|
Name |
Accession |
Description |
Interval |
E-value |
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
29-536 |
0e+00 |
|
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: 763.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 29 NPGLSAVDLLlrRAAACPSALALVDAATGHALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTAL 108
Cdd:cd05904 4 DLPLDSVSFL--FASAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKR-GGRKGDVVLLLSPNSIEFPVAFLAVLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 109 GAVASTANPLYTPREIAKQASDARARLVITVAELLPKVADLRLPVILLDDTAAKSGSSatlySDLVSGVDEADYRRPPTK 188
Cdd:cd05904 81 GAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLASLALPVVLLDSAEFDSLSF----SDLLFEADEAEPPVVVIK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 189 QSDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVTSDQDDRGEGPNVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGF 268
Cdd:cd05904 157 QDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPRF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 269 ALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFPDALICQGYGMTETCGI 348
Cdd:cd05904 237 DLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTGV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 349 ISLEYPEKGQVRQFGSTGTLVTGVEAKIVDVETLKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTIR-QGWLHTGDLGL 427
Cdd:cd05904 317 VAMCFAPEKDRAKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDkEGWLHTGDLCY 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 428 FDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQ 507
Cdd:cd05904 397 IDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQ 476
|
490 500
....*....|....*....|....*....
gi 357113996 508 VTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd05904 477 VAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
13-540 |
0e+00 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 532.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 13 ADGVYRSLRPAARIESNpgLSAVDLLLRRAAACPSALALVDAATGHALTFSGLRSAILASAVALSsRAGVRPGDSVLLVA 92
Cdd:PLN02246 6 EEFIFRSKLPDIYIPNH--LPLHDYCFERLSEFSDRPCLIDGATGRVYTYADVELLSRRVAAGLH-KLGIRQGDVVMLLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 93 PNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVITVAELLPKVADLR----LPVILLDDTAAKSGSsat 168
Cdd:PLN02246 83 PNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLAeddgVTVVTIDDPPEGCLH--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 169 lYSDLVSGvDEADYRRPPTKQSDTAGLLYSSGTTGESKGVVLTHRNfiaaatMVTS--DQDDrGEGPN-------VFLCF 239
Cdd:PLN02246 160 -FSELTQA-DENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKG------LVTSvaQQVD-GENPNlyfhsddVILCV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 240 LPMFHIFGLSVITYGQLQRGNTVVVMSGFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPL 319
Cdd:PLN02246 231 LPMFHIYSLNSVLLCGLRVGAAILIMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 320 GKDVMEAVAKNFPDALICQGYGMTETCGIISL-------EYPEKGqvrqfGSTGTLVTGVEAKIVDVETLKHLPPNQLGE 392
Cdd:PLN02246 311 GKELEDAFRAKLPNAVLGQGYGMTEAGPVLAMclafakePFPVKS-----GSCGTVVRNAELKIVDPETGASLPRNQPGE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 393 ICVRGPHIMQGYFNNVQATEFTI-RQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVV 471
Cdd:PLN02246 386 ICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAV 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 357113996 472 IPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRRELIAKV 540
Cdd:PLN02246 466 VPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAKL 534
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
50-532 |
0e+00 |
|
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: 524.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 50 ALVDAATGHALTFSGLRSAILASAVALSsRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQAS 129
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLR-KLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 130 DARARLVITVAELLPKVADL--RLP----VILLDDTAAKSGSSATLYSDLVSGVDEADYRRPPTKQSDTAGLLYSSGTTG 203
Cdd:cd05911 80 ISKPKVIFTDPDGLEKVKEAakELGpkdkIIVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 204 ESKGVVLTHRNFIAAATMVTSDQDDRGEGPNVFLCFLPMFHIFGLsVITYGQLQRGNTVVVMSGFALDTVMSAVQQHRVT 283
Cdd:cd05911 160 LPKGVCLSHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYHIYGL-FTTLASLLNGATVIIMPKFDSELFLDLIEKYKIT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 284 HLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFPDALICQGYGMTETCGIISLEypeKGQVRQFG 363
Cdd:cd05911 239 FLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVN---PDGDDKPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 364 STGTLVTGVEAKIVDVETLKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTI-RQGWLHTGDLGLFDDEGQLFVVDRLKE 442
Cdd:cd05911 316 SVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFdEDGWLHTGDIGYFDEDGYLYIVDRKKE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 443 LIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQVTYYKRL-KRVTFVS 521
Cdd:cd05911 396 LIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYKQLrGGVVFVD 475
|
490
....*....|.
gi 357113996 522 SVPKSASGKIL 532
Cdd:cd05911 476 EIPKSASGKIL 486
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
13-545 |
5.69e-161 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 469.71 E-value: 5.69e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 13 ADGVYRSLRPAARIESNPGLSAVDLLLRRAAAcPSALALVDAATGHALTFSGLRSAILASAVALSSRAGVRPGDSVLLVA 92
Cdd:PLN02574 21 ETGIYSSKHPPVPLPSDPNLDAVSFIFSHHNH-NGDTALIDSSTGFSISYSELQPLVKSMAAGLYHVMGVRQGDVVLLLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 93 PNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVITVAELLPKVADLRLPVILLDDTA---AKSGSSATL 169
Cdd:PLN02574 100 PNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSPLGVPVIGVPENYdfdSKRIEFPKF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 170 YSDLVSGVDEAdyRRPPTKQSDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVTSDQDDRGEGP---NVFLCFLPMFHIF 246
Cdd:PLN02574 180 YELIKEDFDFV--PKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEYPgsdNVYLAALPMFHIY 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 247 GLSVITYGQLQRGNTVVVMSGFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGK-AGKYDLSSLKFIGSGAAPLGKDVME 325
Cdd:PLN02574 258 GLSLFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKgVCGEVLKSLKQVSCGAAPLSGKFIQ 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 326 AVAKNFPDALICQGYGMTETCGIISLEYPEKgQVRQFGSTGTLVTGVEAKIVDVETLKHLPPNQLGEICVRGPHIMQGYF 405
Cdd:PLN02574 338 DFVQTLPHVDFIQGYGMTESTAVGTRGFNTE-KLSKYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYL 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 406 NNVQATEFTI-RQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPI 484
Cdd:PLN02574 417 NNPKATQSTIdKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPV 496
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357113996 485 AYVVRSPDSSLTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL---IAKVRSSKL 545
Cdd:PLN02574 497 AFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELkrsLTNSVSSRL 560
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
35-536 |
4.90e-156 |
|
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: 453.11 E-value: 4.90e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 35 VDLLLRRAAACPSALALVDAatGHALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVAST 114
Cdd:COG0318 2 ADLLRRAAARHPDRPALVFG--GRRLTYAELDARARRLAAALRAL-GVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 115 ANPLYTPREIAKQASDARARLVITvaellpkvadlrlpvillddtaaksgssatlysdlvsgvdeadyrrpptkqsdtAG 194
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVT------------------------------------------------------AL 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 195 LLYSSGTTGESKGVVLTHRNFIAAATMVTSDQDDRGEgpNVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGFALDTVM 274
Cdd:COG0318 105 ILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPG--DVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 275 SAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFpDALICQGYGMTETCGIISLEyP 354
Cdd:COG0318 183 ELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTVN-P 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 355 EKGQVRQFGSTGTLVTGVEAKIVDVETlKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTIRQGWLHTGDLGLFDDEGQL 434
Cdd:COG0318 261 EDPGERRPGSVGRPLPGVEVRIVDEDG-RELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 435 FVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQVTYYKRL 514
Cdd:COG0318 340 YIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLARYKVP 419
|
490 500
....*....|....*....|..
gi 357113996 515 KRVTFVSSVPKSASGKILRREL 536
Cdd:COG0318 420 RRVEFVDELPRTASGKIDRRAL 441
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
35-536 |
2.12e-142 |
|
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: 418.89 E-value: 2.12e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 35 VDLLLRRAAACPSALALVDaaTGHALTFSGLRSAILASAVALSsRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVAST 114
Cdd:cd05936 2 ADLLEEAARRFPDKTALIF--MGRKLTYRELDALAEAFAAGLQ-NLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 115 ANPLYTPREIAKQASDARARLVITVAELlpkvadlrlpvillddtaaksgssatlySDLVSGVDEADYRRPPTKQsDTAG 194
Cdd:cd05936 79 LNPLYTPRELEHILNDSGAKALIVAVSF----------------------------TDLLAAGAPLGERVALTPE-DVAV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 195 LLYSSGTTGESKGVVLTHRNFIAAATMVTSDQDDRGEGPNVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGFALDTVM 274
Cdd:cd05936 130 LQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGVL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 275 SAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFpDALICQGYGMTETCGIISLEYP 354
Cdd:cd05936 210 KEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELT-GVPIVEGYGLTETSPVVAVNPL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 355 EkgQVRQFGSTGTLVTGVEAKIVDVETlKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTIRQGWLHTGDLGLFDDEGQL 434
Cdd:cd05936 289 D--GPRKPGSIGIPLPGTEVKIVDDDG-EELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYF 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 435 FVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQVTYYKRL 514
Cdd:cd05936 366 FIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVP 445
|
490 500
....*....|....*....|..
gi 357113996 515 KRVTFVSSVPKSASGKILRREL 536
Cdd:cd05936 446 RQVEFRDELPKSAVGKILRREL 467
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
16-540 |
1.95e-137 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 409.37 E-value: 1.95e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 16 VYRSLRPAARIESNpgLSAVDLLLRRAAACPSALALVDAATGHALTFSGLRSAILASAVALSSrAGVRPGDSVLLVAPNC 95
Cdd:PLN02330 14 IFRSRYPSVPVPDK--LTLPDFVLQDAELYADKVAFVEAVTGKAVTYGEVVRDTRRFAKALRS-LGLRKGQVVVVVLPNV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 96 VLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVITVAELLPKVADLRLPVILLDDTaakSGSSATLYSDLVS 175
Cdd:PLN02330 91 AEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGLGLPVIVLGEE---KIEGAVNWKELLE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 176 GVDEA----DYRRppTKQSDTAGLLYSSGTTGESKGVVLTHRNFIAaaTMVTSDQDDRGE--GPNVFLCFLPMFHIFGLS 249
Cdd:PLN02330 168 AADRAgdtsDNEE--ILQTDLCALPFSSGTTGISKGVMLTHRNLVA--NLCSSLFSVGPEmiGQVVTLGLIPFFHIYGIT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 250 VITYGQLQRGNTVVVMSGFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKF--IGSGAAPLGKDVMEAV 327
Cdd:PLN02330 244 GICCATLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLqaIMTAAAPLAPELLTAF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 328 AKNFPDALICQGYGMTE-TCGIISLEYPEKGQ-VRQFGSTGTLVTGVEAKIVDVETLKHLPPNQLGEICVRGPHIMQGYF 405
Cdd:PLN02330 324 EAKFPGVQVQEAYGLTEhSCITLTHGDPEKGHgIAKKNSVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYY 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 406 NNVQATEFTI-RQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPI 484
Cdd:PLN02330 404 NNKEETDRTIdEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPA 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 357113996 485 AYVVRSPDSSLTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRRELIAKV 540
Cdd:PLN02330 484 ACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKM 539
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
36-536 |
3.60e-135 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 402.26 E-value: 3.60e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 36 DLLLRRAAACPSALALVDaaTGHALTFSGL--RSAILASAVAlssRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVAS 113
Cdd:PRK06187 10 RILRHGARKHPDKEAVYF--DGRRTTYAELdeRVNRLANALR---ALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 114 TANPLYTPREIAKQASDARARLVITVAELLPKVADLR--LP----VILLDDTAAK-SGSSATLYSDLVSGVDEaDYRRPP 186
Cdd:PRK06187 85 PINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILpqLPtvrtVIVEGDGPAApLAPEVGEYEELLAAASD-TFDFPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 187 TKQSDTAGLLYSSGTTGESKGVVLTHRNF----IAAATMVTSDQDDrgegpnVFLCFLPMFHIFGLSViTYGQLQRGNTV 262
Cdd:PRK06187 164 IDENDAAAMLYTSGTTGHPKGVVLSHRNLflhsLAVCAWLKLSRDD------VYLVIVPMFHVHAWGL-PYLALMAGAKQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 263 VVMSGFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFpDALICQGYGM 342
Cdd:PRK06187 237 VIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKF-GIDLVQGYGM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 343 TETCGIISLEYPEKGQVRQF---GSTGTLVTGVEAKIVDvETLKHLPPN--QLGEICVRGPHIMQGYFNNVQATEFTIRQ 417
Cdd:PRK06187 316 TETSPVVSVLPPEDQLPGQWtkrRSAGRPLPGVEARIVD-DDGDELPPDggEVGEIIVRGPWLMQGYWNRPEATAETIDG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 418 GWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTE 497
Cdd:PRK06187 395 GWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDA 474
|
490 500 510
....*....|....*....|....*....|....*....
gi 357113996 498 VDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:PRK06187 475 KELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
38-533 |
1.79e-132 |
|
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: 392.36 E-value: 1.79e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 38 LLRRAAACPSALALVDAatGHALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANP 117
Cdd:cd17631 1 LRRRARRHPDRTALVFG--GRSLTYAELDERVNRLAHALRAL-GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 118 LYTPREIAKQASDARARLVItvaellpkvadlrlpvillddtaaksgssatlysdlvsgvdeadyrrpptkqSDTAGLLY 197
Cdd:cd17631 78 RLTPPEVAYILADSGAKVLF----------------------------------------------------DDLALLMY 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 198 SSGTTGESKGVVLTHRNFIAAATMVTSDQDDRGEGpnVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGFALDTVMSAV 277
Cdd:cd17631 106 TSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDD--VLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 278 QQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNfpDALICQGYGMTETCGIISLEYPEkG 357
Cdd:cd17631 184 ERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQAR--GVKFVQGYGMTETSPGVTFLSPE-D 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 358 QVRQFGSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTIRQGWLHTGDLGLFDDEGQLFVV 437
Cdd:cd17631 261 HRRKLGSAGRPVFFVEVRIVD-PDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIV 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 438 DRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQVTYYKRLKRV 517
Cdd:cd17631 340 DRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSV 419
|
490
....*....|....*.
gi 357113996 518 TFVSSVPKSASGKILR 533
Cdd:cd17631 420 EFVDALPRNATGKILK 435
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
35-539 |
1.46e-126 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 380.02 E-value: 1.46e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 35 VDLLLRRAAACPSALALVDAatGHALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVAST 114
Cdd:PRK07656 8 PELLARAARRFGDKEAYVFG--DQRLTYAELNARVRRAAAALAAL-GIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 115 ANPLYTPREIAKQASDARARLVITVAELLP--KVADLRLP-----VILLDDTAAKSGSSATLYSDLVSGvDEADYRRPPT 187
Cdd:PRK07656 85 LNTRYTADEAAYILARGDAKALFVLGLFLGvdYSATTRLPalehvVICETEEDDPHTEKMKTFTDFLAA-GDPAERAPEV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 188 KQSDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVTS----DQDDRgegpnvFLCFLPMFHIFGLSVITYGQLQRGNTVV 263
Cdd:PRK07656 164 DPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEylglTEGDR------YLAANPFFHVFGYKAGVNAPLMRGATIL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 264 VMSGFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFPDALICQGYGMT 343
Cdd:PRK07656 238 PLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVLTGYGLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 344 ETCGIISLEYPEKGQVRQFGSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTIRQ-GWLHT 422
Cdd:PRK07656 318 EASGVTTFNRLDDDRKTVAGTIGTAIAGVENKIVN-ELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDAdGWLHT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 423 GDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQK 502
Cdd:PRK07656 397 GDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEELIA 476
|
490 500 510
....*....|....*....|....*....|....*..
gi 357113996 503 FIETQVTYYKRLKRVTFVSSVPKSASGKILRRELIAK 539
Cdd:PRK07656 477 YCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
39-536 |
1.11e-121 |
|
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: 368.39 E-value: 1.11e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 39 LRRAAACPSALALVDAATGHALTFSGLRSAILASAVALSsRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPL 118
Cdd:cd17642 24 MKRYASVPGTIAFTDAHTGVNYSYAEYLEMSVRLAEALK-KYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 119 YTPREIAKQASDARARLVITVAELLPKVADL--RLP----VILLD---DTAAKSGSSATLYSDLVSGVDEADYRRPP-TK 188
Cdd:cd17642 103 YNERELDHSLNISKPTIVFCSKKGLQKVLNVqkKLKiiktIIILDskeDYKGYQCLYTFITQNLPPGFNEYDFKPPSfDR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 189 QSDTAGLLYSSGTTGESKGVVLTHRNFIAaaTMVTSDQDDRGEGPN---VFLCFLPMFHIFGLsVITYGQLQRGNTVVVM 265
Cdd:cd17642 183 DEQVALIMNSSGSTGLPKGVQLTHKNIVA--RFSHARDPIFGNQIIpdtAILTVIPFHHGFGM-FTTLGYLICGFRVVLM 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 266 SGFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFPDALICQGYGMTET 345
Cdd:cd17642 260 YKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQGYGLTET 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 346 CGIIsLEYPEkGQVRQfGSTGTLVTGVEAKIVDVETLKHLPPNQLGEICVRGPHIMQGYFNNVQAT-EFTIRQGWLHTGD 424
Cdd:cd17642 340 TSAI-LITPE-GDDKP-GAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATkALIDKDGWLHSGD 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 425 LGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFI 504
Cdd:cd17642 417 IAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYV 496
|
490 500 510
....*....|....*....|....*....|...
gi 357113996 505 ETQVTYYKRLK-RVTFVSSVPKSASGKILRREL 536
Cdd:cd17642 497 ASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKI 529
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
191-532 |
5.24e-119 |
|
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: 354.28 E-value: 5.24e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 191 DTAGLLYSSGTTGESKGVVLTHRNFIAAATMVTSDQDDRGEGpnVFLCFLPMFHIFGLSVItYGQLQRGNTVVVMSGFAL 270
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGD--VFLSTLPLFHIGGLFGL-LGALLAGGTVVLLPKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 271 DTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFPDALIcQGYGMTETCGIIS 350
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLV-NGYGLTETGGTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 351 LEYPEkGQVRQFGSTGTLVTGVEAKIVDVETlKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTIRQGWLHTGDLGLFDD 430
Cdd:cd04433 157 TGPPD-DDARKPGSVGRPVPGVEVRIVDPDG-GELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 431 EGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQVTY 510
Cdd:cd04433 235 DGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAP 314
|
330 340
....*....|....*....|..
gi 357113996 511 YKRLKRVTFVSSVPKSASGKIL 532
Cdd:cd04433 315 YKVPRRVVFVDALPRTASGKID 336
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
38-447 |
1.23e-116 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 351.23 E-value: 1.23e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 38 LLRRAAACPSALALVDAaTGHALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANP 117
Cdd:pfam00501 1 LERQAARTPDKTALEVG-EGRRLTYRELDERANRLAAGLRAL-GVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 118 LYTPREIAKQASDARARLVIT--------VAELLPKVADLRLPVILLDDTAAKSGssatLYSDLVSGVDEADYRRPPTKQ 189
Cdd:pfam00501 79 RLPAEELAYILEDSGAKVLITddalkleeLLEALGKLEVVKLVLVLDRDPVLKEE----PLPEEAKPADVPPPPPPPPDP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 190 SDTAGLLYSSGTTGESKGVVLTHRNFIA-AATMVTSDQDDRGEGPN-VFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSG 267
Cdd:pfam00501 155 DDLAYIIYTSGTTGKPKGVMLTHRNLVAnVLSIKRVRPRGFGLGPDdRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 268 FALDTVMS---AVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFPDALIcQGYGMTE 344
Cdd:pfam00501 235 FPALDPAAlleLIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALV-NGYGLTE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 345 TCGIISLEYPEKGQVRQFGSTGTLVTGVEAKIVDVETLKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTI-RQGWLHTG 423
Cdd:pfam00501 314 TTGVVTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFdEDGWYRTG 393
|
410 420
....*....|....*....|....
gi 357113996 424 DLGLFDDEGQLFVVDRLKELIKYK 447
Cdd:pfam00501 394 DLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
46-536 |
4.28e-104 |
|
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: 321.57 E-value: 4.28e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 46 PSALALVDAATGHALTFSGLRSAILASAVALSSrAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIA 125
Cdd:cd05926 1 PDAPALVVPGSTPALTYADLAELVDDLARQLAA-LGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 126 KQASDARARLVIT-------VAELLPKVADLRLPVILLDDTAAKSGSSATLysDLVSGVDEADYRRPPTKQSDTAGLLYS 198
Cdd:cd05926 80 FYLADLGSKLVLTpkgelgpASRAASKLGLAILELALDVGVLIRAPSAESL--SNLLADKKNAKSEGVPLPDDLALILHT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 199 SGTTGESKGVVLTHRNFIAAATMVTS----DQDDRGegpnvfLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGFALDTVM 274
Cdd:cd05926 158 SGTTGRPKGVPLTHRNLAASATNITNtyklTPDDRT------LVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 275 SAVQQHRVTHLFCVPPV-MIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFPDALICqGYGMTETCGIISLEy 353
Cdd:cd05926 232 PDVRDYNATWYTAVPTIhQILLNRPEPNPESPPPKLRFIRSCSASLPPAVLEALEATFGAPVLE-AYGMTEAAHQMTSN- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 354 PEKGQVRQFGSTGtLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQAT-EFTIRQGWLHTGDLGLFDDEG 432
Cdd:cd05926 310 PLPPGPRKPGSVG-KPVGVEVRILD-EDGEILPPGVVGEICLRGPNVTRGYLNNPEANaEAAFKDGWFRTGDLGYLDADG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 433 QLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQVTYYK 512
Cdd:cd05926 388 YLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHLAAFK 467
|
490 500
....*....|....*....|....
gi 357113996 513 RLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd05926 468 VPKKVYFVDELPKTATGKIQRRKV 491
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
34-536 |
1.77e-102 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 319.75 E-value: 1.77e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 34 AVDLLLRRAAACPSALALV-DAATGHA--LTFSGL--RSAILASAVAlssRAGVRPGDSVLLVAPNCVLYPVCFFAVTAL 108
Cdd:COG0365 11 AYNCLDRHAEGRGDKVALIwEGEDGEErtLTYAELrrEVNRFANALR---ALGVKKGDRVAIYLPNIPEAVIAMLACARI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 109 GAVASTANPLYTPREIAKQASDARARLVITVAE---------LLPKVADLR--LP----VILLDDTAAKSGSSATL-YSD 172
Cdd:COG0365 88 GAVHSPVFPGFGAEALADRIEDAEAKVLITADGglrggkvidLKEKVDEALeeLPslehVIVVGRTGADVPMEGDLdWDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 173 LVSGVDeADYRRPPTKQSDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVTS-----DQDDrgegpnVFLCFLPMFHIFG 247
Cdd:COG0365 168 LLAAAS-AEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKyvldlKPGD------VFWCTADIGWATG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 248 LSVITYGQLQRGNTVVVMSG----FALDTVMSAVQQHRVTHLFCVPPVMIALAKHG--KAGKYDLSSLKFIGSGAAPLGK 321
Cdd:COG0365 241 HSYIVYGPLLNGATVVLYEGrpdfPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGdePLKKYDLSSLRLLGSAGEPLNP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 322 DVMEAVAKNFpDALICQGYGMTETCGIISLEYPeKGQVRqFGSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPH-- 399
Cdd:COG0365 321 EVWEWWYEAV-GVPIVDGWGQTETGGIFISNLP-GLPVK-PGSMGKPVPGYDVAVVD-EDGNPVPPGEEGELVIKGPWpg 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 400 IMQGYFNNVQATE---FTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPD 476
Cdd:COG0365 397 MFRGYWNDPERYRetyFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPD 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357113996 477 AEAGEVPIAYVV----RSPDSSLTEvDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:COG0365 477 EIRGQVVKAFVVlkpgVEPSDELAK-ELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
60-536 |
1.16e-99 |
|
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: 308.25 E-value: 1.16e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 60 LTFSGLRSAILASAVALSsRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVITV 139
Cdd:cd05935 2 LTYLELLEVVKKLASFLS-NKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 140 AELlpkvadlrlpvillddtaaksgssatlysdlvsgvdeadyrrpptkqSDTAGLLYSSGTTGESKGVVLTHRNfiAAA 219
Cdd:cd05935 81 SEL-----------------------------------------------DDLALIPYTSGTTGLPKGCMHTHFS--AAA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 220 TMVTSDQDDRGEGPNVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGFALDTVMSAVQQHRVTHLFCVPPVMIALAKHG 299
Cdd:cd05935 112 NALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLATP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 300 KAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFPDALIcQGYGMTETCGIISLEyPEKGQVRQfgSTGTLVTGVEAKIVDV 379
Cdd:cd05935 192 EFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFV-EGYGLTETMSQTHTN-PPLRPKLQ--CLGIP*FGVDARVIDI 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 380 ETLKHLPPNQLGEICVRGPHIMQGYFNNVQATE--FTIRQG--WLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAE 455
Cdd:cd05935 268 ETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEesFIEIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 456 LEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPD--SSLTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILR 533
Cdd:cd05935 348 VEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEyrGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILW 427
|
...
gi 357113996 534 REL 536
Cdd:cd05935 428 RLL 430
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
57-536 |
2.61e-99 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 311.12 E-value: 2.61e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 57 GHALTFSGLRSAILASAVALSSRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLV 136
Cdd:PRK08314 33 GRAISYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 137 ITVAELLPKVA----DLRLP-VIL------LDDTA---------------AKSGSSATLYSDLVsgvdeADYRRPPTKQS 190
Cdd:PRK08314 113 IVGSELAPKVApavgNLRLRhVIVaqysdyLPAEPeiavpawlraepplqALAPGGVVAWKEAL-----AAGLAPPPHTA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 191 ---DTAGLLYSSGTTGESKGVVLTHR----NFIAAATMVTSDQDDrgegpnVFLCFLPMFHIFGLSVITYGQLQRGNTVV 263
Cdd:PRK08314 188 gpdDLAVLPYTSGTTGVPKGCMHTHRtvmaNAVGSVLWSNSTPES------VVLAVLPLFHVTGMVHSMNAPIYAGATVV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 264 VMSGFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGkdvmEAVAKNFPDAL---ICQGY 340
Cdd:PRK08314 262 LMPRWDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMP----EAVAERLKELTgldYVEGY 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 341 GMTETCGIISLEYPEKgQVRQfgSTGTLVTGVEAKIVDVETLKHLPPNQLGEICVRGPHIMQGYFNNVQATE--FTIRQG 418
Cdd:PRK08314 338 GLTETMAQTHSNPPDR-PKLQ--CLGIPTFGVDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAeaFIEIDG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 419 --WLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDS--S 494
Cdd:PRK08314 415 krFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEArgK 494
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 357113996 495 LTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:PRK08314 495 TTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1-535 |
1.91e-93 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 296.53 E-value: 1.91e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 1 MATAAVPSAGYGADGVYRSLRPaariesnPGLSAVDLLLRRAAACPSALALvdAATGHALTFSGLRSAILASAVALSsRA 80
Cdd:PRK05605 8 SAFADKPWLQSYAPWTPHDLDY-------GDTTLVDLYDNAVARFGDRPAL--DFFGATTTYAELGKQVRRAAAGLR-AL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 81 GVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVI---TVAELLPKVAD--------- 148
Cdd:PRK05605 78 GVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIvwdKVAPTVERLRRttpletivs 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 149 --------------LRLPVILLDDTAAKSGSSAT---LYSDLVSG-----VDEADYRRPptKQSDTAGLLYSSGTTGESK 206
Cdd:PRK05605 158 vnmiaampllqrlaLRLPIPALRKARAALTGPAPgtvPWETLVDAaiggdGSDVSHPRP--TPDDVALILYTSGTTGKPK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 207 GVVLTHRNFIAAATMVTSDQDDRGEGPNVFLCFLPMFHIFGLS-VITYGQLQRGnTVVVMSGFALDTVMSAVQQHRVTHL 285
Cdd:PRK05605 236 GAQLTHRNLFANAAQGKAWVPGLGDGPERVLAALPMFHAYGLTlCLTLAVSIGG-ELVLLPAPDIDLILDAMKKHPPTWL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 286 FCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKnFPDALICQGYGMTETCGIIsLEYPeKGQVRQFGST 365
Cdd:PRK05605 315 PGVPPLYEKIAEAAEERGVDLSGVRNAFSGAMALPVSTVELWEK-LTGGLLVEGYGLTETSPII-VGNP-MSDDRRPGYV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 366 GTLVTGVEAKIVDVETL-KHLPPNQLGEICVRGPHIMQGYFNNVQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELI 444
Cdd:PRK05605 392 GVPFPDTEVRIVDPEDPdETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELI 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 445 KYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQVTYYKRLKRVTFVSSVP 524
Cdd:PRK05605 472 ITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELP 551
|
570
....*....|.
gi 357113996 525 KSASGKILRRE 535
Cdd:PRK05605 552 RDQLGKVRRRE 562
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
38-536 |
1.60e-92 |
|
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: 292.61 E-value: 1.60e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 38 LLRRAAACPSALALV---DAATGHALTFSGLRSAILASAVALSsRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVAST 114
Cdd:cd12119 1 LLEHAARLHGDREIVsrtHEGEVHRYTYAEVAERARRLANALR-RLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 115 ANPLYTPREIAKQASDARARLVITVAELLPKVADL--RLP----VILLDDTAAKSGSSATL---YSDLVSGVDeADYRRP 185
Cdd:cd12119 80 INPRLFPEQIAYIINHAEDRVVFVDRDFLPLLEAIapRLPtvehVVVMTDDAAMPEPAGVGvlaYEELLAAES-PEYDWP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 186 PTKQSDTAGLLYSSGTTGESKGVVLTHRNfIAAATMVTSDQDDRGEGPN-VFLCFLPMFHI--FGLSvitYGQLQRGnTV 262
Cdd:cd12119 159 DFDENTAAAICYTSGTTGNPKGVVYSHRS-LVLHAMAALLTDGLGLSESdVVLPVVPMFHVnaWGLP---YAAAMVG-AK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 263 VVMSGFALD--TVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKF--IGSGAAPlgkdvmEAVAKNFPDALI-- 336
Cdd:cd12119 234 LVLPGPYLDpaSLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRvvIGGSAVP------RSLIEAFEERGVrv 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 337 CQGYGMTETCGIISLEYP--------EKGQVRQFGSTGTLVTGVEAKIVDVETlKHLP--PNQLGEICVRGPHIMQGYFN 406
Cdd:cd12119 308 IHAWGMTETSPLGTVARPpsehsnlsEDEQLALRAKQGRPVPGVELRIVDDDG-RELPwdGKAVGELQVRGPWVTKSYYK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 407 NVQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAY 486
Cdd:cd12119 387 NDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAV 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 357113996 487 VVRSPDSSLTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd12119 467 VVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
38-541 |
3.95e-92 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 290.33 E-value: 3.95e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 38 LLRRAAACPSALALVDAatGHALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANP 117
Cdd:PRK03640 8 LKQRAFLTPDRTAIEFE--EKKVTFMELHEAVVSVAGKLAAL-GVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 118 LYTPREIAKQASDARARLVITVAELLPKVadlrlpvillddtaakSGSSATLYSDLVSGVDEADYRRPPTKQSDTAGLLY 197
Cdd:PRK03640 85 RLSREELLWQLDDAEVKCLITDDDFEAKL----------------IPGISVKFAELMNGPKEEAEIQEEFDLDEVATIMY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 198 SSGTTGESKGVVLTHRNFIAAAtmVTS------DQDDRgegpnvFLCFLPMFHIFGLSvITYGQLQRGNTVVVMSGFALD 271
Cdd:PRK03640 149 TSGTTGKPKGVIQTYGNHWWSA--VGSalnlglTEDDC------WLAAVPIFHISGLS-ILMRSVIYGMRVVLVEKFDAE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 272 TVMSAVQQHRVThLFCVPPVMIA--LAKHGKAGkYDlSSLKFIGSGAAPLGKDVME-AVAKNFPdalICQGYGMTETCG- 347
Cdd:PRK03640 220 KINKLLQTGGVT-IISVVSTMLQrlLERLGEGT-YP-SSFRCMLLGGGPAPKPLLEqCKEKGIP---VYQSYGMTETASq 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 348 IISLeyPEKGQVRQFGSTGTLVTGVEAKIVDveTLKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTIRQGWLHTGDLGL 427
Cdd:PRK03640 294 IVTL--SPEDALTKLGSAGKPLFPCELKIEK--DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWFKTGDIGY 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 428 FDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRspDSSLTEVDVQKFIETQ 507
Cdd:PRK03640 370 LDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVTEEELRHFCEEK 447
|
490 500 510
....*....|....*....|....*....|....
gi 357113996 508 VTYYKRLKRVTFVSSVPKSASGKILRRELIAKVR 541
Cdd:PRK03640 448 LAKYKVPKRFYFVEELPRNASGKLLRHELKQLVE 481
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
33-536 |
1.56e-88 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 282.21 E-value: 1.56e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 33 SAVDLLLRRAAA-CPSALALVDAATghALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAV 111
Cdd:PRK08316 11 QTIGDILRRSARrYPDKTALVFGDR--SWTYAELDAAVNRVAAALLDL-GLKKGDRVAALGHNSDAYALLWLACARAGAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 112 ASTANPLYTPREIAKQASDARARLVITVAELLPkvadlrlpviLLDDTAAKSGSSATLYSDLVSGVD------------E 179
Cdd:PRK08316 88 HVPVNFMLTGEELAYILDHSGARAFLVDPALAP----------TAEAALALLPVDTLILSLVLGGREapggwldfadwaE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 180 ADYRRPPT---KQSDTAGLLYSSGTTGESKGVVLTHRNFIA--AATMVTSD--QDDrgegpnVFLCFLPMFHIFGLSVIT 252
Cdd:PRK08316 158 AGSVAEPDvelADDDLAQILYTSGTESLPKGAMLTHRALIAeyVSCIVAGDmsADD------IPLHALPLYHCAQLDVFL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 253 YGQLQRGNTVVVMSGFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFP 332
Cdd:PRK08316 232 GPYLYVGATNVILDAPDPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERLP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 333 DALICQGYGMTETCGIISLEYPEKgQVRQFGSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQATE 412
Cdd:PRK08316 312 GLRFYNCYGQTEIAPLATVLGPEE-HLRRPGSAGRPVLNVETRVVD-DDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 413 FTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPD 492
Cdd:PRK08316 390 EAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAG 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 357113996 493 SSLTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:PRK08316 470 ATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKREL 513
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
38-536 |
2.42e-88 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 282.44 E-value: 2.42e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 38 LLRRAAACPSALALvdAATGHALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANP 117
Cdd:PRK07786 23 LARHALMQPDAPAL--RFLGNTTTWRELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 118 LYTPREIAKQASDARARLVITVAELLPKVADLRLPVILLDDTAAKSGSSATLYSDLVSGVDEADYRRPPTK-QSDTAGL- 195
Cdd:PRK07786 100 RLTPPEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDiPNDSPALi 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 196 LYSSGTTGESKGVVLTHRNFIAAA-TMVTSDQDDRGEgpNVFLCFLPMFHIFGL-SVITYGQLQRGNTVVVMSGFALDTV 273
Cdd:PRK07786 180 MYTSGTTGRPKGAVLTHANLTGQAmTCLRTNGADINS--DVGFVGVPLFHIAGIgSMLPGLLLGAPTVIYPLGAFDPGQL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 274 MSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSsLKFIGSGAAPLGKDVMEAVAKNFPDALICQGYGMTE----TCGII 349
Cdd:PRK07786 258 LDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLA-LRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEmspvTCMLL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 350 SleypeKGQVRQFGSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTIRQGWLHTGDLGLFD 429
Cdd:PRK07786 337 G-----EDAIRKLGSVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQD 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 430 DEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYV-VRSPDSSLTEVDVQKFIETQV 508
Cdd:PRK07786 411 EEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAaVRNDDAALTLEDLAEFLTDRL 490
|
490 500
....*....|....*....|....*...
gi 357113996 509 TYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:PRK07786 491 ARYKHPKALEIVDALPRNPAGKVLKTEL 518
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
35-479 |
2.76e-88 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 283.91 E-value: 2.76e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 35 VDLLLRRAAACPSALALVDAATG--HALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVA 112
Cdd:COG1022 14 PDLLRRRAARFPDRVALREKEDGiwQSLTWAEFAERVRALAAGLLAL-GVKPGDRVAILSDNRPEWVIADLAILAAGAVT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 113 StanPLY---TPREIAKQASDARARLVITV-AELLPKVADLR--LP----VILLDDTAAKSGSSATLYSDL------VSG 176
Cdd:COG1022 93 V---PIYptsSAEEVAYILNDSGAKVLFVEdQEQLDKLLEVRdeLPslrhIVVLDPRGLRDDPRLLSLDELlalgreVAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 177 VDEADYRRPPTKQSDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVtSDQDDRGEGpNVFLCFLPMFHIFGlSVITYGQL 256
Cdd:COG1022 170 PAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARAL-LERLPLGPG-DRTLSFLPLAHVFE-RTVSYYAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 257 QRGNTVvvmsGFA--LDTVMSAVQQHRVTHLFCVPPV--------MIALAKHG---------------KAGKYDLSS--- 308
Cdd:COG1022 247 AAGATV----AFAesPDTLAEDLREVKPTFMLAVPRVwekvyagiQAKAEEAGglkrklfrwalavgrRYARARLAGksp 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 309 --------------------------LKFIGSGAAPLGKDVMEavaknFPDAL---ICQGYGMTETCGIISLEYPekGQV 359
Cdd:COG1022 323 slllrlkhaladklvfsklrealggrLRFAVSGGAALGPELAR-----FFRALgipVLEGYGLTETSPVITVNRP--GDN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 360 RqFGSTGTLVTGVEAKIVDVetlkhlppnqlGEICVRGPHIMQGYFNNVQATEFTIRQ-GWLHTGDLGLFDDEGQLFVVD 438
Cdd:COG1022 396 R-IGTVGPPLPGVEVKIAED-----------GEILVRGPNVMKGYYKNPEATAEAFDAdGWLHTGDIGELDEDGFLRITG 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 357113996 439 RLKELI-----KYkgfqIAPAELEGLLLSHPEILDAVVI----PF------PDAEA 479
Cdd:COG1022 464 RKKDLIvtsggKN----VAPQPIENALKASPLIEQAVVVgdgrPFlaalivPDFEA 515
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
81-538 |
5.53e-86 |
|
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: 271.91 E-value: 5.53e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 81 GVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARArlvitvaellpkvadlrlpvillddta 160
Cdd:cd05912 22 GVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDV--------------------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 161 aksgssatlysdlvsgvdeadyrrpptKQSDTAGLLYSSGTTGESKGVVLTHRNFIAAAtmVTS------DQDDRgegpn 234
Cdd:cd05912 75 ---------------------------KLDDIATIMYTSGTTGKPKGVQQTFGNHWWSA--IGSalnlglTEDDN----- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 235 vFLCFLPMFHIFGLSVITYGqLQRGNTVVVMSGFALDTVMSAVQQHRVTHLFCVPpVMIA--LAKHGkaGKYDlSSLKFI 312
Cdd:cd05912 121 -WLCALPLFHISGLSILMRS-VIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVP-TMLQrlLEILG--EGYP-NNLRCI 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 313 GSGAAPLGKDVME-AVAKNFPdalICQGYGMTETCGIISLEYPEKGQVRqFGSTGTLVTGVEAKIVDVETlkhlPPNQLG 391
Cdd:cd05912 195 LLGGGPAPKPLLEqCKEKGIP---VYQSYGMTETCSQIVTLSPEDALNK-IGSAGKPLFPVELKIEDDGQ----PPYEVG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 392 EICVRGPHIMQGYFNNVQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVV 471
Cdd:cd05912 267 EILLKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGV 346
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357113996 472 IPFPDAEAGEVPIAYVVRspDSSLTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRRELIA 538
Cdd:cd05912 347 VGIPDDKWGQVPVAFVVS--ERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
57-544 |
3.80e-84 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 271.91 E-value: 3.80e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 57 GHALTFSGLRSAILASAVALSsRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLV 136
Cdd:PRK06710 47 GKDITFSVFHDKVKRFANYLQ-KLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 137 ITVAELLPKVADL----RLPVILLDDTAAKSGSSATLY--------SDLVSGVDEAD---------------YRRPPTKQ 189
Cdd:PRK06710 126 LCLDLVFPRVTNVqsatKIEHVIVTRIADFLPFPKNLLypfvqkkqSNLVVKVSESEtihlwnsvekevntgVEVPCDPE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 190 SDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVTSDQDDRGEGPNVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGFA 269
Cdd:PRK06710 206 NDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFD 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 270 LDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFPDALIcQGYGMTETCGII 349
Cdd:PRK06710 286 MKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLV-EGYGLTESSPVT 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 350 SLEYPEKGQVRqfGSTGTLVTGVEAKIVDVETLKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTIRQGWLHTGDLGLFD 429
Cdd:PRK06710 365 HSNFLWEKRVP--GSIGVPWPDTEAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMD 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 430 DEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQVT 509
Cdd:PRK06710 443 EDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLA 522
|
490 500 510
....*....|....*....|....*....|....*
gi 357113996 510 YYKRLKRVTFVSSVPKSASGKILRRELIAKVRSSK 544
Cdd:PRK06710 523 AYKVPKVYEFRDELPKTTVGKILRRVLIEEEKRKN 557
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
61-537 |
3.13e-82 |
|
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: 262.61 E-value: 3.13e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 61 TFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVITva 140
Cdd:cd05934 5 TYAELLRESARIAAALAAL-GIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 141 ellpkvadlrlpvillddtaaksgssatlysdlvsgvdeadyrrpptkqsDTAGLLYSSGTTGESKGVVLTHRNFIAAAT 220
Cdd:cd05934 82 --------------------------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 221 mVTSDQDDRGEGpNVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGK 300
Cdd:cd05934 112 -YSARRFGLGED-DVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPP 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 301 AGKYDLSSLKFIGSGAAPlgKDVMEAVAKNFPDALIcQGYGMTETCGIISLEYPEKGQVrqfGSTGTLVTGVEAKIVDVE 380
Cdd:cd05934 190 SPDDRAHRLRAAYGAPNP--PELHEEFEERFGVRLL-EGYGMTETIVGVIGPRDEPRRP---GSIGRPAPGYEVRIVDDD 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 381 TlKHLPPNQLGEICVR---GPHIMQGYFNNVQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELE 457
Cdd:cd05934 264 G-QELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 458 GLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRRELI 537
Cdd:cd05934 343 RAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
40-543 |
4.45e-82 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 264.80 E-value: 4.45e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 40 RRAAACPSALALVdaATGHALTFSGLRSAILASAVALSSRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLY 119
Cdd:PRK06839 10 KRAYLHPDRIAII--TEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 120 TPREIAKQASDARARLVI------TVAELLPKVADLRLPVILLDdtaaKSGSSATLYSDLVSGVDEADYRrpptkqsdta 193
Cdd:PRK06839 88 TENELIFQLKDSGTTVLFvektfqNMALSMQKVSYVQRVISITS----LKEIEDRKIDNFVEKNESASFI---------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 194 gLLYSSGTTGESKGVVLTHRNFIAAATMVTSDQDDRGEgpNVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGFALDTV 273
Cdd:PRK06839 154 -ICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMH--DRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 274 MSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEA-VAKNFPdalICQGYGMTETCGIISLe 352
Cdd:PRK06839 231 LSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREfIDRGFL---FGQGFGMTETSPTVFM- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 353 YPEKGQVRQFGSTGTLVTGVEAKIVDVETlKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTIRQGWLHTGDLGLFDDEG 432
Cdd:PRK06839 307 LSEEDARRKVGSIGKPVLFCDYELIDENK-NKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 433 QLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQVTYYK 512
Cdd:PRK06839 386 FVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYK 465
|
490 500 510
....*....|....*....|....*....|.
gi 357113996 513 RLKRVTFVSSVPKSASGKILRRELIAKVRSS 543
Cdd:PRK06839 466 IPKEIVFLKELPKNATGKIQKAQLVNQLKSR 496
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
36-531 |
2.31e-81 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 264.37 E-value: 2.31e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 36 DLLLRRAAACPSALALVDAATGHALTFSGLRSAILASAVALSsRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTA 115
Cdd:PRK08315 20 QLLDRTAARYPDREALVYRDQGLRWTYREFNEEVDALAKGLL-ALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 116 NPLYTPREIA---KQaSDARArLVI-----------TVAELLPKVADL--------RLP----VILLDDTAaksgsSATL 169
Cdd:PRK08315 99 NPAYRLSELEyalNQ-SGCKA-LIAadgfkdsdyvaMLYELAPELATCepgqlqsaRLPelrrVIFLGDEK-----HPGM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 170 YS-----DLVSGVDEADY--RRPPTKQSDTAGLLYSSGTTGESKGVVLTHRN------FIAAATMVTsdQDDRgegpnvf 236
Cdd:PRK08315 172 LNfdellALGRAVDDAELaaRQATLDPDDPINIQYTSGTTGFPKGATLTHRNilnngyFIGEAMKLT--EEDR------- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 237 LCF-LPMFHIFGLSVITYGQLQRGNTVVVMS-GFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKF-IG 313
Cdd:PRK08315 243 LCIpVPLYHCFGMVLGNLACVTHGATMVYPGeGFDPLATLAAVEEERCTALYGVPTMFIAELDHPDFARFDLSSLRTgIM 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 314 SGAaPLGKDVMEAVAK--NFPDALICqgYGMTETCGII-------SLEypekgqvRQFGSTGTLVTGVEAKIVDVETLKH 384
Cdd:PRK08315 323 AGS-PCPIEVMKRVIDkmHMSEVTIA--YGMTETSPVStqtrtddPLE-------KRVTTVGRALPHLEVKIVDPETGET 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 385 LPPNQLGEICVRGPHIMQGYFNNVQATEFTI-RQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSH 463
Cdd:PRK08315 393 VPRGEQGELCTRGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTH 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 357113996 464 PEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKI 531
Cdd:PRK08315 473 PKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKI 540
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
57-538 |
1.59e-80 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 262.67 E-value: 1.59e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 57 GHALTFSGL--RSAILAsavALSSRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARAR 134
Cdd:PRK06178 56 GHVITYAELdeLSDRFA---ALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 135 LVITVAELLPKVADLR-------------------LPVILLDDTAAKSGSSATLYSDLVSGVDE--ADYRRPPTKQSDTA 193
Cdd:PRK06178 133 VLLALDQLAPVVEQVRaetslrhvivtsladvlpaEPTLPLPDSLRAPRLAAAGAIDLLPALRActAPVPLPPPALDALA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 194 GLLYSSGTTGESKGVVLTHRNFI---AAATMVTSdqddRGEGPNVFLCFLPMFHI----FGLSVITYGqlqrGNTVVVMS 266
Cdd:PRK06178 213 ALNYTGGTTGMPKGCEHTQRDMVytaAAAYAVAV----VGGEDSVFLSFLPEFWIagenFGLLFPLFS----GATLVLLA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 267 GFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGsgaaplgkdVMEAVAKNFPD-----------AL 335
Cdd:PRK06178 285 RWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQVR---------VVSFVKKLNPDyrqrwraltgsVL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 336 ICQGYGMTET-------CGIISLEYPEKGQvRQFgsTGTLVTGVEAKIVDVETLKHLPPNQLGEICVRGPHIMQGYFNNV 408
Cdd:PRK06178 356 AEAAWGMTEThtcdtftAGFQDDDFDLLSQ-PVF--VGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKP 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 409 QATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVV 488
Cdd:PRK06178 433 EATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQ 512
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 357113996 489 RSPDSSLTEVDVQKFIETQVTYYKrLKRVTFVSSVPKSASGKILRRELIA 538
Cdd:PRK06178 513 LKPGADLTAAALQAWCRENMAVYK-VPEIRIVDALPMTATGKVRKQDLQA 561
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
36-531 |
8.73e-80 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 260.48 E-value: 8.73e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 36 DLLLRRAAACPSALALVDAATGHALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTA 115
Cdd:PRK12583 22 DAFDATVARFPDREALVVRHQALRYTWRQLADAVDRLARGLLAL-GVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 116 NPLYTPREIAKQASDARARLVITVA------------ELLPKVADL--------RLP----VILLDDTAAKSgssATLYS 171
Cdd:PRK12583 101 NPAYRASELEYALGQSGVRWVICADafktsdyhamlqELLPGLAEGqpgalaceRLPelrgVVSLAPAPPPG---FLAWH 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 172 DLVS---GVDEADY--RRPPTKQSDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVTSD----QDDRgegpnvfLCF-LP 241
Cdd:PRK12583 178 ELQArgeTVSREALaeRQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESlgltEHDR-------LCVpVP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 242 MFHIFGLSVITYGQLQRGNTVVVMS-GFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLG 320
Cdd:PRK12583 251 LYHCFGMVLANLGCMTVGACLVYPNeAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 321 KDVMEAVAK--NFPDALIcqGYGMTETCGIISLEYPEKGQVRQFGSTGTLVTGVEAKIVDVETlKHLPPNQLGEICVRGP 398
Cdd:PRK12583 331 IEVMRRVMDemHMAEVQI--AYGMTETSPVSLQTTAADDLERRVETVGRTQPHLEVKVVDPDG-ATVPRGEIGELCTRGY 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 399 HIMQGYFNNVQATEFTI-RQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDA 477
Cdd:PRK12583 408 SVMKGYWNNPEATAESIdEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDE 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 357113996 478 EAGEVPIAYVVRSPDSSLTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKI 531
Cdd:PRK12583 488 KYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKV 541
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
17-540 |
1.27e-78 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 259.12 E-value: 1.27e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 17 YRSLRPAARIESNPgLSAVDL------LLRRAAAC-PSALALV------DAATGHALTFSGLRSAILASAVALSSRaGVR 83
Cdd:PRK07529 4 FATLADIEAIEAVP-LAARDLpastyeLLSRAAARhPDAPALSflldadPLDRPETWTYAELLADVTRTANLLHSL-GVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 84 PGDSVLLVAPNCvlyPVCFFAVTAlGAVASTA---NPLYTPREIAKQASDARARLVIT------------VAELLPKVAD 148
Cdd:PRK07529 82 PGDVVAFLLPNL---PETHFALWG-GEAAGIAnpiNPLLEPEQIAELLRAAGAKVLVTlgpfpgtdiwqkVAEVLAALPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 149 LR--LPVILLDDTAAKSGSSATL-----------YSDLVSG--VDEADYRRPPTkQSDTAGLLYSSGTTGESKGVVLTHR 213
Cdd:PRK07529 158 LRtvVEVDLARYLPGPKRLAVPLirrkaharildFDAELARqpGDRLFSGRPIG-PDDVAAYFHTGGTTGMPKLAQHTHG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 214 NFIAAATMVTSdQDDRGEGPNVFlCFLPMFHIFGLSVITYGQLQRGNTVVVMS--GFALDTVM----SAVQQHRVTHLFC 287
Cdd:PRK07529 237 NEVANAWLGAL-LLGLGPGDTVF-CGLPLFHVNALLVTGLAPLARGAHVVLATpqGYRGPGVIanfwKIVERYRINFLSG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 288 VPPVMIALAKHgKAGKYDLSSLKFIGSGAAPLGkdvmEAVAKNFPDAL---ICQGYGMTETCGIISLEYPEkgQVRQFGS 364
Cdd:PRK07529 315 VPTVYAALLQV-PVDGHDISSLRYALCGAAPLP----VEVFRRFEAATgvrIVEGYGLTEATCVSSVNPPD--GERRIGS 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 365 TGTLVTGVEAKIVDVE----TLKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRL 440
Cdd:PRK07529 388 VGLRLPYQRVRVVILDdagrYLRDCAVDEVGVLCIAGPNVFSGYLEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRA 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 441 KELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQVTyyKRL---KRV 517
Cdd:PRK07529 468 KDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAELLAFARDHIA--ERAavpKHV 545
|
570 580
....*....|....*....|....*..
gi 357113996 518 TFVSSVPKSASGKI----LRRELIAKV 540
Cdd:PRK07529 546 RILDALPKTAVGKIfkpaLRRDAIRRV 572
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
57-536 |
7.90e-78 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 255.36 E-value: 7.90e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 57 GHALTFSGLRSAILASAVALSSRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLV 136
Cdd:PRK08974 46 GEVMTFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 137 ITV---AELLPKVADlRLP---VILL---DDTAAKSGS-------------------SATLYSDLVSGVDEADYRRPPTK 188
Cdd:PRK08974 126 VIVsnfAHTLEKVVF-KTPvkhVILTrmgDQLSTAKGTlvnfvvkyikrlvpkyhlpDAISFRSALHKGRRMQYVKPELV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 189 QSDTAGLLYSSGTTGESKGVVLTHRNFIA--------AATMVTsdqddrgEGPNVFLCFLPMFHIFGLSV-----ITYGq 255
Cdd:PRK08974 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLAnleqakaaYGPLLH-------PGKELVVTALPLYHIFALTVncllfIELG- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 256 lqrGNTVVVMSGFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKF-IGSGAAplgkdVMEAVAKNFPDA 334
Cdd:PRK08974 277 ---GQNLLITNPRDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLsVGGGMA-----VQQAVAERWVKL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 335 LIC---QGYGMTE-----TCGIISLEYPEkgqvrqfGSTGTLVTGVEAKIVDVETlKHLPPNQLGEICVRGPHIMQGYFN 406
Cdd:PRK08974 349 TGQyllEGYGLTEcsplvSVNPYDLDYYS-------GSIGLPVPSTEIKLVDDDG-NEVPPGEPGELWVKGPQVMLGYWQ 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 407 NVQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAY 486
Cdd:PRK08974 421 RPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIF 500
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 357113996 487 VVRSpDSSLTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:PRK08974 501 VVKK-DPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
197-536 |
5.62e-77 |
|
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: 246.42 E-value: 5.62e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 197 YSSGTTGESKGVVLTHRNFIAAATMVTSDQDDRgegPNVFLCF-LPMFHIFGLSVITYGQLQRGNTVV-VMSGFALDTVM 274
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLT---EQDRLCIpVPLFHCFGSVLGVLACLTHGATMVfPSPSFDPLAVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 275 SAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAK--NFPDALICqgYGMTETCGIISLE 352
Cdd:cd05917 86 EAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEvmNMKDVTIA--YGMTETSPVSTQT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 353 YPEKGQVRQFGSTGTLVTGVEAKIVDVETLKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTI-RQGWLHTGDLGLFDDE 431
Cdd:cd05917 164 RTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIdGDGWLHTGDLAVMDED 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 432 GQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQVTYY 511
Cdd:cd05917 244 GYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKAYCKGKIAHY 323
|
330 340
....*....|....*....|....*
gi 357113996 512 KRLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd05917 324 KVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
61-536 |
4.94e-76 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 246.98 E-value: 4.94e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 61 TFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVITVA 140
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQ-GIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 141 ELLPKVADlrlpVILLDDTAAKSGSSATLYSDLvsgvdeadyrrpptKQSDTAGLLYSSGTTGESKGVVLTHRNFIAAAT 220
Cdd:TIGR01923 80 LLEEKDFQ----ADSLDRIEAAGRYETSLSASF--------------NMDQIATLMFTSGTTGKPKAVPHTFRNHYASAV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 221 MVTS----DQDDRgegpnvFLCFLPMFHIFGLSVItYGQLQRGNTVVVMSGFAldTVMSAVQQHRVTHLFCVPPVMIALA 296
Cdd:TIGR01923 142 GSKEnlgfTEDDN------WLLSLPLYHISGLSIL-FRWLIEGATLRIVDKFN--QLLEMIANERVTHISLVPTQLNRLL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 297 KHGkAGKYDLSSLKFIGSGA-APLGKdvmEAVAKNFPdalICQGYGMTETCGIISLEYPEKGQVRqfGSTGTLVTGVEAK 375
Cdd:TIGR01923 213 DEG-GHNENLRKILLGGSAIpAPLIE---EAQQYGLP---IYLSYGMTETCSQVTTATPEMLHAR--PDVGRPLAGREIK 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 376 IVDVETLKHlppnqlGEICVRGPHIMQGYFNNVQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAE 455
Cdd:TIGR01923 284 IKVDNKEGH------GEIMVKGANLMKGYLYQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 456 LEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDvqKFIETQVTYYKRLKRVTFVSSVPKSASGKILRRE 535
Cdd:TIGR01923 358 IETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESDISQAKLI--AYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQ 435
|
.
gi 357113996 536 L 536
Cdd:TIGR01923 436 L 436
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
22-536 |
7.69e-75 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 247.37 E-value: 7.69e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 22 PAARIESNPGLSAVDLL---LRRAAACPSALALvdaatGHALTFSGLRSAILASAVALSSRAGVRPGDSVLLVAPNCVLY 98
Cdd:PRK05677 14 IAAEINPDEYPNIQAVLkqsCQRFADKPAFSNL-----GKTLTYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 99 PVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVITVA-------ELLPK----------VADLrLPVI--LLDDT 159
Cdd:PRK05677 89 PVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLAnmahlaeKVLPKtgvkhvivteVADM-LPPLkrLLINA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 160 AAK---------SGSSATLYSDLVSGVDEADYRRPPTKQSDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVTSDQDDR- 229
Cdd:PRK05677 168 VVKhvkkmvpayHLPQAVKFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNl 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 230 GEGPNVFLCFLPMFHIFGLSVITYGQLQRGN-TVVVMSGFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSS 308
Cdd:PRK05677 248 NEGCEILIAPLPLYHIYAFTFHCMAMMLIGNhNILISNPRDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDFSA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 309 LKFIGSGAAPLGKDVMEAvAKNFPDALICQGYGMTETCGIISLEYPEKGQVrqfGSTGTLVTGVEAKIVDVETlKHLPPN 388
Cdd:PRK05677 328 LKLTLSGGMALQLATAER-WKEVTGCAICEGYGMTETSPVVSVNPSQAIQV---GTIGIPVPSTLCKVIDDDG-NELPLG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 389 QLGEICVRGPHIMQGYFNNVQATEFTI-RQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEIL 467
Cdd:PRK05677 403 EVGELCVKGPQVMKGYWQRPEATDEILdSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVL 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 357113996 468 DAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:PRK05677 483 QCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
24-536 |
1.14e-74 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 246.86 E-value: 1.14e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 24 ARIESNPGLSAVDLLL--------RRAAACpsalalvdaaTGHALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNC 95
Cdd:PRK07059 15 AEIDASQYPSLADLLEesfrqyadRPAFIC----------MGKAITYGELDELSRALAAWLQSR-GLAKGARVAIMMPNV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 96 VLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVI-------TVAELLPKVADLRLPVILLDD---------- 158
Cdd:PRK07059 84 LQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVvlenfatTVQQVLAKTAVKHVVVASMGDllgfkghivn 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 159 ---------TAAKSGSSATLYSDLVSGVDEADYRRPPTKQSDTAGLLYSSGTTGESKGVVLTHRNFIAaaTMVTSD---Q 226
Cdd:PRK07059 164 fvvrrvkkmVPAWSLPGHVRFNDALAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVA--NVLQMEawlQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 227 DDRGEGPNV----FLCFLPMFHIFGLSVITYGQLQRGNTVVV------MSGFaldtvMSAVQQHRVTHLFCVPPVMIALA 296
Cdd:PRK07059 242 PAFEKKPRPdqlnFVCALPLYHIFALTVCGLLGMRTGGRNILipnprdIPGF-----IKELKKYQVHIFPAVNTLYNALL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 297 KHGKAGKYDLSSLKF-IGSGAAplgkdVMEAVAKNFPD---ALICQGYGMTETCGIISLEypeKGQVRQF-GSTGTLVTG 371
Cdd:PRK07059 317 NNPDFDKLDFSKLIVaNGGGMA-----VQRPVAERWLEmtgCPITEGYGLSETSPVATCN---PVDATEFsGTIGLPLPS 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 372 VEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTI-RQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQ 450
Cdd:PRK07059 389 TEVSIRD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMtADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFN 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 451 IAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSpDSSLTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGK 530
Cdd:PRK07059 468 VYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKK-DPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGK 546
|
....*.
gi 357113996 531 ILRREL 536
Cdd:PRK07059 547 ILRREL 552
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
38-539 |
1.24e-74 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 246.11 E-value: 1.24e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 38 LLRRAAA-CPSALALVDAAtgHALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTAN 116
Cdd:PRK07470 12 FLRQAARrFPDRIALVWGD--RSWTWREIDARVDALAAALAAR-GVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 117 PLYTPREIAKQASDARARLVITVAELLPKVADLRLPVILLDDTAAKSGSSATL-YSDLVSGVDEADYRRPPTKQSDTAGL 195
Cdd:PRK07470 89 FRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTHVVAIGGARAGLdYEALVARHLGARVANAAVDHDDPCWF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 196 LYSSGTTGESKGVVLTH-------RNFIAAATMVTSDQDdrgegpnVFLCFLPMFHIFGLSVITygQLQRGNTVVVMSG- 267
Cdd:PRK07470 169 FFTSGTTGRPKAAVLTHgqmafviTNHLADLMPGTTEQD-------ASLVVAPLSHGAGIHQLC--QVARGAATVLLPSe 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 268 -FALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGK-DVMEAVAKNFPdaLICQGYGMTET 345
Cdd:PRK07470 240 rFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRaDQKRALAKLGK--VLVQYFGLGEV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 346 CGIIS-----LEYPEKGQVRQFGSTGTLVTGVEAKIVDVEtLKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTIRQGWL 420
Cdd:PRK07470 318 TGNITvlppaLHDAEDGPDARIGTCGFERTGMEVQIQDDE-GRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 421 HTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDV 500
Cdd:PRK07470 397 RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAEL 476
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 357113996 501 QKFIETQVTYYKRLKRVTFVSSVPKSASGKI----LRRELIAK 539
Cdd:PRK07470 477 LAWLDGKVARYKLPKRFFFWDALPKSGYGKItkkmVREELEER 519
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
36-536 |
1.62e-74 |
|
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: 245.83 E-value: 1.62e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 36 DLLLRRAAACPSALALVDAatGHALTFSGLRSAILASAVALSsRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTA 115
Cdd:COG1021 29 DLLRRRAERHPDRIAVVDG--ERRLSYAELDRRADRLAAGLL-ALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVFA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 116 NPLYTPREIAKQASDARARLVIT------------VAELLPKVADLRLpVILLDDTAaksgsSATLYSDLVSgvDEADYR 183
Cdd:COG1021 106 LPAHRRAEISHFAEQSEAVAYIIpdrhrgfdyralARELQAEVPSLRH-VLVVGDAG-----EFTSLDALLA--APADLS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 184 RPPTKQSDTAGLLYSSGTTGESKGVVLTHR----NFIAAATMVTSDQDDrgegpnVFLCFLPMFHIFGLSVITY-GQLQR 258
Cdd:COG1021 178 EPRPDPDDVAFFQLSGGTTGLPKLIPRTHDdylySVRASAEICGLDADT------VYLAALPAAHNFPLSSPGVlGVLYA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 259 GNTVVVMSGFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGkdvmEAVAKNFPDALIC- 337
Cdd:COG1021 252 GGTVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLS----PELARRVRPALGCt 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 338 --QGYGMTEtcGIIS---LEYPEKgqvRQFGSTGT-LVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQ-- 409
Cdd:COG1021 328 lqQVFGMAE--GLVNytrLDDPEE---VILTTQGRpISPDDEVRIVD-EDGNPVPPGEVGELLTRGPYTIRGYYRAPEhn 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 410 ATEFTiRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVr 489
Cdd:COG1021 402 ARAFT-PDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVV- 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 357113996 490 SPDSSLTEVDVQKFIETQ-VTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:COG1021 480 PRGEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
36-539 |
1.97e-73 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 242.58 E-value: 1.97e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 36 DLLLRRAAACPSALALVDaaTGHALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTA 115
Cdd:PRK06188 16 HLLVSALKRYPDRPALVL--GDTRLTYGQLADRISRYIQAFEAL-GLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 116 NPLYTPREIAKQASDARARLVIT--------VAELLPKVADLRlPVILLDDTAAKSgssatlysDLVSGVDEADYR--RP 185
Cdd:PRK06188 93 HPLGSLDDHAYVLEDAGISTLIVdpapfverALALLARVPSLK-HVLTLGPVPDGV--------DLLAAAAKFGPAplVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 186 PTKQSDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVTSD----QDDRgegpnvFLCFLPMFHIFGLSVITygQLQRGNT 261
Cdd:PRK06188 164 AALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEwewpADPR------FLMCTPLSHAGGAFFLP--TLLRGGT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 262 VVVMSGFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKD-VMEAVAKNFPdaLICQGY 340
Cdd:PRK06188 236 VIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVrLAEAIERFGP--IFAQYY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 341 GMTETCGIISLEYPE---KGQVRQFGSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTIRQ 417
Cdd:PRK06188 314 GQTEAPMVITYLRKRdhdPDDPKRLTSCGRPTPGLRVALLD-EDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 418 GWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTE 497
Cdd:PRK06188 393 GWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDA 472
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 357113996 498 VDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRRELIAK 539
Cdd:PRK06188 473 AELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRAR 514
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
48-538 |
3.03e-71 |
|
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: 234.49 E-value: 3.03e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 48 ALALVDAatGHALTFSGLRSAILASAVALSSRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQ 127
Cdd:cd05941 2 RIAIVDD--GDSITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 128 ASDARARLVItvaellpkvadlrlpvillddtaaksgssatlysdlvsgvdeadyrrpptkqsDTAGLLYSSGTTGESKG 207
Cdd:cd05941 80 ITDSEPSLVL-----------------------------------------------------DPALILYTSGTTGRPKG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 208 VVLTHRNFIAAATMVTSD----QDDrgegpnVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGFALDTVMSAVQQHRVT 283
Cdd:cd05941 107 VVLTHANLAANVRALVDAwrwtEDD------VLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRLMPSIT 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 284 HLFCVPPVMIALAK--------HGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFPDALIcQGYGMTETcgIISLEYPE 355
Cdd:cd05941 181 VFMGVPTIYTRLLQyyeahftdPQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLL-ERYGMTEI--GMALSNPL 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 356 KGQvRQFGSTGTLVTGVEAKIVDVETLKHLPPNQLGEICVRGPHIMQGYFNNVQAT--EFTiRQGWLHTGDLGLFDDEGQ 433
Cdd:cd05941 258 DGE-RRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATkeEFT-DDGWFKTGDLGVVDEDGY 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 434 LFVVDRLK-ELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDS-SLTEVDVQKFIETQVTYY 511
Cdd:cd05941 336 YWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAaALSLEELKEWAKQRLAPY 415
|
490 500
....*....|....*....|....*..
gi 357113996 512 KRLKRVTFVSSVPKSASGKILRRELIA 538
Cdd:cd05941 416 KRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
37-536 |
2.86e-70 |
|
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: 233.35 E-value: 2.86e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 37 LLLRRAAAC-PSALALVDAATGHALTFSGLRSAILASAVAlssRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTA 115
Cdd:cd12118 8 SFLERAAAVyPDRTSIVYGDRRYTWRQTYDRCRRLASALA---ALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 116 NPLYTPREIAKQASDARARLVITVAELLpkvadlrlpvillddtaaksgssatlYSDLVSGVDEADYRRPPTKQSDTAGL 195
Cdd:cd12118 85 NTRLDAEEIAFILRHSEAKVLFVDREFE--------------------------YEDLLAEGDPDFEWIPPADEWDPIAL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 196 LYSSGTTGESKGVVLTHRN-FIAA-ATMVTSDQDDRGegpnVFLCFLPMFHIFGLSvITYGQLQRGNTVVVMSGFALDTV 273
Cdd:cd12118 139 NYTSGTTGRPKGVVYHHRGaYLNAlANILEWEMKQHP----VYLWTLPMFHCNGWC-FPWTVAAVGGTNVCLRKVDAKAI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 274 MSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAV-AKNFPdalICQGYGMTETCGIISL- 351
Cdd:cd12118 214 YDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMeELGFD---VTHVYGLTETYGPATVc 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 352 -------EYPEKGQVRQFGSTGTLVTGVEA-KIVDVETLKHLPPN--QLGEICVRGPHIMQGYFNNVQATEFTIRQGWLH 421
Cdd:cd12118 291 awkpewdELPTEERARLKARQGVRYVGLEEvDVLDPETMKPVPRDgkTIGEIVFRGNIVMKGYLKNPEATAEAFRGGWFH 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 422 TGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQ 501
Cdd:cd12118 371 SGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEEEII 450
|
490 500 510
....*....|....*....|....*....|....*
gi 357113996 502 KFIETQVTYYKRLKRVTFvSSVPKSASGKILRREL 536
Cdd:cd12118 451 AFCREHLAGFMVPKTVVF-GELPKTSTGKIQKFVL 484
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
191-533 |
3.38e-70 |
|
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: 228.15 E-value: 3.38e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 191 DTAGLLYSSGTTGESKGVVLTHRNFIAAATM------VTSDqdDRgegpnvFLCFLPMFHIFGLSVITYGQLQRGNTVVV 264
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAwadcadLTED--DR------YLIINPFFHTFGYKAGIVACLLTGATVVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 265 MSGFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFPDALICQGYGMTE 344
Cdd:cd17638 73 VAVFDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 345 tCGIISLEYPEKGQVRQFGSTGTLVTGVEAKIVDVetlkhlppnqlGEICVRGPHIMQGYFNNVQATEFTI-RQGWLHTG 423
Cdd:cd17638 153 -AGVATMCRPGDDAETVATTCGRACPGFEVRIADD-----------GEVLVRGYNVMQGYLDDPEATAEAIdADGWLHTG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 424 DLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKF 503
Cdd:cd17638 221 DVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAW 300
|
330 340 350
....*....|....*....|....*....|
gi 357113996 504 IETQVTYYKRLKRVTFVSSVPKSASGKILR 533
Cdd:cd17638 301 CRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
195-533 |
4.06e-70 |
|
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: 228.31 E-value: 4.06e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 195 LLYSSGTTGESKGVVLTHRNFIAA-----ATMVTSDQDdrgegpnVFLCFLPMFHIFGLSvITYGQLQRGNTVVVMSGFA 269
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAAnlqliHAMGLTEAD-------VYLNMLPLFHIAGLN-LALATFHAGGANVVMEKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 270 LDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPlgkDVMEAVAKNFPDALICqGYGMTETCGII 349
Cdd:cd17637 77 PAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVLGLDAP---ETIQRFEETTGATFWS-LYGQTETSGLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 350 SL-EYPEKGqvrqfGSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTIRQGWLHTGDLGLF 428
Cdd:cd17637 153 TLsPYRERP-----GSAGRPGPLVRVRIVD-DNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 429 DDEGQLFVVDRL--KELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIET 506
Cdd:cd17637 227 DEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFVGS 306
|
330 340
....*....|....*....|....*..
gi 357113996 507 QVTYYKRLKRVTFVSSVPKSASGKILR 533
Cdd:cd17637 307 RIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
58-508 |
4.14e-70 |
|
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: 231.72 E-value: 4.14e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 58 HALTFSGLRSAILASAVALSSrAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVI 137
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIA-LGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 138 tvaellpkvadlrlpvillddtaaksgssatlysdlvsgVDEADyrrpptkqsDTAGLLYSSGTTGESKGVVLTHRNF-- 215
Cdd:cd05907 83 ---------------------------------------VEDPD---------DLATIIYTSGTTGRPKGVMLSHRNIls 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 216 --IAAATMVTSDQDDRgegpnvFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGfaLDTVMSAVQQHRVTHLFCVPPV-- 291
Cdd:cd05907 115 naLALAERLPATEGDR------HLSFLPLAHVFERRAGLYVPLLAGARIYFASS--AETLLDDLSEVRPTVFLAVPRVwe 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 292 -MIALAKHGKAGKYD--------LSSLKFIGSGAAPLGKDVMEAVAK-NFPdalICQGYGMTETCGIISLEYPEKgqvRQ 361
Cdd:cd05907 187 kVYAAIKVKAVPGLKrklfdlavGGRLRFAASGGAPLPAELLHFFRAlGIP---VYEGYGLTETSAVVTLNPPGD---NR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 362 FGSTGTLVTGVEAKIVDVetlkhlppnqlGEICVRGPHIMQGYFNNVQAT-EFTIRQGWLHTGDLGLFDDEGQLFVVDRL 440
Cdd:cd05907 261 IGTVGKPLPGVEVRIADD-----------GEILVRGPNVMLGYYKNPEATaEALDADGWLHTGDLGEIDEDGFLHITGRK 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 441 KELIKY-KGFQIAPAELEGLLLSHPEILDAVVI----PF------PDAE-----AGEVPIAYvvRSPDSSLTEVDVQKFI 504
Cdd:cd05907 330 KDLIITsGGKNISPEPIENALKASPLISQAVVIgdgrPFlvalivPDPEaleawAEEHGIAY--TDVAELAANPAVRAEI 407
|
....
gi 357113996 505 ETQV 508
Cdd:cd05907 408 EAAV 411
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
57-536 |
3.73e-66 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 224.32 E-value: 3.73e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 57 GHALTFSGLRSAILASAVALSSRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLV 136
Cdd:PRK12492 47 GVTLSYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARAL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 137 I-------TVAELLPKVADLRLPVILLDD--TAAKsgssATLYSDLVSGVDE--ADYRRP------------------PT 187
Cdd:PRK12492 127 VylnmfgkLVQEVLPDTGIEYLIEAKMGDllPAAK----GWLVNTVVDKVKKmvPAYHLPqavpfkqalrqgrglslkPV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 188 KQS--DTAGLLYSSGTTGESKGVVLTHRNFIAAATMV---TSDQDDRG-----EGPNVFLCFLPMFHIFGLSVITYGQLQ 257
Cdd:PRK12492 203 PVGldDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVracLSQLGPDGqplmkEGQEVMIAPLPLYHIYAFTANCMCMMV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 258 RGNTVVVMS------GFaldtvMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKnF 331
Cdd:PRK12492 283 SGNHNVLITnprdipGF-----IKELGKWRFSALLGLNTLFVALMDHPGFKDLDFSALKLTNSGGTALVKATAERWEQ-L 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 332 PDALICQGYGMTETCGIISLEypEKGQVRQFGSTGTLVTGVEAKIVDVETLKhLPPNQLGEICVRGPHIMQGYFNNVQAT 411
Cdd:PRK12492 357 TGCTIVEGYGLTETSPVASTN--PYGELARLGTVGIPVPGTALKVIDDDGNE-LPLGERGELCIKGPQVMKGYWQQPEAT 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 412 EFTI-RQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRS 490
Cdd:PRK12492 434 AEALdAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVAR 513
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 357113996 491 pDSSLTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:PRK12492 514 -DPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
32-544 |
6.55e-66 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 223.29 E-value: 6.55e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 32 LSAVDLLLRRAAACPSALALVDAATGHALTFSGLRSAILASAVAlssRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAV 111
Cdd:PRK08162 18 LTPLSFLERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALA---RRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 112 ASTANPLYTPREIAKQASDARARLVIT-------VAELLPKVADLRLPVILLDDTAAKSGS--SATLYSDLVSGVDEADY 182
Cdd:PRK08162 95 LNTLNTRLDAASIAFMLRHGEAKVLIVdtefaevAREALALLPGPKPLVIDVDDPEYPGGRfiGALDYEAFLASGDPDFA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 183 RRPPTKQSDTAGLLYSSGTTGESKGVVLTHRnfiAAATMVTSDQDDRGEGPN-VFLCFLPMFHIFGLSvITYGQLQRGNT 261
Cdd:PRK08162 175 WTLPADEWDAIALNYTSGTTGNPKGVVYHHR---GAYLNALSNILAWGMPKHpVYLWTLPMFHCNGWC-FPWTVAARAGT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 262 VVVMSGFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLS-SLKFIGSGAAPLGKdVMEAVAKNFPDalICQGY 340
Cdd:PRK08162 251 NVCLRKVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDhPVHAMVAGAAPPAA-VIAKMEEIGFD--LTHVY 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 341 GMTETCGIISL--------EYPEKGQVRQFGSTGT---LVTGVeaKIVDVETLKHLPPN--QLGEICVRGPHIMQGYFNN 407
Cdd:PRK08162 328 GLTETYGPATVcawqpewdALPLDERAQLKARQGVrypLQEGV--TVLDPDTMQPVPADgeTIGEIMFRGNIVMKGYLKN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 408 VQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYV 487
Cdd:PRK08162 406 PKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFV 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 357113996 488 VRSPDSSLTEVDVQKFIETQVTYYKRLKRVTFvSSVPKSASGKILRRELIAKVRSSK 544
Cdd:PRK08162 486 ELKDGASATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQAKSLK 541
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
35-536 |
8.15e-66 |
|
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: 221.61 E-value: 8.15e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 35 VDLLLRRAA-ACPSALALVDAATGHALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVAS 113
Cdd:cd05923 3 VFEMLRRAAsRAPDACAIADPARGLRLTYSELRARIEAVAARLHAR-GLRPGQRVAVVLPNSVEAVIALLALHRLGAVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 114 TANPLYTPREIAK--QASDARARLVITVAELLPKVADLRLPVILLDDTAAKSgsSATLYSDLVSGvdeadyrrPPTKQSD 191
Cdd:cd05923 82 LINPRLKAAELAEliERGEMTAAVIAVDAQVMDAIFQSGVRVLALSDLVGLG--EPESAGPLIED--------PPREPEQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 192 TAGLLYSSGTTGESKGVVLTHRNFIA-AATMVTSDQDDRGEGpNVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGFAL 270
Cdd:cd05923 152 PAFVFYTSGTTGLPKGAVIPQRAAESrVLFMSTQAGLRHGRH-NVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 271 DTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFPdALICQGYGMTETCGIIS 350
Cdd:cd05923 231 ADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLP-GEKVNIYGTTEAMNSLY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 351 LEYPEKGQVRQFGSTGtlvtgvEAKIVDV--ETLKHLPPNQLGEICVR--GPHIMQGYFNNVQATEFTIRQGWLHTGDLG 426
Cdd:cd05923 310 MRDARTGTEMRPGFFS------EVRIVRIggSPDEALANGEEGELIVAaaADAAFTGYLNQPEATAKKLQDGWYRTGDVG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 427 LFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPdSSLTEVDVQKF-IE 505
Cdd:cd05923 384 YVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPRE-GTLSADELDQFcRA 462
|
490 500 510
....*....|....*....|....*....|.
gi 357113996 506 TQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd05923 463 SELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
59-536 |
3.52e-65 |
|
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: 218.40 E-value: 3.52e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 59 ALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVIT 138
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAAL-GVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 139 vaellPKVADLRLPVILLDDTAAksgssatlysdlvsgvdeadyrrpptkqsdtagLLYSSGTTGESKGVVLTHRNFIAA 218
Cdd:cd05903 80 -----PERFRQFDPAAMPDAVAL---------------------------------LLFTSGTTGEPKGVMHSHNTLSAS 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 219 ATMVTSDQDDRGEGpnVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGFALDTVMSAVQQHRVTHLFCVPPVMIALAKH 298
Cdd:cd05903 122 IRQYAERLGLGPGD--VFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPFLTDLLNA 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 299 GKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFpDALICQGYGMTETCGIISLeyPEKGQVRQFGST-GTLVTGVEAKIV 377
Cdd:cd05903 200 VEEAGEPLSRLRTFVCGGATVPRSLARRAAELL-GAKVCSAYGSTECPGAVTS--ITPAPEDRRLYTdGRPLPGVEIKVV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 378 DvETLKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELE 457
Cdd:cd05903 277 D-DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 458 GLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQ-VTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd05903 356 DLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQgVAKQYWPERLVHVDDLPRTPSGKVQKFRL 435
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
46-536 |
2.88e-64 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 217.83 E-value: 2.88e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 46 PSALALVdaATGHALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIA 125
Cdd:PRK06145 16 PDRAALV--YRDQEISYAEFHQRILQAAGMLHAR-GIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 126 KQASDARARLVItVAELLPKVADLRLPVILLDDTAAKSGSSatlysdLVSGVDEADyRRPPTKQSDTAGLLYSSGTTGES 205
Cdd:PRK06145 93 YILGDAGAKLLL-VDEEFDAIVALETPKIVIDAAAQADSRR------LAQGGLEIP-PQAAVAPTDLVRLMYTSGTTDRP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 206 KGVVLTHRNF-------IAAATMVTSDQddrgegpnvFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGFALDTVMSAVQ 278
Cdd:PRK06145 165 KGVMHSYGNLhwksidhVIALGLTASER---------LLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLAAIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 279 QHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFPDALICQGYGMTETCGIISLEypEKG- 357
Cdd:PRK06145 236 RHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLM--EAGr 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 358 QVRQFGSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTIRQGWLHTGDLGLFDDEGQLFVV 437
Cdd:PRK06145 314 EIEKIGSTGRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 438 DRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQVTYYKRLKRV 517
Cdd:PRK06145 393 DRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQL 472
|
490
....*....|....*....
gi 357113996 518 TFVSSVPKSASGKILRREL 536
Cdd:PRK06145 473 KVRDELPRNPSGKVLKRVL 491
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
60-536 |
1.00e-63 |
|
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: 214.51 E-value: 1.00e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 60 LTFSGLR--SAILASAVAlssRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVI 137
Cdd:cd05972 1 WSFRELKreSAKAANVLA---KLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 138 TVAEllpkvadlrlpvillddtaaksgssatlysdlvsgvdeadyrrpptkqsDTAGLLYSSGTTGESKGVVLTHRNFIA 217
Cdd:cd05972 78 TDAE-------------------------------------------------DPALIYFTSGTTGLPKGVLHTHSYPLG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 218 AATMVTSDQDDRGEGpnVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGFALDT--VMSAVQQHRVTHLFCVPPVMIAL 295
Cdd:cd05972 109 HIPTAAYWLGLRPDD--IHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAerILELLERYGVTSFCGPPTAYRML 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 296 AKHGKAGkYDLSSLKFIGSGAAPLGkdvmEAVAKNFPDAL---ICQGYGMTETcGIISLEYPekGQVRQFGSTGTLVTGV 372
Cdd:cd05972 187 IKQDLSS-YKFSHLRLVVSAGEPLN----PEVIEWWRAATglpIRDGYGQTET-GLTVGNFP--DMPVKPGSMGRPTPGY 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 373 EAKIVDVETlKHLPPNQLGEICVR-GPH-IMQGYFNNVQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQ 450
Cdd:cd05972 259 DVAIIDDDG-RELPPGEEGDIAIKlPPPgLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYR 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 451 IAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDV---QKFIETQVTYYKRLKRVTFVSSVPKSA 527
Cdd:cd05972 338 IGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAeelQGHVKKVLAPYKYPREIEFVEELPKTI 417
|
....*....
gi 357113996 528 SGKILRREL 536
Cdd:cd05972 418 SGKIRRVEL 426
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
34-536 |
2.82e-63 |
|
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: 215.31 E-value: 2.82e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 34 AVDLLLRRAAACPSALALVDAATGHaLTFSGLRSAILASAVALSsRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVAS 113
Cdd:cd05959 5 AATLVDLNLNEGRGDKTAFIDDAGS-LTYAELEAEARRVAGALR-ALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 114 TANPLYTPREIAKQASDARARLVITVAELLPKVAD---LRLP----VILLDDTAAKSGssATLYSDLVSGvdEADYRRP- 185
Cdd:cd05959 83 PVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAaltKSEHtlvvLIVSGGAGPEAG--ALLLAELVAA--EAEQLKPa 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 186 PTKQSDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVTSD-----QDDrgegpnVFLCFLPMFHIFGLSVITYGQLQRGN 260
Cdd:cd05959 159 ATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNvlgirEDD------VCFSAAKLFFAYGLGNSLTFPLSVGA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 261 TVVVMSGF-ALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFpDALICQG 339
Cdd:cd05959 233 TTVLMPERpTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARF-GLDILDG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 340 YGMTETCGIISLEYPekGQVRqFGSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTIRQGW 419
Cdd:cd05959 312 IGSTEMLHIFLSNRP--GRVR-YGTTGKPVPGYEVELRD-EDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQGEW 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 420 LHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSP---DSSLT 496
Cdd:cd05959 388 TRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPgyeDSEAL 467
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 357113996 497 EVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd05959 468 EEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
59-536 |
1.01e-62 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 213.79 E-value: 1.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 59 ALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVIT 138
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLAAL-GVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 139 VAELLPKVADL---RLPVIL------------LDDTAAKSGSSATLYSDLVSgvDEADYRRPPTKQsdTAGLLYSSGTTG 203
Cdd:PRK12406 90 HADLLHGLASAlpaGVTVLSvptppeiaaayrISPALLTPPAGAIDWEGWLA--QQEPYDGPPVPQ--PQSMIYTSGTTG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 204 ESKGVvlTHRNFIAAATMVTSDQDDRGEG---PNVFLCFLPMFH----IFGLSVITYGQlqrgnTVVVMSGFALDTVMSA 276
Cdd:PRK12406 166 HPKGV--RRAAPTPEQAAAAEQMRALIYGlkpGIRALLTGPLYHsapnAYGLRAGRLGG-----VLVLQPRFDPEELLQL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 277 VQQHRVTHLFCVPPVMIALAKHGKA--GKYDLSSLKFIGSGAAPLGKDVMEAVAkNFPDALICQGYGMTETcGIISLEYP 354
Cdd:PRK12406 239 IERHRITHMHMVPTMFIRLLKLPEEvrAKYDVSSLRHVIHAAAPCPADVKRAMI-EWWGPVIYEYYGSTES-GAVTFATS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 355 EKGqVRQFGSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQ-GYFNNVQATEFTIRQGWLHTGDLGLFDDEGQ 433
Cdd:PRK12406 317 EDA-LSHPGTVGKAAPGAELRFVD-EDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEIDRGGFITSGDVGYLDADGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 434 LFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQVTYYKR 513
Cdd:PRK12406 395 LFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKARLAGYKV 474
|
490 500
....*....|....*....|...
gi 357113996 514 LKRVTFVSSVPKSASGKILRREL 536
Cdd:PRK12406 475 PKHIEIMAELPREDSGKIFKRRL 497
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
42-541 |
2.77e-62 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 212.36 E-value: 2.77e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 42 AAACPSALALVDAATGHALTFSGLRSAIlASAVALSSRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTP 121
Cdd:PRK09088 5 ARLQPQRLAAVDLALGRRWTYAELDALV-GRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 122 REIAKQASDARARLVITVAEllpkVADLRLPVILLDDTAAKsgssatlysdlVSGVDEADyrRPPTKQSDTAGLLYSSGT 201
Cdd:PRK09088 84 SELDALLQDAEPRLLLGDDA----VAAGRTDVEDLAAFIAS-----------ADALEPAD--TPSIPPERVSLILFTSGT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 202 TGESKGVVLTHRNFIAAAtmVTSDQDDRGEGPNVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGFALDTVMS--AVQQ 279
Cdd:PRK09088 147 SGQPKGVMLSERNLQQTA--HNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGrlGDPA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 280 HRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAP-LGKDVMEAVAKNFPdaLICqGYGMTETCGIISLEYpEKGQ 358
Cdd:PRK09088 225 LGITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPhAAEDILGWLDDGIP--MVD-GFGMSEAGTVFGMSV-DCDV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 359 VR-QFGSTGTLVTGVEAKIVDVETlKHLPPNQLGEICVRGPHIMQGYFNNVQATE--FTiRQGWLHTGDLGLFDDEGQLF 435
Cdd:PRK09088 301 IRaKAGAAGIPTPTVQTRVVDDQG-NDCPAGVPGELLLRGPNLSPGYWRRPQATAraFT-GDGWFRTGDIARRDADGFFW 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 436 VVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQVTYYKRLK 515
Cdd:PRK09088 379 VVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPK 458
|
490 500
....*....|....*....|....*....
gi 357113996 516 RVTFVSSVPKSASGKILR---RELIAKVR 541
Cdd:PRK09088 459 HLRLVDALPRTASGKLQKarlRDALAAGR 487
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
23-536 |
3.05e-62 |
|
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: 211.80 E-value: 3.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 23 AARIESNP---GLSAVDLLLRRAAACPSALALVDAatGHALTFSGLRSAILASAVALSsRAGVRPGDSVLLVAPNCVLYP 99
Cdd:cd05920 3 ARRYRAAGywqDEPLGDLLARSAARHPDRIAVVDG--DRRLTYRELDRRADRLAAGLR-GLGIRPGDRVVVQLPNVAEFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 100 VCFFAVTALGAVASTANPLYTPREIAKQASDARARLVITvaellpkvadlrlpvillddtaaksgssatlySDLVSGVD- 178
Cdd:cd05920 80 VLFFALLRLGAVPVLALPSHRRSELSAFCAHAEAVAYIV--------------------------------PDRHAGFDh 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 179 EADYRRPPTKQSDTAGLLYSSGTTGESKGVVLTHR----NFIAAATMVTSDQDDrgegpnVFLCFLPMFHIFGLSVI-TY 253
Cdd:cd05920 128 RALARELAESIPEVALFLLSGGTTGTPKLIPRTHNdyayNVRASAEVCGLDQDT------VYLAVLPAAHNFPLACPgVL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 254 GQLQRGNTVVVMSGFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGkdvmEAVAKNFPD 333
Cdd:cd05920 202 GTLLAGGRVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLS----PALARRVPP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 334 ALIC---QGYGMTEtcGIISLEYPEKGQVRQFGSTG-TLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQ 409
Cdd:cd05920 278 VLGCtlqQVFGMAE--GLLNYTRLDDPDEVIIHTQGrPMSPDDEIRVVD-EEGNPVPPGEEGELLTRGPYTIRGYYRAPE 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 410 --ATEFTiRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYV 487
Cdd:cd05920 355 hnARAFT-PDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFV 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 357113996 488 VrSPDSSLTEVDVQKFI-ETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd05920 434 V-LRDPPPSAAQLRRFLrERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
40-535 |
1.13e-61 |
|
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: 212.10 E-value: 1.13e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 40 RRAAACPSALALV----DAATGHALTFSGLRSAILASAVALSSRAgvRPGDSVLLVAPNCVLYPVCFFAVTALGAVASta 115
Cdd:cd05931 1 RRAAARPDRPAYTflddEGGREETLTYAELDRRARAIAARLQAVG--KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAV-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 116 nPLYTPREIAKQ------ASDARARLVITVAELLPKVAD-------LRLPVILLDDTAAKSGSsatlysdlvsgvdeADY 182
Cdd:cd05931 77 -PLPPPTPGRHAerlaaiLADAGPRVVLTTAAALAAVRAfaasrpaAGTPRLLVVDLLPDTSA--------------ADW 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 183 RRPPTKQSDTAGLLYSSGTTGESKGVVLTHRNFIA-AATMVTSDQDDRGEgpnVFLCFLPMFHIFGLSVITYGQLQRGNT 261
Cdd:cd05931 142 PPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLAnVRQIRRAYGLDPGD---VVVSWLPLYHDMGLIGGLLTPLYSGGP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 262 VVVMS--GFALDTV--MSAVQQHRVTHLF--------CVPPVMIAlakhgKAGKYDLSSLKFIGSGAAPLGKDVMEAVAK 329
Cdd:cd05931 219 SVLMSpaAFLRRPLrwLRLISRYRATISAapnfaydlCVRRVRDE-----DLEGLDLSSWRVALNGAEPVRPATLRRFAE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 330 -----NFPDALICQGYGMTETCGIISLEYPEKG-----------------------QVRQFGSTGTLVTGVEAKIVDVET 381
Cdd:cd05931 294 afapfGFRPEAFRPSYGLAEATLFVSGGPPGTGpvvlrvdrdalagravavaaddpAARELVSCGRPLPDQEVRIVDPET 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 382 LKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTIRQ-------GWLHTGDLGlFDDEGQLFVVDRLKELIKYKGFQIAPA 454
Cdd:cd05931 374 GRELPDGEVGEIWVRGPSVASGYWGRPEATAETFGAlaatdegGWLRTGDLG-FLHDGELYITGRLKDLIIVRGRNHYPQ 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 455 ELE-GLLLSHPEILDAVVIPF--PDAEAGEVPIAYVVRSPDSSLTEVDVQKFI------ETQVTyykrLKRVTFVS--SV 523
Cdd:cd05931 453 DIEaTAEEAHPALRPGCVAAFsvPDDGEERLVVVAEVERGADPADLAAIAAAIraavarEHGVA----PADVVLVRpgSI 528
|
570
....*....|..
gi 357113996 524 PKSASGKILRRE 535
Cdd:cd05931 529 PRTSSGKIQRRA 540
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
40-543 |
1.97e-60 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 208.83 E-value: 1.97e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 40 RRAAACPSALALVDAaTGHALTFSGLRSAilASAVAL-SSRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPL 118
Cdd:PRK06087 31 QTARAMPDKIAVVDN-HGASYTYSALDHA--ASRLANwLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 119 YTPREIAKQASDARARLVIT---------VAELLPKVADLR-LPVILLDDTAAKSGSSATLYSDLVSGVDEADYrrPPTK 188
Cdd:PRK06087 108 WREAELVWVLNKCQAKMFFAptlfkqtrpVDLILPLQNQLPqLQQIVGVDKLAPATSSLSLSQIIADYEPLTTA--ITTH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 189 QSDTAGLLYSSGTTGESKGVVLTHRNFIA------AATMVTSDqddrgegpNVFLCFLPMFHIFG-LSVITYGQLQrGNT 261
Cdd:PRK06087 186 GDELAAVLFTSGTEGLPKGVMLTHNNILAseraycARLNLTWQ--------DVFMMPAPLGHATGfLHGVTAPFLI-GAR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 262 VVVMSGFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNfpDALICQGYG 341
Cdd:PRK06087 257 SVLLDIFTPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKVARECQQR--GIKLLSVYG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 342 MTETCGIISLEyPEKGQVRQFGSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTI-RQGWL 420
Cdd:PRK06087 335 STESSPHAVVN-LDDPLSRFMHTDGYAAAGVEIKVVD-EARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALdEEGWY 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 421 HTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVV-RSPDSSLTEVD 499
Cdd:PRK06087 413 YSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVlKAPHHSLTLEE 492
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 357113996 500 VQKFIETQ-VTYYKRLKRVTFVSSVPKSASGKI----LRRELIAKVRSS 543
Cdd:PRK06087 493 VVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKIqkflLRKDIMRRLTQD 541
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
41-536 |
5.42e-60 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 206.84 E-value: 5.42e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 41 RAAACPSALALV-DAATGHA--LTFSGLRSAILASA-VALSSraGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTAN 116
Cdd:PRK08008 16 LADVYGHKTALIfESSGGVVrrYSYLELNEEINRTAnLFYSL--GIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPIN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 117 PLYTPREIAKQASDARARLVITVAELLP------KVADLRLPVILLDDTAAKSGSSATLYSDLVS-GVDEADYRrPPTKQ 189
Cdd:PRK08008 94 ARLLREESAWILQNSQASLLVTSAQFYPmyrqiqQEDATPLRHICLTRVALPADDGVSSFTQLKAqQPATLCYA-PPLST 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 190 SDTAGLLYSSGTTGESKGVVLTHRN------FIAAATMVTSDqddrgegpNVFLCFLPMFHI-FGLSViTYGQLQRGNTV 262
Cdd:PRK08008 173 DDTAEILFTSGTTSRPKGVVITHYNlrfagyYSAWQCALRDD--------DVYLTVMPAFHIdCQCTA-AMAAFSAGATF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 263 VVMSGFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAG---KYDLSSLKFIgsgaAPLGKDVMEAVAKNFPDALIcQG 339
Cdd:PRK08008 244 VLLEKYSARAFWGQVCKYRATITECIPMMIRTLMVQPPSAndrQHCLREVMFY----LNLSDQEKDAFEERFGVRLL-TS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 340 YGMTET-CGIISlEYPekGQVRQFGSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRG---PHIMQGYFNNVQATEFTI 415
Cdd:PRK08008 319 YGMTETiVGIIG-DRP--GDKRRWPSIGRPGFCYEAEIRD-DHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 416 R-QGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSS 494
Cdd:PRK08008 395 EaDGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGET 474
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 357113996 495 LTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:PRK08008 475 LSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
36-536 |
4.27e-59 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 205.29 E-value: 4.27e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 36 DLLLRRAAACPSALALVDAATGHA----LTFSGLRSAILASAVALSsRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAV 111
Cdd:PRK13295 28 DDLDACVASCPDKTAVTAVRLGTGaprrFTYRELAALVDRVAVGLA-RLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 112 ASTANPLYTPREIAKQASDARARLVIT------------VAELLPKVADLRLPVILlddtaakSGSSATLYSDLVSGVD- 178
Cdd:PRK13295 107 LNPLMPIFRERELSFMLKHAESKVLVVpktfrgfdhaamARRLRPELPALRHVVVV-------GGDGADSFEALLITPAw 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 179 EADYRRPPTKQS------DTAGLLYSSGTTGESKGVVLTHR----NFIAAATMVTSDQDDrgegpnVFLCFLPMFHIFGL 248
Cdd:PRK13295 180 EQEPDAPAILARlrpgpdDVTQLIYTSGTTGEPKGVMHTANtlmaNIVPYAERLGLGADD------VILMASPMAHQTGF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 249 sviTYG---QLQRGNTVVVMSGFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVME 325
Cdd:PRK13295 254 ---MYGlmmPVMLGATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 326 AvAKNFPDALICQGYGMTEtCGIISLEYPEKGQVRQFGSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYF 405
Cdd:PRK13295 331 R-ARAALGAKIVSAWGMTE-NGAVTLTKLDDPDERASTTDGCPLPGVEVRVVD-ADGAPLPAGQIGRLQVRGCSNFGGYL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 406 NNVQATEfTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIA 485
Cdd:PRK13295 408 KRPQLNG-TDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACA 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 357113996 486 YVVRSPDSSLTEVDVQKFIETQ---VTYYKrlKRVTFVSSVPKSASGKI----LRREL 536
Cdd:PRK13295 487 FVVPRPGQSLDFEEMVEFLKAQkvaKQYIP--ERLVVRDALPRTPSGKIqkfrLREML 542
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
61-538 |
8.61e-59 |
|
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: 201.51 E-value: 8.61e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 61 TFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVITva 140
Cdd:cd05971 8 TFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 141 ellpkvadlrlpvillddtaaksgssatlysdlvsgvDEADyrrpptkqsDTAGLLYSSGTTGESKGVVLTHRNFIaaat 220
Cdd:cd05971 85 -------------------------------------DGSD---------DPALIIYTSGTTGPPKGALHAHRVLL---- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 221 mvtsdqddrGEGPNVFLCFlPMFH--------------IFGLSVITYGQLQRGNTVVV--MSGFALDTVMSAVQQHRVTH 284
Cdd:cd05971 115 ---------GHLPGVQFPF-NLFPrdgdlywtpadwawIGGLLDVLLPSLYFGVPVLAhrMTKFDPKAALDLMSRYGVTT 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 285 LFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFPDAlICQGYGMTETCGIISlEYPEKGQVRQfGS 364
Cdd:cd05971 185 AFLPPTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGVE-VNEFYGQTECNLVIG-NCSALFPIKP-GS 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 365 TGTLVTGVEAKIVDVETlKHLPPNQLGEICVRGPH--IMQGYFNNVQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKE 442
Cdd:cd05971 262 MGKPIPGHRVAIVDDNG-TPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 443 LIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSP---DSSLTEVDVQKFIETQVTYYKRLKRVTF 519
Cdd:cd05971 341 VITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPgetPSDALAREIQELVKTRLAAHEYPREIEF 420
|
490
....*....|....*....
gi 357113996 520 VSSVPKSASGKILRRELIA 538
Cdd:cd05971 421 VNELPRTATGKIRRRELRA 439
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
38-533 |
1.52e-58 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 202.80 E-value: 1.52e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 38 LLRRAAACPSALALvDAATGHALTFSGLRSAILASAVALSSRaGVRPGDSVLL----VAPNCVLYPVCFFAvtalGAVAS 113
Cdd:PRK07514 8 ALRAAFADRDAPFI-ETPDGLRYTYGDLDAASARLANLLVAL-GVKPGDRVAVqvekSPEALALYLATLRA----GAVFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 114 TANPLYTPREIAKQASDARARLVI---TVAELLPKVADLR--LPVILLDdtAAKSGSSATLYSDLvsgvdEADYRRPPTK 188
Cdd:PRK07514 82 PLNTAYTLAELDYFIGDAEPALVVcdpANFAWLSKIAAAAgaPHVETLD--ADGTGSLLEAAAAA-----PDDFETVPRG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 189 QSDTAGLLYSSGTTGESKGVVLTHRNFIA-AATMV-----TSDqddrgegpNVFLCFLPMFHIFGLSVITYGQLQRGNTV 262
Cdd:PRK07514 155 ADDLAAILYTSGTTGRSKGAMLSHGNLLSnALTLVdywrfTPD--------DVLIHALPIFHTHGLFVATNVALLAGASM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 263 VVMSGFALDTVMSAVQqhRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFPDAlICQGYGM 342
Cdd:PRK07514 227 IFLPKFDPDAVLALMP--RATVMMGVPTFYTRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHA-ILERYGM 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 343 TETCGIISleYPEKGQvRQFGSTGTLVTGVEAKIVDVETLKHLPPNQLGEICVRGPHIMQGYFNNVQ--ATEFTiRQGWL 420
Cdd:PRK07514 304 TETNMNTS--NPYDGE-RRAGTVGFPLPGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEktAEEFR-ADGFF 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 421 HTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDV 500
Cdd:PRK07514 380 ITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAI 459
|
490 500 510
....*....|....*....|....*....|....*..
gi 357113996 501 QKFIETQVTYYKRLKRVTFVSSVPKSASGK----ILR 533
Cdd:PRK07514 460 LAALKGRLARFKQPKRVFFVDELPRNTMGKvqknLLR 496
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
73-536 |
1.54e-58 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 200.78 E-value: 1.54e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 73 AVALSSRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARarlvITVAellpkvadlrlp 152
Cdd:cd05958 24 ANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKAR----ITVA------------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 153 villddtaaksgssatLYSDLVSGVDeadyrrpptkqsDTAGLLYSSGTTGESKGVVLTHRNFIAAA-----TMVTSDQD 227
Cdd:cd05958 88 ----------------LCAHALTASD------------DICILAFTSGTTGAPKATMHFHRDPLASAdryavNVLRLRED 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 228 DRgegpnvFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLS 307
Cdd:cd05958 140 DR------FVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLS 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 308 SLKFIGSGAAPLGKDVMEAVAKNFPDALIcQGYGMTETCGIISLEYPEKGQVrqfGSTGTLVTGVEAKIVDVETlKHLPP 387
Cdd:cd05958 214 SLRKCVSAGEALPAALHRAWKEATGIPII-DGIGSTEMFHIFISARPGDARP---GATGKPVPGYEAKVVDDEG-NPVPD 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 388 NQLGEICVRGPHIMQGYFNNVQATEFtiRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEIL 467
Cdd:cd05958 289 GTIGRLAVRGPTGCRYLADKRQRTYV--QGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVA 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357113996 468 DAVVIPFPDAEAGEVPIAYVVRSPDSSLTEV---DVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd05958 367 ECAVVGHPDESRGVVVKAFVVLRPGVIPGPVlarELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
42-538 |
2.97e-58 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 202.85 E-value: 2.97e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 42 AAACPSALALVDAATghALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTP 121
Cdd:PRK07788 59 ARRAPDRAALIDERG--TLTYAELDEQSNALARGLLAL-GVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 122 REIAKQASDARARLVITVAELLPKVADL-----RLPVILLD-DTAAKSGSSATLYSDLVSGVDEADYRRPPTKqsdtAGL 195
Cdd:PRK07788 136 PQLAEVAAREGVKALVYDDEFTDLLSALppdlgRLRAWGGNpDDDEPSGSTDETLDDLIAGSSTAPLPKPPKP----GGI 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 196 -LYSSGTTGESKGVVLTH-RNFIAAATMVTSDQDDRGEgpnVFLCFLPMFHIFGLSVITYGqLQRGNTVVVMSGFALDTV 273
Cdd:PRK07788 212 vILTSGTTGTPKGAPRPEpSPLAPLAGLLSRVPFRAGE---TTLLPAPMFHATGWAHLTLA-MALGSTVVLRRRFDPEAT 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 274 MSAVQQHRVTHLFCVPPV---MIALAKHGKAgKYDLSSLKFIGSGAAPLGKDVMEAVAKNFPDALiCQGYGMTEtCGIIS 350
Cdd:PRK07788 288 LEDIAKHKATALVVVPVMlsrILDLGPEVLA-KYDTSSLKIIFVSGSALSPELATRALEAFGPVL-YNLYGSTE-VAFAT 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 351 LEYPEKGQvRQFGSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFN--NVQateftIRQGWLHTGDLGLF 428
Cdd:PRK07788 365 IATPEDLA-EAPGTVGRPPKGVTVKILD-ENGNEVPRGVVGRIFVGNGFPFEGYTDgrDKQ-----IIDGLLSSGDVGYF 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 429 DDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQV 508
Cdd:PRK07788 438 DEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNL 517
|
490 500 510
....*....|....*....|....*....|
gi 357113996 509 TYYKRLKRVTFVSSVPKSASGKILRRELIA 538
Cdd:PRK07788 518 ARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
65-536 |
3.58e-58 |
|
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: 200.36 E-value: 3.58e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 65 LRSAILASAVALssrAGVRPGDSVLLVAPNCVLYPVCFFAVT----ALGAVASTANPLYTPREIAKQASDARARLVITVA 140
Cdd:cd05922 1 LGVSAAASALLE---AGGVRGERVVLILPNRFTYIELSFAVAyaggRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 141 ELLPKVADlrlpvillddtaaksGSSATLYSDLVSGVDEADYRRPPT-----KQSDTAGLLYSSGTTGESKGVVLTHRNF 215
Cdd:cd05922 78 GAADRLRD---------------ALPASPDPGTVLDADGIRAARASApahevSHEDLALLLYTSGSTGSPKLVRLSHQNL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 216 IAAATMVTSDQDDRGEgpNVFLCFLPMFHIFGLSVITyGQLQRGNTVVVMSGFALD-TVMSAVQQHRVTHLFCVPPVMIA 294
Cdd:cd05922 143 LANARSIAEYLGITAD--DRALTVLPLSYDYGLSVLN-THLLRGATLVLTNDGVLDdAFWEDLREHGATGLAGVPSTYAM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 295 LAKHGKAgKYDLSSLKFIGSGAAPLGKDVMEAVAKNFPDALICQGYGMTETCGIISLEYPEKgQVRQFGSTGTLVTGVEA 374
Cdd:cd05922 220 LTRLGFD-PAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPER-ILEKPGSIGLAIPGGEF 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 375 KIVDVETLKhLPPNQLGEICVRGPHIMQGYFNNVQA-TEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAP 453
Cdd:cd05922 298 EILDDDGTP-TPPGEPGEIVHRGPNVMKGYWNDPPYrRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 454 AELEGLLLSHPEILDAVVIPFPDaEAGEVPIAYVVRSPDSSLTevDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILR 533
Cdd:cd05922 377 TEIEAAARSIGLIIEAAAVGLPD-PLGEKLALFVTAPDKIDPK--DVLRSLAERLPPYKVPATVRVVDELPLTASGKVDY 453
|
...
gi 357113996 534 REL 536
Cdd:cd05922 454 AAL 456
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
50-539 |
1.03e-57 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 200.52 E-value: 1.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 50 ALVDAATGHALTFSGL--RSAILASAVAlssRAGVRPGDSVLLVAPNCV-LYPVCFFAVTAlGAVASTANPLYTPREIAK 126
Cdd:PRK08276 2 AVIMAPSGEVVTYGELeaRSNRLAHGLR---ALGLREGDVVAILLENNPeFFEVYWAARRS-GLYYTPINWHLTAAEIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 127 QASDARARLVITVAELLPKVADLR------LPVILLDDTAAksgSSATLYSDLVSGvdEADYrrPPTKQSDTAGLLYSSG 200
Cdd:PRK08276 78 IVDDSGAKVLIVSAALADTAAELAaelpagVPLLLVVAGPV---PGFRSYEEALAA--QPDT--PIADETAGADMLYSSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 201 TTGESKGVV--LTHRNFIAAATMVTS--DQDDRGEGPNVFLCFLPMFH----IFGLSVitygqLQRGNTVVVMSGFALDT 272
Cdd:PRK08276 151 TTGRPKGIKrpLPGLDPDEAPGMMLAllGFGMYGGPDSVYLSPAPLYHtaplRFGMSA-----LALGGTVVVMEKFDAEE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 273 VMSAVQQHRVTHLFCVPPV---MIALAKHGKAgKYDLSSLKFIGSGAAPLGKDVMEAVAKNFPDALIcQGYGMTETCGI- 348
Cdd:PRK08276 226 ALALIERYRVTHSQLVPTMfvrMLKLPEEVRA-RYDVSSLRVAIHAAAPCPVEVKRAMIDWWGPIIH-EYYASSEGGGVt 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 349 -IS----LEYPekgqvrqfGSTGTLVTGvEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQAT-EFTIRQGWLHT 422
Cdd:PRK08276 304 vITsedwLAHP--------GSVGKAVLG-EVRILD-EDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTaAARNPHGWVTV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 423 GDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQK 502
Cdd:PRK08276 374 GDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDALAAE 453
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 357113996 503 ---FIETQVTYYKRLKRVTFVSSVPKSASGKILRRELIAK 539
Cdd:PRK08276 454 liaWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDR 493
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
55-531 |
1.08e-57 |
|
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: 199.86 E-value: 1.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 55 ATGHALTFSGLRSAILASAVALssRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARAR 134
Cdd:cd05909 3 TLGTSLTYRKLLTGAIALARKL--AKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 135 LVITVAELLPKVADLRLP-------VILLDDTAAKSGSS----ATLYSDLVSGVDEADYRRPPTKQSDTAGLLYSSGTTG 203
Cdd:cd05909 81 TVLTSKQFIEKLKLHHLFdveydarIVYLEDLRAKISKAdkckAFLAGKFPPKWLLRIFGVAPVQPDDPAVILFTSGSEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 204 ESKGVVLTHRNFI----AAATMVTSDQDDrgegpnVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGfALD--TVMSAV 277
Cdd:cd05909 161 LPKGVVLSHKNLLanveQITAIFDPNPED------VVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPN-PLDykKIPELI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 278 QQHRVTHLFCVPPVMIALAKhgKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFpDALICQGYGMTETCGIISLEYPEKG 357
Cdd:cd05909 234 YDKKATILLGTPTFLRGYAR--AAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKF-GIRILEGYGTTECSPVISVNTPQSP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 358 qvRQFGSTGTLVTGVEAKIVDVETLKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTIRQGWLHTGDLGLFDDEGQLFVV 437
Cdd:cd05909 311 --NKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTIT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 438 DRLKELIKYKGFQIAPAELEGLLLSH-PEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQVTYykRLKR 516
Cdd:cd05909 389 GRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTTTDTDPSSLNDILKNAGISNLA--KPSY 466
|
490
....*....|....*
gi 357113996 517 VTFVSSVPKSASGKI 531
Cdd:cd05909 467 IHQVEEIPLLGTGKP 481
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
60-536 |
1.59e-57 |
|
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: 198.07 E-value: 1.59e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 60 LTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVITV 139
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNL-GVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 140 AEllpkvadlrlpvillddtaaksgssatlysdlvsgvdeadyrrpptkqsDTAGLLYSSGTTGESKGVVLTHRNFIAAA 219
Cdd:cd05919 90 AD-------------------------------------------------DIAYLLYSSGTTGPPKGVMHAHRDPLLFA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 220 TMVTSDQDDRGEGPNVFlCFLPMFHIFGLSVITYGQLQRGNTVVVMSGFAL-DTVMSAVQQHRVTHLFCVPPVMIALAKH 298
Cdd:cd05919 121 DAMAREALGLTPGDRVF-SSAKMFFGYGLGNSLWFPLAVGASAVLNPGWPTaERVLATLARFRPTVLYGVPTFYANLLDS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 299 GKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFPDAlICQGYGMTETCGIISLEYPekGQVRqFGSTGTLVTGVEAKIVD 378
Cdd:cd05919 200 CAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGP-ILDGIGATEVGHIFLSNRP--GAWR-LGSTGRPVPGYEIRLVD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 379 VETlKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEG 458
Cdd:cd05919 276 EEG-HTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVES 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 459 LLLSHPEILDAVVIPFPDAEAGEVPIAYVV----RSPDSSLTEvDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRR 534
Cdd:cd05919 355 LIIQHPAVAEAAVVAVPESTGLSRLTAFVVlkspAAPQESLAR-DIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRF 433
|
..
gi 357113996 535 EL 536
Cdd:cd05919 434 KL 435
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
18-536 |
3.36e-57 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 199.98 E-value: 3.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 18 RSLRPAARIesnpgLSAvdLLLRRAAACPSALALVDAATghALTFSGLRSAILASAVALSSrAGVRPGDSVLLVAPNCVL 97
Cdd:PRK06155 14 DPLPPSERT-----LPA--MLARQAERYPDRPLLVFGGT--RWTYAEAARAAAAAAHALAA-AGVKRGDRVALMCGNRIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 98 YPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVITVAELLPKVA-----DLRLPVILLDDtAAKSGSSATLYSd 172
Cdd:PRK06155 84 FLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEaadpgDLPLPAVWLLD-APASVSVPAGWS- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 173 lVSGVDEADYRRPPTKQS--DTAGLLYSSGTTGESKGVVLTHRNFIAAATMVTsdqDDRGEGP-NVFLCFLPMFHIFGLS 249
Cdd:PRK06155 162 -TAPLPPLDAPAPAAAVQpgDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSA---EDLEIGAdDVLYTTLPLFHTNALN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 250 VItYGQLQRGNTVVVMSGFALDTVMSAVQQHRVTHLFCVPP-VMIALAKHGKAGKYDLSSLKFIGSGAAPlgkDVMEAVA 328
Cdd:PRK06155 238 AF-FQALLAGATYVLEPRFSASGFWPAVRRHGATVTYLLGAmVSILLSQPARESDRAHRVRVALGPGVPA---ALHAAFR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 329 KNFPDALIcQGYGMTETCGIISLEYPEkgqvRQFGSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRG--PH-IMQGYF 405
Cdd:PRK06155 314 ERFGVDLL-DGYGSTETNFVIAVTHGS----QRPGSMGRLAPGFEARVVD-EHDQELPDGEPGELLLRAdePFaFATGYF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 406 NNVQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAG-EVPI 484
Cdd:PRK06155 388 GMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEdEVMA 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 357113996 485 AYVVRsPDSSLTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:PRK06155 468 AVVLR-DGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
82-536 |
4.64e-57 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 200.10 E-value: 4.64e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 82 VRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVITVAELLPKVADLrlpvilLDDTAA 161
Cdd:PRK08751 73 LKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQV------IADTPV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 162 KS-----------GSSATLYSDLVSGVDE--ADYRRP-----------------PTKQ---SDTAGLLYSSGTTGESKGV 208
Cdd:PRK08751 147 KQvittglgdmlgFPKAALVNFVVKYVKKlvPEYRINgairfrealalgrkhsmPTLQiepDDIAFLQYTGGTTGVAKGA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 209 VLTHRNFIAAATMVTSDQDDRG---EGPNVFLCFLPMFHIFGLSV--ITYGQLQRGNTVVV----MSGFaldtvMSAVQQ 279
Cdd:PRK08751 227 MLTHRNLVANMQQAHQWLAGTGkleEGCEVVITALPLYHIFALTAngLVFMKIGGCNHLISnprdMPGF-----VKELKK 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 280 HRVTHLFCVPPVMIALAKHGKAGKYDLSSLKF-IGSGAAplgkdVMEAVA---KNFPDALICQGYGMTET----CgIISL 351
Cdd:PRK08751 302 TRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMtLGGGMA-----VQRSVAerwKQVTGLTLVEAYGLTETspaaC-INPL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 352 EYPEKGqvrqfGSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTI-RQGWLHTGDLGLFDD 430
Cdd:PRK08751 376 TLKEYN-----GSIGLPIPSTDACIKD-DAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMdADGWLHTGDIARMDE 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 431 EGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSpDSSLTEVDVQKFIETQVTY 510
Cdd:PRK08751 450 QGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKK-DPALTAEDVKAHARANLTG 528
|
490 500
....*....|....*....|....*.
gi 357113996 511 YKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:PRK08751 529 YKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
80-533 |
1.06e-55 |
|
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: 194.20 E-value: 1.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 80 AGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVITvaellpkvadlrlpvillddt 159
Cdd:cd05914 27 NGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV--------------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 160 aaksgssatlysdlvsgvdeadyrrppTKQSDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVTSdQDDRGEGpNVFLCF 239
Cdd:cd05914 86 ---------------------------SDEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKE-VVLLGKG-DKILSI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 240 LPMFHIFGLSVITYGQLQRGNTVVVMSGFALDTV-MSAVQQHRVTHLFCVPPVMIALAKH-------GKAGKYDLSS--- 308
Cdd:cd05914 137 LPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAKIiALAFAQVTPTLGVPVPLVIEKIFKMdiipkltLKKFKFKLAKkin 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 309 -------------------LKFIGSGAAPLGKDVMEAVAK-NFPdalICQGYGMTETCGIISleYPEKGQVRqFGSTGTL 368
Cdd:cd05914 217 nrkirklafkkvheafggnIKEFVIGGAKINPDVEEFLRTiGFP---YTIGYGMTETAPIIS--YSPPNRIR-LGSAGKV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 369 VTGVEAKIVDVEtlkhlPPNQLGEICVRGPHIMQGYFNNVQAT-EFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELI-KY 446
Cdd:cd05914 291 IDGVEVRIDSPD-----PATGEGEIIVRGPNVMKGYYKNPEATaEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIvLS 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 447 KGFQIAPAELEGLLLSHPEILDAVVIPF---------PDAEAGEVPIAYVVRSPDSSLTEVDVQkfIETQVTYYKRLKRV 517
Cdd:cd05914 366 SGKNIYPEEIEAKINNMPFVLESLVVVQekklvalayIDPDFLDVKALKQRNIIDAIKWEVRDK--VNQKVPNYKKISKV 443
|
490
....*....|....*..
gi 357113996 518 TFVSS-VPKSASGKILR 533
Cdd:cd05914 444 KIVKEeFEKTPKGKIKR 460
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
71-539 |
6.20e-55 |
|
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: 191.56 E-value: 6.20e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 71 ASAVALSSRAGVRPGDSVLLVAPNCvlyPVCFFAVTALGAVASTANPLYT---PREIAKQASDARARLVITVAELlpkva 147
Cdd:cd05969 11 ARFANVLKSLGVGKGDRVFVLSPRS---PELYFSMLGIGKIGAVICPLFSafgPEAIRDRLENSEAKVLITTEEL----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 148 dlrlpvillddtaaksgssatlysdlvsgvdeadYRRppTKQSDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVTSDQD 227
Cdd:cd05969 83 ----------------------------------YER--TDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 228 DRGEgpNVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSG-FALDTVMSAVQQHRVTHLFCVPPVMIALAKHGK--AGKY 304
Cdd:cd05969 127 LHPD--DIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGrFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDelARKY 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 305 DLSSLKFIGSGAAPLGKDV----MEAVAKNFPDalicqGYGMTETCGIISLEYPekGQVRQFGSTGTLVTGVEAKIVDvE 380
Cdd:cd05969 205 DLSSLRFIHSVGEPLNPEAirwgMEVFGVPIHD-----TWWQTETGSIMIANYP--CMPIKPGSMGKPLPGVKAAVVD-E 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 381 TLKHLPPNQLGEICVRG--PHIMQGYFNNVQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEG 458
Cdd:cd05969 277 NGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVES 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 459 LLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTE---VDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRRE 535
Cdd:cd05969 357 ALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDelkEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRV 436
|
....
gi 357113996 536 LIAK 539
Cdd:cd05969 437 LKAK 440
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
65-545 |
2.48e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 192.23 E-value: 2.48e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 65 LRSAILASAVAlssRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLV---ITVAE 141
Cdd:PRK07008 47 RRAKQLAQALA---ALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVlfdLTFLP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 142 LLPKVADlRLPV----ILLDDTAAKSGSSATL--YSDLVSGVDeADYRRPPTKQSDTAGLLYSSGTTGESKGVVLTHRNF 215
Cdd:PRK07008 124 LVDALAP-QCPNvkgwVAMTDAAHLPAGSTPLlcYETLVGAQD-GDYDWPRFDENQASSLCYTSGTTGNPKGALYSHRST 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 216 I----AAA---TMVTSDQDdrgegpnVFLCFLPMFHI--FGL--SVITYGqlqrgnTVVVMSGFALD--TVMSAVQQHRV 282
Cdd:PRK07008 202 VlhayGAAlpdAMGLSARD-------AVLPVVPMFHVnaWGLpySAPLTG------AKLVLPGPDLDgkSLYELIEAERV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 283 THLFCVPPVMIALAKHGKAGKYDLSSLK--FIGSGAAPlgkdvmEAVAKNFPDAL---ICQGYGMTE------TCGIIS- 350
Cdd:PRK07008 269 TFSAGVPTVWLGLLNHMREAGLRFSTLRrtVIGGSACP------PAMIRTFEDEYgveVIHAWGMTEmsplgtLCKLKWk 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 351 -LEYPEKGQVRQFGSTGTLVTGVEAKIVDVETlKHLPPN--QLGEICVRGPHIMQGYFNNvqaTEFTIRQGWLHTGDLGL 427
Cdd:PRK07008 343 hSQLPLDEQRKLLEKQGRVIYGVDMKIVGDDG-RELPWDgkAFGDLQVRGPWVIDRYFRG---DASPLVDGWFPTGDVAT 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 428 FDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQ 507
Cdd:PRK07008 419 IDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELLAFYEGK 498
|
490 500 510
....*....|....*....|....*....|....*...
gi 357113996 508 VTYYKRLKRVTFVSSVPKSASGKILRRELIAKVRSSKL 545
Cdd:PRK07008 499 VAKWWIPDDVVFVDAIPHTATGKLQKLKLREQFRDYVL 536
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
49-536 |
8.56e-54 |
|
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: 189.13 E-value: 8.56e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 49 LALVDAATGHALTFSGLRS-AILASAVALSSRA----GVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLyTPRE 123
Cdd:cd05929 1 LEARDLDRAQVFHQRRLLLlDVYSIALNRNARAaaaeGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSR-APRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 124 IAKQASDARARLVITVAELLPKVadlrlPVILLDDTAAKSGSSATLYSDLVSGVDeadyrrpptkqsdtagLLYSSGTTG 203
Cdd:cd05929 80 EACAIIEIKAAALVCGLFTGGGA-----LDGLEDYEAAEGGSPETPIEDEAAGWK----------------MLYSGGTTG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 204 ESKGVV--LTHRNFIAAATMVTSDQDDRGEGpNVFLCFLPMFHIFGLSViTYGQLQRGNTVVVMSGFALDTVMSAVQQHR 281
Cdd:cd05929 139 RPKGIKrgLPGGPPDNDTLMAAALGFGPGAD-SVYLSPAPLYHAAPFRW-SMTALFMGGTLVLMEKFDPEEFLRLIERYR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 282 VTHLFCVPPVMIALAKHGKA--GKYDLSSLKFIGSGAAPLGKDVMEAVAKNFPDALIcQGYGMTETCG--IIS----LEY 353
Cdd:cd05929 217 VTFAQFVPTMFVRLLKLPEAvrNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIW-EYYGGTEGQGltIINgeewLTH 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 354 PekgqvrqfGSTGTLVTGvEAKIVDvETLKHLPPNQLGEICVRGPHIMQgYFNNVQATEFTIRQ-GWLHTGDLGLFDDEG 432
Cdd:cd05929 296 P--------GSVGRAVLG-KVHILD-EDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEgGWSTLGDVGYLDEDG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 433 QLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQK---FIETQVT 509
Cdd:cd05929 365 YLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTALAEEliaFLRDRLS 444
|
490 500
....*....|....*....|....*..
gi 357113996 510 YYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd05929 445 RYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
39-545 |
1.02e-53 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 191.17 E-value: 1.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 39 LRRAAACPSAlALVDAATGHALTFSGLRSAILASAVALSsRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPL 118
Cdd:PLN02860 13 LTRLATLRGN-AVVTISGNRRRTGHEFVDGVLSLAAGLL-RLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 119 YTPREiAKQASD-ARARLVIT---VAELLPKVADLRLPV----ILLDDTaakSGSSATLYSDLVS---------GVDEAD 181
Cdd:PLN02860 91 WSFEE-AKSAMLlVRPVMLVTdetCSSWYEELQNDRLPSlmwqVFLESP---SSSVFIFLNSFLTtemlkqralGTTELD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 182 YRRPPtkqSDTAGLLYSSGTTGESKGVVLTHRNFI----AAATMVTSDQDDrgegpnVFLCFLPMFHIFGLS-VITygQL 256
Cdd:PLN02860 167 YAWAP---DDAVLICFTSGTTGRPKGVTISHSALIvqslAKIAIVGYGEDD------VYLHTAPLCHIGGLSsALA--ML 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 257 QRGNTVVVMSGFALDTVMSAVQQHRVTHLFCVPPVM---IALAKHGKAGKyDLSSLKFIGSGAAPLGKDVMEAVAKNFPD 333
Cdd:PLN02860 236 MVGACHVLLPKFDAKAALQAIKQHNVTSMITVPAMMadlISLTRKSMTWK-VFPSVRKILNGGGSLSSRLLPDAKKLFPN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 334 ALICQGYGMTETCG---IISLEYPEKGQVRQ----FGSTGTLVTG-------------VEAKIVDVEtlkhlpPNQLGEI 393
Cdd:PLN02860 315 AKLFSAYGMTEACSsltFMTLHDPTLESPKQtlqtVNQTKSSSVHqpqgvcvgkpaphVELKIGLDE------SSRVGRI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 394 CVRGPHIMQGYF-NNVQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVI 472
Cdd:PLN02860 389 LTRGPHVMLGYWgQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 473 PFPDAEAGEVPIAYV----------VRSPDSS----LTEVDVQKFIETQ-VTYYKRLKR-VTFVSSVPKSASGKI----L 532
Cdd:PLN02860 469 GVPDSRLTEMVVACVrlrdgwiwsdNEKENAKknltLSSETLRHHCREKnLSRFKIPKLfVQWRKPFPLTTTGKIrrdeV 548
|
570
....*....|....*
gi 357113996 533 RRELIAKVRS--SKL 545
Cdd:PLN02860 549 RREVLSHLQSlpSNL 563
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
190-539 |
1.08e-53 |
|
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: 185.76 E-value: 1.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 190 SDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVT----SDQDDrgegpnVFLCFLPMFHIFGLSVITYGQLQRGNTVVVM 265
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLAlnslFDPDD------VLLCGLPLFHVNGSVVTLLTPLASGAHVVLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 266 S--GF----ALDTVMSAVQQHRVTHLFCVPPVMIALAKhgKAGKYDLSSLKFIGSGAAPLGKdvmeAVAKNFPDAL---I 336
Cdd:cd05944 76 GpaGYrnpgLFDNFWKLVERYRITSLSTVPTVYAALLQ--VPVNADISSLRFAMSGAAPLPV----ELRARFEDATglpV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 337 CQGYGMTETCGIISLEYPEKGqvRQFGSTGTLVTGVEAKIV----DVETLKHLPPNQLGEICVRGPHIMQGYFNNVQATE 412
Cdd:cd05944 150 VEGYGLTEATCLVAVNPPDGP--KRPGSVGLRLPYARVRIKvldgVGRLLRDCAPDEVGEICVAGPGVFGGYLYTEGNKN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 413 FTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPD 492
Cdd:cd05944 228 AFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPG 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 357113996 493 SSLTEVDVQKFIETQVTYYKRL-KRVTFVSSVPKSASGKI----LRRELIAK 539
Cdd:cd05944 308 AVVEEEELLAWARDHVPERAAVpKHIEVLEELPVTAVGKVfkpaLRADAIHR 359
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
46-536 |
4.81e-53 |
|
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: 186.19 E-value: 4.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 46 PSALALVDAatGHALTFSGL--RSAILASAVAlssRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVastanplYTP-- 121
Cdd:cd05930 1 PDAVAVVDG--DQSLTYAELdaRANRLARYLR---ERGVGPGDLVAVLLERSLEMVVAILAVLKAGAA-------YVPld 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 122 ------ReIAKQASDARARLVITVAellpkvadlrlpvillddtaaksgssatlysdlvsgvdeadyrrpptkqSDTAGL 195
Cdd:cd05930 69 psypaeR-LAYILEDSGAKLVLTDP-------------------------------------------------DDLAYV 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 196 LYSSGTTGESKGVVLTHRNFIAaatMVTSDQDDRGEGPN-VFLCFlpMFHIFGLSVI-TYGQLQRGNTVVVMS---GFAL 270
Cdd:cd05930 99 IYTSGSTGKPKGVMVEHRGLVN---LLLWMQEAYPLTPGdRVLQF--TSFSFDVSVWeIFGALLAGATLVVLPeevRKDP 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 271 DTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGkyDLSSLKFIGSGAAPLGKDVMEAVAKNFPDALICQGYGMTE-----T 345
Cdd:cd05930 174 EALADLLAEEGITVLHLTPSLLRLLLQELELA--ALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEatvdaT 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 346 CGIISLEYPEKGQVrqfgSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTIRQ------GW 419
Cdd:cd05930 252 YYRVPPDDEEDGRV----PIGRPIPNTRVYVLD-ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPnpfgpgER 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 420 LH-TGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEV 498
Cdd:cd05930 327 MYrTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEE 406
|
490 500 510
....*....|....*....|....*....|....*...
gi 357113996 499 DVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd05930 407 ELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
195-529 |
3.64e-51 |
|
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: 178.26 E-value: 3.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 195 LLYSSGTTGESKGVVLTHRNFIAAATMVTSDQDDRGEgpNVFLCFLPMFHIfGLSVITYGQLQRGNTVVVMSGFALDTVM 274
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEG--TVFLNSGPLFHI-GTLMFTLATFHAGGTNVFVRRVDAEEVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 275 SAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFigSGAAPLGKDVMEAVAKNFPDALicQGYGMTETCGIISLEYP 354
Cdd:cd17636 82 ELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRS--SPAAPEWNDMATVDTSPWGRKP--GGYGQTEVMGLATFAAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 355 EKGQVRQFGSTGTLVTgveAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTIRQGWLHTGDLGLFDDEGQL 434
Cdd:cd17636 158 GGGAIGGAGRPSPLVQ---VRILD-EDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRGGWHHTNDLGRREPDGSL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 435 FVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQVTYYKRL 514
Cdd:cd17636 234 SFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRARIASYKKP 313
|
330
....*....|....*
gi 357113996 515 KRVTFVSSVPKSASG 529
Cdd:cd17636 314 KSVEFADALPRTAGG 328
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
58-545 |
4.21e-51 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 183.41 E-value: 4.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 58 HALTFSGLRSAILASAVALSsRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVI 137
Cdd:PRK06018 38 VRTTYAQIHDRALKVSQALD-RDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 138 TVAELLP---KVADlRLP----VILLDDTA---AKSGSSATLYSDLVSGVDeADYRRPPTKQSDTAGLLYSSGTTGESKG 207
Cdd:PRK06018 117 TDLTFVPileKIAD-KLPsverYVVLTDAAhmpQTTLKNAVAYEEWIAEAD-GDFAWKTFDENTAAGMCYTSGTTGDPKG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 208 VVLTHR-NFIAaaTMVTSDQDDRGEG-PNVFLCFLPMFHI--FGLSVITYGQlqrgNTVVVMSGFALD--TVMSAVQQHR 281
Cdd:PRK06018 195 VLYSHRsNVLH--ALMANNGDALGTSaADTMLPVVPLFHAnsWGIAFSAPSM----GTKLVMPGAKLDgaSVYELLDTEK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 282 VTHLFCVPPVMIALAKHGKAGKYDLSSLK--FIGSGAAPlgkdvmEAVAKNFPD--ALICQGYGMTETCGIISL------ 351
Cdd:PRK06018 269 VTFTAGVPTVWLMLLQYMEKEGLKLPHLKmvVCGGSAMP------RSMIKAFEDmgVEVRHAWGMTEMSPLGTLaalkpp 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 352 --EYPEKGQVRQFGSTGTLVTGVEAKIVDVETlKHLP--PNQLGEICVRGPHIMQGYFNnvQATEFTIRQGWLHTGDLGL 427
Cdd:PRK06018 343 fsKLPGDARLDVLQKQGYPPFGVEMKITDDAG-KELPwdGKTFGRLKVRGPAVAAAYYR--VDGEILDDDGFFDTGDVAT 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 428 FDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQ 507
Cdd:PRK06018 420 IDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEILKYMDGK 499
|
490 500 510
....*....|....*....|....*....|....*...
gi 357113996 508 VTYYKRLKRVTFVSSVPKSASGKILRRELIAKVRSSKL 545
Cdd:PRK06018 500 IAKWWMPDDVAFVDAIPHTATGKILKTALREQFKDYKL 537
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
36-530 |
1.82e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 181.62 E-value: 1.82e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 36 DLLLRRAAACPSALALVDAAtgHALTFSGL--RSAILASAvaLSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVAS 113
Cdd:PRK07798 7 DLFEAVADAVPDRVALVCGD--RRLTYAELeeRANRLAHY--LIAQ-GLGPGDHVGIYARNRIEYVEAMLGAFKARAVPV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 114 TANPLYTPREIAKQASDARARLVI-------TVAELLPKVADLRLPVILLDDTAAKSGSSATLYSDLVSGVDEAdyRRPP 186
Cdd:PRK07798 82 NVNYRYVEDELRYLLDDSDAVALVyerefapRVAEVLPRLPKLRTLVVVEDGSGNDLLPGAVDYEDALAAGSPE--RDFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 187 TKQSDTAGLLYSSGTTGESKGVVLTH----------RNFIAAATMVTSDQ---DDRGEGPNVFLCFLPMFHIFGLSViTY 253
Cdd:PRK07798 160 ERSPDDLYLLYTGGTTGMPKGVMWRQedifrvllggRDFATGEPIEDEEElakRAAAGPGMRRFPAPPLMHGAGQWA-AF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 254 GQLQRGNTVVVMSGFALD--TVMSAVQQHRVTHLFCVPPVMIA--LAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAK 329
Cdd:PRK07798 239 AALFSGQTVVLLPDVRFDadEVWRTIEREKVNVITIVGDAMARplLDALEARGPYDLSSLFAIASGGALFSPSVKEALLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 330 NFPDALICQGYGMTETcGIISLEYPEKGQVRQFGSTGTLvtGVEAKIVDVETLKHLPPNQLGEICVRGPHIMQGYFNNVQ 409
Cdd:PRK07798 319 LLPNVVLTDSIGSSET-GFGGSGTVAKGAVHTGGPRFTI--GPRTVVLDEDGNPVEPGSGEIGWIARRGHIPLGYYKDPE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 410 ATEFTIR----QGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIA 485
Cdd:PRK07798 396 KTAETFPtidgVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVA 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 357113996 486 YVVRSPDSSLTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGK 530
Cdd:PRK07798 476 VVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
190-533 |
8.27e-50 |
|
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: 174.76 E-value: 8.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 190 SDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVTSDQDDRGEGpNVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGFA 269
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVG-DVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 270 LDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAA-PLGKDVmeAVAKNFPDALICQGYGMTETCGI 348
Cdd:cd17635 80 YKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSrAIAADV--RFIEATGLTNTAQVYGLSETGTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 349 ISLEYPEkgQVRQFGSTGTLVTGVEAKIVDVETLKhLPPNQLGEICVRGPHIMQGYFNNVQATEFTIRQGWLHTGDLGLF 428
Cdd:cd17635 158 LCLPTDD--DSIEINAVGRPYPGVDVYLAATDGIA-GPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLGER 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 429 DDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKF-IETQ 507
Cdd:cd17635 235 REDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENAIRALKHtIRRE 314
|
330 340
....*....|....*....|....*.
gi 357113996 508 VTYYKRLKRVTFVSSVPKSASGKILR 533
Cdd:cd17635 315 LEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
38-539 |
8.30e-50 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 180.60 E-value: 8.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 38 LLRRAAAC-PSALALVDAATGHALTFSGLRSAILA-SAVALSsragVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTA 115
Cdd:PLN03102 19 FLKRASECyPNRTSIIYGKTRFTWPQTYDRCCRLAaSLISLN----ITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 116 NPLYTPREIAKQASDARAR----------LVITVAELLPKV-ADLRLPVILLD--DTAAKSGSSATLYSDLVSgvdeady 182
Cdd:PLN03102 95 NTRLDATSIAAILRHAKPKilfvdrsfepLAREVLHLLSSEdSNLNLPVIFIHeiDFPKRPSSEELDYECLIQ------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 183 RRPPT-----------KQSDTAGLLYSSGTTGESKGVVLTHRN-FIAAATMVTSDQddRGEGPnVFLCFLPMFHIFGLSv 250
Cdd:PLN03102 168 RGEPTpslvarmfriqDEHDPISLNYTSGTTADPKGVVISHRGaYLSTLSAIIGWE--MGTCP-VYLWTLPMFHCNGWT- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 251 ITYGQLQRGNTVVVMSGFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAK- 329
Cdd:PLN03102 244 FTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRl 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 330 NFPdalICQGYGMTETCG-IISLEY-------PEKGQVRQFGSTGTLVTGV-EAKIVDVETLKHLPPN--QLGEICVRGP 398
Cdd:PLN03102 324 GFQ---VMHAYGLTEATGpVLFCEWqdewnrlPENQQMELKARQGVSILGLaDVDVKNKETQESVPRDgkTMGEIVIKGS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 399 HIMQGYFNNVQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAE 478
Cdd:PLN03102 401 SIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPT 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357113996 479 AGEVPIAYVVRSPDSSLTEVDVQKFI--ETQVTYYKRL--------KRVTFVSSVPKSASGKILRREL--IAK 539
Cdd:PLN03102 481 WGETPCAFVVLEKGETTKEDRVDKLVtrERDLIEYCREnlphfmcpRKVVFLQELPKNGNGKILKPKLrdIAK 553
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
73-471 |
1.06e-49 |
|
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: 176.30 E-value: 1.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 73 AVALSSRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVITVAELLPKVADLRLP 152
Cdd:TIGR01733 13 ARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSALASRLAGLVLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 153 VILLDDTAAKSGSSATLysdlvsgvdeADYRRPPTKQSDTAGLLYSSGTTGESKGVVLTHRNFIA-AATMVTSDQDDRGE 231
Cdd:TIGR01733 93 VILLDPLELAALDDAPA----------PPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNlLAWLARRYGLDPDD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 232 gpnVFLCFLPmfHIFGLSVI-TYGQLQRGNTVVVMSGFALDTVMS----AVQQHRVTHLFCVPPVMIALAKhgkAGKYDL 306
Cdd:TIGR01733 163 ---RVLQFAS--LSFDASVEeIFGALLAGATLVVPPEDEERDDAAllaaLIAEHPVTVLNLTPSLLALLAA---ALPPAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 307 SSLKFIGSGAAPLGKDVMEAVAKNFPDALICQGYGMTETCGIISLEYPEKGQVRQFGST--GTLVTGVEAKIVDvETLKH 384
Cdd:TIGR01733 235 ASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRESPVpiGRPLANTRLYVLD-DDLRP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 385 LPPNQLGEICVRGPHIMQGYFNNVQATE--F-------TIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAE 455
Cdd:TIGR01733 314 VPVGVVGELYIGGPGVARGYLNRPELTAerFvpdpfagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGE 393
|
410
....*....|....*.
gi 357113996 456 LEGLLLSHPEILDAVV 471
Cdd:TIGR01733 394 IEAALLRHPGVREAVV 409
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
34-536 |
1.36e-49 |
|
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: 179.23 E-value: 1.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 34 AVDLLLRRAAACPSALALV---DAATGHALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGA 110
Cdd:cd05970 19 AYDVVDAMAKEYPDKLALVwcdDAGEERIFTFAELADYSDKTANFFKAM-GIGKGDTVMLTLKRRYEFWYSLLALHKLGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 111 VASTANPLYTPREIAKQASDARARLVITVAE-LLPKVADLRLPVILLDDTAAKSGSSATL-YSDLVSGVDEA--DYRRP- 185
Cdd:cd05970 98 IAIPATHQLTAKDIVYRIESADIKMIVAIAEdNIPEEIEKAAPECPSKPKLVWVGDPVPEgWIDFRKLIKNAspDFERPt 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 186 ---PTKQSDTAGLLYSSGTTGESKGVvlTHRNFIAAATMVTS------DQDDR-------GEGPNVFLCFlpmfhifgls 249
Cdd:cd05970 178 ansYPCGEDILLVYFSSGTTGMPKMV--EHDFTYPLGHIVTAkywqnvREGGLhltvadtGWGKAVWGKI---------- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 250 vitYGQLQRGNTVVV--MSGFALDTVMSAVQQHRVTHlFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAV 327
Cdd:cd05970 246 ---YGQWIAGAAVFVydYDKFDPKALLEKLSKYGVTT-FCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 328 aKNFPDALICQGYGMTETCGIISlEYPekGQVRQFGSTGTLVTGVEAKIVDVETlKHLPPNQLGEICVRGPH-----IMQ 402
Cdd:cd05970 322 -KEKTGIKLMEGFGQTETTLTIA-TFP--WMEPKPGSMGKPAPGYEIDLIDREG-RSCEAGEEGEIVIRTSKgkpvgLFG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 403 GYFNNVQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEV 482
Cdd:cd05970 397 GYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQV 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 357113996 483 PIAYVVRSPDSSLTEV---DVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd05970 477 VKATIVLAKGYEPSEElkkELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEI 533
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
14-545 |
2.06e-49 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 179.27 E-value: 2.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 14 DGVYRSLRPAARIESN-PGLSAVDLLLRRAAACPSALALVDAATGHALTFSGLRSAILASAVAlssRAGVRPGDSVLLVA 92
Cdd:PLN02479 1 MAKERDIDDLPKNAANyTALTPLWFLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALA---KRSIGPGSTVAVIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 93 PNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVITVAELLP------------KVADLRLPVILL--DD 158
Cdd:PLN02479 78 PNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQEFFTlaeealkilaekKKSSFKPPLLIVigDP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 159 TAAKSGSSATL------YSDLVSGVDEADYRRPPTKQSDTAGLLYSSGTTGESKGVVLTHRnfiAAATMVTSDQDDRG-- 230
Cdd:PLN02479 158 TCDPKSLQYALgkgaieYEKFLETGDPEFAWKPPADEWQSIALGYTSGTTASPKGVVLHHR---GAYLMALSNALIWGmn 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 231 EGPnVFLCFLPMFHIFGLsVITYGQLQRGNTVVVMSGFALDTVMSAVQQHRVTHlFCVPPVMIALAKHGKAGKYDLS--- 307
Cdd:PLN02479 235 EGA-VYLWTLPMFHCNGW-CFTWTLAALCGTNICLRQVTAKAIYSAIANYGVTH-FCAAPVVLNTIVNAPKSETILPlpr 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 308 SLKFIGSGAAPLGKDVMEAVAKNFPdalICQGYGMTETCGIISL--------EYPEKGQVRQFGSTGTLVTGVEA-KIVD 378
Cdd:PLN02479 312 VVHVMTAGAAPPPSVLFAMSEKGFR---VTHTYGLSETYGPSTVcawkpewdSLPPEEQARLNARQGVRYIGLEGlDVVD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 379 VETLKHLPPN--QLGEICVRGPHIMQGYFNNVQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAEL 456
Cdd:PLN02479 389 TKTMKPVPADgkTMGEIVMRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 457 EGLLLSHPEILDAVVIPFPDAEAGEVPIAYV-----VRSPDSSLTEVDVQKFIETQVTYYKRLKRVTFvSSVPKSASGKI 531
Cdd:PLN02479 469 ENVVYTHPAVLEASVVARPDERWGESPCAFVtlkpgVDKSDEAALAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKI 547
|
570 580
....*....|....*....|
gi 357113996 532 LRRELIAK------VRSSKL 545
Cdd:PLN02479 548 QKHVLRAKakemgpVKKSRL 567
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
40-539 |
2.52e-49 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 177.96 E-value: 2.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 40 RRAAACPSALALVDAATGHALTFSGL--RSAILAsavALSSRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANP 117
Cdd:PRK13391 5 IHAQTTPDKPAVIMASTGEVVTYRELdeRSNRLA---HLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 118 LYTPREIAKQASDARARLVIT------VAELLPKvadlRLPVILLDDTAAKSGSSATLYsdlvsGVDEADYRRPPTK--- 188
Cdd:PRK13391 82 HLTPAEAAYIVDDSGARALITsaakldVARALLK----QCPGVRHRLVLDGDGELEGFV-----GYAEAVAGLPATPiad 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 189 QSDTAGLLYSSGTTGESKGVV-----------LTHRNFIAAATMVTSDQddrgegpnVFLCFLPMFHIFGLSVItyGQLQ 257
Cdd:PRK13391 153 ESLGTDMLYSSGTTGRPKGIKrplpeqppdtpLPLTAFLQRLWGFRSDM--------VYLSPAPLYHSAPQRAV--MLVI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 258 R-GNTVVVMSGFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKA--GKYDLSSLKFIGSGAAPLGKDVMEAVAKNF-Pd 333
Cdd:PRK13391 223 RlGGTVIVMEHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEvrDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWgP- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 334 aLICQGYGMTETCGIISLEYPEkgQVRQFGSTGTLVTGVeAKIVDvETLKHLPPNQLGEICVRGPHIMQgYFNNVQATEF 413
Cdd:PRK13391 302 -IIHEYYAATEGLGFTACDSEE--WLAHPGTVGRAMFGD-LHILD-DDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 414 T--IRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVR-- 489
Cdd:PRK13391 376 ArhPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPvd 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 357113996 490 --SPDSSLTEvDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRRELIAK 539
Cdd:PRK13391 456 gvDPGPALAA-ELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDR 506
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
60-536 |
5.91e-49 |
|
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: 179.05 E-value: 5.91e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 60 LTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPncvLYPVCFFAVTA---LGAVASTANPLYTPREIAKQASDARARLV 136
Cdd:cd05967 83 YTYAELLDEVSRLAGVLRKL-GVVKGDRVIIYMP---MIPEAAIAMLAcarIGAIHSVVFGGFAAKELASRIDDAKPKLI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 137 IT---------VAELLPKVAD-LRLP------VILLDDTAAKSGSSATL----YSDLVSGVDEADYrrPPTKQSDTAGLL 196
Cdd:cd05967 159 VTascgiepgkVVPYKPLLDKaLELSghkphhVLVLNRPQVPADLTKPGrdldWSELLAKAEPVDC--VPVAATDPLYIL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 197 YSSGTTGESKGVVLTHRNFIAAatMVTSDQDDRGEGP-NVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGFALDT--- 272
Cdd:cd05967 237 YTSGTTGKPKGVVRDNGGHAVA--LNWSMRNIYGIKPgDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPVGTpdp 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 273 --VMSAVQQHRVTHLFCVPPVMIALAK---HGKAG-KYDLSSLKFIGSGAAPLGKDVMEAVAKNFPDALIcQGYGMTETC 346
Cdd:cd05967 315 gaFWRVIEKYQVNALFTAPTAIRAIRKedpDGKYIkKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVI-DHWWQTETG 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 347 GIISLEYpeKGQVR---QFGSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGP---HIMQGYFNN---VQATEFTIRQ 417
Cdd:cd05967 394 WPITANP--VGLEPlpiKAGSPGKPVPGYQVQVLD-EDGEPVGPNELGNIVIKLPlppGCLLTLWKNderFKKLYLSKFP 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 418 GWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTE 497
Cdd:cd05967 471 GYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITA 550
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 357113996 498 VDVQK----FIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd05967 551 EELEKelvaLVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTL 593
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
24-531 |
1.74e-48 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 180.89 E-value: 1.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 24 ARIESNPGLSAVdlLLRRAAACPSALALVDAaTGHALTFSGLRSAILASAVALssRAGVRPGDSVLLVAPNCVLYPVCFF 103
Cdd:PRK08633 609 SRKEALPPLAEA--WIDTAKRNWSRLAVADS-TGGELSYGKALTGALALARLL--KRELKDEENVGILLPPSVAGALANL 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 104 AVTALGAVASTANplYTPREIAKQASDARARL--VIT----VAELLPKVADLRLP----VILLDDTAAKSGSSATLYSDL 173
Cdd:PRK08633 684 ALLLAGKVPVNLN--YTASEAALKSAIEQAQIktVITsrkfLEKLKNKGFDLELPenvkVIYLEDLKAKISKVDKLTALL 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 174 V-----SGVDEADYRRPPTKQsDTAGLLYSSGTTGESKGVVLTHRNFI----AAATMVTSDQDDrgegpnVFLCFLPMFH 244
Cdd:PRK08633 762 AarllpARLLKRLYGPTFKPD-DTATIIFSSGSEGEPKGVMLSHHNILsnieQISDVFNLRNDD------VILSSLPFFH 834
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 245 IFGLSVITYGQLQRGNTVVV----MSGFaldTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLG 320
Cdd:PRK08633 835 SFGLTVTLWLPLLEGIKVVYhpdpTDAL---GIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLK 911
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 321 KDVMEAVAKNFpDALICQGYGMTETCGIISLEYP---EKGQVRQF----GSTGTLVTGVEAKIVDVETLKHLPPNQLGEI 393
Cdd:PRK08633 912 PEVADAFEEKF-GIRILEGYGATETSPVASVNLPdvlAADFKRQTgskeGSVGMPLPGVAVRIVDPETFEELPPGEDGLI 990
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 394 CVRGPHIMQGYFNNVQATEFTIR----QGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLshpEILDA 469
Cdd:PRK08633 991 LIGGPQVMKGYLGDPEKTAEVIKdidgIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELA---KALGG 1067
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357113996 470 VVIPF-----PDAEAGEvPIAYVVRSPDSSLTEVdVQKFIETQVTYYKRLKRVTFVSSVPKSASGKI 531
Cdd:PRK08633 1068 EEVVFavtavPDEKKGE-KLVVLHTCGAEDVEEL-KRAIKESGLPNLWKPSRYFKVEALPLLGSGKL 1132
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
191-540 |
1.50e-47 |
|
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: 168.28 E-value: 1.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 191 DTAGLLYSSGTTGESKGVVLTHRNFIAAATMVTSDQDDRGEGpnVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGFAL 270
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGD--SWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 271 dtvMSAVQQHRVTHLFCVPPvmiALAK--HGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNfpDALICQGYGMTETCGI 348
Cdd:cd17630 79 ---AEDLAPPGVTHVSLVPT---QLQRllDSGQGPAALKSLRAVLLGGAPIPPELLERAADR--GIPLYTTYGMTETASQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 349 ISL-EYPEKGQvrqfGSTGTLVTGVEAKIVDVetlkhlppnqlGEICVRGPHIMQGYFNNVQATEFTiRQGWLHTGDLGL 427
Cdd:cd17630 151 VATkRPDGFGR----GGVGVLLPGRELRIVED-----------GEIWVGGASLAMGYLRGQLVPEFN-EDGWFTTKDLGE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 428 FDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVrsPDSSLTEVDVQKFIETQ 507
Cdd:cd17630 215 LHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIV--GRGPADPAELRAWLKDK 292
|
330 340 350
....*....|....*....|....*....|...
gi 357113996 508 VTYYKRLKRVTFVSSVPKSASGKILRRELIAKV 540
Cdd:cd17630 293 LARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
197-533 |
1.52e-47 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 167.97 E-value: 1.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 197 YSSGTTGESKGVVLTHRNFIAaaTMVTSDQDDRGEGPNVFLCFLPMFHIFGLSVITYGqLQRGNTVVVMSGFALDTVMSA 276
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIE--SFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISA-LYLGGTFIGQRKFNPKSWIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 277 VQQHRVTHLFCVPPVMIALAKHGKAgkydLSSLKFIGSGAAPLGKDVMEAVAKNFPDALICQGYGMTETCGIISLEYpek 356
Cdd:cd17633 84 INQYNATVIYLVPTMLQALARTLEP----ESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYNFN--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 357 GQVRQFGSTGTLVTGVEAKIVDVETlkhlppNQLGEICVRGPHIMQGYF--NNVQATeftirqGWLHTGDLGLFDDEGQL 434
Cdd:cd17633 157 QESRPPNSVGRPFPNVEIEIRNADG------GEIGKIFVKSEMVFSGYVrgGFSNPD------GWMSVGDIGYVDEEGYL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 435 FVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVrspDSSLTEVDVQKFIETQVTYYKRL 514
Cdd:cd17633 225 YLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS---GDKLTYKQLKRFLKQKLSRYEIP 301
|
330
....*....|....*....
gi 357113996 515 KRVTFVSSVPKSASGKILR 533
Cdd:cd17633 302 KKIIFVDSLPYTSSGKIAR 320
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
41-540 |
4.06e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 170.94 E-value: 4.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 41 RAAACPSALALVDAAT--GHALTFSGLRSAilASAVAlssrAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPL 118
Cdd:PRK07787 5 NPAAVAAAADIADAVRigGRVLSRSDLAGA--ATAVA----ERVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 119 YTPREIAKQASDARARLVITVaellPKVADLRLPVILLDDTAAksgssatlysdlvsgvdeADYRRPPTKQSDTAGLLYS 198
Cdd:PRK07787 79 SGVAERRHILADSGAQAWLGP----APDDPAGLPHVPVRLHAR------------------SWHRYPEPDPDAPALIVYT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 199 SGTTGESKGVVLThRNFIAAatmvtsDQDDRGE-----GPNVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGFALDTV 273
Cdd:PRK07787 137 SGTTGPPKGVVLS-RRAIAA------DLDALAEawqwtADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPEAY 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 274 MSAVQQhRVTHLFCVPPVMIALAKHGKAGKYdLSSLKFIGSGAAPLGKDVMEAVAKNFPDALIcQGYGMTETcgIISLEY 353
Cdd:PRK07787 210 AQALSE-GGTLYFGVPTVWSRIAADPEAARA-LRGARLLVSGSAALPVPVFDRLAALTGHRPV-ERYGMTET--LITLST 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 354 PEKGQvRQFGSTGTLVTGVEAKIVDvETLKHLP--PNQLGEICVRGPHIMQGYFNNVQATE--FTiRQGWLHTGDLGLFD 429
Cdd:PRK07787 285 RADGE-RRPGWVGLPLAGVETRLVD-EDGGPVPhdGETVGELQVRGPTLFDGYLNRPDATAaaFT-ADGWFRTGDVAVVD 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 430 DEGQLFVVDRLK-ELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTE-VDvqkFIETQ 507
Cdd:PRK07787 362 PDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAADElID---FVAQQ 438
|
490 500 510
....*....|....*....|....*....|...
gi 357113996 508 VTYYKRLKRVTFVSSVPKSASGKILRRELIAKV 540
Cdd:PRK07787 439 LSVHKRPREVRFVDALPRNAMGKVLKKQLLSEG 471
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
48-538 |
1.50e-46 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 171.23 E-value: 1.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 48 ALALVDAATGHALTFSGLRsailasavALSSRA-------GVRPGDSVLLVAPN-CVLYpVCFFAVTALGAVAStanPLY 119
Cdd:PRK04319 62 ALRYLDASRKEKYTYKELK--------ELSNKFanvlkelGVEKGDRVFIFMPRiPELY-FALLGALKNGAIVG---PLF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 120 T---PREIAKQASDARARLVITVAELLPKVADLRLP----VILLDDTAAKSGSSATLYSDLVSGVDEADYrrPPTKQSDT 192
Cdd:PRK04319 130 EafmEEAVRDRLEDSEAKVLITTPALLERKPADDLPslkhVLLVGEDVEEGPGTLDFNALMEQASDEFDI--EWTDREDG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 193 AGLLYSSGTTGESKGVVLTHRNFI---AAATMVTSDQDDrgegpNVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSG-F 268
Cdd:PRK04319 208 AILHYTSGSTGKPKGVLHVHNAMLqhyQTGKYVLDLHED-----DVYWCTADPGWVTGTSYGIFAPWLNGATNVIDGGrF 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 269 ALDTVMSAVQQHRVTHLFCVPPVMIALAKHGK--AGKYDLSSLKFIGSGAAPLGKDV----MEAVAKNFPDalicqGYGM 342
Cdd:PRK04319 283 SPERWYRILEDYKVTVWYTAPTAIRMLMGAGDdlVKKYDLSSLRHILSVGEPLNPEVvrwgMKVFGLPIHD-----NWWM 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 343 TETCGIISLEYPekGQVRQFGSTGTLVTGVEAKIVDVETlKHLPPNQLGEICVRG--PHIMQGYFNNVQATEFTIRQGWL 420
Cdd:PRK04319 358 TETGGIMIANYP--AMDIKPGSMGKPLPGIEAAIVDDQG-NELPPNRMGNLAIKKgwPSMMRGIWNNPEKYESYFAGDWY 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 421 HTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVV-RS---PDSSLT 496
Cdd:PRK04319 435 VSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVAlRPgyePSEELK 514
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 357113996 497 EvDVQKFIEtqvtyyKRL------KRVTFVSSVPKSASGKILRRELIA 538
Cdd:PRK04319 515 E-EIRGFVK------KGLgahaapREIEFKDKLPKTRSGKIMRRVLKA 555
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
81-532 |
2.53e-45 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 168.14 E-value: 2.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 81 GVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVITVAE---------LLPKVADLRL 151
Cdd:cd17634 105 GVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGgvragrsvpLKKNVDDALN 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 152 P-------VILLDDTAAK---SGSSATLYSDLVSGVdEADYRRPPTKQSDTAGLLYSSGTTGESKGVVLTHRNFIAAATM 221
Cdd:cd17634 185 PnvtsvehVIVLKRTGSDidwQEGRDLWWRDLIAKA-SPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAAT 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 222 VTSDQDDRGEGpNVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGF----ALDTVMSAVQQHRVTHLFCVPPVMIALAK 297
Cdd:cd17634 264 TMKYVFDYGPG-DIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVpnwpTPARMWQVVDKHGVNILYTAPTAIRALMA 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 298 HGKAG--KYDLSSLKFIGSGAAPLGKDVMEAVAKNFPDAL--ICQGYGMTETCGIISLEYPEKGQVRQfGSTGTLVTGVE 373
Cdd:cd17634 343 AGDDAieGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKcpVVDTWWQTETGGFMITPLPGAIELKA-GSATRPVFGVQ 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 374 AKIVDVETlKHLPPNQLGEICVRG--PHIMQGYFNN---VQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKG 448
Cdd:cd17634 422 PAVVDNEG-HPQPGGTEGNLVITDpwPGQTRTLFGDherFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAG 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 449 FQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSP---DSSLTEVDVQKFIETQVTYYKRLKRVTFVSSVPK 525
Cdd:cd17634 501 HRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHgvePSPELYAELRNWVRKEIGPLATPDVVHWVDSLPK 580
|
....*..
gi 357113996 526 SASGKIL 532
Cdd:cd17634 581 TRSGKIM 587
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
40-536 |
4.55e-45 |
|
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: 165.59 E-value: 4.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 40 RRAAACPSALALVDAatGHALTFSGL--RSAILASAVAlssRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANP 117
Cdd:cd17651 3 RQAARTPDAPALVAE--GRRLTYAELdrRANRLAHRLR---ARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 118 LYTPREIAKQASDARARLVITVAELLPKVADLRLPVILLDDTAAKSGSSATlysdlvsgvdeadyRRPPTKQSDTAGLLY 197
Cdd:cd17651 78 AYPAERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADAE--------------PDPALDADDLAYVIY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 198 SSGTTGESKGVVLTHR---NFIAAATMVTS-DQDDRGegpnvfLCFLPM-FHIFGLSVITYgqLQRGNTVVVMS---GFA 269
Cdd:cd17651 144 TSGSTGRPKGVVMPHRslaNLVAWQARASSlGPGART------LQFAGLgFDVSVQEIFST--LCAGATLVLPPeevRTD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 270 LDTVMSAVQQHRVTHLFcVPPVMI-ALAKHGKAGKYDLSSLK--FIGSGAAPLGKDVMEAVAKnFPDALICQGYGMTETC 346
Cdd:cd17651 216 PPALAAWLDEQRISRVF-LPTVALrALAEHGRPLGVRLAALRylLTGGEQLVLTEDLREFCAG-LPGLRLHNHYGPTETH 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 347 GIISLEYP-EKGQVRQFGSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQATE-------FTIRQG 418
Cdd:cd17651 294 VVTALSLPgDPAAWPAPPPIGRPIDNTRVYVLD-AALRPVPPGVPGELYIGGAGLARGYLNRPELTAerfvpdpFVPGAR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 419 WLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEV 498
Cdd:cd17651 373 MYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAA 452
|
490 500 510
....*....|....*....|....*....|....*...
gi 357113996 499 DVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd17651 453 ELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
15-539 |
5.09e-45 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 166.47 E-value: 5.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 15 GVYRSLRP--AARIES---NPGLSAVDLLLRRAAACPSALALVDAATghALTFSGLRSAILASAVALSsRAGVRPGDSVL 89
Cdd:PRK13382 21 GLIAPMRPdrYLRIVAamrREGMGPTSGFAIAAQRCPDRPGLIDELG--TLTWRELDERSDALAAALQ-ALPIGEPRVVG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 90 LVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVITVAELLPKVADLrlpvilLDDTAAKSGSSA-- 167
Cdd:PRK13382 98 IMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDEEFSATVDRA------LADCPQATRIVAwt 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 168 -TLYSDLVSG-VDEADYRRPPTKQSDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVTSDQDDRGEGPNVFLCflPMFHI 245
Cdd:PRK13382 172 dEDHDLTVEVlIAAHAGQRPEPTGRKGRVILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVA--PMFHA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 246 FGLSVITYGQLQRgNTVVVMSGFALDTVMSAVQQHRVTHLfCVPPVM----IALAKHGKAgKYDLSSLKFIGSGAAPLGK 321
Cdd:PRK13382 250 WGFSQLVLAASLA-CTIVTRRRFDPEATLDLIDRHRATGL-AVVPVMfdriMDLPAEVRN-RYSGRSLRFAAASGSRMRP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 322 DVMEAVAKNFPDAlICQGYGMTETcGIISLEYPEKGQvRQFGSTGTLVTGVEAKIVDVEtLKHLPPNQLGEICVRGPHIM 401
Cdd:PRK13382 327 DVVIAFMDQFGDV-IYNNYNATEA-GMIATATPADLR-AAPDTAGRPAEGTEIRILDQD-FREVPTGEVGTIFVRNDTQF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 402 QGYfnnVQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGE 481
Cdd:PRK13382 403 DGY---TSGSTKDFHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQ 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 357113996 482 VPIAYVVRSPDSSLTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRRELIAK 539
Cdd:PRK13382 480 RLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
36-536 |
3.08e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 164.53 E-value: 3.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 36 DLLLRRAAACPSALALVDAATghALTFSGLRSAILASAVALSsRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTA 115
Cdd:PRK06164 14 SLLDAHARARPDAVALIDEDR--PLSRAELRALVDRLAAWLA-AQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 116 NPLYTPREIAKQASDARARLV--------ITVAELL---PKVADLRLPVILL-----DDTAAKSGSSATLYSDLVSGVDE 179
Cdd:PRK06164 91 NTRYRSHEVAHILGRGRARWLvvwpgfkgIDFAAILaavPPDALPPLRAIAVvddaaDATPAPAPGARVQLFALPDPAPP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 180 ADYRRPPTKQSDTAGLLYSSGTTGESKGV------VLTHRNFIAAATMVtsDQDDrgegpnVFLCFLPMFHIFGLSVITy 253
Cdd:PRK06164 171 AAAGERAADPDAGALLFTTSGTTSGPKLVlhrqatLLRHARAIARAYGY--DPGA------VLLAALPFCGVFGFSTLL- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 254 GQLQRGNTVVVMSGFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGkAGKYDLSSLKFIGSGA-APLGKDVM-EAVAKNF 331
Cdd:PRK06164 242 GALAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTA-GERADFPSARLFGFASfAPALGELAaLARARGV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 332 PDALIcqgYGMTETCGIISL---EYPEkgQVRQFGStGTLVTG-VEAKIVDVETLKHLPPNQLGEICVRGPHIMQGYFNN 407
Cdd:PRK06164 321 PLTGL---YGSSEVQALVALqpaTDPV--SVRIEGG-GRPASPeARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 408 VQATEFTIR-QGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFpDAEAGEVPIAY 486
Cdd:PRK06164 395 PDATARALTdDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA-TRDGKTVPVAF 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 357113996 487 VVRSPDSSLTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASG---KILRREL 536
Cdd:PRK06164 474 VIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRL 526
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
22-536 |
7.59e-44 |
|
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: 163.22 E-value: 7.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 22 PAARIESNPGlSAVDLLLRRAAACPSA-LALVDAA-TGHALTFSGLrsaiLASAVALSS---RAGVRPGDSVLLVAPNCV 96
Cdd:cd05906 1 PLHRPEGAPR-TLLELLLRAAERGPTKgITYIDADgSEEFQSYQDL----LEDARRLAAglrQLGLRPGDSVILQFDDNE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 97 LYPVCFFAVTALGAVA--STANPLYT-PREIAKQASDARARL----VITVAELLPKVADLR-LPVILLDDTAAKSGSSAT 168
Cdd:cd05906 76 DFIPAFWACVLAGFVPapLTVPPTYDePNARLRKLRHIWQLLgspvVLTDAELVAEFAGLEtLSGLPGIRVLSIEELLDT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 169 lysdlvsgvdEADYRRPPTKQSDTAGLLYSSGTTGESKGVVLTHRNFIA--AATMVTSDQDDRgegpNVFLCFLPMFHIF 246
Cdd:cd05906 156 ----------AADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILArsAGKIQHNGLTPQ----DVFLNWVPLDHVG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 247 GLsvitygqlqrgntvvVMSG-FALDTVMSAVQ------------------QHRVTHLFcVPPVMIAL----AKHGKAGK 303
Cdd:cd05906 222 GL---------------VELHlRAVYLGCQQVHvpteeiladplrwldlidRYRVTITW-APNFAFALlndlLEEIEDGT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 304 YDLSSLKFIGSGA----APLGKDVMEAVAK-NFPDALICQGYGMTETC-GII---SLEYPEKGQVRQFGSTGTLVTGVEA 374
Cdd:cd05906 286 WDLSSLRYLVNAGeavvAKTIRRLLRLLEPyGLPPDAIRPAFGMTETCsGVIysrSFPTYDHSQALEFVSLGRPIPGVSM 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 375 KIVDVETlKHLPPNQLGEICVRGPHIMQGYFNNVQATE--FTiRQGWLHTGDLGlFDDEGQLFVVDRLKELIKYKGFQIA 452
Cdd:cd05906 366 RIVDDEG-QLLPEGEVGRLQVRGPVVTKGYYNNPEANAeaFT-EDGWFRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYY 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 453 PAELEGLLlshpEILDAVVIPF--------PDAEAGEVPIAYVVRS-PDSSLTEVdVQKfIETQVTYYKRLKRVTFV--- 520
Cdd:cd05906 443 SHEIEAAV----EEVPGVEPSFtaafavrdPGAETEELAIFFVPEYdLQDALSET-LRA-IRSVVSREVGVSPAYLIplp 516
|
570
....*....|....*..
gi 357113996 521 -SSVPKSASGKILRREL 536
Cdd:cd05906 517 kEEIPKTSLGKIQRSKL 533
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
35-536 |
1.17e-43 |
|
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: 166.96 E-value: 1.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 35 VDLLLRRAAACPSALALVDAatGHALTFSGL--RSAILASAVAlssRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAva 112
Cdd:COG1020 479 HELFEAQAARTPDAVAVVFG--DQSLTYAELnaRANRLAHHLR---ALGVGPGDLVGVCLERSLEMVVALLAVLKAGA-- 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 113 stA----NPLYtPRE-IAKQASDARARLVITVAELLPKVADLRLPVILLDDTAAKSGSSATLYSDLVSgvdeadyrrppt 187
Cdd:COG1020 552 --AyvplDPAY-PAErLAYMLEDAGARLVLTQSALAARLPELGVPVLALDALALAAEPATNPPVPVTP------------ 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 188 kqSDTAGLLYSSGTTGESKGVVLTHRNfiaAATMVTSDQDDRGEGPN-VFLCFLPMfhIFGLSVI-TYGQLQRGNTVVVM 265
Cdd:COG1020 617 --DDLAYVIYTSGSTGRPKGVMVEHRA---LVNLLAWMQRRYGLGPGdRVLQFASL--SFDASVWeIFGALLSGATLVLA 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 266 ------SGFALdtvMSAVQQHRVTHLFCVPPVMIALAKHGKAgkyDLSSLKFIGSGAAPLGKDVMEAVAKNFPDALICQG 339
Cdd:COG1020 690 ppearrDPAAL---AELLARHRVTVLNLTPSLLRALLDAAPE---ALPSLRLVLVGGEALPPELVRRWRARLPGARLVNL 763
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 340 YGMTETCgIISLEYP-EKGQVRQFGST-GTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQATE----- 412
Cdd:COG1020 764 YGPTETT-VDSTYYEvTPPDADGGSVPiGRPIANTRVYVLD-AHLQPVPVGVPGELYIGGAGLARGYLNRPELTAerfva 841
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 413 --FTIRQG-WLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVR 489
Cdd:COG1020 842 dpFGFPGArLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVP 921
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 357113996 490 SPDSSLTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:COG1020 922 EAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLAL 968
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
23-534 |
2.94e-43 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 161.59 E-value: 2.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 23 AARIESNPGLSAVDLLLRRAAACPSALALVDAATGHALTFSGLRSAILASAVALSsRAGVRPGDSVLLVAPNCVLYPVCF 102
Cdd:PRK05852 7 AAPMASDFGPRIADLVEVAATRLPEAPALVVTADRIAISYRDLARLVDDLAGQLT-RSGLLPGDRVALRMGSNAEFVVAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 103 FAVTALGAVASTANPLYTPRE--IAKQASDARARLVITVAELLPKVADLRLPVILLDDTAAKSGSSATLYSDL-VSGVDE 179
Cdd:PRK05852 86 LAASRADLVVVPLDPALPIAEqrVRSQAAGARVVLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLdAATEPT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 180 ADYRRPPTKQSDTAGLLYSSGTTGESKGVVLTHRNFiaaATMVTSDQDDRGEGP-NVFLCFLPMFHIFGLSVITYGQLQR 258
Cdd:PRK05852 166 PATSTPEGLRPDDAMIMFTGGTTGLPKMVPWTHANI---ASSVRAIITGYRLSPrDATVAVMPLYHGHGLIAALLATLAS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 259 GNTVVVMS--GFALDTVMSAVQQHRVTHLFCVPPV---MIALAKHGKAGKYDlSSLKFIGSGAAPLGKDVMEAVAKNFPD 333
Cdd:PRK05852 243 GGAVLLPArgRFSAHTFWDDIKAVGATWYTAVPTIhqiLLERAATEPSGRKP-AALRFIRSCSAPLTAETAQALQTEFAA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 334 ALICqGYGMTE-TCGIISLEYPEKGQVRQFGSTGTLV---TGVEAKIVDVETLKhLPPNQLGEICVRGPHIMQGYFNNVQ 409
Cdd:PRK05852 322 PVVC-AFGMTEaTHQVTTTQIEGIGQTENPVVSTGLVgrsTGAQIRIVGSDGLP-LPAGAVGEVWLRGTTVVRGYLGDPT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 410 ATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVR 489
Cdd:PRK05852 400 ITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVP 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 357113996 490 SPDSSLTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRR 534
Cdd:PRK05852 480 RESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
185-477 |
3.02e-43 |
|
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: 161.61 E-value: 3.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 185 PPTKQSDTAGLLYSSGTTGESKGVVLTHRNfIAAATMVTSDQDDRGEGPN---VFLCFLPMFHIFGLSVITYgQLQRGNT 261
Cdd:cd05927 109 PPPKPEDLATICYTSGTTGNPKGVMLTHGN-IVSNVAGVFKILEILNKINptdVYISYLPLAHIFERVVEAL-FLYHGAK 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 262 VVVMSGfALDTVMSAVQQHRVThLFCVPP---------VMIALAKHG--------KAGKYDLSSLK-------------- 310
Cdd:cd05927 187 IGFYSG-DIRLLLDDIKALKPT-VFPGVPrvlnriydkIFNKVQAKGplkrklfnFALNYKLAELRsgvvraspfwdklv 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 311 -------------FIGSGAAPLGKDVMEaVAKNFPDALICQGYGMTETCGIISLEYPekgQVRQFGSTGTLVTGVEAKIV 377
Cdd:cd05927 265 fnkikqalggnvrLMLTGSAPLSPEVLE-FLRVALGCPVLEGYGQTECTAGATLTLP---GDTSVGHVGGPLPCAEVKLV 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 378 DVETLKHLP--PNQLGEICVRGPHIMQGYFNNVQATEFTIRQ-GWLHTGDLGLFDDEGQLFVVDRLKELIKY-KGFQIAP 453
Cdd:cd05927 341 DVPEMNYDAkdPNPRGEVCIRGPNVFSGYYKDPEKTAEALDEdGWLHTGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAP 420
|
330 340 350
....*....|....*....|....*....|....*..
gi 357113996 454 AELEGLLLSHPEI-------------LDAVVIPFPDA 477
Cdd:cd05927 421 EKIENIYARSPFVaqifvygdslksfLVAIVVPDPDV 457
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
42-536 |
1.27e-42 |
|
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: 158.18 E-value: 1.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 42 AAACPSALALVDaaTGHALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPlYTP 121
Cdd:cd05945 1 AAANPDRPAVVE--GGRTLTYRELKERADALAAALASL-GLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDA-SSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 122 REiakqasdaRARLVITVAEllpkvadlrlPVILLDDtaaksgssatlysdlvsgvdeadyrrpptkQSDTAGLLYSSGT 201
Cdd:cd05945 77 AE--------RIREILDAAK----------PALLIAD------------------------------GDDNAYIIFTSGS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 202 TGESKGVVLTHRN---FIAAAtmvtsDQDDRGEGPNVFLCFLPmFHiFGLSVIT-YGQLQRGNTVVVMSGFALDTV---M 274
Cdd:cd05945 109 TGRPKGVQISHDNlvsFTNWM-----LSDFPLGPGDVFLNQAP-FS-FDLSVMDlYPALASGATLVPVPRDATADPkqlF 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 275 SAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLK---FIGSgaaPLGKDVMEAVAKNFPDALICQGYGMTETCGIISL 351
Cdd:cd05945 182 RFLAEHGITVWVSTPSFAAMCLLSPTFTPESLPSLRhflFCGE---VLPHKTARALQQRFPDARIYNTYGPTEATVAVTY 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 352 EYPEKGQVRQFGS--TGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQATE---FTIR-QGWLHTGDL 425
Cdd:cd05945 259 IEVTPEVLDGYDRlpIGYAKPGAKLVILD-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAaafFPDEgQRAYRTGDL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 426 GLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVV-RSPDSSLTEVDVQKFI 504
Cdd:cd05945 338 VRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVpKPGAEAGLTKAIKAEL 417
|
490 500 510
....*....|....*....|....*....|..
gi 357113996 505 ETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd05945 418 AERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
188-464 |
1.73e-42 |
|
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: 158.92 E-value: 1.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 188 KQSDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVTSDQDDRGEGPNVFLCFLPMFHIFGLSV----------ITYGQLQ 257
Cdd:cd17639 86 KPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGPDDRYLAYLPLAHIFELAAenvclyrggtIGYGSPR 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 258 ----------RGNTVV----VMSGFA--LDTV----------MSAVQQ-----------HRVTHLFCVP---PVMIALAK 297
Cdd:cd17639 166 tltdkskrgcKGDLTEfkptLMVGVPaiWDTIrkgvlaklnpMGGLKRtlfwtayqsklKALKEGPGTPlldELVFKKVR 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 298 HGKAGKydlssLKFIGSGAAPLGKDvmeavAKNFPDALIC---QGYGMTETCGIISLEYPEKGQVrqfGSTGTLVTGVEA 374
Cdd:cd17639 246 AALGGR-----LRYMLSGGAPLSAD-----TQEFLNIVLCpviQGYGLTETCAGGTVQDPGDLET---GRVGPPLPCCEI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 375 KIVDVETLKHL---PPNQlGEICVRGPHIMQGYFNNVQATE--FTiRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYK-G 448
Cdd:cd17639 313 KLVDWEEGGYStdkPPPR-GEILIRGPNVFKGYYKNPEKTKeaFD-GDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnG 390
|
330
....*....|....*.
gi 357113996 449 FQIAPAELEGLLLSHP 464
Cdd:cd17639 391 EYIALEKLESIYRSNP 406
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
40-434 |
2.21e-41 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 156.60 E-value: 2.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 40 RRAAACPSALALVDAATGHALTFSGL--RSAILASAVAlssRAGVRPGD-SVLLVAPNCVLYPVCFfAVTALGAVASTAN 116
Cdd:PRK09274 22 QLAVAVPGGRGADGKLAYDELSFAELdaRSDAIAHGLN---AAGIGRGMrAVLMVTPSLEFFALTF-ALFKAGAVPVLVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 117 PLYTPREIAKQASDARARLVITVAE------LLPKVADLRLPVILLDDTAAKSGSSatlYSDLVSGVDEADYRRPPTKQS 190
Cdd:PRK09274 98 PGMGIKNLKQCLAEAQPDAFIGIPKahlarrLFGWGKPSVRRLVTVGGRLLWGGTT---LATLLRDGAAAPFPMADLAPD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 191 DTAGLLYSSGTTGESKGVVLTHRNFIAaatMVTSDQDDRGEGPN-VFLCFLPMFHIFGLSVitygqlqrGNTVVV--MS- 266
Cdd:PRK09274 175 DMAAILFTSGSTGTPKGVVYTHGMFEA---QIEALREDYGIEPGeIDLPTFPLFALFGPAL--------GMTSVIpdMDp 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 267 ---GFA-LDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFP-DALICQGYG 341
Cdd:PRK09274 244 trpATVdPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAMLPpDAEILTPYG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 342 MTETCGIISLEYPEkgqvrQFGST--------GTLV----TGVEAKIVDV---------ETLKhLPPNQLGEICVRGPHI 400
Cdd:PRK09274 324 ATEALPISSIESRE-----ILFATraatdngaGICVgrpvDGVEVRIIAIsdapipewdDALR-LATGEIGEIVVAGPMV 397
|
410 420 430
....*....|....*....|....*....|....*....
gi 357113996 401 MQGYFNNVQATEFT-IRQG----WLHTGDLGLFDDEGQL 434
Cdd:PRK09274 398 TRSYYNRPEATRLAkIPDGqgdvWHRMGDLGYLDAQGRL 436
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
81-472 |
2.68e-40 |
|
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: 153.01 E-value: 2.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 81 GVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVItvaellpkvadlrlpVILLDDTA 160
Cdd:cd05932 27 GLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALF---------------VGKLDDWK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 161 A-KSGSSATLYSDLVSGVDEADYR---------------RPPTKQSDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVTS 224
Cdd:cd05932 92 AmAPGVPEGLISISLPPPSAANCQyqwddliaqhppleeRPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 225 DQDDRGEgpNVFLCFLPMFHIFGLSVITYGQLQRGNTVVvmsgFA--LDTVMSAVQQHRVTHLFCVP------------- 289
Cdd:cd05932 172 HIGTEEN--DRMLSYLPLAHVTERVFVEGGSLYGGVLVA----FAesLDTFVEDVQRARPTLFFSVPrlwtkfqqgvqdk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 290 ------------PVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVME---AVAKNfpdalICQGYGMTETCGIISLEYP 354
Cdd:cd05932 246 ipqqklnlllkiPVVNSLVKRKVLKGLGLDQCRLAGCGSAPVPPALLEwyrSLGLN-----ILEAYGMTENFAYSHLNYP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 355 EKgqvRQFGSTGTLVTGVEAKIVDVetlkhlppnqlGEICVRGPHIMQGYFNNVQATE--FTiRQGWLHTGDLGLFDDEG 432
Cdd:cd05932 321 GR---DKIGTVGNAGPGVEVRISED-----------GEILVRSPALMMGYYKDPEATAeaFT-ADGFLRTGDKGELDADG 385
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 357113996 433 QLFVVDRLKELIKY-KGFQIAPAELEGLLLSHPEILDAVVI 472
Cdd:cd05932 386 NLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVI 426
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
36-536 |
3.11e-40 |
|
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: 152.36 E-value: 3.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 36 DLLLRRAAACPSALALVDAATghALTFSGL--RSAILASAVAlssRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVAS 113
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDR--SLTYAELneRANRLARRLR---AAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 114 TANPLYTPREIAKQASDARARLVITVAELLPKVADLRLPVILLDDTAAKSGSSAtlysdlvsgvdeadyrRPPTKQSDTA 193
Cdd:cd12117 76 PLDPELPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNP----------------AVPVSPDDLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 194 GLLYSSGTTGESKGVVLTHRNFIAAATmvtsDQDDRGEGPN-VFLCFLPM-FHIFGLSVitYGQLQRGNTVVVMSGFALD 271
Cdd:cd12117 140 YVMYTSGSTGRPKGVAVTHRGVVRLVK----NTNYVTLGPDdRVLQTSPLaFDASTFEI--WGALLNGARLVLAPKGTLL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 272 TVMS---AVQQHRVTHLFCVPPVMIALAKHGKAGkydLSSLKFIGSGAAPLGKDVMEAVAKNFPDALICQGYGMTE---- 344
Cdd:cd12117 214 DPDAlgaLIAEEGVTVLWLTAALFNQLADEDPEC---FAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTEnttf 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 345 -TCGIISLEYPEKGQVrqfgSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQATE-------FTIR 416
Cdd:cd12117 291 tTSHVVTELDEVAGSI----PIGRPIANTRVYVLD-EDGRPVPPGVPGELYVGGDGLALGYLNRPALTAerfvadpFGPG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 417 QGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVrsPDSSLT 496
Cdd:cd12117 366 ERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVV--AEGALD 443
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 357113996 497 EVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd12117 444 AAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
59-472 |
4.94e-40 |
|
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: 151.36 E-value: 4.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 59 ALTFSGLRSAILASAVALSSrAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVAstanplyTPReiakqASDArarlviT 138
Cdd:cd17640 5 RITYKDLYQEILDFAAGLRS-LGVKAGEKVALFADNSPRWLIADQGIMALGAVD-------VVR-----GSDS------S 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 139 VAELLPKVADLRLPVILLDDTaaksgssatlysdlvsgvdeadyrrpptkQSDTAGLLYSSGTTGESKGVVLTHRNFI-- 216
Cdd:cd17640 66 VEELLYILNHSESVALVVEND-----------------------------SDDLATIIYTSGTTGNPKGVMLTHANLLhq 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 217 --AAATMVTSDQDDRgegpnvFLCFLPMFHIFGLS----VITYGQLQRGNTVVVMSgfaldtvmSAVQQHRVTHLFCVPP 290
Cdd:cd17640 117 irSLSDIVPPQPGDR------FLSILPIWHSYERSaeyfIFACGCSQAYTSIRTLK--------DDLKRVKPHYIVSVPR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 291 VMIAL--------AKHGKAGKYDLSSLKFIGSGAAPL-GKDVMEAVAKNFPDAL---ICQGYGMTETCGIISLEYPeKGQ 358
Cdd:cd17640 183 LWESLysgiqkqvSKSSPIKQFLFLFFLSGGIFKFGIsGGGALPPHVDTFFEAIgieVLNGYGLTETSPVVSARRL-KCN 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 359 VRqfGSTGTLVTGVEAKIVDVETLKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTIRQ-GWLHTGDLGLFDDEGQLFVV 437
Cdd:cd17640 262 VR--GSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSdGWFNTGDLGWLTCGGELVLT 339
|
410 420 430
....*....|....*....|....*....|....*.
gi 357113996 438 DRLKELIKYK-GFQIAPAELEGLLLSHPEILDAVVI 472
Cdd:cd17640 340 GRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVV 375
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
36-536 |
4.56e-39 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 149.76 E-value: 4.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 36 DLLLRRAAacPSALALVDAatGHALTFSGL--RSAILASAVAlssRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVAs 113
Cdd:PRK10946 29 DILTRHAA--SDAIAVICG--ERQFSYRELnqASDNLACSLR---RQGIKPGDTALVQLGNVAEFYITFFALLKLGVAP- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 114 tANPLYTPR--EIAKQASDARARLVIT------------VAELLPKVADLRLpVILLDDTAAKSGSSAtLYSDlvsgvdE 179
Cdd:PRK10946 101 -VNALFSHQrsELNAYASQIEPALLIAdrqhalfsdddfLNTLVAEHSSLRV-VLLLNDDGEHSLDDA-INHP------A 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 180 ADYRRPPTKQSDTAGLLYSSGTTGESKGVVLTHRNFI----AAATMVTSDQDDRgegpnvFLCFLPMFHIFGLSVI-TYG 254
Cdd:PRK10946 172 EDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYYysvrRSVEICGFTPQTR------YLCALPAAHNYPMSSPgALG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 255 QLQRGNTVVVMSGFALDTVMSAVQQHRVTHLFCVPP-VMIAL-AKHGKAGKYDLSSLKFIGSGAAPLGkdvmEAVAKNFP 332
Cdd:PRK10946 246 VFLAGGTVVLAPDPSATLCFPLIEKHQVNVTALVPPaVSLWLqAIAEGGSRAQLASLKLLQVGGARLS----ETLARRIP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 333 DALIC---QGYGMTEtcGIISLEYPEKGQVRQFGSTGTLVTGV-EAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNV 408
Cdd:PRK10946 322 AELGCqlqQVFGMAE--GLVNYTRLDDSDERIFTTQGRPMSPDdEVWVAD-ADGNPLPQGEVGRLMTRGPYTFRGYYKSP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 409 Q--ATEFTiRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAY 486
Cdd:PRK10946 399 QhnASAFD-ANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAF 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 357113996 487 -VVRSPdssLTEVDVQKFIETQ-VTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:PRK10946 478 lVVKEP---LKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
32-538 |
6.05e-39 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 150.72 E-value: 6.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 32 LSAVDLLLRR-AAACPSALALV---DAATGHALTFSGLRSAILASAVALSsRAGVRPGDSVLLVAPNCVLYPVCFFAVTA 107
Cdd:cd05968 60 MNIVEQLLDKwLADTRTRPALRwegEDGTSRTLTYGELLYEVKRLANGLR-ALGVGKGDRVGIYLPMIPEIVPAFLAVAR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 108 LGAVASTANPLYTPREIAKQASDARARLVIT---------VAELLPKV--ADLRLP----VIL-----LDDTAAKSGSSA 167
Cdd:cd05968 139 IGGIVVPIFSGFGKEAAATRLQDAEAKALITadgftrrgrEVNLKEEAdkACAQCPtvekVVVvrhlgNDFTPAKGRDLS 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 168 tlYSDLVSGvdeADYRRPPTKQSDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVTSDQDDRGEGPNVFLcFLPMFHIFG 247
Cdd:cd05968 219 --YDEEKET---AGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTW-FTDLGWMMG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 248 LSVItYGQLQRGNTVVVMSGF----ALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKA--GKYDLSSLKFIGSGAAPLGK 321
Cdd:cd05968 293 PWLI-FGGLILGATMVLYDGApdhpKADRLWRMVEDHEITHLGLSPTLIRALKPRGDApvNAHDLSSLRVLGSTGEPWNP 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 322 D----VMEAVAK-NFPdalICQGYGMTETCGIISLEYPEKgQVRQFGSTGTlVTGVEAKIVDvETLKHLPPnQLGEICVR 396
Cdd:cd05968 372 EpwnwLFETVGKgRNP---IINYSGGTEISGGILGNVLIK-PIKPSSFNGP-VPGMKADVLD-ESGKPARP-EVGELVLL 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 397 GPHI-------------MQGYFNNVQATeftirqgWLHtGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSH 463
Cdd:cd05968 445 APWPgmtrgfwrdedryLETYWSRFDNV-------WVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAH 516
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 357113996 464 PEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEV---DVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRRELIA 538
Cdd:cd05968 517 PAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEAlaeELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRA 594
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
42-536 |
8.29e-39 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 148.62 E-value: 8.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 42 AAACPSALALVDAATGHALTFSGL--RSAILASAValsSRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLY 119
Cdd:PRK13390 7 AQIAPDRPAVIVAETGEQVSYRQLddDSAALARVL---YDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 120 TPREIAKQASDARARLVITVAELlpkvadlrlpvillDDTAAKSGSSATLYSDLVSGVDE-ADYRR------PP-TKQSD 191
Cdd:PRK13390 84 TAPEADYIVGDSGARVLVASAAL--------------DGLAAKVGADLPLRLSFGGEIDGfGSFEAalagagPRlTEQPC 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 192 TAGLLYSSGTTGESKGVV--LTHRNF---------IAAATMVTSDQDdrgegpnVFLCFLPMFHIFGLSVITYGQlQRGN 260
Cdd:PRK13390 150 GAVMLYSSGTTGFPKGIQpdLPGRDVdapgdpivaIARAFYDISESD-------IYYSSAPIYHAAPLRWCSMVH-ALGG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 261 TVVVMSGFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKA--GKYDLSSLKFIGSGAAPLGKDVMEAVAkNFPDALICQ 338
Cdd:PRK13390 222 TVVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLLKLDADvrTRYDVSSLRAVIHAAAPCPVDVKHAMI-DWLGPIVYE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 339 GYGMTETCGIISLEYPEkgQVRQFGSTGTLVTGvEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQAT---EFTI 415
Cdd:PRK13390 301 YYSSTEAHGMTFIDSPD--WLAHPGSVGRSVLG-DLHICD-DDGNELPAGRIGTVYFERDRLPFRYLNDPEKTaaaQHPA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 416 RQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYV-----VRS 490
Cdd:PRK13390 377 HPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIqlvegIRG 456
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 357113996 491 PDSSLTE-VDvqkFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:PRK13390 457 SDELARElID---YTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
81-539 |
1.33e-38 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) 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 widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 149.63 E-value: 1.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 81 GVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVITVAEL--------LPKVADLRL- 151
Cdd:cd05966 105 GVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKLVITADGGyrggkvipLKEIVDEALe 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 152 ------PVILLDDTAAK---SGSSATLYSDLVSGVDEADyrrPPTKQS--DTAGLLYSSGTTGESKGVVLTHRNFI--AA 218
Cdd:cd05966 185 kcpsveKVLVVKRTGGEvpmTEGRDLWWHDLMAKQSPEC---EPEWMDseDPLFILYTSGSTGKPKGVVHTTGGYLlyAA 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 219 ATM--VTSDQDDrgegpNVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGFAL----DTVMSAVQQHRVTHLFCVPPVM 292
Cdd:cd05966 262 TTFkyVFDYHPD-----DIYWCTADIGWITGHSYIVYGPLANGATTVMFEGTPTypdpGRYWDIVEKHKVTIFYTAPTAI 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 293 IALAKHGKA--GKYDLSSLKFIGSGAAPLGKdvmEA-------VAKNfpDALICQGYGMTETCGII--SL--EYPEKGqv 359
Cdd:cd05966 337 RALMKFGDEwvKKHDLSSLRVLGSVGEPINP---EAwmwyyevIGKE--RCPIVDTWWQTETGGIMitPLpgATPLKP-- 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 360 rqfGSTGTLVTGVEAKIVDVETlKHLPPNQLGEICVRG--PHIMQGYFNNVQA---TEFTIRQGWLHTGDLGLFDDEGQL 434
Cdd:cd05966 410 ---GSATRPFFGIEPAILDEEG-NEVEGEVEGYLVIKRpwPGMARTIYGDHERyedTYFSKFPGYYFTGDGARRDEDGYY 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 435 FVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVV----RSPDSSLTEvDVQKFIETQVTY 510
Cdd:cd05966 486 WITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTlkdgEEPSDELRK-ELRKHVRKEIGP 564
|
490 500 510
....*....|....*....|....*....|.
gi 357113996 511 YKRLKRVTFVSSVPKSASGKILRREL--IAK 539
Cdd:cd05966 565 IATPDKIQFVPGLPKTRSGKIMRRILrkIAA 595
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
72-536 |
4.57e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 146.08 E-value: 4.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 72 SAVALSSRAGvRPgDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVITVAELLPKVADLRL 151
Cdd:PRK07638 39 VANWLNEKES-KN-KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTERYKLNDLPDEEG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 152 PVILLDDTAAKSGSSATLYSDLVSGVDEADYrrpptkqsdtagLLYSSGTTGESKGVVLTHRNFIAAATMVTSD----QD 227
Cdd:PRK07638 117 RVIEIDEWKRMIEKYLPTYAPIENVQNAPFY------------MGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDfhmkRE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 228 DRGEGPNVflcflpMFHifglSVITYG---QLQRGNTVVVMSGFALDTVMSAVQQHRVTHLFCVPPVMIALAKhgkAGKY 304
Cdd:PRK07638 185 DSVLIAGT------LVH----SLFLYGaisTLYVGQTVHLMRKFIPNQVLDKLETENISVMYTVPTMLESLYK---ENRV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 305 DLSSLKFIGSGAApLGKDVMEAVAKNFPDALICQGYGMTETCGIISLeYPEKGQvRQFGSTGTLVTGVEAKIVDvETLKH 384
Cdd:PRK07638 252 IENKMKIISSGAK-WEAEAKEKIKNIFPYAKLYEFYGASELSFVTAL-VDEESE-RRPNSVGRPFHNVQVRICN-EAGEE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 385 LPPNQLGEICVRGPHIMQGYFNNVQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHP 464
Cdd:PRK07638 328 VQKGEIGTVYVKSPQFFMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHP 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357113996 465 EILDAVVIPFPDAEAGEVPIAYVvrspDSSLTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:PRK07638 408 AVDEIVVIGVPDSYWGEKPVAII----KGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
60-545 |
5.20e-38 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 147.24 E-value: 5.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 60 LTFS--GLRSAILASAvaLSSRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVAstaNPLYTP------REIAKQASD- 130
Cdd:PRK05620 39 TTFAaiGARAAALAHA--LHDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVF---NPLNKQlmndqiVHIINHAEDe 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 131 ---ARARLVITVAELLPKVADLRLPVIL----LDDTAAKSGSSATLYSdLVSGVDE--ADYRRPPTKQSDTAGLLYSSGT 201
Cdd:PRK05620 114 vivADPRLAEQLGEILKECPCVRAVVFIgpsdADSAAAHMPEGIKVYS-YEALLDGrsTVYDWPELDETTAAAICYSTGT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 202 TGESKGVVLTHRN-FIAAATMVTSDQDDRGEGPNvFLCFLPMFHIFGLSViTYGQLQRGnTVVVMSGFALDT-----VMS 275
Cdd:PRK05620 193 TGAPKGVVYSHRSlYLQSLSLRTTDSLAVTHGES-FLCCVPIYHVLSWGV-PLAAFMSG-TPLVFPGPDLSAptlakIIA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 276 AVQQhRVTHlfCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFP-DALICqgYGMTETCGIISLEYP 354
Cdd:PRK05620 270 TAMP-RVAH--GVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGvDVVHV--WGMTETSPVGTVARP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 355 E---KGQVRQF--GSTGTLVTGVEAKIV-DVETLKHLPPNQlGEICVRGPHIMQGYF------NNVQATEFTIRQ----- 417
Cdd:PRK05620 345 PsgvSGEARWAyrVSQGRFPASLEYRIVnDGQVMESTDRNE-GEIQVRGNWVTASYYhspteeGGGAASTFRGEDvedan 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 418 ------GWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSP 491
Cdd:PRK05620 424 drftadGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAP 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357113996 492 DSSLTEvdvqkfiETQVTYYKRLKRV----------TFVSSVPKSASGKILRRELIAKVRSSKL 545
Cdd:PRK05620 504 GIEPTR-------ETAERLRDQLRDRlpnwmlpeywTFVDEIDKTSVGKFDKKDLRQHLADGDF 560
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
66-476 |
2.40e-37 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 146.40 E-value: 2.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 66 RSAILASAVALssraGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVAStanPLYT---PREIAKQASDARARLVITVAEL 142
Cdd:PLN02736 88 RTAIGSGLVQH----GIPKGACVGLYFINRPEWLIVDHACSAYSYVSV---PLYDtlgPDAVKFIVNHAEVAAIFCVPQT 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 143 LP-------KVADLRLPVI------LLDDTAAKSGSSATLYSDLVS-GVDEADYRRPPtKQSDTAGLLYSSGTTGESKGV 208
Cdd:PLN02736 161 LNtllsclsEIPSVRLIVVvggadePLPSLPSGTGVEIVTYSKLLAqGRSSPQPFRPP-KPEDVATICYTSGTTGTPKGV 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 209 VLTHRNFIAAATMVTSDQDdrgEGPN-VFLCFLPMFHI-----------FGLSVITYgqlqRGNTVVVMSGFAL------ 270
Cdd:PLN02736 240 VLTHGNLIANVAGSSLSTK---FYPSdVHISYLPLAHIyervnqivmlhYGVAVGFY----QGDNLKLMDDLAAlrptif 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 271 -----------DTVMSAVQQHRV--THLFcvppvMIALAKHGKA---GK-----YD---LSSLK--------FIGSGAAP 318
Cdd:PLN02736 313 csvprlynriyDGITNAVKESGGlkERLF-----NAAYNAKKQAlenGKnpspmWDrlvFNKIKaklggrvrFMSSGASP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 319 LGKDVMEAVAKNFpDALICQGYGMTETCGIISLEYPEKgqvRQFGSTGTLVTGVEAKIVDVETLKHLP---PNQLGEICV 395
Cdd:PLN02736 388 LSPDVMEFLRICF-GGRVLEGYGMTETSCVISGMDEGD---NLSGHVGSPNPACEVKLVDVPEMNYTSedqPYPRGEICV 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 396 RGPHIMQGYFNN-VQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKY-KGFQIAPAELEGLLLSHPEI------- 466
Cdd:PLN02736 464 RGPIIFKGYYKDeVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIENVYAKCKFVaqcfvyg 543
|
490
....*....|....*.
gi 357113996 467 ------LDAVVIPFPD 476
Cdd:PLN02736 544 dslnssLVAVVVVDPE 559
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
81-536 |
3.85e-37 |
|
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: 142.71 E-value: 3.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 81 GVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPreiakqaSDARARLVITVAellpkvadlrlpvillddta 160
Cdd:cd05974 21 GVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTP-------DDLRDRVDRGGA-------------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 161 aksgssatlysdLVSGVDEAdyrrppTKQSDTAGLLYSSGTTGESKGVVLTHRNFIAA--ATM---------VTSDQDDR 229
Cdd:cd05974 74 ------------VYAAVDEN------THADDPMLLYFTSGTTSKPKLVEHTHRSYPVGhlSTMywiglkpgdVHWNISSP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 230 GEGPNVFLCFLPMFHIfGLSVITYGQLQrgntvvvmsgFALDTVMSAVQQHRVThLFCVPPVMIALAKHGKAGKYDLSSL 309
Cdd:cd05974 136 GWAKHAWSCFFAPWNA-GATVFLFNYAR----------FDAKRVLAALVRYGVT-TLCAPPTVWRMLIQQDLASFDVKLR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 310 KFIGSGAaPLGKDVMEAVAKNFpDALICQGYGMTETCGIISleyPEKGQVRQFGSTGTLVTGVEAKIVDVETlkhlPPNQ 389
Cdd:cd05974 204 EVVGAGE-PLNPEVIEQVRRAW-GLTIRDGYGQTETTALVG---NSPGQPVKAGSMGRPLPGYRVALLDPDG----APAT 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 390 LGEICV-----RGPHIMQGYFNNVQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHP 464
Cdd:cd05974 275 EGEVALdlgdtRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHP 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 357113996 465 EILDAVVIPFPDAEAGEVPIAYVV------RSPDSSLtevDVQKFIETQVTYYKRLKRVTFVsSVPKSASGKILRREL 536
Cdd:cd05974 355 AVAEAAVVPSPDPVRLSVPKAFIVlragyePSPETAL---EIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRRVEL 428
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
73-536 |
3.49e-36 |
|
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: 141.45 E-value: 3.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 73 AVALSSRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVITVAELLPKVADLRLP 152
Cdd:cd05928 55 ANVLSGACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 153 VILLDDTAAKSGSSATLYSDLVSGVDEADYRRP--PTKQSDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVTSDQDDRG 230
Cdd:cd05928 135 CPSLKTKLLVSEKSRDGWLNFKELLNEASTEHHcvETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 231 EGpNVFLCFLPMfhifGLSVITYGQL----QRGNTVVV--MSGFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAgKY 304
Cdd:cd05928 215 AS-DIMWNTSDT----GWIKSAWSSLfepwIQGACVFVhhLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLS-SY 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 305 DLSSLKFIGSGAAPLGKDVMEAvAKNFPDALICQGYGMTETcGIISLEYpeKGQVRQFGSTGTLVTGVEAKIVDVETlKH 384
Cdd:cd05928 289 KFPSLQHCVTGGEPLNPEVLEK-WKAQTGLDIYEGYGQTET-GLICANF--KGMKIKPGSMGKASPPYDVQIIDDNG-NV 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 385 LPPNQLGEICVR-GPH----IMQGYFNNVQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGL 459
Cdd:cd05928 364 LPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESA 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 460 LLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPD------SSLTEvDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILR 533
Cdd:cd05928 444 LIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQflshdpEQLTK-ELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQR 522
|
...
gi 357113996 534 REL 536
Cdd:cd05928 523 NEL 525
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
35-536 |
8.68e-36 |
|
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: 139.72 E-value: 8.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 35 VDLLLRRAAACPSALALVDaaTGHALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVAST 114
Cdd:cd17646 1 HALVAEQAARTPDAPAVVD--EGRTLTYRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 115 ANPLYTPREIAKQASDARARLVITVAELLPKVADLrLPVILLDDTAAKSGSsatlysdlvsgvdeADYRRPPTKQSDTAG 194
Cdd:cd17646 78 LDPGYPADRLAYMLADAGPAVVLTTADLAARLPAG-GDVALLGDEALAAPP--------------ATPPLVPPRPDNLAY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 195 LLYSSGTTGESKGVVLTHRnfiAAATMVTSDQDDRGEGP-NVFLCFLPMfhIFGLSVIT-YGQLQRGNTVVVmsgfA--- 269
Cdd:cd17646 143 VIYTSGSTGRPKGVMVTHA---GIVNRLLWMQDEYPLGPgDRVLQKTPL--SFDVSVWElFWPLVAGARLVV----Arpg 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 270 ----LDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGkyDLSSLKFIGSGAAPLGKDVMEAVAKnFPDALICQGYGMTET 345
Cdd:cd17646 214 ghrdPAYLAALIREHGVTTCHFVPSMLRVFLAEPAAG--SCASLRRVFCSGEALPPELAARFLA-LPGAELHNLYGPTEA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 346 CGIISLEYPEKGQVRQFGSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFN--NVQATEFT---IRQG-- 418
Cdd:cd17646 291 AIDVTHWPVRGPAETPSVPIGRPVPNTRLYVLD-DALRPVPVGVPGELYLGGVQLARGYLGrpALTAERFVpdpFGPGsr 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 419 WLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPD-SSLTE 497
Cdd:cd17646 370 MYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGaAGPDT 449
|
490 500 510
....*....|....*....|....*....|....*....
gi 357113996 498 VDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd17646 450 AALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
36-538 |
2.15e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 139.43 E-value: 2.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 36 DLLLRRAAACPSALALVDAATGHALTFSGlrSAILASAVALSSRAGVRPGDSVLLvaPNCVLYPVCFFAVTALGAVASTA 115
Cdd:PRK07867 9 ELLLPLAEDDDRGLYFEDSFTSWREHIRG--SAARAAALRARLDPTRPPHVGVLL--DNTPEFSLLLGAAALSGIVPVGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 116 NPLYTPREIAKQASDARARLVITVAELLPKVADLRLPVILLD-DTAAksgssatlYSDLVSGVDEADYRRPPTKQSDTAG 194
Cdd:PRK07867 85 NPTRRGAALARDIAHADCQLVLTESAHAELLDGLDPGVRVINvDSPA--------WADELAAHRDAEPPFRVADPDDLFM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 195 LLYSSGTTGESKGVVLTHRNFIAAATMVTsdqDDRGEGP-NVFLCFLPMFH----IFGLSVitygQLQRGNTVVVMSGFA 269
Cdd:PRK07867 157 LIFTSGTSGDPKAVRCTHRKVASAGVMLA---QRFGLGPdDVCYVSMPLFHsnavMAGWAV----ALAAGASIALRRKFS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 270 LDTVMSAVQQHRVTHLFCV-PPVMIALAKHGKAGKYDlSSLKFI-GSGAAPlgKDVmEAVAKNFpDALICQGYGMTETCG 347
Cdd:PRK07867 230 ASGFLPDVRRYGATYANYVgKPLSYVLATPERPDDAD-NPLRIVyGNEGAP--GDI-ARFARRF-GCVVVDGFGSTEGGV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 348 IISLE--YPEkgqvrqfGSTGTLVTGVeaKIVDVETLKHLPPNQL------------GEIC-VRGPHIMQGYFNNVQATE 412
Cdd:PRK07867 305 AITRTpdTPP-------GALGPLPPGV--AIVDPDTGTECPPAEDadgrllnadeaiGELVnTAGPGGFEGYYNDPEADA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 413 FTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPD 492
Cdd:PRK07867 376 ERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPG 455
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 357113996 493 SSLTEVDVQKFIETQVTYYKRL--KRVTFVSSVPKSASGKILRRELIA 538
Cdd:PRK07867 456 AKFDPDAFAEFLAAQPDLGPKQwpSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
32-533 |
5.51e-35 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 141.07 E-value: 5.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 32 LSAVDLLLRRAAACPSALAL--VDAATGHALTFS----GLRSAILASAvaLSSRAGvrPGDSVLLVAPNCVLYPVCFFAV 105
Cdd:PRK05691 9 LTLVQALQRRAAQTPDRLALrfLADDPGEGVVLSyrdlDLRARTIAAA--LQARAS--FGDRAVLLFPSGPDYVAAFFGC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 106 TALGAVASTANPLYTPRE-----IAKQASDARARLVITVAELLPKVADLrlpvilldDTAAKSGSSATLYSDLVSGVDEA 180
Cdd:PRK05691 85 LYAGVIAVPAYPPESARRhhqerLLSIIADAEPRLLLTVADLRDSLLQM--------EELAAANAPELLCVDTLDPALAE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 181 DYRRPPTKQSDTAGLLYSSGTTGESKGVVLTHRNFIAAATMV------TSDQDDrgegpnVFLCFLPMFHIFGLsviTYG 254
Cdd:PRK05691 157 AWQEPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIrhgfgiDLNPDD------VIVSWLPLYHDMGL---IGG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 255 QLQ---RGNTVVVMS-GFALDTV---MSAVQQHRVT--------HLFCVPPVM-IALAKhgkagkYDLSSLKFIGSGAAP 318
Cdd:PRK05691 228 LLQpifSGVPCVLMSpAYFLERPlrwLEAISEYGGTisggpdfaYRLCSERVSeSALER------LDLSRWRVAYSGSEP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 319 LGKDVMEAVAKNF------PDALICQgYGMTETC----------GIISLE---------YPEKGQVRQFGSTGTLVTGVE 373
Cdd:PRK05691 302 IRQDSLERFAEKFaacgfdPDSFFAS-YGLAEATlfvsggrrgqGIPALEldaealarnRAEPGTGSVLMSCGRSQPGHA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 374 AKIVDVETLKHLPPNQLGEICVRGPHIMQGYFNNVQATE--FTIRQG--WLHTGDLGlFDDEGQLFVVDRLKELIKYKGF 449
Cdd:PRK05691 381 VLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAktFVEHDGrtWLRTGDLG-FLRDGELFVTGRLKDMLIVRGH 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 450 QIAPAELEGLLLSHPEIL-DAVVIPFPDAEAGEVPI---AYVVRSPDSSLTEVDVQKFIETQV--TYYKRLKRVTFVS-- 521
Cdd:PRK05691 460 NLYPQDIEKTVEREVEVVrKGRVAAFAVNHQGEEGIgiaAEISRSVQKILPPQALIKSIRQAVaeACQEAPSVVLLLNpg 539
|
570
....*....|..
gi 357113996 522 SVPKSASGKILR 533
Cdd:PRK05691 540 ALPKTSSGKLQR 551
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
60-533 |
7.56e-35 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 136.11 E-value: 7.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 60 LTFSGLRSAILASAVALSSrAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVAStanPLYT---PREIAKQASDARARLV 136
Cdd:cd05973 1 LTFGELRALSARFANALQE-LGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQ---PLFTafgPKAIEHRLRTSGARLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 137 ITVAELLPKVAdlrlpvillddtaaksgssatlysdlvsgvdeadyrrpptkqSDTAGLLYSSGTTGESKGVVLTHRNFI 216
Cdd:cd05973 77 VTDAANRHKLD------------------------------------------SDPFVMMFTSGTTGLPKGVPVPLRALA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 217 AAATMVTSDQDDRGEgpNVFLCFLPMFHIFGLSVITYGQLQRGN-TVVVMSGFALDTVMSAVQQHRVTHLFCVPPVMIAL 295
Cdd:cd05973 115 AFGAYLRDAVDLRPE--DSFWNAADPGWAYGLYYAITGPLALGHpTILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLL 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 296 AKHGKAGKYDLS-SLKFIGSGAAPLGKDVMEAVAKNFpDALICQGYGMTETCGIISLEYPEKGQVRQfGSTGTLVTGVEA 374
Cdd:cd05973 193 MAAGAEVPARPKgRLRRVSSAGEPLTPEVIRWFDAAL-GVPIHDHYGQTELGMVLANHHALEHPVHA-GSAGRAMPGWRV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 375 KIVDvETLKHLPPNQLGEICV---RGPHI-MQGYFNNVQATeftIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQ 450
Cdd:cd05973 271 AVLD-DDGDELGPGEPGRLAIdiaNSPLMwFRGYQLPDTPA---IDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYR 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 451 IAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEV---DVQKFIETQVTYYKRLKRVTFVSSVPKSA 527
Cdd:cd05973 347 IGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPAladELQLHVKKRLSAHAYPRTIHFVDELPKTP 426
|
....*.
gi 357113996 528 SGKILR 533
Cdd:cd05973 427 SGKIQR 432
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
35-542 |
1.29e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 137.05 E-value: 1.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 35 VDLLLRRAAACPSALALVDAATGHALTFSGLRSAILASAVALSSrAGVRPGDSV-LLVAPNCVLYPVCFfAVTALGAvAS 113
Cdd:PRK07768 5 TEKMYANARTSPRGMVTGEPDAPVRHTWGEVHERARRIAGGLAA-AGVGPGDAVaVLAGAPVEIAPTAQ-GLWMRGA-SL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 114 TANPLYTPR-EIAKQASDARARLvitvAELLPKVADLRLPVILLDDTAAKSGSSATLYSDLVsgvDEADYRRPPTKQSDT 192
Cdd:PRK07768 82 TMLHQPTPRtDLAVWAEDTLRVI----GMIGAKAVVVGEPFLAAAPVLEEKGIRVLTVADLL---AADPIDPVETGEDDL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 193 AGLLYSSGTTGESKGVVLTHRNFIA-AATMVTSDQDDrgEGPNVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMS--GFA 269
Cdd:PRK07768 155 ALMQLTSGSTGSPKAVQITHGNLYAnAEAMFVAAEFD--VETDVMVSWLPLFHDMGMVGFLTVPMYFGAELVKVTpmDFL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 270 LDTVMSA--VQQHRVThlfcvppvMIA------------LAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEA---VAKNF- 331
Cdd:PRK07768 233 RDPLLWAelISKYRGT--------MTAapnfayallarrLRRQAKPGAFDLSSLRFALNGAEPIDPADVEDlldAGARFg 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 332 --PDALICqGYGMTETCGIISL-----------------------EYPEKGQVRQFGSTGTLVTGVEAKIVDvETLKHLP 386
Cdd:PRK07768 305 lrPEAILP-AYGMAEATLAVSFspcgaglvvdevdadllaalrraVPATKGNTRRLATLGPPLPGLEVRVVD-EDGQVLP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 387 PNQLGEICVRGPHIMQGYFNNVQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEI 466
Cdd:PRK07768 383 PRGVGVIELRGESVTPGYLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGV 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 467 L--DAVVIPFPDAEAGEvPIAYVVRSPDSSltEVDVQKFIETQVTY--------YKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:PRK07768 463 RpgNAVAVRLDAGHSRE-GFAVAVESNAFE--DPAEVRRIRHQVAHevvaevgvRPRNVVVLGPGSIPKTPSGKLRRANA 539
|
....*.
gi 357113996 537 IAKVRS 542
Cdd:PRK07768 540 AELVTP 545
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
66-539 |
1.47e-34 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 136.79 E-value: 1.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 66 RSAILASAValsSRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVITVAELLpK 145
Cdd:cd05915 33 RARRLMGGL---RALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPNLL-P 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 146 VADLRLPVILLDDTAAKSGSSATLYSDLVSGVDEADYRRPPTKQSDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVTSD 225
Cdd:cd05915 109 LVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPVRVPERAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 226 QDDRGEGPNVFLCFLPMFHIFGLSVItYGQLQRGNTVVVMSGFALDTVM-SAVQQHRVTHLFCVPPVMIALAKHGKAGKY 304
Cdd:cd05915 189 DGTALSEKDVVLPVVPMFHVNAWCLP-YAATLVGAKQVLPGPRLDPASLvELFDGEGVTFTAGVPTVWLALADYLESTGH 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 305 DLS-SLKFIGSGAAPlgKDVMEAVaKNFPDALICQGYGMTETCGIISL--------EYPEKGQVRQFGSTGTLVTGVEAK 375
Cdd:cd05915 268 RLKtLRRLVVGGSAA--PRSLIAR-FERMGVEVRQGYGLTETSPVVVQnfvkshleSLSEEEKLTLKAKTGLPIPLVRLR 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 376 IVDVETLKhLPPN--QLGEICVRGPHIMQGYFNNVQATE-FTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIA 452
Cdd:cd05915 345 VADEEGRP-VPKDgkALGEVQLKGPWITGGYYGNEEATRsALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWIS 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 453 PAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYvVRSPDSSLTEVDVQKFIETQVTYYKRL-KRVTFVSSVPKSASGKI 531
Cdd:cd05915 424 SVDLENALMGHPKVKEAAVVAIPHPKWQERPLAV-VVPRGEKPTPEELNEHLLKAGFAKWQLpDAYVFAEEIPRTSAGKF 502
|
....*...
gi 357113996 532 lRRELIAK 539
Cdd:cd05915 503 -LKRALRE 509
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
46-536 |
1.97e-34 |
|
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: 135.86 E-value: 1.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 46 PSALALVDAAtgHALTFSGLRSAILASAVALSsRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVastanplYTPREIA 125
Cdd:cd12114 1 PDATAVICGD--GTLTYGELAERARRVAGALK-AAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAA-------YVPVDID 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 126 KQA-------SDARARLVITVAELLPKVADLRLPVILLDDTAAKSGSSATlysdlvsgvdeadyrrPPTKQSDTAGLLYS 198
Cdd:cd12114 71 QPAarreailADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPP----------------VDVAPDDLAYVIFT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 199 SGTTGESKGVVLTHRnfiaaATMVTSDQDDR----GEGPNVF----LCF-LPMFHIFGLsvitygqLQRGNTVV-VMSGF 268
Cdd:cd12114 135 SGSTGTPKGVMISHR-----AALNTILDINRrfavGPDDRVLalssLSFdLSVYDIFGA-------LSAGATLVlPDEAR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 269 ALDTV--MSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFPDA-LICQGyGMTET 345
Cdd:cd12114 203 RRDPAhwAELIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDArLISLG-GATEA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 346 cGIISLEYPEKGQVRQFGST--GTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQATE---FTIRQG-- 418
Cdd:cd12114 282 -SIWSIYHPIDEVPPDWRSIpyGRPLANQRYRVLD-PRGRDCPDWVPGELWIGGRGVALGYLGDPELTAarfVTHPDGer 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 419 WLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEV 498
Cdd:cd12114 360 LYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTPIAPD 439
|
490 500 510
....*....|....*....|....*....|....*...
gi 357113996 499 DVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd12114 440 ALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
16-536 |
5.84e-34 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 135.12 E-value: 5.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 16 VYRSLRPAARIESNPglsaVDLLLRRAAACPSALALVDaaTGHALTFSGLRSAILASAVALSsRAGVRPGDSVLLVAPNC 95
Cdd:PRK13383 23 VLRLLREASRGGTNP----YTLLAVTAARWPGRTAIID--DDGALSYRELQRATESLARRLT-RDGVAPGRAVGVMCRNG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 96 VLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVITVAELLPKVADLRLPVILLDDTAAKSGSSATlysdlvs 175
Cdd:PRK13383 96 RGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGADDAVAVIDPATAGAEESGG------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 176 gvdeadyrRPPTKQSDTAGLLySSGTTGESKGVVLTHRNFIAAATMVTSDQDDRGEGPNVFLCFLPMFHIFGLSVITYgQ 255
Cdd:PRK13383 169 --------RPAVAAPGRIVLL-TSGTTGKPKGVPRAPQLRSAVGVWVTILDRTRLRTGSRISVAMPMFHGLGLGMLML-T 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 256 LQRGNTVVVMSGFALDTVMSAVQQHRVTHLFCVPPVM---IALAKHGKAgKYDLSSLKFIGSGAAPLGKDVMEAVAKNFP 332
Cdd:PRK13383 239 IALGGTVLTHRHFDAEAALAQASLHRADAFTAVPVVLariLELPPRVRA-RNPLPQLRVVMSSGDRLDPTLGQRFMDTYG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 333 DALIcQGYGMTETcGIISLEYPekGQVRQFGST-GTLVTGVEAKIVDVETlKHLPPNQLGEICVRGPHIMQGYFNNVQAT 411
Cdd:PRK13383 318 DILY-NGYGSTEV-GIGALATP--ADLRDAPETvGKPVAGCPVRILDRNN-RPVGPRVTGRIFVGGELAGTRYTDGGGKA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 412 eftIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSP 491
Cdd:PRK13383 393 ---VVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHP 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 357113996 492 DSSLTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:PRK13383 470 GSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
61-472 |
8.91e-34 |
|
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: 135.24 E-value: 8.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 61 TFSGLRSAILASAVALSSrAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVAStanPLYT---PREIAKQASDARARLVI 137
Cdd:cd17641 13 TWADYADRVRAFALGLLA-LGVGRGDVVAILGDNRPEWVWAELAAQAIGALSL---GIYQdsmAEEVAYLLNYTGARVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 138 T--------VAELLPKVADLRLpVILLDDTAAKSGSSATL--YSDLVSGVDEADYRRP--------PTKQSDTAGLLYSS 199
Cdd:cd17641 89 AedeeqvdkLLEIADRIPSVRY-VIYCDPRGMRKYDDPRLisFEDVVALGRALDRRDPglyerevaAGKGEDVAVLCTTS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 200 GTTGESKGVVLTHRNFIA-AATMVTSDQDDRGEGpnvFLCFLPMFHIfGLSVITYGQ-LQRGNTVvvmsGF--ALDTVMS 275
Cdd:cd17641 168 GTTGKPKLAMLSHGNFLGhCAAYLAADPLGPGDE---YVSVLPLPWI-GEQMYSVGQaLVCGFIV----NFpeEPETMME 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 276 AVQQHRVTHLFCVP------------------PVMIALAKHG-----KAGKYD--------------------------- 305
Cdd:cd17641 240 DLREIGPTFVLLPPrvwegiaadvrarmmdatPFKRFMFELGmklglRALDRGkrgrpvslwlrlaswladallfrplrd 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 306 ---LSSLKFIGSGAAPLGKDVMEavaknFPDAL---ICQGYGMTETCGIISLEypEKGQVRqFGSTGTLVTGVEAKIVDV 379
Cdd:cd17641 320 rlgFSRLRSAATGGAALGPDTFR-----FFHAIgvpLKQLYGQTELAGAYTVH--RDGDVD-PDTVGVPFPGTEVRIDEV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 380 etlkhlppnqlGEICVRGPHIMQGYFNNVQATEFTIRQ-GWLHTGDLGLFDDEGQLFVVDRLKELIK-YKGFQIAPAELE 457
Cdd:cd17641 392 -----------GEILVRSPGVFVGYYKNPEATAEDFDEdGWLHTGDAGYFKENGHLVVIDRAKDVGTtSDGTRFSPQFIE 460
|
490
....*....|....*
gi 357113996 458 GLLLSHPEILDAVVI 472
Cdd:cd17641 461 NKLKFSPYIAEAVVL 475
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
36-536 |
1.76e-33 |
|
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: 132.44 E-value: 1.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 36 DLLLRRAAACPSALALVDAAtgHALTFSGL--RSAILASAVAlssRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVAS 113
Cdd:cd12115 3 DLVEAQAARTPDAIALVCGD--ESLTYAELnrRANRLAARLR---AAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 114 TANPLYTPREIAKQASDARARLVITVAEllpkvadlrlpvillddtaaksgssatlysdlvsgvdeadyrrpptkqsDTA 193
Cdd:cd12115 78 PLDPAYPPERLRFILEDAQARLVLTDPD-------------------------------------------------DLA 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 194 GLLYSSGTTGESKGVVLTHRNFIA----AATMVTSDQDdRGEGPNVFLCF-LPMFHIFG-LSVitygqlqrGNTVVVMSG 267
Cdd:cd12115 109 YVIYTSGSTGRPKGVAIEHRNAAAflqwAAAAFSAEEL-AGVLASTSICFdLSVFELFGpLAT--------GGKVVLADN 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 268 fALDTVMSAVQQhRVTHLFCVPPVMIALAKHGKAGKydlsSLKFIGSGAAPLGKDVMEAVAKNFPDALICQGYGMTETCG 347
Cdd:cd12115 180 -VLALPDLPAAA-EVTLINTVPSAAAELLRHDALPA----SVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTT 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 348 IISLEYPEKGQVRQFgSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTIRQGWLH------ 421
Cdd:cd12115 254 YSTVAPVPPGASGEV-SIGRPLANTQAYVLD-RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarly 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 422 -TGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDV 500
Cdd:cd12115 332 rTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDL 411
|
490 500 510
....*....|....*....|....*....|....*.
gi 357113996 501 QKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd12115 412 RRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
195-530 |
3.26e-33 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 130.19 E-value: 3.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 195 LLYSSGTTGESKGVVLTHRNF---------IAAATMVTSDQDDR---GEGPNVFLCFLPMFHifGLSVITYGQLQRGNTV 262
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIfrmlmggadFGTGEFTPSEDAHKaaaAAAGTVMFPAPPLMH--GTGSWTAFGGLLGGQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 263 VVMSG--FALDTVMSAVQQHRVTHLFCVPPVMIA--LAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFPDALICQ 338
Cdd:cd05924 86 VVLPDdrFDPEEVWRTIEKHKVTSMTIVGDAMARplIDALRDAGPYDLSSLFAISSGGALLSPEVKQGLLELVPNITLVD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 339 GYGMTETCGI---ISLEYPEKGQVRQFGSTGTLVtgveakiVDvETLKHLPPNQ--LGEICVRGpHIMQGYFNNVQATEF 413
Cdd:cd05924 166 AFGSSETGFTgsgHSAGSGPETGPFTRANPDTVV-------LD-DDGRVVPPGSggVGWIARRG-HIPLGYYGDEAKTAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 414 TIR----QGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVR 489
Cdd:cd05924 237 TFPevdgVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQL 316
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 357113996 490 SPDSSLTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGK 530
Cdd:cd05924 317 REGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
59-533 |
8.68e-33 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 132.44 E-value: 8.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 59 ALTFSGLRsailASAVALSSR---AGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVAStANPLYTP---RE-----IAKQ 127
Cdd:PRK09192 49 ALPYQTLR----ARAEAGARRllaLGLKPGDRVALIAETDGDFVEAFFACQYAGLVPV-PLPLPMGfggREsyiaqLRGM 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 128 ASDARARLVITVAELLPKVADlrlpvILLDDTAAKSGSSATLYSdlvsgVDEADYRRPPTKQSDTAGLLYSSGTTGESKG 207
Cdd:PRK09192 124 LASAQPAAIITPDELLPWVNE-----ATHGNPLLHVLSHAWFKA-----LPEADVALPRPTPDDIAYLQYSSGSTRFPRG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 208 VVLTHRNFIAAATMVTSD-----QDDRGegpnvfLCFLPMFHIFGL-----SVITyGQL--------------------- 256
Cdd:PRK09192 194 VIITHRALMANLRAISHDglkvrPGDRC------VSWLPFYHDMGLvgfllTPVA-TQLsvdylptrdfarrplqwldli 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 257 --QRGnTVVVMSGFALDTVMSAVQQHRVTHLfcvppvmialakhgkagkyDLSSLKFIGSGAAPLGKDVMEAVAKNFPDA 334
Cdd:PRK09192 267 srNRG-TISYSPPFGYELCARRVNSKDLAEL-------------------DLSCWRVAGIGADMIRPDVLHQFAEAFAPA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 335 -------LICqgYGMTET----------CGIIS-------LEY--------PEKGQVRQFGSTGTLVTGVEAKIVDvETL 382
Cdd:PRK09192 327 gfddkafMPS--YGLAEAtlavsfsplgSGIVVeevdrdrLEYqgkavapgAETRRVRTFVNCGKALPGHEIEIRN-EAG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 383 KHLPPNQLGEICVRGPHIMQGYFNNVQATEFTIRQGWLHTGDLGlFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLS 462
Cdd:PRK09192 404 MPLPERVVGHICVRGPSLMSGYFRDEESQDVLAADGWLDTGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQ 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 463 HPEILDAVVIPFP-DAEAGEVPIAYV-VRSPDssltEVDVQKFIEtQVTyyKRLKRVTFVS---------SVPKSASGKI 531
Cdd:PRK09192 483 EPELRSGDAAAFSiAQENGEKIVLLVqCRISD----EERRGQLIH-ALA--ALVRSEFGVEaavelvpphSLPRTSSGKL 555
|
..
gi 357113996 532 LR 533
Cdd:PRK09192 556 SR 557
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
109-538 |
3.40e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 130.15 E-value: 3.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 109 GAVASTANPLYTPREIAKQASDARARLVITVAELLPKVADLRLP--VILLDDTAAksgssatlYSDLVSGVDEADYRRPP 186
Cdd:PRK13388 76 GYVLVGLNTTRRGAALAADIRRADCQLLVTDAEHRPLLDGLDLPgvRVLDVDTPA--------YAELVAAAGALTPHREV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 187 TKqSDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVTS----DQDDrgegpnVFLCFLPMFH----IFGLSVItygqLQR 258
Cdd:PRK13388 148 DA-MDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTErfglTRDD------VCYVSMPLFHsnavMAGWAPA----VAS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 259 GNTVVVMSGFALDTVMSAVQQHRVTHLFCVppvmialakhGKAGKYDLSS------------LKFiGSGAAPlgKDVmEA 326
Cdd:PRK13388 217 GAAVALPAKFSASGFLDDVRRYGATYFNYV----------GKPLAYILATperpddadnplrVAF-GNEASP--RDI-AE 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 327 VAKNFpDALICQGYGMTETCGIISLE--YPEkgqvrqfGSTGTLVTGVEakIVDVETLKHLPPNQL-------------G 391
Cdd:PRK13388 283 FSRRF-GCQVEDGYGSSEGAVIVVREpgTPP-------GSIGRGAPGVA--IYNPETLTECAVARFdahgallnadeaiG 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 392 EICVR-GPHIMQGYFNNVQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAV 470
Cdd:PRK13388 353 ELVNTaGAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVA 432
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357113996 471 VIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQ----VTYYKRLKRVTfvSSVPKSASGKILRRELIA 538
Cdd:PRK13388 433 VYAVPDERVGDQVMAALVLRDGATFDPDAFAAFLAAQpdlgTKAWPRYVRIA--ADLPSTATNKVLKRELIA 502
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
34-538 |
4.74e-32 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 130.45 E-value: 4.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 34 AVDlllRRAAACPSALALVDAAT----GHALTFSGLRSAILASAVALSSrAGVRPGDSVLLVAPncvLYPVCFFAVTA-- 107
Cdd:PRK10524 58 AVD---RHLAKRPEQLALIAVSTetdeERTYTFRQLHDEVNRMAAMLRS-LGVQRGDRVLIYMP---MIAEAAFAMLAca 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 108 -LGAVASTANPLYTPREIAKQASDARARLVITVAellpkvADLR----LPVILLDDTA---AKSGSSATLYSD------- 172
Cdd:PRK10524 131 rIGAIHSVVFGGFASHSLAARIDDAKPVLIVSAD------AGSRggkvVPYKPLLDEAialAQHKPRHVLLVDrglapma 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 173 LVSG--VDEADYRR-------PPT--KQSDTAGLLYSSGTTGESKGVvlthrnfiaaatmvtsdQDDRGeGPNVFLCfLP 241
Cdd:PRK10524 205 RVAGrdVDYATLRAqhlgarvPVEwlESNEPSYILYTSGTTGKPKGV-----------------QRDTG-GYAVALA-TS 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 242 MFHIF------------------GLSVITYGQLQRGNTVVVMSGFAL--DTVM--SAVQQHRVTHLFCVPPVMIALAKHG 299
Cdd:PRK10524 266 MDTIFggkagetffcasdigwvvGHSYIVYAPLLAGMATIMYEGLPTrpDAGIwwRIVEKYKVNRMFSAPTAIRVLKKQD 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 300 KA--GKYDLSSLKFIGSGAAPLGkdvmEAVAKNFPDAL---ICQGYGMTETcG--IISLEYPEKGQVRQFGSTGTLVTGV 372
Cdd:PRK10524 346 PAllRKHDLSSLRALFLAGEPLD----EPTASWISEALgvpVIDNYWQTET-GwpILAIARGVEDRPTRLGSPGVPMYGY 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 373 EAKIVDVETLKHLPPNQLGEICVRGP--------------HIMQGYFNNVQATEFTirqgwlhTGDLGLFDDEGQLFVVD 438
Cdd:PRK10524 421 NVKLLNEVTGEPCGPNEKGVLVIEGPlppgcmqtvwgdddRFVKTYWSLFGRQVYS-------TFDWGIRDADGYYFILG 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 439 RLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVV-RSPDSSLT-------EVDVQKFIETQVTY 510
Cdd:PRK10524 494 RTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVpKDSDSLADrearlalEKEIMALVDSQLGA 573
|
570 580
....*....|....*....|....*...
gi 357113996 511 YKRLKRVTFVSSVPKSASGKILRRELIA 538
Cdd:PRK10524 574 VARPARVWFVSALPKTRSGKLLRRAIQA 601
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
41-536 |
4.81e-32 |
|
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: 128.98 E-value: 4.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 41 RAAACPSALALVdaATGHALTFSGL--RSAILASAValssRA-GVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANP 117
Cdd:cd17655 6 QAEKTPDHTAVV--FEDQTLTYRELneRANQLARTL----REkGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 118 LYTPREIAKQASDARARLVITVAELLPKVADLRLpVILLDDTAAKSGSSATLysdlvsgvdeadyrRPPTKQSDTAGLLY 197
Cdd:cd17655 80 DYPEERIQYILEDSGADILLTQSHLQPPIAFIGL-IDLLDEDTIYHEESENL--------------EPVSKSDDLAYVIY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 198 SSGTTGESKGVVLTHR---NFIAAA--TMVTSDQDDrgegpnvFLCFLPMfhIFGLSVIT-YGQLQRGNTVVVMSGFAL- 270
Cdd:cd17655 145 TSGSTGKPKGVMIEHRgvvNLVEWAnkVIYQGEHLR-------VALFASI--SFDASVTEiFASLLSGNTLYIVRKETVl 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 271 --DTVMSAVQQHRVTHLFCVPPVMIALAKhgkAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFPDA-LICQGYGMTETCG 347
Cdd:cd17655 216 dgQALTQYIRQNRITIIDLTPAHLKLLDA---ADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNpTITNAYGPTETTV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 348 IISLEYPEKGQVRQFG-STGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQATE-------FTIRQGW 419
Cdd:cd17655 293 DASIYQYEPETDQQVSvPIGKPLGNTRIYILD-QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAekfvddpFVPGERM 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 420 LHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDssLTEVD 499
Cdd:cd17655 372 YRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKE--LPVAQ 449
|
490 500 510
....*....|....*....|....*....|....*..
gi 357113996 500 VQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd17655 450 LREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
80-476 |
5.48e-32 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 130.71 E-value: 5.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 80 AGVRPGDSVLLVAPNCvlyPVCFFAVTALGAVASTANPLYT---PREIAKQASDARARLVIT----VAELL-PKVADL-R 150
Cdd:PLN02430 96 SGAEPGSRVGIYGSNC---PQWIVAMEACAAHSLICVPLYDtlgPGAVDYIVDHAEIDFVFVqdkkIKELLePDCKSAkR 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 151 LPVIL--------LDDTAAKSGSSATLYSDLVSGVDEADYRRPPTKQSDTAGLLYSSGTTGESKGVVLTHRnfiAAATMV 222
Cdd:PLN02430 173 LKAIVsftsvteeESDKASQIGVKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHE---AVATFV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 223 TS-----DQ-DDRGEGPNVFLCFLPMFHIFGLSVITYGqLQRGNTVVVMSGfALDTVMSAVQQHRVTHLFCVPPV----- 291
Cdd:PLN02430 250 RGvdlfmEQfEDKMTHDDVYLSFLPLAHILDRMIEEYF-FRKGASVGYYHG-DLNALRDDLMELKPTLLAGVPRVferih 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 292 ----------------------------MIALAKHGKAGKY-DL-----------SSLKFIGSGAAPLGKDVmEAVAKNF 331
Cdd:PLN02430 328 egiqkalqelnprrrlifnalykyklawMNRGYSHKKASPMaDFlafrkvkaklgGRLRLLISGGAPLSTEI-EEFLRVT 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 332 PDALICQGYGMTETCGIISLEYPEkgQVRQFGSTGTLVTGVEAKIVDVETLKHLP--PNQLGEICVRGPHIMQGYFNNVQ 409
Cdd:PLN02430 407 SCAFVVQGYGLTETLGPTTLGFPD--EMCMLGTVGAPAVYNELRLEEVPEMGYDPlgEPPRGEICVRGKCLFSGYYKNPE 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 410 ATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKY-KGFQIAPAELEGLLLSHPEILD-------------AVVIPFP 475
Cdd:PLN02430 485 LTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLsQGEYVALEYLENVYGQNPIVEDiwvygdsfksmlvAVVVPNE 564
|
.
gi 357113996 476 D 476
Cdd:PLN02430 565 E 565
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
195-457 |
3.53e-31 |
|
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: 127.86 E-value: 3.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 195 LLYSSGTTGESKGVVLTHRN--FIAAATMVTSDQDDRGEGPNVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGFALD- 271
Cdd:cd05933 155 LIYTSGTTGMPKGVMLSHDNitWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIWLPIKVGGQVYFAQPDALKg 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 272 TVMSAVQQHRVTHLFCVPPV---------------------MIALAK---------------HGKAGKYDLSSL------ 309
Cdd:cd05933 235 TLVKTLREVRPTAFMGVPRVwekiqekmkavgaksgtlkrkIASWAKgvgletnlklmggesPSPLFYRLAKKLvfkkvr 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 310 KFIG--------SGAAPLGKDVMEA-VAKNFPdalICQGYGMTETCGIISLEYPekgQVRQFGSTGTLVTGVEAKIVDVE 380
Cdd:cd05933 315 KALGldrcqkffTGAAPISRETLEFfLSLNIP---IMELYGMSETSGPHTISNP---QAYRLLSCGKALPGCKTKIHNPD 388
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 357113996 381 TlkhlppNQLGEICVRGPHIMQGYFNNVQATEFTI-RQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQ-IAPAELE 457
Cdd:cd05933 389 A------DGIGEICFWGRHVFMGYLNMEDKTEEAIdEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGEnVPPVPIE 461
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
33-545 |
7.21e-30 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 123.19 E-value: 7.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 33 SAVDLLLRRAAACPSALALVDAATGHALTFSGLRSAILASAVALSSRAgVRPGDSVLLVAPNCvlyPVCFFAVTA---LG 109
Cdd:PRK05857 15 TVLDRVFEQARQQPEAIALRRCDGTSALRYRELVAEVGGLAADLRAQS-VSRGSRVLVISDNG---PETYLSVLAcakLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 110 AVASTANPLYTPREIAK--QASDARARLVI----TVAELLPKVADlRLPVILLDDTAAKSGSSATLYSDLVSGvdeadyr 183
Cdd:PRK05857 91 AIAVMADGNLPIAAIERfcQITDPAAALVApgskMASSAVPEALH-SIPVIAVDIAAVTRESEHSLDAASLAG------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 184 RPPTKQSDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVtsdqddRGEGPN--------VFLCFLPMFHIFGLSVITYGq 255
Cdd:PRK05857 163 NADQGSEDPLAMIFTSGTTGEPKAVLLANRTFFAVPDIL------QKEGLNwvtwvvgeTTYSPLPATHIGGLWWILTC- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 256 LQRGNTVVVmSGFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAA-PLGKDVMEAVAKNFPDA 334
Cdd:PRK05857 236 LMHGGLCVT-GGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGSrAIAADVRFIEATGVRTA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 335 licQGYGMTETcGIISLEYP-EKGQVRQF--GSTGTLVTGVEAKIVDVE-----TLKHLPPNQLGEICVRGPHIMQGYFN 406
Cdd:PRK05857 315 ---QVYGLSET-GCTALCLPtDDGSIVKIeaGAVGRPYPGVDVYLAATDgigptAPGAGPSASFGTLWIKSPANMLGYWN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 407 NVQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAY 486
Cdd:PRK05857 391 NPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLA 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 357113996 487 VVRSpdsslTEVDVQKFIETQVTYYKRLKR----------VTFVSSVPKSASGKILRRELIAKVRSSKL 545
Cdd:PRK05857 471 VVAS-----AELDESAARALKHTIAARFRResepmarpstIVIVTDIPRTQSGKVMRASLAAAATADKA 534
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
46-536 |
7.31e-29 |
|
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: 119.33 E-value: 7.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 46 PSALALVDAatGHALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIA 125
Cdd:cd17643 1 PEAVAVVDE--DRRLTYGELDARANRLARTLRAE-GVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 126 KQASDARARLVITVAEllpkvadlrlpvillddtaaksgssatlysdlvsgvdeadyrrpptkqsDTAGLLYSSGTTGES 205
Cdd:cd17643 78 FILADSGPSLLLTDPD-------------------------------------------------DLAYVIYTSGSTGRP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 206 KGVVLTHRNFIA--AAT---MVTSDQDDrgegpnvflcfLPMFH--IFGLSVI-TYGQLQRGNTVVVMSgfaLDTVMSA- 276
Cdd:cd17643 109 KGVVVSHANVLAlfAATqrwFGFNEDDV-----------WTLFHsyAFDFSVWeIWGALLHGGRLVVVP---YEVARSPe 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 277 -----VQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFPD--ALICQGYGMTETC--- 346
Cdd:cd17643 175 dfarlLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLdrPQLVNMYGITETTvhv 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 347 --GIISLEYPEKGQVrqfGSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFN--NVQATEFTIRQGWL-- 420
Cdd:cd17643 255 tfRPLDAADLPAAAA---SPIGRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAGVARGYLGrpELTAERFVANPFGGpg 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 421 ----HTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLT 496
Cdd:cd17643 331 srmyRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAAD 410
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 357113996 497 EVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd17643 411 IAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
81-464 |
3.36e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 119.31 E-value: 3.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 81 GVRPGDSVLLVAPNCVLYPVCFFAVTALGAVAST--ANP-----LYTPREIAKQASDARARLVITVAELLPKVADLRLPV 153
Cdd:PTZ00216 142 GLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATvyANLgedalAYALRETECKAIVCNGKNVPNLLRLMKSGGMPNTTI 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 154 ILLDDTAAKSGS-SATLYS--DLVS-GVDEADYR--RPPTKQSDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVtsdqD 227
Cdd:PTZ00216 222 IYLDSLPASVDTeGCRLVAwtDVVAkGHSAGSHHplNIPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILAL----E 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 228 DR----------GEgpnVFLCFLPMFHIFGLSVITYgQLQRGNTV------VVMSGFA--------------------LD 271
Cdd:PTZ00216 298 DRlndligppeeDE---TYCSYLPLAHIMEFGVTNI-FLARGALIgfgsprTLTDTFArphgdltefrpvfligvpriFD 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 272 TVMSAVQQHrvthlfcVPPV---------------MIALakhgKAGK---------YDL------SSLKFIGSGAAPLGK 321
Cdd:PTZ00216 374 TIKKAVEAK-------LPPVgslkrrvfdhayqsrLRAL----KEGKdtpywnekvFSApravlgGRVRAMLSGGGPLSA 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 322 DVMEAVAKNFpdALICQGYGMTET--CGII----SLEYpekgqvrqfGSTGTLVTGVEAKIVDVETLKHL-PPNQLGEIC 394
Cdd:PTZ00216 443 ATQEFVNVVF--GMVIQGWGLTETvcCGGIqrtgDLEP---------NAVGQLLKGVEMKLLDTEEYKHTdTPEPRGEIL 511
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357113996 395 VRGPHIMQGYFNNVQATEFTI-RQGWLHTGDLGLFDDEGQLFVVDRLKELIK-YKGFQIAPAELEGLLLSHP 464
Cdd:PTZ00216 512 LRGPFLFKGYYKQEELTREVLdEDGWFHTGDVGSIAANGTLRIIGRVKALAKnCLGEYIALEALEALYGQNE 583
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
52-531 |
3.97e-28 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 119.69 E-value: 3.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 52 VDAATGHALTFSGL--RSAILASAValssRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQAS 129
Cdd:PRK06814 651 VEDPVNGPLTYRKLltGAFVLGRKL----KKNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACK 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 130 DARARLVITV------AELLPKVADLR--LPVILLDDTAAKSGSSATLYSDLVSGVDEADYRRPptKQSDTAGLLYSSGT 201
Cdd:PRK06814 727 AAQVKTVLTSrafiekARLGPLIEALEfgIRIIYLEDVRAQIGLADKIKGLLAGRFPLVYFCNR--DPDDPAVILFTSGS 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 202 TGESKGVVLTHRNFIAAATMVTSdQDDRGEGPNVFlCFLPMFHIFGLSVitygqlqrGNTVVVMSGFAL---------DT 272
Cdd:PRK06814 805 EGTPKGVVLSHRNLLANRAQVAA-RIDFSPEDKVF-NALPVFHSFGLTG--------GLVLPLLSGVKVflypsplhyRI 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 273 VMSAVQQHRVTHLFCVPPVMIALAKHgkAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFpDALICQGYGMTETCGIISLE 352
Cdd:PRK06814 875 IPELIYDTNATILFGTDTFLNGYARY--AHPYDFRSLRYVFAGAEKVKEETRQTWMEKF-GIRILEGYGVTETAPVIALN 951
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 353 YPekgQVRQFGSTGTLVTGVEAKIVDVETLkhlppNQLGEICVRGPHIMQGYF---NN--VQATEftirQGWLHTGDLGL 427
Cdd:PRK06814 952 TP---MHNKAGTVGRLLPGIEYRLEPVPGI-----DEGGRLFVRGPNVMLGYLraeNPgvLEPPA----DGWYDTGDIVT 1019
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 428 FDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEvPIAYVVRSPDssLTEVDVQKFIET- 506
Cdd:PRK06814 1020 IDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGE-RIILLTTASD--ATRAAFLAHAKAa 1096
|
490 500
....*....|....*....|....*
gi 357113996 507 QVTYYKRLKRVTFVSSVPKSASGKI 531
Cdd:PRK06814 1097 GASELMVPAEIITIDEIPLLGTGKI 1121
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
187-466 |
2.75e-27 |
|
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: 114.87 E-value: 2.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 187 TKQSDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVTSDQDDRGEGpnVFLCFLPMFHIFGLSVitygqlqrGNTVVV-- 264
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGE--VDLATFPLFALFGPAL--------GLTSVIpd 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 265 MSGFALDT-----VMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFPD-ALICQ 338
Cdd:cd05910 152 MDPTRPARadpqkLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLSDeAEILT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 339 GYGMTETCGIISLE----------YPEKGQvrqfGS-TGTLVTGVEAKIVDV--------ETLKHLPPNQLGEICVRGPH 399
Cdd:cd05910 232 PYGATEALPVSSIGsrellatttaATSGGA----GTcVGRPIPGVRVRIIEIddepiaewDDTLELPRGEIGEITVTGPT 307
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357113996 400 IMQGYFNNVQATEFT----IRQGWLH-TGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEI 466
Cdd:cd05910 308 VTPTYVNRPVATALAkiddNSEGFWHrMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGV 379
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
60-473 |
3.64e-27 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 116.09 E-value: 3.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 60 LTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCvlyPVCFFAVTALGAVASTANPLYT---PREIAKQASDARARLV 136
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSR-GVNPGDRCGIYGSNC---PEWIIAMEACNSQGITYVPLYDtlgANAVEFIINHAEVSIA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 137 I-------TVAELLPKVADLRLPVILLDDTAAKSGSSA-----TLYS-DLVSGVDEADYRRPPTKQSDTAGLLYSSGTTG 203
Cdd:PLN02861 154 FvqeskisSILSCLPKCSSNLKTIVSFGDVSSEQKEEAeelgvSCFSwEEFSLMGSLDCELPPKQKTDICTIMYTSGTTG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 204 ESKGVVLTHRNFIAAatMVTSDQ-----DDRGEGPNVFLCFLPMFHIFGLSVITYGqLQRGNTVVVMSGfALDTVMSAVQ 278
Cdd:PLN02861 234 EPKGVILTNRAIIAE--VLSTDHllkvtDRVATEEDSYFSYLPLAHVYDQVIETYC-ISKGASIGFWQG-DIRYLMEDVQ 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 279 QHRVThLFC-VPPV----------------MIALAKHGKAGKYDLSSLK-----------------------------FI 312
Cdd:PLN02861 310 ALKPT-IFCgVPRVydriytgimqkissggMLRKKLFDFAYNYKLGNLRkglkqeeasprldrlvfdkikeglggrvrLL 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 313 GSGAAPLGKDVmEAVAKNFPDALICQGYGMTETCG----IISLEYPekgqvrQFGSTGTLVTGVEAKIVDV-----ETLK 383
Cdd:PLN02861 389 LSGAAPLPRHV-EEFLRVTSCSVLSQGYGLTESCGgcftSIANVFS------MVGTVGVPMTTIEARLESVpemgyDALS 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 384 HLPPnqlGEICVRGPHIMQGYFNNVQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKY-KGFQIAPAELEGLLLS 462
Cdd:PLN02861 462 DVPR---GEICLRGNTLFSGYHKRQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLsQGEYVAVENLENTYSR 538
|
490 500
....*....|....*....|....
gi 357113996 463 HPEI-------------LDAVVIP 473
Cdd:PLN02861 539 CPLIasiwvygnsfesfLVAVVVP 562
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
46-536 |
5.85e-27 |
|
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: 113.93 E-value: 5.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 46 PSALALVDAatGHALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYtPRE-I 124
Cdd:cd12116 1 PDATAVRDD--DRSLSYAELDERANRLAARLRAR-GVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDY-PADrL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 125 AKQASDARARLVITVAELlPKVADLRLPVILLDDTAAKSGSSAtlysdlvsgvdeadyRRPPTKQSDTAGLLYSSGTTGE 204
Cdd:cd12116 77 RYILEDAEPALVLTDDAL-PDRLPAGLPVLLLALAAAAAAPAA---------------PRTPVSPDDLAYVIYTSGSTGR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 205 SKGVVLTHRNFIAaatMVTSDQDDRGEGPNVFLCFL--PMFHIFGLSVitYGQLQRGNTVVVMSGfalDTVMSA------ 276
Cdd:cd12116 141 PKGVVVSHRNLVN---FLHSMRERLGLGPGDRLLAVttYAFDISLLEL--LLPLLAGARVVIAPR---ETQRDPealarl 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 277 VQQHRVTHLFCVPPVMIALAkhgKAGKYDLSSLKFIGSGaaplgkdvmEAVAKNFPDALICQG------YGMTETC--GI 348
Cdd:cd12116 213 IEAHSITVMQATPATWRMLL---DAGWQGRAGLTALCGG---------EALPPDLAARLLSRVgslwnlYGPTETTiwST 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 349 ISLEYPEKGQVrqfgSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQATE--------FTIRQGWL 420
Cdd:cd12116 281 AARVTAAAGPI----PIGRPLANTQVYVLD-AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAerfvpdpfAGPGSRLY 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 421 HTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVpIAYVVRSPDSSLTEVDV 500
Cdd:cd12116 356 RTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRL-VAYVVLKAGAAPDAAAL 434
|
490 500 510
....*....|....*....|....*....|....*.
gi 357113996 501 QKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd12116 435 RAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
182-533 |
5.97e-27 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 115.22 E-value: 5.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 182 YRRPPTKQSDTAGLLYSSGTTGESKGVVLTHRNFIAA-----ATMVTSDQddrgegPNVFLCFLPM----FHIFglsviT 252
Cdd:PTZ00237 246 YEYVPVESSHPLYILYTSGTTGNSKAVVRSNGPHLVGlkyywRSIIEKDI------PTVVFSHSSIgwvsFHGF-----L 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 253 YGQLQRGNTVVVMSGFAL------DTVMSAVQQHRVTHLFCVPPVMIALAKHGKAG-----KYDLSSLKFIGSGAAPLGK 321
Cdd:PTZ00237 315 YGSLSLGNTFVMFEGGIIknkhieDDLWNTIEKHKVTHTLTLPKTIRYLIKTDPEAtiirsKYDLSNLKEIWCGGEVIEE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 322 DVMEAVAKNfpdaLICQ---GYGMTETcGIISLeYPEKGQVRQFGSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGP 398
Cdd:PTZ00237 395 SIPEYIENK----LKIKssrGYGQTEI-GITYL-YCYGHINIPYNATGVPSIFIKPSILS-EDGKELNVNEIGEVAFKLP 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 399 ----HIMQGYFNNVQATE-FTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIP 473
Cdd:PTZ00237 468 mppsFATTFYKNDEKFKQlFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIG 547
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357113996 474 FPDAEAGEVPIAYVVRSPDSSLTEVDVQKF-------IETQVTYYKRLKRVTFVSSVPKSASGKILR 533
Cdd:PTZ00237 548 IYDPDCYNVPIGLLVLKQDQSNQSIDLNKLkneinniITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
46-536 |
7.46e-27 |
|
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: 113.12 E-value: 7.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 46 PSALALVDAatGHALTFSGL--RSAILASAVAlssRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPRE 123
Cdd:cd17652 1 PDAPAVVFG--DETLTYAELnaRANRLARLLA---ARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 124 IAKQASDARARLVITVAEllpkvadlrlpvillddtaaksgssatlysdlvsgvdeadyrrpptkqsDTAGLLYSSGTTG 203
Cdd:cd17652 76 IAYMLADARPALLLTTPD-------------------------------------------------NLAYVIYTSGSTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 204 ESKGVVLTHRNfIAAATMVTSDQDDRGEGPNVFLCFLPMFHIFGLSVItyGQLQRGNTVVVMSGFAL---DTVMSAVQQH 280
Cdd:cd17652 107 RPKGVVVTHRG-LANLAAAQIAAFDVGPGSRVLQFASPSFDASVWELL--MALLAGATLVLAPAEELlpgEPLADLLREH 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 281 RVTHLFCVPPVMIALAKHgkagkyDLSSLKFIGSG--AAPLgkdvmEAVAKNFPDALICQGYGMTET--CGIISLEYPEK 356
Cdd:cd17652 184 RITHVTLPPAALAALPPD------DLPDLRTLVVAgeACPA-----ELVDRWAPGRRMINAYGPTETtvCATMAGPLPGG 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 357 GQVrqfgSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQATE-------FTIRQGWLH-TGDLGLF 428
Cdd:cd17652 253 GVP----PIGRPVPGTRVYVLD-ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAerfvadpFGAPGSRMYrTGDLARW 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 429 DDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQV 508
Cdd:cd17652 328 RADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERL 407
|
490 500
....*....|....*....|....*...
gi 357113996 509 TYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd17652 408 PGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
36-537 |
9.46e-27 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 112.79 E-value: 9.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 36 DLLLRRAAACPSALALVDAatGHALTFSGLRSAilASAVALS-SRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVast 114
Cdd:cd17653 1 DAFERIAAAHPDAVAVESL--GGSLTYGELDAA--SNALANRlLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 115 anplYTPREIAKqasdARARLVITVaellpkvadlrlpvillddtaakSGSSATLysdLVSgvdeadyrrpPTKQSDTAG 194
Cdd:cd17653 74 ----YVPLDAKL----PSARIQAIL-----------------------RTSGATL---LLT----------TDSPDDLAY 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 195 LLYSSGTTGESKGVVLTHRNfIAAATMVTSDQDDRGEGPNVFLCFLPMFHIFGLSVitYGQLQRGNTVVVMSgfALDTVM 274
Cdd:cd17653 110 IIFTSGSTGIPKGVMVPHRG-VLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEI--FSTLCNGGTLVLAD--PSDPFA 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 275 SAVQQhrVTHLFCVPPVMIALAKHgkagkyDLSSLKFIGSGAAPLGKDVMEAVAKNfpdALICQGYGMTETCGIISLEYP 354
Cdd:cd17653 185 HVART--VDALMSTPSILSTLSPQ------DFPNLKTIFLGGEAVPPSLLDRWSPG---RRLYNAYGPTECTISSTMTEL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 355 EKGQVRQFGSTgtlVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQAT-----EFTIRQGWLH--TGDLGL 427
Cdd:cd17653 254 LPGQPVTIGKP---IPNSTCYILD-ADLQPVPEGVVGEICISGVQVARGYLGNPALTaskfvPDPFWPGSRMyrTGDYGR 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 428 FDDEGQLFVVDRLKELIKYKGFQIA-PAELEGLLLSHPEILDAVVIpfpdaEAGEVPIAYVVrsPDSSLTEvDVQKFIET 506
Cdd:cd17653 330 WTEDGGLEFLGREDNQVKVRGFRINlEEIEEVVLQSQPEVTQAAAI-----VVNGRLVAFVT--PETVDVD-GLRSELAK 401
|
490 500 510
....*....|....*....|....*....|.
gi 357113996 507 QVTYYKRLKRVTFVSSVPKSASGKILRRELI 537
Cdd:cd17653 402 HLPSYAVPDRIIALDSFPLTANGKVDRKALR 432
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
25-463 |
1.25e-26 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 113.76 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 25 RIESNPGLSAVDLLLRRAAACPSALALVDAATGhALTFSGLRSAILASAVALSSRagvrPGDSVLLVAPNCVLYPVCFFA 104
Cdd:PRK06334 12 RGKLRSGKTVLESFLKLCSEMTTATVCWDEQLG-KLSYNQVRKAVIALATKVSKY----PDQHIGIMMPASAGAYIAYFA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 105 VTALGAVASTANPLYTPREIAKQASDARARLVITVAELLPKVA-----DLRLPVILLD-DTAAKSGS-----SATLYSDL 173
Cdd:PRK06334 87 TLLSGKIPVMINWSQGLREVTACANLVGVTHVLTSKQLMQHLAqthgeDAEYPFSLIYmEEVRKELSfwekcRIGIYMSI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 174 ----------VSGVDeadyrrpptkQSDTAGLLYSSGTTGESKGVVLTHRNFI----AAATMVTSDQDDrgegpnVFLCF 239
Cdd:PRK06334 167 pfewlmrwfgVSDKD----------PEDVAVILFTSGTEKLPKGVPLTHANLLanqrACLKFFSPKEDD------VMMSF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 240 LPMFHIFGLSVITYGQLQRGNTVVvmsgFALD-----TVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGS 314
Cdd:PRK06334 231 LPPFHAYGFNSCTLFPLLSGVPVV----FAYNplypkKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 315 GAAPLGKDVMEAVAKNFPDALICQGYGMTETCGIISLEypEKGQVRQFGSTGTLVTGVEAKIVDVETLKHLPPNQLGEIC 394
Cdd:PRK06334 307 GGDAFKDSLYQEALKTFPHIQLRQGYGTTECSPVITIN--TVNSPKHESCVGMPIRGMDVLIVSEETKVPVSSGETGLVL 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357113996 395 VRGPHIMQGYFNNVQATEFTIRQG--WLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSH 463
Cdd:PRK06334 385 TRGTSLFSGYLGEDFGQGFVELGGetWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
14-481 |
1.68e-26 |
|
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: 113.70 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 14 DGVYRSLRPAARIE---SNPGLSAVDLLLR-------RAAACPSALALV-DAATGHA----------LTFSGLRSAILAS 72
Cdd:cd17632 1 DPQFAAAAPLEAVTeaiRRPGLRLAQIIATvmtgyadRPALGQRATELVtDPATGRTtlrllprfetITYAELWERVGAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 73 AVALSSRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVAStanPLytpreiakQASDARARLVITVAELLPK------- 145
Cdd:cd17632 81 AAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSV---PL--------QAGASAAQLAPILAETEPRllavsae 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 146 --------VADLRLP--VILLD----------------DTAAKSGSSATLYSDLVSGVDEADYRRPPTKQSDT---AGLL 196
Cdd:cd17632 150 hldlaveaVLEGGTPprLVVFDhrpevdahraalesarERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEPDDdplALLI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 197 YSSGTTGESKGVVLTHRNFIAAATMVTSDQDDRgEGPNVFLCFLPMFHIFGLSVItYGQLQRGNTVVVMSGFALDTVMSA 276
Cdd:cd17632 230 YTSGSTGTPKGAMYTERLVATFWLKVSSIQDIR-PPASITLNFMPMSHIAGRISL-YGTLARGGTAYFAAASDMSTLFDD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 277 VQQHRVTHLFCVPPV--MI-------------------ALAKHGKA-------GKYDLSSLkfigSGAAPLGKDvMEAVA 328
Cdd:cd17632 308 LALVRPTELFLVPRVcdMLfqryqaeldrrsvagadaeTLAERVKAelrervlGGRLLAAV----CGSAPLSAE-MKAFM 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 329 KNFPDALICQGYGMTETCGIISLEYPEKGQVrqfgstgtlvtgVEAKIVDVETLKHL---PPNQLGEICVRGPHIMQGYF 405
Cdd:cd17632 383 ESLLDLDLHDGYGSTEAGAVILDGVIVRPPV------------LDYKLVDVPELGYFrtdRPHPRGELLVKTDTLFPGYY 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 406 NNVQAT-EFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKY-KGFQIAPAELEGLLLSHPEI-------------LDAV 470
Cdd:cd17632 451 KRPEVTaEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVrqifvygnserayLLAV 530
|
570
....*....|.
gi 357113996 471 VIPFPDAEAGE 481
Cdd:cd17632 531 VVPTQDALAGE 541
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
42-497 |
6.40e-26 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 110.73 E-value: 6.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 42 AAACPSALALVDAatGHALTFSGLRSAILASAVALSsRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTP 121
Cdd:PRK09029 13 AQVRPQAIALRLN--DEVLTWQQLCARIDQLAAGFA-QQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 122 REIAKqasdararlvitvaeLLPkvaDLRLPVILLDDTAAKSGSSATLYSDLVSGVDEADY--RRPPTkqsdtagLLYSS 199
Cdd:PRK09029 90 PLLEE---------------LLP---SLTLDFALVLEGENTFSALTSLHLQLVEGAHAVAWqpQRLAT-------MTLTS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 200 GTTGESKGVVLTHRNFIAAATMVTS----DQDDRgegpnvFLCFLPMFHIFGLSvITYGQLQRGNTVVVMSGFALDtvmS 275
Cdd:PRK09029 145 GSTGLPKAAVHTAQAHLASAEGVLSlmpfTAQDS------WLLSLPLFHVSGQG-IVWRWLYAGATLVVRDKQPLE---Q 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 276 AVQQhrVTHLFCVPPVMIALakhgkagkydLSSLkfigsgAAPLG-KDVM---EAVAKNFPDALICQ------GYGMTEt 345
Cdd:PRK09029 215 ALAG--CTHASLVPTQLWRL----------LDNR------SEPLSlKAVLlggAAIPVELTEQAEQQgircwcGYGLTE- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 346 cgiisleypekgqvrqFGST------------GTLVTGVEAKIVDvetlkhlppnqlGEICVRGPHIMQGYFNNVQATEF 413
Cdd:PRK09029 276 ----------------MASTvcakradglagvGSPLPGREVKLVD------------GEIWLRGASLALGYWRQGQLVPL 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 414 TIRQGWLHTGDLGLFDDeGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAyVVRSPDS 493
Cdd:PRK09029 328 VNDEGWFATRDRGEWQN-GELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVA-VVESDSE 405
|
....
gi 357113996 494 SLTE 497
Cdd:PRK09029 406 AAVV 409
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
18-480 |
1.55e-25 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 110.73 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 18 RSLRPAARIESNPGLSAVDLLLRRAAACPSALALVDAatGHALTFSGLrsAILASAVA--LSSRaGVRPGDSVLLVAPNC 95
Cdd:PRK08279 23 RGLKRTALITPDSKRSLGDVFEEAAARHPDRPALLFE--DQSISYAEL--NARANRYAhwAAAR-GVGKGDVVALLMENR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 96 VLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVITVAELLPKV----ADLRLPVILLDDTAAKSGSSATlYS 171
Cdd:PRK08279 98 PEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFeearADLARPPRLWVAGGDTLDDPEG-YE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 172 DLVSGVDEADYRRPPTKQS----DTAGLLYSSGTTGESKGVVLTHRNFIAA----ATMVTSDQDDRgegpnvFLCFLPMF 243
Cdd:PRK08279 177 DLAAAAAGAPTTNPASRSGvtakDTAFYIYTSGTTGLPKAAVMSHMRWLKAmggfGGLLRLTPDDV------LYCCLPLY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 244 HIFGLSVITYGQLQRGNTVVV-----MSGFALDtvmsaVQQHRVTH----------LFCVPPvmialakhgKAGKYDLSS 308
Cdd:PRK08279 251 HNTGGTVAWSSVLAAGATLALrrkfsASRFWDD-----VRRYRATAfqyigelcryLLNQPP---------KPTDRDHRL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 309 LKFIGSGAAPlgkDVMEAVAKNFPDALICQGYGMTEtcGIISL----EYPekgqvrqfGSTG--TLVTGVEAKIV--DVE 380
Cdd:PRK08279 317 RLMIGNGLRP---DIWDEFQQRFGIPRILEFYAASE--GNVGFinvfNFD--------GTVGrvPLWLAHPYAIVkyDVD 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 381 TLKHL----------PPNQ----LGEICVRGPhiMQGYfNNVQATEFTI-----RQG--WLHTGDLGLFDDEGQLFVVDR 439
Cdd:PRK08279 384 TGEPVrdadgrcikvKPGEvgllIGRITDRGP--FDGY-TDPEASEKKIlrdvfKKGdaWFNTGDLMRDDGFGHAQFVDR 460
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 357113996 440 LKELIKYKGFQIAPAELEGLLLSHPEILDAVV----IPFPDAEAG 480
Cdd:PRK08279 461 LGDTFRWKGENVATTEVENALSGFPGVEEAVVygveVPGTDGRAG 505
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
30-536 |
3.72e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 111.02 E-value: 3.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 30 PGLSAVDLLLRRAAACPSALALVDAatGHALTFSGL--RSAILASAVALSsraGVRPGDSVLLVAPNCVLYPVCFFAVTA 107
Cdd:PRK12467 1572 LARLVHQLIEDQAAATPEAVALVFG--EQELTYGELnrRANRLAHRLIAL---GVGPEVLVGIAVERSLEMVVGLLAILK 1646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 108 LGAVASTANPLYTPREIAKQASDARARLVITVAELLPkvadlRLPV-----ILLDDTAaksgssatlySDLVSGVDEADY 182
Cdd:PRK12467 1647 AGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQA-----RLPLpdglrSLVLDQE----------DDWLEGYSDSNP 1711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 183 RRPPTKQsDTAGLLYSSGTTGESKGVVLTH----RNFIAAATMVTSDQDDrgegpnVFLCFLPmfHIFGLSV--ITYGQL 256
Cdd:PRK12467 1712 AVNLAPQ-NLAYVIYTSGSTGRPKGAGNRHgalvNRLCATQEAYQLSAAD------VVLQFTS--FAFDVSVweLFWPLI 1782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 257 QRGNTVVVMSGFALD--TVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKFIGSGAApLGKDVMEAVAKNFPDA 334
Cdd:PRK12467 1783 NGARLVIAPPGAHRDpeQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEA-LEVEALRPWLERLPDT 1861
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 335 LICQGYGMTETC-----GIISLEYPEKgqvRQFGSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFN--N 407
Cdd:PRK12467 1862 GLFNLYGPTETAvdvthWTCRRKDLEG---RDSVPIGQPIANLSTYILD-ASLNPVPIGVAGELYLGGVGLARGYLNrpA 1937
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 408 VQATEF------TIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPfPDAEAGE 481
Cdd:PRK12467 1938 LTAERFvadpfgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIA-QDGANGK 2016
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 357113996 482 VPIAYVVRSpDSSLTEVDVQkfietQVTYYKRLKR--------------VTFVSSVPKSASGKILRREL 536
Cdd:PRK12467 2017 QLVAYVVPT-DPGLVDDDEA-----QVALRAILKNhlkaslpeymvpahLVFLARMPLTPNGKLDRKAL 2079
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
36-536 |
3.76e-25 |
|
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: 108.40 E-value: 3.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 36 DLLLRRAAACPSALAlVDAATGHaLTFSGLRSaiLASAVA--LSSRaGVRPGDSVLLVAPNCVLYPVCFFAVT-ALGAVA 112
Cdd:cd05918 3 DLIEERARSQPDAPA-VCAWDGS-LTYAELDR--LSSRLAhhLRSL-GVGPGVFVPLCFEKSKWAVVAMLAVLkAGGAFV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 113 S--TANPLYTPREIAKqasDARARLVITvaellpkvadlrlpvillddtaakSGSSATLYsdlvsgvdeadyrrpptkqs 190
Cdd:cd05918 78 PldPSHPLQRLQEILQ---DTGAKVVLT------------------------SSPSDAAY-------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 191 dtagLLYSSGTTGESKGVVLTHRNFiaaATMVTSDQDDRGEGPNV-FLCFLPmfHIFGLSVI-TYGQLQRGNTVVVMSGF 268
Cdd:cd05918 111 ----VIFTSGSTGKPKGVVIEHRAL---STSALAHGRALGLTSESrVLQFAS--YTFDVSILeIFTTLAAGGCLCIPSEE 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 269 A-LDTVMSAVQQHRVTHLFCVPPVMIALAKHgkagkyDLSSLKFIGSGAAPLGKDVMEAVAknfPDALICQGYGMTETCg 347
Cdd:cd05918 182 DrLNDLAGFINRLRVTWAFLTPSVARLLDPE------DVPSLRTLVLGGEALTQSDVDTWA---DRVRLINAYGPAECT- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 348 iISLEYPEKGQVRQFGSTGTLVTGVeAKIVDVETL-KHLPPNQLGEICVRGPHIMQGYFNNVQATE--FTIRQGWLH--- 421
Cdd:cd05918 252 -IAATVSPVVPSTDPRNIGRPLGAT-CWVVDPDNHdRLVPIGAVGELLIEGPILARGYLNDPEKTAaaFIEDPAWLKqeg 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 422 ---------TGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEG-LLLSHPEILDAVV--IPFPDAEAGEVPIAYVVR 489
Cdd:cd05918 330 sgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHhLRQSLPGAKEVVVevVKPKDGSSSPQLVAFVVL 409
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357113996 490 SPDSSLTEVDVQKFIETQVTYYKRLKRVT-----------------FVSSVPKSASGKILRREL 536
Cdd:cd05918 410 DGSSSGSGDGDSLFLEPSDEFRALVAELRsklrqrlpsymvpsvflPLSHLPLTASGKIDRRAL 473
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
190-538 |
7.49e-25 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 105.90 E-value: 7.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 190 SDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVtsdqDDRGEGPNVFLCFLPMFHIFGLSVITYGQLQRGNTVV--VMSG 267
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTASADAT----HDRLGGPGQWLLALPAHHIAGLQVLVRSVIAGSEPVEldVSAG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 268 FALDTVMSAVQQ----HRVTHLFcvpPVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKnfPDALICQGYGMT 343
Cdd:PRK07824 111 FDPTALPRAVAElgggRRYTSLV---PMQLAKALDDPAATAALAELDAVLVGGGPAPAPVLDAAAA--AGINVVRTYGMS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 344 ETCGiisleypekGQVRQfgstGTLVTGVEAKIVDvetlkhlppnqlGEICVRGPHIMQGYFNNVQATEFTiRQGWLHTG 423
Cdd:PRK07824 186 ETSG---------GCVYD----GVPLDGVRVRVED------------GRIALGGPTLAKGYRNPVDPDPFA-EPGWFRTD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 424 DLGLFDDeGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKF 503
Cdd:PRK07824 240 DLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLEALRAH 318
|
330 340 350
....*....|....*....|....*....|....*
gi 357113996 504 IETQVTYYKRLKRVTFVSSVPKSASGKILRRELIA 538
Cdd:PRK07824 319 VARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
182-470 |
9.13e-25 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 108.57 E-value: 9.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 182 YRRPPTKQSDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVTSDQDDRGEG---PNVFLCFLPMFHIFGLSV----ITYG 254
Cdd:PLN02614 215 YDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANAAltvKDVYLSYLPLAHIFDRVIeecfIQHG 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 255 Q---LQRGNTVVVMSGFA-------------LDTVMSAVQQ-----------------------------HRVTHLFCvP 289
Cdd:PLN02614 295 AaigFWRGDVKLLIEDLGelkptifcavprvLDRVYSGLQKklsdggflkkfvfdsafsykfgnmkkgqsHVEASPLC-D 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 290 PVMIALAKHGKAGkydlsSLKFIGSGAAPLGKDVmEAVAKNFPDALICQGYGMTETCGIISLEYPEkgQVRQFGSTGTLV 369
Cdd:PLN02614 374 KLVFNKVKQGLGG-----NVRIILSGAAPLASHV-ESFLRVVACCHVLQGYGLTESCAGTFVSLPD--ELDMLGTVGPPV 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 370 TGVEAKIVDVETLKH--LPPNQLGEICVRGPHIMQGYFNNVQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKY- 446
Cdd:PLN02614 446 PNVDIRLESVPEMEYdaLASTPRGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLs 525
|
330 340
....*....|....*....|....
gi 357113996 447 KGFQIAPAELEGlLLSHPEILDAV 470
Cdd:PLN02614 526 QGEYVAVENIEN-IYGEVQAVDSV 548
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
37-538 |
6.04e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 106.97 E-value: 6.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 37 LLLRRAAACPSALALVDAATghALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTAN 116
Cdd:PRK12316 516 LFEEQVERTPEAPALAFGEE--TLDYAELNRRANRLAHALIER-GVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLD 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 117 PLYTPREIAKQASDARARLVITVAELLPKVA-DLRLPVILLDDTAAKSGSsatlYSDlvsgvdeadyrRPPTKQSDT--- 192
Cdd:PRK12316 593 PEYPAERLAYMLEDSGVQLLLSQSHLGRKLPlAAGVQVLDLDRPAAWLEG----YSE-----------ENPGTELNPenl 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 193 AGLLYSSGTTGESKGVVLTHRNFIAAAT-MVTSDQDDRGEGpnvFLCFLPMfhIFGLSVIT-YGQLQRGNTVVVMS---G 267
Cdd:PRK12316 658 AYVIYTSGSTGKPKGAGNRHRALSNRLCwMQQAYGLGVGDT---VLQKTPF--SFDVSVWEfFWPLMSGARLVVAApgdH 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 268 FALDTVMSAVQQHRVTHLFCVPPVMIALAKhgKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFPDALICQGYGMTETcg 347
Cdd:PRK12316 733 RDPAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEA-- 808
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 348 iiSLEYPEKGQVRQFGST---GTLVTGVEAKIVDVEtLKHLPPNQLGEICVRGPHIMQGYFNNVQAT-------EFTIRQ 417
Cdd:PRK12316 809 --AIDVTHWTCVEEGGDSvpiGRPIANLACYILDAN-LEPVPVGVLGELYLAGRGLARGYHGRPGLTaerfvpsPFVAGE 885
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 418 GWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIpfpdAEAGEVPIAYVVRSPDSSLTE 497
Cdd:PRK12316 886 RMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGKQLVGYVVLESEGGDWR 961
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 357113996 498 VDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRRELIA 538
Cdd:PRK12316 962 EALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPA 1002
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
21-536 |
8.92e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 106.58 E-value: 8.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 21 RPAARIESNPGLSAvdLLLRRAAACPSALALVdaATGHALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPV 100
Cdd:PRK12316 1994 RTPEAYPRGPGVHQ--RIAEQAARAPEAIAVV--FGDQHLSYAELDSRANRLAHRLRAR-GVGPEVRVAIAAERSFELVV 2068
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 101 CFFAVTALGAVASTANPLYtPRE-IAKQASDARARLVIT---VAELLPKVADLrlPVILLDDTAAKSGSSATlysdlvsg 176
Cdd:PRK12316 2069 ALLAVLKAGGAYVPLDPNY-PAErLAYMLEDSGAALLLTqrhLLERLPLPAGV--ARLPLDRDAEWADYPDT-------- 2137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 177 vdeadYRRPPTKQSDTAGLLYSSGTTGESKGVVLTHR---NFIAAAT----MVTSDQ---------DDRGEGpnvflCFL 240
Cdd:PRK12316 2138 -----APAVQLAGENLAYVIYTSGSTGLPKGVAVSHGalvAHCQAAGeryeLSPADCelqfmsfsfDGAHEQ-----WFH 2207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 241 PMFHifGLSVITygqlqRGNTVvvmsgFALDTVMSAVQQHRVThLFCVPPVMI-ALAKHGKAGKYDLSSLKFIGSGAApL 319
Cdd:PRK12316 2208 PLLN--GARVLI-----RDDEL-----WDPEQLYDEMERHGVT-ILDFPPVYLqQLAEHAERDGRPPAVRVYCFGGEA-V 2273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 320 GKDVMEAVAKNFPDALICQGYGMTETCgIISLEY---PEKGQVRQFGSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVR 396
Cdd:PRK12316 2274 PAASLRLAWEALRPVYLFNGYGPTEAV-VTPLLWkcrPQDPCGAAYVPIGRALGNRRAYILD-ADLNLLAPGMAGELYLG 2351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 397 GPHIMQGYFNNVQATE-------FTIRQGWLH-TGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILD 468
Cdd:PRK12316 2352 GEGLARGYLNRPGLTAerfvpdpFSASGERLYrTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVRE 2431
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 357113996 469 AVVIPFpDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:PRK12316 2432 AVVVAQ-DGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
37-536 |
1.09e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 106.19 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 37 LLLRRAAACPSALALVdaATGHALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTAN 116
Cdd:PRK12316 4556 LVAERARMTPDAVAVV--FDEEKLTYAELNRRANRLAHALIAR-GVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLD 4632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 117 PLYtPRE-IAKQASDARARLVITVAELLPkvadlRLPVillddtAAKSGSSATLYSDLVSGVDEADYRRPPTKQsDTAGL 195
Cdd:PRK12316 4633 PEY-PRErLAYMMEDSGAALLLTQSHLLQ-----RLPI------PDGLASLALDRDEDWEGFPAHDPAVRLHPD-NLAYV 4699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 196 LYSSGTTGESKGVVLTHRNFIA------AATMVTSDqdDRgegpnvFLCFLPM-FHIFGLSVitYGQLQRGNTVVVMSGF 268
Cdd:PRK12316 4700 IYTSGSTGRPKGVAVSHGSLVNhlhatgERYELTPD--DR------VLQFMSFsFDGSHEGL--YHPLINGASVVIRDDS 4769
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 269 ALD--TVMSAVQQHRVTHLFCVPPVMIALAKHGKAgKYDLSSLKFIGSGAAPLGKDVMEAVAKNFPDALICQGYGMTETC 346
Cdd:PRK12316 4770 LWDpeRLYAEIHEHRVTVLVFPPVYLQQLAEHAER-DGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETT 4848
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 347 GIISLEYPEKGQV--RQFGSTGTLVTGVEAKIVDVEtLKHLPPNQLGEICVRGPHIMQGYFNNVQATE-------FTIRQ 417
Cdd:PRK12316 4849 VTVLLWKARDGDAcgAAYMPIGTPLGNRSGYVLDGQ-LNPLPVGVAGELYLGGEGVARGYLERPALTAerfvpdpFGAPG 4927
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 418 GWLH-TGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAeAGEVPIAYVVrSPDSSLT 496
Cdd:PRK12316 4928 GRLYrTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGA-VGKQLVGYVV-PQDPALA 5005
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 357113996 497 EVDvqkfiETQVTYYKRLKR--------------VTFVSSVPKSASGKILRREL 536
Cdd:PRK12316 5006 DAD-----EAQAELRDELKAalrerlpeymvpahLVFLARMPLTPNGKLDRKAL 5054
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
60-545 |
1.87e-23 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 104.59 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 60 LTFSGLRSAILASAVALSSrAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVITV 139
Cdd:PLN02654 121 LTYSELLDRVCQLANYLKD-VGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 140 AELL--PKVADLRLPVILLDDTAAKSGSS--ATLYSDLVSGVDEADYR--------------RPPTK-------QSDTAG 194
Cdd:PLN02654 200 NAVKrgPKTINLKDIVDAALDESAKNGVSvgICLTYENQLAMKREDTKwqegrdvwwqdvvpNYPTKcevewvdAEDPLF 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 195 LLYSSGTTGESKGVVLTHRNF-IAAATMVTSDQDDRGEgpNVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGFA---- 269
Cdd:PLN02654 280 LLYTSGSTGKPKGVLHTTGGYmVYTATTFKYAFDYKPT--DVYWCTADCGWITGHSYVTYGPMLNGATVLVFEGAPnypd 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 270 LDTVMSAVQQHRVTHLFCVPPVMIALAKHGK--AGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFPDAL--ICQGYGMTET 345
Cdd:PLN02654 358 SGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDeyVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDSRcpISDTWWQTET 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 346 CG--IISLE--YPEKGqvrqfGSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRG--PHIMQGYFNN---VQATEFTIR 416
Cdd:PLN02654 438 GGfmITPLPgaWPQKP-----GSATFPFFGVQPVIVD-EKGKEIEGECSGYLCVKKswPGAFRTLYGDherYETTYFKPF 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 417 QGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLT 496
Cdd:PLN02654 512 AGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYS 591
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 357113996 497 EVDVQKFIET---QVTYYKRLKRVTFVSSVPKSASGKILRReLIAKVRSSKL 545
Cdd:PLN02654 592 EELRKSLILTvrnQIGAFAAPDKIHWAPGLPKTRSGKIMRR-ILRKIASRQL 642
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
46-536 |
4.97e-23 |
|
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: 102.06 E-value: 4.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 46 PSALALVDAatGHALTFSGL--RSAILASAVAlssRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPRE 123
Cdd:cd17649 1 PDAVALVFG--DQSLSYAELdaRANRLAHRLR---ALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 124 IAKQASDARARLVITvaellpkvadlrlpvillddtaaksgssatlysdlvsgvdeadyRRPPTkqsdTAGLLYSSGTTG 203
Cdd:cd17649 76 LRYMLEDSGAGLLLT--------------------------------------------HHPRQ----LAYVIYTSGSTG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 204 ESKGVVLTHRNfIAAATMVTSDQDDRGEGpNVFLCFLPM-FHIFGLSVitYGQLQRGNTVVVMSGFALDTV---MSAVQQ 279
Cdd:cd17649 108 TPKGVAVSHGP-LAAHCQATAERYGLTPG-DRELQFASFnFDGAHEQL--LPPLICGACVVLRPDELWASAdelAEMVRE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 280 HRVTHLfCVPPV----MIALAKHGKAGKYdlSSLKFIGSGAAPLGKDVMEAVAKNfpDALICQGYGMTETCGIISLEYPE 355
Cdd:cd17649 184 LGVTVL-DLPPAylqqLAEEADRTGDGRP--PSLRLYIFGGEALSPELLRRWLKA--PVRLFNAYGPTEATVTPLVWKCE 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 356 KGQVRQFGST--GTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQATE--------FTIRQGWLHTGDL 425
Cdd:cd17649 259 AGAARAGASMpiGRPLGGRSAYILD-ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAerfvpdpfGAPGSRLYRTGDL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 426 GLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAeAGEVPIAYVVRSPDSSLTEVDVQ--KF 503
Cdd:cd17649 338 ARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGA-GGKQLVAYVVLRAAAAQPELRAQlrTA 416
|
490 500 510
....*....|....*....|....*....|...
gi 357113996 504 IETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd17649 417 LRASLPDYMVPAHLVFLARLPLTPNGKLDRKAL 449
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
73-539 |
5.81e-23 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 102.91 E-value: 5.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 73 AVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVITVAEL--------LP 144
Cdd:PRK00174 112 ANALKSL-GVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSAEALADRIIDAGAKLVITADEGvrggkpipLK 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 145 KVAD--LRLP-----VILLDDTAAKSGSSAT---LYSDLVSGVDeaDYRRP-PTKQSDTAGLLYSSGTTGESKGVV---- 209
Cdd:PRK00174 191 ANVDeaLANCpsvekVIVVRRTGGDVDWVEGrdlWWHELVAGAS--DECEPePMDAEDPLFILYTSGSTGKPKGVLhttg 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 210 --LTHrnfiAAATM--VTSDQDDrgegpNVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGfALDT-----VMSAVQQH 280
Cdd:PRK00174 269 gyLVY----AAMTMkyVFDYKDG-----DVYWCTADVGWVTGHSYIVYGPLANGATTLMFEG-VPNYpdpgrFWEVIDKH 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 281 RVTHLFCVPPVMIALAKHGKA--GKYDLSSLKFIGSGAAPLgkdvmeavakNfPDA------LICQG-------YGMTET 345
Cdd:PRK00174 339 KVTIFYTAPTAIRALMKEGDEhpKKYDLSSLRLLGSVGEPI----------N-PEAwewyykVVGGErcpivdtWWQTET 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 346 CGI-ISleyPEKGQVRQF-GSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRG--PHIMQGYFNN----VQaTEFTIRQ 417
Cdd:PRK00174 408 GGImIT---PLPGATPLKpGSATRPLPGIQPAVVD-EEGNPLEGGEGGNLVIKDpwPGMMRTIYGDherfVK-TYFSTFK 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 418 GWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVV----RSPDS 493
Cdd:PRK00174 483 GMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTlkggEEPSD 562
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 357113996 494 SLTEvDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL--IAK 539
Cdd:PRK00174 563 ELRK-ELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILrkIAE 609
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
119-541 |
1.34e-22 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 101.13 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 119 YTPRE-IAKQASDARARLVITVAELLPKVADLrlPVILLDD-TAAKSGSSATLYSDLVSGvdeadyrrpptkqSDTAGLL 196
Cdd:PRK04813 85 SSPAErIEMIIEVAKPSLIIATEELPLEILGI--PVITLDElKDIFATGNPYDFDHAVKG-------------DDNYYII 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 197 YSSGTTGESKGVVLTHRNFIAAATMVTSDqDDRGEGPnVFLCFLPmfHIFGLSVIT-YGQLQRGNTVvvmsgFALDTVM- 274
Cdd:PRK04813 150 FTSGTTGKPKGVQISHDNLVSFTNWMLED-FALPEGP-QFLNQAP--YSFDLSVMDlYPTLASGGTL-----VALPKDMt 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 275 -------SAVQQHRVTHLFCVPPVM-IAL------AKHgkagkydLSSLK-FIGSGAApLGKDVMEAVAKNFPDALICQG 339
Cdd:PRK04813 221 anfkqlfETLPQLPINVWVSTPSFAdMCLldpsfnEEH-------LPNLThFLFCGEE-LPHKTAKKLLERFPSATIYNT 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 340 YGMTETCG-----IISLEYPEK------GQVRQfgstgtlvtGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNV 408
Cdd:PRK04813 293 YGPTEATVavtsiEITDEMLDQykrlpiGYAKP---------DSPLLIID-EEGTKLPDGEQGEIVISGPSVSKGYLNNP 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 409 QATE--FTIRQGW--LHTGDLGLFDDeGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPI 484
Cdd:PRK04813 363 EKTAeaFFTFDGQpaYHTGDAGYLED-GLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLI 441
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357113996 485 AYVVrspdssLTEVDVQKfiETQVTyyKRLK--------------RVTFVSSVPKSASGKILRRELIAKVR 541
Cdd:PRK04813 442 AYVV------PKEEDFER--EFELT--KAIKkelkerlmeymiprKFIYRDSLPLTPNGKIDRKALIEEVN 502
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
20-534 |
3.07e-22 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 100.59 E-value: 3.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 20 LRPAARIESNPGLSAVDLLLRRAAACPSALA--LVD---AATGHA--LTFSGLRSAIlaSAVALSSRAGVRPGDSVLLVA 92
Cdd:PRK12476 22 LDADGNIALPPGTTLISLIERNIANVGDTVAyrYLDhshSAAGCAveLTWTQLGVRL--RAVGARLQQVAGPGDRVAILA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 93 PNCVLYPVCFFAVTALGAVAStanPLYTPrEIAKQA-------SDARARLVIT-------VAELLPKVADLRLP-VILLD 157
Cdd:PRK12476 100 PQGIDYVAGFFAAIKAGTIAV---PLFAP-ELPGHAerldtalRDAEPTVVLTttaaaeaVEGFLRNLPRLRRPrVIAID 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 158 DTAAKSGssatlysdlvsgvdeADYRRPPTKQSDTAGLLYSSGTTGESKGVVLTHRnfiAAAT----MVTS----DQDDR 229
Cdd:PRK12476 176 AIPDSAG---------------ESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHR---AVGTnlvqMILSidllDRNTH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 230 GegpnvfLCFLPMFHIFGLSVITYGQLQrGNTVVVMSGFA--------LDTVMSAVQQHRVthLFCVPPVMIALAKH--- 298
Cdd:PRK12476 238 G------VSWLPLYHDMGLSMIGFPAVY-GGHSTLMSPTAfvrrpqrwIKALSEGSRTGRV--VTAAPNFAYEWAAQrgl 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 299 -GKAGKYDLSSLKFIgSGAAPLGKDVMEAVAKNF-----PDALICQGYGMTETCGIISLEYP--EKGQV----RQFG--- 363
Cdd:PRK12476 309 pAEGDDIDLSNVVLI-IGSEPVSIDAVTTFNKAFapyglPRTAFKPSYGIAEATLFVATIAPdaEPSVVyldrEQLGagr 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 364 ---------------STGTLVTGVEAKIVDVETLKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTIR--------QG-- 418
Cdd:PRK12476 388 avrvaadapnavahvSCGQVARSQWAVIVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFGaklqsrlaEGsh 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 419 ---------WLHTGDLGLFDDeGQLFVVDRLKELIKYKGFQIAPAELEGLL-LSHPEILDAVVIPFP-DAEAGEVPIAYV 487
Cdd:PRK12476 468 adgaaddgtWLRTGDLGVYLD-GELYITGRIADLIVIDGRNHYPQDIEATVaEASPMVRRGYVTAFTvPAEDNERLVIVA 546
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 357113996 488 VRSPDSSLTE-VDVQKFIETQVT--YYKRLKRVTFVSS--VPKSASGKILRR 534
Cdd:PRK12476 547 ERAAGTSRADpAPAIDAIRAAVSrrHGLAVADVRLVPAgaIPRTTSGKLARR 598
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
46-536 |
3.52e-22 |
|
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: 99.40 E-value: 3.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 46 PSALALVDAATghALTFSGLRSAILASAVALSSRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIA 125
Cdd:cd17648 1 PDRVAVVYGDK--RLTYRELNERANRLAHYLLSVAEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 126 KQASDARARLVITvaellpkvadlrlpvillddtaaksgssatlysdlvsgvdeadyrrpptKQSDTAGLLYSSGTTGES 205
Cdd:cd17648 79 FILEDTGARVVIT-------------------------------------------------NSTDLAYAIYTSGTTGKP 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 206 KGVVLTHRNFIAAATMVTSDQDDRGEGPNVFLCFLPmfHIFGLSV-ITYGQLQRGNTVVVMSG---FALDTVMSAVQQHR 281
Cdd:cd17648 110 KGVLVEHGSVVNLRTSLSERYFGRDNGDEAVLFFSN--YVFDFFVeQMTLALLNGQKLVVPPDemrFDPDRFYAYINREK 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 282 VTHLFCVPPVMialakhgkaGKYDLS---SLKFIGSGAAPLGKDVMEAVAKNFPdALICQGYGMTETcGIISLEYPEKGQ 358
Cdd:cd17648 188 VTYLSGTPSVL---------QQYDLArlpHLKRVDAAGEEFTAPVFEKLRSRFA-GLIINAYGPTET-TVTNHKRFFPGD 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 359 VRQFGSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFN-----------NVQATEFTIRQG----WLHTG 423
Cdd:cd17648 257 QRFDKSLGRPVRNTKCYVLN-DAMKRVPVGAVGELYLGGDGVARGYLNrpeltaerflpNPFQTEQERARGrnarLYKTG 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 424 DLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPI-----AYVVRSPDsSLTEV 498
Cdd:cd17648 336 DLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSRIqkylvGYYLPEPG-HVPES 414
|
490 500 510
....*....|....*....|....*....|....*...
gi 357113996 499 DVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd17648 415 DLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
21-536 |
4.78e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 101.01 E-value: 4.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 21 RPAARIESNP------GLSAVDLLLRRAAACPSALALVdaATGHALTFSGLRsailASAVALSSR---AGVRPGDSVLLV 91
Cdd:PRK12467 495 RARELVRWNApateyaPDCVHQLIEAQARQHPERPALV--FGEQVLSYAELN----RQANRLAHVliaAGVGPDVLVGIA 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 92 APNCVLYPVCFFAVTALGAVASTANPLYtPRE-IAKQASDARARLVIT---VAELLPKVADLRlpVILLDDTAaksgssa 167
Cdd:PRK12467 569 VERSIEMVVGLLAVLKAGGAYVPLDPEY-PQDrLAYMLDDSGVRLLLTqshLLAQLPVPAGLR--SLCLDEPA------- 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 168 tlysDLVSGVDEADyrrPPTKQS--DTAGLLYSSGTTGESKGVVLTHRNfIAAATMVTSDQDDRGEGPNVFLCFLPMFHI 245
Cdd:PRK12467 639 ----DLLCGYSGHN---PEVALDpdNLAYVIYTSGSTGQPKGVAISHGA-LANYVCVIAERLQLAADDSMLMVSTFAFDL 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 246 FGLSVitYGQLQRGNTVVVMS-GFALD--TVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKydLSSLKFIGSGAAPLGKD 322
Cdd:PRK12467 711 GVTEL--FGALASGATLHLLPpDCARDaeAFAALMADQGVTVLKIVPSHLQALLQASRVAL--PRPQRALVCGGEALQVD 786
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 323 VMEAVAKNFPDALICQGYGMTETCgIISLEYPEKGQVRQFGST--GTLVTGVEAKIVDVEtLKHLPPNQLGEICVRGPHI 400
Cdd:PRK12467 787 LLARVRALGPGARLINHYGPTETT-VGVSTYELSDEERDFGNVpiGQPLANLGLYILDHY-LNPVPVGVVGELYIGGAGL 864
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 401 MQGYFNNVQATE-------FTIRQGWLH-TGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVI 472
Cdd:PRK12467 865 ARGYHRRPALTAerfvpdpFGADGGRLYrTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVL 944
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357113996 473 PFPdAEAGEVPIAYVVrsPDSSLTEVDVQKFIETQVTYYKRL-------KRVTFVSSVPKSASGKILRREL 536
Cdd:PRK12467 945 AQP-GDAGLQLVAYLV--PAAVADGAEHQATRDELKAQLRQVlpdymvpAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
46-536 |
1.30e-21 |
|
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: 97.54 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 46 PSALALVDAATghALTFSGL--RSAILASAVAlssRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPRE 123
Cdd:cd17650 1 PDAIAVSDATR--QLTYRELneRANQLARTLR---GLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 124 IAKQASDARARLVITVAEllpkvadlrlpvillddtaaksgssatlysdlvsgvdeadyrrpptkqsDTAGLLYSSGTTG 203
Cdd:cd17650 76 LQYMLEDSGAKLLLTQPE-------------------------------------------------DLAYVIYTSGTTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 204 ESKGVVLTHRNFIAAAtmVTSDQDDRGEGPNVFLCFLPMFHI------FGLSVITYGQLqrgntVVVMSGFALDTVM--S 275
Cdd:cd17650 107 KPKGVMVEHRNVAHAA--HAWRREYELDSFPVRLLQMASFSFdvfagdFARSLLNGGTL-----VICPDEVKLDPAAlyD 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 276 AVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLKF--IGSGAAPLgKDVMEAVAKNFPDALICQGYGMTETCgiISLEY 353
Cdd:cd17650 180 LILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLliVGSDGCKA-QDFKTLAARFGQGMRIINSYGVTEAT--IDSTY 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 354 PEKGQVRQFGS----TGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQATE-------FTIRQGWLHT 422
Cdd:cd17650 257 YEEGRDPLGDSanvpIGRPLPNTAMYVLD-ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAerfvenpFAPGERMYRT 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 423 GDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVrsPDSSLTEVDVQK 502
Cdd:cd17650 336 GDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVV--AAATLNTAELRA 413
|
490 500 510
....*....|....*....|....*....|....
gi 357113996 503 FIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd17650 414 FLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
57-506 |
1.53e-21 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 97.42 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 57 GHALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLV 136
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSL-GLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 137 ITvaellpkvadlrlpvillddtaaksgssatlysdlvsgvdeadyrrpptkqsDTAGLLYSSGTTGESKGVVLTHRNFI 216
Cdd:cd05940 80 VV----------------------------------------------------DAALYIYTSGTTGLPKAAIISHRRAW 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 217 AAATMVTS----DQDDRgegpnVFLCfLPMFHIFGLSVITYGQLQRGNTVVVMSGFALDTVMSAVQQHRVT--------- 283
Cdd:cd05940 108 RGGAFFAGsggaLPSDV-----LYTC-LPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATifqyigelc 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 284 -HLFCVPPVmIALAKHgkagkydlsSLKFI-GSGAAPlgkDVMEAVAKNFPDALICQGYGMTE-TCGIISLEypekGQVR 360
Cdd:cd05940 182 rYLLNQPPK-PTERKH---------KVRMIfGNGLRP---DIWEEFKERFGVPRIAEFYAATEgNSGFINFF----GKPG 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 361 QFGSTGTLVTGV-EAKIV--DVET----------LKHLPPNQ----LGEICVRGPhiMQGYFNNVQATEFTIR----QG- 418
Cdd:cd05940 245 AIGRNPSLLRKVaPLALVkyDLESgepirdaegrCIKVPRGEpgllISRINPLEP--FDGYTDPAATEKKILRdvfkKGd 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 419 -WLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVV----IPFPDAEAGEVPIayVVRSPds 493
Cdd:cd05940 323 aWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygvqVPGTDGRAGMAAI--VLQPN-- 398
|
490
....*....|...
gi 357113996 494 slTEVDVQKFIET 506
Cdd:cd05940 399 --EEFDLSALAAH 409
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
76-539 |
1.79e-21 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 98.57 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 76 LSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVITVAELLPKVAdlrlPVIL 155
Cdd:PRK06060 47 LRNR-GLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRFQ----PSRV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 156 LDdtaaksgsSATLYSDlVSGVDEADYRrpPTKQSDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVTSDQdDRGEGPNV 235
Cdd:PRK06060 122 AE--------AAELMSE-AARVAPGGYE--PMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKA-LRLTPEDT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 236 FLCFLPMFHIFGLSVITYGQLQRGNTVVVMS---GFALDTVMSAVQQHRVthLFCVPPVMIALAKHGKAGKYdlSSLKFI 312
Cdd:PRK06060 190 GLCSARMYFAYGLGNSVWFPLATGGSAVINSapvTPEAAAILSARFGPSV--LYGVPNFFARVIDSCSPDSF--RSLRCV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 313 GSGAAPLGKDVMEAVAKNFPDALICQGYGMTETCGIISLEYPEKGQVrqfGSTGTLVTGVEAKIVDVETLKHLPPNQlGE 392
Cdd:PRK06060 266 VSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTFVSNRVDEWRL---GTLGRVLPPYEIRVVAPDGTTAGPGVE-GD 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 393 ICVRGPHIMQGYFNnvQATEFTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVI 472
Cdd:PRK06060 342 LWVRGPAIAKGYWN--RPDSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVV 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 473 PFPDAEAGEVPIAYVVRSPDSSLTEV---DVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRRELIAK 539
Cdd:PRK06060 420 AVRESTGASTLQAFLVATSGATIDGSvmrDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQ 489
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
31-536 |
1.92e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 99.08 E-value: 1.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 31 GLSAVDLLLRRAAACPSALALVDAatGHALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGA 110
Cdd:PRK12467 3094 ERLVHQLIEAQVARTPEAPALVFG--DQQLSYAELNRRANRLAHRLIAI-GVGPDVLVGVAVERSVEMIVALLAVLKAGG 3170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 111 VASTANPLYtPRE-IAKQASDARARLVITVAELLPkvadlRLPVillddtaAKSGSSATLysDLVSGVDEADYRRPPTKQ 189
Cdd:PRK12467 3171 AYVPLDPEY-PRErLAYMIEDSGVKLLLTQAHLLE-----QLPA-------PAGDTALTL--DRLDLNGYSENNPSTRVM 3235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 190 SDT-AGLLYSSGTTGESKGVVLTHRNFI----AAATMVTSDQDDRgegpnvFLCFLPMfhIFGLSVI-TYGQLQRGNTVV 263
Cdd:PRK12467 3236 GENlAYVIYTSGSTGKPKGVGVRHGALAnhlcWIAEAYELDANDR------VLLFMSF--SFDGAQErFLWTLICGGCLV 3307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 264 VMSGFALD--TVMSAVQQHRVTHLFCVPPVMIALAKHGKAGkyDLSSLKFIGSGAAPLGKDVMEAVAKNFPDALICQGYG 341
Cdd:PRK12467 3308 VRDNDLWDpeELWQAIHAHRISIACFPPAYLQQFAEDAGGA--DCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYG 3385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 342 MTETCGIISLEYPEKGQVRQFGST--GTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQATE------- 412
Cdd:PRK12467 3386 PTEAVVTVTLWKCGGDAVCEAPYApiGRPVAGRSIYVLD-GQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAerfvadp 3464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 413 FTIRQGWLH-TGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFpDAEAGEVPIAYVV-RS 490
Cdd:PRK12467 3465 FSGSGGRLYrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVpAD 3543
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 357113996 491 PDSSLTEVdVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:PRK12467 3544 PQGDWRET-LRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
197-544 |
3.02e-21 |
|
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: 96.79 E-value: 3.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 197 YSSGTTGESKGVVLTHRNFI----AAATMVTSDQDDRgegpnvFLCFLPMFHIFGLSVITYGQLQRGNTVVVM--SGFAL 270
Cdd:cd05908 113 FSSGSTGDPKGVMLTHENLVhnmfAILNSTEWKTKDR------ILSWMPLTHDMGLIAFHLAPLIAGMNQYLMptRLFIR 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 271 DTV--MSAVQQHRVTHLfCVP----PVMIALAKHGKAGKYDLSSLKFIGSGAAPLGKDVMEavakNFPDAliCQGYGMTE 344
Cdd:cd05908 187 RPIlwLKKASEHKATIV-SSPnfgyKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCH----EFLDH--MSKYGLKR 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 345 TC-----GI-------------------------ISLEYPEKGQVRQ------FGSTGTLVTGVEAKIVDvETLKHLPPN 388
Cdd:cd05908 260 NAilpvyGLaeasvgaslpkaqspfktitlgrrhVTHGEPEPEVDKKdsecltFVEVGKPIDETDIRICD-EDNKILPDG 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 389 QLGEICVRGPHIMQGYFNNVQATEFTIRQ-GWLHTGDLGLFDDeGQLFVVDRLKELIKYKGFQIAP-------AELEGLL 460
Cdd:cd05908 339 YIGHIQIRGKNVTPGYYNNPEATAKVFTDdGWLKTGDLGFIRN-GRLVITGREKDIIFVNGQNVYPhdieriaEELEGVE 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 461 LSHpeildAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQVTYYK--RLKRVTFVSSVPKSASGKILRRELIA 538
Cdd:cd05908 418 LGR-----VVACGVNNSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHLNKRGgwQINEVLPIRRIPKTTSGKVKRYELAQ 492
|
....*.
gi 357113996 539 KVRSSK 544
Cdd:cd05908 493 RYQSGE 498
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
153-464 |
1.83e-20 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 95.18 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 153 VILLDDTAAKSGSSATLYSDLV----SGVDEADYRRP-----PTKqSDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVT 223
Cdd:PLN02387 205 VIYMDDEGVDSDSSLSGSSNWTvssfSEVEKLGKENPvdpdlPSP-NDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVM 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 224 SDQDDRGEGpNVFLCFLPMFHIFGL----------SVITYG----------QLQRGN---------TVVVMSGFALDTVM 274
Cdd:PLN02387 284 TVVPKLGKN-DVYLAYLPLAHILELaaesvmaavgAAIGYGspltltdtsnKIKKGTkgdasalkpTLMTAVPAILDRVR 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 275 SAVQQH------RVTHLFcvppvMIALAKHGKA------GKYDLSSL------------------KFIGSGAAPLGKDVM 324
Cdd:PLN02387 363 DGVRKKvdakggLAKKLF-----DIAYKRRLAAiegswfGAWGLEKLlwdalvfkkiravlggriRFMLSGGAPLSGDTQ 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 325 EAVAKNFpDALICQGYGMTETCGIISLEYPEKGQVrqfGSTGTLVTGVEAKIVDVETLKHL---PPNQLGEICVRGPHIM 401
Cdd:PLN02387 438 RFINICL-GAPIGQGYGLTETCAGATFSEWDDTSV---GRVGPPLPCCYVKLVSWEEGGYLisdKPMPRGEIVIGGPSVT 513
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357113996 402 QGYFNNVQAT-------EFTIRqgWLHTGDLGLFDDEGQLFVVDRLKELIKYK-GFQIAPAELEGLLLSHP 464
Cdd:PLN02387 514 LGYFKNQEKTdevykvdERGMR--WFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAALSVSP 582
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
186-496 |
3.25e-20 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 94.39 E-value: 3.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 186 PTKQSDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVTSDQD----DRgegpnvFLCFLPMFHIFGLSVITYGQLQRGNT 261
Cdd:PRK08043 361 KQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADftpnDR------FMSALPLFHSFGLTVGLFTPLLTGAE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 262 VVVM-SGFALDTVMSAVQQHRVTHLFCVPPVMIALAKHgkAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFpDALICQGY 340
Cdd:PRK08043 435 VFLYpSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARF--ANPYDFARLRYVVAGAEKLQESTKQLWQDKF-GLRILEGY 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 341 GMTETCGIISLEYPEKGQVrqfGSTGTLVTGVEAKIVDVETLKhlppnQLGEICVRGPHIMQGYF-------------NN 407
Cdd:PRK08043 512 GVTECAPVVSINVPMAAKP---GTVGRILPGMDARLLSVPGIE-----QGGRLQLKGPNIMNGYLrvekpgvlevptaEN 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 408 VQATeftIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLS-HPEILDAVVIPfPDAEAGEvpiAY 486
Cdd:PRK08043 584 ARGE---MERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGvSPDKQHATAIK-SDASKGE---AL 656
|
330
....*....|
gi 357113996 487 VVRSPDSSLT 496
Cdd:PRK08043 657 VLFTTDSELT 666
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
30-536 |
3.43e-20 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 95.11 E-value: 3.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 30 PGLSAVDLLLRRAAACPSALALVDAatGHALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALG 109
Cdd:PRK10252 456 PETTLSALVAQQAAKTPDAPALADA--RYQFSYREMREQVVALANLLRER-GVKPGDSVAVALPRSVFLTLALHAIVEAG 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 110 AVASTANPLYTPREIAKQASDARARLVITVAELLPKVADLRLPVILLDDTAAKSGSSATLysdlvsgvdeadyrrPPTKQ 189
Cdd:PRK10252 533 AAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLAPQGAAPL---------------QLSQP 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 190 SDTAGLLYSSGTTGESKGVVLTHR------------------NFIAAATMVTSDQddrgegpNVFLCFLPMfhifglsvi 251
Cdd:PRK10252 598 HHTAYIIFTSGSTGRPKGVMVGQTaivnrllwmqnhypltadDVVLQKTPCSFDV-------SVWEFFWPF--------- 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 252 tygqlqrgntvvvMSGFALdtVMSAVQQHR-------------VTHLFCVPPVMIAlakhgkagkydlsslkFIGSGAAP 318
Cdd:PRK10252 662 -------------IAGAKL--VMAEPEAHRdplamqqffaeygVTTTHFVPSMLAA----------------FVASLTPE 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 319 LGKDVMEAVAKNFpdaliCQG----------------------YGMTETCGIISLeYPEKGQvRQFGSTGTLV------- 369
Cdd:PRK10252 711 GARQSCASLRQVF-----CSGealpadlcrewqqltgaplhnlYGPTEAAVDVSW-YPAFGE-ELAAVRGSSVpigypvw 783
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 370 -TGVEakIVDvETLKHLPPNQLGEICVRGPHIMQGYFNN--VQATEFT---IRQG--WLHTGDLGLFDDEGQLFVVDRLK 441
Cdd:PRK10252 784 nTGLR--ILD-ARMRPVPPGVAGDLYLTGIQLAQGYLGRpdLTASRFIadpFAPGerMYRTGDVARWLDDGAVEYLGRSD 860
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 442 ELIKYKGFQIAPAELEGLLLSHPEI----LDAVVIPFPDAEAGEVP--IAYVVRSPDSSLTEVDVQKFIETQVTYYkrLK 515
Cdd:PRK10252 861 DQLKIRGQRIELGEIDRAMQALPDVeqavTHACVINQAAATGGDARqlVGYLVSQSGLPLDTSALQAQLRERLPPH--MV 938
|
570 580
....*....|....*....|...
gi 357113996 516 RVTFV--SSVPKSASGKILRREL 536
Cdd:PRK10252 939 PVVLLqlDQLPLSANGKLDRKAL 961
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
36-538 |
3.82e-20 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 95.24 E-value: 3.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 36 DLLLRRAAACPSALALVDAatGHALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTA 115
Cdd:PRK05691 2192 GLFAAQAARTPQAPALTFA--GQTLSYAELDARANRLARALRER-GVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPL 2268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 116 NPLYTPREIAKQASDARARLVITVAELLPKVADLRLPV---ILLDDTAAKSGssatlYSDlvsgvDEADYRRPPTKQsdt 192
Cdd:PRK05691 2269 DPEYPLERLHYMIEDSGIGLLLSDRALFEALGELPAGVarwCLEDDAAALAA-----YSD-----APLPFLSLPQHQ--- 2335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 193 AGLLYSSGTTGESKGVVLTH-------RNFIAAATMVTSDqddrgegpnvflCFLPMFHI--------------FGLSVI 251
Cdd:PRK05691 2336 AYLIYTSGSTGKPKGVVVSHgeiamhcQAVIERFGMRADD------------CELHFYSInfdaaserllvpllCGARVV 2403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 252 TYGQLQrgntvvvmsgFALDTVMSAVQQHRVTHLFCVPPVMIALAKHgKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNF 331
Cdd:PRK05691 2404 LRAQGQ----------WGAEEICQLIREQQVSILGFTPSYGSQLAQW-LAGQGEQLPVRMCITGGEALTGEHLQRIRQAF 2472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 332 PDALICQGYGMTETCgIISLEYPEKGQVRQFGST---GTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNV 408
Cdd:PRK05691 2473 APQLFFNAYGPTETV-VMPLACLAPEQLEEGAASvpiGRVVGARVAYILD-ADLALVPQGATGELYVGGAGLAQGYHDRP 2550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 409 Q-------ATEFTIRQGWLH-TGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFpDAEAG 480
Cdd:PRK05691 2551 GltaerfvADPFAADGGRLYrTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSG 2629
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357113996 481 EVPIAYVVrSPDSSLTEVD-------VQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRRELIA 538
Cdd:PRK05691 2630 KQLAGYLV-SAVAGQDDEAqaalreaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPA 2693
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
12-539 |
4.86e-20 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 93.87 E-value: 4.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 12 GADGVYRSLRPAARIESNPG--LSAVDLLLRRAAAcPSALALVDAATGHA--LTFSGLRSAILASAVALSsRAGVRPGDS 87
Cdd:cd05943 48 PYDVVVVSGRIMPGARWFPGarLNYAENLLRHADA-DDPAAIYAAEDGERteVTWAELRRRVARLAAALR-ALGVKPGDR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 88 VLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVITVAE---------LLPKVADLR--LP---- 152
Cdd:cd05943 126 VAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDAytyngkrhdVREKVAELVkgLPslla 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 153 VILLDDTAAK------SGSSATLYSDLVSGVD--EADYRRPPTkqSDTAGLLYSSGTTGESK-------GVVLTH-RNFI 216
Cdd:cd05943 206 VVVVPYTVAAgqpdlsKIAKALTLEDFLATGAagELEFEPLPF--DHPLYILYSSGTTGLPKcivhgagGTLLQHlKEHI 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 217 AaatmvtsdQDDRGEGPNVFL---CFLPMFH--IFGLSVitygqlqrGNTVVVMSG----FALDTVMSAVQQHRVTHLFC 287
Cdd:cd05943 284 L--------HCDLRPGDRLFYyttCGWMMWNwlVSGLAV--------GATIVLYDGspfyPDTNALWDLADEEGITVFGT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 288 VPPVMIALAKHGK--AGKYDLSSLKFIGSGAAPLGKDVMEAVAKNF-PDALICQGYGMTETCGIISLEYPE----KGQ-- 358
Cdd:cd05943 348 SAKYLDALEKAGLkpAETHDLSSLRTILSTGSPLKPESFDYVYDHIkPDVLLASISGGTDIISCFVGGNPLlpvyRGEiq 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 359 -------VRQFGSTGTLVTGveakivdvetlkhlppnQLGE-ICVRGPHIMQGYFNN------VQATEFTIRQG-WLHtG 423
Cdd:cd05943 428 crglgmaVEAFDEEGKPVWG-----------------EKGElVCTKPFPSMPVGFWNdpdgsrYRAAYFAKYPGvWAH-G 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 424 DLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEvDVQKF 503
Cdd:cd05943 490 DWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDD-ELRKR 568
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 357113996 504 IETQVtyykRLK--------RVTFVSSVPKSASGKILrrELIAK 539
Cdd:cd05943 569 IRSTI----RSAlsprhvpaKIIAVPDIPRTLSGKKV--EVAVK 606
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
83-457 |
6.32e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 93.26 E-value: 6.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 83 RPGDSVLLVAPNCVLYPVCFFAVTALGAVAStanPLYTPREIAKqasdararlvitvAELLPKVADLRLPVILLDDTAAK 162
Cdd:PRK07769 77 KPGDRVAILAPQNLDYLIAFFGALYAGRIAV---PLFDPAEPGH-------------VGRLHAVLDDCTPSAILTTTDSA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 163 SGSSAtLYSDL-------VSGVDE------ADYRRPPTKQSDTAGLLYSSGTTGESKGVVLTHRNfiaAAT----MVTS- 224
Cdd:PRK07769 141 EGVRK-FFRARpakerprVIAVDAvpdevgATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLN---LPTnvlqVIDAl 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 225 --DQDDRGegpnvfLCFLPMFHIFGLSVITYGQLQrGNTVVVMSGFALdtVMS--------AVQQHRVTHLFCVPP---- 290
Cdd:PRK07769 217 egQEGDRG------VSWLPFFHDMGLITVLLPALL-GHYITFMSPAAF--VRRpgrwirelARKPGGTGGTFSAAPnfaf 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 291 ---VMIALAKHGKAgKYDLSSLKFIGSGAAPLGKDVM----EAVAK-NFPDALICQGYGMTETC------------GIIS 350
Cdd:PRK07769 288 ehaAARGLPKDGEP-PLDLSNVKGLLNGSEPVSPASMrkfnEAFAPyGLPPTAIKPSYGMAEATlfvsttpmdeepTVIY 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 351 LEYPE-------------KGQVRQFgSTGTLVTGVEAKIVDVETLKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTIR- 416
Cdd:PRK07769 367 VDRDElnagrfvevpadaPNAVAQV-SAGKVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFQn 445
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 357113996 417 -----------QG------WLHTGDLGLFDDeGQLFVVDRLKELIKYKGFQIAPAELE 457
Cdd:PRK07769 446 ilksrlseshaEGapddalWVRTGDYGVYFD-GELYITGRVKDLVIIDGRNHYPQDLE 502
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
60-535 |
9.29e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 92.70 E-value: 9.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 60 LTFSGLRSAILASAVALSSRAgvRPGDSVLLVAPNCVLYPVCFFAVTALGAVAStanPLYTPreiAKQASDARARLVITV 139
Cdd:PRK05850 36 LTWSQLYRRTLNVAEELRRHG--STGDRAVILAPQGLEYIVAFLGALQAGLIAV---PLSVP---QGGAHDERVSAVLRD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 140 AEllpkvadlrlPVILLddTAAKSGSSATLYSDLVSG--------VDEADYRRP------PTKQSDTAGLLYSSGTTGES 205
Cdd:PRK05850 108 TS----------PSVVL--TTSAVVDDVTEYVAPQPGqsappvieVDLLDLDSPrgsdarPRDLPSTAYLQYTSGSTRTP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 206 KGVVLTHRNFIAAATMVTSDQ-DDRGEGP---NVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGFAldtvmsavqqhr 281
Cdd:PRK05850 176 AGVMVSHRNVIANFEQLMSDYfGDTGGVPppdTTVVSWLPFYHDMGLVLGVCAPILGGCPAVLTSPVA------------ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 282 vthlFCVPPV--MIALAKHGK----------------------AGkYDLSSLKFIGSGA-----APLGKDVMEAVAKNFP 332
Cdd:PRK05850 244 ----FLQRPArwMQLLASNPHafsaapnfafelavrktsdddmAG-LDLGGVLGIISGServhpATLKRFADRFAPFNLR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 333 DALICQGYGMTE-TCGIISLEY----------PEK---GQVRQFGS-TGT-LVT-GV----EAKIVDVETLKHLPPNQLG 391
Cdd:PRK05850 319 ETAIRPSYGLAEaTVYVATREPgqppesvrfdYEKlsaGHAKRCETgGGTpLVSyGSprspTVRIVDPDTCIECPAGTVG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 392 EICVRGPHIMQGYFNNVQATE--F----------TIRQGWLHTGDLGlFDDEGQLFVVDRLKELIKYKGFQIAPAELEGL 459
Cdd:PRK05850 399 EIWVHGDNVAAGYWQKPEETErtFgatlvdpspgTPEGPWLRTGDLG-FISEGELFIVGRIKDLLIVDGRNHYPDDIEAT 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 460 LlshPEI----LDAVVIPFPDAEAgEVPIAYVVRSPDSSLTEVDVQKFIETQVT------YYKRLKRVTFVS--SVPKSA 527
Cdd:PRK05850 478 I---QEItggrVAAISVPDDGTEK-LVAIIELKKRGDSDEEAMDRLRTVKREVTsaisksHGLSVADLVLVApgSIPITT 553
|
....*...
gi 357113996 528 SGKILRRE 535
Cdd:PRK05850 554 SGKIRRAA 561
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
187-536 |
6.16e-19 |
|
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: 89.42 E-value: 6.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 187 TKQSDTAGLLYSSGTTGESKGVVLTHR---NF----IAAATMVTSDQddrgEGPNVFLCF-LPMFHIFGLsvitygqLQR 258
Cdd:cd17644 103 TQPENLAYVIYTSGSTGKPKGVMIEHQslvNLshglIKEYGITSSDR----VLQFASIAFdVAAEEIYVT-------LLS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 259 GNTVVVMSG---FALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDL-SSLKFIGSGAAPLGKDVMEAVAKNFPDA 334
Cdd:cd17644 172 GATLVLRPEemrSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLpSSLRLVIVGGEAVQPELVRQWQKNVGNF 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 335 LIC-QGYGMTETCGIISLEYPEKGQVRQFGST--GTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQAT 411
Cdd:cd17644 252 IQLiNVYGPTEATIAATVCRLTQLTERNITSVpiGRPIANTQVYILD-ENLQPVPVGVPGELHIGGVGLARGYLNRPELT 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 412 -EFTIRQGWLH--------TGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEV 482
Cdd:cd17644 331 aEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKR 410
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 357113996 483 PIAYVVRSPDSSLTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd17644 411 LVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
36-431 |
1.79e-18 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 88.78 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 36 DLLLRRAAACPSALALVDAATGHA---LTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVA 112
Cdd:PRK08180 43 DRLVHWAQEAPDRVFLAERGADGGwrrLTYAEALERVRAIAQALLDR-GLSAERPLMILSGNSIEHALLALAAMYAGVPY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 113 STANPLYTpreiakQASDARARLVITVAELLPK----------------VADLRLPVILLddTAAKSGSSATLYSDLV-- 174
Cdd:PRK08180 122 APVSPAYS------LVSQDFGKLRHVLELLTPGlvfaddgaafaralaaVVPADVEVVAV--RGAVPGRAATPFAALLat 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 175 ---SGVDEADYRRPPtkqsDT-AGLLYSSGTTGESKGVVLTHRNFIAAATMVTSDQDDRGEGPNVFLCFLPMFHIFGLSV 250
Cdd:PRK08180 194 pptAAVDAAHAAVGP----DTiAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEPPVLVDWLPWNHTFGGNH 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 251 ITYGQLQRGNTVVVMSG------FAlDTV--MSAVQQhrvTHLFCVP-------PVM---IALAKHGkagkydLSSLKFI 312
Cdd:PRK08180 270 NLGIVLYNGGTLYIDDGkptpggFD-ETLrnLREISP---TVYFNVPkgwemlvPALerdAALRRRF------FSRLKLL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 313 GSGAAPLGKDV---MEAVAKNFPDA--LICQGYGMTETCG-IISLEYPEKGQvrqfGSTGTLVTGVEAKIVdvetlkhlP 386
Cdd:PRK08180 340 FYAGAALSQDVwdrLDRVAEATCGEriRMMTGLGMTETAPsATFTTGPLSRA----GNIGLPAPGCEVKLV--------P 407
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 357113996 387 PNQLGEICVRGPHIMQGYFNNVQATE--FTiRQGWLHTGDLGLFDDE 431
Cdd:PRK08180 408 VGGKLEVRVKGPNVTPGYWRAPELTAeaFD-EEGYYRSGDAVRFVDP 453
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
237-536 |
5.60e-18 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 86.59 E-value: 5.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 237 LCFLPMFHIFGL-----SVITYGQ--------LQRGNTvvvMSGFALDTVMSAV--QQHRVthlfcvppvmiaLAKHGKA 301
Cdd:PRK07445 164 FCVLPLYHVSGLmqfmrSFLTGGKlvilpykrLKSGQE---LPPNPSDFFLSLVptQLQRL------------LQLRPQW 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 302 gkydLSSLKFIGSGAAPLGKDVMEAVAK-NFPDALIcqgYGMTETCGIISLEYPEkgqvrQF----GSTGTLVTGVEAKI 376
Cdd:PRK07445 229 ----LAQFRTILLGGAPAWPSLLEQARQlQLRLAPT---YGMTETASQIATLKPD-----DFlagnNSSGQVLPHAQITI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 377 VdvetlkhlpPNQLGEICVRGPHIMQGYFNNVQATeftirQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAEL 456
Cdd:PRK07445 297 P---------ANQTGNITIQAQSLALGYYPQILDS-----QGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEV 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 457 EGLLLSHPEILDAVVIPFPDAEAGEVPIA-YVVRSPDSSLTEvdVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRRE 535
Cdd:PRK07445 363 EAAILATGLVQDVCVLGLPDPHWGEVVTAiYVPKDPSISLEE--LKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQ 440
|
.
gi 357113996 536 L 536
Cdd:PRK07445 441 L 441
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
13-431 |
7.03e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 87.02 E-value: 7.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 13 ADG--VYRS---LRPAARiesnpglSAVDLLLRRAAACPSALALVDAATGH----ALTFSGLRSAILASAVALSSRaGVR 83
Cdd:PRK12582 32 ADGsiVIKSrhpLGPYPR-------SIPHLLAKWAAEAPDRPWLAQREPGHgqwrKVTYGEAKRAVDALAQALLDL-GLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 84 PGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLY-----------------TPREIAKQASDARARLVITVAELLPKV 146
Cdd:PRK12582 104 PGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYslmshdhaklkhlfdlvKPRVVFAQSGAPFARALAALDLLDVTV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 147 ADLrlpvillddTAAKSGSSATLYSDLVS-----GVDEADYRRPPtkqsDTAG-LLYSSGTTGESKGVVLTHRNFIAAAT 220
Cdd:PRK12582 184 VHV---------TGPGEGIASIAFADLAAtpptaAVAAAIAAITP----DTVAkYLFTSGSTGMPKAVINTQRMMCANIA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 221 MVTS-DQDDRGEGPNVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGFAL----DTVMSAVQQHRVTHLFCVPPVMIAL 295
Cdd:PRK12582 251 MQEQlRPREPDPPPPVSLDWMPWNHTMGGNANFNGLLWGGGTLYIDDGKPLpgmfEETIRNLREISPTVYGNVPAGYAML 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 296 AKHGKA----GKYDLSSLKFIGSGAAPLGKDVME-----AVAKNFPDALICQGYGMTETCGIISLEYPEKGQVrqfGSTG 366
Cdd:PRK12582 331 AEAMEKddalRRSFFKNLRLMAYGGATLSDDLYErmqalAVRTTGHRIPFYTGYGATETAPTTTGTHWDTERV---GLIG 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 357113996 367 TLVTGVEakivdvetLKHLPPNQLGEICVRGPHIMQGYFNNVQATEFTI-RQGWLHTGDLGLFDDE 431
Cdd:PRK12582 408 LPLPGVE--------LKLAPVGDKYEVRVKGPNVTPGYHKDPELTAAAFdEEGFYRLGDAARFVDP 465
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
37-536 |
7.84e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 87.71 E-value: 7.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 37 LLLRRAAACPSALALVDAatGHALTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTAN 116
Cdd:PRK12316 3062 LFEEQVERTPDAVALAFG--EQRLSYAELNRRANRLAHRLIER-GVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLD 3138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 117 PLYTPREIAKQASDARARLVITVAEL-LPKVADLRlpVILLDdtaaksgssatlysdlvSGVDEADYRRPP--TKQSDTA 193
Cdd:PRK12316 3139 PEYPEERLAYMLEDSGAQLLLSQSHLrLPLAQGVQ--VLDLD-----------------RGDENYAEANPAirTMPENLA 3199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 194 GLLYSSGTTGESKGVVLTHRNFIAAATMVtsdQDDRGEGPNVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGFALDTV 273
Cdd:PRK12316 3200 YVIYTSGSTGKPKGVGIRHSALSNHLCWM---QQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDP 3276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 274 MSAVQQHRVTHLFCVPPVMIALAKH-GKAGKYDLSSLKFIGSGAAPLGKDVMEAVAKNFPdalICQGYGMTETCgIISLE 352
Cdd:PRK12316 3277 ALLVELINSEGVDVLHAYPSMLQAFlEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLP---LYNLYGPTEAT-ITVTH 3352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 353 YPEKGQVRQFGSTGTLVTGVEAKIVDVeTLKHLPPNQLGEICVRGPHIMQGYFNNVQATE-------FTIRQGWLHTGDL 425
Cdd:PRK12316 3353 WQCVEEGKDAVPIGRPIANRACYILDG-SLEPVPVGALGELYLGGEGLARGYHNRPGLTAerfvpdpFVPGERLYRTGDL 3431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 426 GLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIpfpdAEAGEVPIAYVVRSPDSSLTEVDVQKFIE 505
Cdd:PRK12316 3432 ARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYVVPEDEAGDLREALKAHLK 3507
|
490 500 510
....*....|....*....|....*....|.
gi 357113996 506 TQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:PRK12316 3508 ASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
455-530 |
9.19e-18 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 77.58 E-value: 9.19e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 357113996 455 ELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSPDSSLTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGK 530
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
48-536 |
2.88e-17 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 85.09 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 48 ALALVD--AATGHALTFSGLRSAILASAVALSSRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIA 125
Cdd:cd05905 1 AYTLLDskGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 126 KQASDARARLVITVaellpkVADLRLPVILLDDTAAKSGSSATL-YSDLVSGVDEADYRR---------PPTKQSDTAGL 195
Cdd:cd05905 81 FLLGTCKVRVALTV------EACLKGLPKKLLKSKTAAEIAKKKgWPKILDFVKIPKSKRsklkkwgphPPTRDGDTAYI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 196 LYSSGTTGESKGVVLTHRNFIAAATMVTSDQDDRGEGPnVFLCFLPM-----FH-----IF-GLSVITYGQlqrgnTVVV 264
Cdd:cd05905 155 EYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRP-LVTVLDFKsglglWHgcllsVYsGHHTILIPP-----ELMK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 265 MSGFALdtvMSAVQQHRVTHLFCVPPVMIALAK-------HGKAGKYDLSSLK-------------FIGSGAAPLGK--- 321
Cdd:cd05905 229 TNPLLW---LQTLSQYKVRDAYVKLRTLHWCLKdlsstlaSLKNRDVNLSSLRmcmvpcenrprisSCDSFLKLFQTlgl 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 322 --DVMEAVAKNFPDALIC-QGYGMTETC-----------GIISLEYPEKGQVRQFGSTGTLVTGVEAKIVDVETLKHLPP 387
Cdd:cd05905 306 spRAVSTEFGTRVNPFICwQGTSGPEPSrvyldmralrhGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 388 NQLGEICVRGPHIMQGYFNNVQATEFTIR-------------QGWLHTGDLGLF----------DDEGQLFVVDRLKELI 444
Cdd:cd05905 386 GEIGEIWVNSPANASGYFLLDGETNDTFKvfpstrlstgitnNSYARTGLLGFLrptkctdlnvEEHDLLFVVGSIDETL 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 445 KYKGFQIAPAELEG-LLLSHPEILDAVVipfpdAEAGEVPIAyVVRSPDSS------LTEVDVQKFIET-QVTYYKrlkr 516
Cdd:cd05905 466 EVRGLRHHPSDIEAtVMRVHPYRGRCAV-----FSITGLVVV-VAEQPPGSeeealdLVPLVLNAILEEhQVIVDC---- 535
|
570 580
....*....|....*....|..
gi 357113996 517 VTFVS--SVPKSASGKILRREL 536
Cdd:cd05905 536 VALVPpgSLPKNPLGEKQRMEI 557
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
73-513 |
7.59e-17 |
|
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: 83.49 E-value: 7.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 73 AVALSSRAGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREIAKQASDARARLVITVAELLPKVADLrLP 152
Cdd:cd05938 19 ARALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVAPELQEAVEEV-LP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 153 VILLDDT---AAKSGSSATLYSDLVSGVDEAD------YRRPPTKQSDTAGLLYSSGTTGESKGVVLTHRNFIAAATM-- 221
Cdd:cd05938 98 ALRADGVsvwYLSHTSNTEGVISLLDKVDAASdepvpaSLRAHVTIKSPALYIYTSGTTGLPKAARISHLRVLQCSGFls 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 222 ---VTSDqddrgegpNVFLCFLPMFHIFGLSVITYGQLQRGNTVVVMSGFALDTVMSAVQQHRVT----------HLFCV 288
Cdd:cd05938 178 lcgVTAD--------DVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKHNVTviqyigellrYLCNQ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 289 PPvmialAKHGKAGKYDLSslkfIGSGAAPlgkDVMEAVAKNFPDALICQGYGMTEtcGIIS-LEYPEK-GQVRQFGSTG 366
Cdd:cd05938 250 PQ-----SPNDRDHKVRLA----IGNGLRA---DVWREFLRRFGPIRIREFYGSTE--GNIGfFNYTGKiGAVGRVSYLY 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 367 TLVTGVEAKIVDVETLK----------HLPPNQLG----EICVRGPHImqGYFNNVQATEFTI-----RQG--WLHTGDL 425
Cdd:cd05938 316 KLLFPFELIKFDVEKEEpvrdaqgfciPVAKGEPGllvaKITQQSPFL--GYAGDKEQTEKKLlrdvfKKGdvYFNTGDL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 426 GLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVV--IPFPDAEaGEVPIAYVVRSPDSSLTEVDVQKF 503
Cdd:cd05938 394 LVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVygVTVPGHE-GRIGMAAVKLKPGHEFDGKKLYQH 472
|
490
....*....|
gi 357113996 504 IETQVTYYKR 513
Cdd:cd05938 473 VREYLPAYAR 482
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
46-536 |
7.61e-17 |
|
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: 83.29 E-value: 7.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 46 PSALALVDAAtgHALTFSGLRSAilASAVALSSRA-GVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREI 124
Cdd:cd17656 2 PDAVAVVFEN--QKLTYRELNER--SNQLARFLREkGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 125 AKQASDARARLVITVAELLPKVADLRLPVILLDDTAAK-SGSSATLysdlvsgVDEADyrrpptkqsDTAGLLYSSGTTG 203
Cdd:cd17656 78 IYIMLDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQeDTSNIDY-------INNSD---------DLLYIIYTSGTTG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 204 ESKGVVLTHRNFI-AAATMVTSDQDDRGEG------PNVFLCFLPMFhifglsvityGQLQRGNTVVVMSGFA---LDTV 273
Cdd:cd17656 142 KPKGVQLEHKNMVnLLHFEREKTNINFSDKvlqfatCSFDVCYQEIF----------STLLSGGTLYIIREETkrdVEQL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 274 MSAVQQHRVTHLFCvpPVMIalakhgkagkydlssLKFIGS---GAAPLGKDVMEAVA--------KNFPDALICQG--- 339
Cdd:cd17656 212 FDLVKRHNIEVVFL--PVAF---------------LKFIFSereFINRFPTCVKHIITageqlvitNEFKEMLHEHNvhl 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 340 ---YGMTETCGIISLEYPEKGQVRQFGSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQATE---- 412
Cdd:cd17656 275 hnhYGPSETHVVTTYTINPEAEIPELPPIGKPISNTWIYILD-QEQQLQPQGIVGELYISGASVARGYLNRQELTAekff 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 413 ---FTIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVr 489
Cdd:cd17656 354 pdpFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV- 432
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 357113996 490 sPDSSLTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd17656 433 -MEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
195-536 |
1.89e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 81.62 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 195 LLYSSGTTGESKgvvLTHRNF------IAAATMVTSDQDDrgEGPnVFLCflPMFHIFGLSVITYGQLQRGNTVVVMSGF 268
Cdd:PRK08308 106 LQYSSGTTGEPK---LIRRSWteidreIEAYNEALNCEQD--ETP-IVAC--PVTHSYGLICGVLAALTRGSKPVIITNK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 269 ALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKydlSSLKFIGSGAaPLgkdvmeavaknfPDAL----------ICQ 338
Cdd:PRK08308 178 NPKFALNILRNTPQHILYAVPLMLHILGRLLPGTF---QFHAVMTSGT-PL------------PEAWfyklrerttyMMQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 339 GYGMTETcGIISLEYPekgqVRQFGSTGTLVTGVEAKIVDVEtlkhlppNQLGEICVRgphimqgyfnnvqATEFTIrqg 418
Cdd:PRK08308 242 QYGCSEA-GCVSICPD----MKSHLDLGNPLPHVSVSAGSDE-------NAPEEIVVK-------------MGDKEI--- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 419 wlHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVvrSPDSSLTEV 498
Cdd:PRK08308 294 --FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKV--ISHEEIDPV 369
|
330 340 350
....*....|....*....|....*....|....*...
gi 357113996 499 DVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:PRK08308 370 QLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
38-471 |
3.50e-16 |
|
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: 81.32 E-value: 3.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 38 LLRRAAACPSALALVDAATGHA---LTFSGLRSAILASAVALSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVAST 114
Cdd:cd05921 1 LAHWARQAPDRTWLAEREGNGGwrrVTYAEALRQVRAIAQGLLDL-GLSAERPLLILSGNSIEHALMALAAMYAGVPAAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 115 ANPLY-----------------TPREIAKQASDARARlviTVAELLPkvadLRLPVILLddTAAKSGSSATLYSDLV--S 175
Cdd:cd05921 80 VSPAYslmsqdlaklkhlfellKPGLVFAQDAAPFAR---ALAAIFP----LGTPLVVS--RNAVAGRGAISFAELAatP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 176 GVDEADYRRPPTKQSDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVTSDQDDRGEGPNVFLCFLPMFHIFGLSVITYGQ 255
Cdd:cd05921 151 PTAAVDAAFAAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPPVLVDWLPWNHTFGGNHNFNLV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 256 LQRGNTVVVMSG------FAldTVMSAVQQHRVTHLFCVPP--VMIALAKHGKAG--KYDLSSLKFIGSGAAPLGKDVME 325
Cdd:cd05921 231 LYNGGTLYIDDGkpmpggFE--ETLRNLREISPTVYFNVPAgwEMLVAALEKDEAlrRRFFKRLKLMFYAGAGLSQDVWD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 326 AVaknfpDALICQ----------GYGMTETCGIISLEYpekGQVRQFGSTGTLVTGVEAKIVdvetlkhlPPNQLGEICV 395
Cdd:cd05921 309 RL-----QALAVAtvgeripmmaGLGATETAPTATFTH---WPTERSGLIGLPAPGTELKLV--------PSGGKYEVRV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 396 RGPHIMQGYFNNVQATEFTI-RQGWLHTGDLGLFDDEGQL---FVVD-RLKELIKYKG---FQIAPAELEGLLLSHPEIL 467
Cdd:cd05921 373 KGPNVTPGYWRQPELTAQAFdEEGFYCLGDAAKLADPDDPakgLVFDgRVAEDFKLASgtwVSVGPLRARAVAACAPLVH 452
|
....
gi 357113996 468 DAVV 471
Cdd:cd05921 453 DAVV 456
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
46-536 |
1.55e-15 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 78.75 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 46 PSALALVDaaTGHALTFSGLRSAilASAVALSSR-AGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANPLYTPREI 124
Cdd:cd17645 12 PDHVAVVD--RGQSLTYKQLNEK--ANQLARHLRgKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 125 AKQASDARARLVITVAEllpkvadlrlpvillddtaaksgssatlysdlvsgvdeadyrrpptkqsDTAGLLYSSGTTGE 204
Cdd:cd17645 88 AYMLADSSAKILLTNPD-------------------------------------------------DLAYVIYTSGSTGL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 205 SKGVVLTHRNFIaaaTMVTSDQDDRGEGPN----VFLCFlpMFHIFGLSVITYgqLQRGNTVVVMSG---FALDTVMSAV 277
Cdd:cd17645 119 PKGVMIEHHNLV---NLCEWHRPYFGVTPAdkslVYASF--SFDASAWEIFPH--LTAGAALHVVPSerrLDLDALNDYF 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 278 QQHRVTHLFCVPPV---MIALAKHgkagkydlsSLKFIGSGAaplgkDVMEAVAKNfpDALICQGYGMTE-TCGIISLE- 352
Cdd:cd17645 192 NQEGITISFLPTGAaeqFMQLDNQ---------SLRVLLTGG-----DKLKKIERK--GYKLVNNYGPTEnTVVATSFEi 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 353 YPEKGQVrqfgSTGTLVTGVEAKIVDvETLKHLPPNQLGEICVRGPHIMQGYFNNVQATE-------FTIRQGWLHTGDL 425
Cdd:cd17645 256 DKPYANI----PIGKPIDNTRVYILD-EALQLQPIGVAGELCIAGEGLARGYLNRPELTAekfivhpFVPGERMYRTGDL 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 426 GLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAEAGEVPIAYVVRSpdsslTEVDVQKFIE 505
Cdd:cd17645 331 AKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAP-----EEIPHEELRE 405
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 357113996 506 TQ---------VTYYKRLKrvtfvsSVPKSASGKILRREL 536
Cdd:cd17645 406 WLkndlpdymiPTYFVHLK------ALPLTANGKVDRKAL 439
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
35-536 |
2.37e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 79.83 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 35 VDLLLRRAAACPSALALVDAatGHALTFSGLRSAilASAVALSSR-AGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVAS 113
Cdd:PRK05691 1134 PELLNEQARQTPERIALVWD--GGSLDYAELHAQ--ANRLAHYLRdKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYV 1209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 114 TANPLYTPREIAKQASDARARLVITVAELLPKVADLR-LPVILLDDTAAKSgssatlYSDLVSGVDEADyrrpptkqSDT 192
Cdd:PRK05691 1210 PLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEgVSAIALDSLHLDS------WPSQAPGLHLHG--------DNL 1275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 193 AGLLYSSGTTGESKGVVLTHR------NFIAAATMVTSDQDDRGEGP-----NVFLCFLPMfhifglsvITYGQLqrgnt 261
Cdd:PRK05691 1276 AYVIYTSGSTGQPKGVGNTHAalaerlQWMQATYALDDSDVLMQKAPisfdvSVWECFWPL--------ITGCRL----- 1342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 262 VVVMSGFALDT--VMSAVQQHRVTHLFCVPPVMIALAKHGKAGkyDLSSLKFIGSGAAPLGKDVMEAVAKNFPDALICQG 339
Cdd:PRK05691 1343 VLAGPGEHRDPqrIAELVQQYGVTTLHFVPPLLQLFIDEPLAA--ACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNR 1420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 340 YGMTETcGIISLEYPEKGQVRQFGSTGTLVTGVEAKIVDVEtLKHLPPNQLGEICVRGPHIMQGYFNN--VQATEFTIR- 416
Cdd:PRK05691 1421 YGPTET-AINVTHWQCQAEDGERSPIGRPLGNVLCRVLDAE-LNLLPPGVAGELCIGGAGLARGYLGRpaLTAERFVPDp 1498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 417 -----QGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIPFPDAeAGEVPIAYVVRSP 491
Cdd:PRK05691 1499 lgedgARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGA-AGAQLVGYYTGEA 1577
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 357113996 492 DSSLTEVDVQKFIETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:PRK05691 1578 GQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
191-480 |
3.54e-15 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 77.86 E-value: 3.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 191 DTAGLLYSSGTTGESKGVVLTHRNFIAAATMVTSD--QDDrgeGPNVFLCfLPMFHIFGLSVITYGQLQRGNTVVVMSGF 268
Cdd:cd05937 88 DPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDlnLKN---GDRTYTC-MPLYHGTAAFLGACNCLMSGGTLALSRKF 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 269 ALDTVMSAVQQHRVTHLFCVppvmialakhGKAGKYDLSSLKFI-----------GSGAAPlgkDVMEAVAKNFPDALIC 337
Cdd:cd05937 164 SASQFWKDVRDSGATIIQYV----------GELCRYLLSTPPSPydrdhkvrvawGNGLRP---DIWERFRERFNVPEIG 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 338 QGYGMTEtcGIISLEYPEKG-----QVRQFGSTGTLVTGVEAKIV--DVET-----------LKHLPPNQLGEICVRGPH 399
Cdd:cd05937 231 EFYAATE--GVFALTNHNVGdfgagAIGHHGLIRRWKFENQVVLVkmDPETddpirdpktgfCVRAPVGEPGEMLGRVPF 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 400 I----MQGYFNNVQATEFTI-----RQG--WLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILD 468
Cdd:cd05937 309 KnreaFQGYLHNEDATESKLvrdvfRKGdiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAE 388
|
330
....*....|....*.
gi 357113996 469 AVV----IPFPDAEAG 480
Cdd:cd05937 389 ANVygvkVPGHDGRAG 404
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
185-534 |
6.13e-13 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 71.34 E-value: 6.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 185 PPTKQSDTAGLLYSSGTTGESKGVVLTHRNFIAAATMVtSDQDDRGEGPNVFLCFLPMFHIFGLSVITYGQL------QR 258
Cdd:PRK05851 147 TPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGL-NARVGLDAATDVGCSWLPLYHDMGLAFLLTAALagaplwLA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 259 GNTVVVMSGFALDTVMSavqQHRVThlFCVPPVMialaKHGKAGKY-------DLSSLKFIGSGAAPLGKDVMEAVAK-- 329
Cdd:PRK05851 226 PTTAFSASPFRWLSWLS---DSRAT--LTAAPNF----AYNLIGKYarrvsdvDLGALRVALNGGEPVDCDGFERFATam 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 330 ---NFPDALICQGYGMTE-TCGII-----------SLEYPEKGQVRQFGSTGTLVTGVEAKIVDVETLKHLPPNQLGEIC 394
Cdd:PRK05851 297 apfGFDAGAAAPSYGLAEsTCAVTvpvpgiglrvdEVTTDDGSGARRHAVLGNPIPGMEVRISPGDGAAGVAGREIGEIE 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 395 VRGPHIMQGYFNnvqatEFTIR-QGWLHTGDLGLFDDEGqLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVIP 473
Cdd:PRK05851 377 IRGASMMSGYLG-----QAPIDpDDWFPTGDLGYLVDGG-LVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVA 450
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 357113996 474 FPDAEAGEVP---IAYVVRSPDSSLTEVDVQKFIETQVTYYKrlKRVTFVS--SVPKSASGKiLRR 534
Cdd:PRK05851 451 VGTGEGSARPglvIAAEFRGPDEAGARSEVVQRVASECGVVP--SDVVFVApgSLPRTSSGK-LRR 513
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
198-472 |
1.21e-11 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 66.71 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 198 SSGTTGESKGVVLTHR------NFIA---AATMVTSDqdDRgegpnVFLCFLpmFHIF--GLSViTYGQLQRGNTVVVMS 266
Cdd:COG1541 91 SSGTTGKPTVVGYTRKdldrwaELFArslRAAGVRPG--DR-----VQNAFG--YGLFtgGLGL-HYGAERLGATVIPAG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 267 GFALDTVMSAVQQHRVTHLFCVPPVMIALAKHGKAGKYDLSSLK-----FIG-SGAAPLGKDVMEAVaknfpDALICQGY 340
Cdd:COG1541 161 GGNTERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEEGIDPRDLSlkkgiFGGePWSEEMRKEIEERW-----GIKAYDIY 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 341 GMTETCGIISLEYPEKGqvrqfgstGTLVTG----VEakIVDVETLKHLPPNQLGEICVrgphimqgyfnnvqaTEFT-- 414
Cdd:COG1541 236 GLTEVGPGVAYECEAQD--------GLHIWEdhflVE--IIDPETGEPVPEGEEGELVV---------------TTLTke 290
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357113996 415 ----IRqgwLHTGDLGLFDDE----GQ-----LFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVVI 472
Cdd:COG1541 291 amplIR---YRTGDLTRLLPEpcpcGRthpriGRILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQI 358
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
162-536 |
3.25e-11 |
|
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: 65.57 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 162 KSGSSATLYSDLVSgvDEADYRRPPTKQSDT---AGLLYS---SGTTGESKGVVLTHR---NFIAAAT---MVTSDQDDR 229
Cdd:cd17654 86 KCHVSYLLQNKELD--NAPLSFTPEHRHFNIrtdECLAYVihtSGTTGTPKIVAVPHKcilPNIQHFRslfNITSEDILF 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 230 GEGPNVFLCFLpmFHIFgLSVITYGQLQRGNTVVVMSGFALDTVMSavQQHRVTHLFCVPPVmiaLAKHGKAGKYD---- 305
Cdd:cd17654 164 LTSPLTFDPSV--VEIF-LSLSSGATLLIVPTSVKVLPSKLADILF--KRHRITVLQATPTL---FRRFGSQSIKStvls 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 306 -LSSLKFIGSGAAPLGKDVM-EAVAKNFPDALICQGYGMTETCgIISLEY--PEKGQVRQFGSTgTLVTGVEakIVDVET 381
Cdd:cd17654 236 aTSSLRVLALGGEPFPSLVIlSSWRGKGNRTRIFNIYGITEVS-CWALAYkvPEEDSPVQLGSP-LLGTVIE--VRDQNG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 382 LKHLPPNQLGEICVRGphIMQGYFNNVQATeftirqgWLHTGDLgLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLL 461
Cdd:cd17654 312 SEGTGQVFLGGLNRVC--ILDDEVTVPKGT-------MRATGDF-VTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIE 381
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357113996 462 SHPEILDAVVIPFPDaeagEVPIAYVVRSPDSSLTEVDVQKfieTQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd17654 382 SCLGVESCAVTLSDQ----QRLIAFIVGESSSSRIHKELQL---TLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
193-445 |
1.76e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 63.58 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 193 AGLLYSSGTTGESKGVVLTHRNFIAAATMVTSDQDDRGEGPNVFLCFLPMFHIFGlSVITYGQLQRGNTVVVMSG----F 268
Cdd:PTZ00342 307 TSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKHSIFKKYNPKTHLSYLPISHIYE-RVIAYLSFMLGGTINIWSKdinyF 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 269 ALD---------------------TVMSAVQQHRVTHLFCVPPVmIALAKHGKAGKY--------DLSS---------LK 310
Cdd:PTZ00342 386 SKDiynskgnilagvpkvfnriytNIMTEINNLPPLKRFLVKKI-LSLRKSNNNGGFskflegitHISSkikdkvnpnLE 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 311 FIGSGAAPLGKDVMEAVAkNFPDALICQGYGMTETCGIISLEYPEKGQVRQFGstGTLVTGVEAKIVDVETLK--HLPPN 388
Cdd:PTZ00342 465 VILNGGGKLSPKIAEELS-VLLNVNYYQGYGLTETTGPIFVQHADDNNTESIG--GPISPNTKYKVRTWETYKatDTLPK 541
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 357113996 389 qlGEICVRGPHIMQGYFNNVQATE--FTiRQGWLHTGDLGLFDDEGQLFVVDRLKELIK 445
Cdd:PTZ00342 542 --GELLIKSDSIFSGYFLEKEQTKnaFT-EDGYFKTGDIVQINKNGSLTFLDRSKGLVK 597
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
30-347 |
2.98e-10 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 62.89 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 30 PG--LSAVDLLLRRAAacPSALALVDAATGHA---LTFSGLRSaiLASAVALSSRA-GVRPGDSVLLVAPNCVLYPVCFF 103
Cdd:PRK03584 82 PGarLNYAENLLRHRR--DDRPAIIFRGEDGPrreLSWAELRR--QVAALAAALRAlGVGPGDRVAAYLPNIPETVVAML 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 104 AVTALGAVASTANPLYTPREIAKQASDARARLVITVA---------ELLPKVADLR--LP----VILLD----DTAAKSG 164
Cdd:PRK03584 158 ATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDgyryggkafDRRAKVAELRaaLPslehVVVVPylgpAAAAAAL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 165 SSATLYSDLVSGVDEADYRRPPTKQSDTAGLLYSSGTTGESK-------GVVLTHRNFIAAatmvtsdQDDRGEGPNVFL 237
Cdd:PRK03584 238 PGALLWEDFLAPAEAAELEFEPVPFDHPLWILYSSGTTGLPKcivhghgGILLEHLKELGL-------HCDLGPGDRFFW 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 238 ---CFLPM--FHIFGLSVitygqlqrGNTVVVMSG--FA--LDTVMSAVQQHRVTHLFCVPPVMIALAKHG-KAGK-YDL 306
Cdd:PRK03584 311 yttCGWMMwnWLVSGLLV--------GATLVLYDGspFYpdPNVLWDLAAEEGVTVFGTSAKYLDACEKAGlVPGEtHDL 382
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 357113996 307 SSLKFIGSGAAPLGKDVMEAVAKNF-PDALICQGYGMTETCG 347
Cdd:PRK03584 383 SALRTIGSTGSPLPPEGFDWVYEHVkADVWLASISGGTDICS 424
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
70-536 |
1.32e-08 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 57.43 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 70 LASAVA--LSSRaGVRPGDSVLLVAPNCVLYPVCFFAVTALGAVASTANplytpreiakqasdararlvitvaellpkvA 147
Cdd:cd05939 12 YSNKVAnfFQAQ-GYRSGDVVALFMENRLEFVALWLGLAKIGVETALIN------------------------------S 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 148 DLRLPVILLDDTAAKSGSsatLYSDLVSGVDEADYRRPPTKQ----SDTAGLLYSSGTTGESKGVVLTHRN--FIAA--A 219
Cdd:cd05939 61 NLRLESLLHCITVSKAKA---LIFNLLDPLLTQSSTEPPSQDdvnfRDKLFYIYTSGTTGLPKAAVIVHSRyyRIAAgaY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 220 TMVTSDQDDRgegpnVFLCfLPMFHIFGlSVITYGQ-LQRGNTVVVMSGFALDTVMSAVQQHRVT----------HLFCV 288
Cdd:cd05939 138 YAFGMRPEDV-----VYDC-LPLYHSAG-GIMGVGQaLLHGSTVVIRKKFSASNFWDDCVKYNCTivqyigeicrYLLAQ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 289 PPVMiALAKHgkagKYDLSslkfIGSGAAPlgkDVMEAVAKNFPDALICQGYGMTE-TCGIISLEypekGQVrqfGSTGT 367
Cdd:cd05939 211 PPSE-EEQKH----NVRLA----VGNGLRP---QIWEQFVRRFGIPQIGEFYGATEgNSSLVNID----NHV---GACGF 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 368 L------VTGVEAKIVDVETLKHL-PPNQLGEICVRG-PHIM-------------QGYFNNVQATEFTIRQGWLH----- 421
Cdd:cd05939 272 NsrilpsVYPIRLIKVDEDTGELIrDSDGLCIPCQPGePGLLvgkiiqndplrrfDGYVNEGATNKKIARDVFKKgdsaf 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 422 -TGDLGLFDDEGQLFVVDRLKELIKYKGFQIAPAELEGLLLSHPEILDAVV----IPFPDAEAGEVPIAYVVRspdsslt 496
Cdd:cd05939 352 lSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygveVPGVEGRAGMAAIVDPER------- 424
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 357113996 497 EVDVQKF---IETQVTYYKRLKRVTFVSSVPKSASGKILRREL 536
Cdd:cd05939 425 KVDLDRFsavLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDL 467
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
380-538 |
5.66e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 46.31 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 380 ETLKHLPPNQLGEICVRGPHIMQGYFNNVQATEF--------TIRQGWLHTGDLGLFDDEGQLFVVDRLKELIKYKGFQI 451
Cdd:PRK05691 4056 EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALafvphpfgAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRI 4135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357113996 452 APAELEGLLLSHPEILDAVVIpFPDAEAGEVPIAYVVRSP----DSSLTEvDVQKFIETQVTYYKRLKRVTFVSSVPKSA 527
Cdd:PRK05691 4136 ELGEIEARLHEQAEVREAAVA-VQEGVNGKHLVGYLVPHQtvlaQGALLE-RIKQRLRAELPDYMVPLHWLWLDRLPLNA 4213
|
170
....*....|.
gi 357113996 528 SGKILRRELIA 538
Cdd:PRK05691 4214 NGKLDRKALPA 4224
|
|
| |
