|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
4-539 |
0e+00 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 1047.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 4 ESNETNEFIFRSKLPDIHIPNHLPLHDYVFQNLSKFASRPCLINGATGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMN 83
Cdd:PLN02246 1 EASASEEFIFRSKLPDIYIPNHLPLHDYCFERLSEFSDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 84 LLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIVTMACFYDRVKDLA-ENGVQIVCVDFAVEGCLHF 162
Cdd:PLN02246 81 LLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLAeDDGVTVVTIDDPPEGCLHF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 163 SVLSGADESLAPLVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQMDGQNPNLYYHRNDVILCVLPFFHIYSLN 242
Cdd:PLN02246 161 SELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYFHSDDVILCVLPMFHIYSLN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 243 SILLCGLRVGAAIMIMQKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVRE 322
Cdd:PLN02246 241 SVLLCGLRVGAAILIMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 323 KFPTAILGQGYGMTEAGPVLSMSLAFAKEPFQVKAGACGTVVRNAEMKIVDTETGASLPANSSGEICIRGDQIMKGYLND 402
Cdd:PLN02246 321 KLPNAVLGQGYGMTEAGPVLAMCLAFAKEPFPVKSGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYLND 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 403 LESTKRTIDKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAF 482
Cdd:PLN02246 401 PEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAF 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 778728825 483 VMKANGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELRAKLASG 539
Cdd:PLN02246 481 VVRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAKLAAG 537
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
22-532 |
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: 748.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 22 IPNHLPLHDYVFQNLSKFASRPCLINGATGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYR 101
Cdd:cd05904 1 LPTDLPLDSVSFLFASAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 102 GAIMTAANPFYTAVEIAKQAKAANAKLIVTMACFYDRVKDLaenGVQIVCVDFAVEGCLHFSVLS-GADESLAPLVDFSS 180
Cdd:cd05904 81 GAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLASL---ALPVVLLDSAEFDSLSFSDLLfEADEAEPPVVVIKQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 181 NDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQMDGQNPNLyyHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQK 260
Cdd:cd05904 158 DDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNS--DSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 261 FDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILGQGYGMTEAGP 340
Cdd:cd05904 236 FDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 341 VLSMSLAFAKEPfqVKAGACGTVVRNAEMKIVDTETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLHTGD 420
Cdd:cd05904 316 VVAMCFAPEKDR--AKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 421 IGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFI 500
Cdd:cd05904 394 LCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFV 473
|
490 500 510
....*....|....*....|....*....|..
gi 778728825 501 AKQVVFYKRLKRVFFVNAIPKAPSGKILRKEL 532
Cdd:cd05904 474 AKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
44-528 |
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: 569.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 44 CLINGATGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKA 123
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 124 ANAKLIVTMACFYDRVKDLAEN---GVQIVCVDFAVEGCLH-----FSVLSGADESLAPLVDFSSNDVVALPYSSGTTGL 195
Cdd:cd05911 81 SKPKVIFTDPDGLEKVKEAAKElgpKDKIIVLDDKPDGVLSiedllSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 196 PKGVMLTHKGLITSVAQQMDGQNPNlyYHRNDVILCVLPFFHIYSLNSILLCGLRvGAAIMIMQKFDIVALLQLIEKHRI 275
Cdd:cd05911 161 PKGVCLSHRNLIANLSQVQTFLYGN--DGSNDVILGFLPLYHIYGLFTTLASLLN-GATVIIMPKFDSELFLDLIEKYKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 276 SIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILGQGYGMTEAGPVLSMSLafakePFQV 355
Cdd:cd05911 238 TFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVNP-----DGDD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 356 KAGACGTVVRNAEMKIVDTETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLHTGDIGFVDDDNELFIVDR 435
Cdd:cd05911 313 KPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 436 LKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVFYKRL-KRVF 514
Cdd:cd05911 393 KKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYKQLrGGVV 472
|
490
....*....|....
gi 778728825 515 FVNAIPKAPSGKIL 528
Cdd:cd05911 473 FVDEIPKSASGKIL 486
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
28-540 |
1.19e-151 |
|
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: 441.94 E-value: 1.19e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 28 LHDYVFQNLSKFASRPCLINGatGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTA 107
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG--GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 108 ANPFYTAveiakqakaanaklivtmacfyDRVKDLAEN-GVQIVCVdfavegclhfsvlsgadeslaplvdfssndvVAL 186
Cdd:COG0318 79 LNPRLTA----------------------EELAYILEDsGARALVT-------------------------------ALI 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 187 PYSSGTTGLPKGVMLTHKGLITSVAQQMDGqnpnLYYHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKFDIVAL 266
Cdd:COG0318 106 LYTSGTTGRPKGVMLTHRNLLANAAAIAAA----LGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 267 LQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILgQGYGMTEAGPVLSMSL 346
Cdd:COG0318 182 LELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIV-EGYGLTETSPVVTVNP 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 347 AfakEPFQVKAGACGTVVRNAEMKIVDtETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIdKEGWLHTGDIGFVDD 426
Cdd:COG0318 261 E---DPGERRPGSVGRPLPGVEVRIVD-EDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDE 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 427 DNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVF 506
Cdd:COG0318 336 DGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLAR 415
|
490 500 510
....*....|....*....|....*....|....
gi 778728825 507 YKRLKRVFFVNAIPKAPSGKILRKELRAKLASGA 540
Cdd:COG0318 416 YKVPRRVEFVDELPRTASGKIDRRALRERYAAGA 449
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
1-538 |
1.48e-151 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 445.19 E-value: 1.48e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 1 MAFESNETNEFIFRSKLPDIHIPNHLPLHDYVFQNLSKFASRPCLINGATGDVYTYHDVQLTARRVAAGLHNLGIKKGDV 80
Cdd:PLN02330 3 MEIQKQEDNEHIFRSRYPSVPVPDKLTLPDFVLQDAELYADKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 81 VMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIVTMACFYDRVKDLaenGVQ-IVCVDFAVEGC 159
Cdd:PLN02330 83 VVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGL---GLPvIVLGEEKIEGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 160 LHFS-VLSGADESLAPLV--DFSSNDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQMDGQNPNLYYHRndVILCVLPFF 236
Cdd:PLN02330 160 VNWKeLLEAADRAGDTSDneEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMIGQV--VTLGLIPFF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 237 HIYSLNSILLCGLRVGAAIMIMQKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSV--RVLKSGGAPLGK 314
Cdd:PLN02330 238 HIYGITGICCATLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLklQAIMTAAAPLAP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 315 ELEDAVREKFPTAILGQGYGMTEAGPVLSMSLAFAKEPFQVKAGACGTVVRNAEMKIVDTETGASLPANSSGEICIRGDQ 394
Cdd:PLN02330 318 ELLTAFEAKFPGVQVQEAYGLTEHSCITLTHGDPEKGHGIAKKNSVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQC 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 395 IMKGYLNDLESTKRTIDKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVE 474
Cdd:PLN02330 398 VMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEE 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 778728825 475 AGEVPVAFVMKANGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELRAKLAS 538
Cdd:PLN02330 478 AGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLS 541
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
34-533 |
3.32e-135 |
|
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: 400.40 E-value: 3.32e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 34 QNLSKFASRPCLINGatGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYT 113
Cdd:cd05936 7 EAARRFPDKTALIFM--GRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 114 AVEIAKQAKAANAKLIVTMACFYDRVKdlaengvqivcvdfavegclhfsvlsgADESLAPLVDFSSNDVVALPYSSGTT 193
Cdd:cd05936 85 PRELEHILNDSGAKALIVAVSFTDLLA---------------------------AGAPLGERVALTPEDVAVLQYTSGTT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 194 GLPKGVMLTHKGLItSVAQQMDGQNPNLYYHRnDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKFDIVALLQLIEKH 273
Cdd:cd05936 138 GVPKGAMLTHRNLV-ANALQIKAWLEDLLEGD-DVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGVLKEIRKH 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 274 RISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILgQGYGMTEAGPVLsmslAFAKEPF 353
Cdd:cd05936 216 RVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIV-EGYGLTETSPVV----AVNPLDG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 354 QVKAGACGTVVRNAEMKIVDTEtGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIdKEGWLHTGDIGFVDDDNELFIV 433
Cdd:cd05936 291 PRKPGSIGIPLPGTEVKIVDDD-GEELPPGEVGELWVRGPQVMKGYWNRPEETAEAF-VDGWLRTGDIGYMDEDGYFFIV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 434 DRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVFYKRLKRV 513
Cdd:cd05936 369 DRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQV 448
|
490 500
....*....|....*....|
gi 778728825 514 FFVNAIPKAPSGKILRKELR 533
Cdd:cd05936 449 EFRDELPKSAVGKILRRELR 468
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
3-537 |
7.50e-131 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 392.67 E-value: 7.50e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 3 FESNETNefIFRSKLPDIHIPN--HLPLHDYVFQNlSKFASRPCLINGATGDVYTYHDVQLTARRVAAGLHN-LGIKKGD 79
Cdd:PLN02574 17 WYSPETG--IYSSKHPPVPLPSdpNLDAVSFIFSH-HNHNGDTALIDSSTGFSISYSELQPLVKSMAAGLYHvMGVRQGD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 80 VVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIVTMAcfyDRVKDLAENGVQIVCV------- 152
Cdd:PLN02574 94 VVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSP---ENVEKLSPLGVPVIGVpenydfd 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 153 DFAVEGCLHFSVLSGADESL-APLVdfSSNDVVALPYSSGTTGLPKGVMLTHKGLITSV-------AQQMDgqnpnlYYH 224
Cdd:PLN02574 171 SKRIEFPKFYELIKEDFDFVpKPVI--KQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVelfvrfeASQYE------YPG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 225 RNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDV-SSVR 303
Cdd:PLN02574 243 SDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEVlKSLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 304 VLKSGGAPL-GKELEDAVrEKFPTAILGQGYGMTEAGPVlsMSLAFAKEPFQvKAGACGTVVRNAEMKIVDTETGASLPA 382
Cdd:PLN02574 323 QVSCGAAPLsGKFIQDFV-QTLPHVDFIQGYGMTESTAV--GTRGFNTEKLS-KYSSVGLLAPNMQAKVVDWSTGCLLPP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 383 NSSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKL 462
Cdd:PLN02574 399 GNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEI 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 778728825 463 SDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELRAKLA 537
Cdd:PLN02574 479 IDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLT 553
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
31-533 |
1.49e-125 |
|
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: 378.02 E-value: 1.49e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 31 YVFQNLSKFASRPCLINGATGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANP 110
Cdd:cd17642 22 KAMKRYASVPGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTND 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 111 FYTAVEIAKQAKAANAKLIVTMACFYDRVKDLAENG--VQ-IVCVDFAVE----GCLHFSVLS----GADESLAPLVDFS 179
Cdd:cd17642 102 IYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLkiIKtIIILDSKEDykgyQCLYTFITQnlppGFNEYDFKPPSFD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 180 SNDVVAL-PYSSGTTGLPKGVMLTHKGLITSVAQQMD---GQNPNlyyhRNDVILCVLPFFH---IYSLNSILLCGLRVg 252
Cdd:cd17642 182 RDEQVALiMNSSGSTGLPKGVQLTHKNIVARFSHARDpifGNQII----PDTAILTVIPFHHgfgMFTTLGYLICGFRV- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 253 aaiMIMQKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILGQG 332
Cdd:cd17642 257 ---VLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 333 YGMTEAgpvlSMSLAFAKEPFqVKAGACGTVVRNAEMKIVDTETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIDK 412
Cdd:cd17642 334 YGLTET----TSAILITPEGD-DKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 413 EGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAIS 492
Cdd:cd17642 409 DGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMT 488
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 778728825 493 EEEVKQFIAKQVVFYKRLK-RVFFVNAIPKAPSGKILRKELR 533
Cdd:cd17642 489 EKEVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIR 530
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
29-540 |
1.67e-125 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 377.60 E-value: 1.67e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 29 HDYVFQNLSKFASRPCLING------ATGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRG 102
Cdd:PRK06187 1 MQDYPLTIGRILRHGARKHPdkeavyFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 103 AIMTAANPFYTAVEIAKQAKAANAKLIVTMACFYDRVKDLAE--NGVQIVCV--DFAVEGC----LHFSVLSGADESLAP 174
Cdd:PRK06187 81 AVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPqlPTVRTVIVegDGPAAPLapevGEYEELLAAASDTFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 175 LVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLIT---SVAQQMDgqnpnlyYHRNDVILCVLPFFHIYSLNSILLcGLRV 251
Cdd:PRK06187 161 FPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLhslAVCAWLK-------LSRDDVYLVIVPMFHVHAWGLPYL-ALMA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 252 GAAIMIMQKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILgQ 331
Cdd:PRK06187 233 GAKQVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDLV-Q 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 332 GYGMTEAGPVLSMSLAFAKEPFQV-KAGACGTVVRNAEMKIVDTEtGASLPAN--SSGEICIRGDQIMKGYLNDLESTKR 408
Cdd:PRK06187 312 GYGMTETSPVVSVLPPEDQLPGQWtKRRSAGRPLPGVEARIVDDD-GDELPPDggEVGEIIVRGPWLMQGYWNRPEATAE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 409 TIDKeGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANG 488
Cdd:PRK06187 391 TIDG-GWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPG 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 778728825 489 GAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELRAKLASGA 540
Cdd:PRK06187 470 ATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQYAEGK 521
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
32-441 |
5.67e-124 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 370.10 E-value: 5.67e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 32 VFQNLSKFASRPCLINGaTGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPF 111
Cdd:pfam00501 1 LERQAARTPDKTALEVG-EGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 112 YTAVEIAKQAKAANAKLIVTMACFY----DRVKDLAENGVQIVCVD---FAVEGCLHFSVLSgADESLAPLVDFSSNDVV 184
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDALKleelLEALGKLEVVKLVLVLDrdpVLKEEPLPEEAKP-ADVPPPPPPPPDPDDLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 185 ALPYSSGTTGLPKGVMLTHKGLITSVAQQMDGQNPNLYYHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKF--- 261
Cdd:pfam00501 159 YIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFpal 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 262 DIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILgQGYGMTEAGPV 341
Cdd:pfam00501 239 DPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALV-NGYGLTETTGV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 342 lsMSLAFAKEPFQVKAGACGTVVRNAEMKIVDTETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLHTGDI 421
Cdd:pfam00501 318 --VTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDL 395
|
410 420
....*....|....*....|
gi 778728825 422 GFVDDDNELFIVDRLKELIK 441
Cdd:pfam00501 396 GRRDEDGYLEIVGRKKDQIK 415
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
55-535 |
1.18e-123 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 372.70 E-value: 1.18e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 55 TYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIVTMAC 134
Cdd:PRK07656 32 TYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 135 F----YDRVKDLAENGVQIVC----VDFAVEGCLHFS--VLSGADESLAPLVDfsSNDVVALPYSSGTTGLPKGVMLTHK 204
Cdd:PRK07656 112 FlgvdYSATTRLPALEHVVICeteeDDPHTEKMKTFTdfLAAGDPAERAPEVD--PDDVADILFTSGTTGRPKGAMLTHR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 205 GLItSVAQQMDGqnpNLYYHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKFDIVALLQLIEKHRISIMPIVPPI 284
Cdd:PRK07656 190 QLL-SNAADWAE---YLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLPVFDPDEVFRLIETERITVLPGPPTM 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 285 FLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILGQGYGMTEAGPVLSMSLAfaKEPFQVKAGACGTVV 364
Cdd:PRK07656 266 YNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVLTGYGLSEASGVTTFNRL--DDDRKTVAGTIGTAI 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 365 RNAEMKIVDtETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKA 444
Cdd:PRK07656 344 AGVENKIVN-ELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGG 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 445 FQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPS 524
Cdd:PRK07656 423 FNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNAT 502
|
490
....*....|.
gi 778728825 525 GKILRKELRAK 535
Cdd:PRK07656 503 GKVLKRALREK 513
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
32-529 |
6.76e-119 |
|
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: 357.69 E-value: 6.76e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 32 VFQNLSKFASRPCLINGatGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPF 111
Cdd:cd17631 1 LRRRARRHPDRTALVFG--GRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 112 YTAVEIakqakaanaklivtmacfydrvKDLAENgvqivcvdfavegclhfsvlSGAdeslAPLVDfssnDVVALPYSSG 191
Cdd:cd17631 79 LTPPEV----------------------AYILAD--------------------SGA----KVLFD----DLALLMYTSG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 192 TTGLPKGVMLTHKGLITSVAQQMDGQNPNlyyhRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKFDIVALLQLIE 271
Cdd:cd17631 109 TTGRPKGAMLTHRNLLWNAVNALAALDLG----PDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIE 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 272 KHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKfpTAILGQGYGMTEAGPVLSMSLAfakE 351
Cdd:cd17631 185 RHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQAR--GVKFVQGYGMTETSPGVTFLSP---E 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 352 PFQVKAGACGTVVRNAEMKIVDTEtGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIdKEGWLHTGDIGFVDDDNELF 431
Cdd:cd17631 260 DHRRKLGSAGRPVFFVEVRIVDPD-GREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLY 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 432 IVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVFYKRLK 511
Cdd:cd17631 338 IVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPK 417
|
490
....*....|....*...
gi 778728825 512 RVFFVNAIPKAPSGKILR 529
Cdd:cd17631 418 SVEFVDALPRNATGKILK 435
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
182-528 |
4.13e-115 |
|
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: 344.27 E-value: 4.13e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 182 DVVALPYSSGTTGLPKGVMLTHKGLITSVAqqmdGQNPNLYYHRNDVILCVLPFFHIYSLNSILLCgLRVGAAIMIMQKF 261
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAA----ALAASGGLTEGDVFLSTLPLFHIGGLFGLLGA-LLAGGTVVLLPKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 262 DIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILgQGYGMTEAGPV 341
Cdd:cd04433 76 DPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLV-NGYGLTETGGT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 342 LSMSLAFAKEpfqVKAGACGTVVRNAEMKIVDTETGAsLPANSSGEICIRGDQIMKGYLNDLEsTKRTIDKEGWLHTGDI 421
Cdd:cd04433 155 VATGPPDDDA---RKPGSVGRPVPGVEVRIVDPDGGE-LPPGEIGELVVRGPSVMKGYWNNPE-ATAAVDEDGWYRTGDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 422 GFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIA 501
Cdd:cd04433 230 GRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVR 309
|
330 340
....*....|....*....|....*..
gi 778728825 502 KQVVFYKRLKRVFFVNAIPKAPSGKIL 528
Cdd:cd04433 310 ERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
55-532 |
2.50e-98 |
|
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: 304.40 E-value: 2.50e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 55 TYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQakaanaklivtmac 134
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYI-------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 135 fydrvkdLAENGVQIVCVDFAVEgclhfsvlsgadeslaplvdfssnDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQM 214
Cdd:cd05935 69 -------LNDSGAKVAVVGSELD------------------------DLALIPYTSGTTGLPKGCMHTHFSAAANALQSA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 215 DGQNPNlyyhRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEF 294
Cdd:cd05935 118 VWTGLT----PSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEF 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 295 EKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILgQGYGMTEAgpvlsMSLAFAKEPFQVKAGACGTVVRNAEMKIVDT 374
Cdd:cd05935 194 KTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFV-EGYGLTET-----MSQTHTNPPLRPKLQCLGIP*FGVDARVIDI 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 375 ETGASLPANSSGEICIRGDQIMKGYLNDLESTKR---TIDKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAE 451
Cdd:cd05935 268 ETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEEsfiEIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 452 LEALLITHPKLSDAAVIGMPDVEAGEVPVAFVM--KANGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILR 529
Cdd:cd05935 348 VEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVlrPEYRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILW 427
|
...
gi 778728825 530 KEL 532
Cdd:cd05935 428 RLL 430
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
40-533 |
1.85e-97 |
|
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: 304.24 E-value: 1.85e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 40 ASRPCLINGATGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAK 119
Cdd:cd05926 1 PDAPALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 120 QAKAANAKLIVTMAC-----------FYDRVKDLAENGVQIVCVDFAVEGCLHFSVLSGADESLAPLVDfssnDVVALPY 188
Cdd:cd05926 81 YLADLGSKLVLTPKGelgpasraaskLGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGVPLPD----DLALILH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 189 SSGTTGLPKGVMLTHKGLITSVaqqmdgQNPNLYYH--RNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKFDIVAL 266
Cdd:cd05926 157 TSGTTGRPKGVPLTHRNLAASA------TNITNTYKltPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 267 LQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDV-SSVRVLKSGGAPLGKELEDAVREKFPTAILgQGYGMTEAGP-VLSM 344
Cdd:cd05926 231 WPDVRDYNATWYTAVPTIHQILLNRPEPNPESPpPKLRFIRSCSASLPPAVLEALEATFGAPVL-EAYGMTEAAHqMTSN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 345 SLafakEPFQVKAGACGTVVrNAEMKIVDtETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLHTGDIGFV 424
Cdd:cd05926 310 PL----PPGPRKPGSVGKPV-GVEVRILD-EDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 425 DDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQV 504
Cdd:cd05926 384 DADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHL 463
|
490 500
....*....|....*....|....*....
gi 778728825 505 VFYKRLKRVFFVNAIPKAPSGKILRKELR 533
Cdd:cd05926 464 AAFKVPKKVYFVDELPKTATGKIQRRKVA 492
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
27-532 |
1.89e-94 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 298.87 E-value: 1.89e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 27 PLHDYVFQNLSKFASRPCLinGATGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMT 106
Cdd:PRK06710 25 PLHKYVEQMASRYPEKKAL--HFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 107 AANPFYTAVEIAKQAKAANAKLIVTMACFYDRV------------------------KDLAENGVQ------IVCVDFAV 156
Cdd:PRK06710 103 QTNPLYTERELEYQLHDSGAKVILCLDLVFPRVtnvqsatkiehvivtriadflpfpKNLLYPFVQkkqsnlVVKVSESE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 157 EGCLHFSVLSGADESLAPLVDfSSNDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQMDGqnpnLY--YHRNDVILCVLP 234
Cdd:PRK06710 183 TIHLWNSVEKEVNTGVEVPCD-PENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQW----LYncKEGEEVVLGVLP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 235 FFHIYSLNSILLCGLRVGAAIMIMQKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGK 314
Cdd:PRK06710 258 FFHVYGMTAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 315 EledaVREKFPTAILG---QGYGMTEAGPVLSMSLAFAKEpfqvKAGACGTVVRNAEMKIVDTETGASLPANSSGEICIR 391
Cdd:PRK06710 338 E----VQEKFETVTGGklvEGYGLTESSPVTHSNFLWEKR----VPGSIGVPWPDTEAMIMSLETGEALPPGEIGEIVVK 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 392 GDQIMKGYLNDLESTKRTIdKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMP 471
Cdd:PRK06710 410 GPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVP 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 778728825 472 DVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKEL 532
Cdd:PRK06710 489 DPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
29-537 |
9.74e-94 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 297.02 E-value: 9.74e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 29 HDYVFQNLSKFASRPCLI-NGATGDV--YTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIM 105
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIwEGEDGEErtLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 106 TAANPFYTAVEIAKQAKAANAKLIVTMACFYDRVK--DLAEN---------GVQIVCV------DFAVEGCLHFS-VLSG 167
Cdd:COG0365 92 SPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKviDLKEKvdealeelpSLEHVIVvgrtgaDVPMEGDLDWDeLLAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 168 ADESLAPlVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLI----TSVAQQMDgqnpnlyYHRNDVILCVLPFFHIYSLNS 243
Cdd:COG0365 172 ASAEFEP-EPTDADDPLFILYTSGTTGKPKGVVHTHGGYLvhaaTTAKYVLD-------LKPGDVFWCTADIGWATGHSY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 244 ILLCGLRVGAAIMIMQK----FDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEF--EKYDVSSVRVLKSGGAPLGKELE 317
Cdd:COG0365 244 IVYGPLLNGATVVLYEGrpdfPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEplKKYDLSSLRLLGSAGEPLNPEVW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 318 DAVREKFPTAILgQGYGMTEAGpvLSMSLAFAKEPfqVKAGACGTVVRNAEMKIVDtETGASLPANSSGEICIRGDQ--I 395
Cdd:COG0365 324 EWWYEAVGVPIV-DGWGQTETG--GIFISNLPGLP--VKPGSMGKPVPGYDVAVVD-EDGNPVPPGEEGELVIKGPWpgM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 396 MKGYLNDLESTKRTI--DKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDV 473
Cdd:COG0365 398 FRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDE 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 778728825 474 EAGEVPVAFVMKANGGAISEE---EVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELRAKLA 537
Cdd:COG0365 478 IRGQVVKAFVVLKPGVEPSDElakELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAE 544
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
28-539 |
3.95e-92 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 293.06 E-value: 3.95e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 28 LHDYVFQNLSKFASRPCL-INGATgdvYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMT 106
Cdd:PRK05605 34 LVDLYDNAVARFGDRPALdFFGAT---TTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 107 AANPFYTAVEIAKQAKAANAKLIVtmacFYDRVKDLAENGVQ------IVCVDF-------------------------- 154
Cdd:PRK05605 111 EHNPLYTAHELEHPFEDHGARVAI----VWDKVAPTVERLRRttpletIVSVNMiaampllqrlalrlpipalrkaraal 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 155 --AVEGCLHFSVLSGA----DESLAPLVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLITSVAQqmdGQN--PNLYyHRN 226
Cdd:PRK05605 187 tgPAPGTVPWETLVDAaiggDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQ---GKAwvPGLG-DGP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 227 DVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLK 306
Cdd:PRK05605 263 ERVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAF 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 307 SGGAPLGKELedaVR--EKFPTAILGQGYGMTEAGPVLsmslafAKEPFQV--KAGACGTVVRNAEMKIVDTET-GASLP 381
Cdd:PRK05605 343 SGAMALPVST---VElwEKLTGGLLVEGYGLTETSPII------VGNPMSDdrRPGYVGVPFPDTEVRIVDPEDpDETMP 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 382 ANSSGEICIRGDQIMKGYLNDLESTKRTIdKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPK 461
Cdd:PRK05605 414 DGEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPG 492
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 778728825 462 LSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELRAKLASG 539
Cdd:PRK05605 493 VEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREELLEK 570
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
38-540 |
2.13e-90 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 286.83 E-value: 2.13e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 38 KFASRPCLINGATgdVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEI 117
Cdd:PRK08316 23 RYPDKTALVFGDR--SWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 118 AKQAKAANAKLIVTMACFYDRVKDLAENGVQ-------IVCVDFAVEGCLHFSVLSGADESLAPLVDFSSNDVVALPYSS 190
Cdd:PRK08316 101 AYILDHSGARAFLVDPALAPTAEAALALLPVdtlilslVLGGREAPGGWLDFADWAEAGSVAEPDVELADDDLAQILYTS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 191 GTTGLPKGVMLTHKGLI-----TSVAQQMDGqnpnlyyhrNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKFDIVA 265
Cdd:PRK08316 181 GTESLPKGAMLTHRALIaeyvsCIVAGDMSA---------DDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAPDPEL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 266 LLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILGQGYGMTEAGPvLSMS 345
Cdd:PRK08316 252 ILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERLPGLRFYNCYGQTEIAP-LATV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 346 LAfaKEPFQVKAGACGTVVRNAEMKIVDtETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIdKEGWLHTGDIGFVD 425
Cdd:PRK08316 331 LG--PEEHLRRPGSAGRPVLNVETRVVD-DDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMD 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 426 DDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVV 505
Cdd:PRK08316 407 EEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLA 486
|
490 500 510
....*....|....*....|....*....|....*
gi 778728825 506 FYKRLKRVFFVNAIPKAPSGKILRKELRAKLASGA 540
Cdd:PRK08316 487 GFKVPKRVIFVDELPRNPSGKILKRELRERYAGAF 521
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
182-533 |
7.25e-90 |
|
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: 279.93 E-value: 7.25e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 182 DVVALPYSSGTTGLPKGVMLTHKGLIT---SVAQQMDgqnpnlyYHRNDVILCVLPFFHIY-SLNSILLCGLRVGAAIMI 257
Cdd:cd05917 3 DVINIQFTSGTTGSPKGATLTHHNIVNngyFIGERLG-------LTEQDRLCIPVPLFHCFgSVLGVLACLTHGATMVFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 258 MQKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILGQGYGMTE 337
Cdd:cd05917 76 SPSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 338 AGPVLSMSlaFAKEPFQVKAGACGTVVRNAEMKIVDTETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLH 417
Cdd:cd05917 156 TSPVSTQT--RTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 418 TGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVK 497
Cdd:cd05917 234 TGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIK 313
|
330 340 350
....*....|....*....|....*....|....*.
gi 778728825 498 QFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELR 533
Cdd:cd05917 314 AYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
51-532 |
4.73e-84 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 271.06 E-value: 4.73e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 51 GDVYTYHDVQLTARRVAAGLHN-LGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLI 129
Cdd:PRK08314 33 GRAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 130 VTMACFYDRVKDLAEN-GVQ-IVCVDFA--------------------VEGCLHFSVLSGAD---ESLAPL-VDFSSNDV 183
Cdd:PRK08314 113 IVGSELAPKVAPAVGNlRLRhVIVAQYSdylpaepeiavpawlraeppLQALAPGGVVAWKEalaAGLAPPpHTAGPDDL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 184 VALPYSSGTTGLPKGVMLTHKGLITSVAQQMDGQNPnlyyHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKFDI 263
Cdd:PRK08314 193 AVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNS----TPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMPRWDR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 264 VALLQLIEKHRISIMPIVPPI---FLAiakSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILgQGYGMTEagp 340
Cdd:PRK08314 269 EAAARLIERYRVTHWTNIPTMvvdFLA---SPGLAERDLSSLRYIGGGGAAMPEAVAERLKELTGLDYV-EGYGLTE--- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 341 vlSMSLAFAKEPFQVKAGACGTVVRNAEMKIVDTETGASLPANSSGEICIRGDQIMKGYLNDLESTKR---TIDKEGWLH 417
Cdd:PRK08314 342 --TMAQTHSNPPDRPKLQCLGIPTFGVDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEafiEIDGKRFFR 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 418 TGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAF-VMKANG-GAISEEE 495
Cdd:PRK08314 420 TGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVvVLRPEArGKTTEEE 499
|
490 500 510
....*....|....*....|....*....|....*..
gi 778728825 496 VKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKEL 532
Cdd:PRK08314 500 IIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
55-536 |
2.84e-83 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 267.21 E-value: 2.84e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 55 TYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIVTMAC 134
Cdd:PRK03640 29 TFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 135 FYDRvkdlaENGVQIVCVDfavegclhfSVLSGADESLAPLVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLITS-VAQQ 213
Cdd:PRK03640 109 FEAK-----LIPGISVKFA---------ELMNGPKEEAEIQEEFDLDEVATIMYTSGTTGKPKGVIQTYGNHWWSaVGSA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 214 MdgqnpNLYYHRNDVILCVLPFFHIYSLnSILLCGLRVGAAIMIMQKFDIVALLQLIEKHRISIMPIVPpIFLA--IAKS 291
Cdd:PRK03640 175 L-----NLGLTEDDCWLAAVPIFHISGL-SILMRSVIYGMRVVLVEKFDAEKINKLLQTGGVTIISVVS-TMLQrlLERL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 292 PEfEKYDvSSVRVLKSGGAPLGKE-LEDAVREKFPtaiLGQGYGMTE-AGPVLSMSLAFAKEpfqvKAGACGTVVRNAEM 369
Cdd:PRK03640 248 GE-GTYP-SSFRCMLLGGGPAPKPlLEQCKEKGIP---VYQSYGMTEtASQIVTLSPEDALT----KLGSAGKPLFPCEL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 370 KIVDTetGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIdKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAP 449
Cdd:PRK03640 319 KIEKD--GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 450 AELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKanGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILR 529
Cdd:PRK03640 396 AEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLR 473
|
....*..
gi 778728825 530 KELRAKL 536
Cdd:PRK03640 474 HELKQLV 480
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
38-533 |
1.18e-82 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 267.79 E-value: 1.18e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 38 KFASRPCLINGATGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEI 117
Cdd:PRK12583 30 RFPDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 118 AKQAKAANAKLIVTMACF----Y-----DRVKDLAENGV-QIVCVDF------------AVEGCLHFSVLSGADESLAPL 175
Cdd:PRK12583 110 EYALGQSGVRWVICADAFktsdYhamlqELLPGLAEGQPgALACERLpelrgvvslapaPPPGFLAWHELQARGETVSRE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 176 ------VDFSSNDVVALPYSSGTTGLPKGVMLTHKGLITSVAqqMDGQNPNLYYHrnDViLCV-LPFFHIYSLN-SILLC 247
Cdd:PRK12583 190 alaerqASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGY--FVAESLGLTEH--DR-LCVpVPLYHCFGMVlANLGC 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 248 gLRVGAAIMIMQK-FDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPT 326
Cdd:PRK12583 265 -MTVGACLVYPNEaFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHM 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 327 AILGQGYGMTEAGPVLSMSLAfaKEPFQVKAGACGTVVRNAEMKIVDTEtGASLPANSSGEICIRGDQIMKGYLNDLEST 406
Cdd:PRK12583 344 AEVQIAYGMTETSPVSLQTTA--ADDLERRVETVGRTQPHLEVKVVDPD-GATVPRGEIGELCTRGYSVMKGYWNNPEAT 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 407 KRTIDKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKA 486
Cdd:PRK12583 421 AESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLH 500
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 778728825 487 NGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELR 533
Cdd:PRK12583 501 PGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMR 547
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
54-534 |
7.43e-82 |
|
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: 261.13 E-value: 7.43e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 54 YTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAkqakaanaklivtma 133
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELA--------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 134 cfyDRVKDLaengvqivcvdfavegclhfsvlsgadeslaplvDFSSNDVVALPYSSGTTGLPKGVMLTHKGLITSVAqq 213
Cdd:cd05912 67 ---FQLKDS----------------------------------DVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAI-- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 214 mdGQNPNLYYHRNDVILCVLPFFHIYSLnSILLCGLRVGAAIMIMQKFDIVALLQLIEKHRISIMPIVPPIFLAIAKspE 293
Cdd:cd05912 108 --GSALNLGLTEDDNWLCALPLFHISGL-SILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRLLE--I 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 294 FEKYDVSSVRVLKSGGAPLGKELEDAVREK-FPtaiLGQGYGMTEAGpvlSMSLAFAKEPFQVKAGACGTVVRNAEMKIV 372
Cdd:cd05912 183 LGEGYPNNLRCILLGGGPAPKPLLEQCKEKgIP---VYQSYGMTETC---SQIVTLSPEDALNKIGSAGKPLFPVELKIE 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 373 DtetgASLPANSSGEICIRGDQIMKGYLNDLESTKRTIdKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAEL 452
Cdd:cd05912 257 D----DGQPPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEI 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 453 EALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKAngGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKEL 532
Cdd:cd05912 332 EEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE--RPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
..
gi 778728825 533 RA 534
Cdd:cd05912 410 KQ 411
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
22-533 |
1.84e-80 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 262.07 E-value: 1.84e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 22 IPNHLPLHDY-----VFQ-NLSKFASRPCLINgaTGDVYTYHDVQLTARRVAAGL-HNLGIKKGDVVMNLLPNSPEFVFT 94
Cdd:PRK12492 14 VPSTIDLAAYksvveVFErSCKKFADRPAFSN--LGVTLSYAELERHSAAFAAYLqQHTDLVPGDRIAVQMPNVLQYPIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 95 FLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIVTMACFYDRVKD-LAENGVQIVCV----DF--AVEGCLHFSVLS- 166
Cdd:PRK12492 92 VFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLNMFGKLVQEvLPDTGIEYLIEakmgDLlpAAKGWLVNTVVDk 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 167 ----------------------GADESLAPlVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLITSVAQ------QMDGQN 218
Cdd:PRK12492 172 vkkmvpayhlpqavpfkqalrqGRGLSLKP-VPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQvraclsQLGPDG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 219 PNLYYHRNDVILCVLPFFHIYSLNSILLCGLRVGA-AIMIMQKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKY 297
Cdd:PRK12492 251 QPLMKEGQEVMIAPLPLYHIYAFTANCMCMMVSGNhNVLITNPRDIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKDL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 298 DVSSVRVLKSGGAPLGKELedAVR-EKFPTAILGQGYGMTEAGPVLSMSlafakePF--QVKAGACGTVVRNAEMKIVDT 374
Cdd:PRK12492 331 DFSALKLTNSGGTALVKAT--AERwEQLTGCTIVEGYGLTETSPVASTN------PYgeLARLGTVGIPVPGTALKVIDD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 375 EtGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEA 454
Cdd:PRK12492 403 D-GNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIED 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 778728825 455 LLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGaISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELR 533
Cdd:PRK12492 482 VVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPG-LSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
37-533 |
2.87e-80 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 261.67 E-value: 2.87e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 37 SKFASRPCLINGATGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVE 116
Cdd:PRK08315 27 ARYPDREALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 117 IAKQAKAANAKLIVTMACF---------YDRVKDLA--ENG---------VQIVCV--DFAVEGCLHFS--VLSGADESL 172
Cdd:PRK08315 107 LEYALNQSGCKALIAADGFkdsdyvamlYELAPELAtcEPGqlqsarlpeLRRVIFlgDEKHPGMLNFDelLALGRAVDD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 173 APLVDFSS----NDVVALPYSSGTTGLPKGVMLTHKGLIT---SVAQQMDgqnpnlYYHRNDVILCVlPFFHIYSLNSIL 245
Cdd:PRK08315 187 AELAARQAtldpDDPINIQYTSGTTGFPKGATLTHRNILNngyFIGEAMK------LTEEDRLCIPV-PLYHCFGMVLGN 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 246 LCGLRVGAAIMIM-QKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKF 324
Cdd:PRK08315 260 LACVTHGATMVYPgEGFDPLATLAAVEEERCTALYGVPTMFIAELDHPDFARFDLSSLRTGIMAGSPCPIEVMKRVIDKM 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 325 PTAILGQGYGMTEAGPVLSMSLAfaKEPFQVKAGACGTVVRNAEMKIVDTETGASLPANSSGEICIRGDQIMKGYLNDLE 404
Cdd:PRK08315 340 HMSEVTIAYGMTETSPVSTQTRT--DDPLEKRVTTVGRALPHLEVKIVDPETGETVPRGEQGELCTRGYSVMKGYWNDPE 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 405 STKRTIDKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVM 484
Cdd:PRK08315 418 KTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWII 497
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 778728825 485 KANGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELR 533
Cdd:PRK08315 498 LRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMR 546
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
19-533 |
4.01e-80 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 261.11 E-value: 4.01e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 19 DIHIPNHLPLHDYVFQNLSKFASRPCLIngATGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGA 98
Cdd:PRK07059 16 EIDASQYPSLADLLEESFRQYADRPAFI--CMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 99 SYRGAIMTAANPFYTAVEIAKQAKAANAKLIVTMACFYDRVKDLAEN---------------GVQIVCVDFAVE------ 157
Cdd:PRK07059 94 LRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLENFATTVQQVLAKtavkhvvvasmgdllGFKGHIVNFVVRrvkkmv 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 158 ------GCLHF-SVLS-GADESLAPlVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQMDGQNPNLYYHRND-- 227
Cdd:PRK07059 174 pawslpGHVRFnDALAeGARQTFKP-VKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAFEKKPRPdq 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 228 -VILCVLPFFHIYSLNSILLCGLRVGA-AIMIMQKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVL 305
Cdd:PRK07059 253 lNFVCALPLYHIFALTVCGLLGMRTGGrNILIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 306 KSGGAPLGKELEDAVREKFPTAILgQGYGMTEAGPVLSMSLAFAKEpFqvkAGACGTVVRNAEMKIVDtETGASLPANSS 385
Cdd:PRK07059 333 NGGGMAVQRPVAERWLEMTGCPIT-EGYGLSETSPVATCNPVDATE-F---SGTIGLPLPSTEVSIRD-DDGNDLPLGEP 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 386 GEICIRGDQIMKGYLNDLESTKRTIDKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDA 465
Cdd:PRK07059 407 GEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEV 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 778728825 466 AVIGMPDVEAGEVPVAFVMKANgGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELR 533
Cdd:PRK07059 487 AAVGVPDEHSGEAVKLFVVKKD-PALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
54-533 |
4.38e-79 |
|
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: 257.17 E-value: 4.38e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 54 YTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIVTMA 133
Cdd:cd12119 26 YTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 134 CF---YDRVKDLAENGVQIVCVDFAVEGC-------LHFSVLSGADESLAPLVDFSSNDVVALPYSSGTTGLPKGVMLTH 203
Cdd:cd12119 106 DFlplLEAIAPRLPTVEHVVVMTDDAAMPepagvgvLAYEELLAAESPEYDWPDFDENTAAAICYTSGTTGNPKGVVYSH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 204 KGLI--TSVAQQMDGqnpnLYYHRNDVILCVLPFFHIYSLNSILLCGLrVGAAIMIMQKFDIVA-LLQLIEKHRISIMPI 280
Cdd:cd12119 186 RSLVlhAMAALLTDG----LGLSESDVVLPVVPMFHVNAWGLPYAAAM-VGAKLVLPGPYLDPAsLAELIEREGVTFAAG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 281 VPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAIlgQGYGMTEAGPVLSMSL---------AFAKE 351
Cdd:cd12119 261 VPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEERGVRVI--HAWGMTETSPLGTVARppsehsnlsEDEQL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 352 PFQVKAG--ACGTvvrnaEMKIVDTETGAsLPA--NSSGEICIRGDQIMKGYLNDLESTKRtIDKEGWLHTGDIGFVDDD 427
Cdd:cd12119 339 ALRAKQGrpVPGV-----ELRIVDDDGRE-LPWdgKAVGELQVRGPWVTKSYYKNDEESEA-LTEDGWLRTGDVATIDED 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 428 NELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVFY 507
Cdd:cd12119 412 GYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLADKVAKW 491
|
490 500
....*....|....*....|....*.
gi 778728825 508 KRLKRVFFVNAIPKAPSGKILRKELR 533
Cdd:cd12119 492 WLPDDVVFVDEIPKTSTGKIDKKALR 517
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
51-533 |
1.33e-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. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 250.67 E-value: 1.33e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 51 GDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKqakaanakliv 130
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAY----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 131 tmacfydrvkDLAENGVQIVCVDfavegclhfsvlsgadeslaplvdfssndVVALPYSSGTTGLPKGVMLTHKGLITSV 210
Cdd:cd05934 70 ----------IIDHSGAQLVVVD-----------------------------PASILYTSGTTGPPKGVVITHANLTFAG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 211 AQQMDGqnpnLYYHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKFDIVALLQLIEKHRISIMPIVPPIFLAIAK 290
Cdd:cd05934 111 YYSARR----FGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLLA 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 291 SPEFEKYDVSSVRVlkSGGAPLGKELEDAVREKFPTAILGqGYGMTEAG-PVLSmslafaKEPFQVKAGACGTVVRNAEM 369
Cdd:cd05934 187 QPPSPDDRAHRLRA--AYGAPNPPELHEEFEERFGVRLLE-GYGMTETIvGVIG------PRDEPRRPGSIGRPAPGYEV 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 370 KIVDtETGASLPANSSGEICIRGDQ---IMKGYLNDLESTkRTIDKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQ 446
Cdd:cd05934 258 RIVD-DDGQELPAGEPGELVIRGLRgwgFFKGYYNMPEAT-AEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGEN 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 447 VAPAELEALLITHPKLSDAAVIGMPDVEAG-EVPVAFVMKAnGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSG 525
Cdd:cd05934 336 ISSAEVERAILRHPAVREAAVVAVPDEVGEdEVKAVVVLRP-GETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTE 414
|
....*...
gi 778728825 526 KILRKELR 533
Cdd:cd05934 415 KVAKAQLR 422
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
182-529 |
2.11e-77 |
|
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: 247.03 E-value: 2.11e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 182 DVVALPYSSGTTGLPKGVMLTHKGLITSVAQQMDgqnpNLYYHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKF 261
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWAD----CADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 262 DIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILGQGYGMTEAGPV 341
Cdd:cd17638 77 DVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 342 lsmSLAFAKEPFQVKAGACGTVVRNAEMKIVDtetgaslpansSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLHTGDI 421
Cdd:cd17638 157 ---TMCRPGDDAETVATTCGRACPGFEVRIAD-----------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 422 GFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIA 501
Cdd:cd17638 223 GELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCR 302
|
330 340
....*....|....*....|....*...
gi 778728825 502 KQVVFYKRLKRVFFVNAIPKAPSGKILR 529
Cdd:cd17638 303 ERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
34-533 |
1.60e-76 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 251.99 E-value: 1.60e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 34 QNLSKFASRPCLINgaTGDVYTYHDVQLTARRVAAGL-HNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFY 112
Cdd:PRK05677 32 QSCQRFADKPAFSN--LGKTLTYGELYKLSGAFAAWLqQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 113 TAVEIAKQAKAANAKLIVTMACFYDRV-KDLAENGVQIVCVD---------------------------FAVEGCLHFS- 163
Cdd:PRK05677 110 TAREMEHQFNDSGAKALVCLANMAHLAeKVLPKTGVKHVIVTevadmlpplkrllinavvkhvkkmvpaYHLPQAVKFNd 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 164 VLS-GADESLAPlVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLITSVAQ--QMDGQNPNlyyHRNDVILCVLPFFHIYS 240
Cdd:PRK05677 190 ALAkGAGQPVTE-ANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQcrALMGSNLN---EGCEILIAPLPLYHIYA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 241 LNSILLCGLRVGA-AIMIMQKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLgkELEDA 319
Cdd:PRK05677 266 FTFHCMAMMLIGNhNILISNPRDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMAL--QLATA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 320 VREKFPT--AILgQGYGMTEAGPVLSMSlafakePFQ-VKAGACGTVVRNAEMKIVDTEtGASLPANSSGEICIRGDQIM 396
Cdd:PRK05677 344 ERWKEVTgcAIC-EGYGMTETSPVVSVN------PSQaIQVGTIGIPVPSTLCKVIDDD-GNELPLGEVGELCVKGPQVM 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 397 KGYLNDLESTKRTIDKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAG 476
Cdd:PRK05677 416 KGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSG 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 778728825 477 EVPVAFVMKANGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELR 533
Cdd:PRK05677 496 EAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
27-537 |
1.73e-76 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 251.88 E-value: 1.73e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 27 PLHDYVFQNLSKFASRPCLIngATGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMT 106
Cdd:PRK06178 34 PLTEYLRAWARERPQRPAII--FYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 107 AANPFYTAVEIAKQAKAANAKLIVTMACFYDRVKD-LAENGVQIVCV----DF------------------AVEGCLHFS 163
Cdd:PRK06178 112 PVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQvRAETSLRHVIVtslaDVlpaeptlplpdslraprlAAAGAIDLL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 164 VLSGADESLAPLVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLI------TSVAQQMDgqnpnlyyhRNDVILCVLPFFH 237
Cdd:PRK06178 192 PALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVytaaaaYAVAVVGG---------EDSVFLSFLPEFW 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 238 IYSLNSILLCGLRVGAAIMIMQKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVR-------VLKsgga 310
Cdd:PRK06178 263 IAGENFGLLFPLFSGATLVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRqvrvvsfVKK---- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 311 pLGKELEDAVREKFPTAILGQGYGMTEAGPVLSMSLAFAKEPFQVKAGA--CGTVVRNAEMKIVDTETGASLPANSSGEI 388
Cdd:PRK06178 339 -LNPDYRQRWRALTGSVLAEAAWGMTETHTCDTFTAGFQDDDFDLLSQPvfVGLPVPGTEFKICDFETGELLPLGAEGEI 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 389 CIRGDQIMKGYLNDLESTKRTIdKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVI 468
Cdd:PRK06178 418 VVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVV 496
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 778728825 469 GMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVFYKrLKRVFFVNAIPKAPSGKILRKELRAKLA 537
Cdd:PRK06178 497 GRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYK-VPEIRIVDALPMTATGKVRKQDLQALAE 564
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
42-534 |
2.47e-76 |
|
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: 247.97 E-value: 2.47e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 42 RPCLIngATGDVYTYHD-VQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQ 120
Cdd:cd05941 2 RIAIV--DDGDSITYADlVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 121 akaanaklivtmacfydrvkdLAENGVQIVcvdfaVEGCLhfsvlsgadeslaplvdfssndvvaLPYSSGTTGLPKGVM 200
Cdd:cd05941 80 ---------------------ITDSEPSLV-----LDPAL-------------------------ILYTSGTTGRPKGVV 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 201 LTHKGLITSVAQQMDGQNpnlyYHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKFDIVALLQLIEKHRISIMPI 280
Cdd:cd05941 109 LTHANLAANVRALVDAWR----WTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRLMPSITVFMG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 281 VPPIFLAIAKSPEFEKYDV--------SSVRVLKSGGAPLGKEledaVREKFpTAILGQG----YGMTEAGPVLSMSLAF 348
Cdd:cd05941 185 VPTIYTRLLQYYEAHFTDPqfaraaaaERLRLMVSGSAALPVP----TLEEW-EAITGHTllerYGMTEIGMALSNPLDG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 349 AKepfqvKAGACGTVVRNAEMKIVDTETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLHTGDIGFVDDDN 428
Cdd:cd05941 260 ER-----RPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 429 ELFIVDRLK-ELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFV-MKANGGAISEEEVKQFIAKQVVF 506
Cdd:cd05941 335 YYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVvLRAGAAALSLEELKEWAKQRLAP 414
|
490 500
....*....|....*....|....*...
gi 778728825 507 YKRLKRVFFVNAIPKAPSGKILRKELRA 534
Cdd:cd05941 415 YKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
54-532 |
3.59e-76 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 249.01 E-value: 3.59e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 54 YTYHDVQLTARRVAAGL-HNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIVTM 132
Cdd:PRK06839 28 MTYKQLHEYVSKVAAYLiYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 133 ACFydrvkdlaENGVQIVCVDFAVEGCLHFSVLSG-ADESLAPLVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLITSVA 211
Cdd:PRK06839 108 KTF--------QNMALSMQKVSYVQRVISITSLKEiEDRKIDNFVEKNESASFIICYTSGTTGKPKGAVLTQENMFWNAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 212 QQMdgqnPNLYYHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKFDIVALLQLIEKHRISIMPIVPPIFLAIAKS 291
Cdd:PRK06839 180 NNT----FAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINC 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 292 PEFEKYDVSSVRVLKSGGAPLGKELEDAVREK-FPtaiLGQGYGMTEAGPVLSMslaFAKEPFQVKAGACGTVVRNAEMK 370
Cdd:PRK06839 256 SKFETTNLQSVRWFYNGGAPCPEELMREFIDRgFL---FGQGFGMTETSPTVFM---LSEEDARRKVGSIGKPVLFCDYE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 371 IVDTETGaSLPANSSGEICIRGDQIMKGYLNDLESTKRTIdKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPA 450
Cdd:PRK06839 330 LIDENKN-KVEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 451 ELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRK 530
Cdd:PRK06839 408 EVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKA 487
|
..
gi 778728825 531 EL 532
Cdd:PRK06839 488 QL 489
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
34-533 |
5.08e-76 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 250.36 E-value: 5.08e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 34 QNLSKFASRPCLINgaTGDVYTYHDVQLTARRVAAGLHN-LGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFY 112
Cdd:PRK08974 31 QAVARYADQPAFIN--MGEVMTFRKLEERSRAFAAYLQNgLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 113 TAVEIAKQAKAANAKLIVTMACFYDRVKDLAEN-----------GVQI-----VCVDFAVE------------GCLHF-S 163
Cdd:PRK08974 109 TPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFKtpvkhviltrmGDQLstakgTLVNFVVKyikrlvpkyhlpDAISFrS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 164 VLSGADESLAPLVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQMDGQNPnLYYHRNDVILCVLPFFHIYSLNS 243
Cdd:PRK08974 189 ALHKGRRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGP-LLHPGKELVVTALPLYHIFALTV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 244 ILLCGLRVGA-AIMIMQKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKeledAVRE 322
Cdd:PRK08974 268 NCLLFIELGGqNLLITNPRDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGGMAVQQ----AVAE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 323 KFPTAI---LGQGYGMTEAGPVLSMSlafakePFQVK--AGACGTVVRNAEMKIVDTEtGASLPANSSGEICIRGDQIMK 397
Cdd:PRK08974 344 RWVKLTgqyLLEGYGLTECSPLVSVN------PYDLDyySGSIGLPVPSTEIKLVDDD-GNEVPPGEPGELWVKGPQVML 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 398 GYLNDLESTKRTIdKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGE 477
Cdd:PRK08974 417 GYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGE 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 778728825 478 VPVAFVMKaNGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELR 533
Cdd:PRK08974 496 AVKIFVVK-KDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
39-534 |
4.14e-74 |
|
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: 243.36 E-value: 4.14e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 39 FASRPCLINGATgdVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIA 118
Cdd:cd12118 17 YPDRTSIVYGDR--RYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 119 KQakaanaklivtmacfydrvkdLAENGVQIVCVD--FAVEgclhfSVLSGADESLAPLVDFSSNDVVALPYSSGTTGLP 196
Cdd:cd12118 95 FI---------------------LRHSEAKVLFVDreFEYE-----DLLAEGDPDFEWIPPADEWDPIALNYTSGTTGRP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 197 KGVMLTHKG-----LITSVAQQMDgQNPnlyyhrndVILCVLPFFH------IYSLNSillcglrVGAAIMIMQKFDIVA 265
Cdd:cd12118 149 KGVVYHHRGaylnaLANILEWEMK-QHP--------VYLWTLPMFHcngwcfPWTVAA-------VGGTNVCLRKVDAKA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 266 LLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVS-SVRVLKSGGAPLGKELEDAVREKFPTAilgQGYGMTEA-GPVLS 343
Cdd:cd12118 213 IYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPhRVHVMTAGAPPPAAVLAKMEELGFDVT---HVYGLTETyGPATV 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 344 M-------SLAfAKEPFQVKAGACGTVVRNAEMKIVDTETGASLPANSS--GEICIRGDQIMKGYLNDLESTKRTIdKEG 414
Cdd:cd12118 290 CawkpewdELP-TEERARLKARQGVRYVGLEEVDVLDPETMKPVPRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 415 WLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEE 494
Cdd:cd12118 368 WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEE 447
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 778728825 495 EVKQFIAKQVVFYKRLKRVFFVNaIPKAPSGKILRKELRA 534
Cdd:cd12118 448 EIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVLRD 486
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
25-537 |
8.80e-73 |
|
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: 241.20 E-value: 8.80e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 25 HLPLHDYVFQNLSKFASRPCLINGATgdVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAI 104
Cdd:COG1021 24 GETLGDLLRRRAERHPDRIAVVDGER--RLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 105 MTAANPFYTAVEIAKQAKAANAKLIVTMA--------CFYDRVKDLAEnGVQIVCVDFAVEGCLHFSVLSGADESL-APL 175
Cdd:COG1021 102 PVFALPAHRRAEISHFAEQSEAVAYIIPDrhrgfdyrALARELQAEVP-SLRHVLVVGDAGEFTSLDALLAAPADLsEPR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 176 VDfsSNDVVALPYSSGTTGLPKGVMLTHkglitsvaqqmdgqNPNLYYHR----------NDVILCVLPFFHIYSLNSI- 244
Cdd:COG1021 181 PD--PDDVAFFQLSGGTTGLPKLIPRTH--------------DDYLYSVRasaeicgldaDTVYLAALPAAHNFPLSSPg 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 245 LLCGLRVGAAIMIMQKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKF 324
Cdd:COG1021 245 VLGVLYAGGTVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPAL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 325 PtAILGQGYGMTEaGPVLSMSLAfakEPFQVKAGACGTVVRNA-EMKIVDtETGASLPANSSGEICIRGDQIMKGYLNDL 403
Cdd:COG1021 325 G-CTLQQVFGMAE-GLVNYTRLD---DPEEVILTTQGRPISPDdEVRIVD-EDGNPVPPGEVGELLTRGPYTIRGYYRAP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 404 ESTKRTIDKEGWLHTGDIGFVDDDNELFIVDRLKELI-----KfkafqVAPAELEALLITHPKLSDAAVIGMPDVEAGEV 478
Cdd:COG1021 399 EHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQInrggeK-----IAAEEVENLLLAHPAVHDAAVVAMPDEYLGER 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 479 PVAFVMkANGGAISEEEVKQFI-AKQVVFYKRLKRVFFVNAIPKAPSGKILRKELRAKLA 537
Cdd:COG1021 474 SCAFVV-PRGEPLTLAELRRFLrERGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
51-539 |
1.38e-71 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 238.14 E-value: 1.38e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 51 GDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIV 130
Cdd:PRK07786 40 GNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 131 T---MACFYDRVKDLAEN-GVQIVCVDFAVEGCLHF-SVLSGADESLAPlVDFSSNDVVALPYSSGTTGLPKGVMLTHKG 205
Cdd:PRK07786 120 TeaaLAPVATAVRDIVPLlSTVVVAGGSSDDSVLGYeDLLAEAGPAHAP-VDIPNDSPALIMYTSGTTGRPKGAVLTHAN 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 206 LitsVAQQMDGQNPNLYYHRNDVILCVLPFFHIYSLNSILlCGLRVGAAIMI--MQKFDIVALLQLIEKHRISIMPIVPP 283
Cdd:PRK07786 199 L---TGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGSML-PGLLLGAPTVIypLGAFDPGQLLDVLEAEKVTGIFLVPA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 284 IFLAIAKSPEFEKYDVSsVRVLKSGGAPLGKELEDAVREKFPTAILGQGYGMTEAGPVLSMSLAfakEPFQVKAGACGTV 363
Cdd:PRK07786 275 QWQAVCAEQQARPRDLA-LRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSPVTCMLLG---EDAIRKLGSVGKV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 364 VRNAEMKIVDtETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIDKeGWLHTGDIGFVDDDNELFIVDRLKELIKFK 443
Cdd:PRK07786 351 IPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMIISG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 444 AFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGA-ISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKA 522
Cdd:PRK07786 429 GENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAaLTLEDLAEFLTDRLARYKHPKALEIVDALPRN 508
|
490
....*....|....*..
gi 778728825 523 PSGKILRKELRAKLASG 539
Cdd:PRK07786 509 PAGKVLKTELRERYGAC 525
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
43-540 |
5.92e-71 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 235.57 E-value: 5.92e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 43 PCLINGATGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAK 122
Cdd:PRK08276 1 PAVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 123 AANAKLIVTMACFYDRVKDLAE---NGVQIVCVDF-AVEGCLHFSVLsGADESLAPLVDFSSNDVVAlpYSSGTTGLPKG 198
Cdd:PRK08276 81 DSGAKVLIVSAALADTAAELAAelpAGVPLLLVVAgPVPGFRSYEEA-LAAQPDTPIADETAGADML--YSSGTTGRPKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 199 VM--LTHK-------GLITSVAQQMDGQNPNLYyhrndviLCVLPFFH----IYSLNSILLCGLRVgaaimIMQKFDIVA 265
Cdd:PRK08276 158 IKrpLPGLdpdeapgMMLALLGFGMYGGPDSVY-------LSPAPLYHtaplRFGMSALALGGTVV-----VMEKFDAEE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 266 LLQLIEKHRISIMPIVPPIFLAIAKSPE--FEKYDVSSVRVLKSGGAPLGKELEDAVREKF-PtaILGQGYGMTEAGPV- 341
Cdd:PRK08276 226 ALALIERYRVTHSQLVPTMFVRMLKLPEevRARYDVSSLRVAIHAAAPCPVEVKRAMIDWWgP--IIHEYYASSEGGGVt 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 342 LSMSLAFAKEPfqvkagacGTVVR--NAEMKIVDtETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLHTG 419
Cdd:PRK08276 304 VITSEDWLAHP--------GSVGKavLGEVRILD-EDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 420 DIGFVDDDNELFIVDRlkelikfKAFQVA-------PAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAIS 492
Cdd:PRK08276 375 DVGYLDEDGYLYLTDR-------KSDMIIsggvniyPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAG 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 778728825 493 EE---EVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELRAKLASGA 540
Cdd:PRK08276 448 DAlaaELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWEGR 498
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
30-533 |
7.87e-70 |
|
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: 232.64 E-value: 7.87e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 30 DYVFQNLSK-FASRPCLINGAtgDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAA 108
Cdd:cd05959 7 TLVDLNLNEgRGDKTAFIDDA--GSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 109 NPFYTAVEIAKQAKAANAKLIVTMACFYDRVKDLAENGVQIVCVDFAVEGC------LHFSVLSGADESLAPLVDFSSND 182
Cdd:cd05959 85 NTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAgpeagaLLLAELVAAEAEQLKPAATHADD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 183 VVALPYSSGTTGLPKGVMLTHKGLItsVAQQMDGQNPnLYYHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKFD 262
Cdd:cd05959 165 PAFWLYSSGSTGRPKGVVHLHADIY--WTAELYARNV-LGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 263 IVAL-LQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILgQGYGMTEAGPV 341
Cdd:cd05959 242 TPAAvFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDIL-DGIGSTEMLHI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 342 LSMSLAFAKEPfqvkaGACGTVVRNAEMKIVDtETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIdKEGWLHTGDI 421
Cdd:cd05959 321 FLSNRPGRVRY-----GTTGKPVPGYEVELRD-EDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 422 GFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANG---GAISEEEVKQ 498
Cdd:cd05959 394 YVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGyedSEALEEELKE 473
|
490 500 510
....*....|....*....|....*....|....*
gi 778728825 499 FIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELR 533
Cdd:cd05959 474 FVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
36-533 |
4.08e-68 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 229.38 E-value: 4.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 36 LSKFASRPCLINgaTGDVYTYHDVQLTARRVAAGLHN-LGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTA 114
Cdd:PRK08751 35 VAKFADRPAYHS--FGKTITYREADQLVEQFAAYLLGeLQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 115 VEIAKQAKAANAKLIVTMACFYDRVKD-LAENGVQIVC-------VDFAVEGCLHFSV-----------LSGA---DESL 172
Cdd:PRK08751 113 RELKHQLIDSGASVLVVIDNFGTTVQQvIADTPVKQVIttglgdmLGFPKAALVNFVVkyvkklvpeyrINGAirfREAL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 173 A-------PLVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQMDG-QNPNLYYHRNDVILCVLPFFHIYSLNSI 244
Cdd:PRK08751 193 AlgrkhsmPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWlAGTGKLEEGCEVVITALPLYHIFALTAN 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 245 LLCGLRVGAAI-MIMQKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELedAVREK 323
Cdd:PRK08751 273 GLVFMKIGGCNhLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSV--AERWK 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 324 FPTAI-LGQGYGMTEAGPVLSMSlafakePFQVKA--GACGTVVRNAEMKIVDtETGASLPANSSGEICIRGDQIMKGYL 400
Cdd:PRK08751 351 QVTGLtLVEAYGLTETSPAACIN------PLTLKEynGSIGLPIPSTDACIKD-DAGTVLAIGEIGELCIKGPQVMKGYW 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 401 NDLESTKRTIDKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPV 480
Cdd:PRK08751 424 KRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVK 503
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 778728825 481 AFVMKANgGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELR 533
Cdd:PRK08751 504 VVIVKKD-PALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
53-534 |
1.22e-67 |
|
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: 224.95 E-value: 1.22e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 53 VYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIVTM 132
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 133 ACFYDRvkdlaengvqivcvDFAVEGclhfsvlsgadeslaplvdfssNDVVALPYSSGTTGLPKGVMLTHKGLITSVAQ 212
Cdd:cd05903 81 ERFRQF--------------DPAAMP----------------------DAVALLLFTSGTTGEPKGVMHSHNTLSASIRQ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 213 QMDgqnpNLYYHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSP 292
Cdd:cd05903 125 YAE----RLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPFLTDLLNAV 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 293 EFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILGqGYGMTEAGPVLSMSlafakEPFQVKAGAC--GTVVRNAEMK 370
Cdd:cd05903 201 EEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCS-AYGSTECPGAVTSI-----TPAPEDRRLYtdGRPLPGVEIK 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 371 IVDtETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTiDKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPA 450
Cdd:cd05903 275 VVD-DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADA-APEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 451 ELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFI-AKQVVFYKRLKRVFFVNAIPKAPSGKILR 529
Cdd:cd05903 353 EVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKVQK 432
|
....*
gi 778728825 530 KELRA 534
Cdd:cd05903 433 FRLRE 437
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
49-533 |
2.86e-67 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 226.10 E-value: 2.86e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 49 ATGDV--YTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANA 126
Cdd:PRK08008 31 SGGVVrrYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 127 KLIVTMACF---YDRVKDLAENGVQIVCV----DFAVEGCLHFSVLSG-ADESLAPLVDFSSNDVVALPYSSGTTGLPKG 198
Cdd:PRK08008 111 SLLVTSAQFypmYRQIQQEDATPLRHICLtrvaLPADDGVSSFTQLKAqQPATLCYAPPLSTDDTAEILFTSGTTSRPKG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 199 VMLTHKGLitsvaqQMDGqnpnlYY-------HRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKFDIVALLQLIE 271
Cdd:PRK08008 191 VVITHYNL------RFAG-----YYsawqcalRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLLEKYSARAFWGQVC 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 272 KHRISI---MPIVPPIFLAIAKSPEFEKYDVSSVRVLksggAPLGKELEDAVREKFPTAILgQGYGMTEagpvlSMSLAF 348
Cdd:PRK08008 260 KYRATItecIPMMIRTLMVQPPSANDRQHCLREVMFY----LNLSDQEKDAFEERFGVRLL-TSYGMTE-----TIVGII 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 349 AKEPFQVK-------AGACgtvvrnAEMKIVDtETGASLPANSSGEICIRG---DQIMKGYLNDLESTKRTIDKEGWLHT 418
Cdd:PRK08008 330 GDRPGDKRrwpsigrPGFC------YEAEIRD-DHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 419 GDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQ 498
Cdd:PRK08008 403 GDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFA 482
|
490 500 510
....*....|....*....|....*....|....*
gi 778728825 499 FIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELR 533
Cdd:PRK08008 483 FCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
60-542 |
8.87e-67 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 227.53 E-value: 8.87e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 60 QLTAR--RVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGaIMTAANPFYTAVEIAKQAKAANAKLIVTMACFYD 137
Cdd:PRK07529 63 ELLADvtRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAG-IANPINPLLEPEQIAELLRAAGAKVLVTLGPFPG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 138 --------RVKDLAENGVQIVCVDFA-------------VEGCLHFSVLsGADESLAPLVD--------FSSNDVVALPY 188
Cdd:PRK07529 142 tdiwqkvaEVLAALPELRTVVEVDLArylpgpkrlavplIRRKAHARIL-DFDAELARQPGdrlfsgrpIGPDDVAAYFH 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 189 SSGTTGLPKGVMLTHKGLITS--VAQQMDGQNPNlyyhrnDVILCVLPFFHIYSLNSILLCGLRVGAAIMI--------- 257
Cdd:PRK07529 221 TGGTTGMPKLAQHTHGNEVANawLGALLLGLGPG------DTVFCGLPLFHVNALLVTGLAPLARGAHVVLatpqgyrgp 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 258 --MQKFdivalLQLIEKHRISIMPIVPPIFLAIAKSPeFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILgQGYGM 335
Cdd:PRK07529 295 gvIANF-----WKIVERYRINFLSGVPTVYAALLQVP-VDGHDISSLRYALCGAAPLPVEVFRRFEAATGVRIV-EGYGL 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 336 TEAGPVLSMSlaFAKEPfqVKAGACGTVVRNAEMKIVD-TETGASL---PANSSGEICIRGDQIMKGYLNDlESTKRTID 411
Cdd:PRK07529 368 TEATCVSSVN--PPDGE--RRIGSVGLRLPYQRVRVVIlDDAGRYLrdcAVDEVGVLCIAGPNVFSGYLEA-AHNKGLWL 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 412 KEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAI 491
Cdd:PRK07529 443 EDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASA 522
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 778728825 492 SEEEVKQFIAKQVVfyKRL---KRVFFVNAIPKAPSGKILRKELRAKLASGAYN 542
Cdd:PRK07529 523 TEAELLAFARDHIA--ERAavpKHVRILDALPKTAVGKIFKPALRRDAIRRVLR 574
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
41-536 |
1.90e-66 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 223.61 E-value: 1.90e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 41 SRPCLINGatGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQ 120
Cdd:PRK06145 17 DRAALVYR--DQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 121 AKAANAKLIvtmacFYDRVKDL-AENGVQIVCVDFAVEGclHFSVLSGADESLAPLVDFSSNDVVALPYSSGTTGLPKGV 199
Cdd:PRK06145 95 LGDAGAKLL-----LVDEEFDAiVALETPKIVIDAAAQA--DSRRLAQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 200 MLTHKGLITSVAQQMDGqnpnLYYHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKFDIVALLQLIEKHRISIMP 279
Cdd:PRK06145 168 MHSYGNLHWKSIDHVIA----LGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLAAIERHRLTCAW 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 280 IVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAplgKELEDAVRE---KFPTAILGQGYGMTE--AGPVLsMSLAFAKEpfq 354
Cdd:PRK06145 244 MAPVMLSRVLTVPDRDRFDLDSLAWCIGGGE---KTPESRIRDftrVFTRARYIDAYGLTEtcSGDTL-MEAGREIE--- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 355 vKAGACGTVVRNAEMKIVDtETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIdKEGWLHTGDIGFVDDDNELFIVD 434
Cdd:PRK06145 317 -KIGSTGRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 435 RLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVFYKRLKRVF 514
Cdd:PRK06145 394 RKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLK 473
|
490 500
....*....|....*....|..
gi 778728825 515 FVNAIPKAPSGKILRKELRAKL 536
Cdd:PRK06145 474 VRDELPRNPSGKVLKRVLRDEL 495
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
54-534 |
3.02e-66 |
|
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: 221.06 E-value: 3.02e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 54 YTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAkqakaanaklivtma 133
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIE--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 134 cfyDRVKDLaenGVQIVCVDfavegclhfsvlsgadeslaplvdfsSNDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQ 213
Cdd:cd05972 66 ---YRLEAA---GAKAIVTD--------------------------AEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 214 MDGQNpnlyYHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMI--MQKFDIVALLQLIEKHRISIMPIVPPIFLAIAKs 291
Cdd:cd05972 114 AYWLG----LRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVyeGPRFDAERILELLERYGVTSFCGPPTAYRMLIK- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 292 PEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILgQGYGMTEAGPVLSMSlafakePFQ-VKAGACGTVVRNAEMK 370
Cdd:cd05972 189 QDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIR-DGYGQTETGLTVGNF------PDMpVKPGSMGRPTPGYDVA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 371 IVDTEtGASLPANSSGEICIRGD--QIMKGYLNDLESTKRTIdKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVA 448
Cdd:cd05972 262 IIDDD-GRELPPGEEGDIAIKLPppGLFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIG 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 449 PAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEE---EVKQFIAKQVVFYKRLKRVFFVNAIPKAPSG 525
Cdd:cd05972 340 PFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEElaeELQGHVKKVLAPYKYPREIEFVEELPKTISG 419
|
....*....
gi 778728825 526 KILRKELRA 534
Cdd:cd05972 420 KIRRVELRD 428
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
56-533 |
5.76e-66 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 222.65 E-value: 5.76e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 56 YHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIVTMACF 135
Cdd:PRK12406 14 FDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 136 YDRVKDLAENGVQIVCVDFAVEGCLHFSVlsgADESLAP----------LVDFSSNDVVALP------YSSGTTGLPKGV 199
Cdd:PRK12406 94 LHGLASALPAGVTVLSVPTPPEIAAAYRI---SPALLTPpagaidwegwLAQQEPYDGPPVPqpqsmiYTSGTTGHPKGV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 200 mltHKGLITSVAQQMDGQNPNLYY--HRNDVILCVLPFFHiYSLNSILLCGLRVGAAIMIMQKFDIVALLQLIEKHRISI 277
Cdd:PRK12406 171 ---RRAAPTPEQAAAAEQMRALIYglKPGIRALLTGPLYH-SAPNAYGLRAGRLGGVLVLQPRFDPEELLQLIERHRITH 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 278 MPIVPPIFLAIAKSPEF--EKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILgQGYGMTEAGPVlsmslAFA-KEPFQ 354
Cdd:PRK12406 247 MHMVPTMFIRLLKLPEEvrAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGPVIY-EYYGSTESGAV-----TFAtSEDAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 355 VKAGACGTVVRNAEMKIVDtETGASLPANSSGEICIRGDQIMK-GYLNDLEStKRTIDKEGWLHTGDIGFVDDDNELFIV 433
Cdd:PRK12406 321 SHPGTVGKAAPGAELRFVD-EDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEK-RAEIDRGGFITSGDVGYLDADGYLFLC 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 434 DRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVFYKRLKRV 513
Cdd:PRK12406 399 DRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKARLAGYKVPKHI 478
|
490 500
....*....|....*....|
gi 778728825 514 FFVNAIPKAPSGKILRKELR 533
Cdd:PRK12406 479 EIMAELPREDSGKIFKRRLR 498
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
36-540 |
7.49e-66 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 222.55 E-value: 7.49e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 36 LSKFASRPCLINGatGDVYTYHdvQLTAR--RVAAGLHNLGIKKGDVVMNLLPNSPEfVFTFLGASY-RGAIMTAANPFY 112
Cdd:PRK06188 22 LKRYPDRPALVLG--DTRLTYG--QLADRisRYIQAFEALGLGTGDAVALLSLNRPE-VLMAIGAAQlAGLRRTALHPLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 113 T-AVEIAKQAKAANAKLIVTMACFYDRVKDLAEN--GVQIVCVDFAVEGCLHFSVLSGADESlAPLVDFS-SNDVVALPY 188
Cdd:PRK06188 97 SlDDHAYVLEDAGISTLIVDPAPFVERALALLARvpSLKHVLTLGPVPDGVDLLAAAAKFGP-APLVAAAlPPDIAGLAY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 189 SSGTTGLPKGVMLTHKGLITSVAQQM-DGQNPnlyyhRNDVILCVLPFFHIYSLnsILLCGLRVGAAIMIMQKFDIVALL 267
Cdd:PRK06188 176 TGGTTGKPKGVMGTHRSIATMAQIQLaEWEWP-----ADPRFLMCTPLSHAGGA--FFLPTLLRGGTVIVLAKFDPAEVL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 268 QLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGK-ELEDAVREKFPtaILGQGYGMTEAGPVLSMSL 346
Cdd:PRK06188 249 RAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPvRLAEAIERFGP--IFAQYYGQTEAPMVITYLR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 347 AFAKEPFQVKA-GACGTVVRNAEMKIVDtETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIdKEGWLHTGDIGFVD 425
Cdd:PRK06188 327 KRDHDPDDPKRlTSCGRPTPGLRVALLD-EDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVARED 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 426 DDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFI--AKQ 503
Cdd:PRK06188 405 EDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVkeRKG 484
|
490 500 510
....*....|....*....|....*....|....*..
gi 778728825 504 VVFYKrlKRVFFVNAIPKAPSGKILRKELRAKLASGA 540
Cdd:PRK06188 485 SVHAP--KQVDFVDSLPLTALGKPDKKALRARYWEGR 519
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
55-533 |
1.70e-65 |
|
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: 219.26 E-value: 1.70e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 55 TYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPfytaveiakqakaanaklivtmac 134
Cdd:cd05919 12 TYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINP------------------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 135 fydrvkDLAENGVQIVCVDfavegclhfsvlsgadeSLAPLVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLITsVAQQM 214
Cdd:cd05919 68 ------LLHPDDYAYIARD-----------------CEARLVVTSADDIAYLLYSSGTTGPPKGVMHAHRDPLL-FADAM 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 215 dgQNPNLYYHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKF-DIVALLQLIEKHRISIMPIVPPIFLAIAKSPE 293
Cdd:cd05919 124 --AREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWpTAERVLATLARFRPTVLYGVPTFYANLLDSCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 294 FEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILgQGYGMTEAGPVLsmslaFAKEPFQVKAGACGTVVRNAEMKIVD 373
Cdd:cd05919 202 GSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPIL-DGIGATEVGHIF-----LSNRPGAWRLGSTGRPVPGYEIRLVD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 374 tETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIdKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELE 453
Cdd:cd05919 276 -EEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 454 ALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISE---EEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRK 530
Cdd:cd05919 354 SLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQEslaRDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRF 433
|
...
gi 778728825 531 ELR 533
Cdd:cd05919 434 KLR 436
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
42-533 |
2.03e-65 |
|
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: 219.27 E-value: 2.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 42 RPCLINGatGDVYTYHDVQLTARRVAAGL-HNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEiakq 120
Cdd:cd05958 1 RTCLRSP--EREWTYRDLLALANRIANVLvGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKE---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 121 akaanaklivtmacfYDRVKDLAENGVqIVCVDfavegclhfsVLSGADeslaplvdfssnDVVALPYSSGTTGLPKGVM 200
Cdd:cd05958 75 ---------------LAYILDKARITV-ALCAH----------ALTASD------------DICILAFTSGTTGAPKATM 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 201 LTHKGLITSVaqqmDGQNPN-LYYHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKFDIVALLQLIEKHRISIMP 279
Cdd:cd05958 117 HFHRDPLASA----DRYAVNvLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYKPTVLF 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 280 IVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILgQGYGMTEAgpvlsMSLAFAKEPFQVKAGA 359
Cdd:cd05958 193 TAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPII-DGIGSTEM-----FHIFISARPGDARPGA 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 360 CGTVVRNAEMKIVDTEtGASLPANSSGEICIRGDQimkGYLNDLESTKRTIDKEGWLHTGDIGFVDDDNELFIVDRLKEL 439
Cdd:cd05958 267 TGKPVPGYEAKVVDDE-GNPVPDGTIGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDM 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 440 IKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISE---EEVKQFIAKQVVFYKRLKRVFFV 516
Cdd:cd05958 343 IVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPvlaRELQDHAKAHIAPYKYPRAIEFV 422
|
490
....*....|....*..
gi 778728825 517 NAIPKAPSGKILRKELR 533
Cdd:cd05958 423 TELPRTATGKLQRFALR 439
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
15-469 |
2.98e-64 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 220.36 E-value: 2.98e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 15 SKLPDIHIPNHLPlhDYVFQNLSKFASRPCLINGATGD--VYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFV 92
Cdd:COG1022 2 SEFSDVPPADTLP--DLLRRRAARFPDRVALREKEDGIwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 93 FTFLGASYRGAIMTaanPFY---TAVEIAKqakaanaklIVT----MACF------YDRVKDLAENG---VQIVCVD--- 153
Cdd:COG1022 80 IADLAILAAGAVTV---PIYptsSAEEVAY---------ILNdsgaKVLFvedqeqLDKLLEVRDELpslRHIVVLDprg 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 154 -FAVEGCLHFSVL--SGADESLAPLVDF-----SSNDVVALPYSSGTTGLPKGVMLTHKGLITSV--AQQMDGQNPNlyy 223
Cdd:COG1022 148 lRDDPRLLSLDELlaLGREVADPAELEArraavKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNAraLLERLPLGPG--- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 224 hrnDVILCVLPFFHIYSlNSILLCGLRVGAAIMIMQKFD-IVALLQLIekhRISIMPIVPPIF----------------- 285
Cdd:COG1022 225 ---DRTLSFLPLAHVFE-RTVSYYALAAGATVAFAESPDtLAEDLREV---KPTFMLAVPRVWekvyagiqakaeeaggl 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 286 ------LAIAKSPEFEKYDVSS-----------------------------VRVLKSGGAPLGKELEdavreKFPTAI-- 328
Cdd:COG1022 298 krklfrWALAVGRRYARARLAGkspslllrlkhaladklvfsklrealggrLRFAVSGGAALGPELA-----RFFRALgi 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 329 -LGQGYGMTEAGPVLSMSlafakEPFQVKAGACGTVVRNAEMKIVDTetgaslpanssGEICIRGDQIMKGYLNDLESTK 407
Cdd:COG1022 373 pVLEGYGLTETSPVITVN-----RPGDNRIGTVGPPLPGVEVKIAED-----------GEILVRGPNVMKGYYKNPEATA 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 778728825 408 RTIDKEGWLHTGDIGFVDDDNELFIVDRLKELIKF---KafQVAPAELEALLITHPKLSDAAVIG 469
Cdd:COG1022 437 EAFDADGWLHTGDIGELDEDGFLRITGRKKDLIVTsggK--NVAPQPIENALKASPLIEQAVVVG 499
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
55-532 |
1.90e-63 |
|
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: 213.85 E-value: 1.90e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 55 TYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIVTMAC 134
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 135 FydrvkdlAENGVQIVCVDfavegclHFSVLSGADESLAPlvDFSSNDVVALPYSSGTTGLPKGVMLTHKGLITSVAqqm 214
Cdd:TIGR01923 81 L-------EEKDFQADSLD-------RIEAAGRYETSLSA--SFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAV--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 215 dGQNPNLYYHRNDVILCVLPFFHIYSLnSILLCGLRVGAAIMIMQKFDivALLQLIEKHRISIMPIVPPIFLAIAKspef 294
Cdd:TIGR01923 142 -GSKENLGFTEDDNWLLSLPLYHISGL-SILFRWLIEGATLRIVDKFN--QLLEMIANERVTHISLVPTQLNRLLD---- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 295 EKYDVSSVRVLKSGGAPLGKEL-EDAVREKFPTAilgQGYGMTEAGpvlSMSLAFAKEPFQVKAGAcGTVVRNAEMKI-V 372
Cdd:TIGR01923 214 EGGHNENLRKILLGGSAIPAPLiEEAQQYGLPIY---LSYGMTETC---SQVTTATPEMLHARPDV-GRPLAGREIKIkV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 373 DTETGaslpansSGEICIRGDQIMKGYLNDlESTKRTIDKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAEL 452
Cdd:TIGR01923 287 DNKEG-------HGEIMVKGANLMKGYLYQ-GELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEI 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 453 EALLITHPKLSDAAVIGMPDVEAGEVPVAFVmKANgGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKEL 532
Cdd:TIGR01923 359 ETVLYQHPGIQEAVVVPKPDAEWGQVPVAYI-VSE-SDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
182-529 |
5.85e-63 |
|
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: 209.43 E-value: 5.85e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 182 DVVALPYSSGTTGLPKGVMLTHKGLITSVAQQMDGQNPNlyyhRNDVILCVLPFFHIYSLNsILLCGLRVGAAIMIMQKF 261
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLT----EADVYLNMLPLFHIAGLN-LALATFHAGGANVVMEKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 262 DIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLksggapLGKELEDAVrEKFPTAILGQ---GYGMTEA 338
Cdd:cd17637 76 DPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHV------LGLDAPETI-QRFEETTGATfwsLYGQTET 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 339 GPVLSMSlafakePFQVKAGACGTVVRNAEMKIVDtETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIdKEGWLHT 418
Cdd:cd17637 149 SGLVTLS------PYRERPGSAGRPGPLVRVRIVD-DNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 419 GDIGFVDDDNELFIVDRL--KELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEV 496
Cdd:cd17637 221 GDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADEL 300
|
330 340 350
....*....|....*....|....*....|...
gi 778728825 497 KQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILR 529
Cdd:cd17637 301 IEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
32-532 |
1.35e-62 |
|
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: 213.14 E-value: 1.35e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 32 VFQNLSKFASR---PCLINGATGDV-YTYHdvQLTAR--RVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIM 105
Cdd:cd05923 3 VFEMLRRAASRapdACAIADPARGLrLTYS--ELRARieAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 106 TAANPFYTAVEIAKQAKAANAKLIVtmacfydrVKDLAEnGVQIVCVDFAVEGCLHFSVLSGADESLAPLVDFSSNDVVA 185
Cdd:cd05923 81 ALINPRLKAAELAELIERGEMTAAV--------IAVDAQ-VMDAIFQSGVRVLALSDLVGLGEPESAGPLIEDPPREPEQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 186 ---LPYSSGTTGLPKGVMLTHKGlITSVAQQMDGQNPNLYyHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKFD 262
Cdd:cd05923 152 pafVFYTSGTTGLPKGAVIPQRA-AESRVLFMSTQAGLRH-GRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 263 IVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILGQgYGMTEAgpvl 342
Cdd:cd05923 230 PADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNI-YGTTEA---- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 343 sMSLAFAKEPFQVKAGACGTvvrNAEMKIVDTETGAS--LPANSSGEICIR--GDQIMKGYLNDLESTKRTIdKEGWLHT 418
Cdd:cd05923 305 -MNSLYMRDARTGTEMRPGF---FSEVRIVRIGGSPDeaLANGEEGELIVAaaADAAFTGYLNQPEATAKKL-QDGWYRT 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 419 GDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVmKANGGAISEEEVKQ 498
Cdd:cd05923 380 GDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACV-VPREGTLSADELDQ 458
|
490 500 510
....*....|....*....|....*....|....*
gi 778728825 499 F-IAKQVVFYKRLKRVFFVNAIPKAPSGKILRKEL 532
Cdd:cd05923 459 FcRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
28-542 |
2.42e-62 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 213.36 E-value: 2.42e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 28 LHDYVFQNLSKFASRPCLINGAtgDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTA 107
Cdd:PRK07470 9 LAHFLRQAARRFPDRIALVWGD--RSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 108 ANPFYTAVEIAKQAKAANAKLIVTMACFYDRVKdlaenGVQIVCVDFavegcLHFSVLSGAD--ESLAPLVDFSSNDVVA 185
Cdd:PRK07470 87 TNFRQTPDEVAYLAEASGARAMICHADFPEHAA-----AVRAASPDL-----THVVAIGGARagLDYEALVARHLGARVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 186 L-------P----YSSGTTGLPKGVMLTHKGLITSVAQQMDGQNPNLYYHrnDVILCVLPFFH---IYslnsiLLCGLRV 251
Cdd:PRK07470 157 NaavdhddPcwffFTSGTTGRPKAAVLTHGQMAFVITNHLADLMPGTTEQ--DASLVVAPLSHgagIH-----QLCQVAR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 252 GAAIMIM--QKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFpTAIL 329
Cdd:PRK07470 230 GAATVLLpsERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKL-GKVL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 330 GQGYGMTEAG---PVLSMSLAFAKEPFQVKAGACGTVVRNAEMKIVDTEtGASLPANSSGEICIRGDQIMKGYLNDLEST 406
Cdd:PRK07470 309 VQYFGLGEVTgniTVLPPALHDAEDGPDARIGTCGFERTGMEVQIQDDE-GRELPPGETGEICVIGPAVFAGYYNNPEAN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 407 KRTIdKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKA 486
Cdd:PRK07470 388 AKAF-RDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVAR 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 778728825 487 NGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELRAKL-ASGAYN 542
Cdd:PRK07470 467 DGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREELeERGLLD 523
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
42-540 |
7.68e-62 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 211.47 E-value: 7.68e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 42 RPCLINGATGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQA 121
Cdd:PRK13391 13 KPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 122 KAANAKLIVTMACFYDRVKDLAENGVqivcvdfAVEGCLhfsVLSGADESlAPLVDFSsNDVVALP-------------- 187
Cdd:PRK13391 93 DDSGARALITSAAKLDVARALLKQCP-------GVRHRL---VLDGDGEL-EGFVGYA-EAVAGLPatpiadeslgtdml 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 188 YSSGTTGLPKGVM--LTHKGLITSVAQQMDGQNpnLYYHRNDVI-LCVLPFFHIYSLNSILLcGLRVGAAIMIMQKFDIV 264
Cdd:PRK13391 161 YSSGTTGRPKGIKrpLPEQPPDTPLPLTAFLQR--LWGFRSDMVyLSPAPLYHSAPQRAVML-VIRLGGTVIVMEHFDAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 265 ALLQLIEKHRISIMPIVPPIFLAIAKSPE--FEKYDVSSVRVLKSGGAPLGKELEDAVREKF-PtaILGQGYGMTEAGPV 341
Cdd:PRK13391 238 QYLALIEEYGVTHTQLVPTMFSRMLKLPEevRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWgP--IIHEYYAATEGLGF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 342 LSMSlafaKEPFQVKAGACGTVVRnAEMKIVDtETGASLPANSSGEICIRGDQIMKgYLNDLESTKRTIDKEG-WLHTGD 420
Cdd:PRK13391 316 TACD----SEEWLAHPGTVGRAMF-GDLHILD-DDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 421 IGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISE---EEVK 497
Cdd:PRK13391 389 IGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPalaAELI 468
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 778728825 498 QFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELRAKLASGA 540
Cdd:PRK13391 469 AFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDRYWGNK 511
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
40-538 |
4.85e-61 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 209.35 E-value: 4.85e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 40 ASRPCLINGAtGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAK 119
Cdd:PRK07514 16 RDAPFIETPD-GLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 120 QAKAANAKLIVTMACFYDRVKDLAEN-GVQIV-CVDFAVEGCLhFSVLSGADESLAPlVDFSSNDVVALPYSSGTTGLPK 197
Cdd:PRK07514 95 FIGDAEPALVVCDPANFAWLSKIAAAaGAPHVeTLDADGTGSL-LEAAAAAPDDFET-VPRGADDLAAILYTSGTTGRSK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 198 GVMLTHKGLITSVAQQMDgqnpnlYYH--RNDVILCVLPFFHIYSL----NSILLCGlrvgaAIMI-MQKFDIVALLQLI 270
Cdd:PRK07514 173 GAMLSHGNLLSNALTLVD------YWRftPDDVLIHALPIFHTHGLfvatNVALLAG-----ASMIfLPKFDPDAVLALM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 271 EkhRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILgQGYGMTEAGPVLSmslafak 350
Cdd:PRK07514 242 P--RATVMMGVPTFYTRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAIL-ERYGMTETNMNTS------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 351 EPFQVK--AGACGTVVRNAEMKIVDTETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLHTGDIGFVDDDN 428
Cdd:PRK07514 312 NPYDGErrAGTVGFPLPGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 429 ELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVFYK 508
Cdd:PRK07514 392 YVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAILAALKGRLARFK 471
|
490 500 510
....*....|....*....|....*....|
gi 778728825 509 RLKRVFFVNAIPKAPSGKILRKELRAKLAS 538
Cdd:PRK07514 472 QPKRVFFVDELPRNTMGKVQKNLLREQYAD 501
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
54-469 |
1.50e-60 |
|
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: 206.68 E-value: 1.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 54 YTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTaanPFYTaveiakqakaanaklivtma 133
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPV---PIYP-------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 134 cfydrvkdlaengvqivcvDFAVEGCLHfsVLSGADESLApLVDfSSNDVVALPYSSGTTGLPKGVMLTHKGL---ITSV 210
Cdd:cd05907 63 -------------------TSSAEQIAY--ILNDSEAKAL-FVE-DPDDLATIIYTSGTTGRPKGVMLSHRNIlsnALAL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 211 AQQMDGQNpnlyyhrNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQkfDIVALLQLIEKHRISIMPIVP----PIFL 286
Cdd:cd05907 120 AERLPATE-------GDRHLSFLPLAHVFERRAGLYVPLLAGARIYFAS--SAETLLDDLSEVRPTVFLAVPrvweKVYA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 287 AI--AKSPEFEK--YDV---SSVRVLKSGGAPLGKELEdavrEKFptAILG----QGYGMTEAGPVLSMSLafakePFQV 355
Cdd:cd05907 191 AIkvKAVPGLKRklFDLavgGRLRFAASGGAPLPAELL----HFF--RALGipvyEGYGLTETSAVVTLNP-----PGDN 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 356 KAGACGTVVRNAEMKIVDtetgaslpansSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLHTGDIGFVDDDNELFIVDR 435
Cdd:cd05907 260 RIGTVGKPLPGVEVRIAD-----------DGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGR 328
|
410 420 430
....*....|....*....|....*....|....*.
gi 778728825 436 LKELIKfKAF--QVAPAELEALLITHPKLSDAAVIG 469
Cdd:cd05907 329 KKDLII-TSGgkNISPEPIENALKASPLISQAVVIG 363
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
55-534 |
2.40e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 208.63 E-value: 2.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 55 TYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIVTMAC 134
Cdd:PRK07788 76 TYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 135 FYDRVKDLAENGVQIVCVDFAVEGclhFSVLSGADESLAPLVDFSSNDVVALP--------YSSGTTGLPKGVMLTHKGL 206
Cdd:PRK07788 156 FTDLLSALPPDLGRLRAWGGNPDD---DEPSGSTDETLDDLIAGSSTAPLPKPpkpggiviLTSGTTGTPKGAPRPEPSP 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 207 ITSVAQQMDgQNPnlyYHRNDVILCVLPFFHIYSLnSILLCGLRVGAAIMIMQKFDIVALLQLIEKHRISIMpIVPPIFL 286
Cdd:PRK07788 233 LAPLAGLLS-RVP---FRAGETTLLPAPMFHATGW-AHLTLAMALGSTVVLRRRFDPEATLEDIAKHKATAL-VVVPVML 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 287 A-IAKSPE--FEKYDVSSVRVLKSGGAPLGKELEDAVREKF-PtaILGQGYGMTEAgpvlsmslAFAK----EPFQVKAG 358
Cdd:PRK07788 307 SrILDLGPevLAKYDTSSLKIIFVSGSALSPELATRALEAFgP--VLYNLYGSTEV--------AFATiatpEDLAEAPG 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 359 ACGTVVRNAEMKIVDtETGASLPANSSGEICIRGDQIMKGYLNDleSTKRTIDkeGWLHTGDIGFVDDDNELFIVDRLKE 438
Cdd:PRK07788 377 TVGRPPKGVTVKILD-ENGNEVPRGVVGRIFVGNGFPFEGYTDG--RDKQIID--GLLSSGDVGYFDEDGLLFVDGRDDD 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 439 LIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVFYKRLKRVFFVNA 518
Cdd:PRK07788 452 MIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDE 531
|
490
....*....|....*.
gi 778728825 519 IPKAPSGKILRKELRA 534
Cdd:PRK07788 532 LPRNPTGKVLKRELRE 547
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
28-537 |
2.75e-60 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 208.45 E-value: 2.75e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 28 LHDYVFQNLSKFASRPCLINGaTGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTA 107
Cdd:PRK06087 25 LADYWQQTARAMPDKIAVVDN-HGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 108 ANPFYTAVEIAKQAKAANAKLIVTMACFY------------DRVKDLAengvQIVCVDFAVEG--CLHFSVLSGADESLA 173
Cdd:PRK06087 104 LLPSWREAELVWVLNKCQAKMFFAPTLFKqtrpvdlilplqNQLPQLQ----QIVGVDKLAPAtsSLSLSQIIADYEPLT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 174 PLVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQMDGQNPNlyyhRNDVILCVLP------FFHiySLNSILLC 247
Cdd:PRK06087 180 TAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLT----WQDVFMMPAPlghatgFLH--GVTAPFLI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 248 GLRVgaaiMIMQKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELedaVREKFPTA 327
Cdd:PRK06087 254 GARS----VLLDIFTPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKV---ARECQQRG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 328 I-LGQGYGMTEAGPVLSMSLAfakEPFQVKAGACGTVVRNAEMKIVDtETGASLPANSSGEICIRGDQIMKGYLNDLEST 406
Cdd:PRK06087 327 IkLLSVYGSTESSPHAVVNLD---DPLSRFMHTDGYAAAGVEIKVVD-EARKTLPPGCEGEEASRGPNVFMGYLDEPELT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 407 KRTIDKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAF-VMK 485
Cdd:PRK06087 403 ARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYvVLK 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 778728825 486 ANGGAISEEEVKQFIAKQ-VVFYKRLKRVFFVNAIPKAPSGKILRKELRAKLA 537
Cdd:PRK06087 483 APHHSLTLEEVVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDIM 535
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
65-533 |
3.76e-60 |
|
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: 205.75 E-value: 3.76e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 65 RVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASY----RGAIMTAANPFYTAVEIAKQAKAANAKLIVTMACFYDRVK 140
Cdd:cd05922 5 AAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYaggrLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 141 DlaengVQIVCVDFAVegclhfsVLSG----ADESLAPLVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLIT---SVAQQ 213
Cdd:cd05922 85 D-----ALPASPDPGT-------VLDAdgirAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLAnarSIAEY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 214 MDgqnpnlyYHRNDVILCVLPFFHIYSLnSILLCGLRVGAAIMIMQKFDI-VALLQLIEKHRISIMPIVPPIFlAIAKSP 292
Cdd:cd05922 153 LG-------ITADDRALTVLPLSYDYGL-SVLNTHLLRGATLVLTNDGVLdDAFWEDLREHGATGLAGVPSTY-AMLTRL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 293 EFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILGQGYGMTEAGPVLSMSLAfakEPFQVKAGACGTVVRNAEMKIV 372
Cdd:cd05922 224 GFDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPP---ERILEKPGSIGLAIPGGEFEIL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 373 DtETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAEL 452
Cdd:cd05922 301 D-DDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 453 EALLITHPKLSDAAVIGMPDvEAGEVPVAFVMKANGgaISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKEL 532
Cdd:cd05922 380 EAAARSIGLIIEAAAVGLPD-PLGEKLALFVTAPDK--IDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
.
gi 778728825 533 R 533
Cdd:cd05922 457 R 457
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
50-534 |
6.03e-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: 201.89 E-value: 6.03e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 50 TGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAImtaANPFYTaveiakqakaanakLI 129
Cdd:cd05971 3 TPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAI---AVPLFA--------------LF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 130 VTMACFYdRVKDlaengvqivcvdfavegclhfsvlSGAdeslAPLVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLI-- 207
Cdd:cd05971 66 GPEALEY-RLSN------------------------SGA----SALVTDGSDDPALIIYTSGTTGPPKGALHAHRVLLgh 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 208 ---TSVAQQMDGQNPNLYYHRNDvilcvlpFFHIYSLNSILLCGLRVGAAIMI--MQKFDIVALLQLIEKHRISiMPIVP 282
Cdd:cd05971 117 lpgVQFPFNLFPRDGDLYWTPAD-------WAWIGGLLDVLLPSLYFGVPVLAhrMTKFDPKAALDLMSRYGVT-TAFLP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 283 PIFLAIAKS--PEFEKYDVSsVRVLKSGGAPLGKELEDAVREKFPTAIlGQGYGMTEAGPVLSMSLAFakepFQVKAGAC 360
Cdd:cd05971 189 PTALKMMRQqgEQLKHAQVK-LRAIATGGESLGEELLGWAREQFGVEV-NEFYGQTECNLVIGNCSAL----FPIKPGSM 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 361 GTVVRNAEMKIVDTEtGASLPANSSGEICIRGDQ--IMKGYLNDLESTKRTIdKEGWLHTGDIGFVDDDNELFIVDRLKE 438
Cdd:cd05971 263 GKPIPGHRVAIVDDN-GTPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKM-AGDWLLTGDLGRKDSDGYFWYVGRDDD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 439 LIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEE---EVKQFIAKQVVFYKRLKRVFF 515
Cdd:cd05971 341 VITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDAlarEIQELVKTRLAAHEYPREIEF 420
|
490
....*....|....*....
gi 778728825 516 VNAIPKAPSGKILRKELRA 534
Cdd:cd05971 421 VNELPRTATGKIRRRELRA 439
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
54-535 |
7.34e-58 |
|
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: 199.27 E-value: 7.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 54 YTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTaanPFYTAVEiakqakaanaklivtma 133
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVIC---PLFSAFG----------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 134 cfYDRVKDLAENGVQIVCVdfavegclhfsvlsgADESLAPLVDfsSNDVVALPYSSGTTGLPKGVMLTHKGLIT---SV 210
Cdd:cd05969 61 --PEAIRDRLENSEAKVLI---------------TTEELYERTD--PEDPTLLHYTSGTTGTPKGVLHVHDAMIFyyfTG 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 211 AQQMDGQNPNLYYHRNDVILCVLPFFHIYS--LNsillcglrvGAAIMIMQ-KFDIVALLQLIEKHRISIMPIVPPIFLA 287
Cdd:cd05969 122 KYVLDLHPDDIYWCTADPGWVTGTVYGIWApwLN---------GVTNVVYEgRFDAESWYGIIERVKVTVWYTAPTAIRM 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 288 IAKSPEF--EKYDVSSVRVLKSGGAPLGKEledAVR---EKFPTAILgQGYGMTEAGpvlsmSLAFAKEPFQ-VKAGACG 361
Cdd:cd05969 193 LMKEGDElaRKYDLSSLRFIHSVGEPLNPE---AIRwgmEVFGVPIH-DTWWQTETG-----SIMIANYPCMpIKPGSMG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 362 TVVRNAEMKIVDTEtGASLPANSSGEICIRGD--QIMKGYLNDLESTKRTIdKEGWLHTGDIGFVDDDNELFIVDRLKEL 439
Cdd:cd05969 264 KPLPGVKAAVVDEN-GNELPPGTKGILALKPGwpSMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADDI 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 440 IKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEE---EVKQFIAKQVVFYKRLKRVFFV 516
Cdd:cd05969 342 IKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDElkeEIINFVRQKLGAHVAPREIEFV 421
|
490
....*....|....*....
gi 778728825 517 NAIPKAPSGKILRKELRAK 535
Cdd:cd05969 422 DNLPKTRSGKIMRRVLKAK 440
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
42-540 |
7.78e-58 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 200.42 E-value: 7.78e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 42 RPCLINGATGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQA 121
Cdd:PRK09088 11 RLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 122 KAANAKLIVTMAcfydrvkDLAENGVQIVCVD-FAVEgclhfsvLSGADESLAPLVDfssNDVVALP-YSSGTTGLPKGV 199
Cdd:PRK09088 91 QDAEPRLLLGDD-------AVAAGRTDVEDLAaFIAS-------ADALEPADTPSIP---PERVSLIlFTSGTSGQPKGV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 200 MLTHKglitsvAQQMDGQNPNLYYH--RNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKFDIVALLQLIEKHRISI 277
Cdd:PRK09088 154 MLSER------NLQQTAHNFGVLGRvdAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLGDPALGI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 278 MPI--VPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKE-----LEDAVRekfptaiLGQGYGMTEAGPVLSMSLAFAK 350
Cdd:PRK09088 228 THYfcVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEdilgwLDDGIP-------MVDGFGMSEAGTVFGMSVDCDV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 351 epFQVKAGACGTVVRNAEMKIVDtETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLHTGDIGFVDDDNEL 430
Cdd:PRK09088 301 --IRAKAGAAGIPTPTVQTRVVD-DQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 431 FIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVFYKRL 510
Cdd:PRK09088 378 WVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVP 457
|
490 500 510
....*....|....*....|....*....|
gi 778728825 511 KRVFFVNAIPKAPSGKILRKELRAKLASGA 540
Cdd:PRK09088 458 KHLRLVDALPRTASGKLQKARLRDALAAGR 487
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
64-534 |
3.22e-57 |
|
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: 198.37 E-value: 3.22e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 64 RRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIVTMACFYDRVKDLA 143
Cdd:cd05929 8 RAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEACAIIEI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 144 eNGVQIVCVDFAVEGCLhfsvlsGADESLAPLVDFS----SNDVVA---LPYSSGTTGLPKGVMLTHKGLITSVAQQMDG 216
Cdd:cd05929 88 -KAAALVCGLFTGGGAL------DGLEDYEAAEGGSpetpIEDEAAgwkMLYSGGTTGRPKGIKRGLPGGPPDNDTLMAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 217 QNpNLYYHRNDVILCVLPFFH----IYSLNsillcGLRVGAAIMIMQKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSP 292
Cdd:cd05929 161 AL-GFGPGADSVYLSPAPLYHaapfRWSMT-----ALFMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKLP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 293 EFE--KYDVSSVRVLKSGGAPLGKELEDAVREKFPtAILGQGYGMTEA-GPVLSMSLAFAKEPfqvkaGACGTVVRnAEM 369
Cdd:cd05929 235 EAVrnAYDLSSLKRVIHAAAPCPPWVKEQWIDWGG-PIIWEYYGGTEGqGLTIINGEEWLTHP-----GSVGRAVL-GKV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 370 KIVDtETGASLPANSSGEICIRGDQiMKGYLNDLESTKRTIDKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAP 449
Cdd:cd05929 308 HILD-EDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 450 AELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANG---GAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGK 526
Cdd:cd05929 386 QEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGadaGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGK 465
|
....*...
gi 778728825 527 ILRKELRA 534
Cdd:cd05929 466 LYRRLLRD 473
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
48-537 |
6.58e-57 |
|
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: 199.00 E-value: 6.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 48 GATGDVYTYHDVQLTARRVAAGLHNLGiKKGDVVMNLLPNSPEFVFTFLGASYRGAImtaANPFY------TAVEIAKQA 121
Cdd:cd05931 19 GGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAI---AVPLPpptpgrHAERLAAIL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 122 KAANAKLIVTMACFYDRVKDLAENG-----VQIVCVDfavegclhfsVLSGADESLAPLVDFSSNDVVALPYSSGTTGLP 196
Cdd:cd05931 95 ADAGPRVVLTTAAALAAVRAFAASRpaagtPRLLVVD----------LLPDTSAADWPPPSPDPDDIAYLQYTSGSTGTP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 197 KGVMLTHKGLITSVAQQMDGqnpnLYYHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKFDIVA----LLQLIEK 272
Cdd:cd05931 165 KGVVVTHRNLLANVRQIRRA----YGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAAFLRrplrWLRLISR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 273 HRISIMPIvpPIF---LAI--AKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKF------PTAILgQGYGMTEA--- 338
Cdd:cd05931 241 YRATISAA--PNFaydLCVrrVRDEDLEGLDLSSWRVALNGAEPVRPATLRRFAEAFapfgfrPEAFR-PSYGLAEAtlf 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 339 --------GPVLsmsLAFAKEPFQVKAGA-------------CGTVVRNAEMKIVDTETGASLPANSSGEICIRGDQIMK 397
Cdd:cd05931 318 vsggppgtGPVV---LRVDRDALAGRAVAvaaddpaarelvsCGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVAS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 398 GYLNDLESTKRT------IDKEGWLHTGDIGFVDDDnELFIVDRLKELIKFKAFQVAPAELEA-LLITHPKL--SDAAVI 468
Cdd:cd05931 395 GYWGRPEATAETfgalaaTDEGGWLRTGDLGFLHDG-ELYITGRLKDLIIVRGRNHYPQDIEAtAEEAHPALrpGCVAAF 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 778728825 469 GMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVV--FYKRLKRVFFV--NAIPKAPSGKILRKELRAKLA 537
Cdd:cd05931 474 SVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAreHGVAPADVVLVrpGSIPRTSSGKIQRRACRAAYL 546
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
54-529 |
1.56e-56 |
|
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: 196.12 E-value: 1.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 54 YTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIakqakaanaklivtma 133
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEV---------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 134 cfydrvkdlaengvqivcvdfavegclHFSVlsgaDESLAPLVdFSSN--DVVALPYSSGTTGLPKGVMLTHKGLITSVa 211
Cdd:cd05914 72 ---------------------------HHIL----NHSEAKAI-FVSDedDVALINYTSGTTGNSKGVMLTYRNIVSNV- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 212 qqmDGQNPNLYYHRNDVILCVLPFFHIYSLNSILLCGLRVGA----------AIMIMQKFD------IVALLQLIEKhrI 275
Cdd:cd05914 119 ---DGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAhvvfldkipsAKIIALAFAqvtptlGVPVPLVIEK--I 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 276 SIMPIVPPIFLAIAKSPEFEKYDVSSVR------VLK----------SGGAPLGKELEDAVRE-KFPTAIlgqGYGMTEA 338
Cdd:cd05914 194 FKMDIIPKLTLKKFKFKLAKKINNRKIRklafkkVHEafggnikefvIGGAKINPDVEEFLRTiGFPYTI---GYGMTET 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 339 GPVLSMSlafakEPFQVKAGACGTVVRNAEMKIVDTEtgaslPANSSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLHT 418
Cdd:cd05914 271 APIISYS-----PPNRIRLGSAGKVIDGVEVRIDSPD-----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHT 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 419 GDIGFVDDDNELFIVDRLKELIKFKAFQ-VAPAELEALLITHPKLSDAAVIgmpDVEAGEVPVAFV----MKANGGAISE 493
Cdd:cd05914 341 GDLGKIDAEGYLYIRGRKKEMIVLSSGKnIYPEEIEAKINNMPFVLESLVV---VQEKKLVALAYIdpdfLDVKALKQRN 417
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 778728825 494 ------EEVKQFIAKQVVFYKRLKRVFFVNA-IPKAPSGKILR 529
Cdd:cd05914 418 iidaikWEVRDKVNQKVPNYKKISKVKIVKEeFEKTPKGKIKR 460
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
55-534 |
2.11e-56 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 197.97 E-value: 2.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 55 TYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIVTMAC 134
Cdd:PRK13295 57 TYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKT 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 135 F--YD------RVKDLAENGVQIVCVDfaVEGCLHF-SVLSGADESLAPLVD-------FSSNDVVALPYSSGTTGLPKG 198
Cdd:PRK13295 137 FrgFDhaamarRLRPELPALRHVVVVG--GDGADSFeALLITPAWEQEPDAPailarlrPGPDDVTQLIYTSGTTGEPKG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 199 VMLTHKGL---ITSVAQQMD-GQNpnlyyhrnDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKFDIVALLQLIEKHR 274
Cdd:PRK13295 215 VMHTANTLmanIVPYAERLGlGAD--------DVILMASPMAHQTGFMYGLMMPVMLGATAVLQDIWDPARAAELIRTEG 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 275 ISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILGqGYGMTEAGPVLSMSLAfakEPFQ 354
Cdd:PRK13295 287 VTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVS-AWGMTENGAVTLTKLD---DPDE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 355 VKAGACGTVVRNAEMKIVDTEtGASLPANSSGEICIRGDQIMKGYLNDLESTKrtIDKEGWLHTGDIGFVDDDNELFIVD 434
Cdd:PRK13295 363 RASTTDGCPLPGVEVRVVDAD-GAPLPAGQIGRLQVRGCSNFGGYLKRPQLNG--TDADGWFDTGDLARIDADGYIRISG 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 435 RLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQF-----IAKQvvFYKr 509
Cdd:PRK13295 440 RSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFlkaqkVAKQ--YIP- 516
|
490 500
....*....|....*....|....*....
gi 778728825 510 lKRVFFVNAIPKAPSGKI----LRKELRA 534
Cdd:PRK13295 517 -ERLVVRDALPRTPSGKIqkfrLREMLRG 544
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
27-532 |
2.97e-54 |
|
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: 190.62 E-value: 2.97e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 27 PLHDYVFQNLSKFASRPCLINGATGdvYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMT 106
Cdd:cd05920 16 PLGDLLARSAARHPDRIAVVDGDRR--LTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 107 AANPFYTAVEIAKQAKAANAKLIVtmacfydrVKDLAENgvqivcvdfavegclhFSVLSGADESLAplvdfSSNDVVAL 186
Cdd:cd05920 94 LALPSHRRSELSAFCAHAEAVAYI--------VPDRHAG----------------FDHRALARELAE-----SIPEVALF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 187 PYSSGTTGLPKGVMLTHKGLITSV--AQQMDGQNPNlyyhrnDVILCVLPFFHIYSLNS-----ILLCGLRVgaaiMIMQ 259
Cdd:cd05920 145 LLSGGTTGTPKLIPRTHNDYAYNVraSAEVCGLDQD------TVYLAVLPAAHNFPLACpgvlgTLLAGGRV----VLAP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 260 KFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFpTAILGQGYGMTEaG 339
Cdd:cd05920 215 DPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVL-GCTLQQVFGMAE-G 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 340 PVLSMSLafaKEPFQVKAGACG-TVVRNAEMKIVDtETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLHT 418
Cdd:cd05920 293 LLNYTRL---DDPDEVIIHTQGrPMSPDDEIRVVD-EEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRT 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 419 GDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMkANGGAISEEEVKQ 498
Cdd:cd05920 369 GDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVV-LRDPPPSAAQLRR 447
|
490 500 510
....*....|....*....|....*....|....*
gi 778728825 499 FI-AKQVVFYKRLKRVFFVNAIPKAPSGKILRKEL 532
Cdd:cd05920 448 FLrERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
24-538 |
5.96e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 191.31 E-value: 5.96e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 24 NHLPLH--DYVFQNLSKFASRPCLINGATgdVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYR 101
Cdd:PRK08162 14 NYVPLTplSFLERAAEVYPDRPAVIHGDR--RRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 102 GAIMTAANPFYTAVEIAKQAKAANAKLIVTMACFYDRVKDLAE--NGVQIVCVDF---AVEGCLHFS------VLSGADE 170
Cdd:PRK08162 92 GAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTEFAEVAREALAllPGPKPLVIDVddpEYPGGRFIGaldyeaFLASGDP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 171 SLAPLVDFSSNDVVALPYSSGTTGLPKGVMLTHKG-LITSVAQQMDGQNPnlyyhRNDVILCVLPFFHiyslnsillCG- 248
Cdd:PRK08162 172 DFAWTLPADEWDAIALNYTSGTTGNPKGVVYHHRGaYLNALSNILAWGMP-----KHPVYLWTLPMFH---------CNg 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 249 ------LRVGAAIMI-MQKFDIVALLQLIEKHRISIM---PIVppiFLAIAKSPEFEKYDVS-SVRVLKSGGAPLGKELE 317
Cdd:PRK08162 238 wcfpwtVAARAGTNVcLRKVDPKLIFDLIREHGVTHYcgaPIV---LSALINAPAEWRAGIDhPVHAMVAGAAPPAAVIA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 318 DAVREKFPtaiLGQGYGMTEA-GPV-----------LSMSlafakEPFQVKA--GacgtvVR---NAEMKIVDTETGASL 380
Cdd:PRK08162 315 KMEEIGFD---LTHVYGLTETyGPAtvcawqpewdaLPLD-----ERAQLKArqG-----VRyplQEGVTVLDPDTMQPV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 381 PAN--SSGEICIRGDQIMKGYLNDLESTKRTIdKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLIT 458
Cdd:PRK08162 382 PADgeTIGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYR 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 459 HPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVFYKRLKRVFFvNAIPKAPSGKILRKELRAKLAS 538
Cdd:PRK08162 461 HPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQAKS 539
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
51-534 |
6.71e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 190.72 E-value: 6.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 51 GDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIV 130
Cdd:PRK06164 33 DRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 131 TMACFydRVKDLAE--NGVQ---------IVCVDFAVE------GCLHFSVLSGAD--ESLAPLVDFSSNDVVALPYS-S 190
Cdd:PRK06164 113 VWPGF--KGIDFAAilAAVPpdalpplraIAVVDDAADatpapaPGARVQLFALPDpaPPAAAGERAADPDAGALLFTtS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 191 GTTGLPKGVMLTHKGLITSVAQQMDGqnpnLYYHRNDVILCVLPFFHIYSLNSiLLCGLRVGAAIMIMQKFDIVALLQLI 270
Cdd:PRK06164 191 GTTSGPKLVLHRQATLLRHARAIARA----YGYDPGAVLLAALPFCGVFGFST-LLGALAGGAPLVCEPVFDAARTARAL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 271 EKHRISIMPIVPPIFLAIAKSpEFEKYDVSSVRVLKSGG-APLGKELEDAVR-EKFPTAILgqgYGMTEagpVLS-MSLA 347
Cdd:PRK06164 266 RRHRVTHTFGNDEMLRRILDT-AGERADFPSARLFGFASfAPALGELAALARaRGVPLTGL---YGSSE---VQAlVALQ 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 348 FAKEPFQVKAGACGTVVR-NAEMKIVDTETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLHTGDIGFVDD 426
Cdd:PRK06164 339 PATDPVSVRIEGGGRPASpEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRG 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 427 DNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMpDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVF 506
Cdd:PRK06164 419 DGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA-TRDGKTVPVAFVIPTDGASPDEAGLMAACREALAG 497
|
490 500 510
....*....|....*....|....*....|.
gi 778728825 507 YKRLKRVFFVNAIPKAPSG---KILRKELRA 534
Cdd:PRK06164 498 FKVPARVQVVEAFPVTESAngaKIQKHRLRE 528
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
54-533 |
2.11e-53 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 188.89 E-value: 2.11e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 54 YTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIVTMA 133
Cdd:TIGR02262 31 LSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 134 CFYDRVKDLA---ENGVQIVCVDFAVEGCLHFSVLSGADESLAPLVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLITSv 210
Cdd:TIGR02262 111 ALLPVIKAALgksPHLEHRVVVGRPEAGEVQLAELLATESEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWT- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 211 AQQMDGqnPNLYYHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIM-QKFDIVALLQLIEKHRISIMPIVPPIFLAIA 289
Cdd:TIGR02262 190 AELYAR--NTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMgERPTPDAVFDRLRRHQPTIFYGVPTLYAAML 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 290 KSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILgQGYGMTEAGPVLSMSLafakePFQVKAGACGTVVRNAEM 369
Cdd:TIGR02262 268 ADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIV-DGIGSTEMLHIFLSNL-----PGDVRYGTSGKPVPGYRL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 370 KIVDtETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIDKEgWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAP 449
Cdd:TIGR02262 342 RLVG-DGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTFQGE-WTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSP 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 450 AELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILR 529
Cdd:TIGR02262 420 FEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQR 499
|
....
gi 778728825 530 KELR 533
Cdd:TIGR02262 500 FKLR 503
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
39-534 |
3.28e-53 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 189.20 E-value: 3.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 39 FASRPCLINGATgdVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIA 118
Cdd:PRK06155 34 YPDRPLLVFGGT--RWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 119 KQAKAANAKLIVTMACFYDRVK-----DLAENGVQIVCVDFAVEGCLHFSVLS--GADESlAPLVDFSSNDVVALPYSSG 191
Cdd:PRK06155 112 HILRNSGARLLVVEAALLAALEaadpgDLPLPAVWLLDAPASVSVPAGWSTAPlpPLDAP-APAAAVQPGDTAAILYTSG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 192 TTGLPKGVMLTHkglitsvAQQMD-GQN--PNLYYHRNDVILCVLPFFHIYSLNSiLLCGLRVGAAIMIMQKFDIVALLQ 268
Cdd:PRK06155 191 TTGPSKGVCCPH-------AQFYWwGRNsaEDLEIGADDVLYTTLPLFHTNALNA-FFQALLAGATYVLEPRFSASGFWP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 269 LIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPlgKELEDAVREKFPTAILgQGYGMTEAGPVLSMSLAF 348
Cdd:PRK06155 263 AVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVP--AALHAAFRERFGVDLL-DGYGSTETNFVIAVTHGS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 349 AKepfqvkAGACGTVVRNAEMKIVDtETGASLPANSSGEICIRGDQ---IMKGYLNDLESTKRTIdKEGWLHTGDIGFVD 425
Cdd:PRK06155 340 QR------PGSMGRLAPGFEARVVD-EHDQELPDGEPGELLLRADEpfaFATGYFGMPEKTVEAW-RNLWFHTGDRVVRD 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 426 DDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAG-EVPVAFVMKaNGGAISEEEVKQFIAKQV 504
Cdd:PRK06155 412 ADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEdEVMAAVVLR-DGTALEPVALVRHCEPRL 490
|
490 500 510
....*....|....*....|....*....|
gi 778728825 505 VFYKRLKRVFFVNAIPKAPSGKILRKELRA 534
Cdd:PRK06155 491 AYFAVPRYVEFVAALPKTENGKVQKFVLRE 520
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
21-537 |
6.81e-52 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 190.91 E-value: 6.81e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 21 HIPNHLPLHDYVFQNLSKFASRPCLINGATGDVyTYHDVqLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASY 100
Cdd:PRK08633 610 RKEALPPLAEAWIDTAKRNWSRLAVADSTGGEL-SYGKA-LTGALALARLLKRELKDEENVGILLPPSVAGALANLALLL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 101 RGAimTAANPFYTAVE--IAKQAKAANAKLIVTMACFYDRVKD------LAENGVQIVCVDFA-----VEGCLHF---SV 164
Cdd:PRK08633 688 AGK--VPVNLNYTASEaaLKSAIEQAQIKTVITSRKFLEKLKNkgfdleLPENVKVIYLEDLKakiskVDKLTALlaaRL 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 165 LSGADESLAPLVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQMDGQNPNlyyhRNDVILCVLPFFHIYSLNSI 244
Cdd:PRK08633 766 LPARLLKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLR----NDDVILSSLPFFHSFGLTVT 841
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 245 LLCGLRVG-AAIMIMQKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREK 323
Cdd:PRK08633 842 LWLPLLEGiKVVYHPDPTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEK 921
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 324 FPTAILgQGYGMTEAGPVLSMSLAFAKEP---FQV--KAGACGTVVRNAEMKIVDTETGASLPANSSGEICIRGDQIMKG 398
Cdd:PRK08633 922 FGIRIL-EGYGATETSPVASVNLPDVLAAdfkRQTgsKEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKG 1000
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 399 YLNDLESTK---RTIDKEGWLHTGDIGFVDDDNELFIVDRLK-------ELIKFKAfqVAPAELEALLITHPKLsdaAVI 468
Cdd:PRK08633 1001 YLGDPEKTAeviKDIDGIGWYVTGDKGHLDEDGFLTITDRYSrfakiggEMVPLGA--VEEELAKALGGEEVVF---AVT 1075
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 778728825 469 GMPDVEAGEVPVAFVMKangGAISEEEVKQFIAKQvvFYKRL---KRVFFVNAIPKAPSGKI-LR--KELRAKLA 537
Cdd:PRK08633 1076 AVPDEKKGEKLVVLHTC---GAEDVEELKRAIKES--GLPNLwkpSRYFKVEALPLLGSGKLdLKglKELALALL 1145
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
49-534 |
1.61e-51 |
|
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: 183.30 E-value: 1.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 49 ATGDVYTYHDVQLTARRVAAGLHNlGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANpfYTA--VEIAKQAKAANA 126
Cdd:cd05909 3 TLGTSLTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLN--YTAglRELRACIKLAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 127 KLIVTMACFYDRVKDL----AENGVQIVCVD-------FAvEGC---LHFSVLSGADESLAPLVDFSSNDVVALPYSSGT 192
Cdd:cd05909 80 KTVLTSKQFIEKLKLHhlfdVEYDARIVYLEdlrakisKA-DKCkafLAGKFPPKWLLRIFGVAPVQPDDPAVILFTSGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 193 TGLPKGVMLTHKGLITSVAQQMDGQNPNlyyhRNDVILCVLPFFHIYSLNSILLCGLRVGAAI-MIMQKFDIVALLQLIE 271
Cdd:cd05909 159 EGLPKGVVLSHKNLLANVEQITAIFDPN----PEDVVFGALPFFHSFGLTGCLWLPLLSGIKVvFHPNPLDYKKIPELIY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 272 KHRISIMPIVPPIFLAIAKSpeFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILgQGYGMTEAGPVLSMSLafAKE 351
Cdd:cd05909 235 DKKATILLGTPTFLRGYARA--AHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRIL-EGYGTTECSPVISVNT--PQS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 352 PFqvKAGACGTVVRNAEMKIVDTETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIdKEGWLHTGDIGFVDDDNELF 431
Cdd:cd05909 310 PN--KEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 432 IVDRLKELIKFKAFQVAPAELEALLITH-PKLSDAAVIGMPDVEAGEVPVAFVMKANggaISEEEVKQFI-AKQVVFYKR 509
Cdd:cd05909 387 ITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTTTD---TDPSSLNDILkNAGISNLAK 463
|
490 500
....*....|....*....|....*
gi 778728825 510 LKRVFFVNAIPKAPSGKILRKELRA 534
Cdd:cd05909 464 PSYIHQVEEIPLLGTGKPDYVTLKA 488
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
23-538 |
2.06e-51 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 184.62 E-value: 2.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 23 PNHLPLHdyVFQNLSKFAS-RPCLINGATGD-VYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASY 100
Cdd:PLN02860 2 ANHSQAH--ICQCLTRLATlRGNAVVTISGNrRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVAC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 101 RGAIMTAANPFYTAVEIAKQAKAANAKLIVT-MAC--FYDRVK--DLAENGVQIVCVDFAVEGCLHFSVLSGADESLAPL 175
Cdd:PLN02860 80 AGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTdETCssWYEELQndRLPSLMWQVFLESPSSSVFIFLNSFLTTEMLKQRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 176 VD-------FSSNDVVALPYSSGTTGLPKGVMLTHKGLIT-SVAQ-QMDGqnpnlyYHRNDVILCVLPFFHIYSLNSILl 246
Cdd:PLN02860 160 LGtteldyaWAPDDAVLICFTSGTTGRPKGVTISHSALIVqSLAKiAIVG------YGEDDVYLHTAPLCHIGGLSSAL- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 247 CGLRVGAAIMIMQKFDIVALLQLIEKHRISIMPIVPPI---FLAIAKSPEFEKyDVSSVRVLKSGGAPLGKELEDAVREK 323
Cdd:PLN02860 233 AMLMVGACHVLLPKFDAKAALQAIKQHNVTSMITVPAMmadLISLTRKSMTWK-VFPSVRKILNGGGSLSSRLLPDAKKL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 324 FPTAILGQGYGMTEAGPVLS-MSLAFAKE----------------PFQVKAGAC-GTVVRNAEMKIvdtetgaSLPANS- 384
Cdd:PLN02860 312 FPNAKLFSAYGMTEACSSLTfMTLHDPTLespkqtlqtvnqtkssSVHQPQGVCvGKPAPHVELKI-------GLDESSr 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 385 SGEICIRGDQIMKGYLNDLESTKRTIDKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSD 464
Cdd:PLN02860 385 VGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVAS 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 465 AAVIGMPDVEAGEVPVAFV--------------MKANGGAISEEEVKQFIAKQVVFYKRLKRVFFVN--AIPKAPSGKIL 528
Cdd:PLN02860 465 VVVVGVPDSRLTEMVVACVrlrdgwiwsdnekeNAKKNLTLSSETLRHHCREKNLSRFKIPKLFVQWrkPFPLTTTGKIR 544
|
570
....*....|
gi 778728825 529 RKELRAKLAS 538
Cdd:PLN02860 545 RDEVRREVLS 554
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
180-534 |
4.64e-50 |
|
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: 176.13 E-value: 4.64e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 180 SNDVVALPYSSGTTGLPKGVMLTHKGLitsVAQQMDGQNpNLYYHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIM- 258
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNE---VYNAWMLAL-NSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 259 -----QKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEfeKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILgQGY 333
Cdd:cd05944 77 pagyrNPGLFDNFWKLVERYRITSLSTVPTVYAALLQVPV--NADISSLRFAMSGAAPLPVELRARFEDATGLPVV-EGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 334 GMTEAGPVlsMSLAFAKEPfqVKAGACGTVVRNAEMKIV--DTETGASLPA--NSSGEICIRGDQIMKGYLNDlESTKRT 409
Cdd:cd05944 154 GLTEATCL--VAVNPPDGP--KRPGSVGLRLPYARVRIKvlDGVGRLLRDCapDEVGEICVAGPGVFGGYLYT-EGNKNA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 410 IDKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGG 489
Cdd:cd05944 229 FVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGA 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 778728825 490 AISEEEVKQFIAKQVvfYKRL---KRVFFVNAIPKAPSGKILRKELRA 534
Cdd:cd05944 309 VVEEEELLAWARDHV--PERAavpKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
190-536 |
6.62e-50 |
|
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: 174.44 E-value: 6.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 190 SGTTGLPKGVMLTHKGLITSVaqqmDGQNPNLYYHRNDVILCVLPFFHIYSLnSILLCGLRVGAAIMIMQKFDivALLQL 269
Cdd:cd17630 9 SGSTGTPKAVVHTAANLLASA----AGLHSRLGFGGGDSWLLSLPLYHVGGL-AILVRSLLAGAELVLLERNQ--ALAED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 270 IEKHRISIMPIVPPIFLAIAKSPeFEKYDVSSVRVLKSGGAPLGKELEDAVREK-FPTAilgQGYGMTEAGpvlsmSLAF 348
Cdd:cd17630 82 LAPPGVTHVSLVPTQLQRLLDSG-QGPAALKSLRAVLLGGAPIPPELLERAADRgIPLY---TTYGMTETA-----SQVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 349 AKEPFQVKAGACGTVVRNAEMKIVDTetgaslpanssGEICIRGDQIMKGYLNDleSTKRTIDKEGWLHTGDIGFVDDDN 428
Cdd:cd17630 153 TKRPDGFGRGGVGVLLPGRELRIVED-----------GEIWVGGASLAMGYLRG--QLVPEFNEDGWFTTKDLGELHADG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 429 ELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVmkANGGAISEEEVKQFIAKQVVFYK 508
Cdd:cd17630 220 RLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVI--VGRGPADPAELRAWLKDKLARFK 297
|
330 340
....*....|....*....|....*...
gi 778728825 509 RLKRVFFVNAIPKAPSGKILRKELRAKL 536
Cdd:cd17630 298 LPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
55-532 |
4.41e-49 |
|
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: 175.41 E-value: 4.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 55 TYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAImtaanpfYTAVEIAKQAkaanaklivtmac 134
Cdd:cd05930 14 TYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAA-------YVPLDPSYPA------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 135 fyDRVKDLAEN-GVQIVCVDfavegclhfsvlsgaDESLAPLVdfssndvvalpYSSGTTGLPKGVMLTHKGLITSVAqq 213
Cdd:cd05930 74 --ERLAYILEDsGAKLVLTD---------------PDDLAYVI-----------YTSGSTGKPKGVMVEHRGLVNLLL-- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 214 mdGQNPNLYYHRNDVILCVLPFFHIYSLNSILLCgLRVGAAIMIM---QKFDIVALLQLIEKHRISIMPIVPPIFLAIAK 290
Cdd:cd05930 124 --WMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGA-LLAGATLVVLpeeVRKDPEALADLLAEEGITVLHLTPSLLRLLLQ 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 291 SPEFEkyDVSSVRVLKSGGAPLGKELEDAVREKFPTAILGQGYGMTEAGpVLSMSLAFAKEPFQVKAGACGTVVRNAEMK 370
Cdd:cd05930 201 ELELA--ALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEAT-VDATYYRVPPDDEEDGRVPIGRPIPNTRVY 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 371 IVDtETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTI-----DKEGWLH-TGDIGFVDDDNELFIVDRLKELIKFKA 444
Cdd:cd05930 278 VLD-ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFvpnpfGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIRG 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 445 FQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPS 524
Cdd:cd05930 357 YRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPN 436
|
....*...
gi 778728825 525 GKILRKEL 532
Cdd:cd05930 437 GKVDRKAL 444
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
54-469 |
4.61e-49 |
|
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: 176.01 E-value: 4.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 54 YTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGasyrgaIMTAAnpfytaveiakqakaanaklivtma 133
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQG------IMALG------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 134 cfydrvkdlaengvqivCVDfAVEGCLhfsvlSGADE---------SLAPLVDFSSNDVVALPYSSGTTGLPKGVMLTHK 204
Cdd:cd17640 55 -----------------AVD-VVRGSD-----SSVEEllyilnhseSVALVVENDSDDLATIIYTSGTTGNPKGVMLTHA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 205 GLITSVAQQMDGQNPnlyyHRNDVILCVLPFFHIYSLNS---ILLCGlrvgaaimIMQKF-DIVALLQLIEKHRISIMPI 280
Cdd:cd17640 112 NLLHQIRSLSDIVPP----QPGDRFLSILPIWHSYERSAeyfIFACG--------CSQAYtSIRTLKDDLKRVKPHYIVS 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 281 VPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVR---------EKFPTAI---LGQGYGMTEAGPVLSmslaf 348
Cdd:cd17640 180 VPRLWESLYSGIQKQVSKSSPIKQFLFLFFLSGGIFKFGISgggalpphvDTFFEAIgieVLNGYGLTETSPVVS----- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 349 AKEPFQVKAGACGTVVRNAEMKIVDTETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLHTGDIGFVDDDN 428
Cdd:cd17640 255 ARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGG 334
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 778728825 429 ELFIVDRLKELIKFKAFQ-VAPAELEALLITHPKLSDAAVIG 469
Cdd:cd17640 335 ELVLTGRAKDTIVLSNGEnVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
50-534 |
6.17e-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: 178.66 E-value: 6.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 50 TGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLI 129
Cdd:cd05967 79 TERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 130 VTMACFY--DRV--------KDLAENGVQ----IV-------CVDFAVEGCLHFSVLSGADESLAPlVDFSSNDVVALPY 188
Cdd:cd05967 159 VTASCGIepGKVvpykplldKALELSGHKphhvLVlnrpqvpADLTKPGRDLDWSELLAKAEPVDC-VPVAATDPLYILY 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 189 SSGTTGLPKGVMLTHKGLITSVAQQMDgqnpNLY-YHRNDVilcvlpFF----------HIYSLNSILLCGLrvgAAIMI 257
Cdd:cd05967 238 TSGTTGKPKGVVRDNGGHAVALNWSMR----NIYgIKPGDV------WWaasdvgwvvgHSYIVYGPLLHGA---TTVLY 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 258 MQKFDIV----ALLQLIEKHRISIMPIVPPIFLAIAKSPE----FEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAIL 329
Cdd:cd05967 305 EGKPVGTpdpgAFWRVIEKYQVNALFTAPTAIRAIRKEDPdgkyIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVI 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 330 GQgYGMTEAG-PVLSMSLAFAKEPfqVKAGACGTVVRNAEMKIVDtETGASLPANSSGEICIRG--------------DQ 394
Cdd:cd05967 385 DH-WWQTETGwPITANPVGLEPLP--IKAGSPGKPVPGYQVQVLD-EDGEPVGPNELGNIVIKLplppgclltlwkndER 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 395 IMKGYLNDLEstkrtidkeGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVE 474
Cdd:cd05967 461 FKKLYLSKFP---------GYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDEL 531
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 778728825 475 AGEVPVAFVMKANGGAISEEEV-KQFIA---KQVVFYKRLKRVFFVNAIPKAPSGKILRKELRA 534
Cdd:cd05967 532 KGQVPLGLVVLKEGVKITAEELeKELVAlvrEQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRK 595
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
188-534 |
1.18e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 175.18 E-value: 1.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 188 YSSGTTGLPKGVMLTHKglitSVAQQMDGQNPNLYYHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKFDIVALL 267
Cdd:PRK07787 135 YTSGTTGPPKGVVLSRR----AIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPEAYA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 268 QLIEKhRISIMPIVPPIFLAIAKSPEFEKyDVSSVRVLKSGGAPLgkelEDAVREKFpTAILGQG----YGMTEAgpVLS 343
Cdd:PRK07787 211 QALSE-GGTLYFGVPTVWSRIAADPEAAR-ALRGARLLVSGSAAL----PVPVFDRL-AALTGHRpverYGMTET--LIT 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 344 MSLAFAKEPfqvKAGACGTVVRNAEMKIVDtETGASLPAN--SSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLHTGDI 421
Cdd:PRK07787 282 LSTRADGER---RPGWVGLPLAGVETRLVD-EDGGPVPHDgeTVGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDV 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 422 GFVDDDNELFIVDRLK-ELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGgaISEEEVKQFI 500
Cdd:PRK07787 358 AVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADD--VAADELIDFV 435
|
330 340 350
....*....|....*....|....*....|....
gi 778728825 501 AKQVVFYKRLKRVFFVNAIPKAPSGKILRKELRA 534
Cdd:PRK07787 436 AQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
42-533 |
2.22e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 175.20 E-value: 2.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 42 RPCLINGATGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQA 121
Cdd:PRK13390 13 RPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 122 KAANAKLIVTMACFyDRVkdLAENGVQI-VCVDFA--VEGCLHF-SVLSGADeslAPLVDFSSNDVVAlpYSSGTTGLPK 197
Cdd:PRK13390 93 GDSGARVLVASAAL-DGL--AAKVGADLpLRLSFGgeIDGFGSFeAALAGAG---PRLTEQPCGAVML--YSSGTTGFPK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 198 GVM--LTHKGL------ITSVAQQMDGQNpnlyyhRNDVILCVLPFFHIYSLNsilLCGL--RVGAAIMIMQKFDIVALL 267
Cdd:PRK13390 165 GIQpdLPGRDVdapgdpIVAIARAFYDIS------ESDIYYSSAPIYHAAPLR---WCSMvhALGGTVVLAKRFDAQATL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 268 QLIEKHRISIMPIVPPIFLAIAK--SPEFEKYDVSSVRVLKSGGAPLGKELEDAVREkFPTAILGQGYGMTEA-GPVLSM 344
Cdd:PRK13390 236 GHVERYRITVTQMVPTMFVRLLKldADVRTRYDVSSLRAVIHAAAPCPVDVKHAMID-WLGPIVYEYYSSTEAhGMTFID 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 345 SLAFAKEPFQVKAGACGTvvrnaeMKIVDTEtGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIDKEG--WLHTGDIG 422
Cdd:PRK13390 315 SPDWLAHPGSVGRSVLGD------LHICDDD-GNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 423 FVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFI-- 500
Cdd:PRK13390 388 SVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELIdy 467
|
490 500 510
....*....|....*....|....*....|....
gi 778728825 501 -AKQVVFYKRLKRVFFVNAIPKAPSGKILRKELR 533
Cdd:PRK13390 468 tRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
54-533 |
1.68e-47 |
|
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: 171.16 E-value: 1.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 54 YTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTaanPFYTAVEIAKQAKAanaklivtma 133
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQ---PLFTAFGPKAIEHR---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 134 cfydrvkdLAENGVQIVCVDFAvegclhfsvlsgadeSLAPLVDfssnDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQ 213
Cdd:cd05973 68 --------LRTSGARLVVTDAA---------------NRHKLDS----DPFVMMFTSGTTGLPKGVPVPLRALAAFGAYL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 214 MDGqnpnLYYHRNDVILCVLPFFHIYSLNSILLCGLRVG-AAIMIMQKFDIVALLQLIEKHRISIMPIVPPIF-LAIAKS 291
Cdd:cd05973 121 RDA----VDLRPEDSFWNAADPGWAYGLYYAITGPLALGhPTILLEGGFSVESTWRVIERLGVTNLAGSPTAYrLLMAAG 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 292 PEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILGQgYGMTEAGPVLSMSLAFAKEpfqVKAGACGTVVRNAEMKI 371
Cdd:cd05973 197 AEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDH-YGQTELGMVLANHHALEHP---VHAGSAGRAMPGWRVAV 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 372 VDtETGASLPANSSGEICI--RGDQIM--KGYLNDLESTkrtIDKeGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQV 447
Cdd:cd05973 273 LD-DDGDELGPGEPGRLAIdiANSPLMwfRGYQLPDTPA---IDG-GYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRI 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 448 APAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEE---EVKQFIAKQVVFYKRLKRVFFVNAIPKAPS 524
Cdd:cd05973 348 GPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPAladELQLHVKKRLSAHAYPRTIHFVDELPKTPS 427
|
....*....
gi 778728825 525 GKILRKELR 533
Cdd:cd05973 428 GKIQRFLLR 436
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
54-535 |
4.81e-47 |
|
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: 172.29 E-value: 4.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 54 YTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIVTMA 133
Cdd:cd05970 48 FTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 134 --CFYDRVKDLAEN----GVQIVCVDFAVEGCLHF-SVLSGADESLAPLVDFSS--NDVVALPY-SSGTTGLPKgvMLTH 203
Cdd:cd05970 128 edNIPEEIEKAAPEcpskPKLVWVGDPVPEGWIDFrKLIKNASPDFERPTANSYpcGEDILLVYfSSGTTGMPK--MVEH 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 204 K-----GLITSVAQQMDGQNPNLYYHRNDVILCVLPFFHIYSLnsiLLCGlrvgAAIMI--MQKFDIVALLQLIEKHRIS 276
Cdd:cd05970 206 DftyplGHIVTAKYWQNVREGGLHLTVADTGWGKAVWGKIYGQ---WIAG----AAVFVydYDKFDPKALLEKLSKYGVT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 277 IMPIVPPIFLAIAKSpEFEKYDVSSVRVLKSGGAPLGKELEDAVREKfpTAI-LGQGYGMTEagpvlsMSLAFAKEP-FQ 354
Cdd:cd05970 279 TFCAPPTIYRFLIRE-DLSRYDLSSLRYCTTAGEALNPEVFNTFKEK--TGIkLMEGFGQTE------TTLTIATFPwME 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 355 VKAGACGTVVRNAEMKIVDTEtGASLPANSSGEICIRGDQ-----IMKGYLNDLESTKRTIdKEGWLHTGDIGFVDDDNE 429
Cdd:cd05970 350 PKPGSMGKPAPGYEIDLIDRE-GRSCEAGEEGEIVIRTSKgkpvgLFGGYYKDAEKTAEVW-HDGYYHTGDAAWMDEDGY 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 430 LFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEE---EVKQFIAKQVVF 506
Cdd:cd05970 428 LWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEElkkELQDHVKKVTAP 507
|
490 500
....*....|....*....|....*....
gi 778728825 507 YKRLKRVFFVNAIPKAPSGKILRKELRAK 535
Cdd:cd05970 508 YKYPRIVEFVDELPKTISGKIRRVEIRER 536
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
53-533 |
8.81e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 170.35 E-value: 8.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 53 VYTYHDVQLTARRVAAGLHNLGiKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIVTM 132
Cdd:PRK07638 26 VLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 133 ACFydrVKDLAENGVQIVCVDFAVEgclhfsVLSGADESLAPLVDfSSNDVVALPYSSGTTGLPKGVMLTHKGLITSVAq 212
Cdd:PRK07638 105 RYK---LNDLPDEEGRVIEIDEWKR------MIEKYLPTYAPIEN-VQNAPFYMGFTSGSTGKPKAFLRAQQSWLHSFD- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 213 qmdgqnpnlyyhrndvilCVLPFFHIYSLNSILLCG--------------LRVGAAIMIMQKFDIVALLQLIEKHRISIM 278
Cdd:PRK07638 174 ------------------CNVHDFHMKREDSVLIAGtlvhslflygaistLYVGQTVHLMRKFIPNQVLDKLETENISVM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 279 PIVPPIFLAIAKSPEFEKydvSSVRVLKSGgAPLGKELEDAVREKFPTAILGQGYGMTEagpvLSMSLAFAKEPFQVKAG 358
Cdd:PRK07638 236 YTVPTMLESLYKENRVIE---NKMKIISSG-AKWEAEAKEKIKNIFPYAKLYEFYGASE----LSFVTALVDEESERRPN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 359 ACGTVVRNAEMKIVDtETGASLPANSSGEICIRGDQIMKGYLNDLESTkRTIDKEGWLHTGDIGFVDDDNELFIVDRLKE 438
Cdd:PRK07638 308 SVGRPFHNVQVRICN-EAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLA-RELNADGWMTVRDVGYEDEEGFIYIVGREKN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 439 LIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMkangGAISEEEVKQFIAKQVVFYKRLKRVFFVNA 518
Cdd:PRK07638 386 MILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIK----GSATKQQLKSFCLQRLSSFKIPKEWHFVDE 461
|
490
....*....|....*
gi 778728825 519 IPKAPSGKILRKELR 533
Cdd:PRK07638 462 IPYTNSGKIARMEAK 476
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
42-535 |
2.71e-46 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 169.94 E-value: 2.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 42 RPCLINGATGDVYTYHDVQLTArrVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQA 121
Cdd:PRK13382 59 RPGLIDELGTLTWRELDERSDA--LAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 122 KAANAKLIVTMACFYDRV-KDLAENGVQIVCVDFA-VEGCLHFSVLSGADESLAPLVDFSSNDVVALpySSGTTGLPKGV 199
Cdd:PRK13382 137 TREGVDTVIYDEEFSATVdRALADCPQATRIVAWTdEDHDLTVEVLIAAHAGQRPEPTGRKGRVILL--TSGTTGTPKGA 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 200 MLTHKGLITSVAQQMDgQNPnLYYHRNDVIlcVLPFFHIYSLNSILLCGLRvgAAIMIMQ-KFDIVALLQLIEKHRISIM 278
Cdd:PRK13382 215 RRSGPGGIGTLKAILD-RTP-WRAEEPTVI--VAPMFHAWGFSQLVLAASL--ACTIVTRrRFDPEATLDLIDRHRATGL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 279 PIVPPIFLAIAKSPE--FEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILGQgYGMTEAGpvlsMSLAFAKEPFQVK 356
Cdd:PRK13382 289 AVVPVMFDRIMDLPAevRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNN-YNATEAG----MIATATPADLRAA 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 357 AGACGTVVRNAEMKIVDTEtGASLPANSSGEICIRGDQIMKGYLNDleSTKRTIDkeGWLHTGDIGFVDDDNELFIVDRL 436
Cdd:PRK13382 364 PDTAGRPAEGTEIRILDQD-FREVPTGEVGTIFVRNDTQFDGYTSG--STKDFHD--GFMASGDVGYLDENGRLFVVGRD 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 437 KELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVFYKRLKRVFFV 516
Cdd:PRK13382 439 DEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVL 518
|
490
....*....|....*....
gi 778728825 517 NAIPKAPSGKILRKELRAK 535
Cdd:PRK13382 519 DELPRGATGKILRRELQAR 537
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
188-529 |
4.30e-46 |
|
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: 164.12 E-value: 4.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 188 YSSGTTGLPKGVMLTHKGLITSvaqqMDGQNPNLYYHRNDVILCVLPFFHIYSLNSILLcGLRVGAAIMIMQKFDIVALL 267
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIES----FVCNEDLFNISGEDAILAPGPLSHSLFLYGAIS-ALYLGGTFIGQRKFNPKSWI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 268 QLIEKHRISIMPIVPPIFLAIAKspefEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILGQGYGMTEAGPVlsmSLA 347
Cdd:cd17633 82 RKINQYNATVIYLVPTMLQALAR----TLEPESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFI---TYN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 348 FAKEpfQVKAGACGTVVRNAEMKIVDTETGASlpanssGEICIRGDQIMKGYLNDLESTKrtidkEGWLHTGDIGFVDDD 427
Cdd:cd17633 155 FNQE--SRPPNSVGRPFPNVEIEIRNADGGEI------GKIFVKSEMVFSGYVRGGFSNP-----DGWMSVGDIGYVDEE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 428 NELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMkanGGAISEEEVKQFIAKQVVFY 507
Cdd:cd17633 222 GYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS---GDKLTYKQLKRFLKQKLSRY 298
|
330 340
....*....|....*....|..
gi 778728825 508 KRLKRVFFVNAIPKAPSGKILR 529
Cdd:cd17633 299 EIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
42-526 |
4.49e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 169.30 E-value: 4.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 42 RPCLINGATgdVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQA 121
Cdd:PRK07798 19 RVALVCGDR--RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 122 KAANAKLIVTMACFYDRVKDLAEN--GVQIVCVdfaVEGCLHFSVLSGA---DESLA---PLVDF--SSNDVVALPYSSG 191
Cdd:PRK07798 97 DDSDAVALVYEREFAPRVAEVLPRlpKLRTLVV---VEDGSGNDLLPGAvdyEDALAagsPERDFgeRSPDDLYLLYTGG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 192 TTGLPKGVMLTHKGLITSvaqQMDGQNP-------NLYYHRNDV-------ILCVLPFFHIYSLNSI---LLCGLRVgaA 254
Cdd:PRK07798 174 TTGMPKGVMWRQEDIFRV---LLGGRDFatgepieDEEELAKRAaagpgmrRFPAPPLMHGAGQWAAfaaLFSGQTV--V 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 255 IMIMQKFDIVALLQLIEKHRISIMPIV-----PPIFLAIAKSpefEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAIL 329
Cdd:PRK07798 249 LLPDVRFDADEVWRTIEREKVNVITIVgdamaRPLLDALEAR---GPYDLSSLFAIASGGALFSPSVKEALLELLPNVVL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 330 GQGYGMTEAGpvlSMSLAFAKePFQVKAGAcGTVVRNAEMKIVDTETGASLPanSSGEICI--RGDQIMKGYLNDLESTK 407
Cdd:PRK07798 326 TDSIGSSETG---FGGSGTVA-KGAVHTGG-PRFTIGPRTVVLDEDGNPVEP--GSGEIGWiaRRGHIPLGYYKDPEKTA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 408 RT---IDKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVM 484
Cdd:PRK07798 399 ETfptIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQ 478
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 778728825 485 KANGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGK 526
Cdd:PRK07798 479 LREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
54-457 |
2.59e-45 |
|
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: 167.39 E-value: 2.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 54 YTYHDVQLTARRVAAGLHNLGIK--KGDVVMNLLPNSPEFVFTFLGASYRGAIMTaanPFY-----TAVEiakqakaana 126
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTV---PLYdtlgpEAIE---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 127 kLIVtmacfydrvkDLAEngVQIVCVDFAVEGCLHFSVLSGADESLAPLVDFSSNDVVALPYSSGTTGLPKGVMLTHKGL 206
Cdd:cd05927 73 -YIL----------NHAE--ISIVFCDAGVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 207 ITSVAQQMDGQNPNLYYHRNDVILCVLPFFHIYSLNSILLCgLRVGAAIMIMQKfDIVALLQLIEKHRISIMPIVP---- 282
Cdd:cd05927 140 VSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALF-LYHGAKIGFYSG-DIRLLLDDIKALKPTVFPGVPrvln 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 283 ----PIFLAIAKSP----------------EFEKYDVSS-------------------VRVLKSGGAPLGKELEDAVREK 323
Cdd:cd05927 218 riydKIFNKVQAKGplkrklfnfalnyklaELRSGVVRAspfwdklvfnkikqalggnVRLMLTGSAPLSPEVLEFLRVA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 324 FPTAILgQGYGMTE--AGPVLSMslafakePFQVKAGACGTVVRNAEMKIVDT-ETG-ASLPANSSGEICIRGDQIMKGY 399
Cdd:cd05927 298 LGCPVL-EGYGQTEctAGATLTL-------PGDTSVGHVGGPLPCAEVKLVDVpEMNyDAKDPNPRGEVCIRGPNVFSGY 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 778728825 400 LNDLESTKRTIDKEGWLHTGDIGFVDDDNELFIVDRLKELikFKAFQ---VAPAELEALLI 457
Cdd:cd05927 370 YKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNI--FKLSQgeyVAPEKIENIYA 428
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
55-533 |
1.13e-43 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 163.00 E-value: 1.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 55 TYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIVTMAC 134
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 135 FYDRVKDLAEN--GVQ--IVCVDFA------VEGCLHF-SVLSGADESLApLVDFSSNDVVALPYSSGTTGLPKGVMLTH 203
Cdd:PRK06018 121 FVPILEKIADKlpSVEryVVLTDAAhmpqttLKNAVAYeEWIAEADGDFA-WKTFDENTAAGMCYTSGTTGDPKGVLYSH 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 204 KgliTSVAQQMDGQNPN-LYYHRNDVILCVLPFFHIYSLnSILLCGLRVGAAI-MIMQKFDIVALLQLIEKHRISIMPIV 281
Cdd:PRK06018 200 R---SNVLHALMANNGDaLGTSAADTMLPVVPLFHANSW-GIAFSAPSMGTKLvMPGAKLDGASVYELLDTEKVTFTAGV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 282 PPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAIlgQGYGMTEAGPVlsMSLAFAKEPFQVKAGACG 361
Cdd:PRK06018 276 PTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDMGVEVR--HAWGMTEMSPL--GTLAALKPPFSKLPGDAR 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 362 TVVR--------NAEMKIVDTEtGASLP--ANSSGEICIRGDQIMKGYLndlESTKRTIDKEGWLHTGDIGFVDDDNELF 431
Cdd:PRK06018 352 LDVLqkqgyppfGVEMKITDDA-GKELPwdGKTFGRLKVRGPAVAAAYY---RVDGEILDDDGFFDTGDVATIDAYGYMR 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 432 IVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVFYKRLK 511
Cdd:PRK06018 428 ITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEILKYMDGKIAKWWMPD 507
|
490 500
....*....|....*....|..
gi 778728825 512 RVFFVNAIPKAPSGKILRKELR 533
Cdd:PRK06018 508 DVAFVDAIPHTATGKILKTALR 529
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
24-533 |
1.48e-43 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 163.27 E-value: 1.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 24 NHLPLHDYVFQNLSK--FASRPCLINGATGdvYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYR 101
Cdd:PLN03102 10 NNVPLTPITFLKRASecYPNRTSIIYGKTR--FTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 102 GAIMTAANPFYTAVEIAKQAKAANAKLIvtmacFYDR-VKDLAENGVQIVCVDfavEGCLHFSVL--SGADESLAPL--- 175
Cdd:PLN03102 88 GAVLNPINTRLDATSIAAILRHAKPKIL-----FVDRsFEPLAREVLHLLSSE---DSNLNLPVIfiHEIDFPKRPSsee 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 176 VDF---------------------SSNDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQMDGQNPNLYyhrnDVILCVLP 234
Cdd:PLN03102 160 LDYecliqrgeptpslvarmfriqDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTC----PVYLWTLP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 235 FFHIYSLNSILLCGLRVGAAImIMQKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSS-VRVLKSGGAPLG 313
Cdd:PLN03102 236 MFHCNGWTFTWGTAARGGTSV-CMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGpVHVLTGGSPPPA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 314 KELEDAVREKFPTAilgQGYGMTEA-GPVL--SMSLAFAKEP----FQVKAGACGTVVRNAEMKIVDTETGASLP--ANS 384
Cdd:PLN03102 315 ALVKKVQRLGFQVM---HAYGLTEAtGPVLfcEWQDEWNRLPenqqMELKARQGVSILGLADVDVKNKETQESVPrdGKT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 385 SGEICIRGDQIMKGYLNDLESTKRTIdKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSD 464
Cdd:PLN03102 392 MGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLE 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 778728825 465 AAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQ--VVFYKRL--------KRVFFVNAIPKAPSGKILRKELR 533
Cdd:PLN03102 471 TAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKLVTRErdLIEYCREnlphfmcpRKVVFLQELPKNGNGKILKPKLR 549
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
50-539 |
3.05e-43 |
|
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: 161.68 E-value: 3.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 50 TGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAI--MTAANPFYTAVE-----IAKQAK 122
Cdd:cd05906 36 SEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVpaPLTVPPTYDEPNarlrkLRHIWQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 123 AANAKLIVT---MACFYDRVKDLAENGVQIVCVDFAVEGClhfsvlsgadESLAPLVDFSSNDVVALPYSSGTTGLPKGV 199
Cdd:cd05906 116 LLGSPVVLTdaeLVAEFAGLETLSGLPGIRVLSIEELLDT----------AADHDLPQSRPDDLALLMLTSGSTGFPKAV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 200 MLTHKGLITSVAqqmdGQNPNLYYHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKFDIVA----LLQLIEKHRI 275
Cdd:cd05906 186 PLTHRNILARSA----GKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVHVPTEEILAdplrWLDLIDRYRV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 276 SIMpIVPPIFLAI----AKSPEFEKYDVSSVRVLKSGGAP--------LGKELEdavREKFPTAILGQGYGMTEAGPVLS 343
Cdd:cd05906 262 TIT-WAPNFAFALlndlLEEIEDGTWDLSSLRYLVNAGEAvvaktirrLLRLLE---PYGLPPDAIRPAFGMTETCSGVI 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 344 MSLAFAKEPFQ--VKAGACGTVVRNAEMKIVDtETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLHTGDI 421
Cdd:cd05906 338 YSRSFPTYDHSqaLEFVSLGRPIPGVSMRIVD-DEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDL 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 422 GFVDDDNeLFIVDRLKELIKFKAFQVAPAELEALL----ITHPKLSDAAVIGMPDVEAGEVPVAFV-MKANGGAISE--E 494
Cdd:cd05906 417 GFLDNGN-LTITGRTKDTIIVNGVNYYSHEIEAAVeevpGVEPSFTAAFAVRDPGAETEELAIFFVpEYDLQDALSEtlR 495
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 778728825 495 EVKQFIAKQVVFykRLKRVFFV--NAIPKAPSGKILRKELRAKLASG 539
Cdd:cd05906 496 AIRSVVSREVGV--SPAYLIPLpkEEIPKTSLGKIQRSKLKAAFEAG 540
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
42-534 |
4.88e-43 |
|
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: 162.27 E-value: 4.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 42 RPCLI-NGATGDV--YTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIA 118
Cdd:cd05968 77 RPALRwEGEDGTSrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 119 KQAKAANAKLIVTMACFY--DRVKDLAENGVQIVCVDFAVEgclHFSVL--SGADESLAPLVDFSSNDVVALP------- 187
Cdd:cd05968 157 TRLQDAEAKALITADGFTrrGREVNLKEEADKACAQCPTVE---KVVVVrhLGNDFTPAKGRDLSYDEEKETAgdgaert 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 188 ---------YSSGTTGLPKGVMLTHKGLITSVAQ----QMDGQNPNLYYHRNDVILCVLPFfhiyslnsILLCGLRVGAA 254
Cdd:cd05968 234 esedplmiiYTSGTTGKPKGTVHVHAGFPLKAAQdmyfQFDLKPGDLLTWFTDLGWMMGPW--------LIFGGLILGAT 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 255 IMIMQKF----DIVALLQLIEKHRISIMPIVPPIFLAIAKSPE--FEKYDVSSVRVLKSGGAPLGKE-----LEDAVREK 323
Cdd:cd05968 306 MVLYDGApdhpKADRLWRMVEDHEITHLGLSPTLIRALKPRGDapVNAHDLSSLRVLGSTGEPWNPEpwnwlFETVGKGR 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 324 FPtaILGQGYGMTEAGPVLSMSLAfakEPfqVKAGACGTVVRNAEMKIVDtETGASLPaNSSGEICIRGDQI--MKGYLN 401
Cdd:cd05968 386 NP--IINYSGGTEISGGILGNVLI---KP--IKPSSFNGPVPGMKADVLD-ESGKPAR-PEVGELVLLAPWPgmTRGFWR 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 402 D----LESTKRTIDKEgWLHtGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGE 477
Cdd:cd05968 457 DedryLETYWSRFDNV-WVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGE 534
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 478 VPVAFVMKANG---GAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELRA 534
Cdd:cd05968 535 AIVCFVVLKPGvtpTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRA 594
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
55-484 |
5.44e-43 |
|
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: 160.07 E-value: 5.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 55 TYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAImtaanpfytaveiakqakaanaklIVTMac 134
Cdd:cd17639 7 SYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIP------------------------IVTV-- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 135 fYDrvkDLAENGVQivcvdfaveGCLHFSvlsgadESLAPLVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQM 214
Cdd:cd17639 61 -YA---TLGEDALI---------HSLNET------ECSAIFTDGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLG 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 215 DGQNPNLyyHRNDVILCVLPFFHIYSL---NSILLCGLRVG--------AAIMIMQKFDIVALlqliekhRISIMPIVPP 283
Cdd:cd17639 122 DRVPELL--GPDDRYLAYLPLAHIFELaaeNVCLYRGGTIGygsprtltDKSKRGCKGDLTEF-------KPTLMVGVPA 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 284 IFLAIAK--------SPEFEK------YDVSS---------------------------VRVLKSGGAPLGKEledavRE 322
Cdd:cd17639 193 IWDTIRKgvlaklnpMGGLKRtlfwtaYQSKLkalkegpgtplldelvfkkvraalggrLRYMLSGGAPLSAD-----TQ 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 323 KFPTAILG---QGYGMTE---AGPVLsmslafakEPFQVKAGACGTVVRNAEMKIVDTETGASLPANSS--GEICIRGDQ 394
Cdd:cd17639 268 EFLNIVLCpviQGYGLTEtcaGGTVQ--------DPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDKPPprGEILIRGPN 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 395 IMKGYLNDLESTKRTIDKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQ-VAPAELEALLITHPKLSDAAVIGMPDv 473
Cdd:cd17639 340 VFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEyIALEKLESIYRSNPLVNNICVYADPD- 418
|
490
....*....|.
gi 778728825 474 eaGEVPVAFVM 484
Cdd:cd17639 419 --KSYPVAIVV 427
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
183-525 |
2.49e-42 |
|
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: 154.38 E-value: 2.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 183 VVALpYSSGTTGLPKGVMLTHKGLITSVAQQMDGQNPNlyyhRNDVILCVLPFFHIYSLNSiLLCGLRVGAAIMIMQKFD 262
Cdd:cd17636 3 VLAI-YTAAFSGRPNGALLSHQALLAQALVLAVLQAID----EGTVFLNSGPLFHIGTLMF-TLATFHAGGTNVFVRRVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 263 IVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVR--VLKSGGAPLGKELEDAVREKFPtailgqGYGMTEAGP 340
Cdd:cd17636 77 AEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRssPAAPEWNDMATVDTSPWGRKPG------GYGQTEVMG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 341 VLSMSlAFAKEpfqvKAGACGTVVRNAEMKIVDTEtGASLPANSSGEICIRGDQIMKGYLN-DLESTKRTIDkeGWLHTG 419
Cdd:cd17636 151 LATFA-ALGGG----AIGGAGRPSPLVQVRILDED-GREVPDGEVGEIVARGPTVMAGYWNrPEVNARRTRG--GWHHTN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 420 DIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQF 499
Cdd:cd17636 223 DLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEH 302
|
330 340
....*....|....*....|....*.
gi 778728825 500 IAKQVVFYKRLKRVFFVNAIPKAPSG 525
Cdd:cd17636 303 CRARIASYKKPKSVEFADALPRTAGG 328
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
54-528 |
1.06e-41 |
|
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: 158.12 E-value: 1.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 54 YTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIVTMA 133
Cdd:cd17634 85 ISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITAD 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 134 CFYD--RVKDLAENgvqivcVDFAVEGCL----HFSVL--SGADESLAPLVDFSSNDVVA------------------LP 187
Cdd:cd17634 165 GGVRagRSVPLKKN------VDDALNPNVtsveHVIVLkrTGSDIDWQEGRDLWWRDLIAkaspehqpeamnaedplfIL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 188 YSSGTTGLPKGVMLTHKGLITSVAQQMdgqnPNLY-YHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKF----D 262
Cdd:cd17634 239 YTSGTTGKPKGVLHTTGGYLVYAATTM----KYVFdYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVpnwpT 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 263 IVALLQLIEKHRISIMPIVPPIFLAIAKSPE--FEKYDVSSVRVLKSGGAPLGKE-----LEDAVREKFPTAilgQGYGM 335
Cdd:cd17634 315 PARMWQVVDKHGVNILYTAPTAIRALMAAGDdaIEGTDRSSLRILGSVGEPINPEayewyWKKIGKEKCPVV---DTWWQ 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 336 TEAGPVLSMSLAFAKEpfqVKAGACGTVVRNAEMKIVDTEtGASLPANSSGEICIrGDQI---MKGYLND----LESTKR 408
Cdd:cd17634 392 TETGGFMITPLPGAIE---LKAGSATRPVFGVQPAVVDNE-GHPQPGGTEGNLVI-TDPWpgqTRTLFGDherfEQTYFS 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 409 TIDkeGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANG 488
Cdd:cd17634 467 TFK--GMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHG 544
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 778728825 489 GAISEE---EVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKIL 528
Cdd:cd17634 545 VEPSPElyaELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
50-532 |
2.98e-41 |
|
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: 154.33 E-value: 2.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 50 TGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAkqakaanakli 129
Cdd:cd05945 13 GGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIR----------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 130 vtmacfydRVKDLAENGVQIVCVDfavegclhfsvlsgadeslaplvdfssnDVVALPYSSGTTGLPKGVMLTHKGLITS 209
Cdd:cd05945 82 --------EILDAAKPALLIADGD----------------------------DNAYIIFTSGSTGRPKGVQISHDNLVSF 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 210 VAQqMDGQNPnlyYHRNDVILCVLPFFHIYSLNSILlCGLRVGAAIMIM---QKFDIVALLQLIEKHRISIMPIVPPiFL 286
Cdd:cd05945 126 TNW-MLSDFP---LGPGDVFLNQAPFSFDLSVMDLY-PALASGATLVPVprdATADPKQLFRFLAEHGITVWVSTPS-FA 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 287 AIA-KSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILGQGYGMTEAgPVLSMSLAFAKEPF-QVKAGACGTVV 364
Cdd:cd05945 200 AMClLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEA-TVAVTYIEVTPEVLdGYDRLPIGYAK 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 365 RNAEMKIVDtETGASLPANSSGEICIRGDQIMKGYLNDLESTKR---TIDKEGWLHTGDIGFVDDDNELFIVDRLKELIK 441
Cdd:cd05945 279 PGAKLVILD-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAaffPDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVK 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 442 FKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFV-MKANGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIP 520
Cdd:cd05945 358 LNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVvPKPGAEAGLTKAIKAELAERLPPYMIPRRFVYLDELP 437
|
490
....*....|..
gi 778728825 521 KAPSGKILRKEL 532
Cdd:cd05945 438 LNANGKIDRKAL 449
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
54-534 |
5.60e-41 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 155.82 E-value: 5.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 54 YTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMT------AANPFYTAVEIAKQAKaanak 127
Cdd:PRK04319 74 YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGplfeafMEEAVRDRLEDSEAKV----- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 128 LIVTMACFYDRVKDLAENGVQIVCVDFAVE---GCLHF-SVLSGADESLaPLVDFSSNDVVALPYSSGTTGLPKGVMLTH 203
Cdd:PRK04319 149 LITTPALLERKPADDLPSLKHVLLVGEDVEegpGTLDFnALMEQASDEF-DIEWTDREDGAILHYTSGSTGKPKGVLHVH 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 204 KGLIT---SVAQQMDgqnpnlyYHRNDVILC--------------VLPFFHiyslnsillcglrvGAAIMIMQ-KFDIVA 265
Cdd:PRK04319 228 NAMLQhyqTGKYVLD-------LHEDDVYWCtadpgwvtgtsygiFAPWLN--------------GATNVIDGgRFSPER 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 266 LLQLIEKHRISIMPIVPPIF--LAIAKSPEFEKYDVSSVRVLKSGGAPLGKEledAVR---EKFPTAILgQGYGMTEAGP 340
Cdd:PRK04319 287 WYRILEDYKVTVWYTAPTAIrmLMGAGDDLVKKYDLSSLRHILSVGEPLNPE---VVRwgmKVFGLPIH-DNWWMTETGG 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 341 VLsmslaFAKEP-FQVKAGACGTVVRNAEMKIVDtETGASLPANSSGEICIRGD--QIMKGYLNDLESTKRTIdKEGWLH 417
Cdd:PRK04319 363 IM-----IANYPaMDIKPGSMGKPLPGIEAAIVD-DQGNELPPNRMGNLAIKKGwpSMMRGIWNNPEKYESYF-AGDWYV 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 418 TGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEE--- 494
Cdd:PRK04319 436 SGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEElke 515
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 778728825 495 EVKQFiAKqvvfyKRL------KRVFFVNAIPKAPSGKILRKELRA 534
Cdd:PRK04319 516 EIRGF-VK-----KGLgahaapREIEFKDKLPKTRSGKIMRRVLKA 555
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
180-526 |
3.09e-39 |
|
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: 146.76 E-value: 3.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 180 SNDVVALPYSSGTTGLPKGVMLTH-------KG--LITSVAQQMD-------GQNPNLyyhrndVILCVLPFFHIYSLNS 243
Cdd:cd05924 2 SADDLYILYTGGTTGMPKGVMWRQedifrmlMGgaDFGTGEFTPSedahkaaAAAAGT------VMFPAPPLMHGTGSWT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 244 ---ILLCGLRVgaaIMIMQKFDIVALLQLIEKHRISIMPIVPPiflAIAKsP---EFEK---YDVSSVRVLKSGGAPLGK 314
Cdd:cd05924 76 afgGLLGGQTV---VLPDDRFDPEEVWRTIEKHKVTSMTIVGD---AMAR-PlidALRDagpYDLSSLFAISSGGALLSP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 315 ELEDAVREKFPTAILGQGYGMTEAGpvlSMSLAFAKEpfqvKAGACGTVVRNAEMKIVDTETGASLPANSSGEICI-RGD 393
Cdd:cd05924 149 EVKQGLLELVPNITLVDAFGSSETG---FTGSGHSAG----SGPETGPFTRANPDTVVLDDDGRVVPPGSGGVGWIaRRG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 394 QIMKGYLNDLESTKRT---IDKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGM 470
Cdd:cd05924 222 HIPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGR 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 778728825 471 PDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGK 526
Cdd:cd05924 302 PDERWGQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
41-535 |
1.06e-38 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 149.22 E-value: 1.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 41 SRPCLINGATGdvYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQ 120
Cdd:PLN02479 35 TRKSVVHGSVR--YTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 121 AKAANAKLIVTMACFY----DRVKDLAENG-------VQIVCVDFAVE-GCLHFSVLSGADE------------SLAPLV 176
Cdd:PLN02479 113 LEHSKSEVVMVDQEFFtlaeEALKILAEKKkssfkppLLIVIGDPTCDpKSLQYALGKGAIEyekfletgdpefAWKPPA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 177 DfsSNDVVALPYSSGTTGLPKGVMLTHKGlitsvAQQMDGQNPnLYYHRND--VILCVLPFFHI----YSLNSILLCGLR 250
Cdd:PLN02479 193 D--EWQSIALGYTSGTTASPKGVVLHHRG-----AYLMALSNA-LIWGMNEgaVYLWTLPMFHCngwcFTWTLAALCGTN 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 251 VgaaimIMQKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSS--VRVLKSGGAPLGKELEDAVREKFPTAi 328
Cdd:PLN02479 265 I-----CLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETILPLPrvVHVMTAGAAPPPSVLFAMSEKGFRVT- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 329 lgQGYGMTEA-GPvlSMSLAFAKE----PFQVKAGA-CGTVVRNAEMK---IVDTETGASLPAN--SSGEICIRGDQIMK 397
Cdd:PLN02479 339 --HTYGLSETyGP--STVCAWKPEwdslPPEEQARLnARQGVRYIGLEgldVVDTKTMKPVPADgkTMGEIVMRGNMVMK 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 398 GYLNDLESTKRTIdKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGE 477
Cdd:PLN02479 415 GYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGE 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 778728825 478 VPVAFVMKANGGAISEE-----EVKQFIAKQVVFYKRLKRVFFvNAIPKAPSGKILRKELRAK 535
Cdd:PLN02479 494 SPCAFVTLKPGVDKSDEaalaeDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRAK 555
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
43-540 |
2.06e-38 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 148.11 E-value: 2.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 43 PCLINGATGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAK 122
Cdd:PRK05852 33 PALVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 123 AANAKLIV------------TMACFYDRVK----DLAENGVQIVCVDFAVEgclhFSVLSGADESLAPlvdfssnDVVAL 186
Cdd:PRK05852 113 AAGARVVLidadgphdraepTTRWWPLTVNvggdSGPSGGTLSVHLDAATE----PTPATSTPEGLRP-------DDAMI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 187 PYSSGTTGLPKGVMLTHKGLITSV-----AQQMDGQnpnlyyhrnDVILCVLPFFHIYSLNSILLCGLRVGAAIMI--MQ 259
Cdd:PRK05852 182 MFTGGTTGLPKMVPWTHANIASSVraiitGYRLSPR---------DATVAVMPLYHGHGLIAALLATLASGGAVLLpaRG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 260 KF-------DIVAllqlIEKHRISIMPIVPPIFLAIAKSpEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILgQG 332
Cdd:PRK05852 253 RFsahtfwdDIKA----VGATWYTAVPTIHQILLERAAT-EPSGRKPAALRFIRSCSAPLTAETAQALQTEFAAPVV-CA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 333 YGMTEAGPVLSMSLAFAKEPFQVKAGACGTVVRN--AEMKIVDTEtGASLPANSSGEICIRGDQIMKGYLNDLESTKRTI 410
Cdd:PRK05852 327 FGMTEATHQVTTTQIEGIGQTENPVVSTGLVGRStgAQIRIVGSD-GLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANF 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 411 dKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGA 490
Cdd:PRK05852 406 -TDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAP 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 778728825 491 ISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELRAKLASGA 540
Cdd:PRK05852 485 PTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQFGHSV 534
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
55-467 |
2.26e-38 |
|
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: 145.49 E-value: 2.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 55 TYHdvQLTAR--RVAAGLHNL-GIKKGDVVMNLLPNSPEFVFTFL-----GASY-----------RGAIMTAANPfytav 115
Cdd:TIGR01733 1 TYR--ELDERanRLARHLRAAgGVGPGDRVAVLLERSAELVVAILavlkaGAAYvpldpaypaerLAFILEDAGA----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 116 eiakqakaanaKLIVTMACFYDRvkdLAENGVQIVCVDFAVEgclhfsvLSGADESLAPLVD--FSSNDVVALPYSSGTT 193
Cdd:TIGR01733 74 -----------RLLLTDSALASR---LAGLVLPVILLDPLEL-------AALDDAPAPPPPDapSGPDDLAYVIYTSGST 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 194 GLPKGVMLTHKGLITSVAqqmdGQNPNLYYHRNDVILCVLPFFHIYSLNSILLCgLRVGAAIMI----MQKFDIVALLQL 269
Cdd:TIGR01733 133 GRPKGVVVTHRSLVNLLA----WLARRYGLDPDDRVLQFASLSFDASVEEIFGA-LLAGATLVVppedEERDDAALLAAL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 270 IEKHRISIMPIVPPIFLAIAKSPEFekyDVSSVRVLKSGGAPLGKELEDAVREKFPTAILGQGYGMTEAGPVLSMSLAFA 349
Cdd:TIGR01733 208 IAEHPVTVLNLTPSLLALLAAALPP---ALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 350 KEPFQVKAGACGTVVRNAEMKIVDtETGASLPANSSGEICIRGDQIMKGYLNDLESTK--------RTIDKEGWLHTGDI 421
Cdd:TIGR01733 285 DDAPRESPVPIGRPLANTRLYVLD-DDLRPVPVGVVGELYIGGPGVARGYLNRPELTAerfvpdpfAGGDGARLYRTGDL 363
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 778728825 422 GFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAV 467
Cdd:TIGR01733 364 VRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
34-539 |
2.47e-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: 148.48 E-value: 2.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 34 QNLSKFASRPCLI----NGATGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAAN 109
Cdd:cd05966 61 RHLKERGDKVAIIwegdEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 110 PFYTAVEIAKQAKAANAKLIVTMACFYDRVK--DLAENgvqivcVDFAVEGClhFSV-------LSGADESLAPLVDFSS 180
Cdd:cd05966 141 AGFSAESLADRINDAQCKLVITADGGYRGGKviPLKEI------VDEALEKC--PSVekvlvvkRTGGEVPMTEGRDLWW 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 181 NDVVALP------------------YSSGTTGLPKGVMLTHKGLITSVAQQMDgqnpnlY---YHRNDVilcvlpFF--- 236
Cdd:cd05966 213 HDLMAKQspecepewmdsedplfilYTSGSTGKPKGVVHTTGGYLLYAATTFK------YvfdYHPDDI------YWcta 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 237 -------HIYSLNSILLCGlrvgaAIMIMqkFDIVA-------LLQLIEKHRISIMPIVP-PIFLAIAKSPEF-EKYDVS 300
Cdd:cd05966 281 digwitgHSYIVYGPLANG-----ATTVM--FEGTPtypdpgrYWDIVEKHKVTIFYTAPtAIRALMKFGDEWvKKHDLS 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 301 SVRVLKSGGAPLGKELEDAVREKfptaiLGQG-------YGMTEAGPVLSMSLAFAkepFQVKAGACGTVVRNAEMKIVD 373
Cdd:cd05966 354 SLRVLGSVGEPINPEAWMWYYEV-----IGKErcpivdtWWQTETGGIMITPLPGA---TPLKPGSATRPFFGIEPAILD 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 374 tETGASLPANSSGEICIR----GdqIMKGYLNDLESTKRTIDKE--GWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQV 447
Cdd:cd05966 426 -EEGNEVEGEVEGYLVIKrpwpG--MARTIYGDHERYEDTYFSKfpGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRL 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 448 APAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEE---EVKQFIAKQVVFYKRLKRVFFVNAIPKAPS 524
Cdd:cd05966 503 GTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDElrkELRKHVRKEIGPIATPDKIQFVPGLPKTRS 582
|
570
....*....|....*
gi 778728825 525 GKILRKELRaKLASG 539
Cdd:cd05966 583 GKIMRRILR-KIAAG 596
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
39-533 |
3.31e-38 |
|
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: 146.81 E-value: 3.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 39 FASRPCLINGAT--GDV-YTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAV 115
Cdd:cd05915 7 LFGRKEVVSRLHtgEVHrTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 116 EIAKQAKAANAKLIVTMACFYDRVKD---LAENGVQIVCVDFAVEGCLHFsvLSGADESLAPLVDFSSNDVVALPYSSGT 192
Cdd:cd05915 87 EIAYILNHAEDKVLLFDPNLLPLVEAirgELKTVQHFVVMDEKAPEGYLA--YEEALGEEADPVRVPERAACGMAYTTGT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 193 TGLPKGVMLTHKG-----LITSVAQQMDGQNPNLYyhrndviLCVLPFFHIYSLNSILLCGLRVGAAIMIMQKFDIVALL 267
Cdd:cd05915 165 TGLPKGVVYSHRAlvlhsLAASLVDGTALSEKDVV-------LPVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPASLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 268 QLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVS-SVRVLKSGGAPLGKELEDAVREKFPTAIlgqGYGMTEAGPVLSMSL 346
Cdd:cd05915 238 ELFDGEGVTFTAGVPTVWLALADYLESTGHRLKtLRRLVVGGSAAPRSLIARFERMGVEVRQ---GYGLTETSPVVVQNF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 347 AFAK-----EPFQVKAGACGTVVRNAEMKIVDTETGASLPANSSG--EICIRGDQIMKGYLNDLESTKRTIDKEGWLHTG 419
Cdd:cd05915 315 VKSHleslsEEEKLTLKAKTGLPIPLVRLRVADEEGRPVPKDGKAlgEVQLKGPWITGGYYGNEEATRSALTPDGFFRTG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 420 DIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVmKANGGAISEEEVKQF 499
Cdd:cd05915 395 DIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVV-VPRGEKPTPEELNEH 473
|
490 500 510
....*....|....*....|....*....|....*
gi 778728825 500 IAKQVVFYKRL-KRVFFVNAIPKAPSGKILRKELR 533
Cdd:cd05915 474 LLKAGFAKWQLpDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
182-529 |
3.48e-38 |
|
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: 143.17 E-value: 3.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 182 DVVALPYSSGTTGLPKGVMLTHKGLITSVAQQMDGQnpnLYYHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKF 261
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEG---LNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 262 DIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGA-PLGKELedAVREKFPTAILGQGYGMTEAGP 340
Cdd:cd17635 79 TYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSrAIAADV--RFIEATGLTNTAQVYGLSETGT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 341 VLSmsLAFAKEpfQVKAGACGTVVRNAEMKIVDTEtGASLPANSSGEICIRGDQIMKGYLNDLEstkRTIDK--EGWLHT 418
Cdd:cd17635 157 ALC--LPTDDD--SIEINAVGRPYPGVDVYLAATD-GIAGPSASFGTIWIKSPANMLGYWNNPE---RTAEVliDGWVNT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 419 GDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKAnggAISEEEV-- 496
Cdd:cd17635 229 GDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAS---AELDENAir 305
|
330 340 350
....*....|....*....|....*....|....*
gi 778728825 497 --KQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILR 529
Cdd:cd17635 306 alKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
60-534 |
1.96e-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: 143.48 E-value: 1.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 60 QLTAR--RVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAveiakqakaanaklivtmacfyD 137
Cdd:cd05974 5 EMSARssRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTP----------------------D 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 138 RVKDLAENGVQIVCVdfavegclhfsvlsgADESLAplvdfsSNDVVALPYSSGTTGLPKGVMLTHKGLITsvaqqmdGQ 217
Cdd:cd05974 63 DLRDRVDRGGAVYAA---------------VDENTH------ADDPMLLYFTSGTTSKPKLVEHTHRSYPV-------GH 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 218 NPNLYY---HRNDVILCVL-PFF--HIYSlnsILLCGLRVGAAIMIMQ--KFDIVALLQLIEKHRISIMPIVPPIFLAIA 289
Cdd:cd05974 115 LSTMYWiglKPGDVHWNISsPGWakHAWS---CFFAPWNAGATVFLFNyaRFDAKRVLAALVRYGVTTLCAPPTVWRMLI 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 290 KSPeFEKYDVSsVRVLKSGGAPLGKELEDAVREKFPTAILgQGYGMTEAGPVLSMSlafakePFQ-VKAGACGTVVRNAE 368
Cdd:cd05974 192 QQD-LASFDVK-LREVVGAGEPLNPEVIEQVRRAWGLTIR-DGYGQTETTALVGNS------PGQpVKAGSMGRPLPGYR 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 369 MKIVDTETGASlpanSSGEICI-----RGDQIMKGYLNDLESTkRTIDKEGWLHTGDIGFVDDDNELFIVDRLKELIKFK 443
Cdd:cd05974 263 VALLDPDGAPA----TEGEVALdlgdtRPVGLMKGYAGDPDKT-AHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSS 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 444 AFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEE---EVKQFIAKQVVFYKRLKRVFFVNaIP 520
Cdd:cd05974 338 DYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPEtalEIFRFSRERLAPYKRIRRLEFAE-LP 416
|
490
....*....|....
gi 778728825 521 KAPSGKILRKELRA 534
Cdd:cd05974 417 KTISGKIRRVELRR 430
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
49-532 |
3.13e-37 |
|
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: 143.96 E-value: 3.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 49 ATGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKL 128
Cdd:cd17646 19 DEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 129 IVTMAcfydrvkDLAENGVQIVCVDFAVEGCLhfsvlsGADESLAPLVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLIT 208
Cdd:cd17646 99 VLTTA-------DLAARLPAGGDVALLGDEAL------AAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 209 SVAqQMDGQNPNLyyhRNDVILCVLPF-FHIySLNSILLcGLRVGAAIMIMQ---KFDIVALLQLIEKHRISIMPIVP-- 282
Cdd:cd17646 166 RLL-WMQDEYPLG---PGDRVLQKTPLsFDV-SVWELFW-PLVAGARLVVARpggHRDPAYLAALIREHGVTTCHFVPsm 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 283 -PIFLAIAKSPefekyDVSSVRVLKSGGAPLGKELEDAVREKfPTAILGQGYGMTEAgpVLSMSLAFAKEPFQVKAGACG 361
Cdd:cd17646 240 lRVFLAEPAAG-----SCASLRRVFCSGEALPPELAARFLAL-PGAELHNLYGPTEA--AIDVTHWPVRGPAETPSVPIG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 362 TVVRNAEMKIVDTEtGASLPANSSGEICIRGDQIMKGYLNDLESTK---------------RTIDKEGWLHTGDIGFvdd 426
Cdd:cd17646 312 RPVPNTRLYVLDDA-LRPVPVGVPGELYLGGVQLARGYLGRPALTAerfvpdpfgpgsrmyRTGDLARWRPDGALEF--- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 427 dnelfiVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGA-ISEEEVKQFIAKQVV 505
Cdd:cd17646 388 ------LGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAgPDTAALRAHLAERLP 461
|
490 500
....*....|....*....|....*..
gi 778728825 506 FYKRLKRVFFVNAIPKAPSGKILRKEL 532
Cdd:cd17646 462 EYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
55-469 |
4.39e-37 |
|
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: 144.81 E-value: 4.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 55 TYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAanpFYTAveiakqakaanaklIVTMAC 134
Cdd:cd05933 10 TYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVG---IYTT--------------NSPEAC 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 135 FYdrvkdLAENG-VQIVCVD--------FAVEGCL-HFSVL-------------------------SGADESLAPLVD-F 178
Cdd:cd05933 73 QY-----VAETSeANILVVEnqkqlqkiLQIQDKLpHLKAIiqykeplkekepnlyswdefmelgrSIPDEQLDAIISsQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 179 SSNDVVALPYSSGTTGLPKGVMLTHKGLI---TSVAQQMDGQNPNlyyHRNDVILCVLPFFHIYSLNSILLCGLRVGAAI 255
Cdd:cd05933 148 KPNQCCTLIYTSGTTGMPKGVMLSHDNITwtaKAASQHMDLRPAT---VGQESVVSYLPLSHIAAQILDIWLPIKVGGQV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 256 MIMQ----KFDIVALLQLIEKHRISIMPIV-------------------------------------------PPIFLAI 288
Cdd:cd05933 225 YFAQpdalKGTLVKTLREVRPTAFMGVPRVwekiqekmkavgaksgtlkrkiaswakgvgletnlklmggespSPLFYRL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 289 AKSPEFEK----YDVSSVRVLKSGGAPLGKELEDavrekFPTAI---LGQGYGMTE-AGPVlSMSLafakePFQVKAGAC 360
Cdd:cd05933 305 AKKLVFKKvrkaLGLDRCQKFFTGAAPISRETLE-----FFLSLnipIMELYGMSEtSGPH-TISN-----PQAYRLLSC 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 361 GTVVRNAEMKIVDTEtgaslpANSSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLHTGDIGFVDDDNELFIVDRLKELI 440
Cdd:cd05933 374 GKALPGCKTKIHNPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELI 447
|
490 500 510
....*....|....*....|....*....|.
gi 778728825 441 KFKAFQ-VAPAELEALLITH-PKLSDAAVIG 469
Cdd:cd05933 448 ITAGGEnVPPVPIEDAVKKElPIISNAMLIG 478
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
42-533 |
6.76e-37 |
|
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: 142.87 E-value: 6.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 42 RPCLINGatGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQA 121
Cdd:cd17651 11 APALVAE--GRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFML 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 122 KAANAKLIVTMACFYDRVKDLAENGVQIvcvdfavegcLHFSVLSGADesLAPLVDFSSNDVVALPYSSGTTGLPKGVML 201
Cdd:cd17651 89 ADAGPVLVLTHPALAGELAVELVAVTLL----------DQPGAAAGAD--AEPDPALDADDLAYVIYTSGSTGRPKGVVM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 202 THkgliTSVAQQMDGQNPNLYYHRNDVILCVLPFFHIYSLNSIL--LCGlrvGAAIMIM---QKFDIVALLQLIEKHRIS 276
Cdd:cd17651 157 PH----RSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFstLCA---GATLVLPpeeVRTDPPALAAWLDEQRIS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 277 IMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGkeLEDAVREKF---PTAILGQGYGMTEAGPVLSMSLAFAKEPF 353
Cdd:cd17651 230 RVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLV--LTEDLREFCaglPGLRLHNHYGPTETHVVTALSLPGDPAAW 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 354 QVKAgACGTVVRNAEMKIVDtETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIDKEGWL------HTGDIGFVDDD 427
Cdd:cd17651 308 PAPP-PIGRPIDNTRVYVLD-AALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 428 NELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVFY 507
Cdd:cd17651 386 GELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEY 465
|
490 500
....*....|....*....|....*.
gi 778728825 508 KRLKRVFFVNAIPKAPSGKILRKELR 533
Cdd:cd17651 466 MVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
52-541 |
2.03e-36 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 142.84 E-value: 2.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 52 DVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAImTAANPFYTAV--------EIAKQAKA 123
Cdd:PRK09192 48 EALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLV-PVPLPLPMGFggresyiaQLRGMLAS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 124 ANAKLIVTMACFYDRVKDLAENgvQIVCVDFAVEgclHFSVLSGADeslAPLVDFSSNDVVALPYSSGTTGLPKGVMLTH 203
Cdd:PRK09192 127 AQPAAIITPDELLPWVNEATHG--NPLLHVLSHA---WFKALPEAD---VALPRPTPDDIAYLQYSSGSTRFPRGVIITH 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 204 KGLITsvaqqmdgqnpNLYYHRNDVIL------CV--LPFFHIYSLNSILL----CGLRVGaaIMIMQKFDIVAL--LQL 269
Cdd:PRK09192 199 RALMA-----------NLRAISHDGLKvrpgdrCVswLPFYHDMGLVGFLLtpvaTQLSVD--YLPTRDFARRPLqwLDL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 270 IEKHRISImPIVPPIFLAI----AKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKF------PTAILGQgYGMTEAG 339
Cdd:PRK09192 266 ISRNRGTI-SYSPPFGYELcarrVNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEAFapagfdDKAFMPS-YGLAEAT 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 340 PVLSMS----------------------LAFAKEPFQVKAGA-CGTVVRNAEMKIVDtETGASLPANSSGEICIRGDQIM 396
Cdd:PRK09192 344 LAVSFSplgsgivveevdrdrleyqgkaVAPGAETRRVRTFVnCGKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLM 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 397 KGYLNDLESTkRTIDKEGWLHTGDIGFVDDDnELFIVDRLKELIKFKAFQVAPAELEALLITHPKL--SDAAVIGMPDvE 474
Cdd:PRK09192 423 SGYFRDEESQ-DVLAADGWLDTGDLGYLLDG-YLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELrsGDAAAFSIAQ-E 499
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 778728825 475 AGEVPVAFVMkangGAISEEEVKQFIAKQVVfyKRLKRVFFVN---------AIPKAPSGKILRKELRAKLASGAY 541
Cdd:PRK09192 500 NGEKIVLLVQ----CRISDEERRGQLIHALA--ALVRSEFGVEaavelvpphSLPRTSSGKLSRAKAKKRYLSGAF 569
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
12-453 |
2.41e-36 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 143.32 E-value: 2.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 12 IFRSKLPDIHIPNHLP-------LHDYVFQNLSKFASRPCL-----INGATGDvY---TYHDVQlTARR-VAAGLHNLGI 75
Cdd:PLN02736 23 VYRSARSPLKLVSRFPdhpeigtLHDNFVYAVETFRDYKYLgtrirVDGTVGE-YkwmTYGEAG-TARTaIGSGLVQHGI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 76 KKGDVVMNLLPNSPEFVFTFLGASyrgAIMTAANPFYT-----AVEiakqakaanakLIVTMA------CFYDRVKDLAE 144
Cdd:PLN02736 101 PKGACVGLYFINRPEWLIVDHACS---AYSYVSVPLYDtlgpdAVK-----------FIVNHAevaaifCVPQTLNTLLS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 145 NGVQIVCVDFAVegclhfsVLSGADESLAPL--------VDFSS-----------------NDVVALPYSSGTTGLPKGV 199
Cdd:PLN02736 167 CLSEIPSVRLIV-------VVGGADEPLPSLpsgtgveiVTYSKllaqgrsspqpfrppkpEDVATICYTSGTTGTPKGV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 200 MLTHKGLITSVAqqmdGQNPNLYYHRNDVILCVLPFFHIYSLNSILLCgLRVGAAIMIMQKfDIVALLQLIEKHRISIMP 279
Cdd:PLN02736 240 VLTHGNLIANVA----GSSLSTKFYPSDVHISYLPLAHIYERVNQIVM-LHYGVAVGFYQG-DNLKLMDDLAALRPTIFC 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 280 IVP----PIFLAI--------------------AK----------SPEFEKYDVSS--------VRVLKSGGAPLGKELE 317
Cdd:PLN02736 314 SVPrlynRIYDGItnavkesgglkerlfnaaynAKkqalengknpSPMWDRLVFNKikaklggrVRFMSSGASPLSPDVM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 318 DAVREKFPTAILgQGYGMTEAGPVLSmslafAKEPFQVKAGACGTVVRNAEMKIVD------TETGASLPansSGEICIR 391
Cdd:PLN02736 394 EFLRICFGGRVL-EGYGMTETSCVIS-----GMDEGDNLSGHVGSPNPACEVKLVDvpemnyTSEDQPYP---RGEICVR 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 778728825 392 GDQIMKGYLNDLESTKRTIDKEGWLHTGDIGFVDDDNELFIVDRLKELikFKAFQ---VAPAELE 453
Cdd:PLN02736 465 GPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNI--FKLAQgeyIAPEKIE 527
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
74-535 |
8.91e-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: 140.29 E-value: 8.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 74 GIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIVTMACFYDRVKDLAEN----GVQI 149
Cdd:cd05928 63 GLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASEcpslKTKL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 150 VCVDFAVEGCLHFSVLSGADESLAPLVDFSSNDVVALPYSSGTTGLPKGVMLTHK----GLITSVAQQMDGQNPNLYYHR 225
Cdd:cd05928 143 LVSEKSRDGWLNFKELLNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSslglGLKVNGRYWLDLTASDIMWNT 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 226 NDV--ILCVlpffhIYSLNSILLCGlrvgAAIMI--MQKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSpEFEKYDVSS 301
Cdd:cd05928 223 SDTgwIKSA-----WSSLFEPWIQG----ACVFVhhLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQ-DLSSYKFPS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 302 VRVLKSGGAPLGKELEDAVREKfpTAI-LGQGYGMTEAGPVLSMSlafakEPFQVKAGACGTVVRNAEMKIVDtETGASL 380
Cdd:cd05928 293 LQHCVTGGEPLNPEVLEKWKAQ--TGLdIYEGYGQTETGLICANF-----KGMKIKPGSMGKASPPYDVQIID-DNGNVL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 381 PANSSGEICIRGDQ-----IMKGYLNDLESTKRTIDKEGWLhTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEAL 455
Cdd:cd05928 365 PPGTEGDIGIRVKPirpfgLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESA 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 456 LITHPKLSDAAVIGMPDVEAGEVPVAFVM-----KANGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRK 530
Cdd:cd05928 444 LIEHPAVVESAVVSSPDPIRGEVVKAFVVlapqfLSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRN 523
|
....*
gi 778728825 531 ELRAK 535
Cdd:cd05928 524 ELRDK 528
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
42-532 |
1.16e-35 |
|
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: 139.33 E-value: 1.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 42 RPCLINGAtgDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAImtaanpfYTAVEIAKQA 121
Cdd:cd12114 3 ATAVICGD--GTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAA-------YVPVDIDQPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 122 kaanaklivtmacfyDRVKDLAENG---VQIVCVDFAVEGCLHFSVLSGADESLAPLVDFSSndVVALP-------YSSG 191
Cdd:cd12114 74 ---------------ARREAILADAgarLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPP--VDVAPddlayviFTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 192 TTGLPKGVMLTHKGLITSVAQ--QMDGQNPNlyyhrnDVILCVLPFFHIYSLNSILlCGLRVGAAIMIM---QKFDIVAL 266
Cdd:cd12114 137 STGTPKGVMISHRAALNTILDinRRFAVGPD------DRVLALSSLSFDLSVYDIF-GALSAGATLVLPdeaRRRDPAHW 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 267 LQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVR-VLKSGG-APLGkeLEDAVREKFPTA-ILGQGyGMTEAGpVLS 343
Cdd:cd12114 210 AELIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRlVLLSGDwIPLD--LPARLRALAPDArLISLG-GATEAS-IWS 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 344 MSLAFAKEPFQVKAGACGTVVRNAEMKIVDtETGASLPANSSGEICIRGDQIMKGYLNDLESTKRT----IDKEGWLHTG 419
Cdd:cd12114 286 IYHPIDEVPPDWRSIPYGRPLANQRYRVLD-PRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARfvthPDGERLYRTG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 420 DIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQF 499
Cdd:cd12114 365 DLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTPIAPDALRAF 444
|
490 500 510
....*....|....*....|....*....|...
gi 778728825 500 IAKQVVFYKRLKRVFFVNAIPKAPSGKILRKEL 532
Cdd:cd12114 445 LAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
177-471 |
1.48e-35 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 139.95 E-value: 1.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 177 DFSSNDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQMDGQNPNlyyhRNDVILCVLPFFHIYSLNSI----LLCGLRVG 252
Cdd:PRK06334 179 DKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPK----EDDVMMSFLPPFHAYGFNSCtlfpLLSGVPVV 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 253 AAIMIMQKFDIVallQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILGQG 332
Cdd:PRK06334 255 FAYNPLYPKKIV---EMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQG 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 333 YGMTEAGPVLSMSLafAKEPfqvKAGAC-GTVVRNAEMKIVDTETGASLPANSSGEICIRGDQIMKGYL-NDLESTKRTI 410
Cdd:PRK06334 332 YGTTECSPVITINT--VNSP---KHESCvGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLgEDFGQGFVEL 406
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 778728825 411 DKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDA------AVIGMP 471
Cdd:PRK06334 407 GGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNAAdhagplVVCGLP 473
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
51-536 |
1.95e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 139.46 E-value: 1.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 51 GDV--YTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAkqakaanakL 128
Cdd:PRK07008 35 GDIhrYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIA---------Y 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 129 IVtmacfydrvkDLAENgvQIVCVD--FA--VEG----C---LHFSVLSGADESLA---PLV----------------DF 178
Cdd:PRK07008 106 IV----------NHAED--RYVLFDltFLplVDAlapqCpnvKGWVAMTDAAHLPAgstPLLcyetlvgaqdgdydwpRF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 179 SSNDVVALPYSSGTTGLPKGVMLTHKgliTSVAQQMDGQNPN-LYYHRNDVILCVLPFFHI------YSlnsillCGLrV 251
Cdd:PRK07008 174 DENQASSLCYTSGTTGNPKGALYSHR---STVLHAYGAALPDaMGLSARDAVLPVVPMFHVnawglpYS------APL-T 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 252 GAAIMIM-QKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILg 330
Cdd:PRK07008 244 GAKLVLPgPDLDGKSLYELIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVI- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 331 QGYGMTEAGPVLSMS------LAFAKEPFQVKAGACGTVVRNAEMKIVDtETGASLP--ANSSGEICIRGDQIMKGYLND 402
Cdd:PRK07008 323 HAWGMTEMSPLGTLCklkwkhSQLPLDEQRKLLEKQGRVIYGVDMKIVG-DDGRELPwdGKAFGDLQVRGPWVIDRYFRG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 403 LESTKRtidkEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAF 482
Cdd:PRK07008 402 DASPLV----DGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLV 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 778728825 483 VMKANGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELRAKL 536
Cdd:PRK07008 478 VVKRPGAEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQF 531
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
23-541 |
2.92e-35 |
|
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: 141.53 E-value: 2.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 23 PNHLPLHDYVFQNLSKFASRPCLINGatGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFL-----G 97
Cdd:COG1020 473 PADATLHELFEAQAARTPDAVAVVFG--DQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLavlkaG 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 98 ASY-----------RGAIMTAANPfytaveiakqakaanaKLIVTMACFYDRvkdLAENGVQIVCVDfavegclhfSVLS 166
Cdd:COG1020 551 AAYvpldpaypaerLAYMLEDAGA----------------RLVLTQSALAAR---LPELGVPVLALD---------ALAL 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 167 GADESLAPLVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLitsvAQQMDGQNPNLYYHRNDVILCVLPF---FHIYSLNS 243
Cdd:COG1020 603 AAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRAL----VNLLAWMQRRYGLGPGDRVLQFASLsfdASVWEIFG 678
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 244 ILLCglrvGAAIMIMQK---FDIVALLQLIEKHRISIMPIVPPIFLAIAkspEFEKYDVSSVRVLKSGGAPLGKELEDAV 320
Cdd:COG1020 679 ALLS----GATLVLAPPearRDPAALAELLARHRVTVLNLTPSLLRALL---DAAPEALPSLRLVLVGGEALPPELVRRW 751
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 321 REKFPTAILGQGYGMTEAGpVlsMSLAFAKEPFQVKAGAC--GTVVRNAEMKIVDtETGASLPANSSGEICIRGDQIMKG 398
Cdd:COG1020 752 RARLPGARLVNLYGPTETT-V--DSTYYEVTPPDADGGSVpiGRPIANTRVYVLD-AHLQPVPVGVPGELYIGGAGLARG 827
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 399 YLNDLESTKR-------TIDKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMP 471
Cdd:COG1020 828 YLNRPELTAErfvadpfGFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVARE 907
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 472 DVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELRAKLASGAY 541
Cdd:COG1020 908 DAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAA 977
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
51-532 |
3.31e-35 |
|
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: 138.10 E-value: 3.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 51 GDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIV 130
Cdd:cd12117 20 DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 131 TMACFYDRVKDLAENGVQIVCVDFAVEGclhfsvlsgadeslAPLVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLITSV 210
Cdd:cd12117 100 TDRSLAGRAGGLEVAVVIDEALDAGPAG--------------NPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 211 aqqmdgQNPNLYYHR-NDVILCV--LPF----FHIYS--LNsillcglrvGAAIMIMQK---FDIVALLQLIEKHRISIM 278
Cdd:cd12117 166 ------KNTNYVTLGpDDRVLQTspLAFdastFEIWGalLN---------GARLVLAPKgtlLDPDALGALIAEEGVTVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 279 PIVPPIFLAIAKS-PE-FekydvSSVRVLKSGGAPLGKELEDAVREKFPTAILGQGYGMTEaGPVLSMSLAFAKEPFQVK 356
Cdd:cd12117 231 WLTAALFNQLADEdPEcF-----AGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTE-NTTFTTSHVVTELDEVAG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 357 AGACGTVVRNAEMKIVDtETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIDKEGWL------HTGDIGFVDDDNEL 430
Cdd:cd12117 305 SIPIGRPIANTRVYVLD-EDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 431 FIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVmkANGGAISEEEVKQFIAKQVVFYKRL 510
Cdd:cd12117 384 EFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYV--VAEGALDAAELRAFLRERLPAYMVP 461
|
490 500
....*....|....*....|..
gi 778728825 511 KRVFFVNAIPKAPSGKILRKEL 532
Cdd:cd12117 462 AAFVVLDELPLTANGKVDRRAL 483
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
53-539 |
4.05e-35 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 139.70 E-value: 4.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 53 VYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIVTM 132
Cdd:PRK10524 84 TYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPVLIVSA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 133 ------------ACFYDRVKDLAEN---GVQIVC-------------VDFAVEGCLHFsvlsGADeslAPLVDFSSNDVV 184
Cdd:PRK10524 164 dagsrggkvvpyKPLLDEAIALAQHkprHVLLVDrglapmarvagrdVDYATLRAQHL----GAR---VPVEWLESNEPS 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 185 ALPYSSGTTGLPKGVMLTHKGLITSVAQQMD----GQNPNLYYHRNDVILCVLPFFHIYS-----LNSILLCGL--RVGA 253
Cdd:PRK10524 237 YILYTSGTTGKPKGVQRDTGGYAVALATSMDtifgGKAGETFFCASDIGWVVGHSYIVYApllagMATIMYEGLptRPDA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 254 AImimqkfdivaLLQLIEKHRISIMPIVPPIFLAIAKSPE--FEKYDVSSVRVLKSGGAPLGKeledavrekfPTA---- 327
Cdd:PRK10524 317 GI----------WWRIVEKYKVNRMFSAPTAIRVLKKQDPalLRKHDLSSLRALFLAGEPLDE----------PTAswis 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 328 -ILGQ----GYGMTEAG-PVLSMSLAFAKEPfqVKAGACGTVVRNAEMKIVDTETGASLPANSSGEICIRG--------- 392
Cdd:PRK10524 377 eALGVpvidNYWQTETGwPILAIARGVEDRP--TRLGSPGVPMYGYNVKLLNEVTGEPCGPNEKGVLVIEGplppgcmqt 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 393 -----DQIMKGYLndlestkRTIDKEGWlHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAV 467
Cdd:PRK10524 455 vwgddDRFVKTYW-------SLFGRQVY-STFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAV 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 468 IGMPDVEAGEVPVAFVMKANGGAIS--------EEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELRAkLASG 539
Cdd:PRK10524 527 VGVKDALKGQVAVAFVVPKDSDSLAdrearlalEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQA-IAEG 605
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
55-532 |
1.85e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 130.50 E-value: 1.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 55 TYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIVTMAC 134
Cdd:PRK13383 62 SYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 135 FYDRVkdlAENGVQIVCVDFAVEGCLHfsvlSGADESLAPlvdfsSNDVVALpySSGTTGLPKGVMLTHK-----GLITS 209
Cdd:PRK13383 142 FAERI---AGADDAVAVIDPATAGAEE----SGGRPAVAA-----PGRIVLL--TSGTTGKPKGVPRAPQlrsavGVWVT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 210 VAQQMDgqnpnlyYHRNDVILCVLPFFHIYSLNSILLCgLRVGAAIMIMQKFDIVALLQLIEKHRISIMPIVPPIFLAIA 289
Cdd:PRK13383 208 ILDRTR-------LRTGSRISVAMPMFHGLGLGMLMLT-IALGGTVLTHRHFDAEAALAQASLHRADAFTAVPVVLARIL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 290 KSPE--FEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTaILGQGYGMTEAG-PVLSMSLAFAKEPFQVKAGACGTVVRn 366
Cdd:PRK13383 280 ELPPrvRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGD-ILYNGYGSTEVGiGALATPADLRDAPETVGKPVAGCPVR- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 367 aemkIVDtETGASLPANSSGEICIRGDQIMKGYLNDleSTKRTIDkeGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQ 446
Cdd:PRK13383 358 ----ILD-RNNRPVGPRVTGRIFVGGELAGTRYTDG--GGKAVVD--GMTSTGDMGYLDNAGRLFIVGREDDMIISGGEN 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 447 VAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGK 526
Cdd:PRK13383 429 VYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGK 508
|
....*.
gi 778728825 527 ILRKEL 532
Cdd:PRK13383 509 VLRKEL 514
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
55-538 |
2.03e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 130.89 E-value: 2.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 55 TYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAAN-PFYT------AVEIAKQAKAANAK 127
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHqPTPRtdlavwAEDTLRVIGMIGAK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 128 LIVTMACFYDRVKDLAENGVQIVCVDFAVEGclhfsvlsgadESLAPlVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLI 207
Cdd:PRK07768 111 AVVVGEPFLAAAPVLEEKGIRVLTVADLLAA-----------DPIDP-VETGEDDLALMQLTSGSTGSPKAVQITHGNLY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 208 TSVAQQMDGQNpnlYYHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKFDIVA--LL--QLIEKHRISImpIVPP 283
Cdd:PRK07768 179 ANAEAMFVAAE---FDVETDVMVSWLPLFHDMGMVGFLTVPMYFGAELVKVTPMDFLRdpLLwaELISKYRGTM--TAAP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 284 IF----LA--IAKSPEFEKYDVSSVRVLKSGGAPLgkelEDAVREKF----------PTAILgQGYGMTEA--------- 338
Cdd:PRK07768 254 NFayalLArrLRRQAKPGAFDLSSLRFALNGAEPI----DPADVEDLldagarfglrPEAIL-PAYGMAEAtlavsfspc 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 339 --GPVL---------SMSLAFAKEPFQVKAGAC-GTVVRNAEMKIVDtETGASLPANSSGEICIRGDQIMKGYLnDLEST 406
Cdd:PRK07768 329 gaGLVVdevdadllaALRRAVPATKGNTRRLATlGPPLPGLEVRVVD-EDGQVLPPRGVGVIELRGESVTPGYL-TMDGF 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 407 KRTIDKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEallithpklsdAAVIGMPDVEAGEVpVAFVMKA 486
Cdd:PRK07768 407 IPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE-----------RAAARVEGVRPGNA-VAVRLDA 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 778728825 487 NG------------GAISEEEVKQfIAKQV---VFYK-----RLKRVFFVNAIPKAPSGKILRKELRAKLAS 538
Cdd:PRK07768 475 GHsregfavavesnAFEDPAEVRR-IRHQVaheVVAEvgvrpRNVVVLGPGSIPKTPSGKLRRANAAELVTP 545
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
55-532 |
4.66e-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: 4.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 55 TYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAveiakqakaanaklivtmac 134
Cdd:cd17655 24 TYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPE-------------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 135 fyDRVKDLAEN-GVQIVCVDFAVEGCLHF----------SVLSGADESLAPLVDFSsnDVVALPYSSGTTGLPKGVMLTH 203
Cdd:cd17655 84 --ERIQYILEDsGADILLTQSHLQPPIAFiglidlldedTIYHEESENLEPVSKSD--DLAYVIYTSGSTGKPKGVMIEH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 204 KGLITSVaqqmDGQNPNLYYHRNDVILCVLPFFHIYSLNSI---LLCglrvGAAIMIMQK---FDIVALLQLIEKHRISI 277
Cdd:cd17655 160 RGVVNLV----EWANKVIYQGEHLRVALFASISFDASVTEIfasLLS----GNTLYIVRKetvLDGQALTQYIRQNRITI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 278 MPIVPPIFLAIAKSPEFEKydvSSVRVLKSGGAPLGKELEDAVREKFPTAI-LGQGYGMTEAgPVLSMSLAFAKEPFQVK 356
Cdd:cd17655 232 IDLTPAHLKLLDAADDSEG---LSLKHLIVGGEALSTELAKKIIELFGTNPtITNAYGPTET-TVDASIYQYEPETDQQV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 357 AGACGTVVRNAEMKIVDTEtGASLPANSSGEICIRGDQIMKGYLNDLESTK---------------RTIDKEGWLHTGDI 421
Cdd:cd17655 308 SVPIGKPLGNTRIYILDQY-GRPQPVGVAGELYIGGEGVARGYLNRPELTAekfvddpfvpgermyRTGDLARWLPDGNI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 422 GFvdddnelfiVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANggAISEEEVKQFIA 501
Cdd:cd17655 387 EF---------LGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEK--ELPVAQLREFLA 455
|
490 500 510
....*....|....*....|....*....|...
gi 778728825 502 KQVVFYkrLKRVFFV--NAIPKAPSGKILRKEL 532
Cdd:cd17655 456 RELPDY--MIPSYFIklDEIPLTPNGKVDRKAL 486
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
48-542 |
1.33e-31 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 128.75 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 48 GATGDVYTYHDVQLTARRVAAGLHN-LGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANA 126
Cdd:PRK05620 33 GAEQEQTTFAAIGARAAALAHALHDeLGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAED 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 127 KLIVTMACFYDRVKDLAE-----NGVQIVCVDF----AVEGCLHFSVLSGadESLA---------PLVDfsSNDVVALPY 188
Cdd:PRK05620 113 EVIVADPRLAEQLGEILKecpcvRAVVFIGPSDadsaAAHMPEGIKVYSY--EALLdgrstvydwPELD--ETTAAAICY 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 189 SSGTTGLPKGVMLTHKGLITsvaQQMDGQNPNLYYHRNDV-ILCVLPFFHIYSLnSILLCGLRVGAAiMIMQKFDIVA-- 265
Cdd:PRK05620 189 STGTTGAPKGVVYSHRSLYL---QSLSLRTTDSLAVTHGEsFLCCVPIYHVLSW-GVPLAAFMSGTP-LVFPGPDLSApt 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 266 LLQLIEkhriSIMPI----VPPIFLAI-----AKSPEfekydVSSVRVLKSGGAPLGKELEDAVREKFPTAILgQGYGMT 336
Cdd:PRK05620 264 LAKIIA----TAMPRvahgVPTLWIQLmvhylKNPPE-----RMSLQEIYVGGSAVPPILIKAWEERYGVDVV-HVWGMT 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 337 EAGPVLSMslafAKEPfqvkAGACGTVVRN-----------AEMKIVDTETGASLPANSSGEICIRGDQIMKGYLND--- 402
Cdd:PRK05620 334 ETSPVGTV----ARPP----SGVSGEARWAyrvsqgrfpasLEYRIVNDGQVMESTDRNEGEIQVRGNWVTASYYHSpte 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 403 ----LESTKRTIDKE---------GWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIG 469
Cdd:PRK05620 406 egggAASTFRGEDVEdandrftadGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 470 MPDVEAGEVPVAFVMKANGGAISEEEVKQfiakqvvFYKRLKRVF----------FVNAIPKAPSGKILRKELRAKLASG 539
Cdd:PRK05620 486 YPDDKWGERPLAVTVLAPGIEPTRETAER-------LRDQLRDRLpnwmlpeywtFVDEIDKTSVGKFDKKDLRQHLADG 558
|
...
gi 778728825 540 AYN 542
Cdd:PRK05620 559 DFE 561
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
51-534 |
7.24e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 125.95 E-value: 7.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 51 GDVYTYHDVQLTARRVAAGLHNL---------GIkkgdvvmnLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQA 121
Cdd:PRK07867 26 DSFTSWREHIRGSAARAAALRARldptrpphvGV--------LLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 122 KAANAKLIVTMACFYDRVKDLaENGVQIVCVDFAvegcLHFSVLSGADESLAPLVDFSSNDVVALPYSSGTTGLPKGVML 201
Cdd:PRK07867 98 AHADCQLVLTESAHAELLDGL-DPGVRVINVDSP----AWADELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRC 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 202 THKGLitSVAQQMDGQNPNLyyHRNDVILCVLPFFHIyslNSILLC---GLRVGAAIMIMQKFDIVALLQLIEKHRISIM 278
Cdd:PRK07867 173 THRKV--ASAGVMLAQRFGL--GPDDVCYVSMPLFHS---NAVMAGwavALAAGASIALRRKFSASGFLPDVRRYGATYA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 279 PIV-PPIFLAIAKSPEFEKYDvSSVRVL--KSGGAPlgkeleDAVR--EKFPTAILgQGYGMTEAGpvlsmsLAFAKEPf 353
Cdd:PRK07867 246 NYVgKPLSYVLATPERPDDAD-NPLRIVygNEGAPG------DIARfaRRFGCVVV-DGFGSTEGG------VAITRTP- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 354 QVKAGACGTVVrnAEMKIVDTETGASLP------------ANSSGEIC-IRGDQIMKGYLNDLESTKRTIdKEGWLHTGD 420
Cdd:PRK07867 311 DTPPGALGPLP--PGVAIVDPDTGTECPpaedadgrllnaDEAIGELVnTAGPGGFEGYYNDPEADAERM-RGGVYWSGD 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 421 IGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFI 500
Cdd:PRK07867 388 LAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFL 467
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 778728825 501 A-------KQVVFYKRLkrvffVNAIPKAPSGKILRKELRA 534
Cdd:PRK07867 468 AaqpdlgpKQWPSYVRV-----CAELPRTATFKVLKRQLSA 503
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
51-540 |
1.10e-30 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 127.98 E-value: 1.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 51 GDVYTYHDVQLTARRVAAGLHNLGiKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVE-----IAKQAKAAN 125
Cdd:PRK05691 38 GVVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESARRhhqerLLSIIADAE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 126 AKLIVTMACFYDRVKDL----AENGVQIVCVDfAVEGCLhfsvlsgADESLAPLVDfsSNDVVALPYSSGTTGLPKGVML 201
Cdd:PRK05691 117 PRLLLTVADLRDSLLQMeelaAANAPELLCVD-TLDPAL-------AEAWQEPALQ--PDDIAFLQYTSGSTALPKGVQV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 202 THKGLITSvaQQMDGQNPNLYYHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKFDIVA----LLQLIEKHRISI 277
Cdd:PRK05691 187 SHGNLVAN--EQLIRHGFGIDLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPAYFLErplrWLEAISEYGGTI 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 278 MPivPPIF---LAIAKSPE--FEKYDVSSVRVLKSGGAPLGKELEDAVREKF------PTAILGQgYGMTEAG------- 339
Cdd:PRK05691 265 SG--GPDFayrLCSERVSEsaLERLDLSRWRVAYSGSEPIRQDSLERFAEKFaacgfdPDSFFAS-YGLAEATlfvsggr 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 340 -----PVLSM-SLAFAKEPFQVKAGA----CGTVVRNAEMKIVDTETGASLPANSSGEICIRGDQIMKGYLNDLESTKRT 409
Cdd:PRK05691 342 rgqgiPALELdAEALARNRAEPGTGSvlmsCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKT 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 410 I---DKEGWLHTGDIGFVdDDNELFIVDRLKELIKFKAFQVAPAELEallithpKLSDAAVigmPDVEAGEVpVAFVMKA 486
Cdd:PRK05691 422 FvehDGRTWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIE-------KTVEREV---EVVRKGRV-AAFAVNH 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 778728825 487 NG--GAISEEEVKQFIAKQV---VFYKRLKR------------VFFVN--AIPKAPSGKILRKELRAKLASGA 540
Cdd:PRK05691 490 QGeeGIGIAAEISRSVQKILppqALIKSIRQavaeacqeapsvVLLLNpgALPKTSSGKLQRSACRLRLADGS 562
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
54-538 |
2.68e-30 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 124.33 E-value: 2.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 54 YTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLgasyrgAIMTAA----NPFYT--AVEIAKQAKAANAK 127
Cdd:PRK10946 49 FSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFF------ALLKLGvapvNALFShqRSELNAYASQIEPA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 128 LIVTmacfyDRVKDLAENGvqivcvDF-----AVEGCLHFSVLSGAD--ESLAPLVDFSSNDVVALP----------YSS 190
Cdd:PRK10946 123 LLIA-----DRQHALFSDD------DFlntlvAEHSSLRVVLLLNDDgeHSLDDAINHPAEDFTATPspadevaffqLSG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 191 GTTGLPKGVMLTHKGLITSVAQQMD--GQNPNLYYhrndviLCVLPFFHIYSLNS-----ILLCGlrvGAAIMIMqkfDI 263
Cdd:PRK10946 192 GSTGTPKLIPRTHNDYYYSVRRSVEicGFTPQTRY------LCALPAAHNYPMSSpgalgVFLAG---GTVVLAP---DP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 264 VALL--QLIEKHRISIMPIVPP---IFLAIAKSPEFeKYDVSSVRVLKSGGAPLGkeleDAVREKFPTAI---LGQGYGM 335
Cdd:PRK10946 260 SATLcfPLIEKHQVNVTALVPPavsLWLQAIAEGGS-RAQLASLKLLQVGGARLS----ETLARRIPAELgcqLQQVFGM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 336 TEaGPVLSMSLafaKEPFQVKAGACGTVVRNA-EMKIVDtETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIDKEG 414
Cdd:PRK10946 335 AE-GLVNYTRL---DDSDERIFTTQGRPMSPDdEVWVAD-ADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 415 WLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANggAISEE 494
Cdd:PRK10946 410 FYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKE--PLKAV 487
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 778728825 495 EVKQFIAKQ-VVFYKRLKRVFFVNAIPKAPSGKILRKELRAKLAS 538
Cdd:PRK10946 488 QLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLAS 532
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
54-532 |
4.52e-29 |
|
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: 120.09 E-value: 4.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 54 YTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAveiakqakaanaklivtma 133
Cdd:cd12116 13 LSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPA------------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 134 cfyDRVKD-LAENGVQIVCVDFAVEGCLHFSVLSGADESLAPLVDFSSNDVVALP-------YSSGTTGLPKGVMLTHKG 205
Cdd:cd12116 74 ---DRLRYiLEDAEPALVLTDDALPDRLPAGLPVLLLALAAAAAAPAAPRTPVSPddlayviYTSGSTGRPKGVVVSHRN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 206 LI---TSVAQQMdGQNPnlyyhrNDVILCVLPF-FHIYSLNsiLLCGLRVGAAIMIMQKFDIV---ALLQLIEKHRISIM 278
Cdd:cd12116 151 LVnflHSMRERL-GLGP------GDRLLAVTTYaFDISLLE--LLLPLLAGARVVIAPRETQRdpeALARLIEAHSITVM 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 279 PIVPPIFLAIAKSpEFEKYDvsSVRVLKSGGA---PLGKELEDAVREkfptaiLGQGYGMTEAgPVLS--MSLAFAKEPF 353
Cdd:cd12116 222 QATPATWRMLLDA-GWQGRA--GLTALCGGEAlppDLAARLLSRVGS------LWNLYGPTET-TIWStaARVTAAAGPI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 354 QVkagacGTVVRNAEMKIVDtETGASLPANSSGEICIRGDQIMKGYLN--DLESTKRTIDKEG-----WLHTGDIGFVDD 426
Cdd:cd12116 292 PI-----GRPLANTQVYVLD-AALRPVPPGVPGELYIGGDGVAQGYLGrpALTAERFVPDPFAgpgsrLYRTGDLVRRRA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 427 DNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVpVAFVMKANGGAISEEEVKQFIAKQVVF 506
Cdd:cd12116 366 DGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRL-VAYVVLKAGAAPDAAALRAHLRATLPA 444
|
490 500
....*....|....*....|....*.
gi 778728825 507 YKRLKRVFFVNAIPKAPSGKILRKEL 532
Cdd:cd12116 445 YMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
181-541 |
6.68e-29 |
|
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: 119.90 E-value: 6.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 181 NDVVALPYSSGTTGLPKGVMLTHKGLIT---SVAQQMDgqnpnlyYHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMI 257
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTHENLVHnmfAILNSTE-------WKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 258 M--QKFDIVALLQL--IEKHRISImpIVPP-----IFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFP--- 325
Cdd:cd05908 179 MptRLFIRRPILWLkkASEHKATI--VSSPnfgykYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSkyg 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 326 ---TAILgQGYGMTEAGpvLSMSLAFAKEPFQV-------------------KAGACGTVVR------NAEMKIVDtETG 377
Cdd:cd05908 257 lkrNAIL-PVYGLAEAS--VGASLPKAQSPFKTitlgrrhvthgepepevdkKDSECLTFVEvgkpidETDIRICD-EDN 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 378 ASLPANSSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLHTGDIGFVdDDNELFIVDRLKELIKFKAFQVAPAELE--AL 455
Cdd:cd05908 333 KILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIEriAE 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 456 LITHPKLSDAAVIGMPDVEAGEVPV-AFVMKANggaiSEEEvkqFIA-----KQVVFYK---RLKRVFFVNAIPKAPSGK 526
Cdd:cd05908 412 ELEGVELGRVVACGVNNSNTRNEEIfCFIEHRK----SEDD---FYPlgkkiKKHLNKRggwQINEVLPIRRIPKTTSGK 484
|
410
....*....|....*
gi 778728825 527 ILRKELRAKLASGAY 541
Cdd:cd05908 485 VKRYELAQRYQSGEF 499
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
52-535 |
3.93e-28 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 118.98 E-value: 3.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 52 DVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIVT 131
Cdd:PRK06060 29 DVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 132 MACFYDR-----VKDLAEngvqiVCVDFAVEGCLHFSVLSGADESLAplvdfssndvvalPYSSGTTGLPKGVMLTHKGL 206
Cdd:PRK06060 109 SDALRDRfqpsrVAEAAE-----LMSEAARVAPGGYEPMGGDALAYA-------------TYTSGTTGPPKAAIHRHADP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 207 ITSVaqqmDGQNPN-LYYHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQ---KFDIVALLQliEKHRISIMPIVP 282
Cdd:PRK06060 171 LTFV----DAMCRKaLRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSapvTPEAAAILS--ARFGPSVLYGVP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 283 PIFLAI--AKSPEfekyDVSSVRVLKSGGAPLGKELEDAVREKFPTAILGQGYGMTEAGPV-LSMSLAfakepfQVKAGA 359
Cdd:PRK06060 245 NFFARVidSCSPD----SFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTfVSNRVD------EWRLGT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 360 CGTVVRNAEMKIVDTEtGASLPANSSGEICIRGDQIMKGYLNDLEStkrTIDKEGWLHTGDIGFVDDDNELFIVDRLKEL 439
Cdd:PRK06060 315 LGRVLPPYEIRVVAPD-GTTAGPGVEGDLWVRGPAIAKGYWNRPDS---PVANEGWLDTRDRVCIDSDGWVTYRCRADDT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 440 IKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISE---EEVKQFIAKQVVFYKRLKRVFFV 516
Cdd:PRK06060 391 EVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGsvmRDLHRGLLNRLSAFKVPHRFAVV 470
|
490
....*....|....*....
gi 778728825 517 NAIPKAPSGKILRKELRAK 535
Cdd:PRK06060 471 DRLPRTPNGKLVRGALRKQ 489
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
188-533 |
4.86e-28 |
|
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: 116.70 E-value: 4.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 188 YSSGTTGLPKGVMLTHKGLITSVAQQMDgqnpnlYY--HRNDVILcvlpffHIYSLNS-----ILLCGLRVGAAIMIM-- 258
Cdd:cd17649 101 YTSGSTGTPKGVAVSHGPLAAHCQATAE------RYglTPGDREL------QFASFNFdgaheQLLPPLICGACVVLRpd 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 259 -QKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDV-SSVRVLKSGGAPLGKELedaVREKFPTAI-LGQGYGM 335
Cdd:cd17649 169 eLWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDGRpPSLRLYIFGGEALSPEL---LRRWLKAPVrLFNAYGP 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 336 TEAgpvLSMSLAFAKEPFQVKAGA---CGTVVRNAEMKIVDTEtGASLPANSSGEICIRGDQIMKGYLNDLEST-KRTID 411
Cdd:cd17649 246 TEA---TVTPLVWKCEAGAARAGAsmpIGRPLGGRSAYILDAD-LNPVPVGVTGELYIGGEGLARGYLGRPELTaERFVP 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 412 ----KEG--WLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVeAGEVPVAFVMK 485
Cdd:cd17649 322 dpfgAPGsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGA-GGKQLVAYVVL 400
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 778728825 486 ANGGAISE--EEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELR 533
Cdd:cd17649 401 RAAAAQPElrAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
54-489 |
1.37e-27 |
|
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: 116.03 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 54 YTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLgasyrgAIMTAAnpfYTAVEIAKQAKAANAKLIVT-- 131
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDL------AIWMAG---HISVPLYPTLNPDTIRYVLEhs 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 132 --MACFYDRVKDLA--ENGVQ---IVCV--------------DFAVEGCLHFSVLSGADESLAPLVdfssndvvalpYSS 190
Cdd:cd05932 78 esKALFVGKLDDWKamAPGVPeglISISlpppsaancqyqwdDLIAQHPPLEERPTRFPEQLATLI-----------YTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 191 GTTGLPKGVMLTHKGLITSVAQQMD--GQNPNlyyhrnDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKFDivALLQ 268
Cdd:cd05932 147 GTTGQPKGVMLTFGSFAWAAQAGIEhiGTEEN------DRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLD--TFVE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 269 LIEKHRISIMPIVP-------------------------PIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVReK 323
Cdd:cd05932 219 DVQRARPTLFFSVPrlwtkfqqgvqdkipqqklnlllkiPVVNSLVKRKVLKGLGLDQCRLAGCGSAPVPPALLEWYR-S 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 324 FPTAILgQGYGMTEagpvlSMSLAFAKEPFQVKAGACGTVVRNAEMKIVDTetgaslpanssGEICIRGDQIMKGYLNDL 403
Cdd:cd05932 298 LGLNIL-EAYGMTE-----NFAYSHLNYPGRDKIGTVGNAGPGVEVRISED-----------GEILVRSPALMMGYYKDP 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 404 ESTKRTIDKEGWLHTGDIGFVDDDNELFIVDRLKELIKF-KAFQVAPAELEALLITHPKLSDAAVIGmpdvEAGEVPVAF 482
Cdd:cd05932 361 EATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVIG----SGLPAPLAL 436
|
....*..
gi 778728825 483 VMKANGG 489
Cdd:cd05932 437 VVLSEEA 443
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
179-441 |
3.25e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 116.23 E-value: 3.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 179 SSNDVVAL-PYSSGTTGLPKGVMLTHkGLITSVAQQMDGQNPNLY--YHRNDVILCVLPFFHIYSLN--SILLcgLRvGA 253
Cdd:PTZ00216 261 ENNDDLALiMYTSGTTGDPKGVMHTH-GSLTAGILALEDRLNDLIgpPEEDETYCSYLPLAHIMEFGvtNIFL--AR-GA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 254 AI------MIMQKF-----DIVAllqliekHRISIMPIVPPIFLAIAKSPE-------------FEKYDVSSVRVLK--- 306
Cdd:PTZ00216 337 LIgfgsprTLTDTFarphgDLTE-------FRPVFLIGVPRIFDTIKKAVEaklppvgslkrrvFDHAYQSRLRALKegk 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 307 -------------------------SGGAPLGKELEDAVREKFptAILGQGYGMTEAGPVLSMSLAFAKEPfqvkaGACG 361
Cdd:PTZ00216 410 dtpywnekvfsapravlggrvramlSGGGPLSAATQEFVNVVF--GMVIQGWGLTETVCCGGIQRTGDLEP-----NAVG 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 362 TVVRNAEMKIVDTE----TGASLPansSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLHTGDIGFVDDDNELFIVDRLK 437
Cdd:PTZ00216 483 QLLKGVEMKLLDTEeykhTDTPEP---RGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVK 559
|
....
gi 778728825 438 ELIK 441
Cdd:PTZ00216 560 ALAK 563
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
51-471 |
1.40e-26 |
|
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: 112.45 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 51 GDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANpfytaveiakqakaanakliv 130
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALIN--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 131 tmacFYDRVKDLAEngvqivCVDFAveGCLHFSVlsgadeslaplvdfssnDVVALPYSSGTTGLPKGVMLTHKGLI--T 208
Cdd:cd05940 60 ----YNLRGESLAH------CLNVS--SAKHLVV-----------------DAALYIYTSGTTGLPKAAIISHRRAWrgG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 209 SVAQQMDGQNPNlyyhrnDVILCVLPFFHiyslNSILLCG----LRVGAAIMIMQKFDIVALLQLIEKHRISIMPIVPPI 284
Cdd:cd05940 111 AFFAGSGGALPS------DVLYTCLPLYH----STALIVGwsacLASGATLVIRKKFSASNFWDDIRKYQATIFQYIGEL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 285 FLAIAKSPEFEKYDVSSVRVLKSGGapLGKELEDAVREKFPTAILGQGYGMTEAgpvlsmSLAFAKepFQVKAGACG--- 361
Cdd:cd05940 181 CRYLLNQPPKPTERKHKVRMIFGNG--LRPDIWEEFKERFGVPRIAEFYAATEG------NSGFIN--FFGKPGAIGrnp 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 362 -TVVRNAEMKIV--DTETGASL----------PANSSGE-IC-IRGDQIMKGYLNDLESTK---RTIDKEG--WLHTGDI 421
Cdd:cd05940 251 sLLRKVAPLALVkyDLESGEPIrdaegrcikvPRGEPGLlISrINPLEPFDGYTDPAATEKkilRDVFKKGdaWFNTGDL 330
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 778728825 422 GFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMP 471
Cdd:cd05940 331 MRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQ 380
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
84-534 |
1.93e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 112.81 E-value: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 84 LLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIVTMACFYDRVKDLAENGVQIVCVDFAvegclHFS 163
Cdd:PRK13388 58 LLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLLVTDAEHRPLLDGLDLPGVRVLDVDTP-----AYA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 164 VLSGADESLAPLVDFSSNDVVALPYSSGTTGLPKGVMLTHkGLITSVAQQMDGQnpnlY-YHRNDVILCVLPFFHIYSLN 242
Cdd:PRK13388 133 ELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSH-GRLAFAGRALTER----FgLTRDDVCYVSMPLFHSNAVM 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 243 SILLCGLRVGAAIMIMQKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVlksggaPLGKELEDAVRE 322
Cdd:PRK13388 208 AGWAPAVASGAAVALPAKFSASGFLDDVRRYGATYFNYVGKPLAYILATPERPDDADNPLRV------AFGNEASPRDIA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 323 KFPT---AILGQGYGMTEAGpvlsmsLAFAKEPfQVKAGACGtvvRNAE-MKIVDTET------------GASL-PANSS 385
Cdd:PRK13388 282 EFSRrfgCQVEDGYGSSEGA------VIVVREP-GTPPGSIG---RGAPgVAIYNPETltecavarfdahGALLnADEAI 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 386 GEIC-IRGDQIMKGYLNDLESTKRTIdKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSD 464
Cdd:PRK13388 352 GELVnTAGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINR 430
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 778728825 465 AAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQ----VVFYKRLKRVffVNAIPKAPSGKILRKELRA 534
Cdd:PRK13388 431 VAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAFLAAQpdlgTKAWPRYVRI--AADLPSTATNKVLKRELIA 502
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
51-532 |
2.21e-26 |
|
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: 112.02 E-value: 2.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 51 GDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQakaanakliv 130
Cdd:cd17643 10 DRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFI---------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 131 tmacfydrvkdLAENGVQIVCVDfavegclhfsvlsgadeslaplvdfsSNDVVALPYSSGTTGLPKGVMLTHKGLITSV 210
Cdd:cd17643 80 -----------LADSGPSLLLTD--------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALF 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 211 AqqmdGQNPNLYYHRNDVILcvlpFFHIYSLN-------SILLCGLRVgaaimIMQKFDI----VALLQLIEKHRISIMP 279
Cdd:cd17643 123 A----ATQRWFGFNEDDVWT----LFHSYAFDfsvweiwGALLHGGRL-----VVVPYEVarspEDFARLLRDEGVTVLN 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 280 IVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLG-KELED-AVREKFPTAILGQGYGMTEAG-----PVLSMSLAFAKEP 352
Cdd:cd17643 190 QTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEaAMLRPwAGRFGLDRPQLVNMYGITETTvhvtfRPLDAADLPAAAA 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 353 FQVKAGACGTVVRnaemkIVDtETGASLPANSSGEICIRGDQIMKGYLN--DLESTKRTIDKEG-----WLHTGDIGFVD 425
Cdd:cd17643 270 SPIGRPLPGLRVY-----VLD-ADGRPVPPGVVGELYVSGAGVARGYLGrpELTAERFVANPFGgpgsrMYRTGDLARRL 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 426 DDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVV 505
Cdd:cd17643 344 PDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKELLP 423
|
490 500
....*....|....*....|....*..
gi 778728825 506 FYKRLKRVFFVNAIPKAPSGKILRKEL 532
Cdd:cd17643 424 DYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
55-532 |
7.91e-26 |
|
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: 110.25 E-value: 7.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 55 TYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAveiakqakaanaklivtmac 134
Cdd:cd17650 14 TYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPA-------------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 135 fyDRVKDLAEngvqivcvdfavegclhfsvlsgadESLAPLVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLITSVAQ-- 212
Cdd:cd17650 74 --ERLQYMLE-------------------------DSGAKLLLTQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAwr 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 213 ---QMDGQNPNLyyhrndviLCVLPF-FHIYSlnSILLCGLRVGAAIMIMQ---KFDIVALLQLIEKHRISIMPIVPPIF 285
Cdd:cd17650 127 reyELDSFPVRL--------LQMASFsFDVFA--GDFARSLLNGGTLVICPdevKLDPAALYDLILKSRITLMESTPALI 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 286 LAIAKSPEFEKYDVSSVRVLKsggapLGKELEDAVREKFPTAILGQG------YGMTEAgpvlSMSLAFAKEPfQVKAGA 359
Cdd:cd17650 197 RPVMAYVYRNGLDLSAMRLLI-----VGSDGCKAQDFKTLAARFGQGmriinsYGVTEA----TIDSTYYEEG-RDPLGD 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 360 CGTV-----VRNAEMKIVDtETGASLPANSSGEICIRGDQIMKGYLNDLESTK---------------RTIDKEGWLHTG 419
Cdd:cd17650 267 SANVpigrpLPNTAMYVLD-ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAerfvenpfapgermyRTGDLARWRADG 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 420 DIGFvdddnelfiVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANggAISEEEVKQF 499
Cdd:cd17650 346 NVEL---------LGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAA--TLNTAELRAF 414
|
490 500 510
....*....|....*....|....*....|...
gi 778728825 500 IAKQVVFYKRLKRVFFVNAIPKAPSGKILRKEL 532
Cdd:cd17650 415 LAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
53-469 |
1.22e-25 |
|
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: 110.98 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 53 VYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIVtm 132
Cdd:cd17641 11 EFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVI-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 133 ACFYDRVKDLAENGVQIVCVDFAV-----------------------EGCLHFSVLSGADESLapLVDFSSNDVVALPYS 189
Cdd:cd17641 89 AEDEEQVDKLLEIADRIPSVRYVIycdprgmrkyddprlisfedvvaLGRALDRRDPGLYERE--VAAGKGEDVAVLCTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 190 SGTTGLPKGVMLTHKGLITSVA--QQMDGQNPNlyyhrnDVILCVLPFF----HIYSLNSILLCGLRV------------ 251
Cdd:cd17641 167 SGTTGKPKLAMLSHGNFLGHCAayLAADPLGPG------DEYVSVLPLPwigeQMYSVGQALVCGFIVnfpeepetmmed 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 252 -----------------GAAIMIMQK-----------FDI---VALLQLIEKHRISIMPIVPPIFLAIAKSPEFE----K 296
Cdd:cd17641 241 lreigptfvllpprvweGIAADVRARmmdatpfkrfmFELgmkLGLRALDRGKRGRPVSLWLRLASWLADALLFRplrdR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 297 YDVSSVRVLKSGGAPLGKELEDavrekFPTAI---LGQGYGMTEAgpvlsMSLAFAKEPFQVKAGACGTVVRNAEMKIVD 373
Cdd:cd17641 321 LGFSRLRSAATGGAALGPDTFR-----FFHAIgvpLKQLYGQTEL-----AGAYTVHRDGDVDPDTVGVPFPGTEVRIDE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 374 TetgaslpanssGEICIRGDQIMKGYLNDLESTKRTIDKEGWLHTGDIGFVDDDNELFIVDRLKELIKF-KAFQVAPAEL 452
Cdd:cd17641 391 V-----------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTsDGTRFSPQFI 459
|
490
....*....|....*..
gi 778728825 453 EALLITHPKLSDAAVIG 469
Cdd:cd17641 460 ENKLKFSPYIAEAVVLG 476
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
51-532 |
2.38e-25 |
|
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: 108.80 E-value: 2.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 51 GDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQakaanakliv 130
Cdd:cd17645 21 GQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYM---------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 131 tmacfydrvkdLAENGVQIVCVDfavegclhfsvlsgadeslaplvdfsSNDVVALPYSSGTTGLPKGVMLTHKGLItsv 210
Cdd:cd17645 91 -----------LADSSAKILLTN--------------------------PDDLAYVIYTSGSTGLPKGVMIEHHNLV--- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 211 aqqmdgqnpNL-YYHRNDVILCVLPFFHIYSLNSI------LLCGLRVGAAIMIM---QKFDIVALLQLIEKHRISIMpi 280
Cdd:cd17645 131 ---------NLcEWHRPYFGVTPADKSLVYASFSFdasaweIFPHLTAGAALHVVpseRRLDLDALNDYFNQEGITIS-- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 281 vppiFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKeledAVREKFPtaiLGQGYGMTEaGPVLSMSLAFAKEPFQVkagAC 360
Cdd:cd17645 200 ----FLPTGAAEQFMQLDNQSLRVLLTGGDKLKK----IERKGYK---LVNNYGPTE-NTVVATSFEIDKPYANI---PI 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 361 GTVVRNAEMKIVDtETGASLPANSSGEICIRGDQIMKGYLNDLESTKRT------IDKEGWLHTGDIG-FVDDDNELFIv 433
Cdd:cd17645 265 GKPIDNTRVYILD-EALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKfivhpfVPGERMYRTGDLAkFLPDGNIEFL- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 434 DRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANggAISEEEVKQFIAKQVVFYkrLKRV 513
Cdd:cd17645 343 GRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPE--EIPHEELREWLKNDLPDY--MIPT 418
|
490 500
....*....|....*....|.
gi 778728825 514 FFV--NAIPKAPSGKILRKEL 532
Cdd:cd17645 419 YFVhlKALPLTANGKVDRKAL 439
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
181-469 |
9.79e-25 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 108.36 E-value: 9.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 181 NDVVALPYSSGTTGLPKGVMLTHKGLITSVA------QQMDGQNPNlyyhrNDVILCVLPFFHIYSlNSILLCGLRVGAA 254
Cdd:PLN02430 220 LDICTIMYTSGTSGDPKGVVLTHEAVATFVRgvdlfmEQFEDKMTH-----DDVYLSFLPLAHILD-RMIEEYFFRKGAS 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 255 I------MIMQKFDIVAL---------------LQLIEKHRISIMPIVPPIFLAIAK---------------SP-----E 293
Cdd:PLN02430 294 VgyyhgdLNALRDDLMELkptllagvprvferiHEGIQKALQELNPRRRLIFNALYKyklawmnrgyshkkaSPmadflA 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 294 FEKYDV---SSVRVLKSGGAPLGKELEDAVREKfPTAILGQGYGMTEA-GPVlsmSLAFAKEPFQVkaGACGTVVRNAEM 369
Cdd:PLN02430 374 FRKVKAklgGRLRLLISGGAPLSTEIEEFLRVT-SCAFVVQGYGLTETlGPT---TLGFPDEMCML--GTVGAPAVYNEL 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 370 KIVDT-ETGAS-LPANSSGEICIRGDQIMKGYLNDLESTKRTIdKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQ- 446
Cdd:PLN02430 448 RLEEVpEMGYDpLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEy 526
|
330 340
....*....|....*....|...
gi 778728825 447 VAPAELEALLITHPKLSDAAVIG 469
Cdd:PLN02430 527 VALEYLENVYGQNPIVEDIWVYG 549
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
164-533 |
9.89e-25 |
|
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: 106.62 E-value: 9.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 164 VLSGADESLApLVDFSSNDVVALPYSSGTTGLPKGVMLTHKGlITSVAQQMdgqNPNLYYHRNDVILCVLPFFHIYSLNS 243
Cdd:cd17653 89 ILRTSGATLL-LTTDSPDDLAYIIFTSGSTGIPKGVMVPHRG-VLNYVSQP---PARLDVGPGSRVAQVLSIAFDACIGE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 244 ILLCGLRVGAAIMIMQKFDIVALLQliekhRISIMPIVPPIfLAIAKSPEFekydvSSVRVLKSGGAPLGKELEDAVRek 323
Cdd:cd17653 164 IFSTLCNGGTLVLADPSDPFAHVAR-----TVDALMSTPSI-LSTLSPQDF-----PNLKTIFLGGEAVPPSLLDRWS-- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 324 fPTAILGQGYGMTEAGPVLSMSLAFAKEPFQVkagacGTVVRNAEMKIVDtETGASLPANSSGEICIRGDQIMKGYLND- 402
Cdd:cd17653 231 -PGRRLYNAYGPTECTISSTMTELLPGQPVTI-----GKPIPNSTCYILD-ADLQPVPEGVVGEICISGVQVARGYLGNp 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 403 -LESTKRTIDKE--GWLH--TGDIGFVDDDNELFIVDRLKELIKFKAFQVapaELEALLIT----HPKLSDAAVIgmpdv 473
Cdd:cd17653 304 aLTASKFVPDPFwpGSRMyrTGDYGRWTEDGGLEFLGREDNQVKVRGFRI---NLEEIEEVvlqsQPEVTQAAAI----- 375
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 474 EAGEVPVAFVMKANggaISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELR 533
Cdd:cd17653 376 VVNGRLVAFVTPET---VDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALR 432
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
55-532 |
1.13e-24 |
|
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: 107.17 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 55 TYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIVTMAC 134
Cdd:cd17656 15 TYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLTQRH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 135 FYDRvkdLAENGVQIVCVDFavegclhfSVLSGADESLAPLVDfsSNDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQM 214
Cdd:cd17656 95 LKSK---LSFNKSTILLEDP--------SISQEDTSNIDYINN--SDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 215 DGQNPNLYyhrNDVILCVLPFFHIySLNSILLCGLRVGAAIMIMQ--KFDIVALLQLIEKHRISIMpIVPPIFLA-IAKS 291
Cdd:cd17656 162 EKTNINFS---DKVLQFATCSFDV-CYQEIFSTLLSGGTLYIIREetKRDVEQLFDLVKRHNIEVV-FLPVAFLKfIFSE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 292 PEFEKYDVSSVRVLKSGGAPL--GKELEDAVREKFPTaiLGQGYGMTEAGPVLSMSlaFAKEPFQVKAGACGTVVRNAEM 369
Cdd:cd17656 237 REFINRFPTCVKHIITAGEQLviTNEFKEMLHEHNVH--LHNHYGPSETHVVTTYT--INPEAEIPELPPIGKPISNTWI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 370 KIVDTEtGASLPANSSGEICIRGDQIMKGYLNDLESTK---------------RTIDKEGWLHTGDIGFvdddnelfiVD 434
Cdd:cd17656 313 YILDQE-QQLQPQGIVGELYISGASVARGYLNRQELTAekffpdpfdpnermyRTGDLARYLPDGNIEF---------LG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 435 RLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANggAISEEEVKQFIAKQVVFYKRLKRVF 514
Cdd:cd17656 383 RADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQ--ELNISQLREYLAKQLPEYMIPSFFV 460
|
490
....*....|....*...
gi 778728825 515 FVNAIPKAPSGKILRKEL 532
Cdd:cd17656 461 PLDQLPLTPNGKVDRKAL 478
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
23-540 |
1.54e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 108.89 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 23 PNHLPLHDYVFQNLSKFASRPCLINGatGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRG 102
Cdd:PRK12316 2000 PRGPGVHQRIAEQAARAPEAIAVVFG--DQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAG 2077
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 103 AIMTAANPFYTAVEIAKQAKAANAKLIVTMACFYDRVKDLAEngvqIVCVDFAVEGCLHfsvlsgADESLAPLVDFSSND 182
Cdd:PRK12316 2078 GAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPAG----VARLPLDRDAEWA------DYPDTAPAVQLAGEN 2147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 183 VVALPYSSGTTGLPKGVMLTHKGLITSVaqQMDGQnpnlyYHRNDVILCVLPF--FHIYSLNSILLCGLRVGAAIMIM-- 258
Cdd:PRK12316 2148 LAYVIYTSGSTGLPKGVAVSHGALVAHC--QAAGE-----RYELSPADCELQFmsFSFDGAHEQWFHPLLNGARVLIRdd 2220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 259 QKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVsSVRVLKSGGAPLGKELEDAVREKFPTAILGQGYGMTEA 338
Cdd:PRK12316 2221 ELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPP-AVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEA 2299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 339 GPVLSMSLAFAKEPFQVKAGACGTVVRNAEMKIVDTETGAsLPANSSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLH- 417
Cdd:PRK12316 2300 VVTPLLWKCRPQDPCGAAYVPIGRALGNRRAYILDADLNL-LAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSAs 2378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 418 ------TGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMpDVEAGEVPVAFVMKANGGAI 491
Cdd:PRK12316 2379 gerlyrTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAAED 2457
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 778728825 492 SEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELRAKLASGA 540
Cdd:PRK12316 2458 LLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQL 2506
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
53-542 |
1.68e-24 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 107.53 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 53 VYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTaanpfytaveiakqakaanakliVTM 132
Cdd:PRK00174 98 KITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHS-----------------------VVF 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 133 ACF-----YDRVKDlAENGVQIVC---------------VDFAVEGCLHF-SVL----SGADESLAPLVDFSSNDVVALP 187
Cdd:PRK00174 155 GGFsaealADRIID-AGAKLVITAdegvrggkpiplkanVDEALANCPSVeKVIvvrrTGGDVDWVEGRDLWWHELVAGA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 188 ------------------YSSGTTGLPKGVMLTHKGLITSVAQQM----DgqnpnlyYHRNDVILC------VLPffHIY 239
Cdd:PRK00174 234 sdecepepmdaedplfilYTSGSTGKPKGVLHTTGGYLVYAAMTMkyvfD-------YKDGDVYWCtadvgwVTG--HSY 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 240 SLNSILLCGlrvgaAIMIMqkF-------DIVALLQLIEKHRISIMPIVP-PIFLAIAKSPEF-EKYDVSSVRVLKSGGA 310
Cdd:PRK00174 305 IVYGPLANG-----ATTLM--FegvpnypDPGRFWEVIDKHKVTIFYTAPtAIRALMKEGDEHpKKYDLSSLRLLGSVGE 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 311 PLGkeledavrekfPTA------ILGQG-------YGMTEAGPVLSMSLAFAkepFQVKAGACGTVVRNAEMKIVDtETG 377
Cdd:PRK00174 378 PIN-----------PEAwewyykVVGGErcpivdtWWQTETGGIMITPLPGA---TPLKPGSATRPLPGIQPAVVD-EEG 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 378 ASLPANSSGEICIR----GdqIMKGYLNDLESTKRTIDKE--GWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAE 451
Cdd:PRK00174 443 NPLEGGEGGNLVIKdpwpG--MMRTIYGDHERFVKTYFSTfkGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAE 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 452 LEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEE---EVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKIL 528
Cdd:PRK00174 521 IESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDElrkELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIM 600
|
570
....*....|....
gi 778728825 529 RKELRaKLASGAYN 542
Cdd:PRK00174 601 RRILR-KIAEGEEI 613
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
168-532 |
1.76e-24 |
|
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: 106.25 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 168 ADESLAPLVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLITSV--------AQQMDGqnpnlyyhrndvILCVLPF---F 236
Cdd:cd12115 92 LEDAQARLVLTDPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLqwaaaafsAEELAG------------VLASTSIcfdL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 237 HIYSLNSILLCGLRVGAAIMIMQKFDIVALLQliekhrISIMPIVPPiflAIAKSPEFEKYdVSSVRVLKSGGAPLGKEL 316
Cdd:cd12115 160 SVFELFGPLATGGKVVLADNVLALPDLPAAAE------VTLINTVPS---AAAELLRHDAL-PASVRVVNLAGEPLPRDL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 317 EDAVREKFPTAILGQGYGMTEAgpvLSMSLAFAKEPFQVKAGACGTVVRNAEMKIVDtETGASLPANSSGEICIRGDQIM 396
Cdd:cd12115 230 VQRLYARLQVERVVNLYGPSED---TTYSTVAPVPPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVPGELYIGGAGVA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 397 KGYLNDLESTK---RTIDKEGWLH---TGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGM 470
Cdd:cd12115 306 RGYLGRPGLTAerfLPDPFGPGARlyrTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAI 385
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 778728825 471 PDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKEL 532
Cdd:cd12115 386 GDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
181-442 |
2.66e-24 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 107.03 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 181 NDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQMDG-QNPNLYYHRNDVILCVLPFFHIYSlNSILLCGLRVGAAIMIMQ 259
Cdd:PLN02614 223 SDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLlKSANAALTVKDVYLSYLPLAHIFD-RVIEECFIQHGAAIGFWR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 260 KfDIVALLQLIEKHRISIMPIVPPI----------------FLA---------------------IAKSPEFEKYDVS-- 300
Cdd:PLN02614 302 G-DVKLLIEDLGELKPTIFCAVPRVldrvysglqkklsdggFLKkfvfdsafsykfgnmkkgqshVEASPLCDKLVFNkv 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 301 ------SVRVLKSGGAPLGKELEDAVREKFPTAILgQGYGMTEagpvlSMSLAFAKEPFQVKA-GACGTVVRNAEMKI-- 371
Cdd:PLN02614 381 kqglggNVRIILSGAAPLASHVESFLRVVACCHVL-QGYGLTE-----SCAGTFVSLPDELDMlGTVGPPVPNVDIRLes 454
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 778728825 372 VDTETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIdKEGWLHTGDIGFVDDDNELFIVDRLKELIKF 442
Cdd:PLN02614 455 VPEMEYDALASTPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRKKNIFKL 524
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
55-532 |
2.98e-24 |
|
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: 105.41 E-value: 2.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 55 TYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIVTMAc 134
Cdd:cd17652 14 TYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLTTP- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 135 fydrvkdlaengvqivcvdfavegclhfsvlsgadESLAPLVdfssndvvalpYSSGTTGLPKGVMLTHKGLITSVAQQM 214
Cdd:cd17652 93 -----------------------------------DNLAYVI-----------YTSGSTGRPKGVVVTHRGLANLAAAQI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 215 DGQNPNlyyHRNDVILCVLPFF--HIYSLNSILLCglrvGAAIMIMQKFDIVA---LLQLIEKHRISIMpIVPPIFLAiA 289
Cdd:cd17652 127 AAFDVG---PGSRVLQFASPSFdaSVWELLMALLA----GATLVLAPAEELLPgepLADLLREHRITHV-TLPPAALA-A 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 290 KSPEfekyDVSSVRVLKSGGAPLGKELedaVREKFPTAILGQGYGMTEAGPVLSMSLAFAKEPfqvkAGACGTVVRNAEM 369
Cdd:cd17652 198 LPPD----DLPDLRTLVVAGEACPAEL---VDRWAPGRRMINAYGPTETTVCATMAGPLPGGG----VPPIGRPVPGTRV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 370 KIVDtETGASLPANSSGEICIRGDQIMKGYLN--DLESTKRTIDKEGWL-----HTGDIGFVDDDNELFIVDRLKELIKF 442
Cdd:cd17652 267 YVLD-ARLRPVPPGVPGELYIAGAGLARGYLNrpGLTAERFVADPFGAPgsrmyRTGDLARWRADGQLEFLGRADDQVKI 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 443 KAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKA 522
Cdd:cd17652 346 RGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLT 425
|
490
....*....|
gi 778728825 523 PSGKILRKEL 532
Cdd:cd17652 426 PNGKLDRRAL 435
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
179-460 |
4.90e-24 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 106.35 E-value: 4.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 179 SSNDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQMDGQnPNLyyHRNDVILCVLPFFHIYSLNS-ILLCGlrVGAAI-- 255
Cdd:PLN02387 248 SPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVV-PKL--GKNDVYLAYLPLAHILELAAeSVMAA--VGAAIgy 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 256 ---MIM----------QKFDIVALlqliekhRISIMPIVPPIF------------------------------LAI---- 288
Cdd:PLN02387 323 gspLTLtdtsnkikkgTKGDASAL-------KPTLMTAVPAILdrvrdgvrkkvdakgglakklfdiaykrrlAAIegsw 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 289 --AKSPEFEKYDV-----------SSVRVLKSGGAPLGKELEDAVREKFpTAILGQGYGMTE--AGPVLSmslafakEPF 353
Cdd:PLN02387 396 fgAWGLEKLLWDAlvfkkiravlgGRIRFMLSGGAPLSGDTQRFINICL-GAPIGQGYGLTEtcAGATFS-------EWD 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 354 QVKAGACGTVVRNAEMKIVDTETGASLPANS---SGEICIRGDQIMKGYLNDLESTKRT--IDKEG--WLHTGDIGFVDD 426
Cdd:PLN02387 468 DTSVGRVGPPLPCCYVKLVSWEEGGYLISDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHP 547
|
330 340 350
....*....|....*....|....*....|....*
gi 778728825 427 DNELFIVDRLKELIKFKAFQ-VAPAELEALLITHP 460
Cdd:PLN02387 548 DGCLEIIDRKKDIVKLQHGEyVSLGKVEAALSVSP 582
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
172-540 |
1.44e-23 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 105.43 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 172 LAPLVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLITSVAQ---QMDgqnpnlyYHRNDVILCVLPFFHIYslnsillcG 248
Cdd:PRK06814 784 LVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQvaaRID-------FSPEDKVFNALPVFHSF--------G 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 249 LRVGAAIMIMQKFDIV---------ALLQLIEKHRISIMpIVPPIFLA-IAKSPEfeKYDVSSVRVLKSGGAPLGKELED 318
Cdd:PRK06814 849 LTGGLVLPLLSGVKVFlypsplhyrIIPELIYDTNATIL-FGTDTFLNgYARYAH--PYDFRSLRYVFAGAEKVKEETRQ 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 319 AVREKFPTAILgQGYGMTEAGPVLSMSlafakEPFQVKAGACGTVVRNAEMKIVDTETgaslpANSSGEICIRGDQIMKG 398
Cdd:PRK06814 926 TWMEKFGIRIL-EGYGVTETAPVIALN-----TPMHNKAGTVGRLLPGIEYRLEPVPG-----IDEGGRLFVRGPNVMLG 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 399 YLndLESTKRTID--KEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAG 476
Cdd:PRK06814 995 YL--RAENPGVLEppADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKG 1072
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 778728825 477 EVPVAFVMKAngGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKI----LRKELRAKLASGA 540
Cdd:PRK06814 1073 ERIILLTTAS--DATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKIdyvaVTKLAEEAAAKPE 1138
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
65-536 |
1.86e-23 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 103.93 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 65 RVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAAN-AKLIVTMACFYDRvKDLA 143
Cdd:PRK05857 53 GLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDpAAALVAPGSKMAS-SAVP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 144 ENGVQIVCVDFAVEGCLHFSVLSGADESLAPLVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLItSVAQQMDGQNPN-LY 222
Cdd:PRK05857 132 EALHSIPVIAVDIAAVTRESEHSLDAASLAGNADQGSEDPLAMIFTSGTTGEPKAVLLANRTFF-AVPDILQKEGLNwVT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 223 YHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKfdIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSV 302
Cdd:PRK05857 211 WVVGETTYSPLPATHIGGLWWILTCLMHGGLCVTGGEN--TTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 303 RVLKSGGAplgKELEDAVREKFPTAI-LGQGYGMTEAG------PVLSMSLAfakepfQVKAGACGTVVRNAEMKIVDTE 375
Cdd:PRK05857 289 RLVGYGGS---RAIAADVRFIEATGVrTAQVYGLSETGctalclPTDDGSIV------KIEAGAVGRPYPGVDVYLAATD 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 376 TG-----ASLPANSSGEICIRGDQIMKGYLNDLESTkRTIDKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPA 450
Cdd:PRK05857 360 GIgptapGAGPSASFGTLWIKSPANMLGYWNNPERT-AEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPD 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 451 ELEALLITHPKLSDAAVIGMPDVEAGE-VPVAFVMKANGGAISEEEVKQFIA----KQVVFYKRLKRVFFVNAIPKAPSG 525
Cdd:PRK05857 439 EVDRIAEGVSGVREAACYEIPDEEFGAlVGLAVVASAELDESAARALKHTIAarfrRESEPMARPSTIVIVTDIPRTQSG 518
|
490
....*....|.
gi 778728825 526 KILRKELRAKL 536
Cdd:PRK05857 519 KVMRASLAAAA 529
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
55-469 |
2.49e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 103.97 E-value: 2.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 55 TYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTaveiakqakaanaklivTMAC 134
Cdd:PRK12582 82 TYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYS-----------------LMSH 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 135 FYDRVKDLAE------------------------NGVQIVCVDFAVEG--CLHFSVL------SGADESLAPLvdfsSND 182
Cdd:PRK12582 145 DHAKLKHLFDlvkprvvfaqsgapfaralaaldlLDVTVVHVTGPGEGiaSIAFADLaatpptAAVAAAIAAI----TPD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 183 VVA-LPYSSGTTGLPKGVMLTHkGLITSVAQQMDGQNPNLYYHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMqkf 261
Cdd:PRK12582 221 TVAkYLFTSGSTGMPKAVINTQ-RMMCANIAMQEQLRPREPDPPPPVSLDWMPWNHTMGGNANFNGLLWGGGTLYID--- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 262 DIVALLQLIEK-----HRIS--IMPIVPPIFLAIAksPEFEKYDV------SSVRVLKSGGAPLGKELED-----AVREK 323
Cdd:PRK12582 297 DGKPLPGMFEEtirnlREISptVYGNVPAGYAMLA--EAMEKDDAlrrsffKNLRLMAYGGATLSDDLYErmqalAVRTT 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 324 FPTAILGQGYGMTEAGPVlSMSLAFAKEpfqvKAGACGTVVRNAEMKIVdtetgaslPANSSGEICIRGDQIMKGYLNDL 403
Cdd:PRK12582 375 GHRIPFYTGYGATETAPT-TTGTHWDTE----RVGLIGLPLPGVELKLA--------PVGDKYEVRVKGPNVTPGYHKDP 441
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 778728825 404 ESTKRTIDKEGWLHTGDIG-FVD-DDNELFIV--DRLKELIKFKA---FQVAPAELEALLITHPKLSDAAVIG 469
Cdd:PRK12582 442 ELTAAAFDEEGFYRLGDAArFVDpDDPEKGLIfdGRVAEDFKLSTgtwVSVGTLRPDAVAACSPVIHDAVVAG 514
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
23-540 |
3.40e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 104.65 E-value: 3.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 23 PNHLPLHDYVFQNLSKFASRPCLINGATgdVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRG 102
Cdd:PRK12316 508 PLQRGVHRLFEEQVERTPEAPALAFGEE--TLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAG 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 103 AIMTAANPFYTAVEIAKQAKAANAKLIVTMAcFYDRVKDLAEnGVQIVCVDFAVegclhfSVLSGADESlAPLVDFSSND 182
Cdd:PRK12316 586 GAYVPLDPEYPAERLAYMLEDSGVQLLLSQS-HLGRKLPLAA-GVQVLDLDRPA------AWLEGYSEE-NPGTELNPEN 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 183 VVALPYSSGTTGLPKGVMLTHKGLITSV--AQQMDGQNPNlyyhrnDVILCVLPFFHIYSLNSILLcGLRVGAAIMIM-- 258
Cdd:PRK12316 657 LAYVIYTSGSTGKPKGAGNRHRALSNRLcwMQQAYGLGVG------DTVLQKTPFSFDVSVWEFFW-PLMSGARLVVAap 729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 259 -QKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEkyDVSSVRVLKSGGAPLGKELEDAVREKFPTAILGQGYGMTE 337
Cdd:PRK12316 730 gDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVA--SCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTE 807
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 338 AGPVLSMSLAfakepfqVKAGA----CGTVVRNAEMKIVDTETGAsLPANSSGEICIRGDQIMKGYLNDLESTKRT---- 409
Cdd:PRK12316 808 AAIDVTHWTC-------VEEGGdsvpIGRPIANLACYILDANLEP-VPVGVLGELYLAGRGLARGYHGRPGLTAERfvps 879
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 410 --IDKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIgmpdVEAGEVPVAFVMKAN 487
Cdd:PRK12316 880 pfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGKQLVGYVVLES 955
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 778728825 488 GGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELRAKLASGA 540
Cdd:PRK12316 956 EGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVA 1008
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
51-532 |
1.03e-22 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 103.32 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 51 GDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIV 130
Cdd:PRK05691 1154 GGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLL 1233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 131 TMACFYDRVKdlAENGVQIVCVDfavegCLHFSVLSgadeSLAPLVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLitsv 210
Cdd:PRK05691 1234 TQSHLLERLP--QAEGVSAIALD-----SLHLDSWP----SQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAAL---- 1298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 211 AQQMDGQNPNLYYHRNDVILCVLPF-FHIyslnSILLC--GLRVGAAIMIM---QKFDIVALLQLIEKHRISIMPIVPPI 284
Cdd:PRK05691 1299 AERLQWMQATYALDDSDVLMQKAPIsFDV----SVWECfwPLITGCRLVLAgpgEHRDPQRIAELVQQYGVTTLHFVPPL 1374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 285 FLAIAKSPEFEkyDVSSVRVLKSGGAPLGKELEDAVREKFPTAILGQGYGMTEAgpvlsmSLAFAKEPFQVKAGACGTVV 364
Cdd:PRK05691 1375 LQLFIDEPLAA--ACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTET------AINVTHWQCQAEDGERSPIG 1446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 365 R---NAEMKIVDTETgASLPANSSGEICIRGDQIMKGYLND--LESTKRTIDKEG-----WLHTGDIGFVDDDNELFIVD 434
Cdd:PRK05691 1447 RplgNVLCRVLDAEL-NLLPPGVAGELCIGGAGLARGYLGRpaLTAERFVPDPLGedgarLYRTGDRARWNADGALEYLG 1525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 435 RLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVeAGEVPVAFVMKANGGAISEEEVKQFIAKQVVFYKRLKRVF 514
Cdd:PRK05691 1526 RLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGA-AGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLI 1604
|
490
....*....|....*...
gi 778728825 515 FVNAIPKAPSGKILRKEL 532
Cdd:PRK05691 1605 RLDQMPLGPSGKLDRRAL 1622
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
23-541 |
1.13e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 103.11 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 23 PNHLPLHDYVFQNLSKFASRPCLINGatGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRG 102
Cdd:PRK12316 4548 PATRCVHQLVAERARMTPDAVAVVFD--EEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAG 4625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 103 AIMTAANPFYTAVEIAKQAKAANAKLIVTMACFYDRVKdlAENGVQIVCVDFAVEgclhfsvLSGADESlAPLVDFSSND 182
Cdd:PRK12316 4626 GAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLP--IPDGLASLALDRDED-------WEGFPAH-DPAVRLHPDN 4695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 183 VVALPYSSGTTGLPKGVMLTHKGLI--TSVAQQMDGQNPnlyyhrNDVILCVLPF-FHIYSLNsiLLCGLRVGAAIMIM- 258
Cdd:PRK12316 4696 LAYVIYTSGSTGRPKGVAVSHGSLVnhLHATGERYELTP------DDRVLQFMSFsFDGSHEG--LYHPLINGASVVIRd 4767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 259 -QKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEfEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILGQGYGMTE 337
Cdd:PRK12316 4768 dSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAE-RDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTE 4846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 338 AGPVLSMSLAFAKEPFQVKAGACGTVVRNAEMKIVDTEtGASLPANSSGEICIRGDQIMKGYLNDLEST-KRTI----DK 412
Cdd:PRK12316 4847 TTVTVLLWKARDGDACGAAYMPIGTPLGNRSGYVLDGQ-LNPLPVGVAGELYLGGEGVARGYLERPALTaERFVpdpfGA 4925
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 413 EG--WLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVeAGEVPVAFVMKAngga 490
Cdd:PRK12316 4926 PGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGA-VGKQLVGYVVPQ---- 5000
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 778728825 491 isEEEVKQFIAKQVVFYKRLKR--------------VFFVNAIPKAPSGKILRK---ELRAKLASGAY 541
Cdd:PRK12316 5001 --DPALADADEAQAELRDELKAalrerlpeymvpahLVFLARMPLTPNGKLDRKalpQPDASLLQQAY 5066
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
55-538 |
1.38e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 102.93 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 55 TYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIVTMAC 134
Cdd:PRK12467 1601 TYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSH 1680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 135 FYDRVKdlAENGVQIVCVDFAVEGclhfsvLSGADESlAPLVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLI-----TS 209
Cdd:PRK12467 1681 LQARLP--LPDGLRSLVLDQEDDW------LEGYSDS-NPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVnrlcaTQ 1751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 210 VAQQMDGQNPNLYYHRNDVILCVLPFFHIyslnsiLLCGLRVGAAIMIMQKfDIVALLQLIEKHRISIMPIVPPIFLAIA 289
Cdd:PRK12467 1752 EAYQLSAADVVLQFTSFAFDVSVWELFWP------LINGARLVIAPPGAHR-DPEQLIQLIERQQVTTLHFVPSMLQQLL 1824
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 290 KSPEFEKyDVSSVRVLKSGGAPLGKELEDAVREKFPTAILGQGYGMTEAGPVLSMSLAFAKEPFQVKAGACGTVVRNAEM 369
Cdd:PRK12467 1825 QMDEQVE-HPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCRRKDLEGRDSVPIGQPIANLST 1903
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 370 KIVDtETGASLPANSSGEICIRGDQIMKGYLNDLEST-KRTI-----DKEGWLH-TGDIGFVDDDNELFIVDRLKELIKF 442
Cdd:PRK12467 1904 YILD-ASLNPVPIGVAGELYLGGVGLARGYLNRPALTaERFVadpfgTVGSRLYrTGDLARYRADGVIEYLGRIDHQVKI 1982
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 443 KAFQVAPAELEALLITHPKLSDAAVIGMpDVEAGEVPVAFVMKANGGAISEEEvkqfiaKQVVFYKRLKR---------- 512
Cdd:PRK12467 1983 RGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVPTDPGLVDDDE------AQVALRAILKNhlkaslpeym 2055
|
490 500 510
....*....|....*....|....*....|
gi 778728825 513 ----VFFVNAIPKAPSGKILRKELRAKLAS 538
Cdd:PRK12467 2056 vpahLVFLARMPLTPNGKLDRKALPAPDAS 2085
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1-440 |
1.53e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 101.73 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 1 MAFEsnetNEFIFRSKlpdIHIPNHLPLHDYVFQNL----SKFASRpcLINGATGDVYTYHDV---QLTARR--VAAGLH 71
Cdd:PRK07769 3 MAFH----NPFDVNGK---IRFPPNTNLVRHVERWAkvrgDKLAYR--FLDFSTERDGVARDLtwsQFGARNraVGARLQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 72 NLGiKKGDVVMNLLPNSPEFVFTFLGASYRGAImtaANPFYTAVE------IAKQAKAANAKLIVTMACFYDRVKDL--- 142
Cdd:PRK07769 74 QVT-KPGDRVAILAPQNLDYLIAFFGALYAGRI---AVPLFDPAEpghvgrLHAVLDDCTPSAILTTTDSAEGVRKFfra 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 143 --AENGVQIVCVDfavegclhfSVLSGADESLAPlVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQMDGqnpn 220
Cdd:PRK07769 150 rpAKERPRVIAVD---------AVPDEVGATWVP-PEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDA---- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 221 LYYHRNDVILCVLPFFHIYSLNSILLCGLrVGAAIMIMQKfdiVALLQliEKHR-ISIMPIVPP-IFLAIAKSPEFeKYD 298
Cdd:PRK07769 216 LEGQEGDRGVSWLPFFHDMGLITVLLPAL-LGHYITFMSP---AAFVR--RPGRwIRELARKPGgTGGTFSAAPNF-AFE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 299 VSSVRVL-KSGGAPL----------GKE-LEDAVREKF----------PTAIlGQGYGMTEAGPVLSmSLAFAKEP---- 352
Cdd:PRK07769 289 HAAARGLpKDGEPPLdlsnvkgllnGSEpVSPASMRKFneafapyglpPTAI-KPSYGMAEATLFVS-TTPMDEEPtviy 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 353 -----------FQVKAGA--------CGTVVRNAEMKIVDTETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTI--- 410
Cdd:PRK07769 367 vdrdelnagrfVEVPADApnavaqvsAGKVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqni 446
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 778728825 411 --------------DKEGWLHTGDIGfVDDDNELFIVDRLKELI 440
Cdd:PRK07769 447 lksrlseshaegapDDALWVRTGDYG-VYFDGELYITGRVKDLV 489
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
51-483 |
2.66e-22 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 99.56 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 51 GDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAkqakaanakliv 130
Cdd:PRK09029 26 DEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLE------------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 131 tmacfydrvKDLAENGVQIVcvdFAVEGCLHFSVLSGADESL---APLVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLI 207
Cdd:PRK09029 94 ---------ELLPSLTLDFA---LVLEGENTFSALTSLHLQLvegAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 208 TS---VAQQMDgqnpnlyYHRNDVILCVLPFFHIySLNSILLCGLRVGAAIMIMQKFDIVALL-----------QLiekH 273
Cdd:PRK09029 162 ASaegVLSLMP-------FTAQDSWLLSLPLFHV-SGQGIVWRWLYAGATLVVRDKQPLEQALagcthaslvptQL---W 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 274 RISIMPIVPpiflaiakspefekydVSSVRVLKsGGAPLGKELEDAVREKFPTAILGqgYGMTEAGpvlsmSLAFAKEPf 353
Cdd:PRK09029 231 RLLDNRSEP----------------LSLKAVLL-GGAAIPVELTEQAEQQGIRCWCG--YGLTEMA-----STVCAKRA- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 354 QVKAGAcGTVVRNAEMKIVDtetgaslpanssGEICIRGDQIMKGYLNDLESTKRTiDKEGWLHTGDIGFVDDdNELFIV 433
Cdd:PRK09029 286 DGLAGV-GSPLPGREVKLVD------------GEIWLRGASLALGYWRQGQLVPLV-NDEGWFATRDRGEWQN-GELTIL 350
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 778728825 434 DRLKELikfkaF-----QVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFV 483
Cdd:PRK09029 351 GRLDNL-----FfsggeGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVV 400
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
186-534 |
5.67e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 98.18 E-value: 5.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 186 LPYSSGTTGLPKgvmlthkgLI----TSVAQQMDGQNPNLYYHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQ-- 259
Cdd:PRK08308 106 LQYSSGTTGEPK--------LIrrswTEIDREIEAYNEALNCEQDETPIVACPVTHSYGLICGVLAALTRGSKPVIITnk 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 260 --KFdIVALLQLIEKHrisIMPIVPPIFLAIAK-SPEFEKYDvssvRVLKSGgAPLGKELEDAVREKfpTAILGQGYGMT 336
Cdd:PRK08308 178 npKF-ALNILRNTPQH---ILYAVPLMLHILGRlLPGTFQFH----AVMTSG-TPLPEAWFYKLRER--TTYMMQQYGCS 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 337 EAGPV-LSMSLAFAKEpfqvkagaCGTVVRNAEMKIVDTEtgaslpaNSSGEICIRGDQimkgylndlestkRTIdkegw 415
Cdd:PRK08308 247 EAGCVsICPDMKSHLD--------LGNPLPHVSVSAGSDE-------NAPEEIVVKMGD-------------KEI----- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 416 lHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGE-VPVAFVMKangGAISEE 494
Cdd:PRK08308 294 -FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGErVKAKVISH---EEIDPV 369
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 778728825 495 EVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELRA 534
Cdd:PRK08308 370 QLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLEL 409
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
42-532 |
8.06e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 100.24 E-value: 8.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 42 RPCLINGatGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQA 121
Cdd:PRK12467 528 RPALVFG--EQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYML 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 122 KAANAKLIVTMACFYDRVkDLAEnGVQIVCVDFA---VEGClhfsvlSGADESLAplvdFSSNDVVALPYSSGTTGLPKG 198
Cdd:PRK12467 606 DDSGVRLLLTQSHLLAQL-PVPA-GLRSLCLDEPadlLCGY------SGHNPEVA----LDPDNLAYVIYTSGSTGQPKG 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 199 VMLTHKGL---ITSVAQQMDgqnpnlyYHRNDVILCVLPF-FHIYSLnsILLCGLRVGAAIMIMQK---FDIVALLQLIE 271
Cdd:PRK12467 674 VAISHGALanyVCVIAERLQ-------LAADDSMLMVSTFaFDLGVT--ELFGALASGATLHLLPPdcaRDAEAFAALMA 744
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 272 KHRISIMPIVPPIFLAIAKSPEFEKydVSSVRVLKSGGAPLGKELEDAVREKFPTAILGQGYGMTEAgPVLSMSLAFAKE 351
Cdd:PRK12467 745 DQGVTVLKIVPSHLQALLQASRVAL--PRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTET-TVGVSTYELSDE 821
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 352 PFQVKAGACGTVVRNAEMKIVDTETgASLPANSSGEICIRGDQIMKGYLN--DLESTKRTIDKEG-----WLHTGDIGFV 424
Cdd:PRK12467 822 ERDFGNVPIGQPLANLGLYILDHYL-NPVPVGVVGELYIGGAGLARGYHRrpALTAERFVPDPFGadggrLYRTGDLARY 900
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 425 DDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDvEAGEVPVAFVMKANG-----GAISEEEVKQF 499
Cdd:PRK12467 901 RADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPG-DAGLQLVAYLVPAAVadgaeHQATRDELKAQ 979
|
490 500 510
....*....|....*....|....*....|...
gi 778728825 500 IAKQVVFYKRLKRVFFVNAIPKAPSGKILRKEL 532
Cdd:PRK12467 980 LRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
308-533 |
9.20e-22 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 98.14 E-value: 9.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 308 GGAPLGKEL-EDAVREKFPtaiLGQGYGMTEAGpvlSMSLAFAKEPFQVKAGACGTVVRNAEMKIVDTETGaslpanssg 386
Cdd:PRK07445 238 GGAPAWPSLlEQARQLQLR---LAPTYGMTETA---SQIATLKPDDFLAGNNSSGQVLPHAQITIPANQTG--------- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 387 EICIRGDQIMKGYLNDLestkrtIDKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAA 466
Cdd:PRK07445 303 NITIQAQSLALGYYPQI------LDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVC 376
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 778728825 467 VIGMPDVEAGEVPVAFVMKANGgAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELR 533
Cdd:PRK07445 377 VLGLPDPHWGEVVTAIYVPKDP-SISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
28-538 |
2.86e-21 |
|
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: 96.84 E-value: 2.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 28 LHDYVFQNLSkfaSRP--CLINGATGDVyTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIM 105
Cdd:cd05918 1 VHDLIEERAR---SQPdaPAVCAWDGSL-TYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 106 TAANPFYTAveiakqakaanaklivtmacfyDRVKDLAEngvqivcvdfAVEGCLhfsVLSGADESLAPLVdfssndvva 185
Cdd:cd05918 77 VPLDPSHPL----------------------QRLQEILQ----------DTGAKV---VLTSSPSDAAYVI--------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 186 lpYSSGTTGLPKGVMLTHKGLITSvaqqMDGQNPNLYYHRNDVILCvlpfFHIY----SLNSIlLCGLRVGAAIMIMQKF 261
Cdd:cd05918 113 --FTSGSTGKPKGVVIEHRALSTS----ALAHGRALGLTSESRVLQ----FASYtfdvSILEI-FTTLAAGGCLCIPSEE 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 262 DIV-ALLQLIEKHRISIMPIVPPifLAIAKSPEfekyDVSSVRVLKSGGAPLGKEL----EDAVRekfptaiLGQGYGMT 336
Cdd:cd05918 182 DRLnDLAGFINRLRVTWAFLTPS--VARLLDPE----DVPSLRTLVLGGEALTQSDvdtwADRVR-------LINAYGPA 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 337 EAGPVLSMSLAFAKEPFQVKAGACGTVVRnaemkIVDTETGASL-PANSSGEICIRGDQIMKGYLNDLESTKRT-IDKEG 414
Cdd:cd05918 249 ECTIAATVSPVVPSTDPRNIGRPLGATCW-----VVDPDNHDRLvPIGAVGELLIEGPILARGYLNDPEKTAAAfIEDPA 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 415 WLH------------TGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHP---KLSDAAVIGMPDVEAGEVP 479
Cdd:cd05918 324 WLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLpgaKEVVVEVVKPKDGSSSPQL 403
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 778728825 480 VAFVMKANGGAISEEEVKQFIAKQVVFYKRLKRV-----------------FFVNAIPKAPSGKILRKELRAKLAS 538
Cdd:cd05918 404 VAFVVLDGSSSGSGDGDSLFLEPSDEFRALVAELrsklrqrlpsymvpsvfLPLSHLPLTASGKIDRRALRELAES 479
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
23-532 |
4.45e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 97.92 E-value: 4.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 23 PNHLPLHDYVFQNLSKFASRPCLINGatGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRG 102
Cdd:PRK12467 3092 PSERLVHQLIEAQVARTPEAPALVFG--DQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAG 3169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 103 AIMTAANPFYTAVEIAKQAKAANAKLIVTMACFYDRVKDLAenGVQIVCVDFAVEGCLhfsvlsgADESLAPLVDfsSND 182
Cdd:PRK12467 3170 GAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPAPA--GDTALTLDRLDLNGY-------SENNPSTRVM--GEN 3238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 183 VVALPYSSGTTGLPKGVMLTHKGLI--TSVAQQ---MDGqnpnlyyhrNDVILCVLPF-FHIYSLNSI--LLCGLRVgaA 254
Cdd:PRK12467 3239 LAYVIYTSGSTGKPKGVGVRHGALAnhLCWIAEayeLDA---------NDRVLLFMSFsFDGAQERFLwtLICGGCL--V 3307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 255 IMIMQKFDIVALLQLIEKHRISIMPIVPPIFLAIAkspEFEK-YDVSSVRVLKSGGAPLGKELEDAVREKFPTAILGQGY 333
Cdd:PRK12467 3308 VRDNDLWDPEELWQAIHAHRISIACFPPAYLQQFA---EDAGgADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGY 3384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 334 GMTEAGPVLSMSLAFAKEPFQVKAGACGTVVRNAEMKIVDTETGaSLPANSSGEICIRGDQIMKGYLN--DLeSTKRTI- 410
Cdd:PRK12467 3385 GPTEAVVTVTLWKCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLN-PVPVGVAGELYIGGVGLARGYHQrpSL-TAERFVa 3462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 411 ----DKEGWLH-TGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMpDVEAGEVPVAFVMK 485
Cdd:PRK12467 3463 dpfsGSGGRLYrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVP 3541
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 778728825 486 ANGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKEL 532
Cdd:PRK12467 3542 ADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
182-538 |
9.40e-21 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 93.96 E-value: 9.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 182 DVVALPYS-SGTTGLPKGVMLTHKGLITS---VAQQMDGqnPNLYyhrndviLCVLPFFHIYSLnSILLCGLRVGA---A 254
Cdd:PRK07824 35 DDVALVVAtSGTTGTPKGAMLTAAALTASadaTHDRLGG--PGQW-------LLALPAHHIAGL-QVLVRSVIAGSepvE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 255 IMIMQKFDIVALLQLI-----EKHRISIMPIvppiflAIAKSPEfekyDVSSVRVLKS------GGAPLGKELEDAVREK 323
Cdd:PRK07824 105 LDVSAGFDPTALPRAVaelggGRRYTSLVPM------QLAKALD----DPAATAALAEldavlvGGGPAPAPVLDAAAAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 324 FPTAIlgQGYGMTEAgpvlsmslafakepfqvkAGAC---GTVVRNAEMKIVDtetgaslpanssGEICIRGDQIMKGYL 400
Cdd:PRK07824 175 GINVV--RTYGMSET------------------SGGCvydGVPLDGVRVRVED------------GRIALGGPTLAKGYR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 401 NDLESTkrTIDKEGWLHTGDIGFVDDdNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPV 480
Cdd:PRK07824 223 NPVDPD--PFAEPGWFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVV 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 778728825 481 AFVMKANGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELRAKLAS 538
Cdd:PRK07824 300 AAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRFAG 357
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
55-469 |
1.39e-20 |
|
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: 95.19 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 55 TYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLI---VT 131
Cdd:cd05921 27 TYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLMSQDLAKLKHLFELLkpgLV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 132 MA----CFYDRVKDLAENGVQIVCVDFAVEG--CLHFSVLSG--ADESLAPLVDFSSNDVVA-LPYSSGTTGLPKGVMLT 202
Cdd:cd05921 107 FAqdaaPFARALAAIFPLGTPLVVSRNAVAGrgAISFAELAAtpPTAAVDAAFAAVGPDTVAkFLFTSGSTGLPKAVINT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 203 HkGLITSVAQQMDGQNPnlyYHRND--VILCVLPFFHIYSLNSILLCGLRVGAAIMIMQKFDIVALLQLIEKHRISIMPI 280
Cdd:cd05921 187 Q-RMLCANQAMLEQTYP---FFGEEppVLVDWLPWNHTFGGNHNFNLVLYNGGTLYIDDGKPMPGGFEETLRNLREISPT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 281 ----VPPIFLAIAksPEFEKYDV------SSVRVLKSGGAPLGKELED-----AVREKFPTAILGQGYGMTEAGPvlsmS 345
Cdd:cd05921 263 vyfnVPAGWEMLV--AALEKDEAlrrrffKRLKLMFYAGAGLSQDVWDrlqalAVATVGERIPMMAGLGATETAP----T 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 346 LAFAKEPfQVKAGACGTVVRNAEMKIVdtetgaslPANSSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLHTGD-IGFV 424
Cdd:cd05921 337 ATFTHWP-TERSGLIGLPAPGTELKLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDaAKLA 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 778728825 425 DDDNE---LFIVDRLKELIKFKA---FQVAPAELEALLITHPKLSDAAVIG 469
Cdd:cd05921 408 DPDDPakgLVFDGRVAEDFKLASgtwVSVGPLRARAVAACAPLVHDAVVAG 458
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
176-529 |
1.89e-20 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 95.19 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 176 VDFSSNDVVALPYSSGTTGLPKGVMLTHKGLITSVA---QQMDGQNPNLYYHRNDVILCVLpfFHIYslnsilLCGLRVG 252
Cdd:PTZ00237 249 VPVESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKyywRSIIEKDIPTVVFSHSSIGWVS--FHGF------LYGSLSL 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 253 AAIMIMQKFDIVA-------LLQLIEKHRISIMPIVPPIFLAIAKS-PEFE----KYDVSSVRVLKSGGAPLGKELEDAV 320
Cdd:PTZ00237 321 GNTFVMFEGGIIKnkhieddLWNTIEKHKVTHTLTLPKTIRYLIKTdPEATiirsKYDLSNLKEIWCGGEVIEESIPEYI 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 321 REKFPTAILGqGYGMTEAGPVLSMSLAFAKEPFQvkagACGTVVRNAEMKIVdTETGASLPANSSGEICIR----GDQIM 396
Cdd:PTZ00237 401 ENKLKIKSSR-GYGQTEIGITYLYCYGHINIPYN----ATGVPSIFIKPSIL-SEDGKELNVNEIGEVAFKlpmpPSFAT 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 397 KGYLNDlESTKRTIDK-EGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEA 475
Cdd:PTZ00237 475 TFYKND-EKFKQLFSKfPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDC 553
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 778728825 476 GEVPVAFVMKANGGAIS-------EEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILR 529
Cdd:PTZ00237 554 YNVPIGLLVLKQDQSNQsidlnklKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
186-529 |
2.08e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 94.62 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 186 LPYSSGTTGLPKGVMLTHKGLITSVAQQMDGqnpnlYY-HRNDV------ILCVLPFFH----IYSLNSILLCGLRvgAA 254
Cdd:PRK05850 165 LQYTSGSTRTPAGVMVSHRNVIANFEQLMSD-----YFgDTGGVpppdttVVSWLPFYHdmglVLGVCAPILGGCP--AV 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 255 IMimqkfDIVALL-------QLIEKHRISIMpiVPPIF---LAIAKSPE--FEKYDVSSVRVLKSGG-----APLGKELE 317
Cdd:PRK05850 238 LT-----SPVAFLqrparwmQLLASNPHAFS--AAPNFafeLAVRKTSDddMAGLDLGGVLGIISGServhpATLKRFAD 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 318 DAVREKFPTAILGQGYGMTEAgpVLSMSLAFAKEP-----FQV------KAGACGT----------VVRNAEMKIVDTET 376
Cdd:PRK05850 311 RFAPFNLRETAIRPSYGLAEA--TVYVATREPGQPpesvrFDYeklsagHAKRCETgggtplvsygSPRSPTVRIVDPDT 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 377 GASLPANSSGEICIRGDQIMKGYLNDLESTKRTID----------KEG-WLHTGDIGFVDDDnELFIVDRLKELIKFKAF 445
Cdd:PRK05850 389 CIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGatlvdpspgtPEGpWLRTGDLGFISEG-ELFIVGRIKDLLIVDGR 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 446 QVAPAELEALL--ITHPKlsdAAVIGMPDvEAGEVPVAFV-MKANGGAISE-----EEVKQFIAKQVVFYKRLKRVFFV- 516
Cdd:PRK05850 468 NHYPDDIEATIqeITGGR---VAAISVPD-DGTEKLVAIIeLKKRGDSDEEamdrlRTVKREVTSAISKSHGLSVADLVl 543
|
410
....*....|....*.
gi 778728825 517 ---NAIPKAPSGKILR 529
Cdd:PRK05850 544 vapGSIPITTSGKIRR 559
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
51-469 |
2.77e-20 |
|
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: 93.65 E-value: 2.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 51 GDVYTYHDVQLTARRVAAGLH-NLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANpfytaveiakqakaanakli 129
Cdd:cd05937 3 GKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFIN-------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 130 vtmacfYDRVKDlaengvqivcvdfaveGCLHFSVLSGADeslapLVDFSSNDVVALPYSSGTTGLPKGVMLT-HKGLIT 208
Cdd:cd05937 63 ------YNLSGD----------------PLIHCLKLSGSR-----FVIVDPDDPAILIYTSGTTGLPKAAAISwRRTLVT 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 209 S--VAQQMDGQNPNLYYHrndvilCvLPFFHIYSLNSILLCGLRVGAAIMIMQKFDIVALLQLIEKHRISIMPIVPPI-- 284
Cdd:cd05937 116 SnlLSHDLNLKNGDRTYT------C-MPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATIIQYVGELcr 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 285 -FLAIAKSPEFEKYdvsSVRVLKSGGapLGKELEDAVREKFPTAILGQGYGMTEAgpvLSMSLAFAKEPFqvKAGACG-- 361
Cdd:cd05937 189 yLLSTPPSPYDRDH---KVRVAWGNG--LRPDIWERFRERFNVPEIGEFYAATEG---VFALTNHNVGDF--GAGAIGhh 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 362 ------------TVVR---NAEMKIVDTETG--ASLPANSSGEICIR----GDQIMKGYLNDLESTK----RTIDKEG-- 414
Cdd:cd05937 259 glirrwkfenqvVLVKmdpETDDPIRDPKTGfcVRAPVGEPGEMLGRvpfkNREAFQGYLHNEDATEsklvRDVFRKGdi 338
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 778728825 415 WLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIG 469
Cdd:cd05937 339 YFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYG 393
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
159-534 |
2.04e-19 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 92.92 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 159 CLHFSVLSGADESLAPLVDFSSNDVVA-LPYSSGTTGLPKGVMLTHkGLITSVAQQMDGQnpnlYYHRNDVilCVLpffH 237
Cdd:PRK05691 2310 CLEDDAAALAAYSDAPLPFLSLPQHQAyLIYTSGSTGKPKGVVVSH-GEIAMHCQAVIER----FGMRADD--CEL---H 2379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 238 IYSLN---------SILLCGLRVgaaIMIMQ-KFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEfEKYDVSSVRVLKS 307
Cdd:PRK05691 2380 FYSINfdaaserllVPLLCGARV---VLRAQgQWGAEEICQLIREQQVSILGFTPSYGSQLAQWLA-GQGEQLPVRMCIT 2455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 308 GGAPLGKELEDAVREKFPTAILGQGYGMTEAgpvLSMSLAfAKEPFQVKAGAC----GTVVRNAEMKIVDTETgASLPAN 383
Cdd:PRK05691 2456 GGEALTGEHLQRIRQAFAPQLFFNAYGPTET---VVMPLA-CLAPEQLEEGAAsvpiGRVVGARVAYILDADL-ALVPQG 2530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 384 SSGEICIRGDQIMKGYLN--DLESTKRTID----KEGWLH-TGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALL 456
Cdd:PRK05691 2531 ATGELYVGGAGLAQGYHDrpGLTAERFVADpfaaDGGRLYrTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRL 2610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 457 ITHPKLSDAAVIGMpDVEAGEVPVAFVMKANGGAISE------EEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRK 530
Cdd:PRK05691 2611 LEHPAVREAVVLAL-DTPSGKQLAGYLVSAVAGQDDEaqaalrEALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRR 2689
|
....
gi 778728825 531 ELRA 534
Cdd:PRK05691 2690 ALPA 2693
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
451-526 |
2.38e-19 |
|
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: 82.21 E-value: 2.38e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 778728825 451 ELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGK 526
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
32-479 |
1.45e-18 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 89.16 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 32 VFQNL-SKFASRPCLINGatGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAI------ 104
Cdd:PRK08279 42 VFEEAaARHPDRPALLFE--DQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVvallnt 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 105 ----------MTAANPfytaveiakqakaanAKLIVTMACF--YDRVKDLAENGVQIVcvdfaVEGCLHFSVLSGADESL 172
Cdd:PRK08279 120 qqrgavlahsLNLVDA---------------KHLIVGEELVeaFEEARADLARPPRLW-----VAGGDTLDDPEGYEDLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 173 APLVDF------SSNDVVA-----LPYSSGTTGLPKGVMLTHKGLITSvaqqMDGQNPNLYYHRNDVILCVLPFFHIYSL 241
Cdd:PRK08279 180 AAAAGApttnpaSRSGVTAkdtafYIYTSGTTGLPKAAVMSHMRWLKA----MGGFGGLLRLTPDDVLYCCLPLYHNTGG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 242 NSILLCGLRVGAAIMIMQKFDIVALLQLIEKHRISimpivppIFLAI-------AKSPEFEKYDVSSVRVLKsgGAPLGK 314
Cdd:PRK08279 256 TVAWSSVLAAGATLALRRKFSASRFWDDVRRYRAT-------AFQYIgelcrylLNQPPKPTDRDHRLRLMI--GNGLRP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 315 ELEDAVREKFPTAILGQGYGMTEAGpvLSMSLAFAKEpfqvkaGACGTV----VRNAEMKIVDTETGASL---------- 380
Cdd:PRK08279 327 DIWDEFQQRFGIPRILEFYAASEGN--VGFINVFNFD------GTVGRVplwlAHPYAIVKYDVDTGEPVrdadgrcikv 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 381 PANSSGEIC--IRGDQIMKGYlNDLESTKRTI--D--KEG--WLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAEL 452
Cdd:PRK08279 399 KPGEVGLLIgrITDRGPFDGY-TDPEASEKKIlrDvfKKGdaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEV 477
|
490 500
....*....|....*....|....*..
gi 778728825 453 EALLITHPKLSDAAVIGMpdveagEVP 479
Cdd:PRK08279 478 ENALSGFPGVEEAVVYGV------EVP 498
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
168-541 |
1.78e-18 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 88.64 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 168 ADESLAPlVDFSSNDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQM---DGQNPNLYYhrndviLCVLPFFHIYSLNSI 244
Cdd:PRK12476 181 AGESFVP-VELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMIlsiDLLDRNTHG------VSWLPLYHDMGLSMI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 245 LLCGLrVGAAIMIMQKFDIVA-----LLQLIEKHRISIMPIVPPIF---LAIAKS--PEFEKYDVSSVrVLKSGGAPLGK 314
Cdd:PRK12476 254 GFPAV-YGGHSTLMSPTAFVRrpqrwIKALSEGSRTGRVVTAAPNFayeWAAQRGlpAEGDDIDLSNV-VLIIGSEPVSI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 315 eleDAVReKFPTAILGQG---------YGMTEAGPVLSmSLAFAKEPF-------QVKAG----------------ACGT 362
Cdd:PRK12476 332 ---DAVT-TFNKAFAPYGlprtafkpsYGIAEATLFVA-TIAPDAEPSvvyldreQLGAGravrvaadapnavahvSCGQ 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 363 VVRNAEMKIVDTETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTI------------------DKEGWLHTGDIGFV 424
Cdd:PRK12476 407 VARSQWAVIVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegshadgaaDDGTWLRTGDLGVY 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 425 dDDNELFIVDRLKELIKFKAFQVAPAELEAllithpKLSDAAvigmPDVEAGEVpVAFVMKANGGA----ISE------- 493
Cdd:PRK12476 487 -LDGELYITGRIADLIVIDGRNHYPQDIEA------TVAEAS----PMVRRGYV-TAFTVPAEDNErlviVAEraagtsr 554
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 778728825 494 -------EEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELRAKLASGAY 541
Cdd:PRK12476 555 adpapaiDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGRL 609
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
21-538 |
1.91e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 89.63 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 21 HIPNHLPLHDYVFQNLSKFASRPCLINGatGDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASY 100
Cdd:PRK12316 3052 EYPLERGVHRLFEEQVERTPDAVALAFG--EQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILK 3129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 101 RGAIMTAANPFYTAVEIAKQAKAANAKLIVTMAcfydRVKDLAENGVQIVCVDFAVEGClhfsvlsgadESLAPLVDFSS 180
Cdd:PRK12316 3130 AGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQS----HLRLPLAQGVQVLDLDRGDENY----------AEANPAIRTMP 3195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 181 NDVVALPYSSGTTGLPKGVMLTHKGLiTSVAQQMDGQnpnLYYHRNDVILCVLPF-FHIYSLNsiLLCGLRVGAAIMIM- 258
Cdd:PRK12316 3196 ENLAYVIYTSGSTGKPKGVGIRHSAL-SNHLCWMQQA---YGLGVGDRVLQFTTFsFDVFVEE--LFWPLMSGARVVLAg 3269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 259 --QKFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYdvSSVRVLKSGGAPLGKELEDAVREKFPtaiLGQGYGMT 336
Cdd:PRK12316 3270 peDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRC--TSLKRIVCGGEALPADLQQQVFAGLP---LYNLYGPT 3344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 337 EAgPVLSMSLAFAKEpfQVKAGACGTVVRNAEMKIVDtETGASLPANSSGEICIRGDQIMKGYLN--DLESTKRTIDK-- 412
Cdd:PRK12316 3345 EA-TITVTHWQCVEE--GKDAVPIGRPIANRACYILD-GSLEPVPVGALGELYLGGEGLARGYHNrpGLTAERFVPDPfv 3420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 413 --EGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMpdveAGEVPVAFVMKANGGA 490
Cdd:PRK12316 3421 pgERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAV----DGRQLVAYVVPEDEAG 3496
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 778728825 491 ISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELRAKLAS 538
Cdd:PRK12316 3497 DLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAA 3544
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
178-532 |
4.33e-18 |
|
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: 86.75 E-value: 4.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 178 FSSNDVVALPYSSGTTGLPKGVMLTHK---GLITSVAQQMDgqnpnlyYHRNDVILCVLPFFhiyslnSILLCGLRVGAA 254
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGtfaAQIDALRQLYG-------IRPGEVDLATFPLF------ALFGPALGLTSV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 255 IMIMQ-----KFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKF-PTAI 328
Cdd:cd05910 149 IPDMDptrpaRADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLsDEAE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 329 LGQGYGMTEAGPVLSMS----LAFAKEPFQVKAGAC-GTVVRNAEMKIVD-TETGAS-------LPANSSGEICIRGDQI 395
Cdd:cd05910 229 ILTPYGATEALPVSSIGsrelLATTTAATSGGAGTCvGRPIPGVRVRIIEiDDEPIAewddtleLPRGEIGEITVTGPTV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 396 MKGYLNDLESTKRT-IDKEG---WLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMp 471
Cdd:cd05910 309 TPTYVNRPVATALAkIDDNSegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV- 387
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 778728825 472 DVEAGEVPVAFVMKANGGAIS----EEEVKQfIAKQVVFYKRLKRVFFVNAIPKAP--SGKILRKEL 532
Cdd:cd05910 388 GKPGCQLPVLCVEPLPGTITPrarlEQELRA-LAKDYPHTQRIGRFLIHPSFPVDIrhNAKIFREKL 453
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
170-527 |
8.44e-18 |
|
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: 85.91 E-value: 8.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 170 ESLAPLVDFSSNDVVALPYSSGTTGLPKGVMLTHKG---LITSVAQQMDGQNpnlyyHRNDVILcvlpFFHIY----SLN 242
Cdd:cd17648 83 DTGARVVITNSTDLAYAIYTSGTTGKPKGVLVEHGSvvnLRTSLSERYFGRD-----NGDEAVL----FFSNYvfdfFVE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 243 SILLcGLRVGAAIMIMQ---KFDIVALLQLIEKHRISIMPIVPPIflaiakspeFEKYDVSSVRVLKSGGApLGKELE-- 317
Cdd:cd17648 154 QMTL-ALLNGQKLVVPPdemRFDPDRFYAYINREKVTYLSGTPSV---------LQQYDLARLPHLKRVDA-AGEEFTap 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 318 --DAVREKFPTAILgQGYGMTEAGPVLSMSLAFAKEPFQvkaGACGTVVRNAEMKIVDTETgASLPANSSGEICIRGDQI 395
Cdd:cd17648 223 vfEKLRSRFAGLII-NAYGPTETTVTNHKRFFPGDQRFD---KSLGRPVRNTKCYVLNDAM-KRVPVGAVGELYLGGDGV 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 396 MKGYLNDLEST-KRTI------DKEGWL-------HTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPK 461
Cdd:cd17648 298 ARGYLNRPELTaERFLpnpfqtEQERARgrnarlyKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPG 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 778728825 462 LSDAAVIGMPDVEAGEVP-----VAFVMkANGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKI 527
Cdd:cd17648 378 VRECAVVAKEDASQAQSRiqkylVGYYL-PEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
55-532 |
1.24e-17 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 85.56 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 55 TYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAveiakqakaanaklivtmac 134
Cdd:cd17644 27 TYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQ-------------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 135 fyDRVKDLAENgVQIvcvdfavegclhfSVLSGADESLAPLVdfssndvvalpYSSGTTGLPKGVMLTHKglitSVAQQM 214
Cdd:cd17644 87 --ERLTYILED-AQI-------------SVLLTQPENLAYVI-----------YTSGSTGKPKGVMIEHQ----SLVNLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 215 DGQNPNLYYHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMIMQK--FDIVALLQLIEKHRISIMPIVPPIF--LAIAK 290
Cdd:cd17644 136 HGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEmrSSLEDFVQYIQQWQLTVLSLPPAYWhlLVLEL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 291 SPEFEKYDvSSVRVLKSGGAPLGKELEDAVRE---KFPTAIlgQGYGMTEAGPVLSMSLAFAKEPFQVKAGACGTVVRNA 367
Cdd:cd17644 216 LLSTIDLP-SSLRLVIVGGEAVQPELVRQWQKnvgNFIQLI--NVYGPTEATIAATVCRLTQLTERNITSVPIGRPIANT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 368 EMKIVDtETGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLH--------TGDIGFVDDDNELFIVDRLKEL 439
Cdd:cd17644 293 QVYILD-ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 440 IKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVPVAFVMKANGGAISEEEVKQFIAKQVVFYKRLKRVFFVNAI 519
Cdd:cd17644 372 VKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEEL 451
|
490
....*....|...
gi 778728825 520 PKAPSGKILRKEL 532
Cdd:cd17644 452 PLTPNGKIDRRAL 464
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
55-538 |
1.47e-17 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 86.10 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 55 TYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLIVTMAC 134
Cdd:PLN02654 122 TYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITCNA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 135 FYDRVKDL-------------AENGVqivcvdfAVEGCLHF---SVLSGADESLAPLVDFSSNDVVA------------- 185
Cdd:PLN02654 202 VKRGPKTInlkdivdaaldesAKNGV-------SVGICLTYenqLAMKREDTKWQEGRDVWWQDVVPnyptkcevewvda 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 186 -----LPYSSGTTGLPKGVMLTHKGLI----TSVAQQMDgqnpnlyYHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIM 256
Cdd:PLN02654 275 edplfLLYTSGSTGKPKGVLHTTGGYMvytaTTFKYAFD-------YKPTDVYWCTADCGWITGHSYVTYGPMLNGATVL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 257 IMQKF----DIVALLQLIEKHRISIMPIVPPIFLAIAKS-PEF-EKYDVSSVRVLKSGGAPLGkeledavrekfPTA--- 327
Cdd:PLN02654 348 VFEGApnypDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDgDEYvTRHSRKSLRVLGSVGEPIN-----------PSAwrw 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 328 ---ILGQG-------YGMTEAGPVLSMSLAFAkepFQVKAGACGTVVRNAEMKIVDtETGASLPANSSGEICIRGD--QI 395
Cdd:PLN02654 417 ffnVVGDSrcpisdtWWQTETGGFMITPLPGA---WPQKPGSATFPFFGVQPVIVD-EKGKEIEGECSGYLCVKKSwpGA 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 396 MKGYLNDLESTKRTIDK--EGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDV 473
Cdd:PLN02654 493 FRTLYGDHERYETTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHE 572
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 778728825 474 EAGEVPVAFVMKANGGAISEEEVKQFIA---KQVVFYKRLKRVFFVNAIPKAPSGKILRKELRaKLAS 538
Cdd:PLN02654 573 VKGQGIYAFVTLVEGVPYSEELRKSLILtvrNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR-KIAS 639
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
162-469 |
2.04e-17 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 85.66 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 162 FSVLSGADESLAPLvdfSSNDVVALPYSSGTTGLPKGVMLTHKGLItsvAQQMDGQNPNLYYHR----NDVILCVLPFFH 237
Cdd:PLN02861 204 FSLMGSLDCELPPK---QKTDICTIMYTSGTTGEPKGVILTNRAII---AEVLSTDHLLKVTDRvateEDSYFSYLPLAH 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 238 IYSLNSILLCgLRVGAAIMIMQKfDIVALLQLIEKHRISIMPIVPPIFL--------------AIAK------------- 290
Cdd:PLN02861 278 VYDQVIETYC-ISKGASIGFWQG-DIRYLMEDVQALKPTIFCGVPRVYDriytgimqkissggMLRKklfdfaynyklgn 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 291 ----------SPEFEKYDVSS--------VRVLKSGGAPLGKELEDAVREKfPTAILGQGYGMTE--AGPVLSMSLAFAK 350
Cdd:PLN02861 356 lrkglkqeeaSPRLDRLVFDKikeglggrVRLLLSGAAPLPRHVEEFLRVT-SCSVLSQGYGLTEscGGCFTSIANVFSM 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 351 epfqvkAGACGTVVRNAEMKIVDT-ETG-ASLPANSSGEICIRGDQIMKGYLNDLESTKRTIdKEGWLHTGDIGFVDDDN 428
Cdd:PLN02861 435 ------VGTVGVPMTTIEARLESVpEMGyDALSDVPRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNG 507
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 778728825 429 ELFIVDRLKELIKFKAFQ-VAPAELEALLITHPKLSDAAVIG 469
Cdd:PLN02861 508 AMKIIDRKKNIFKLSQGEyVAVENLENTYSRCPLIASIWVYG 549
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
55-470 |
1.64e-16 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 82.62 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 55 TYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLI----- 129
Cdd:PRK08180 71 TYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAYSLVSQDFGKLRHVLELLtpglv 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 130 -VTMACFYDRVKDLAE-NGVQIVCVDFAVEG--CLHFSVL------SGADESLAPLvdfSSNDVVALPYSSGTTGLPKGV 199
Cdd:PRK08180 151 fADDGAAFARALAAVVpADVEVVAVRGAVPGraATPFAALlatpptAAVDAAHAAV---GPDTIAKFLFTSGSTGLPKAV 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 200 MLTHkGLITSVAQQMDGQNPNLYyHRNDVILCVLPFFHIYSLNSILLCGLRVGAAIMI------MQKFDivallQLIEKH 273
Cdd:PRK08180 228 INTH-RMLCANQQMLAQTFPFLA-EEPPVLVDWLPWNHTFGGNHNLGIVLYNGGTLYIddgkptPGGFD-----ETLRNL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 274 RiSIMPI----VPPIFLAIAksPEFEKYDV------SSVRVLKSGGAPLGKELEDAVrEKFPTAILGQ------GYGMTE 337
Cdd:PRK08180 301 R-EISPTvyfnVPKGWEMLV--PALERDAAlrrrffSRLKLLFYAGAALSQDVWDRL-DRVAEATCGErirmmtGLGMTE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 338 AGPvlsmSLAFAKEPfQVKAGACGTVVRNAEMKIVdtetgaslPANSSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLH 417
Cdd:PRK08180 377 TAP----SATFTTGP-LSRAGNIGLPAPGCEVKLV--------PVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYR 443
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 778728825 418 TGDIG-FVD-DDNEL-FIVD-RLKEliKFK----AF-QVAPAELEALLITHPKLSDAAVIGM 470
Cdd:PRK08180 444 SGDAVrFVDpADPERgLMFDgRIAE--DFKlssgTWvSVGPLRARAVSAGAPLVQDVVITGH 503
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
174-498 |
3.52e-16 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 81.48 E-value: 3.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 174 PLVDFSSNDVVALPYSSGTTGLPKGVMLTHkGLITSVAQQMDgqnpNLYYHR-NDVILCVLPFFHIYSLnsilLCGLRvg 252
Cdd:PRK09274 167 PMADLAPDDMAAILFTSGSTGTPKGVVYTH-GMFEAQIEALR----EDYGIEpGEIDLPTFPLFALFGP----ALGMT-- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 253 AAIMIMQ-----KFDIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFP-T 326
Cdd:PRK09274 236 SVIPDMDptrpaTVDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAMLPpD 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 327 AILGQGYGMTEAGPVLSMS----LAFAKEPFQVKAGAC-GTVVRNAEMKIVDTETGA--------SLPANSSGEICIRGD 393
Cdd:PRK09274 316 AEILTPYGATEALPISSIEsreiLFATRAATDNGAGICvGRPVDGVEVRIIAISDAPipewddalRLATGEIGEIVVAGP 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 394 QIMKGYLNDLESTK--RTIDKEG--WLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIG 469
Cdd:PRK09274 396 MVTRSYYNRPEATRlaKIPDGQGdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVG 475
|
330 340
....*....|....*....|....*....
gi 778728825 470 MPdVEAGEVPVAFVMKANGGAISEEEVKQ 498
Cdd:PRK09274 476 VG-VPGAQRPVLCVELEPGVACSKSALYQ 503
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
54-324 |
8.77e-16 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 80.22 E-value: 8.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 54 YTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTA-------------Veiakq 120
Cdd:PRK03584 115 LSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVqgvldrfgqiepkV----- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 121 akaanakLIVTMACFY-----DRVKDLAE-----NGVQIVC-VDFavegcLHFSVLSGADESLAPLVDFSSN------DV 183
Cdd:PRK03584 190 -------LIAVDGYRYggkafDRRAKVAElraalPSLEHVVvVPY-----LGPAAAAAALPGALLWEDFLAPaeaaelEF 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 184 VALP--------YSSGTTGLPK-------GVMLTHkglITSVAQQMDgqnpnlyYHRNDVilcvlpfFHIYSLNS----- 243
Cdd:PRK03584 258 EPVPfdhplwilYSSGTTGLPKcivhghgGILLEH---LKELGLHCD-------LGPGDR-------FFWYTTCGwmmwn 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 244 ILLCGLRVGAAIMImqkFD-------IVALLQLIEKHRISIMPIVPPIFLAIAKS---PEfEKYDVSSVRVLKSGGAPLG 313
Cdd:PRK03584 321 WLVSGLLVGATLVL---YDgspfypdPNVLWDLAAEEGVTVFGTSAKYLDACEKAglvPG-ETHDLSALRTIGSTGSPLP 396
|
330
....*....|.
gi 778728825 314 KELEDAVREKF 324
Cdd:PRK03584 397 PEGFDWVYEHV 407
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
181-441 |
1.12e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 80.15 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 181 NDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQMDG---QNPNLYYHrndviLCVLPFFHIYSLNSILLCGLRvGAAIMI 257
Cdd:PTZ00342 304 DFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKHsifKKYNPKTH-----LSYLPISHIYERVIAYLSFML-GGTINI 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 258 MQKfDIVALLQLIEKHRISIMPIVPPIF--------LAIAKSPEFEKYDVSSVRVLKSGG--APLGKELE---------- 317
Cdd:PTZ00342 378 WSK-DINYFSKDIYNSKGNILAGVPKVFnriytnimTEINNLPPLKRFLVKKILSLRKSNnnGGFSKFLEgithisskik 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 318 DAVREKFPTAILG---------------------QGYGMTE-AGPVLsmsLAFAKEPFQVKAGacGTVVRNAEMKIVDTE 375
Cdd:PTZ00342 457 DKVNPNLEVILNGggklspkiaeelsvllnvnyyQGYGLTEtTGPIF---VQHADDNNTESIG--GPISPNTKYKVRTWE 531
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 778728825 376 TGASLPANSSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLHTGDIGFVDDDNELFIVDRLKELIK 441
Cdd:PTZ00342 532 TYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVK 597
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
51-471 |
1.58e-15 |
|
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: 79.26 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 51 GDVYTYHDVQLTARRVAAGLHN-LGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAANAKLI 129
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 130 VTMACFYDRVK-DLAENGVQIVCVDFAVEGCLHFSVlsgadESLAPLVDFSSNDVV--ALP------------YSSGTTG 194
Cdd:cd05938 83 VVAPELQEAVEeVLPALRADGVSVWYLSHTSNTEGV-----ISLLDKVDAASDEPVpaSLRahvtikspalyiYTSGTTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 195 LPKGVMLTHKGLITSVA-QQMDGqnpnlyYHRNDVILCVLPFFH-IYSLNSILLCgLRVGAAIMIMQKFDIVALLQLIEK 272
Cdd:cd05938 158 LPKAARISHLRVLQCSGfLSLCG------VTADDVIYITLPLYHsSGFLLGIGGC-IELGATCVLKPKFSASQFWDDCRK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 273 HRISIMPIVPPIFLAIAKSPEFEKYDVSSVRVlksggaPLGKELEDAVREKF-----PTAILgQGYGMTEAgpvlsmSLA 347
Cdd:cd05938 231 HNVTVIQYIGELLRYLCNQPQSPNDRDHKVRL------AIGNGLRADVWREFlrrfgPIRIR-EFYGSTEG------NIG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 348 FAKepfqvKAGACGTVVR-NAEMKIV--------DTETGASLpANSSGeICIR------GDQIMK--------GYLNDLE 404
Cdd:cd05938 298 FFN-----YTGKIGAVGRvSYLYKLLfpfelikfDVEKEEPV-RDAQG-FCIPvakgepGLLVAKitqqspflGYAGDKE 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 778728825 405 STK----RTIDKEG--WLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIGMP 471
Cdd:cd05938 371 QTEkkllRDVFKKGdvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVT 443
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
54-520 |
3.21e-15 |
|
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: 78.24 E-value: 3.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 54 YTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAAN------PFYTAVEIAKqakaanak 127
Cdd:cd05939 4 WTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINsnlrleSLLHCITVSK-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 128 livTMACFYDRVKDLaengvqivcvdfavegclhfsvLSGADESLAPLVDFSSNDVVALPYSSGTTGLPKGVMLTHKGL- 206
Cdd:cd05939 76 ---AKALIFNLLDPL----------------------LTQSSTEPPSQDDVNFRDKLFYIYTSGTTGLPKAAVIVHSRYy 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 207 -ITSVAQQMDGQNPnlyyhrNDVILCVLPFFH----IYSLNSILLCGLRVgaaiMIMQKFDIVALLQLIEKHRISIMPIV 281
Cdd:cd05939 131 rIAAGAYYAFGMRP------EDVVYDCLPLYHsaggIMGVGQALLHGSTV----VIRKKFSASNFWDDCVKYNCTIVQYI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 282 PPI---FLAIAKSPEFEKYdvsSVRVLKSGGapLGKELEDAVREKFPTAILGQGYGMTEAgpvlSMSLAfakePFQVKAG 358
Cdd:cd05939 201 GEIcryLLAQPPSEEEQKH---NVRLAVGNG--LRPQIWEQFVRRFGIPQIGEFYGATEG----NSSLV----NIDNHVG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 359 ACGTV--------------VRNAEMKIVDTETGASLPA--NSSGEIC---IRGDQIMK--GYLNDLESTK---RTIDKEG 414
Cdd:cd05939 268 ACGFNsrilpsvypirlikVDEDTGELIRDSDGLCIPCqpGEPGLLVgkiIQNDPLRRfdGYVNEGATNKkiaRDVFKKG 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 415 --WLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIG--MPDVEAgevpvafvmKANGGA 490
Cdd:cd05939 348 dsAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGveVPGVEG---------RAGMAA 418
|
490 500 510
....*....|....*....|....*....|
gi 778728825 491 ISEEEVKQFIAKqvvFYKRLKRVFFVNAIP 520
Cdd:cd05939 419 IVDPERKVDLDR---FSAVLAKSLPPYARP 445
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
188-534 |
1.49e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 77.13 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 188 YSSGTTGLPKGVMLTHKGLITSVAQQMdgqnPNLYYHRNDVI---------LCVLPFFhiyslnsillcglrvgAAIMIM 258
Cdd:PRK05691 3876 YTSGSTGLPKGVMVEQRGMLNNQLSKV----PYLALSEADVIaqtasqsfdISVWQFL----------------AAPLFG 3935
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 259 QKFDIV---------ALLQLIEKHRISIMPIVPPIflaIAKSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAIL 329
Cdd:PRK05691 3936 ARVEIVpnaiahdpqGLLAHVQAQGITVLESVPSL---IQGMLAEDRQALDGLRWMLPTGEAMPPELARQWLQRYPQIGL 4012
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 330 GQGYGMTEAgpvlSMSLAFAKEPFQVKAGA---CGTVVRNAEMKIVDtETGASLPANSSGEICIRGDQIMKGYLNDLEST 406
Cdd:PRK05691 4013 VNAYGPAEC----SDDVAFFRVDLASTRGSylpIGSPTDNNRLYLLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRT 4087
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 407 KRTI-------DKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAViGMPDVEAGEVP 479
Cdd:PRK05691 4088 ALAFvphpfgaPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAV-AVQEGVNGKHL 4166
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 778728825 480 VAFVMKANGGAISE---EEVKQFIAKQVVFYKRLKRVFFVNAIPKAPSGKILRKELRA 534
Cdd:PRK05691 4167 VGYLVPHQTVLAQGallERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPA 4224
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
28-532 |
2.43e-14 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 76.24 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 28 LHDYVFQNLSKFASRPCLINGATGDVYTYHDVQLTArrVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTA 107
Cdd:PRK10252 460 LSALVAQQAAKTPDAPALADARYQFSYREMREQVVA--LANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 108 ANPFYTAVEIAKQAKAANAKLIVTMACFYDRVKDLAenGVQIVCVDFAVegclhfsvlsgADESLAPLVDFSSNDVVALP 187
Cdd:PRK10252 538 LDTGYPDDRLKMMLEDARPSLLITTADQLPRFADVP--DLTSLCYNAPL-----------APQGAAPLQLSQPHHTAYII 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 188 YSSGTTGLPKGVMLTHKGlITSVAQQMDGQNPnlyYHRNDVIL----C-----VLPFFHIyslnsiLLCGlrvgaAIMIM 258
Cdd:PRK10252 605 FTSGSTGRPKGVMVGQTA-IVNRLLWMQNHYP---LTADDVVLqktpCsfdvsVWEFFWP------FIAG-----AKLVM 669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 259 QK----FDIVALLQLIEKHRISIMPIVPP---IFLAiAKSPEFEKYDVSSVR-VLKSGGAplgkeLEDAVREKFPTAI-- 328
Cdd:PRK10252 670 AEpeahRDPLAMQQFFAEYGVTTTHFVPSmlaAFVA-SLTPEGARQSCASLRqVFCSGEA-----LPADLCREWQQLTga 743
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 329 -LGQGYGMTEAGPVLSMSLAFAKEPFQVKAGAC--GTVVRNAEMKIVDtETGASLPANSSGEICIRGDQIMKGYLN--DL 403
Cdd:PRK10252 744 pLHNLYGPTEAAVDVSWYPAFGEELAAVRGSSVpiGYPVWNTGLRILD-ARMRPVPPGVAGDLYLTGIQLAQGYLGrpDL 822
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 404 eSTKRTIDK-----EGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKL----SDAAVIGMPDVE 474
Cdd:PRK10252 823 -TASRFIADpfapgERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVeqavTHACVINQAAAT 901
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 778728825 475 AGEVP--VAFVMKANGGAISEEEVKQFIAKQVVFYkrLKRVFFV--NAIPKAPSGKILRKEL 532
Cdd:PRK10252 902 GGDARqlVGYLVSQSGLPLDTSALQAQLRERLPPH--MVPVVLLqlDQLPLSANGKLDRKAL 961
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
26-460 |
2.78e-14 |
|
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: 75.57 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 26 LPLHDYVFQNLSKFASRPCLINGATGDVYTYHDVQLTARRVA-----------------AGLHNLG--IKKGDVVMNLLP 86
Cdd:cd17632 22 LRLAQIIATVMTGYADRPALGQRATELVTDPATGRTTLRLLPrfetityaelwervgavAAAHDPEqpVRPGDFVAVLGF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 87 NSPEFVFTFLGASYRGAImtaANPFYTAVEIAKQAKAAN----AKLIVTMACFYDRVKDLAENG--VQIVCVDFAVEGCL 160
Cdd:cd17632 102 TSPDYATVDLALTRLGAV---SVPLQAGASAAQLAPILAetepRLLAVSAEHLDLAVEAVLEGGtpPRLVVFDHRPEVDA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 161 HFSVLSGADESLA-----------------------PLVDFSSND-VVALPYSSGTTGLPKGVMLTHKGLITSVAQQMDG 216
Cdd:cd17632 179 HRAALESARERLAavgipvttltliavrgrdlppapLFRPEPDDDpLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 217 QNPnlyYHRNDVILCVLPFFHIYSLNSiLLCGLRVGAAIMIMQKFDIVALLQLIEKHRISIMPIVPPI-------FLAIA 289
Cdd:cd17632 259 QDI---RPPASITLNFMPMSHIAGRIS-LYGTLARGGTAYFAAASDMSTLFDDLALVRPTELFLVPRVcdmlfqrYQAEL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 290 KSPEFEKYDVSSV----------RVLK-------SGGAPLGKELEDAVREKFPTAILgQGYGMTEAGPVLSMslafakep 352
Cdd:cd17632 335 DRRSVAGADAETLaervkaelreRVLGgrllaavCGSAPLSAEMKAFMESLLDLDLH-DGYGSTEAGAVILD-------- 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 353 fqvkagacGTVVRNA--EMKIVDT-ETG---ASLPaNSSGEICIRGDQIMKGYLNDLESTKRTIDKEGWLHTGDIGFVDD 426
Cdd:cd17632 406 --------GVIVRPPvlDYKLVDVpELGyfrTDRP-HPRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELG 476
|
490 500 510
....*....|....*....|....*....|....*
gi 778728825 427 DNELFIVDRLKELIKFKAFQ-VAPAELEALLITHP 460
Cdd:cd17632 477 PDRLVYVDRRNNVLKLSQGEfVTVARLEAVFAASP 511
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
51-453 |
6.21e-14 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 74.16 E-value: 6.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 51 GDVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAimtAANP--FYTAVEIakqakaanakl 128
Cdd:PRK04813 25 GEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGH---AYIPvdVSSPAER----------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 129 iVTMacfydrVKDLAENGVQIVCVDFAVEGcLHFSVLSGAD--ESLAPL--VDFSS----NDVVALPYSSGTTGLPKGVM 200
Cdd:PRK04813 91 -IEM------IIEVAKPSLIIATEELPLEI-LGIPVITLDElkDIFATGnpYDFDHavkgDDNYYIIFTSGTTGKPKGVQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 201 LTHKGLItSVAQQM--DGQNPNlyyhrNDVILCVLPFFHIYSLNSILLCgLRVGAAIMIMQKfDIVA----LLQLIEKHR 274
Cdd:PRK04813 163 ISHDNLV-SFTNWMleDFALPE-----GPQFLNQAPYSFDLSVMDLYPT-LASGGTLVALPK-DMTAnfkqLFETLPQLP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 275 ISIMpIVPPIFLAIA-KSPEFEKYDVSSVRVLKSGGAPLGKELEDAVREKFPTAILGQGYGMTEAGPVLSmSLAFAKE-- 351
Cdd:PRK04813 235 INVW-VSTPSFADMClLDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATVAVT-SIEITDEml 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 352 ------PF-QVKAGacgtvvrnaeMKI-VDTETGASLPANSSGEICIRGDQIMKGYLNDLESTKR---TIDKEGWLHTGD 420
Cdd:PRK04813 313 dqykrlPIgYAKPD----------SPLlIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEaffTFDGQPAYHTGD 382
|
410 420 430
....*....|....*....|....*....|...
gi 778728825 421 IGFVDDDnELFIVDRLKELIKFKAFQVapaELE 453
Cdd:PRK04813 383 AGYLEDG-LLFYQGRIDFQIKLNGYRI---ELE 411
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
298-539 |
1.88e-13 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 72.88 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 298 DVSSVRVLKSGGAPLGKE-----LEDAVREKFPTAILGQGYGMTEAG-----PVLSMSLAFAkepfQVKAGACGTVVRNA 367
Cdd:PRK05851 270 DLGALRVALNGGEPVDCDgferfATAMAPFGFDAGAAAPSYGLAESTcavtvPVPGIGLRVD----EVTTDDGSGARRHA 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 368 ---------EMKIVDTETGASLPANSSGEICIRGDQIMKGYLNDlestkRTIDKEGWLHTGDIGFVDDDnELFIVDRLKE 438
Cdd:PRK05851 346 vlgnpipgmEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQ-----APIDPDDWFPTGDLGYLVDG-GLVVCGRAKE 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 439 LIKFKAFQVAPAELEALLITHPKLSDAAVIGMPDVEAGEVP---VAFVMKANGGAISEEEVKQFIAKQ-------VVFYK 508
Cdd:PRK05851 420 LITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSARPglvIAAEFRGPDEAGARSEVVQRVASEcgvvpsdVVFVA 499
|
250 260 270
....*....|....*....|....*....|.
gi 778728825 509 RlkrvffvNAIPKAPSGKILRKELRAKLASG 539
Cdd:PRK05851 500 P-------GSLPRTSSGKLRRLAVKRSLEAA 523
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
40-336 |
2.94e-13 |
|
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: 72.30 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 40 ASRPCLINGATG---DVYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTA-- 114
Cdd:cd05943 82 ADDPAAIYAAEDgerTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVpg 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 115 -----VEIakqakaANAKLIVTMACFY-----DRVKDLAE------NGVQIVCVDFAVEGCLH-------FSVLSG--AD 169
Cdd:cd05943 162 vldrfGQI------EPKVLFAVDAYTYngkrhDVREKVAElvkglpSLLAVVVVPYTVAAGQPdlskiakALTLEDflAT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 170 ESLAPLvDFSS---NDVVALPYSSGTTGLPKGVMLTHKGLitsvaqqmdgqnpnLYYHRNDVIL-CVLPF---FHIYSL- 241
Cdd:cd05943 236 GAAGEL-EFEPlpfDHPLYILYSSGTTGLPKCIVHGAGGT--------------LLQHLKEHILhCDLRPgdrLFYYTTc 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 242 -----NSiLLCGLRVGAAIMImqkFD-------IVALLQLIEKHRISIMPIVPPIFLAIAKS--PEFEKYDVSSVRVLKS 307
Cdd:cd05943 301 gwmmwNW-LVSGLAVGATIVL---YDgspfypdTNALWDLADEEGITVFGTSAKYLDALEKAglKPAETHDLSSLRTILS 376
|
330 340 350
....*....|....*....|....*....|
gi 778728825 308 GGAPLGKELEDAVREKF-PTAILGQGYGMT 336
Cdd:cd05943 377 TGSPLKPESFDYVYDHIkPDVLLASISGGT 406
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
188-482 |
1.16e-12 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 70.51 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 188 YSSGTTGLPKGVMLTHKGLITSVAQQMDGQNpnlyYHRNDVILCVLPFFHIYSLNSILLCGLRVGAaimimqkfdivall 267
Cdd:PRK08043 372 FTSGSEGHPKGVVHSHKSLLANVEQIKTIAD----FTPNDRFMSALPLFHSFGLTVGLFTPLLTGA-------------- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 268 qliekhRISIMP------IVPPI--------------FL---AIAKSPefekYDVSSVRVLKSGGAPLGKELEDAVREKF 324
Cdd:PRK08043 434 ------EVFLYPsplhyrIVPELvydrnctvlfgtstFLgnyARFANP----YDFARLRYVVAGAEKLQESTKQLWQDKF 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 325 PTAILgQGYGMTEAGPVLSMSLafakePFQVKAGACGTVVRNAEMKIVdtetgaSLPA-NSSGEICIRGDQIMKGYL--- 400
Cdd:PRK08043 504 GLRIL-EGYGVTECAPVVSINV-----PMAAKPGTVGRILPGMDARLL------SVPGiEQGGRLQLKGPNIMNGYLrve 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 401 --NDLES----TKRTIDKEGWLHTGDIGFVDDDNELFIVDRLKELIKFKAFQVAPAELEAL-LITHPKLSDAAVIgMPDV 473
Cdd:PRK08043 572 kpGVLEVptaeNARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLaLGVSPDKQHATAI-KSDA 650
|
....*....
gi 778728825 474 EAGEVPVAF 482
Cdd:PRK08043 651 SKGEALVLF 659
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
47-534 |
3.91e-09 |
|
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: 59.28 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 47 NGATGDVYTYHDVQLTARRVAAGLHN-LGIKKGDVVMNLLPNSPEFVFTFLGASYRGAIMTAANPFYTAVEIAKQAKAAN 125
Cdd:cd05905 8 KGKEATTLTWGKLLSRAEKIAAVLQKkVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 126 AKLIVTM-ACFYDRVKDLAENGVQIVCVDFavEGCLHFSVLSGADESLAPLVDFSS-------NDVVALPYSSGTTGLPK 197
Cdd:cd05905 88 VRVALTVeACLKGLPKKLLKSKTAAEIAKK--KGWPKILDFVKIPKSKRSKLKKWGphpptrdGDTAYIEYSFSSDGSLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 198 GVMLTHKGLIT---SVAQQMDgqnpnlYYHrNDVILCVLPFFHIYSLNSILLCGLRVGA-AIMIMQ---KFDIVALLQLI 270
Cdd:cd05905 166 GVAVSHSSLLAhcrALKEACE------LYE-SRPLVTVLDFKSGLGLWHGCLLSVYSGHhTILIPPelmKTNPLLWLQTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 271 EKHRISI----MPIVPPIFLAIAKSPEFEKY---DVSSVRVLKsggAPLGKELEDAVREKF----------PTAILG--- 330
Cdd:cd05905 239 SQYKVRDayvkLRTLHWCLKDLSSTLASLKNrdvNLSSLRMCM---VPCENRPRISSCDSFlklfqtlglsPRAVSTefg 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 331 ---------QGYGMTEAGPV-LSMS--------LAFAKEPFQVKAGACGTVVRNAEMKIVDTETGASLPANSSGEICIRG 392
Cdd:cd05905 316 trvnpficwQGTSGPEPSRVyLDMRalrhgvvrLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEIGEIWVNS 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 393 DQIMKGY--LNDLES---------TKRTIDKE-GWLHTGDIGFV----------DDDNELFIVDRLKELIKFKAFQVAPA 450
Cdd:cd05905 396 PANASGYflLDGETNdtfkvfpstRLSTGITNnSYARTGLLGFLrptkctdlnvEEHDLLFVVGSIDETLEVRGLRHHPS 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 451 ELEA-LLITHPKLSDAAVIgmpdvEAGEVPVaFVMKANGGaiSEEEVKQFIAKQVV-----FYKRLKRVFFV--NAIPKA 522
Cdd:cd05905 476 DIEAtVMRVHPYRGRCAVF-----SITGLVV-VVAEQPPG--SEEEALDLVPLVLNaileeHQVIVDCVALVppGSLPKN 547
|
570
....*....|..
gi 778728825 523 PSGKILRKELRA 534
Cdd:cd05905 548 PLGEKQRMEIRQ 559
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
189-468 |
4.86e-09 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 58.62 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 189 SSGTTGLPKGVMLTHKGL---ITSVAQQMDGQnpnlYYHRNDVILCVLPffhiYSLNS----ILLCGLRVGAAIMIMQKF 261
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDLdrwAELFARSLRAA----GVRPGDRVQNAFG----YGLFTgglgLHYGAERLGATVIPAGGG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 262 DIVALLQLIEKHRISIMPIVPPIFLAIAKSPEFEKYDV--SSVRVLKSGGAPLGKELEDAVREKFPTAILgQGYGMTEAG 339
Cdd:COG1541 163 NTERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEEGIDPrdLSLKKGIFGGEPWSEEMRKEIEERWGIKAY-DIYGLTEVG 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 340 PVLsmslafakepfqvkAGAC----GTVVRNAE--MKIVDTETGASLPANSSGEICIrgdqimkgylndlesTkrTIDKE 413
Cdd:COG1541 242 PGV--------------AYECeaqdGLHIWEDHflVEIIDPETGEPVPEGEEGELVV---------------T--TLTKE 290
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 778728825 414 GW----LHTGDIGFVDDDNE---------LFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVI 468
Cdd:COG1541 291 AMplirYRTGDLTRLLPEPCpcgrthpriGRILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQI 358
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
189-532 |
4.81e-08 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 55.56 E-value: 4.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 189 SSGTTGLPKGVMLTHKGL---ITSVAQQMDGQNPNLYYhrndviLCVLPFFHIYSLNSILlcGLRVGAAIMIMQKFDIV- 264
Cdd:cd17654 126 TSGTTGTPKIVAVPHKCIlpnIQHFRSLFNITSEDILF------LTSPLTFDPSVVEIFL--SLSSGATLLIVPTSVKVl 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 265 -ALLQ--LIEKHRISIMPIVPPIF--LAIAKSPEFEKYDVSSVRVLKSGGAPLGKELED-AVREKFPTAILGQGYGMTEa 338
Cdd:cd17654 198 pSKLAdiLFKRHRITVLQATPTLFrrFGSQSIKSTVLSATSSLRVLALGGEPFPSLVILsSWRGKGNRTRIFNIYGITE- 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 339 gpVLSMSLAF----AKEPFQVKAGACGTVVRnaemkiVDTETGASLPANSSGEICIRGdQIMKGYLNDLESTKRTidkeg 414
Cdd:cd17654 277 --VSCWALAYkvpeEDSPVQLGSPLLGTVIE------VRDQNGSEGTGQVFLGGLNRV-CILDDEVTVPKGTMRA----- 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 415 wlhTGDigFVD-DDNELFIVDRLKELIKFKAFQVAPAELEALLITHPKLSDAAVIgmpdVEAGEVPVAF-VMKANGGAIS 492
Cdd:cd17654 343 ---TGD--FVTvKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVT----LSDQQRLIAFiVGESSSSRIH 413
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 778728825 493 EEEVKQFIAKQVVfykrLKRVFFVNAIPKAPSGKILRKEL 532
Cdd:cd17654 414 KELQLTLLSSHAI----PDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
459-542 |
2.52e-03 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 40.83 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778728825 459 HPKLSDAAVIGMPDVEAG--EVPVAFVMKA-NGGAISEEEVKQFIAKQVVfyKRLKRVFFVNAI------PKAPSGKILR 529
Cdd:PLN03052 635 DESVLETAAIGVPPPGGGpeQLVIAAVLKDpPGSNPDLNELKKIFNSAIQ--KKLNPLFKVSAVvivpsfPRTASNKVMR 712
|
90
....*....|...
gi 778728825 530 KELRAKLASGAYN 542
Cdd:PLN03052 713 RVLRQQLAQELSR 725
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
48-86 |
3.77e-03 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 39.75 E-value: 3.77e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 778728825 48 GATGD----VYTYHDVQLTARRVAAGLHNLGIKKGDVVMNLLP 86
Cdd:COG1541 93 GTTGKptvvGYTRKDLDRWAELFARSLRAAGVRPGDRVQNAFG 135
|
|
| |
