksylsslkyivqFNecsddikemarendfrlwsFNEFVEMGKKQKhrPHVPPTPETLA-TISFTSGTTGRPKGVMLTH-- 283
Cdd:cd12118 111 ------------FE-------------------YEDLLAEGDPDF--EWIPPADEWDPiALNYTSGTTGRPKGVVYHHrg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 284 --LNMCSATMsceefENEAGVQDAYLSYLPLAHiyerlC-----LLSNFMI-GSRIGFSRGDPKLLVDDVQALAPRSFAT 355
Cdd:cd12118 158 ayLNALANIL-----EWEMKQHPVYLWTLPMFH-----CngwcfPWTVAAVgGTNVCLRKVDAKAIYDLIEKHKVTHFCG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 356 VPRVIDkihkavmkqvqdkplkkMILNAAIAYKlyhykmtgkatrktwvdKYVLHKIQMLLGpnirqlilGAAKSdvSAM 435
Cdd:cd12118 228 APTVLN-----------------MLANAPPSDA-----------------RPLPHRVHVMTA--------GAPPP--AAV 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 436 RFARGAFGVEVLEGYGQTETSGPTTLqlvgdtrigCVG-------PPMACAMIKL-----------IDV--PELGYSVDK 495
Cdd:cd12118 264 LAKMEELGFDVTHVYGLTETYGPATV---------CAWkpewdelPTEERARLKArqgvryvgleeVDVldPETMKPVPR 334
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 17541856 496 NG---GEVLVKGHNVTSGYYKNPEATASSFtEDGYMKTGDIGRFTAEGSLQIIDRRKNV 551
Cdd:cd12118 335 DGktiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDI 392
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
101-595 |
3.94e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 94.23 E-value: 3.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 101 GKRVMKDGKLEWEWISYDQAfetSDHASQAIRKLGIEIGEesKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDDM 180
Cdd:PRK08316 26 DKTALVFGDRSWTYAELDAA---VNRVAAALLDLGLKKGD--RVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 181 HYITNLCEISLMFVDAEIKtkQLIRDKSYLSSLKYIVQfnECSDDIKEM-ARENDFRLWSFNEFVEMgkkqkhrPHVPPT 259
Cdd:PRK08316 101 AYILDHSGARAFLVDPALA--PTAEAALALLPVDTLIL--SLVLGGREApGGWLDFADWAEAGSVAE-------PDVELA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 260 PETLATISFTSGTTGRPKGVMLTHLNMCSATMSCeEFENEAGVQDAYLSYLPLAHIYERLC-LLSNFMIGSR-IGFSRGD 337
Cdd:PRK08316 170 DDDLAQILYTSGTESLPKGAMLTHRALIAEYVSC-IVAGDMSADDIPLHALPLYHCAQLDVfLGPYLYVGATnVILDAPD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 338 PKLLVDDVQALAPRSFATVPRVidkihkavmkqvqdkplkkmilnaaiayklyhykmtgkatrktWvdkyvlhkIQMLLG 417
Cdd:PRK08316 249 PELILRTIEAERITSFFAPPTV-------------------------------------------W--------ISLLRH 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 418 PNIrqlilgaAKSDVSAMRfaRGAFG-----VEVLEG-------------YGQTETsGP--TTLQLV-GDTRIGCVGPPM 476
Cdd:PRK08316 278 PDF-------DTRDLSSLR--KGYYGasimpVEVLKElrerlpglrfyncYGQTEI-APlaTVLGPEeHLRRPGSAGRPV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 477 ACAMIKLID-----VPElgysvdknG--GEVLVKGHNVTSGYYKNPEATASSFtEDGYMKTGDIGRFTAEGSLQIIDRRK 549
Cdd:PRK08316 348 LNVETRVVDddgndVAP--------GevGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKK 418
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 17541856 550 NVFKMpQGKFVAP-DLTESLYTSSSfVQQIYVHGDMEKPWL---VAIVVP 595
Cdd:PRK08316 419 DMIKT-GGENVASrEVEEALYTHPA-VAEVAVIGLPDPKWIeavTAVVVP 466
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
253-603 |
9.17e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 92.95 E-value: 9.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 253 RPHVPPtpETLATISFTSGTTGRPKGVMLTHLNMCSATMSceeFENEAGVqDAYLSYL---PLAHIyerLCLLSN----F 325
Cdd:PRK09088 129 TPSIPP--ERVSLILFTSGTSGQPKGVMLSERNLQQTAHN---FGVLGRV-DAHSSFLcdaPMFHI---IGLITSvrpvL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 326 MIGSRIGFSRG-DPK----LLVDdvQALAPRSFATVPRVidkihkavMKQVQDKPlkkmilnAAIAYKLYHYK--MTGKA 398
Cdd:PRK09088 200 AVGGSILVSNGfEPKrtlgRLGD--PALGITHYFCVPQM--------AQAFRAQP-------GFDAAALRHLTalFTGGA 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 399 trktwvdkyvlhkiqmllgPNIRQLILGAAksdvsamrfargAFGVEVLEGYGQTETSgpTTLQL-----VGDTRIGCVG 473
Cdd:PRK09088 263 -------------------PHAAEDILGWL------------DDGIPMVDGFGMSEAG--TVFGMsvdcdVIRAKAGAAG 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 474 PPMACAMIKLID---------VPelgysvdkngGEVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQI 544
Cdd:PRK09088 310 IPTPTVQTRVVDdqgndcpagVP----------GELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWV 379
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17541856 545 IDRRKNVFkMPQGKFVAPDLTESLYTSSSFVQQIYVHGDMEKPW-----LVAIVVP----DPEYLASY 603
Cdd:PRK09088 380 VDRKKDMF-ISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWgevgyLAIVPADgaplDLERIRSH 446
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
264-571 |
9.53e-20 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 93.37 E-value: 9.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 264 ATISFTSGTTGRPKGVMLTHLNMCSATMSCEEFENE----AGVQDAYLSYLPLAHIYErlclLSNFMIG------SRIGF 333
Cdd:PLN02574 201 AAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASqyeyPGSDNVYLAALPMFHIYG----LSLFVVGllslgsTIVVM 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 334 SRGDPKLLVDDVQALAPRSFATVPRVIDKIHKAVmKQVQDKPLKKMILNAaiayklyhykmTGKAtrktwvdkyvlhkiq 413
Cdd:PLN02574 277 RRFDASDMVKVIDRFKVTHFPVVPPILMALTKKA-KGVCGEVLKSLKQVS-----------CGAA--------------- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 414 mllgPNIRQLIlgaaksdvsaMRFARGAFGVEVLEGYGQTE-----TSGPTTLQLVGDTRIGCVGPPMACamiKLIDVPE 488
Cdd:PLN02574 330 ----PLSGKFI----------QDFVQTLPHVDFIQGYGMTEstavgTRGFNTEKLSKYSSVGLLAPNMQA---KVVDWST 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 489 LGYSVDKNGGEVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMpQGKFVAPDLTESL 568
Cdd:PLN02574 393 GCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQIAPADLEAV 471
|
...
gi 17541856 569 YTS 571
Cdd:PLN02574 472 LIS 474
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
261-613 |
1.10e-19 |
|
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: 91.17 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 261 ETLATISFTSGTTGRPKGVMLTHLNMCSATMSCEEFENEAGVQDAYLSYLPLAHIYERLCLLSNFMIGSR--IGFSRGDP 338
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLcvTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 339 KLLVDDVQALAPRSFATVPRVIDKIhkavmkqvqdkplkKMILNAAIAYKlyhykmtgkatrktwvdkyvlhkiqmllgP 418
Cdd:cd17635 81 KSLFKILTTNAVTTTCLVPTLLSKL--------------VSELKSANATV-----------------------------P 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 419 NIRQLILGAAKSDVSAMRFARGAFGVEVLEGYGQTETSGPTTLQLVGDTR-IGCVGPPMACAMIKLIDVPELGYSVDKNG 497
Cdd:cd17635 118 SLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLPTDDDSIeINAVGRPYPGVDVYLAATDGIAGPSASFG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 498 gEVLVKGHNVTSGYYKNPEATASSFTeDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMpQGKFVAPDLTESLYTSSSFVQQ 577
Cdd:cd17635 198 -TIWIKSPANMLGYWNNPERTAEVLI-DGWVNTGDLGERREDGFLFITGRSSESINC-GGVKIAPDEVERIAEGVSGVQE 274
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 17541856 578 --IYVHGDMEKPWLVAIVVPDPEYLASYALT--KHNINGK 613
Cdd:cd17635 275 caCYEISDEEFGELVGLAVVASAELDENAIRalKHTIRRE 314
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
259-536 |
1.67e-19 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 93.02 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 259 TPETLATISFTSGTTGRPKGVMLTHLNMCS------ATMSceEFENEAGVqdaYLSYLPLAHIYErlcllSNFMIGsrIG 332
Cdd:PRK08180 207 GPDTIAKFLFTSGSTGLPKAVINTHRMLCAnqqmlaQTFP--FLAEEPPV---LVDWLPWNHTFG-----GNHNLG--IV 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 333 FSRG-----D-----PKLL---VDDVQALAPRSFATVPRVIDKIHKAvMKQvqDKPLKKMILNAAiayKLYHYkmtGKAT 399
Cdd:PRK08180 275 LYNGgtlyiDdgkptPGGFdetLRNLREISPTVYFNVPKGWEMLVPA-LER--DAALRRRFFSRL---KLLFY---AGAA 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 400 rktwvdkyvlhkiqmlLGPNIRQLIlgaaksdvsaMRFARGAFG--VEVLEGYGQTETSGPTTLQLVGDTRIGCVGPPMA 477
Cdd:PRK08180 346 ----------------LSQDVWDRL----------DRVAEATCGerIRMMTGLGMTETAPSATFTTGPLSRAGNIGLPAP 399
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17541856 478 CAMIKLidVPelgysvdkNGG--EVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRF 536
Cdd:PRK08180 400 GCEVKL--VP--------VGGklEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRF 450
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
260-553 |
1.94e-19 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 92.55 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 260 PETLATISFTSGTTGRPKGVMLTHLNMCSATMS-------CEEfeneagvqDAYLSYLPLAHIYERLCLLSNFMIGS-RI 331
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSALIVQSLAkiaivgyGED--------DVYLHTAPLCHIGGLSSALAMLMVGAcHV 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 332 GFSRGDPKLLVDDVQALAPRSFATVPrvidkihkAVMKQVqdkplkkmilnaaIAYklyhykmtgkaTRKTWVDKyvlhk 411
Cdd:PLN02860 243 LLPKFDAKAALQAIKQHNVTSMITVP--------AMMADL-------------ISL-----------TRKSMTWK----- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 412 iqmlLGPNIRQLILGAAKSDVSAMRFARGAF-GVEVLEGYGQTET---------------SGPTTLQLVGDTRIGCVGPP 475
Cdd:PLN02860 286 ----VFPSVRKILNGGGSLSSRLLPDAKKLFpNAKLFSAYGMTEAcssltfmtlhdptleSPKQTLQTVNQTKSSSVHQP 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 476 MACAMIKLIDVPELGYSVDKNG--GEVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFK 553
Cdd:PLN02860 362 QGVCVGKPAPHVELKIGLDESSrvGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIK 441
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
254-548 |
2.09e-19 |
|
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: 91.17 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 254 PHVPPTPETLATISFTSGTTGRPKGVMLTHLNMCSATMSC-EEFENEAGvqDAYLSYLPLAH---IYErlcLLSNFMIGS 329
Cdd:TIGR01733 113 PDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLaRRYGLDPD--DRVLQFASLSFdasVEE---IFGALLAGA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 330 RIgfsrgdpkLLVDDVQALAPRSFATVPRVIDKIhkAVMKQVqdkPlkkmilnaaiayklyhykmtgkatrkTWVDKYVL 409
Cdd:TIGR01733 188 TL--------VVPPEDEERDDAALLAALIAEHPV--TVLNLT---P--------------------------SLLALLAA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 410 HKIQMLlgPNIRQLILG--AAKSDVsAMRFARGAFGVEVLEGYGQTETSGPTTLQLV-----GDTRIGCVGPPMACAMIk 482
Cdd:TIGR01733 229 ALPPAL--ASLRLVILGgeALTPAL-VDRWRARGPGARLINLYGPTETTVWSTATLVdpddaPRESPVPIGRPLANTRL- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 483 lidvpelgYSVDKNG--------GEVLVKGHNVTSGYYKNPEATASSFTEDGYM--------KTGDIGRFTAEGSLQIID 546
Cdd:TIGR01733 305 --------YVLDDDLrpvpvgvvGELYIGGPGVARGYLNRPELTAERFVPDPFAggdgarlyRTGDLVRYLPDGNLEFLG 376
|
..
gi 17541856 547 RR 548
Cdd:TIGR01733 377 RI 378
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
104-644 |
2.39e-19 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 92.18 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 104 VMKDGKLEWEWISYDQafETSDHASqAIRKLGIEIGEesKIGIYSNNRPEWILSEMAIHNFSNVSV---PLYDT------ 174
Cdd:PRK08315 36 VYRDQGLRWTYREFNE--EVDALAK-GLLALGIEKGD--RVGIWAPNVPEWVLTQFATAKIGAILVtinPAYRLseleya 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 175 ITNDDMH------------YITNLCEISlmfvdAEIKTKQLIRDKSY-LSSLKYIVQfnecsddikeMARENDFRLWSFN 241
Cdd:PRK08315 111 LNQSGCKaliaadgfkdsdYVAMLYELA-----PELATCEPGQLQSArLPELRRVIF----------LGDEKHPGMLNFD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 242 EFVEMGKKqkhrphvpPTPETLATIS------------FTSGTTGRPKGVMLTHLNmcsatmsceefeneagvqdaylsy 309
Cdd:PRK08315 176 ELLALGRA--------VDDAELAARQatldpddpiniqYTSGTTGFPKGATLTHRN------------------------ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 310 lplahiyerlcLLSN-FMIGSRIGFSRGDpKL-------------------------LVDDVQALAPrsfatvprvidki 363
Cdd:PRK08315 224 -----------ILNNgYFIGEAMKLTEED-RLcipvplyhcfgmvlgnlacvthgatMVYPGEGFDP------------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 364 hKAVMKQVQDKplkkmilnaaiayklyhykmtgKATrktwvdkyVLHK-----IQMLLGPN--------IRQLILGAAKS 430
Cdd:PRK08315 279 -LATLAAVEEE----------------------RCT--------ALYGvptmfIAELDHPDfarfdlssLRTGIMAGSPC 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 431 DVSAMRFARGAFGV-EVLEGYGQTETSgPTTLQ-LVGDT---RIGCVGPPMACAMIKLIDvPELGYSVDKNG-GEVLVKG 504
Cdd:PRK08315 328 PIEVMKRVIDKMHMsEVTIAYGMTETS-PVSTQtRTDDPlekRVTTVGRALPHLEVKIVD-PETGETVPRGEqGELCTRG 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 505 HNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRK--------NVFkmPQgkfvapDLTESLYTsssfvq 576
Cdd:PRK08315 406 YSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKdmiirggeNIY--PR------EIEEFLYT------ 471
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 577 qiyvhgdMEKPWLVAIV-VPDPEYlasyaltkhninGktyEQLCnipilADDVLRQFVELTEED------------KRPR 643
Cdd:PRK08315 472 -------HPKIQDVQVVgVPDEKY------------G---EEVC-----AWIILRPGATLTEEDvrdfcrgkiahyKIPR 524
|
.
gi 17541856 644 Y 644
Cdd:PRK08315 525 Y 525
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
259-599 |
6.21e-19 |
|
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: 89.89 E-value: 6.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 259 TPETLATISFTSGTTGRPKGVMLTH---LNMCSATMscEEFENEAGvqDAYLSYLPLA---HIYERLCLLSNfmiGSRIg 332
Cdd:cd05930 91 DPDDLAYVIYTSGSTGKPKGVMVEHrglVNLLLWMQ--EAYPLTPG--DRVLQFTSFSfdvSVWEIFGALLA---GATL- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 333 fsrgdpkLLVDDVQALAPRSFAtvpRVIDKiHKA-VMKQVqdkP-LKKMILNAAiayklyhykmtgkatrktwvdkyvlh 410
Cdd:cd05930 163 -------VVLPEEVRKDPEALA---DLLAE-EGItVLHLT---PsLLRLLLQEL-------------------------- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 411 kiQMLLGPNIRQLILGAAKSDVSAMR-FARGAFGVEVLEGYGQTETSGPTTLQLVGDTRIG----CVGPPMACAMIklid 485
Cdd:cd05930 203 --ELAALPSLRLVLVGGEALPPDLVRrWRELLPGARLVNLYGPTEATVDATYYRVPPDDEEdgrvPIGRPIPNTRV---- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 486 vpelgYSVDKNG--------GEVLVKGHNVTSGYYKNPEATASSFTEDGYM------KTGDIGRFTAEGSLQIIDRRKNV 551
Cdd:cd05930 277 -----YVLDENLrpvppgvpGELYIGGAGLARGYLNRPELTAERFVPNPFGpgermyRTGDLVRWLPDGNLEFLGRIDDQ 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 17541856 552 FKMpQGKFVAPDLTESLYTSSSFVQQIYV---HGDMEKPWLVAIVVPDPEY 599
Cdd:cd05930 352 VKI-RGYRIELGEIEAALLAHPGVREAAVvarEDGDGEKRLVAYVVPDEGG 401
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
255-595 |
1.32e-18 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 89.56 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 255 HVPPTPETL----ATISFTSGTTGRPKGVMLTHLNMCSATMS-CEEFEneAGVQDAYLSYLPLAHIYERLC-LLSNFMIG 328
Cdd:PRK05852 166 PATSTPEGLrpddAMIMFTGGTTGLPKMVPWTHANIASSVRAiITGYR--LSPRDATVAVMPLYHGHGLIAaLLATLASG 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 329 SRIGF-SRG--DPKLLVDDVQALAPRSFATVPrvidKIHKAVMKQVQDKPlkkmilnaaiayklyhykmtgkATRKTwvd 405
Cdd:PRK05852 244 GAVLLpARGrfSAHTFWDDIKAVGATWYTAVP----TIHQILLERAATEP----------------------SGRKP--- 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 406 kyvlhkiqmllgPNIRQLILGAAKSDVSAMRFARGAFGVEVLEGYGQTETsgptTLQlVGDTRIGCVG----PPMACAMI 481
Cdd:PRK05852 295 ------------AALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEA----THQ-VTTTQIEGIGqtenPVVSTGLV 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 482 KLIDVPEL------GYSVDKNG-GEVLVKGHNVTSGYYKNPEATASSFTeDGYMKTGDIGRFTAEGSLQIIDRRKNVFKM 554
Cdd:PRK05852 358 GRSTGAQIrivgsdGLPLPAGAvGEVWLRGTTVVRGYLGDPTITAANFT-DGWLRTGDLGSLSAAGDLSIRGRIKELINR 436
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 17541856 555 pQGKFVAPDLTESLYTSSSFVQQIYVHGDMEKPW---LVAIVVP 595
Cdd:PRK05852 437 -GGEKISPERVEGVLASHPNVMEAAVFGVPDQLYgeaVAAVIVP 479
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
253-548 |
1.93e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 88.89 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 253 RPHVP-------------PTPETLATISFTSGTTGRPKGVMLTHlnmcSATMSCEEFENEA---GVQDAYLSYLPLAHIY 316
Cdd:PRK07787 107 LPHVPvrlharswhrypePDPDAPALIVYTSGTTGPPKGVVLSR----RAIAADLDALAEAwqwTADDVLVHGLPLFHVH 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 317 ErLCL--LSNFMIGSR-IGFSRGDPkllvdDVQALAPRSFAT----VPRVIDKIhkavmkqVQDkplkkmiLNAAIAykl 389
Cdd:PRK07787 183 G-LVLgvLGPLRIGNRfVHTGRPTP-----EAYAQALSEGGTlyfgVPTVWSRI-------AAD-------PEAARA--- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 390 yhykmtgkatrktwvdkyvlhkiqmlLGPnIRQLILGAAKSDVSAMRFARGAFGVEVLEGYGQTETSGPTTLQLVGDTRI 469
Cdd:PRK07787 240 --------------------------LRG-ARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRP 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 470 GCVGPPMACAMIKLID-----VPELGYSVdkngGEVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQI 544
Cdd:PRK07787 293 GWVGLPLAGVETRLVDedggpVPHDGETV----GELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRI 368
|
....
gi 17541856 545 IDRR 548
Cdd:PRK07787 369 VGRE 372
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
134-553 |
3.85e-18 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 88.30 E-value: 3.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 134 LGIEIGEesKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDDMHYITNLCEISLMFVDAEIKtKQLIRDKSYLSSL 213
Cdd:PRK05620 59 LGITGDQ--RVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPRLA-EQLGEILKECPCV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 214 KYIVQFNECSDDIKEMARENDFRLWSFNEFVEMGKKQKHRPHVPPTpeTLATISFTSGTTGRPKGVMLTHLNMCSATMS- 292
Cdd:PRK05620 136 RAVVFIGPSDADSAAAHMPEGIKVYSYEALLDGRSTVYDWPELDET--TAAAICYSTGTTGAPKGVVYSHRSLYLQSLSl 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 293 --CEEFENEAGVqdAYLSYLPLAHIYERLCLLSNFMIGSRIGFSRGD--PKLLVDDVQALAPRSFATVPRVIDKIHKAVM 368
Cdd:PRK05620 214 rtTDSLAVTHGE--SFLCCVPIYHVLSWGVPLAAFMSGTPLVFPGPDlsAPTLAKIIATAMPRVAHGVPTLWIQLMVHYL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 369 KqvqdKPLKKMILnaaiayklyhykmtgkatrktwvdkyvlhkiqmllgpniRQLILGAAKSDVSAMRFARGAFGVEVLE 448
Cdd:PRK05620 292 K----NPPERMSL---------------------------------------QEIYVGGSAVPPILIKAWEERYGVDVVH 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 449 GYGQTETSGPTTLQ-----LVGDTRIG---CVGPPMACAMIKLIDVPELGYSVDKNGGEVLVKGHNVTSGYYKNP----- 515
Cdd:PRK05620 329 VWGMTETSPVGTVArppsgVSGEARWAyrvSQGRFPASLEYRIVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPteegg 408
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 17541856 516 -----------EATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFK 553
Cdd:PRK05620 409 gaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIR 457
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
240-551 |
4.06e-18 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 88.40 E-value: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 240 FNEFVEMGKKqkHR-PHVPPTPETLATISFTSGTTGRPKGVMLTHLNMCSATMSCEEFENEAGV----QDAYLSYLPLAH 314
Cdd:PRK08751 188 FREALALGRK--HSmPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKleegCEVVITALPLYH 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 315 IYerlCLLSNFMIGSRIGfsrGDPKLLVDdvqalaPRSFATVPRVIDKIHKAVMKQVQDkpLKKMILNAAiayklyhykm 394
Cdd:PRK08751 266 IF---ALTANGLVFMKIG---GCNHLISN------PRDMPGFVKELKKTRFTAFTGVNT--LFNGLLNTP---------- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 395 tgkatrktWVDKYVLHKIQMLLGPnirqlilGAAKSDVSAMRFARgAFGVEVLEGYGQTETS-----GPTTLQLVGdtri 469
Cdd:PRK08751 322 --------GFDQIDFSSLKMTLGG-------GMAVQRSVAERWKQ-VTGLTLVEAYGLTETSpaaciNPLTLKEYN---- 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 470 GCVGPPMAC--AMIKlidvpelgysvDKNG--------GEVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAE 539
Cdd:PRK08751 382 GSIGLPIPStdACIK-----------DDAGtvlaigeiGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQ 450
|
330
....*....|..
gi 17541856 540 GSLQIIDRRKNV 551
Cdd:PRK08751 451 GFVYIVDRKKDM 462
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
72-598 |
1.66e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 86.19 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 72 PLQHGWFEGVLTTySGIRRGPtvggkemlGKRVMKDGKLEWewiSYDQAFETSDHASQAIRKLGIEIGeeSKIGIYSNNR 151
Cdd:PRK06188 7 LLHSGATYGHLLV-SALKRYP--------DRPALVLGDTRL---TYGQLADRISRYIQAFEALGLGTG--DAVALLSLNR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 152 PEWILSEMAIHNFSNVSVPLYDTITNDDMHYITNLCEISLMFVDAEIKTKQLIRDKSYLSSLKYIVQFNECSDdikemar 231
Cdd:PRK06188 73 PEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGISTLIVDPAPFVERALALLARVPSLKHVLTLGPVPD------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 232 endfrlwsFNEFVEMGKKQKHRPHVPPT-PETLATISFTSGTTGRPKGVMLTHLNMcsATMS---CEEFENEAGVQdaYL 307
Cdd:PRK06188 146 --------GVDLLAAAAKFGPAPLVAAAlPPDIAGLAYTGGTTGKPKGVMGTHRSI--ATMAqiqLAEWEWPADPR--FL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 308 SYLPLAHIYERLcLLSNFMIGSRIGFSRG-DPkllvddvqalaprsfATVPRVI--DKIhKAVMKqvqdkpLKKMIlnaa 384
Cdd:PRK06188 214 MCTPLSHAGGAF-FLPTLLRGGTVIVLAKfDP---------------AEVLRAIeeQRI-TATFL------VPTMI---- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 385 iaYKLyhykMTGKATRKTwvDkyvLHKIQMLLgpnirqliLGAakSDVSAMRFARG--AFGVEVLEGYGQTETSGPTTLQ 462
Cdd:PRK06188 267 --YAL----LDHPDLRTR--D---LSSLETVY--------YGA--SPMSPVRLAEAieRFGPIFAQYYGQTEAPMVITYL 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 463 LVGD------TRIGCVGPPMACAMIKLIDvpELGYSVdKNG--GEVLVKGHNVTSGYYKNPEATASSFtEDGYMKTGDIG 534
Cdd:PRK06188 326 RKRDhdpddpKRLTSCGRPTPGLRVALLD--EDGREV-AQGevGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVA 401
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17541856 535 RFTAEGSLQIIDRRK--------NVFkmpqgkfvaPDLTESLYTSSSFVQQIYVHGDMEKPW---LVAIVVPDPE 598
Cdd:PRK06188 402 REDEDGFYYIVDRKKdmivtggfNVF---------PREVEDVLAEHPAVAQVAVIGVPDEKWgeaVTAVVVLRPG 467
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
257-549 |
8.32e-17 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 84.24 E-value: 8.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 257 PPTPETLATISFTSGTTGRPKGVMLTHLNM-----CSATMSceefenEAGVQDAYLSYLPLAHIYERL-CLLSNF----- 325
Cdd:PRK07529 209 PIGPDDVAAYFHTGGTTGMPKLAQHTHGNEvanawLGALLL------GLGPGDTVFCGLPLFHVNALLvTGLAPLargah 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 326 -MIGSRIGFsRGDPklLVDD----VQALAPRSFATVPRVIdkihkAVMKQVqdkPlkkmilnaaiayklyhykmtgkatr 400
Cdd:PRK07529 283 vVLATPQGY-RGPG--VIANfwkiVERYRINFLSGVPTVY-----AALLQV---P------------------------- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 401 ktwVDkyvlhkiqmllGPNIRQL---ILGAAKSDVSAMRFARGAFGVEVLEGYGQTE-TSGPTTLQLVGDTRIGCVGPPM 476
Cdd:PRK07529 327 ---VD-----------GHDISSLryaLCGAAPLPVEVFRRFEAATGVRIVEGYGLTEaTCVSSVNPPDGERRIGSVGLRL 392
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17541856 477 ACAMIKLIDVPELG-YSVDKNGGEV---LVKGHNVTSGYYkNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRK 549
Cdd:PRK07529 393 PYQRVRVVILDDAGrYLRDCAVDEVgvlCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAK 468
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
259-598 |
1.07e-16 |
|
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: 83.36 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 259 TPETLATISFTSGTTGRPKGVMLTHLNMCSATMS-CEEFEneAGVQDAYL---SYLPLAHIYERLC-LLSNFM--IGSRi 331
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAhGRALG--LTSESRVLqfaSYTFDVSILEIFTtLAAGGClcIPSE- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 332 gfsrgdpKLLVDDVQALAPRSFAT----VPRVIDKIHKAVMkqvqdkplkkmilnaaiayklyhykmtgkatrktwvdky 407
Cdd:cd05918 181 -------EDRLNDLAGFINRLRVTwaflTPSVARLLDPEDV--------------------------------------- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 408 vlhkiqmllgPNIRQLILG--AAKSDVsamrFARGAFGVEVLEGYGQTETSGPTTLQLVG-DTRIGCVGPPMACAMikli 484
Cdd:cd05918 215 ----------PSLRTLVLGgeALTQSD----VDTWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRPLGATC---- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 485 dvpelgYSVDKNG----------GEVLVKGHNVTSGYYKNPEATASSFTED------------GYM-KTGDIGRFTAEGS 541
Cdd:cd05918 277 ------WVVDPDNhdrlvpigavGELLIEGPILARGYLNDPEKTAAAFIEDpawlkqegsgrgRRLyRTGDLVRYNPDGS 350
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17541856 542 LQIIDRRKNVFKMpQGKFVapDLTE---SLYTSSSFVQQIYV-----HGDMEKPWLVAIVVPDPE 598
Cdd:cd05918 351 LEYVGRKDTQVKI-RGQRV--ELGEiehHLRQSLPGAKEVVVevvkpKDGSSSPQLVAFVVLDGS 412
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
111-547 |
4.10e-16 |
|
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: 81.61 E-value: 4.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 111 EWEWISYDQAFETSDHASQAIRKLGIeiGEESKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDDMHYITNLCEIS 190
Cdd:cd17655 19 EDQTLTYRELNERANQLARTLREKGV--GPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 191 LMFVDAEIKTKqlirdksyLSSLKYIVQFNEcsDDIKEMARENdfrlwsfnefvemgkkqkhrPHVPPTPETLATISFTS 270
Cdd:cd17655 97 ILLTQSHLQPP--------IAFIGLIDLLDE--DTIYHEESEN--------------------LEPVSKSDDLAYVIYTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 271 GTTGRPKGVMLTHLNMCSATmsceEFENEAGVQDAYLSYLPLAHIYERLCLLSNFMI---GSRIGFSRGDPKLlvdDVQA 347
Cdd:cd17655 147 GSTGKPKGVMIEHRGVVNLV----EWANKVIYQGEHLRVALFASISFDASVTEIFASllsGNTLYIVRKETVL---DGQA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 348 LaprsfatvprvIDKIHKAVMKQVQDKPLkkmilnaaiayklyHYKMtgkatrktwvdkyvLHKIQMLLGPNIRQLILG- 426
Cdd:cd17655 220 L-----------TQYIRQNRITIIDLTPA--------------HLKL--------------LDAADDSEGLSLKHLIVGg 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 427 -AAKSDVSAMRFARGAFGVEVLEGYGQTETS-GPTTLQLVGDTRIGcVGPPmacamiklIDVPELG---YSVDKNG---- 497
Cdd:cd17655 261 eALSTELAKKIIELFGTNPTITNAYGPTETTvDASIYQYEPETDQQ-VSVP--------IGKPLGNtriYILDQYGrpqp 331
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 498 ----GEVLVKGHNVTSGYYKNPEATASSFTEDGYM------KTGDIGRFTAEGSLQIIDR 547
Cdd:cd17655 332 vgvaGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGR 391
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
254-608 |
6.98e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 81.09 E-value: 6.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 254 PHVPPTPETLATISFTSGTTGRPKGVMLTHLNMcsatmSCEEFENEAGV----QDAYLSYLPLAHIyeRLCLLsnfmigs 329
Cdd:PRK06145 142 PQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNL-----HWKSIDHVIALgltaSERLLVVGPLYHV--GAFDL------- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 330 rigfsrgdPKLLVddvqaLAPRSFATVPRVIDKihKAVMKQVQDKPLkkmilNAAIAYKLYHYKMTGKATRktwvDKYVL 409
Cdd:PRK06145 208 --------PGIAV-----LWVGGTLRIHREFDP--EAVLAAIERHRL-----TCAWMAPVMLSRVLTVPDR----DRFDL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 410 HKIQMLLGpnirqlilGAAKSDVSAMR-FARGAFGVEVLEGYGQTETSGPTTLQLVGDT--RIGCVGPPMACAMIKLIDv 486
Cdd:PRK06145 264 DSLAWCIG--------GGEKTPESRIRdFTRVFTRARYIDAYGLTETCSGDTLMEAGREieKIGSTGRALAHVEIRIAD- 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 487 pELGYSVDKN-GGEVLVKGHNVTSGYYKNPEATASSFTeDGYMKTGDIGRFTAEGSLQIIDRRKNVFkMPQGKFVAPDLT 565
Cdd:PRK06145 335 -GAGRWLPPNmKGEICMRGPKVTKGYWKDPEKTAEAFY-GDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEV 411
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 17541856 566 ESLYTSSSFVQQIYVHGDMEKPW---LVAIVVPDP-EYLASYALTKH 608
Cdd:PRK06145 412 ERVIYELPEVAEAAVIGVHDDRWgerITAVVVLNPgATLTLEALDRH 458
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
254-598 |
1.04e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 80.86 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 254 PHVPPTPETLATISFTSGTTGRPKGVMLTHLNMCSATMSCEEFENEAGVQDAYLSYLPLAHIY-ERLCLLSNFMIGSR-I 331
Cdd:PRK06178 202 PLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAgENFGLLFPLFSGATlV 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 332 GFSRGDPKLLVDDVQALaprsfatvprvidKIHKAVMkqVQDKPLKKMILNAAIAYKLYHYKMTGKATrktWVDKyvlhk 411
Cdd:PRK06178 282 LLARWDAVAFMAAVERY-------------RVTRTVM--LVDNAVELMDHPRFAEYDLSSLRQVRVVS---FVKK----- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 412 iqmlLGPNIRQlilgaaksdvsamRFaRGAFGVEVLEG-YGQTETSGPTTLQL---VGD----TRIGCVGPPMACAMIKL 483
Cdd:PRK06178 339 ----LNPDYRQ-------------RW-RALTGSVLAEAaWGMTETHTCDTFTAgfqDDDfdllSQPVFVGLPVPGTEFKI 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 484 ID------VPeLGYSvdkngGEVLVKGHNVTSGYYKNPEATASSFtEDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMpQG 557
Cdd:PRK06178 401 CDfetgelLP-LGAE-----GEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV-NG 472
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 17541856 558 KFVAPDLTESLYTSSSFVQQIYVHG--DMEKPWL-VAIVVPDPE 598
Cdd:PRK06178 473 MSVFPSEVEALLGQHPAVLGSAVVGrpDPDKGQVpVAFVQLKPG 516
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
257-551 |
2.54e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 79.22 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 257 PPTPETLA-TISFTSGTTGRPKGVMLTH----LNMCSATMSCEefeneAGVQDAYLSYLPLAHiyerlCLLSNF------ 325
Cdd:PRK08162 177 LPADEWDAiALNYTSGTTGNPKGVVYHHrgayLNALSNILAWG-----MPKHPVYLWTLPMFH-----CNGWCFpwtvaa 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 326 MIGSRIGFSRGDPKLLVDDVQALAPRSFATVPRVIDkihkavmkqvqdkplkkMILNAAIAYKlyhykmtGKATRKtwvd 405
Cdd:PRK08162 247 RAGTNVCLRKVDPKLIFDLIREHGVTHYCGAPIVLS-----------------ALINAPAEWR-------AGIDHP---- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 406 kyvlhkiqmllgpnIRQLILGAA--KSDVSAMRfargAFGVEVLEGYGQTETSGPTTL--------------QLVGDTRI 469
Cdd:PRK08162 299 --------------VHAMVAGAAppAAVIAKME----EIGFDLTHVYGLTETYGPATVcawqpewdalpldeRAQLKARQ 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 470 GCVGPPMACAMIklIDvPELGYSVDKNG---GEVLVKGHNVTSGYYKNPEATASSFtEDGYMKTGDIGRFTAEGSLQIID 546
Cdd:PRK08162 361 GVRYPLQEGVTV--LD-PDTMQPVPADGetiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKD 436
|
....*
gi 17541856 547 RRKNV 551
Cdd:PRK08162 437 RSKDI 441
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
252-548 |
3.91e-15 |
|
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: 79.52 E-value: 3.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 252 HRPHVPPTPETLATISFTSGTTGRPKGVMLTHLNMCSATMSCEEfENEAGVQDAYLSYLPLAH---IYERLCLLSNfmiG 328
Cdd:COG1020 608 TNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQR-RYGLGPGDRVLQFASLSFdasVWEIFGALLS---G 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 329 SRIgfsrgdpkLLVDDVQALAPRSFAtvpRVIDKiHKA-VMKQVqdkP-LKKMILNAAIAyklyhykmtgkatrktwvdk 406
Cdd:COG1020 684 ATL--------VLAPPEARRDPAALA---ELLAR-HRVtVLNLT---PsLLRALLDAAPE-------------------- 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 407 yvlhkiqmlLGPNIRQLILG--AAKSDVSAmRFARGAFGVEVLEGYGQTETSGPTTLQLVGDTRIGC----VGPPMACAM 480
Cdd:COG1020 729 ---------ALPSLRLVLVGgeALPPELVR-RWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADGgsvpIGRPIANTR 798
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 481 IklidvpelgYSVDKNG--------GEVLVKGHNVTSGYYKNPEATASSFTEDGYM-------KTGDIGRFTAEGSLQII 545
Cdd:COG1020 799 V---------YVLDAHLqpvpvgvpGELYIGGAGLARGYLNRPELTAERFVADPFGfpgarlyRTGDLARWLPDGNLEFL 869
|
...
gi 17541856 546 DRR 548
Cdd:COG1020 870 GRA 872
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
252-598 |
8.91e-15 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 77.32 E-value: 8.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 252 HRPHVPPTPETLATISFTSGTTGRPKGVMLTHLNMCS--ATMsCEEFENEAGvqDAYLSYLPLA---HIYErlcLLSNFM 326
Cdd:cd17646 129 TPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNrlLWM-QDEYPLGPG--DRVLQKTPLSfdvSVWE---LFWPLV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 327 IGSRIGFSR----GDPKLLVddvqalaprsfatvpRVIDkihkavmkqvqdkplkkmilnaaiayklyHYKMTgkatrkt 402
Cdd:cd17646 203 AGARLVVARpgghRDPAYLA---------------ALIR-----------------------------EHGVT------- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 403 wvdkyVLHKIQMLLGPNIRQLILGAAKS-----------DVSAMRFARGAFGVEVLEGYGQTETS-GPTTLQLVGDTRIG 470
Cdd:cd17646 232 -----TCHFVPSMLRVFLAEPAAGSCASlrrvfcsgealPPELAARFLALPGAELHNLYGPTEAAiDVTHWPVRGPAETP 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 471 CV--GPPMACAMIKLID-----VPelgysvDKNGGEVLVKGHNVTSGYYKNPEATASSFTED-----GYM-KTGDIGRFT 537
Cdd:cd17646 307 SVpiGRPVPNTRLYVLDdalrpVP------VGVPGELYLGGVQLARGYLGRPALTAERFVPDpfgpgSRMyRTGDLARWR 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17541856 538 AEGSLQIIDRRKNVFKMpQGKFVAPDLTESLYTSSSFVQQIYV---HGDMEKPWLVAIVVPDPE 598
Cdd:cd17646 381 PDGALEFLGRSDDQVKI-RGFRVEPGEIEAALAAHPAVTHAVVvarAAPAGAARLVGYVVPAAG 443
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
268-545 |
2.56e-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: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 268 FTSGTTGRPKGVMLTHLN-MCSATMSceefeneAGVQDA-----YLSYLPLAHIYERLCLLSNFMIGSRIGF-SRGDPKL 340
Cdd:cd17636 7 YTAAFSGRPNGALLSHQAlLAQALVL-------AVLQAIdegtvFLNSGPLFHIGTLMFTLATFHAGGTNVFvRRVDAEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 341 LVDDVQALAPRSFATVPRVIDKIHKavmkqvqdkplkkmiLNAAIAYklyhykmtgkatrktwvdkyvlhkiqmllgpNI 420
Cdd:cd17636 80 VLELIEAERCTHAFLLPPTIDQIVE---------------LNADGLY-------------------------------DL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 421 RQLILGAAKSDVSAMRFARGAFGVEVLEGYGQTETSGPTTLQLVGDTRIGCVGPPMACAMIKLIDvpELGYSV-DKNGGE 499
Cdd:cd17636 114 SSLRSSPAAPEWNDMATVDTSPWGRKPGGYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILD--EDGREVpDGEVGE 191
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 17541856 500 VLVKGHNVTSGYYKNPEATASSFTeDGYMKTGDIGRFTAEGSLQII 545
Cdd:cd17636 192 IVARGPTVMAGYWNRPEVNARRTR-GGWHHTNDLGRREPDGSLSFV 236
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
167-551 |
3.22e-14 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 75.94 E-value: 3.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 167 VSVPLYDTITNDDMHYITNLCEISLMFVDAEIKT----KQLIRDKSYLSSLKYIVQFN----ECSDDIKEMARENDFRLW 238
Cdd:PRK06087 100 VSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQtrpvDLILPLQNQLPQLQQIVGVDklapATSSLSLSQIIADYEPLT 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 239 SFnefvemgkkqkhrphVPPTPETLATISFTSGTTGRPKGVMLTHLNMCSATMS-CEEFENEAgvQDAYLSYLPLAHIYE 317
Cdd:PRK06087 180 TA---------------ITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAyCARLNLTW--QDVFMMPAPLGHATG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 318 RL-CLLSNFMIGSRigfsrgdpkllvddvqalaprsfatvprvidkihkAVMKQvqdkplkkmILNAAIAYKLYHYKmtg 396
Cdd:PRK06087 243 FLhGVTAPFLIGAR-----------------------------------SVLLD---------IFTPDACLALLEQQ--- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 397 katRKTWVdkyvlhkiqMLLGPNIRQLI--LGAAKSDVSAMRF------------ARGAF--GVEVLEGYGQTETSgPTT 460
Cdd:PRK06087 276 ---RCTCM---------LGATPFIYDLLnlLEKQPADLSALRFflcggttipkkvARECQqrGIKLLSVYGSTESS-PHA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 461 -------LQLVGDTRigcvGPPMACAMIKLID-----VPeLGysvdkNGGEVLVKGHNVTSGYYKNPEATASSFTEDGYM 528
Cdd:PRK06087 343 vvnlddpLSRFMHTD----GYAAAGVEIKVVDearktLP-PG-----CEGEEASRGPNVFMGYLDEPELTARALDEEGWY 412
|
410 420
....*....|....*....|...
gi 17541856 529 KTGDIGRFTAEGSLQIIDRRKNV 551
Cdd:PRK06087 413 YSGDLCRMDEAGYIKITGRKKDI 435
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
259-598 |
1.14e-13 |
|
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: 73.88 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 259 TPETLATISFTSGTTGRPKGVMLTHLN---MCSATMSCEEFeNEAGVQDAYLSY----------LPLAHiyerlcllsnf 325
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANvlaLFAATQRWFGF-NEDDVWTLFHSYafdfsvweiwGALLH----------- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 326 miGSRIgfsrgdpkLLVDDVQALAPRSFAtvpRVIDKIHKAVMKQVqdkPlkkmilnAAIaYKLyhykMTGKATRKTWVd 405
Cdd:cd17643 159 --GGRL--------VVVPYEVARSPEDFA---RLLRDEGVTVLNQT---P-------SAF-YQL----VEAADRDGRDP- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 406 kyvlhkiqmllgPNIRQLILGAAKSDVSAMRFARGAFGV---EVLEGYGQTETSGPTT--------LQLVGDTRIGCvgp 474
Cdd:cd17643 210 ------------LALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTfrpldaadLPAAAASPIGR--- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 475 pmacamikliDVPELG-YSVDKNG--------GEVLVKGHNVTSGYYKNPEATASSFTEDG-------YMKTGDIGRFTA 538
Cdd:cd17643 275 ----------PLPGLRvYVLDADGrpvppgvvGELYVSGAGVARGYLGRPELTAERFVANPfggpgsrMYRTGDLARRLP 344
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17541856 539 EGSLQIIDRRKNVFKMpQGKFVAPDLTESLYTSSSFVQQIYV---HGDMEKPWLVAIVVPDPE 598
Cdd:cd17643 345 DGELEYLGRADEQVKI-RGFRIELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVADDG 406
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
250-542 |
1.99e-13 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 73.39 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 250 QKHRPHVPP----TPETLATISFTSGTTGRPKGVMLTHLNMCS-ATMSCEEFENEAGVQDayLSYLPLahiyerlcllsn 324
Cdd:PRK09274 159 RDGAAAPFPmadlAPDDMAAILFTSGSTGTPKGVVYTHGMFEAqIEALREDYGIEPGEID--LPTFPL------------ 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 325 fmigsrigFSRGDPKL----LVDDVQALAPrsfATV-PrviDKIHKAVmkqvQDKPLKKMILNAAIAYKLYHYkmtGKAt 399
Cdd:PRK09274 225 --------FALFGPALgmtsVIPDMDPTRP---ATVdP---AKLFAAI----ERYGVTNLFGSPALLERLGRY---GEA- 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 400 rktwvdkyvlHKIQMllgPNIRQLILGAAKSDVSAMRFARGAF--GVEVLEGYGQTEtSGPTTL----QLVGDTRIG--- 470
Cdd:PRK09274 283 ----------NGIKL---PSLRRVISAGAPVPIAVIERFRAMLppDAEILTPYGATE-ALPISSiesrEILFATRAAtdn 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 471 ----CVGPPMACAMIKLIDV-----PEL-GYSVDKNG--GEVLVKGHNVTSGYYKNPEATASSFTEDG----YMKTGDIG 534
Cdd:PRK09274 349 gagiCVGRPVDGVEVRIIAIsdapiPEWdDALRLATGeiGEIVVAGPMVTRSYYNRPEATRLAKIPDGqgdvWHRMGDLG 428
|
....*...
gi 17541856 535 RFTAEGSL 542
Cdd:PRK09274 429 YLDAQGRL 436
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
252-596 |
2.79e-13 |
|
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: 72.71 E-value: 2.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 252 HRPHVPPTPETLATISFTSGTTGRPKGVMLTHLNmcsatmsceefeneagvqdaylsylplahiyerlclLSNFM--IGS 329
Cdd:cd12116 117 AAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRN------------------------------------LVNFLhsMRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 330 RIGFSRGDpKLLvddvqALAPRSF--------------ATVpRVIDKIHkavmkQVQDKPLKKMILNAAIAyklyhykmT 395
Cdd:cd12116 161 RLGLGPGD-RLL-----AVTTYAFdisllelllpllagARV-VIAPRET-----QRDPEALARLIEAHSIT--------V 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 396 GKATRKTWvdkyvlhkiQMLLG------PNIRQLILGAAKSDVSAMRF-ARGAfgvEVLEGYGQTETSGPTTLQLVGDtr 468
Cdd:cd12116 221 MQATPATW---------RMLLDagwqgrAGLTALCGGEALPPDLAARLlSRVG---SLWNLYGPTETTIWSTAARVTA-- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 469 iGCVGPPmacamiklIDVPELGYSV---DKNG--------GEVLVKGHNVTSGYYKNPEATASSFTEDGYM-------KT 530
Cdd:cd12116 287 -AAGPIP--------IGRPLANTQVyvlDAALrpvppgvpGELYIGGDGVAQGYLGRPALTAERFVPDPFAgpgsrlyRT 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17541856 531 GDIGRFTAEGSLQIIDRRKNVFKMpQGKFVAPDLTESLYTSSSFVQQ--IYVHGDMEKPWLVAIVVPD 596
Cdd:cd12116 358 GDLVRRRADGRLEYLGRADGQVKI-RGHRIELGEIEAALAAHPGVAQaaVVVREDGGDRRLVAYVVLK 424
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
250-598 |
3.89e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 73.45 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 250 QKHRPHVPPTPETLATISFTSGTTGRPKGVMLTHLNMCSATMSCEEFENeAGVQDAYLSYLPLAHIYERLCLLSNFMIGS 329
Cdd:PRK12316 3185 AEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYG-LGVGDRVLQFTTFSFDVFVEELFWPLMSGA 3263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 330 RIgfsrgdpkLLVDDVQALAPRsfatvpRVIDKIHKAVMKQVQdkplkkmilnaaiayklyhykmtgkATRKTWVDKYVL 409
Cdd:PRK12316 3264 RV--------VLAGPEDWRDPA------LLVELINSEGVDVLH-------------------------AYPSMLQAFLEE 3304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 410 HKIQMLLGpnIRQLILG--AAKSDVSAMRFARGAfgveVLEGYGQTETSGPTTLQLVGDTRIGC--VGPPMACAMIKLID 485
Cdd:PRK12316 3305 EDAHRCTS--LKRIVCGgeALPADLQQQVFAGLP----LYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILD 3378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 486 VpELGYSVDKNGGEVLVKGHNVTSGYYKNPEATASSFTEDGYM------KTGDIGRFTAEGSLQIIDRRKNVFKMpQGKF 559
Cdd:PRK12316 3379 G-SLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVpgerlyRTGDLARYRADGVIEYIGRVDHQVKI-RGFR 3456
|
330 340 350
....*....|....*....|....*....|....*....
gi 17541856 560 VAPDLTESLYTSSSFVQQIYVHGDmEKPWLVAIVVPDPE 598
Cdd:PRK12316 3457 IELGEIEARLLEHPWVREAVVLAV-DGRQLVAYVVPEDE 3494
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
258-551 |
6.31e-13 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 71.97 E-value: 6.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 258 PTPETLA------------TISFTSGTTGRPKGVMLTHLNMCSATMSCEeFENEAGVQDAYLSYLPLAHiyerlCLLSNF 325
Cdd:PLN03102 171 PTPSLVArmfriqdehdpiSLNYTSGTTADPKGVVISHRGAYLSTLSAI-IGWEMGTCPVYLWTLPMFH-----CNGWTF 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 326 MIGSRigfSRGDPKLLVDDVqalaprsfaTVPRVIDKIHKAVMKQVQDKPlkkmilnaaiayKLYHYKMTGKATRKTwvd 405
Cdd:PLN03102 245 TWGTA---ARGGTSVCMRHV---------TAPEIYKNIEMHNVTHMCCVP------------TVFNILLKGNSLDLS--- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 406 kyvlHKiqmllGPNIRQLILGAAKSDVSAMRFARgaFGVEVLEGYGQTETSGPTTL--------------QLVGDTRIGC 471
Cdd:PLN03102 298 ----PR-----SGPVHVLTGGSPPPAALVKKVQR--LGFQVMHAYGLTEATGPVLFcewqdewnrlpenqQMELKARQGV 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 472 VGPPMACAMIKLIDVPElgySVDKNG---GEVLVKGHNVTSGYYKNPEATASSFtEDGYMKTGDIGRFTAEGSLQIIDRR 548
Cdd:PLN03102 367 SILGLADVDVKNKETQE---SVPRDGktmGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRS 442
|
...
gi 17541856 549 KNV 551
Cdd:PLN03102 443 KDI 445
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
258-551 |
7.58e-13 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 71.62 E-value: 7.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 258 PTPETLATISFTSGTTGRPKGVMLTHLNMCSATMSCEEfENEAGVQDAYLSYLPLAHiyerlclLSNFMIGSRIgfsrgd 337
Cdd:PRK13295 194 PGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAE-RLGLGADDVILMASPMAH-------QTGFMYGLMM------ 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 338 PKLLvddvQAlaprsfatvprvidkihKAVMkqvQDkplkkmILNAAIAYKLYhykmtgKATRKTWV--------DkyvL 409
Cdd:PRK13295 260 PVML----GA-----------------TAVL---QD------IWDPARAAELI------RTEGVTFTmastpfltD---L 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 410 HKIQMLLGPNIRQL---ILGAAKSDVSAMRFARGAFGVEVLEGYGQTETsGPTTLQLVGD------TRIGCVGPPMAcam 480
Cdd:PRK13295 301 TRAVKESGRPVSSLrtfLCAGAPIPGALVERARAALGAKIVSAWGMTEN-GAVTLTKLDDpderasTTDGCPLPGVE--- 376
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17541856 481 IKLIDVPELGYSVDKNGgEVLVKGHNVTSGYYKNPEATASSFteDGYMKTGDIGRFTAEGSLQIIDRRKNV 551
Cdd:PRK13295 377 VRVVDADGAPLPAGQIG-RLQVRGCSNFGGYLKRPQLNGTDA--DGWFDTGDLARIDADGYIRISGRSKDV 444
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
262-553 |
9.35e-13 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 71.32 E-value: 9.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 262 TLATISFTSGTTGRPKGVMLTHL-NMCSATMSCEEFENEAGVQDAYLSYLPLAHiyerlcllSNfmiGSRIGFSrgdpkl 340
Cdd:PRK06018 178 TAAGMCYTSGTTGDPKGVLYSHRsNVLHALMANNGDALGTSAADTMLPVVPLFH--------AN---SWGIAFS------ 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 341 lvddvqalAPRSFAtvprvidkihKAVMkqvqdkPLKKMilNAAIAYKLYHY-KMTGKATRKT-WvdkyvlhkiQMLLG- 417
Cdd:PRK06018 241 --------APSMGT----------KLVM------PGAKL--DGASVYELLDTeKVTFTAGVPTvW---------LMLLQy 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 418 --------PNIRQLILGAAKSDVSAMRfARGAFGVEVLEGYGQTETSGPTTL--------QLVGDTRIGCVG----PPMA 477
Cdd:PRK06018 286 mekeglklPHLKMVVCGGSAMPRSMIK-AFEDMGVEVRHAWGMTEMSPLGTLaalkppfsKLPGDARLDVLQkqgyPPFG 364
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17541856 478 CAMiKLIDvpELGYSVDKNG---GEVLVKGHNVTSGYYKnpeATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFK 553
Cdd:PRK06018 365 VEM-KITD--DAGKELPWDGktfGRLKVRGPAVAAAYYR---VDGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIK 437
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
254-598 |
1.02e-12 |
|
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: 70.81 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 254 PHVPPTPETLATISFTSGTTGRPKGVMLTH------LNMCSATMSCEEFeneAGVQDAY-----LSylplahIYERLCLL 322
Cdd:cd12115 98 RLVLTDPDDLAYVIYTSGSTGRPKGVAIEHrnaaafLQWAAAAFSAEEL---AGVLASTsicfdLS------VFELFGPL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 323 SnfmIGSRIgfsrgdpkLLVDDVQAL--APRS-----FATVPRVIDKI--HKAVMKQVQdkplkkmILNAAiayklyhyk 393
Cdd:cd12115 169 A---TGGKV--------VLADNVLALpdLPAAaevtlINTVPSAAAELlrHDALPASVR-------VVNLA--------- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 394 mtGKATRKTWVdkyvlHKIQMLLGpnirqlilgaaksdvsamrfargafGVEVLEGYGQTETSGPTTLQLV--GDTRIGC 471
Cdd:cd12115 222 --GEPLPRDLV-----QRLYARLQ-------------------------VERVVNLYGPSEDTTYSTVAPVppGASGEVS 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 472 VGPPMACAMIklidvpelgYSVDKNG--------GEVLVKGHNVTSGYYKNPEATASSFTEDGYM------KTGDIGRFT 537
Cdd:cd12115 270 IGRPLANTQA---------YVLDRALqpvplgvpGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWR 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17541856 538 AEGSLQIIDRRKNVFKMpQGKFVAPDLTESLYTSSSFVQQ--IYVHGD-MEKPWLVAIVVPDPE 598
Cdd:cd12115 341 PDGLLEFLGRADNQVKV-RGFRIELGEIEAALRSIPGVREavVVAIGDaAGERRLVAYIVAEPG 403
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
116-553 |
1.11e-12 |
|
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: 70.44 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 116 SYDQAFETSDHASQAIRKLGIEIGEesKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDDMHYitnlceislmfvd 195
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGD--RVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEY------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 196 aEIKTkqlirdksylSSLKYIVqfnecSDDikemarendfrlwsfnefvemgkkqkhrphvpptpETLATISFTSGTTGR 275
Cdd:cd05972 67 -RLEA----------AGAKAIV-----TDA-----------------------------------EDPALIYFTSGTTGL 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 276 PKGVMLTHlnmcsatmsceefeneagvqdaylSYlPLAHIyerlcllsnfmigsrigfsrgdpkLLVDDVQALAPrsfat 355
Cdd:cd05972 96 PKGVLHTH------------------------SY-PLGHI------------------------PTAAYWLGLRP----- 121
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 356 vprviDKIHKAV-----MKQVQDKPLKKMILNAAIAykLYHYKmtgKATRKTWVDKYVLHKIQMLLGP--NIRQLI---- 424
Cdd:cd05972 122 -----DDIHWNIadpgwAKGAWSSFFGPWLLGATVF--VYEGP---RFDAERILELLERYGVTSFCGPptAYRMLIkqdl 191
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 425 ----LGAAKSDVSA--------MRFARGAFGVEVLEGYGQTETSgpTTLQLVGDTRI--GCVGPPMACAMIKLIDvpELG 490
Cdd:cd05972 192 ssykFSHLRLVVSAgeplnpevIEWWRAATGLPIRDGYGQTETG--LTVGNFPDMPVkpGSMGRPTPGYDVAIID--DDG 267
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17541856 491 YSVDKNG-GEVLVK--GHNVTSGYYKNPEATASSFTEDgYMKTGDIGRFTAEGSLQIIDRRKNVFK 553
Cdd:cd05972 268 RELPPGEeGDIAIKlpPPGLFLGYVGDPEKTEASIRGD-YYLTGDRAYRDEDGYFWFVGRADDIIK 332
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
98-553 |
1.17e-12 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 70.94 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 98 EMLGKRVM-KDGKLEWewiSYDQAFETSDHASQAIRKLGIEIGEesKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTIT 176
Cdd:PRK06155 32 ERYPDRPLlVFGGTRW---TYAEAARAAAAAAHALAAAGVKRGD--RVALMCGNRIEFLDVFLGCAWLGAIAVPINTALR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 177 NDDMHYITNLCEISLMFVDAEiktkqlirdksYLSSLKYIvqfnecsdDIKEMAREndfRLWSFNEFVEMGKKQKHR--- 253
Cdd:PRK06155 107 GPQLEHILRNSGARLLVVEAA-----------LLAALEAA--------DPGDLPLP---AVWLLDAPASVSVPAGWStap 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 254 --------PHVPPTPETLATISFTSGTTGRPKGVMLTHLNM-CSATMSCEEFENEAGvqDAYLSYLPLAHI------YER 318
Cdd:PRK06155 165 lppldapaPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFyWWGRNSAEDLEIGAD--DVLYTTLPLFHTnalnafFQA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 319 LCLLSNFMIGSRIGFSRgdpklLVDDVQalapRSFATVPRVIDkihkAVMKQVQDKPlkkmilnaaiayklyhykmTGKA 398
Cdd:PRK06155 243 LLAGATYVLEPRFSASG-----FWPAVR----RHGATVTYLLG----AMVSILLSQP-------------------ARES 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 399 TRKtwvdkyvlHKIQMLLGPnirqlilGAAKSDVSAMRfARgaFGVEVLEGYGQTETSGPTTLQLvGDTRIGCVGPPMAC 478
Cdd:PRK06155 291 DRA--------HRVRVALGP-------GVPAALHAAFR-ER--FGVDLLDGYGSTETNFVIAVTH-GSQRPGSMGRLAPG 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17541856 479 AMIKLIDvpELGYSV-DKNGGEVLVKG---HNVTSGYYKNPEATASSFtEDGYMKTGDIGRFTAEGSLQIIDRRKNVFK 553
Cdd:PRK06155 352 FEARVVD--EHDQELpDGEPGELLLRAdepFAFATGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIKDAIR 427
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
260-551 |
1.35e-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: 341266 [Multi-domain] Cd Length: 359 Bit Score: 69.82 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 260 PETLATISFTSGTTGRPKGVMLTHLNMcSATMSCEEFENEAGVQDAYLSYLPLAHIYERLC-LLSNFMIGSRIGFS---- 334
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNE-VYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVtLLTPLASGAHVVLAgpag 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 335 -RGdpKLLVDDVQALAPR----SFATVPRVIdkihkAVMKQVQDkplkkmilNAAIAyklyhykmtgkatrktwvdkyvl 409
Cdd:cd05944 80 yRN--PGLFDNFWKLVERyritSLSTVPTVY-----AALLQVPV--------NADIS----------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 410 hkiqmllgpNIRQLILGAAKSDVSAMRFARGAFGVEVLEGYGQTETSGPTTLQLV-GDTRIGCVGPPM--ACAMIKLIDv 486
Cdd:cd05944 122 ---------SLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLpyARVRIKVLD- 191
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17541856 487 PELGYSVDKNGGEV---LVKGHNVTSGYYkNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNV 551
Cdd:cd05944 192 GVGRLLRDCAPDEVgeiCVAGPGVFGGYL-YTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDL 258
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
259-547 |
1.68e-12 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 70.09 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 259 TPETLATISFTSGTTGRPKGVMLTH--LNM-CSATMSCeeFENEAGvqDAYLSYLPLAHIYERLCLLSNFMIGSRIgfsr 335
Cdd:cd17649 92 HPRQLAYVIYTSGSTGTPKGVAVSHgpLAAhCQATAER--YGLTPG--DRELQFASFNFDGAHEQLLPPLICGACV---- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 336 gdpklLVDDVQALAPrsfatvPRVIDKIHKAVMKQVQDKPlkkmilnaaiayKLYHYKMTGKATRKTWVDKyvlhkiqml 415
Cdd:cd17649 164 -----VLRPDELWAS------ADELAEMVRELGVTVLDLP------------PAYLQQLAEEADRTGDGRP--------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 416 lgPNIRQLILGAAKSDVSAMRFARGAfGVEVLEGYGQTETSgPTTLQLVGDTRIGCVGPPMAcamiklIDVPELGYSV-- 493
Cdd:cd17649 212 --PSLRLYIFGGEALSPELLRRWLKA-PVRLFNAYGPTEAT-VTPLVWKCEAGAARAGASMP------IGRPLGGRSAyi 281
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 494 -DKNG--------GEVLVKGHNVTSGYYKNPEATASSFTEDGYM-------KTGDIGRFTAEGSLQIIDR 547
Cdd:cd17649 282 lDADLnpvpvgvtGELYIGGEGLARGYLGRPELTAERFVPDPFGapgsrlyRTGDLARWRDDGVIEYLGR 351
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
252-573 |
1.86e-12 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 70.51 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 252 HRPHVPPTPETLATISFTSGTTGRPKGVMLTHlnmCSATMSCEEFENEAGV--QDAYLSYLPLAHIYE-RLCLLSNFMIG 328
Cdd:PRK08043 356 RLAQVKQQPEDAALILFTSGSEGHPKGVVHSH---KSLLANVEQIKTIADFtpNDRFMSALPLFHSFGlTVGLFTPLLTG 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 329 SRIGFSrgdPkllvddvqalAPRSFATVPRVidkihkavmkqVQDKplkkmilNAAIAYK----LYHYKmtgkatrkTWV 404
Cdd:PRK08043 433 AEVFLY---P----------SPLHYRIVPEL-----------VYDR-------NCTVLFGtstfLGNYA--------RFA 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 405 DKYVLHKIqmllgpniRQLILGAAKSDVSAMRFARGAFGVEVLEGYGQTETSGPTTLQLVGDTRIGCVG---PPMACami 481
Cdd:PRK08043 474 NPYDFARL--------RYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGrilPGMDA--- 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 482 KLIDVPELgysvdKNGGEVLVKGHNVTSGYYK--NP---EATASS----FTEDGYMKTGDIGRFTAEGSLQIIDRRKNVF 552
Cdd:PRK08043 543 RLLSVPGI-----EQGGRLQLKGPNIMNGYLRveKPgvlEVPTAEnargEMERGWYDTGDIVRFDEQGFVQIQGRAKRFA 617
|
330 340
....*....|....*....|.
gi 17541856 553 KMpQGKFVAPDLTESLYTSSS 573
Cdd:PRK08043 618 KI-AGEMVSLEMVEQLALGVS 637
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
254-548 |
2.15e-12 |
|
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: 69.92 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 254 PHVPPTPETLATISFTSGTTGRPKGVMLTHlnmcsatmsceefeneAGVQdaylsylplahiyeRLCLLSNFmigsrIGF 333
Cdd:cd12117 129 PAVPVSPDDLAYVMYTSGSTGRPKGVAVTH----------------RGVV--------------RLVKNTNY-----VTL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 334 SRGDPKLLvddvqaLAPRSF--------------ATVpRVIDKihkavmkqvqDKPLKKMILNAAIAyklyhykmTGKAT 399
Cdd:cd12117 174 GPDDRVLQ------TSPLAFdastfeiwgallngARL-VLAPK----------GTLLDPDALGALIA--------EEGVT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 400 rKTWV-----DKYVLHKIQMLLGpnIRQLILGAAKSDVSAMRFARGAF-GVEVLEGYGQTETSGPTTLQLVgdTRIGCVG 473
Cdd:cd12117 229 -VLWLtaalfNQLADEDPECFAG--LRELLTGGEVVSPPHVRRVLAACpGLRLVNGYGPTENTTFTTSHVV--TELDEVA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 474 PPMacamikLIDVPELG---YSVDKNG--------GEVLVKGHNVTSGYYKNPEATASSFTEDGYM------KTGDIGRF 536
Cdd:cd12117 304 GSI------PIGRPIANtrvYVLDEDGrpvppgvpGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARW 377
|
330
....*....|..
gi 17541856 537 TAEGSLQIIDRR 548
Cdd:cd12117 378 LPDGRLEFLGRI 389
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
115-606 |
2.46e-12 |
|
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: 69.71 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 115 ISYDQAFETSDHASQAIRKLGIEigEESKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDDMHYITNLCEISLMFV 194
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVK--REERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 195 DAEIKtkQLIRDKSYLSS-LKYIVqfnecsdDIKEMARENDFRLWsFNEFVEmgkkqKHRPHVPPT---PETLATISFTS 270
Cdd:cd05959 108 SGELA--PVLAAALTKSEhTLVVL-------IVSGGAGPEAGALL-LAELVA-----AEAEQLKPAathADDPAFWLYSS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 271 GTTGRPKGVMLTHLNMcsaTMSCEEF-ENEAGVQ--DAYLSYLPLAHIYErlclLSN-----FMIGSRIGF--SRGDPKL 340
Cdd:cd05959 173 GSTGRPKGVVHLHADI---YWTAELYaRNVLGIRedDVCFSAAKLFFAYG----LGNsltfpLSVGATTVLmpERPTPAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 341 LVDDVQALAPRSFATVPrvidkihkavmkqvqdkplkkmILNAAiayklyhykmtgkatrktwvdkyvlhkiqMLLGPNi 420
Cdd:cd05959 246 VFKRIRRYRPTVFFGVP----------------------TLYAA-----------------------------MLAAPN- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 421 rqlilgAAKSDVSAMRFARGA---------------FGVEVLEGYGQTETSGPTTLQLVGDTRIGCVGPPMACAMIKLID 485
Cdd:cd05959 274 ------LPSRDLSSLRLCVSAgealpaevgerwkarFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRD 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 486 vpELGYSV-DKNGGEVLVKGHNVTSGYYKNPEATASSFtEDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMpQGKFVAPDL 564
Cdd:cd05959 348 --EDGGDVaDGEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDMLKV-SGIWVSPFE 423
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 17541856 565 TESLYTSSSFVQQIYV----HGD-MEKPwlVAIVVPDPEYLASYALT 606
Cdd:cd05959 424 VESALVQHPAVLEAAVvgveDEDgLTKP--KAFVVLRPGYEDSEALE 468
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
268-597 |
2.62e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 69.68 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 268 FTSGTTGRPKGVMLTHLNM--------CSATMSCEEfeneagvQDAYLSYLPLAH---IYerlcLLSNFMIGSRIGFSRG 336
Cdd:PRK07470 170 FTSGTTGRPKAAVLTHGQMafvitnhlADLMPGTTE-------QDASLVVAPLSHgagIH----QLCQVARGAATVLLPS 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 337 DpKLLVDDVQALAPR----SFATVPrVIDKI---HKAVmKQVQDKPLKKMILNAAIAYKlyhykmtgkatrktwVD-KYV 408
Cdd:PRK07470 239 E-RFDPAEVWALVERhrvtNLFTVP-TILKMlveHPAV-DRYDHSSLRYVIYAGAPMYR---------------ADqKRA 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 409 LHKiqmlLGPNIRQLI-LGAAKSDVSamrfargafgveVLEGYGQTETSGPttlqlvgDTRIGCVGPPMACAMIKLIDvp 487
Cdd:PRK07470 301 LAK----LGKVLVQYFgLGEVTGNIT------------VLPPALHDAEDGP-------DARIGTCGFERTGMEVQIQD-- 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 488 ELGYSVDKN-GGEVLVKGHNVTSGYYKNPEATASSFtEDGYMKTGDIGRFTAEGSLQIIDRRKNVFkMPQGKFVAPDLTE 566
Cdd:PRK07470 356 DEGRELPPGeTGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPREIE 433
|
330 340 350
....*....|....*....|....*....|..
gi 17541856 567 slytsssfvQQIYVHGDMEKpwlVAIV-VPDP 597
Cdd:PRK07470 434 ---------EKLLTHPAVSE---VAVLgVPDP 453
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
258-551 |
5.23e-12 |
|
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: 68.63 E-value: 5.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 258 PTPETLATISFTSGTTGRPKGVMLTHlN--MCSATMSCEEfeneAGV--QDAYLSYLPLAHIYERLC--LLSNFMIGSRI 331
Cdd:COG1021 181 PDPDDVAFFQLSGGTTGLPKLIPRTH-DdyLYSVRASAEI----CGLdaDTVYLAALPAAHNFPLSSpgVLGVLYAGGTV 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 332 GFSRgDPKLlvDDVQALAPRSFAT----VPrvidkihkavmkqvqdkPLKKMILNAAIAyklyhykmtgkatrktwvDKY 407
Cdd:COG1021 256 VLAP-DPSP--DTAFPLIERERVTvtalVP-----------------PLALLWLDAAER------------------SRY 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 408 VLhkiqmllgPNIRQLILGAAKSDVSAMRFARGAFGVEVLEGYGQTEtsGpttlqLV--------GDTRIGCVGPPMACA 479
Cdd:COG1021 298 DL--------SSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE--G-----LVnytrlddpEEVILTTQGRPISPD 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 480 -MIKLID-----VPElgysvdknG--GEVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNV 551
Cdd:COG1021 363 dEVRIVDedgnpVPP--------GevGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQ 434
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
269-608 |
5.25e-12 |
|
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: 68.51 E-value: 5.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 269 TSGTTGRPKGVMLTH----LNMCSATMSCEefeneAGVQDAYLSYLPLAHIYERLC--LLSNFMIGSRIGFSR-GDPkll 341
Cdd:cd05920 147 SGGTTGTPKLIPRTHndyaYNVRASAEVCG-----LDQDTVYLAVLPAAHNFPLACpgVLGTLLAGGRVVLAPdPSP--- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 342 vDDVQALAPRSFATVPRVIdkihkavmkqvqdKPLKKMILNAAIAYKLyhykmtgkatrktwvDKYVLHKIQmllgpnir 421
Cdd:cd05920 219 -DAAFPLIEREGVTVTALV-------------PALVSLWLDAAASRRA---------------DLSSLRLLQ-------- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 422 qliLGAAKSDVSAMRFARGAFGVEVLEGYGQTEtsGP---TTLQLVGDTRIGCVGPPMaCAMIKLIDVPELGYSV-DKNG 497
Cdd:cd05920 262 ---VGGARLSPALARRVPPVLGCTLQQVFGMAE--GLlnyTRLDDPDEVIIHTQGRPM-SPDDEIRVVDEEGNPVpPGEE 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 498 GEVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMPQGKFVAPDLTESLYTSSSfVQQ 577
Cdd:cd05920 336 GELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPA-VHD 414
|
330 340 350
....*....|....*....|....*....|....*
gi 17541856 578 IYVHGdMEKPWL----VAIVVPDPEYLASYALTKH 608
Cdd:cd05920 415 AAVVA-MPDELLgersCAFVVLRDPPPSAAQLRRF 448
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
254-552 |
1.43e-11 |
|
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: 67.65 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 254 PHVPPTPETLATISFTSGTTGRPKGVMLTHLNM---CSATMSCeeFENEAGvqDAYLSYLPLAH----IyerLCLLSNFM 326
Cdd:cd05931 142 PPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLlanVRQIRRA--YGLDPG--DVVVSWLPLYHdmglI---GGLLTPLY 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 327 IGSRIGFsrgdpkllvddvqaLAPRSFATVP----RVIDKiHKAVMkqvqdkplkkmilNAA--IAYKLYHYKMTGKATR 400
Cdd:cd05931 215 SGGPSVL--------------MSPAAFLRRPlrwlRLISR-YRATI-------------SAApnFAYDLCVRRVRDEDLE 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 401 KtwVDkyvlhkiqmlLGpNIRQLILGAAKSDVSAMR-----FARGAFGVEVLE-GYGQTET----------SGPTTLQLV 464
Cdd:cd05931 267 G--LD----------LS-SWRVALNGAEPVRPATLRrfaeaFAPFGFRPEAFRpSYGLAEAtlfvsggppgTGPVVLRVD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 465 GD----------------TRIGCVGPPmACAMIKLIDVPELGYSVDKNG-GEVLVKGHNVTSGYYKNPEATASSF----- 522
Cdd:cd05931 334 RDalagravavaaddpaaRELVSCGRP-LPDQEVRIVDPETGRELPDGEvGEIWVRGPSVASGYWGRPEATAETFgalaa 412
|
330 340 350
....*....|....*....|....*....|.
gi 17541856 523 -TEDGYMKTGDIGrFTAEGSLQIIDRRKNVF 552
Cdd:cd05931 413 tDEGGWLRTGDLG-FLHDGELYITGRLKDLI 442
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
259-554 |
1.47e-11 |
|
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: 67.27 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 259 TPETLATISFTSGTTGRPKGVMLTHlnmcsatmsceefeneagvqDAYLSYLplAHIyerlclLSNFMIGSRigfsrgdp 338
Cdd:cd05945 95 DGDDNAYIIFTSGSTGRPKGVQISH--------------------DNLVSFT--NWM------LSDFPLGPG-------- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 339 kllvDDVQALAPRSF--------------ATVprvidkihKAVMKQVQDKPLKkmiLNAAIAyklyHYKMTgkatrkTWV 404
Cdd:cd05945 139 ----DVFLNQAPFSFdlsvmdlypalasgATL--------VPVPRDATADPKQ---LFRFLA----EHGIT------VWV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 405 DkyVLHKIQMLLG---------PNIRQ-------LILGAAKSDVSAMRFARgafgveVLEGYGQTETSGPTTL------Q 462
Cdd:cd05945 194 S--TPSFAAMCLLsptftpeslPSLRHflfcgevLPHKTARALQQRFPDAR------IYNTYGPTEATVAVTYievtpeV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 463 LVGDTRIGcVGPPMACAMIKLIDvpELGYSVDKNG-GEVLVKGHNVTSGYYKNPEATASSF-TEDGY--MKTGDIGRFTA 538
Cdd:cd05945 266 LDGYDRLP-IGYAKPGAKLVILD--EDGRPVPPGEkGELVISGPSVSKGYLNNPEKTAAAFfPDEGQraYRTGDLVRLEA 342
|
330
....*....|....*.
gi 17541856 539 EGSLQIIDRRKNVFKM 554
Cdd:cd05945 343 DGLLFYRGRLDFQVKL 358
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
246-549 |
1.84e-11 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 67.68 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 246 MGKKQKHRPHVPPT---PETLATISFTSGTTGRPKGVMLTHLNM---CSATMSCEEFeneaGVQDAYLSYLPLAHIYerl 319
Cdd:PRK06814 775 KGLLAGRFPLVYFCnrdPDDPAVILFTSGSEGTPKGVVLSHRNLlanRAQVAARIDF----SPEDKVFNALPVFHSF--- 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 320 cllsNFMIGSRIGFSRGDPKLLVDdvqalAPRSFATVPRVIDKIHKAVMKQVqDKPLKKMIlNAAIAYKLY--HYKMTG- 396
Cdd:PRK06814 848 ----GLTGGLVLPLLSGVKVFLYP-----SPLHYRIIPELIYDTNATILFGT-DTFLNGYA-RYAHPYDFRslRYVFAGa 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 397 ----KATRKTWVDKyvlhkiqmllgpnirqlilgaaksdvsamrfargaFGVEVLEGYGQTETSGPTTLQLVGDTRIGCV 472
Cdd:PRK06814 917 ekvkEETRQTWMEK-----------------------------------FGIRILEGYGVTETAPVIALNTPMHNKAGTV 961
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17541856 473 GPPMACAMIKLIDVPelgySVDKnGGEVLVKGHNVTSGYYK--NPEATASsfTEDGYMKTGDIGRFTAEGSLQIIDRRK 549
Cdd:PRK06814 962 GRLLPGIEYRLEPVP----GIDE-GGRLFVRGPNVMLGYLRaeNPGVLEP--PADGWYDTGDIVTIDEEGFITIKGRAK 1033
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
260-542 |
2.71e-11 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 66.76 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 260 PETLATISFTSGTTGRPKGVMLTHLNMCSATMSCEEFENEAgVQDAYLSYLPLAHIYE-RLCLLSNFMIGSRIGFSRG-- 336
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPK-EDDVMMSFLPPFHAYGfNSCTLFPLLSGVPVVFAYNpl 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 337 DPKLLVDDVQALAPRSFATVPRVIDKIHKAVMKQVQDKPLKKMILNAAIAYKLYHYKMTGKatrktwvdkyvlhkiqmlL 416
Cdd:PRK06334 261 YPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALK------------------T 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 417 GPNIrqlilgaaksdvsAMRfargafgvevlEGYGQTETSGPTTLQLVGDTRI-GCVGPPMAcAMIKLIdVPELGYSVDK 495
Cdd:PRK06334 323 FPHI-------------QLR-----------QGYGTTECSPVITINTVNSPKHeSCVGMPIR-GMDVLI-VSEETKVPVS 376
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 17541856 496 NG--GEVLVKGHNVTSGYYKNPEatASSFTE---DGYMKTGDIGRFTAEGSL 542
Cdd:PRK06334 377 SGetGLVLTRGTSLFSGYLGEDF--GQGFVElggETWYVTGDLGYVDRHGEL 426
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
124-607 |
3.66e-11 |
|
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: 65.98 E-value: 3.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 124 SDHASQAIRKLGIEIGEesKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDDMHYITNLCEISLMFVDAEIKTKQL 203
Cdd:cd05970 57 SDKTANFFKAMGIGKGD--TVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDNIPEE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 204 IRD-KSYLSSLKYIVQfneCSDDIKEMarendfrlW-SFNEFVEMGKKQKHRPHVPPTP--ETLATISFTSGTTGRPKGV 279
Cdd:cd05970 135 IEKaAPECPSKPKLVW---VGDPVPEG--------WiDFRKLIKNASPDFERPTANSYPcgEDILLVYFSSGTTGMPKMV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 280 M------LTHLNMCSATMSCEEFENEAGVQDAYLSYLPLAHIYerlcllSNFMIGSRI---GFSRGDPKLLVDDVQALAP 350
Cdd:cd05970 204 EhdftypLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWGKIY------GQWIAGAAVfvyDYDKFDPKALLEKLSKYGV 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 351 RSFATVPRVidkihkavmkqvqdkplkkmilnaaiayklYHYKMTGKATRktwvdkYVLHKIQMLLgpnirqlILGAAKS 430
Cdd:cd05970 278 TTFCAPPTI------------------------------YRFLIREDLSR------YDLSSLRYCT-------TAGEALN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 431 DVSAMRFaRGAFGVEVLEGYGQTEtsgpTTLQLVG----DTRIGCVGPPMACAMIKLIDvPElGYSVDK-NGGEVLV--- 502
Cdd:cd05970 315 PEVFNTF-KEKTGIKLMEGFGQTE----TTLTIATfpwmEPKPGSMGKPAPGYEIDLID-RE-GRSCEAgEEGEIVIrts 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 503 KGHNVT--SGYYKNPEATASSFtEDGYMKTGDIGRFTAEGSLQIIDRRKNVFKmPQGKFVAPDLTESLYTSSSFVQQIYV 580
Cdd:cd05970 388 KGKPVGlfGGYYKDAEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVESALIQHPAVLECAV 465
|
490 500 510
....*....|....*....|....*....|
gi 17541856 581 HG--DMEKPWLV-AIVVPDPEYLASYALTK 607
Cdd:cd05970 466 TGvpDPIRGQVVkATIVLAKGYEPSEELKK 495
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
259-597 |
7.21e-11 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 64.97 E-value: 7.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 259 TPETLATISFTSGTTGRPKGVMLTHLNMCSATMSCEEFENeAGVQDAYLSYLPL---AHIYErlcLLSNFMIGSRigfsr 335
Cdd:cd17652 91 TPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFD-VGPGSRVLQFASPsfdASVWE---LLMALLAGAT----- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 336 gdpklLVddvqaLAPRSfATVPrvidkihkavmkqvqDKPLKKMIlnaaIAYKLYHYKMTGKATRKTWVDKYvlhkiqml 415
Cdd:cd17652 162 -----LV-----LAPAE-ELLP---------------GEPLADLL----REHRITHVTLPPAALAALPPDDL-------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 416 lgPNIRQLILGAakSDVSAMRFARGAFGVEVLEGYGQTETS-GPTTLQLVGDTRIGCVGPPMACAMIKLID-----VPel 489
Cdd:cd17652 204 --PDLRTLVVAG--EACPAELVDRWAPGRRMINAYGPTETTvCATMAGPLPGGGVPPIGRPVPGTRVYVLDarlrpVP-- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 490 gYSVDkngGEVLVKGHNVTSGYYKNPEATASSFTEDGY-------MKTGDIGRFTAEGSLQIIDRRKNVFKMpQGKFVAP 562
Cdd:cd17652 278 -PGVP---GELYIAGAGLARGYLNRPGLTAERFVADPFgapgsrmYRTGDLARWRADGQLEFLGRADDQVKI-RGFRIEL 352
|
330 340 350
....*....|....*....|....*....|....*...
gi 17541856 563 DLTESLYTSSSFVQQ--IYVHGD-MEKPWLVAIVVPDP 597
Cdd:cd17652 353 GEVEAALTEHPGVAEavVVVRDDrPGDKRLVAYVVPAP 390
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
260-547 |
9.30e-11 |
|
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: 64.41 E-value: 9.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 260 PETLATISFTSGTTGRPKGVMLTHLNMCSATmsceefeneAGVQDAYlsylPLAHIYERLCLLSNFMIGSRIG-FSRGdp 338
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAA---------HAWRREY----ELDSFPVRLLQMASFSFDVFAGdFARS-- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 339 kllvddvqALAPRSFATVPRvidkihKAVMKQVQdkpLKKMILNAAIAYklyhykMTGKATRKTWVDKYVLHKIQMLlgP 418
Cdd:cd17650 157 --------LLNGGTLVICPD------EVKLDPAA---LYDLILKSRITL------MESTPALIRPVMAYVYRNGLDL--S 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 419 NIRQLILGaakSDVSAMR-----FARGAFGVEVLEGYGQTETSGPTTLQLVGDTRIGC-----VGPPMACAMIKLID--- 485
Cdd:cd17650 212 AMRLLIVG---SDGCKAQdfktlAARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGDsanvpIGRPLPNTAMYVLDerl 288
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 486 --VPeLGYSvdkngGEVLVKGHNVTSGYYKNPEATASSFTEDGYM------KTGDIGRFTAEGSLQIIDR 547
Cdd:cd17650 289 qpQP-VGVA-----GELYIGGAGVARGYLNRPELTAERFVENPFApgermyRTGDLARWRADGNVELLGR 352
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
252-602 |
9.76e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 65.75 E-value: 9.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 252 HRPHVPPTPETLATISFTSGTTGRPKGVMLTHLNMCSATMSCEEFEnEAGVQDAYLSYLPLAHIYERLCLLSNFMIGSRI 331
Cdd:PRK12316 4685 HDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERY-ELTPDDRVLQFMSFSFDGSHEGLYHPLINGASV 4763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 332 gfsrgdpkLLVDDVQALAPRSFATVPRviDKIHKAVMKQVQDKPLKKMILNAAIAYKLYHYKMTGKAtrktwvdkyvlhk 411
Cdd:PRK12316 4764 --------VIRDDSLWDPERLYAEIHE--HRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEA------------- 4820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 412 iqmlLGPNIRQLILGAAKSdvsamrfargafgVEVLEGYGQTETS-GPTTLQLVGDTRIGC----VGPPMACAMIKLIDV 486
Cdd:PRK12316 4821 ----VAQASYDLAWRALKP-------------VYLFNGYGPTETTvTVLLWKARDGDACGAaympIGTPLGNRSGYVLDG 4883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 487 pELGYSVDKNGGEVLVKGHNVTSGYYKNPEATASSFTEDGY-------MKTGDIGRFTAEGSLQIIDR-----RKNVFKM 554
Cdd:PRK12316 4884 -QLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapggrlYRTGDLARYRADGVIDYLGRvdhqvKIRGFRI 4962
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 17541856 555 PQGKFVA-----PDLTESLytsssFVQQIYVHGDMekpwLVAIVVPDPEYLAS 602
Cdd:PRK12316 4963 ELGEIEArlrehPAVREAV-----VIAQEGAVGKQ----LVGYVVPQDPALAD 5006
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
115-547 |
1.24e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 65.18 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 115 ISYDQAFETSDHASQAIRKLGIeiGEESKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDDMHYitnlceislMFV 194
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGV--GPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAY---------MLD 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 195 DAEIKTkqLIRDKSYLSSLkyivqfnECSDDIKEMARENDFRLWSfnefvemgKKQKHRPHVPPTPETLATISFTSGTTG 274
Cdd:PRK12467 607 DSGVRL--LLTQSHLLAQL-------PVPAGLRSLCLDEPADLLC--------GYSGHNPEVALDPDNLAYVIYTSGSTG 669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 275 RPKGVMLTHLNMCS-ATMSCEEFENEAgvQDAYLSYLPLAHIYERLCLLSNFMIGSRIgfsrgdpkLLVDDVQALAPRSF 353
Cdd:PRK12467 670 QPKGVAISHGALANyVCVIAERLQLAA--DDSMLMVSTFAFDLGVTELFGALASGATL--------HLLPPDCARDAEAF 739
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 354 AtvpRVIDKIHKAVMKQVQDkplkkmilnaaiayklyHYKMTGKATRKTWVDKYvlhkiqmllgpniRQLILGAAKSDVS 433
Cdd:PRK12467 740 A---ALMADQGVTVLKIVPS-----------------HLQALLQASRVALPRPQ-------------RALVCGGEALQVD 786
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 434 AM-RFARGAFGVEVLEGYGQTETS-GPTTLQLVGDTRIGC---VGPPMACAMIKLIDvPELGYSVDKNGGEVLVKGHNVT 508
Cdd:PRK12467 787 LLaRVRALGPGARLINHYGPTETTvGVSTYELSDEERDFGnvpIGQPLANLGLYILD-HYLNPVPVGVVGELYIGGAGLA 865
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 17541856 509 SGYYKNPEATASSFTEDGY-------MKTGDIGRFTAEGSLQIIDR 547
Cdd:PRK12467 866 RGYHRRPALTAERFVPDPFgadggrlYRTGDLARYRADGVIEYLGR 911
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
261-605 |
1.38e-10 |
|
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: 64.02 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 261 ETLATISFTSGTTGRPKGVMLTHLNMcsaTMSCEEFENEA-GVQ--DAYLSylpLAHIYERLCLLSNFMIGSRIGFSrgd 337
Cdd:cd05919 91 DDIAYLLYSSGTTGPPKGVMHAHRDP---LLFADAMAREAlGLTpgDRVFS---SAKMFFGYGLGNSLWFPLAVGAS--- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 338 pkLLVDDVQALAPRSFATVPRVidkihkavmkqvqdKPlkKMILNAAIAYKlyhykmtgkatrktwvdkyvlhkiQMLLG 417
Cdd:cd05919 162 --AVLNPGWPTAERVLATLARF--------------RP--TVLYGVPTFYA------------------------NLLDS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 418 PNIRQLILGAAKSDVSA--------MRFARGAFGVEVLEGYGQTETSGPTTLQLVGDTRIGCVGPPMACAMIKLIDvpEL 489
Cdd:cd05919 200 CAGSPDALRSLRLCVSAgealprglGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD--EE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 490 GYSV-DKNGGEVLVKGHNVTSGYYKNPEATASSFtEDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMpQGKFVAPDLTESL 568
Cdd:cd05919 278 GHTIpPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGRADDMLKV-GGQWVSPVEVESL 355
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 17541856 569 YTSSSFVQQIYVHGDMEKPWLV---AIVVPDPEYLASYAL 605
Cdd:cd05919 356 IIQHPAVAEAAVVAVPESTGLSrltAFVVLKSPAAPQESL 395
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
253-598 |
1.87e-10 |
|
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: 63.90 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 253 RPHVPPTPETLATISFTSGTTGRPKGVMLTH---LNMCSAtmsceefeneagvQDAYLSYLPLAHIyerlcllSNFM-IG 328
Cdd:cd17651 128 EPDPALDADDLAYVIYTSGSTGRPKGVVMPHrslANLVAW-------------QARASSLGPGART-------LQFAgLG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 329 SRIGFSRGDPKLLVDDVQALAPRSFATVPRvidkihkAVMKQVQDKPLKKMIL-NAAIAYKLYHYKMTGKAtrktwvdky 407
Cdd:cd17651 188 FDVSVQEIFSTLCAGATLVLPPEEVRTDPP-------ALAAWLDEQRISRVFLpTVALRALAEHGRPLGVR--------- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 408 vlhkiqmllGPNIRQLILGAAKSDVSAM--RFARGAFGVEVLEGYGQTETSGPTTLQLVGDT----RIGCVGPPMACAMI 481
Cdd:cd17651 252 ---------LAALRYLLTGGEQLVLTEDlrEFCAGLPGLRLHNHYGPTETHVVTALSLPGDPaawpAPPPIGRPIDNTRV 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 482 KLID---------VPelgysvdkngGEVLVKGHNVTSGYYKNPEATASSFTEDGYM------KTGDIGRFTAEGSLQIID 546
Cdd:cd17651 323 YVLDaalrpvppgVP----------GELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLG 392
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 17541856 547 RRKNVFKMpQGKFVAPDLTESLYTSSSFVQQIYV----HGDMEKpWLVAIVVPDPE 598
Cdd:cd17651 393 RADDQVKI-RGFRIELGEIEAALARHPGVREAVVlareDRPGEK-RLVAYVVGDPE 446
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
254-533 |
3.27e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 63.16 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 254 PHVPPTPETLATISFTSGTTGRPKGVMLTHLNMCSA-TMSCEEFEneAGVQD-AYLSyLPLAHiyerlcllSNFMIGsri 331
Cdd:PRK07867 145 PFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAgVMLAQRFG--LGPDDvCYVS-MPLFH--------SNAVMA--- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 332 GFSrgdPKLLVDDVQALaPRSFaTVPRVIDKIHKavmkqvqdkplkkmilnaaiayklYHykmtgkATRKTWVDK---YV 408
Cdd:PRK07867 211 GWA---VALAAGASIAL-RRKF-SASGFLPDVRR------------------------YG------ATYANYVGKplsYV 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 409 LHKIQMllgPNIRQ----LILGAAKSDVSAMRFARgAFGVEVLEGYGQTEtsGPTTLQLVGDTRIGCVGPPMAcaMIKLI 484
Cdd:PRK07867 256 LATPER---PDDADnplrIVYGNEGAPGDIARFAR-RFGCVVVDGFGSTE--GGVAITRTPDTPPGALGPLPP--GVAIV 327
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17541856 485 DvPELGYSV-----DKNG--------GE-VLVKGHNVTSGYYKNPEATASSFtEDGYMKTGDI 533
Cdd:PRK07867 328 D-PDTGTECppaedADGRllnadeaiGElVNTAGPGGFEGYYNDPEADAERM-RGGVYWSGDL 388
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
256-554 |
8.09e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 61.94 E-value: 8.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 256 VPPTPETLATISFTSGTTGRPKGVMLTHLN-------MCSATmsceEFENEAGVQdayLSYLPLAHiyerlcllSNFMIG 328
Cdd:PRK07768 147 VETGEDDLALMQLTSGSTGSPKAVQITHGNlyanaeaMFVAA----EFDVETDVM---VSWLPLFH--------DMGMVG 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 329 S-RIGFSRGDPKLLVDDVQALapRSFATVPRVIDKiHKAVMkqvqdkplkkmilNAA--IAYKLYHYKMTGKATRKTwvd 405
Cdd:PRK07768 212 FlTVPMYFGAELVKVTPMDFL--RDPLLWAELISK-YRGTM-------------TAApnFAYALLARRLRRQAKPGA--- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 406 kYVLHKIQMLLGpnirqlilGAAKSDVSAM-RFAR-GA-FGVE---VLEGYGQTETS-----GPTTLQLVGDT------- 467
Cdd:PRK07768 273 -FDLSSLRFALN--------GAEPIDPADVeDLLDaGArFGLRpeaILPAYGMAEATlavsfSPCGAGLVVDEvdadlla 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 468 --------------RIGCVGPPMACAMIKLIDvpELGYSVDKNG-GEVLVKGHNVTSGYyknpeATASSFT----EDGYM 528
Cdd:PRK07768 344 alrravpatkgntrRLATLGPPLPGLEVRVVD--EDGQVLPPRGvGVIELRGESVTPGY-----LTMDGFIpaqdADGWL 416
|
330 340
....*....|....*....|....*.
gi 17541856 529 KTGDIGRFTAEGSLQIIDRRKNVFKM 554
Cdd:PRK07768 417 DTGDLGYLTEEGEVVVCGRVKDVIIM 442
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
498-597 |
3.76e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 59.76 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 498 GEVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMpQGKFVAPDLTESLYTSSSFVQQ 577
Cdd:PRK06164 378 GEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRL-GGFLVNPAEIEHALEALPGVAA 456
|
90 100
....*....|....*....|..
gi 17541856 578 IYVHG-DME-KPWLVAIVVPDP 597
Cdd:PRK06164 457 AQVVGaTRDgKTVPVAFVIPTD 478
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
115-547 |
1.02e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 59.20 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 115 ISYDQAFETSDHASQAIRKLGIeiGEESKIGIYSNNRPEWILSEMAIHNFSNVSVPLydtitndDMHYITNlcEISLMFV 194
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGV--GPEVRVAIAAERSFELVVALLAVLKAGGAYVPL-------DPNYPAE--RLAYMLE 2097
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 195 DAEIKTkqLIRDKSYLSSLKyivqfneCSDDIKEMARENDFRLWSFNEfvemgkkqkHRPHVPPTPETLATISFTSGTTG 274
Cdd:PRK12316 2098 DSGAAL--LLTQRHLLERLP-------LPAGVARLPLDRDAEWADYPD---------TAPAVQLAGENLAYVIYTSGSTG 2159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 275 RPKGVMLTHLNMCSATMSCEEFeNEAGVQDAYLSYLPLAHIYERLCLLSNFMIGSRIgfsrgdpkLLVDDVQALAPRSFA 354
Cdd:PRK12316 2160 LPKGVAVSHGALVAHCQAAGER-YELSPADCELQFMSFSFDGAHEQWFHPLLNGARV--------LIRDDELWDPEQLYD 2230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 355 TVPR--VIDKIHKAVMKQVQDKplkkmilnaaiayklyHYKMTGKAtrktwvdkyvlhkiqmllgPNIRQLILGA-AKSD 431
Cdd:PRK12316 2231 EMERhgVTILDFPPVYLQQLAE----------------HAERDGRP-------------------PAVRVYCFGGeAVPA 2275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 432 VSAMRFARGAFGVEVLEGYGQTETS-GPTTLQLVGDTRIGCVGPPMACAMIKLidvpeLGYSVDKN--------GGEVLV 502
Cdd:PRK12316 2276 ASLRLAWEALRPVYLFNGYGPTEAVvTPLLWKCRPQDPCGAAYVPIGRALGNR-----RAYILDADlnllapgmAGELYL 2350
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 17541856 503 KGHNVTSGYYKNPEATASSFTEDGY-------MKTGDIGRFTAEGSLQIIDR 547
Cdd:PRK12316 2351 GGEGLARGYLNRPGLTAERFVPDPFsasgerlYRTGDLARYRADGVVEYLGR 2402
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
260-551 |
1.10e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 59.03 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 260 PETLATISFTSGTTGRPKGVMLTHLNMCS-ATMSCEEFENEAGVQDAYLSYLPLAHiyerlcllSNFMIGSRIG--FSrG 336
Cdd:PRK05691 165 PDDIAFLQYTSGSTALPKGVQVSHGNLVAnEQLIRHGFGIDLNPDDVIVSWLPLYH--------DMGLIGGLLQpiFS-G 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 337 DPKLLvddvqaLAPRSFATVP-RVIDKIHKaVMKQVQDKPlkkmilnaAIAYKLYHYKMTGKATRKTWVDKYvlhKIQML 415
Cdd:PRK05691 236 VPCVL------MSPAYFLERPlRWLEAISE-YGGTISGGP--------DFAYRLCSERVSESALERLDLSRW---RVAYS 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 416 LGPNIRQLILGAAKSDVSAMRFARGAFgvevLEGYGQTETS----------GPTTLQLVGDT------RIGCVGPPMACA 479
Cdd:PRK05691 298 GSEPIRQDSLERFAEKFAACGFDPDSF----FASYGLAEATlfvsggrrgqGIPALELDAEAlarnraEPGTGSVLMSCG 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 480 M------IKLIDVPELGYSVDKNGGEVLVKGHNVTSGYYKNPEATASSFTE-DG--YMKTGDIGrFTAEGSLQIIDRRKN 550
Cdd:PRK05691 374 RsqpghaVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEhDGrtWLRTGDLG-FLRDGELFVTGRLKD 452
|
.
gi 17541856 551 V 551
Cdd:PRK05691 453 M 453
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
258-559 |
1.10e-08 |
|
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: 57.86 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 258 PTPETLATISFTSGTTGRPKGVMLTHlNMCSATMSC--EEFENEAGVQDayLSYLPLahiyerlcllsnfmigsrigFSR 335
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRH-GTFAAQIDAlrQLYGIRPGEVD--LATFPL--------------------FAL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 336 GDPKLlvdDVQALAPRSFATVPRVIDKihKAVMKQVQDKPLKKMILNAAIAYKLYHYKMTgkatrktwvdkyvlHKIQMl 415
Cdd:cd05910 139 FGPAL---GLTSVIPDMDPTRPARADP--QKLVGAIRQYGVSIVFGSPALLERVARYCAQ--------------HGITL- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 416 lgPNIRQLILGAAKSDVSAMRFARGAF--GVEVLEGYGQTE--------------TSGPTTLQLVGDtrigCVGPPMACA 479
Cdd:cd05910 199 --PSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEalpvssigsrellaTTTAATSGGAGT----CVGRPIPGV 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 480 MIKLI-----DVPELGYSVDKNG---GEVLVKGHNVTSGYYKNPEATASSFTEDG----YMKTGDIGRFTAEGSLQIIDR 547
Cdd:cd05910 273 RVRIIeiddePIAEWDDTLELPRgeiGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGR 352
|
330
....*....|..
gi 17541856 548 RKNVFKMPQGKF 559
Cdd:cd05910 353 KAHRVITTGGTL 364
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
257-551 |
1.66e-08 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 57.55 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 257 PPTPE--TLAtISFTSGTTGRPKGVMLTHLNMCSATMSCEEF--ENEAGVqdaYLSYLPLAHIyERLCllsnfmigsrig 332
Cdd:PLN02479 190 PPADEwqSIA-LGYTSGTTASPKGVVLHHRGAYLMALSNALIwgMNEGAV---YLWTLPMFHC-NGWC------------ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 333 FSRGdpkllvddVQALAPRSFAtvprvidkihkavMKQVQDKPLKKMILNaaiaYKLYHYkMTGKATRKTWVDKYVLHKI 412
Cdd:PLN02479 253 FTWT--------LAALCGTNIC-------------LRQVTAKAIYSAIAN----YGVTHF-CAAPVVLNTIVNAPKSETI 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 413 QMLlgPNIRQLILGAAKSDVSAMrFARGAFGVEVLEGYGQTETSGPTT----------LQLVGDTRIGCVGPPMACAMIK 482
Cdd:PLN02479 307 LPL--PRVVHVMTAGAAPPPSVL-FAMSEKGFRVTHTYGLSETYGPSTvcawkpewdsLPPEEQARLNARQGVRYIGLEG 383
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17541856 483 LiDV--PELGYSVDKNG---GEVLVKGHNVTSGYYKNPEATASSFtEDGYMKTGDIGRFTAEGSLQIIDRRKNV 551
Cdd:PLN02479 384 L-DVvdTKTMKPVPADGktmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDI 455
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
260-553 |
2.63e-08 |
|
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: 56.67 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 260 PETLATISFTSGTTGRPKG------VMLTHLnmcsatmSCEEFENEAGVQDAYLSYLP-------------LAHIYERLC 320
Cdd:cd05971 87 SDDPALIIYTSGTTGPPKGalhahrVLLGHL-------PGVQFPFNLFPRDGDLYWTPadwawigglldvlLPSLYFGVP 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 321 LLSNFMigsrigfSRGDPKLLVDDVQALAPRSfATVPRVIDKIHKAVMKQVQDKPLkkmilnaaiayklyhykmtgkatr 400
Cdd:cd05971 160 VLAHRM-------TKFDPKAALDLMSRYGVTT-AFLPPTALKMMRQQGEQLKHAQV------------------------ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 401 ktwvdkyvlhkiqmllgpNIRQLILGAAKSDVSAMRFARGAFGVEVLEGYGQTETSgpttlQLVGDTRIgcVGPPMACAM 480
Cdd:cd05971 208 ------------------KLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECN-----LVIGNCSA--LFPIKPGSM 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 481 IKlidvPELGYSV---DKNG--------GEVLVKGHNVTS--GYYKNPEATASSFTEDgYMKTGDIGRFTAEGSLQIIDR 547
Cdd:cd05971 263 GK----PIPGHRVaivDDNGtplppgevGEIAVELPDPVAflGYWNNPSATEKKMAGD-WLLTGDLGRKDSDGYFWYVGR 337
|
....*.
gi 17541856 548 RKNVFK 553
Cdd:cd05971 338 DDDVIT 343
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
439-601 |
2.88e-08 |
|
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: 56.81 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 439 RGAFGVEVLEGYGQTETSGpttlqLVGDT-----RIGCVGPPMACAMIKLIDvpELGYSVDKngGEV-LVKGHN----VT 508
Cdd:cd05974 221 RRAWGLTIRDGYGQTETTA-----LVGNSpgqpvKAGSMGRPLPGYRVALLD--PDGAPATE--GEVaLDLGDTrpvgLM 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 509 SGYYKNPEATASSFtEDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMPQGKfVAPDLTESLYTSSSFVQQiyvhgdmekpw 588
Cdd:cd05974 292 KGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYR-ISPFELESVLIEHPAVAE----------- 358
|
170
....*....|....*
gi 17541856 589 lvAIVV--PDPEYLA 601
Cdd:cd05974 359 --AAVVpsPDPVRLS 371
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
254-548 |
3.44e-08 |
|
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: 56.51 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 254 PHVPPTPETLATISFTSGTTGRPKGVMLTH---LNMCSATmsceefeNEA---GVQDAYLSYLPLAH---IYERLCLLSn 324
Cdd:cd12114 119 PPVDVAPDDLAYVIFTSGSTGTPKGVMISHraaLNTILDI-------NRRfavGPDDRVLALSSLSFdlsVYDIFGALS- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 325 fmIGSRIGF----SRGDPKLLVDDVQALAPRSFATVPrvidkihkAVMKqvqdkplkkMILNAAIAYKlyhykMTGKATR 400
Cdd:cd12114 191 --AGATLVLpdeaRRRDPAHWAELIERHGVTLWNSVP--------ALLE---------MLLDVLEAAQ-----ALLPSLR 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 401 ktwvdkYVLHK---IQMLLGPNIRQLilgAAKSDVSAMrfargafgvevleGyGQTETSGPTTLQLVGDtrigcvgPPMA 477
Cdd:cd12114 247 ------LVLLSgdwIPLDLPARLRAL---APDARLISL-------------G-GATEASIWSIYHPIDE-------VPPD 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 478 CAMIKLiDVPELG---YSVDKNG--------GEVLVKGHNVTSGYYKNPEATASSFTEDG-----YmKTGDIGRFTAEGS 541
Cdd:cd12114 297 WRSIPY-GRPLANqryRVLDPRGrdcpdwvpGELWIGGRGVALGYLGDPELTAARFVTHPdgerlY-RTGDLGRYRPDGT 374
|
....*..
gi 17541856 542 LQIIDRR 548
Cdd:cd12114 375 LEFLGRR 381
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
115-547 |
3.97e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 56.43 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 115 ISYDQAFETSDHASQAIRKLGIEIGEesKIGIYSNNRPEWIlsEMAIHNFSNVSVPLydtitNDDMHYITNlcEISLMFV 194
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGPGD--HVGIYARNRIEYV--EAMLGAFKARAVPV-----NVNYRYVED--ELRYLLD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 195 DAEIKTkqLIRDKSY----------LSSLKYIVQFNECSDdikemareNDFRLW--SFNEFVEMGKKQkhRPHVPPTPET 262
Cdd:PRK07798 98 DSDAVA--LVYEREFaprvaevlprLPKLRTLVVVEDGSG--------NDLLPGavDYEDALAAGSPE--RDFGERSPDD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 263 LATIsFTSGTTGRPKGVMLTHLNMCSATMSCEEFENEAGVQDAY--------------LSYLPLAHIYERLCLLSNFMIG 328
Cdd:PRK07798 166 LYLL-YTGGTTGMPKGVMWRQEDIFRVLLGGRDFATGEPIEDEEelakraaagpgmrrFPAPPLMHGAGQWAAFAALFSG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 329 SRIGFSRgDPKLLVDDVQALAPRsfatvprvidkiHKA-VMKQVQD---KPLKKMILN---------AAIAyklyhykmT 395
Cdd:PRK07798 245 QTVVLLP-DVRFDADEVWRTIER------------EKVnVITIVGDamaRPLLDALEArgpydlsslFAIA--------S 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 396 GKAtrktwvdkyvlhkiqmLLGPNIRQLILGAAKsdvsamrfargafGVEVLEGYGQTET-SGPTTLQLVGDTRIGCVGP 474
Cdd:PRK07798 304 GGA----------------LFSPSVKEALLELLP-------------NVVLTDSIGSSETgFGGSGTVAKGAVHTGGPRF 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17541856 475 PMAcAMIKLIDvpELGYSVDKNGGEV--LVKGHNVTSGYYKNPEATASSFTE-DG--YMKTGDIGRFTAEGSLQIIDR 547
Cdd:PRK07798 355 TIG-PRTVVLD--EDGNPVEPGSGEIgwIARRGHIPLGYYKDPEKTAETFPTiDGvrYAIPGDRARVEADGTITLLGR 429
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
260-598 |
7.88e-08 |
|
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: 55.52 E-value: 7.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 260 PETLATISFTSGTTGRPKGVMLTHLNMCSATMsceefeneaGVQDAYlsylplaHIYERLCLLSNFMIGSRIGFSRGDPK 339
Cdd:cd17644 105 PENLAYVIYTSGSTGKPKGVMIEHQSLVNLSH---------GLIKEY-------GITSSDRVLQFASIAFDVAAEEIYVT 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 340 LLVDDVQALAPRS-FATVPRVIDKIhkavmkqvQDKPLKkmILNAAIAYklYHykmtgkatrkTWVDKYVLHKIQmllGP 418
Cdd:cd17644 169 LLSGATLVLRPEEmRSSLEDFVQYI--------QQWQLT--VLSLPPAY--WH----------LLVLELLLSTID---LP 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 419 N-IRQLILGAAKSDVSAMRFARGAFG--VEVLEGYGQTETSGPTTLQLVGD------TRIgCVGPPMACAMIKLID---- 485
Cdd:cd17644 224 SsLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQlterniTSV-PIGRPIANTQVYILDenlq 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 486 -VPeLGYSvdkngGEVLVKGHNVTSGYYKNPEATASSFTEDGYM--------KTGDIGRFTAEGSLQIIDRRKNVFKMpQ 556
Cdd:cd17644 303 pVP-VGVP-----GELHIGGVGLARGYLNRPELTAEKFISHPFNsseserlyKTGDLARYLPDGNIEYLGRIDNQVKI-R 375
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 17541856 557 GKFVAPDLTESLYTSSSFVQQIYVHGDMEKP---WLVAIVVPDPE 598
Cdd:cd17644 376 GFRIELGEIEAVLSQHNDVKTAVVIVREDQPgnkRLVAYIVPHYE 420
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
250-547 |
1.07e-07 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 55.01 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 250 QKHRPHvPPTPeTLAT----ISFTSGTTGRPKGVMLT---HLNMCSATMSceefeNEAGVQD----------------AY 306
Cdd:cd05967 217 AKAEPV-DCVP-VAATdplyILYTSGTTGKPKGVVRDnggHAVALNWSMR-----NIYGIKPgdvwwaasdvgwvvghSY 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 307 LSYLPLAH-----IYErlcllsnfmigsrigfsrGDPKLLVDdvqalaPRSFAtvpRVIDKiHKAvmkqvqdkplkKMIL 381
Cdd:cd05967 290 IVYGPLLHgattvLYE------------------GKPVGTPD------PGAFW---RVIEK-YQV-----------NALF 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 382 NAAIAYKlyhykmtgkATRK-----TWVDKYVLHkiqmllgpNIRQLILGAAKSDVSAMRFARGAFGVEVLEGYGQTETS 456
Cdd:cd05967 331 TAPTAIR---------AIRKedpdgKYIKKYDLS--------SLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETG 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 457 GPTTLQLVG----DTRIGCVGPPMACAMIKLIDvpELGYSVDKNG-GEVLVKGH---NVTSGYYKNPEATASSFTED--G 526
Cdd:cd05967 394 WPITANPVGleplPIKAGSPGKPVPGYQVQVLD--EDGEPVGPNElGNIVIKLPlppGCLLTLWKNDERFKKLYLSKfpG 471
|
330 340
....*....|....*....|.
gi 17541856 527 YMKTGDIGRFTAEGSLQIIDR 547
Cdd:cd05967 472 YYDTGDAGYKDEDGYLFIMGR 492
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
253-548 |
1.58e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 54.52 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 253 RPHVPPTPETL-ATISFTSGTTGRPKGVM--LTHL------NMCSATMSCEEFENEAGVqdaYLSYLPLAHIYE-RLCLL 322
Cdd:PRK08276 131 QPDTPIADETAgADMLYSSGTTGRPKGIKrpLPGLdpdeapGMMLALLGFGMYGGPDSV---YLSPAPLYHTAPlRFGMS 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 323 SNFMIGSRIGFSRGDPKllvddvQALaprsfatvpRVIDKihkavmkqvqdkplkkmilnaaiayklyHykmtgKATRKT 402
Cdd:PRK08276 208 ALALGGTVVVMEKFDAE------EAL---------ALIER----------------------------Y-----RVTHSQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 403 WVDkyvLHKIQML-LGPNIRqlilgaAKSDVSAMRFARGA---------------FGVEVLEGYGQTETSGPTTLQ---- 462
Cdd:PRK08276 240 LVP---TMFVRMLkLPEEVR------ARYDVSSLRVAIHAaapcpvevkramidwWGPIIHEYYASSEGGGVTVITsedw 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 463 LvgdTRIGCVGPPMAcAMIKLidvpelgysVDKNG--------GEVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIG 534
Cdd:PRK08276 311 L---AHPGSVGKAVL-GEVRI---------LDEDGnelppgeiGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVG 377
|
330
....*....|....
gi 17541856 535 RFTAEGSLQIIDRR 548
Cdd:PRK08276 378 YLDEDGYLYLTDRK 391
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
259-598 |
2.27e-07 |
|
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: 53.66 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 259 TPETLATISFTSGTTGRPKGVMLTHLNMcsatmsceefeneagvqdaYLSYLPLAHIYErlcllsnfMIGSRIGFSRGDP 338
Cdd:cd05969 87 DPEDPTLLHYTSGTTGTPKGVLHVHDAM-------------------IFYYFTGKYVLD--------LHPDDIYWCTADP 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 339 KLLVDDVQALAPRSFATVPRVIDKihkavmkqvqdkplkkmilnaaiayklyhykmtGKATRKTWVDKYVLHKIQ-MLLG 417
Cdd:cd05969 140 GWVTGTVYGIWAPWLNGVTNVVYE---------------------------------GRFDAESWYGIIERVKVTvWYTA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 418 P-NIRQLI-LG---AAKSDVSAMRFARG---------------AFGVEVLEGYGQTETSGPTTLQLVG-DTRIGCVGPPM 476
Cdd:cd05969 187 PtAIRMLMkEGdelARKYDLSSLRFIHSvgeplnpeairwgmeVFGVPIHDTWWQTETGSIMIANYPCmPIKPGSMGKPL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 477 ACAMIKLIDVPELGYSVDKNGGEVLVKGH-NVTSGYYKNPEATASSFTeDGYMKTGDIGRFTAEGSLQIIDRRKNVFKMp 555
Cdd:cd05969 267 PGVKAAVVDENGNELPPGTKGILALKPGWpSMFRGIWNDEERYKNSFI-DGWYLTGDLAYRDEDGYFWFVGRADDIIKT- 344
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 17541856 556 QGKFVAPDLTESLYTSSSFVQQIYVHGdmekpwlvaivVPDPE 598
Cdd:cd05969 345 SGHRVGPFEVESALMEHPAVAEAGVIG-----------KPDPL 376
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
413-553 |
3.64e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 53.17 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 413 QMLLG---------PNIRQLILGAAKSDVSAMRFARGAFGVEVLEGYGQTETSGPTTL--------QLVGDTRIGCV--- 472
Cdd:PRK07008 279 LGLLNhmreaglrfSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLcklkwkhsQLPLDEQRKLLekq 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 473 GPPMACAMIKLID-----VPELGysvdKNGGEVLVKGHNVTSGYYKNPEatasSFTEDGYMKTGDIGRFTAEGSLQIIDR 547
Cdd:PRK07008 359 GRVIYGVDMKIVGddgreLPWDG----KAFGDLQVRGPWVIDRYFRGDA----SPLVDGWFPTGDVATIDADGFMQITDR 430
|
....*.
gi 17541856 548 RKNVFK 553
Cdd:PRK07008 431 SKDVIK 436
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
254-547 |
3.74e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 54.01 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 254 PHVPPTPETLATISFTSGTTGRPKGVMLTH---LNMCSATMscEEFENEAgvQDAYLSYLPLAHIYERLCLLSNFMIGSR 330
Cdd:PRK12467 1711 PAVNLAPQNLAYVIYTSGSTGRPKGAGNRHgalVNRLCATQ--EAYQLSA--ADVVLQFTSFAFDVSVWELFWPLINGAR 1786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 331 IgfsrgdpkLLVDDVQALAPRSFAtvpRVIDKIHKAVMKQVQDkplkkmILNAAIAyklyhykmtgkatrktwVDKYVLH 410
Cdd:PRK12467 1787 L--------VIAPPGAHRDPEQLI---QLIERQQVTTLHFVPS------MLQQLLQ-----------------MDEQVEH 1832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 411 KiqmllgPNIRQLILGAAKSDVSAMRFARGAFG-VEVLEGYGQTETS-GPT--TLQLVGDTRIGCV--GPPMACAMIKLI 484
Cdd:PRK12467 1833 P------LSLRRVVCGGEALEVEALRPWLERLPdTGLFNLYGPTETAvDVThwTCRRKDLEGRDSVpiGQPIANLSTYIL 1906
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 485 DVpELGYSVDKNGGEVLVKGHNVTSGYYKNPEATASSFTEDGY-------MKTGDIGRFTAEGSLQIIDR 547
Cdd:PRK12467 1907 DA-SLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgtvgsrlYRTGDLARYRADGVIEYLGR 1975
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
259-608 |
6.20e-07 |
|
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: 52.40 E-value: 6.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 259 TPETLATISFTSGTTGRPKGVMLTHLNMCSATMSCEEfeneagvqdaylSYLPLAHIYERLCLLSNF--------MIGSR 330
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSE------------RYFGRDNGDEAVLFFSNYvfdffveqMTLAL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 331 IGfsrGDPKLLVDDVQALAPRSFatvPRVIDKiHKavmkqvqdkplkkmilnaaIAYklyhykMTGKATrktwvdkyVLH 410
Cdd:cd17648 160 LN---GQKLVVPPDEMRFDPDRF---YAYINR-EK-------------------VTY------LSGTPS--------VLQ 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 411 KIQMLLGPNIRQLIlgAAKSDVSAMRFA--RGAFGVEVLEGYGQTETSGPTTLQLV-GDTR----IGCVGPPMACAMI-- 481
Cdd:cd17648 200 QYDLARLPHLKRVD--AAGEEFTAPVFEklRSRFAGLIINAYGPTETTVTNHKRFFpGDQRfdksLGRPVRNTKCYVLnd 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 482 KLIDVPELGYsvdkngGEVLVKGHNVTSGYYKNPEATASSFTEDGYM--------------KTGDIGRFTAEGSLQIIDR 547
Cdd:cd17648 278 AMKRVPVGAV------GELYLGGDGVARGYLNRPELTAERFLPNPFQteqerargrnarlyKTGDLVRWLPSGELEYLGR 351
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17541856 548 RKNVFKMpQGKFVAPDLTESLYTSSSFVQQIYV--------HGDMEKPWLVAIVVPDPEYLASYALTKH 608
Cdd:cd17648 352 NDFQVKI-RGQRIEPGEVEAALASYPGVRECAVvakedasqAQSRIQKYLVGYYLPEPGHVPESDLLSF 419
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
252-547 |
8.81e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 52.86 E-value: 8.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 252 HRPHVPPTPETLATISFTSGTTGRPKGVMLTHlnmCSATMSCEEFEN--EAGVQDAYLSYLPLAHIYERLCLLSNFMIGS 329
Cdd:PRK12467 3228 NNPSTRVMGENLAYVIYTSGSTGKPKGVGVRH---GALANHLCWIAEayELDANDRVLLFMSFSFDGAQERFLWTLICGG 3304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 330 RIgfsrgdpkllvddvqALAPRSFATVPRVIDKIHKavmKQVQdkplkkmILNAAIAYkLYHYKMTGKATRKTWVDKYVL 409
Cdd:PRK12467 3305 CL---------------VVRDNDLWDPEELWQAIHA---HRIS-------IACFPPAY-LQQFAEDAGGADCASLDIYVF 3358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 410 HkiqmllgpnirqlilGAAKSDVSAMRFARGAFGVEVLEGYGQTETS-GPTTLQLVGDTRIGCVGPPMAcamiklIDVPE 488
Cdd:PRK12467 3359 G---------------GEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVvTVTLWKCGGDAVCEAPYAPIG------RPVAG 3417
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17541856 489 LG-YSVDKNG--------GEVLVKGHNVTSGYYKNPEATASSFTEDGYM-------KTGDIGRFTAEGSLQIIDR 547
Cdd:PRK12467 3418 RSiYVLDGQLnpvpvgvaGELYIGGVGLARGYHQRPSLTAERFVADPFSgsggrlyRTGDLARYRADGVIEYLGR 3492
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
269-547 |
9.39e-07 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 51.58 E-value: 9.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 269 TSGTTGRPKGVMLTHLNMCSATMSCEEFENEAGvqdAYLSYLPLAHIYERLCLLSNFMIGSR---IGFSRG-DPKLLVDD 344
Cdd:PRK07824 43 TSGTTGTPKGAMLTAAALTASADATHDRLGGPG---QWLLALPAHHIAGLQVLVRSVIAGSEpveLDVSAGfDPTALPRA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 345 VQALA-PRSFAT-VPRVIDKihkavmkqVQDKPlkkmilnAAIAyklyhykmtgkatrktwvdkyVLHKIQMLLgpnirq 422
Cdd:PRK07824 120 VAELGgGRRYTSlVPMQLAK--------ALDDP-------AATA---------------------ALAELDAVL------ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 423 liLGAAKSDVSAMRFARGAfGVEVLEGYGQTETSGpttlqlvgdtriGCV--GPPMACAMIKLIDvpelgysvdkngGEV 500
Cdd:PRK07824 158 --VGGGPAPAPVLDAAAAA-GINVVRTYGMSETSG------------GCVydGVPLDGVRVRVED------------GRI 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 17541856 501 LVKGHNVTSGyYKNPEaTASSFTEDGYMKTGDIGRFTaEGSLQIIDR 547
Cdd:PRK07824 211 ALGGPTLAKG-YRNPV-DPDPFAEPGWFRTDDLGALD-DGVLTVLGR 254
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
257-643 |
1.33e-06 |
|
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: 51.36 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 257 PPTPETLATISFTSGTTGRPKGVMLTHLNMCS--ATMSCEEfENEAGVQDAYLSYLPLAHIyerlcllsnfmigsrIGFS 334
Cdd:cd05923 146 PREPEQPAFVFYTSGTTGLPKGAVIPQRAAESrvLFMSTQA-GLRHGRHNVVLGLMPLYHV---------------IGFF 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 335 rgdpKLLVddvQALAPRSFATVPRVIDKIHkaVMKQVQDKPLKKMILNAAIAYKLYHYkMTGKATRKTWVDKYVLhkiqm 414
Cdd:cd05923 210 ----AVLV---AALALDGTYVVVEEFDPAD--ALKLIEQERVTSLFATPTHLDALAAA-AEFAGLKLSSLRHVTF----- 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 415 llgpnirqliLGAAKSDVSAMRFARgAFGVEVLEGYGQTETSGPTTLQlvgDTRIGCVGPPMACAMIKLIDVPELGYSVD 494
Cdd:cd05923 275 ----------AGATMPDAVLERVNQ-HLPGEKVNIYGTTEAMNSLYMR---DARTGTEMRPGFFSEVRIVRIGGSPDEAL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 495 KNG--GEVLVK--GHNVTSGYYKNPEATASSFtEDGYMKTGDIGRFTAEGSLQIIDRRKNVFkMPQGKFVAPDLTESLYT 570
Cdd:cd05923 341 ANGeeGELIVAaaADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLS 418
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17541856 571 SSSFVQQIYVHGDMEKPW---LVAIVVPDPEYLASYALtkhningktyEQLCNIPILADdvlrqFvelteedKRPR 643
Cdd:cd05923 419 RHPGVTEVVVIGVADERWgqsVTACVVPREGTLSADEL----------DQFCRASELAD-----F-------KRPR 472
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
260-598 |
3.01e-06 |
|
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: 50.25 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 260 PETLATISFTSGTTGRPKGVMLTH---LNMCSATMSCeeFenEAGVQDAYLSYLPLAHIYERLCLLSNFMIGSRIGFSRG 336
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHhnlVNLCEWHRPY--F--GVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPS 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 337 DPKLlvdDVQALApRSFATVPRVIDkihkavmkqvqdkplkkmilnaaiayklyhYKMTGKATRKTWVDKYVLhkiqmll 416
Cdd:cd17645 179 ERRL---DLDALN-DYFNQEGITIS------------------------------FLPTGAAEQFMQLDNQSL------- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 417 gpniRQLILGAAKSDvsamRFARGAFgvEVLEGYGQTE-TSGPTTLQLVGDTRIGCVGPPMACAMIKLID----VPELGY 491
Cdd:cd17645 218 ----RVLLTGGDKLK----KIERKGY--KLVNNYGPTEnTVVATSFEIDKPYANIPIGKPIDNTRVYILDealqLQPIGV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 492 SvdkngGEVLVKGHNVTSGYYKNPEATASSFTEDGYM------KTGDIGRFTAEGSLQIIDRRKNVFKMpQGKFVAPDLT 565
Cdd:cd17645 288 A-----GELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEI 361
|
330 340 350
....*....|....*....|....*....|....*.
gi 17541856 566 ESLYTSSSFVQQIYVHGDMEK---PWLVAIVVPDPE 598
Cdd:cd17645 362 EPFLMNHPLIELAAVLAKEDAdgrKYLVAYVTAPEE 397
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
450-598 |
4.47e-06 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 49.61 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 450 YGQTETSGPTTLQLVGDTRIG--CVGPPMACAMIKLIDVPElgysvdkngGEVLVKGHNVTSGYYKNPEATASSFTedgy 527
Cdd:PRK07445 261 YGMTETASQIATLKPDDFLAGnnSSGQVLPHAQITIPANQT---------GNITIQAQSLALGYYPQILDSQGIFE---- 327
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17541856 528 mkTGDIGRFTAEGSLQIIDRRKNVFkMPQGKFVAPDLTESLYTSSSFVQQIYVHGDMEKPW---LVAIVVPDPE 598
Cdd:PRK07445 328 --TDDLGYLDAQGYLHILGRNSQKI-ITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWgevVTAIYVPKDP 398
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
251-547 |
9.59e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 48.77 E-value: 9.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 251 KHRPHVPPTPETLATIS-FTSGTTGRPKGVMLTHLnmcSATMSCEEF-------ENEAGVQDAylsylPLAHIYERLCLL 322
Cdd:PRK07788 196 GSSTAPLPKPPKPGGIViLTSGTTGTPKGAPRPEP---SPLAPLAGLlsrvpfrAGETTLLPA-----PMFHATGWAHLT 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 323 SNFMIGSRIGFSRG-DPKLLVDDVQALAPRSFATVPrvidkihkaVMkqvqdkpLKKMilnaaiayklyhykmtgkatrk 401
Cdd:PRK07788 268 LAMALGSTVVLRRRfDPEATLEDIAKHKATALVVVP---------VM-------LSRI---------------------- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 402 twVDkyvlhkiqmlLGPNIRqlilgaAKSDVSAMRF---------------ARGAFGvEVLEG-YGQTETSGPT--TLQl 463
Cdd:PRK07788 310 --LD----------LGPEVL------AKYDTSSLKIifvsgsalspelatrALEAFG-PVLYNlYGSTEVAFATiaTPE- 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 464 vgDTRI--GCVGPPMACAMIKLIDvpELGYSVDKNG-GEVLVKGHNVTSGYY--KNPEatassfTEDGYMKTGDIGRFTA 538
Cdd:PRK07788 370 --DLAEapGTVGRPPKGVTVKILD--ENGNEVPRGVvGRIFVGNGFPFEGYTdgRDKQ------IIDGLLSSGDVGYFDE 439
|
....*....
gi 17541856 539 EGSLQIIDR 547
Cdd:PRK07788 440 DGLLFVDGR 448
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
253-540 |
1.06e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 48.48 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 253 RPHVPPTPETLATISFTSGTTGRPKGVMLTH--LNMCSATMsCEEFENEAgvQD-AYLSyLPLAH---IYE--------- 317
Cdd:PRK13388 142 TPHREVDAMDPFMLIFTSGTTGAPKAVRCSHgrLAFAGRAL-TERFGLTR--DDvCYVS-MPLFHsnaVMAgwapavasg 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 318 -RLCLLSNFmigSRIGFsrgdpkllVDDVQALAPRSFATVPRvidkihkavmkqvqdkplkkmilnaAIAYKLyhykmtg 396
Cdd:PRK13388 218 aAVALPAKF---SASGF--------LDDVRRYGATYFNYVGK-------------------------PLAYIL------- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 397 kATRKTWVDkyvlhkiqmllGPNIRQLILGAAKSDVSAMRFARgAFGVEVLEGYGQTETSGPTTlqLVGDTRIGCVGPPM 476
Cdd:PRK13388 255 -ATPERPDD-----------ADNPLRVAFGNEASPRDIAEFSR-RFGCQVEDGYGSSEGAVIVV--REPGTPPGSIGRGA 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 477 ACAMI------KLIDVPELgysvDKNG---------GE-VLVKGHNVTSGYYKNPEATASSFtEDGYMKTGDIGRFTAEG 540
Cdd:PRK13388 320 PGVAIynpetlTECAVARF----DAHGallnadeaiGElVNTAGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRDADG 394
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
498-551 |
1.11e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 48.79 E-value: 1.11e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17541856 498 GEVLVKGHNVTSGYYKNPEATASSF----------TEDG-YMKTGDIGrFTAEGSLQIIDRRKNV 551
Cdd:PRK05850 398 GEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgTPEGpWLRTGDLG-FISEGELFIVGRIKDL 461
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
253-283 |
1.43e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 48.50 E-value: 1.43e-05
10 20 30
....*....|....*....|....*....|.
gi 17541856 253 RPHVPPTPETLATISFTSGTTGRPKGVMLTH 283
Cdd:PRK10252 590 APLQLSQPHHTAYIIFTSGSTGRPKGVMVGQ 620
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
444-551 |
1.78e-05 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 48.08 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 444 VEVLEGYGQTETSGPTTLQLvgDTRIGCvGPPMACAMIKLID-----VPELGYsvdkngGEVLVKGHNVTSGYYKNPEaT 518
Cdd:PRK09192 362 RDRLEYQGKAVAPGAETRRV--RTFVNC-GKALPGHEIEIRNeagmpLPERVV------GHICVRGPSLMSGYFRDEE-S 431
|
90 100 110
....*....|....*....|....*....|...
gi 17541856 519 ASSFTEDGYMKTGDIGrFTAEGSLQIIDRRKNV 551
Cdd:PRK09192 432 QDVLAADGWLDTGDLG-YLLDGYLYITGRAKDL 463
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
256-550 |
1.90e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 47.80 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 256 VPPTP--ETLATISFTSGTTGRPKGVMLTHLNMCSATM----SCEEFENEAGVqdaylSYLPLAHIYERLCLLSNFMIGS 329
Cdd:PRK07769 173 VPPEAneDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLqvidALEGQEGDRGV-----SWLPFFHDMGLITVLLPALLGH 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 330 RIGFsrgdpkllvddvqaLAPRSFATVP-RVIdkihkavmKQVQDKP-LKKMILNAAIAYKLYHYKMTG--KATRKTWvD 405
Cdd:PRK07769 248 YITF--------------MSPAAFVRRPgRWI--------RELARKPgGTGGTFSAAPNFAFEHAAARGlpKDGEPPL-D 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 406 KyvlhkiqmllgPNIRQLILGAAKSDVSAMRFARGAFG------VEVLEGYGQTETS----------GPTTLQL----VG 465
Cdd:PRK07769 305 L-----------SNVKGLLNGSEPVSPASMRKFNEAFApyglppTAIKPSYGMAEATlfvsttpmdeEPTVIYVdrdeLN 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 466 DTRIGCVGP--PMACAMIKLIDV----------PELGYSV-DKNGGEVLVKGHNVTSGYYKNPEATASSF---------- 522
Cdd:PRK07769 374 AGRFVEVPAdaPNAVAQVSAGKVgvsewavivdPETASELpDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrlse 453
|
330 340 350
....*....|....*....|....*....|....*
gi 17541856 523 ------TEDG-YMKTGDIGRFTaEGSLQIIDRRKN 550
Cdd:PRK07769 454 shaegaPDDAlWVRTGDYGVYF-DGELYITGRVKD 487
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
261-595 |
2.39e-05 |
|
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: 47.47 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 261 ETLATISFTSGTTGRPKGVMLTHLNMCSATmsceEFENEAGVQDAYLSYLPLAHIYERLC---LLSNFMIGSRIGFSRGD 337
Cdd:cd17656 128 DDLLYIIYTSGTTGKPKGVQLEHKNMVNLL----HFEREKTNINFSDKVLQFATCSFDVCyqeIFSTLLSGGTLYIIREE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 338 PKLLVDDVQALAPRsfatvprviDKIHKAVMKQVqdkpLKKMILNaaiaykLYHYKMTgkatrktwvdkyvlhkiqmlLG 417
Cdd:cd17656 204 TKRDVEQLFDLVKR---------HNIEVVFLPVA----FLKFIFS------EREFINR--------------------FP 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 418 PNIRQLILGAAKSDVS-AMRFARGAFGVEVLEGYGQTETSGPTTLQLVGDTRIGC---VGPPMACAMIklidvpelgYSV 493
Cdd:cd17656 245 TCVKHIITAGEQLVITnEFKEMLHEHNVHLHNHYGPSETHVVTTYTINPEAEIPElppIGKPISNTWI---------YIL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 494 DKNG--------GEVLVKGHNVTSGYYKNPEATASSFTEDGY------MKTGDIGRFTAEGSLQIIDRRKNVFKMpQGKF 559
Cdd:cd17656 316 DQEQqlqpqgivGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-RGYR 394
|
330 340 350
....*....|....*....|....*....|....*....
gi 17541856 560 VAPDLTESLYTSSSFVQQ--IYVHGDME-KPWLVAIVVP 595
Cdd:cd17656 395 IELGEIEAQLLNHPGVSEavVLDKADDKgEKYLCAYFVM 433
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
115-553 |
3.20e-05 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 47.08 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 115 ISYDQAFETSDHASQAIRKLGIEigEESKIGIYSNNRPEWILSEMAIHNFSNVSVPLydtitnddmhyitnlceislmfv 194
Cdd:cd17654 17 VSYADLAEKISNLSNFLRKKFQT--EERAIGLRCDRGTESPVAILAILFLGAAYAPI----------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 195 daeiktkqlirDKSYLSSLKYIVqFNECSDDIKEmarENDFRLWSFNEFVEmgkkqKHRPHVPPTPETLATISFTSGTTG 274
Cdd:cd17654 72 -----------DPASPEQRSLTV-MKKCHVSYLL---QNKELDNAPLSFTP-----EHRHFNIRTDECLAYVIHTSGTTG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 275 RPKGVMLTHL----NMCSATMSCEEFENEAGVQDAYLSYLPlahiyerlCLLSNFMigsriGFSRGDPKLLVDDVQALAP 350
Cdd:cd17654 132 TPKIVAVPHKcilpNIQHFRSLFNITSEDILFLTSPLTFDP--------SVVEIFL-----SLSSGATLLIVPTSVKVLP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 351 RSFATvprVIDKIHKAVMKQvqdkplkkmiLNAAIayklyhYKMTGKATRKTwvdkYVLHKIQmllgpNIRQLILG--AA 428
Cdd:cd17654 199 SKLAD---ILFKRHRITVLQ----------ATPTL------FRRFGSQSIKS----TVLSATS-----SLRVLALGgePF 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 429 KSDVSAMRFARGAFGVEVLEGYGQTETSGPTTLQLVGDTRIGC-VGPPMACAMIklidvpelgYSVDKNG----GEVLVK 503
Cdd:cd17654 251 PSLVILSSWRGKGNRTRIFNIYGITEVSCWALAYKVPEEDSPVqLGSPLLGTVI---------EVRDQNGsegtGQVFLG 321
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 17541856 504 GHN---VTSGYYKNPEATassftedgYMKTGDIGRFTaEGSLQIIDRRKNVFK 553
Cdd:cd17654 322 GLNrvcILDDEVTVPKGT--------MRATGDFVTVK-DGELFFLGRKDSQIK 365
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
254-599 |
3.80e-05 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 46.79 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 254 PHVPPTPETLATISFTSGTTGRPKGVMLTHLN-MCSATMSCEEFENEAgvQDAYLSYLPLAH-----IYERLcLLSnfmi 327
Cdd:PRK09029 128 HAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAhLASAEGVLSLMPFTA--QDSWLLSLPLFHvsgqgIVWRW-LYA---- 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 328 GSRIGFsRGDPKLLvddvQALAPRSFAT-VP----RVIDKIHKAVmkqvqdkPLKKMIL-NAAIAYKLyhykmTGKATRK 401
Cdd:PRK09029 201 GATLVV-RDKQPLE----QALAGCTHASlVPtqlwRLLDNRSEPL-------SLKAVLLgGAAIPVEL-----TEQAEQQ 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 402 twvdkyvlhkiqmllgpnirqlilgaaksdvsamrfargafGVEVLEGYGQTETsGPTTLQLVGDTRIGcVGPPMACAMI 481
Cdd:PRK09029 264 -----------------------------------------GIRCWCGYGLTEM-ASTVCAKRADGLAG-VGSPLPGREV 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 482 KLIDvpelgysvdkngGEVLVKGHNVTSGYYKNPEATasSFT-EDGYMKTGDIGRFtAEGSLQIIDRRKNVFkMPQGKFV 560
Cdd:PRK09029 301 KLVD------------GEIWLRGASLALGYWRQGQLV--PLVnDEGWFATRDRGEW-QNGELTILGRLDNLF-FSGGEGI 364
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 17541856 561 APDLTESLYTSSSFVQQiyvhgdmekpwlvAIVVP--DPEY 599
Cdd:PRK09029 365 QPEEIERVINQHPLVQQ-------------VFVVPvaDAEF 392
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
250-550 |
3.90e-05 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 46.62 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 250 QKHRPHVPPTPETLATISFTSGTTGRPKGVmlthlnmcsatmscEEFENEAGvqdaylsylpLAHIYERlcllsnfMIGS 329
Cdd:PRK12406 141 AQQEPYDGPPVPQPQSMIYTSGTTGHPKGV--------------RRAAPTPE----------QAAAAEQ-------MRAL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 330 RIGFSRGDPKLLVDDVQALAPRSFATVP-RVIDKIhkAVMKQVQDKPLKKMILnaaiAYKLYHYKMTgkatrktwvdKYV 408
Cdd:PRK12406 190 IYGLKPGIRALLTGPLYHSAPNAYGLRAgRLGGVL--VLQPRFDPEELLQLIE----RHRITHMHMV----------PTM 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 409 LHKIqMLLGPNIRqlilgaAKSDVSAMRFARGA---------------FGVEVLEGYGQTETsGPTTLQLVGD--TRIGC 471
Cdd:PRK12406 254 FIRL-LKLPEEVR------AKYDVSSLRHVIHAaapcpadvkramiewWGPVIYEYYGSTES-GAVTFATSEDalSHPGT 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 472 VGPPMACAMIKLIDvpELGYSVDKNG-GEVLVKGHNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRKN 550
Cdd:PRK12406 326 VGKAAPGAELRFVD--EDGRPLPQGEiGEIYSRIAGNPDFTYHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRD 403
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
498-607 |
4.65e-05 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 46.43 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 498 GEVLVKGHNVTSGYYKNPEATASSF-TEDGY--MKTGDIGRFtAEGSLQI---IDrrknvFkmpQGKF---------VAP 562
Cdd:PRK04813 345 GEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGYL-EDGLLFYqgrID-----F---QIKLngyrieleeIEQ 415
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 17541856 563 DLTESLYTSSSFVQQIYVHGDMEKpwLVAIVVP-DPEYLASYALTK 607
Cdd:PRK04813 416 NLRQSSYVESAVVVPYNKDHKVQY--LIAYVVPkEEDFEREFELTK 459
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
443-551 |
5.72e-05 |
|
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: 46.30 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 443 GVEVLEGYGQTETSGPTTLQLVGDTRIGCVGPPMACAMIKLIDVpelgysvdknGGEVLVKGHN--------------VT 508
Cdd:cd05928 316 GLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDD----------NGNVLPPGTEgdigirvkpirpfgLF 385
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 17541856 509 SGYYKNPEATASSFTEDGYMkTGDIGRFTAEGSLQIIDRRKNV 551
Cdd:cd05928 386 SGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDV 427
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
242-292 |
1.73e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 45.16 E-value: 1.73e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 17541856 242 EFVEMGKKQKHRPHVPPTPETLATISFTSGTTGRPKGVMLTHLNMCSATMS 292
Cdd:PRK05691 3850 EEVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLS 3900
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
113-283 |
2.65e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 44.12 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 113 EWISYDQAFETSDHASQAIRKLGIEIGEesKIGIYSNNRPEWILSEMAIHNFSNVSVPLYDTITNDDMHYITNLCEislm 192
Cdd:PRK04319 72 EKYTYKELKELSNKFANVLKELGVEKGD--RVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSE---- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 193 fVDAEIKTKQLIRDK--SYLSSLKYIVQFNEcsddikemARENDFRLWSFNEfvEMGKKQKHRPHVPPTPETLATISFTS 270
Cdd:PRK04319 146 -AKVLITTPALLERKpaDDLPSLKHVLLVGE--------DVEEGPGTLDFNA--LMEQASDEFDIEWTDREDGAILHYTS 214
|
170
....*....|...
gi 17541856 271 GTTGRPKGVMLTH 283
Cdd:PRK04319 215 GSTGKPKGVLHVH 227
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
560-698 |
2.77e-04 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 44.46 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 560 VAPDLtESLYTSSSFVQQIYVHGDMEKPwLVAIVVP-----DPEYLASYALTK-----HNINGKTYEQLCNIPILADDVL 629
Cdd:PTZ00297 871 IAAEL-ERIFSQSRYVNDIFLYADPSRP-IIAIVSPnrdtvEFEWRQSHCMGEgggpaRQLGWTELVAYASSLLTADFAC 948
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17541856 630 RQFVELTEEDKRPRYegvygVHLTPVAFSAENGLTTPTLKNKRNAIAQFFKAEIDGMYKKIETSELSNL 698
Cdd:PTZ00297 949 IAKENGLHPSNVPEY-----VHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIERFYSDVETTPLPTP 1012
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
254-547 |
3.01e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 44.56 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 254 PHVPPTPETLATISFTSGTTGRPKGVMLTHLNMcSATMSCEEFENEAGVQDAYLSYLPLAHIYERLCLLSNFMIGSRI-- 331
Cdd:PRK12316 648 PGTELNPENLAYVIYTSGSTGKPKGAGNRHRAL-SNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLvv 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 332 ---GFSRgDPKLLVDDVQALAPRSFATVPRVIDK-IHKAVMKQVQdkPLKKMILnaaiayklyhykmTGKAtrktwvdky 407
Cdd:PRK12316 727 aapGDHR-DPAKLVELINREGVDTLHFVPSMLQAfLQDEDVASCT--SLRRIVC-------------SGEA--------- 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 408 vlhkiqmllgpnirqlILGAAKSDVSAMRFARGAFGVevlegYGQTETSGPTT----LQLVGDTRigCVGPPMACAMIKL 483
Cdd:PRK12316 782 ----------------LPADAQEQVFAKLPQAGLYNL-----YGPTEAAIDVThwtcVEEGGDSV--PIGRPIANLACYI 838
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17541856 484 ID-----VPeLGYSvdkngGEVLVKGHNVTSGYYKNPEATASSFTEDGYM------KTGDIGRFTAEGSLQIIDR 547
Cdd:PRK12316 839 LDanlepVP-VGVL-----GELYLAGRGLARGYHGRPGLTAERFVPSPFVagermyRTGDLARYRADGVIEYAGR 907
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
253-548 |
3.93e-04 |
|
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: 43.52 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 253 RPHVPPTPETLAT-ISFTSGTTGRPKGVMLTHlnmcsatmSCEEFENEAGV----------QDAYLSYLPLAHIY-ERLC 320
Cdd:cd05929 116 SPETPIEDEAAGWkMLYSGGTTGRPKGIKRGL--------PGGPPDNDTLMaaalgfgpgaDSVYLSPAPLYHAApFRWS 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 321 LLSNFMIGSRIGFSRGDPKLLVDDVQALAPRSFATVPRVIDKIHK---AVMKQVQDKPLKKMILNAAIAyklyhykmtgk 397
Cdd:cd05929 188 MTALFMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKlpeAVRNAYDLSSLKRVIHAAAPC----------- 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 398 atrKTWVdkyvlhKIQML-LGPNIrqlilgaaksdvsamrfargafgveVLEGYGQTETSGPTTLQlvGD---TRIGCVG 473
Cdd:cd05929 257 ---PPWV------KEQWIdWGGPI-------------------------IWEYYGGTEGQGLTIIN--GEewlTHPGSVG 300
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17541856 474 PPMAcAMIKLIDvpELGYSVDKNG-GEVLVKGhNVTSGYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRR 548
Cdd:cd05929 301 RAVL-GKVHILD--EDGNEVPPGEiGEVYFAN-GPGFEYTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRR 372
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
254-334 |
5.50e-04 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 43.05 E-value: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541856 254 PHVPPTPETLATISFTSGTTGRPKGVMLTHLN--MCSA-TMSCeefenEAGVQDAYLSYLPLAHiyerlcllsnfMIGSR 330
Cdd:cd05938 137 LRAHVTIKSPALYIYTSGTTGLPKAARISHLRvlQCSGfLSLC-----GVTADDVIYITLPLYH-----------SSGFL 200
|
....
gi 17541856 331 IGFS 334
Cdd:cd05938 201 LGIG 204
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
510-549 |
7.39e-04 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 42.67 E-value: 7.39e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 17541856 510 GYYKNPEATASSFTEDGYMKTGDIGRFTAEGSLQIIDRRK 549
Cdd:PRK10946 393 GYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREK 432
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
260-283 |
7.78e-03 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 39.66 E-value: 7.78e-03
10 20
....*....|....*....|....
gi 17541856 260 PETLATISFTSGTTGRPKGVMLTH 283
Cdd:TIGR03443 414 PDSNPTLSFTSGSEGIPKGVLGRH 437
|
|
| |
