|
Name |
Accession |
Description |
Interval |
E-value |
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
33-514 |
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: 656.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 33 LPSKESLDITTFISSQTYRGKTAFIDAATDHRISFSDLWMAVDRVADCLlHDVGIRRGDVVLVLSPNTISIPIVCLSVMS 112
Cdd:cd05904 1 LPTDLPLDSVSFLFASAHPSRPALIDAATGRALTYAELERRVRRLAAGL-AKRGGRKGDVVLLLSPNSIEFPVAFLAVLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 113 LGAVLTTANPLNTASEILRQIADSNPKLAFTTPELAPKIASSGISIVLErveDTLRVPRGLKVVGnltemMKKEPSGQAV 192
Cdd:cd05904 80 LGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLASLALPVVLL---DSAEFDSLSFSDL-----LFEADEAEPP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 193 RNQVHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVARYIA--EPFEQPQQTFICTVPLFHTFGLLNFVLATLALGTTVV 270
Cdd:cd05904 152 VVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAgeGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 271 ILPRFDLGEMMAAVEKYRATTLILVPPVLVTMINKAdqIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVDVYQGYA 350
Cdd:cd05904 232 VMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSP--IVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 351 LTESNGAGASIESVEESR-RYGAVGLLSCGVEARIVDPNTGQVMGLNQTGELWLKGPSIAKGYFRNEE---EIITSEGWL 426
Cdd:cd05904 310 MTESTGVVAMCFAPEKDRaKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEataATIDKEGWL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 427 KTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKV 506
Cdd:cd05904 390 HTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEI 469
|
....*...
gi 1063734905 507 IDFISKQV 514
Cdd:cd05904 470 MDFVAKQV 477
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
55-514 |
8.85e-153 |
|
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: 445.12 E-value: 8.85e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 55 AFIDAATDHRISFSDLWMAVDRVAdCLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIA 134
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLA-AGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 135 DSNPKLAFTTPELAPKI------ASSGISIVL--ERVEDTLRVPRGLKVVGNLTEMMKKEPSGQAvrnqvhKDDTAMLLY 206
Cdd:cd05911 80 ISKPKVIFTDPDGLEKVkeaakeLGPKDKIIVldDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDG------KDDTAAILY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 207 SSGTTGRSKGVNSSHGNLIAHV--ARYIAEPFEQPQQTFICTVPLFHTFGLlNFVLATLALGTTVVILPRFDLGEMMAAV 284
Cdd:cd05911 154 SSGTTGLPKGVCLSHRNLIANLsqVQTFLYGNDGSNDVILGFLPLYHIYGL-FTTLASLLNGATVIIMPKFDSELFLDLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 285 EKYRATTLILVPPVLVTMINkaDQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVDVYQGYALTESNGAgaSIESV 364
Cdd:cd05911 233 EKYKITFLYLVPPIAAALAK--SPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGI--LTVNP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 365 EESRRYGAVGLLSCGVEARIVDPNTGQVMGLNQTGELWLKGPSIAKGYFRNEE---EIITSEGWLKTGDLCYIDNDGFLF 441
Cdd:cd05911 309 DGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEatkETFDEDGWLHTGDIGYFDEDGYLY 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063734905 442 IVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKVIDFISKQV 514
Cdd:cd05911 389 IVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKV 461
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
17-514 |
9.22e-148 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 435.04 E-value: 9.22e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 17 FCTSNSTFYSKRKPLALPSKESLDITTFI-SSQTYRGKTAFIDAATDHRISFSDLWMAVDRVADCLLHDVGIRRGDVVLV 95
Cdd:PLN02574 18 YSPETGIYSSKHPPVPLPSDPNLDAVSFIfSHHNHNGDTALIDSSTGFSISYSELQPLVKSMAAGLYHVMGVRQGDVVLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 96 LSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLAFTTPELAPKIASSGISIVLerVEDTLRVPRGLKV 175
Cdd:PLN02574 98 LLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSPLGVPVIG--VPENYDFDSKRIE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 176 VGNLTEMMKKEPsGQAVRNQVHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHV---ARYIAEPFEQP--QQTFICTVPLF 250
Cdd:PLN02574 176 FPKFYELIKEDF-DFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVelfVRFEASQYEYPgsDNVYLAALPMF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 251 HTFGLLNFVLATLALGTTVVILPRFDLGEMMAAVEKYRATTLILVPPVLVTMINKADQIMKKYDVSfLRTVRCGGAPLSK 330
Cdd:PLN02574 255 HIYGLSLFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLKS-LKQVSCGAAPLSG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 331 EVTQGFMKKYPTVDVYQGYALTESNGAGASIESVEESRRYGAVGLLSCGVEARIVDPNTGQVMGLNQTGELWLKGPSIAK 410
Cdd:PLN02574 334 KFIQDFVQTLPHVDFIQGYGMTESTAVGTRGFNTEKLSKYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMK 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 411 GYFRNEEEIITS---EGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQ 487
Cdd:PLN02574 414 GYLNNPKATQSTidkDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGE 493
|
490 500
....*....|....*....|....*..
gi 1063734905 488 FPMAYVARKPESNLCEKKVIDFISKQV 514
Cdd:PLN02574 494 IPVAFVVRRQGSTLSQEAVINYVAKQV 520
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
48-514 |
1.96e-125 |
|
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: 373.76 E-value: 1.96e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 48 QTYRGKTAFIDAatDHRISFSDLWMAVDRVAdCLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTAS 127
Cdd:COG0318 10 ARHPDRPALVFG--GRRLTYAELDARARRLA-AALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 128 EILRQIADSNPKLAFTtpelapkiassgisivlervedtlrvprglkvvgnltemmkkepsgqavrnqvhkddtAMLLYS 207
Cdd:COG0318 87 ELAYILEDSGARALVT----------------------------------------------------------ALILYT 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 208 SGTTGRSKGVNSSHGNLIAHVARYIAEPFEQPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPRFDLGEMMAAVEKY 287
Cdd:COG0318 109 SGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVLELIERE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 288 RATTLILVPPVLVTMINKADQimKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYpTVDVYQGYALTESNGAGASIESVEES 367
Cdd:COG0318 189 RVTVLFGVPTMLARLLRHPEF--ARYDLSSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTVNPEDPGE 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 368 RRYGAVGLLSCGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEEEiiTSE----GWLKTGDLCYIDNDGFLFIV 443
Cdd:COG0318 266 RRPGSVGRPLPGVEVRIVDED-GRELPPGEVGEIVVRGPNVMKGYWNDPEA--TAEafrdGWLRTGDLGRLDEDGYLYIV 342
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063734905 444 DRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKVIDFISKQV 514
Cdd:COG0318 343 GRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERL 413
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
24-514 |
4.03e-125 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 376.24 E-value: 4.03e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 24 FYSKRKPLALPSKESLDITTFISSQTYRGKTAFIDAATDHRISFSDLWMAVDRVADCLlHDVGIRRGDVVLVLSPNTISI 103
Cdd:PLN02246 10 FRSKLPDIYIPNHLPLHDYCFERLSEFSDRPCLIDGATGRVYTYADVELLSRRVAAGL-HKLGIRQGDVVMLLLPNCPEF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 104 PIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLAFTTPELAPKI----ASSGISIVL--ERVEDTLRvprglkvVG 177
Cdd:PLN02246 89 VLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYVDKLkglaEDDGVTVVTidDPPEGCLH-------FS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 178 NLTEMMKKEPsgQAVRnqVHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVARYI--AEP--FEQPQQTFICTVPLFHTF 253
Cdd:PLN02246 162 ELTQADENEL--PEVE--ISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVdgENPnlYFHSDDVILCVLPMFHIY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 254 GLLNFVLATLALGTTVVILPRFDLGEMMAAVEKYRATTLILVPPVLVTmINKADqIMKKYDVSFLRTVRCGGAPLSKEVT 333
Cdd:PLN02246 238 SLNSVLLCGLRVGAAILIMPKFEIGALLELIQRHKVTIAPFVPPIVLA-IAKSP-VVEKYDLSSIRMVLSGAAPLGKELE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 334 QGFMKKYPTVDVYQGYALTEsngAGASIE-SVEESRRYGAVGLLSCGV-----EARIVDPNTGQVMGLNQTGELWLKGPS 407
Cdd:PLN02246 316 DAFRAKLPNAVLGQGYGMTE---AGPVLAmCLAFAKEPFPVKSGSCGTvvrnaELKIVDPETGASLPRNQPGEICIRGPQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 408 IAKGYFRNEE---EIITSEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKE 484
Cdd:PLN02246 393 IMKGYLNDPEataNTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEV 472
|
490 500 510
....*....|....*....|....*....|
gi 1063734905 485 AGQFPMAYVARKPESNLCEKKVIDFISKQV 514
Cdd:PLN02246 473 AGEVPVAFVVRSNGSEITEDEIKQFVAKQV 502
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
46-514 |
3.11e-106 |
|
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: 325.29 E-value: 3.11e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 46 SSQTYRGKTAFIDaaTDHRISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNT 125
Cdd:cd05936 8 AARRFPDKTALIF--MGRKLTYRELDALAEAFAA-GLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 126 ASEILRQIADSNPKLAFTTPELAPKIASSgisivlervEDTLRVPrglkvvgnltemmkkepsgqavrnQVHKDDTAMLL 205
Cdd:cd05936 85 PRELEHILNDSGAKALIVAVSFTDLLAAG---------APLGERV------------------------ALTPEDVAVLQ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 206 YSSGTTGRSKGVNSSHGNLIAHVARYIA--EPFEQPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPRFDLGEMMAA 283
Cdd:cd05936 132 YTSGTTGVPKGAMLTHRNLVANALQIKAwlEDLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGVLKE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 284 VEKYRATTLILVPPVLVTMINKADqiMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYpTVDVYQGYALTESnGAGASIES 363
Cdd:cd05936 212 IRKHRVTIFPGVPTMYIALLNAPE--FKKRDFSSLRLCISGGAPLPVEVAERFEELT-GVPIVEGYGLTET-SPVVAVNP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 364 VEESRRYGAVGLLSCGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEEEiiTSE----GWLKTGDLCYIDNDGF 439
Cdd:cd05936 288 LDGPRKPGSIGIPLPGTEVKIVDDD-GEELPPGEVGELWVRGPQVMKGYWNRPEE--TAEafvdGWLRTGDIGYMDEDGY 364
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063734905 440 LFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKVIDFISKQV 514
Cdd:cd05936 365 FFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQL 439
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
52-514 |
2.06e-105 |
|
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: 325.25 E-value: 2.06e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 52 GKTAFIDAATDHRISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILR 131
Cdd:cd17642 32 GTIAFTDAHTGVNYSYAEYLEMSVRLAE-ALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 132 QIADSNPKLAFTTPELAPKIAS--------SGIsIVLERVEDTlrvpRGLKVVGNLTEmmKKEPSGQAVRNQV-----HK 198
Cdd:cd17642 111 SLNISKPTIVFCSKKGLQKVLNvqkklkiiKTI-IILDSKEDY----KGYQCLYTFIT--QNLPPGFNEYDFKppsfdRD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 199 DDTAMLLYSSGTTGRSKGVNSSHGNLIAHVARYIAEPFEQ---PQQTFICTVPLFHTFGLLNfVLATLALGTTVVILPRF 275
Cdd:cd17642 184 EQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNqiiPDTAILTVIPFHHGFGMFT-TLGYLICGFRVVLMYKF 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 276 DLGEMMAAVEKYRATTLILVPPvLVTMINKAdQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVDVYQGYALTESN 355
Cdd:cd17642 263 EEELFLRSLQDYKVQSALLVPT-LFAFFAKS-TLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQGYGLTETT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 356 GAgaSIESVEESRRYGAVGLLSCGVEARIVDPNTGQVMGLNQTGELWLKGPSIAKGYFRNEE---EIITSEGWLKTGDLC 432
Cdd:cd17642 341 SA--ILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEatkALIDKDGWLHSGDIA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 433 YIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKVIDFISK 512
Cdd:cd17642 419 YYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYVAS 498
|
..
gi 1063734905 513 QV 514
Cdd:cd17642 499 QV 500
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
48-453 |
1.99e-104 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 318.87 E-value: 1.99e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 48 QTYRGKTAFIDAaTDHRISFSDLWMAVDRVADCLLHdVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTAS 127
Cdd:pfam00501 6 ARTPDKTALEVG-EGRRLTYRELDERANRLAAGLRA-LGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 128 EILRQIADSNPKLAFTTPEL----APKIASSGISIVLERVEDTLRVPRGlkvvGNLTEMMKKEPSGQAVRNQVHKDDTAM 203
Cdd:pfam00501 84 ELAYILEDSGAKVLITDDALkleeLLEALGKLEVVKLVLVLDRDPVLKE----EPLPEEAKPADVPPPPPPPPDPDDLAY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 204 LLYSSGTTGRSKGVNSSHGNLIAHVARYIAEPFEQ----PQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPRF---D 276
Cdd:pfam00501 160 IIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGfglgPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFpalD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 277 LGEMMAAVEKYRATTLILVPPVLVTMINKADqiMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVdVYQGYALTESNG 356
Cdd:pfam00501 240 PAALLELIERYKVTVLYGVPTLLNMLLEAGA--PKRALLSSLRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTETTG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 357 AGASIESVEES-RRYGAVGLLSCGVEARIVDPNTGQVMGLNQTGELWLKGPSIAKGYFRNEE---EIITSEGWLKTGDLC 432
Cdd:pfam00501 317 VVTTPLPLDEDlRSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPEltaEAFDEDGWYRTGDLG 396
|
410 420
....*....|....*....|.
gi 1063734905 433 YIDNDGFLFIVDRLKELIKYK 453
Cdd:pfam00501 397 RRDEDGYLEIVGRKKDQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
200-513 |
6.63e-103 |
|
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: 311.91 E-value: 6.63e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 200 DTAMLLYSSGTTGRSKGVNSSHGNLIAHVARYIAEPFEQPQQTFICTVPLFHTFGLlNFVLATLALGTTVVILPRFDLGE 279
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGL-FGLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 280 MMAAVEKYRATTLILVPPVLVTMINKADQimKKYDVSFLRTVRCGGAPLSKEVTQGFMKKyPTVDVYQGYALTESNGAGA 359
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPES--AGYDLSSLRALVSGGAPLPPELLERFEEA-PGIKLVNGYGLTETGGTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 360 SIESVEESRRYGAVGLLSCGVEARIVDPNTGQVmGLNQTGELWLKGPSIAKGYFRNEE--EIITSEGWLKTGDLCYIDND 437
Cdd:cd04433 157 TGPPDDDARKPGSVGRPVPGVEVRIVDPDGGEL-PPGEIGELVVRGPSVMKGYWNNPEatAAVDEDGWYRTGDLGRLDED 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063734905 438 GFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKVIDFISKQ 513
Cdd:cd04433 236 GYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRER 311
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
24-514 |
4.22e-101 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 314.61 E-value: 4.22e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 24 FYSKRKPLALPSKESLDITTFISSQTYRGKTAFIDAATDHRISFSDLWMAVDRVADCLlHDVGIRRGDVVLVLSPNTISI 103
Cdd:PLN02330 15 FRSRYPSVPVPDKLTLPDFVLQDAELYADKVAFVEAVTGKAVTYGEVVRDTRRFAKAL-RSLGLRKGQVVVVVLPNVAEY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 104 PIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLAFTTPELAPKIASSGIS-IVLERVEDTLRVprglkvvgNLTEM 182
Cdd:PLN02330 94 GIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGLGLPvIVLGEEKIEGAV--------NWKEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 183 MK--KEPSGQAVRNQVHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVAR--YIAEPFEQPQQTFICTVPLFHTFGLLNF 258
Cdd:PLN02330 166 LEaaDRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSslFSVGPEMIGQVVTLGLIPFFHIYGITGI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 259 VLATLALGTTVVILPRFDLGEMMAAVEKYRATTLILVPPVLVTMINkaDQIMKKYDVSFL--RTVRCGGAPLSKEVTQGF 336
Cdd:PLN02330 246 CCATLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVK--NPIVEEFDLSKLklQAIMTAAAPLAPELLTAF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 337 MKKYPTVDVYQGYALTESngAGASIESVEESRRYG-----AVGLLSCGVEARIVDPNTGQVMGLNQTGELWLKGPSIAKG 411
Cdd:PLN02330 324 EAKFPGVQVQEAYGLTEH--SCITLTHGDPEKGHGiakknSVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 412 YFRNEEEI---ITSEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQF 488
Cdd:PLN02330 402 YYNNKEETdrtIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEI 481
|
490 500
....*....|....*....|....*.
gi 1063734905 489 PMAYVARKPESNLCEKKVIDFISKQV 514
Cdd:PLN02330 482 PAACVVINPKAKESEEDILNFVAANV 507
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
48-509 |
8.91e-95 |
|
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: 294.52 E-value: 8.91e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 48 QTYRGKTAFIDAatDHRISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTAS 127
Cdd:cd17631 6 RRHPDRTALVFG--GRSLTYAELDERVNRLAH-ALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 128 EILRQIADSNPKLAFttpelapkiassgisivlervedtlrvprglkvvgnltemmkkepsgqavrnqvhkDDTAMLLYS 207
Cdd:cd17631 83 EVAYILADSGAKVLF--------------------------------------------------------DDLALLMYT 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 208 SGTTGRSKGVNSSHGNLIAHVARYIAEPFEQPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPRFDLGEMMAAVEKY 287
Cdd:cd17631 107 SGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIERH 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 288 RATTLILVPPVLVTMINKADqiMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYptVDVYQGYALTESNGAGASIESVEES 367
Cdd:cd17631 187 RVTSFFLVPTMIQALLQHPR--FATTDLSSLRAVIYGGAPMPERLLRALQARG--VKFVQGYGMTETSPGVTFLSPEDHR 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 368 RRYGAVGLLSCGVEARIVDPNTGQVmGLNQTGELWLKGPSIAKGYFRNEEEiiTSE----GWLKTGDLCYIDNDGFLFIV 443
Cdd:cd17631 263 RKLGSAGRPVFFVEVRIVDPDGREV-PPGEVGEIVVRGPHVMAGYWNRPEA--TAAafrdGWFHTGDLGRLDEDGYLYIV 339
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063734905 444 DRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKVIDF 509
Cdd:cd17631 340 DRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAH 405
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
48-509 |
1.39e-93 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 294.12 E-value: 1.39e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 48 QTYRGKTAFIDAatDHRISFSDLWMAVDRVADCLLhDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTAS 127
Cdd:PRK07656 16 RRFGDKEAYVFG--DQRLTYAELNARVRRAAAALA-ALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 128 EILRQIADSNPKLAFTTPELAPKIASSGISI-VLERV---EDTLRVPRGLKVvGNLTEMMKKEPSGQAVRnQVHKDDTAM 203
Cdd:PRK07656 93 EAAYILARGDAKALFVLGLFLGVDYSATTRLpALEHVvicETEEDDPHTEKM-KTFTDFLAAGDPAERAP-EVDPDDVAD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 204 LLYSSGTTGRSKGVNSSHGNLIAHvARYIAEPFE-QPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPRFDLGEMMA 282
Cdd:PRK07656 171 ILFTSGTTGRPKGAMLTHRQLLSN-AADWAEYLGlTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLPVFDPDEVFR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 283 AVEKYRATTLILVPPVLVTMINKADQimKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVDVYQGYALTESNGAgASIE 362
Cdd:PRK07656 250 LIETERITVLPGPPTMYNSLLQHPDR--SAEDLSSLRLAVTGAASMPVALLERFESELGVDIVLTGYGLSEASGV-TTFN 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 363 SVEESRRYGA--VGLLSCGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEE---EIITSEGWLKTGDLCYIDND 437
Cdd:PRK07656 327 RLDDDRKTVAgtIGTAIAGVENKIVNEL-GEEVPVGEVGELLVRGPNVMKGYYDDPEataAAIDADGWLHTGDLGRLDEE 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063734905 438 GFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKVIDF 509
Cdd:PRK07656 406 GYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEELIAY 477
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
45-498 |
5.30e-86 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 275.30 E-value: 5.30e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 45 ISSQTYRGKTAFIdaATDHRISFSDLWMAVDRVADCLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLN 124
Cdd:PRK08314 18 VSARRYPDKTAIV--FYGRAISYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 125 TASEILRQIADSNPKLAFTTPELAPKIASSGISIVLERV-----EDTLRVPRGLKVvgnlTEMMKKEPSGQAVRN----- 194
Cdd:PRK08314 96 REEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRHVivaqySDYLPAEPEIAV----PAWLRAEPPLQALAPggvva 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 195 --------------QVHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVARYIAEPFEQPQQTFICTVPLFHTFGLLNFVL 260
Cdd:PRK08314 172 wkealaaglappphTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 261 ATLALGTTVVILPRFDLGEMMAAVEKYRATTLILVPPVLVTMInkADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKY 340
Cdd:PRK08314 252 APIYAGATVVLMPRWDREAAARLIERYRVTHWTNIPTMVVDFL--ASPGLAERDLSSLRYIGGGGAAMPEAVAERLKELT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 341 pTVDVYQGYALTESngAGASIESVEESRRYGAVGLLSCGVEARIVDPNTGQVMGLNQTGELWLKGPSIAKGYFRNEEE-- 418
Cdd:PRK08314 330 -GLDYVEGYGLTET--MAQTHSNPPDRPKLQCLGIPTFGVDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEAta 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 419 --IITSEG--WLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVA 494
Cdd:PRK08314 407 eaFIEIDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVV 486
|
....
gi 1063734905 495 RKPE 498
Cdd:PRK08314 487 LRPE 490
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
60-514 |
1.34e-83 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 268.21 E-value: 1.34e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 60 ATDHRISFSDLWMAVDRVADCLLhDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLttaNPLNT---ASEILRQIADS 136
Cdd:PRK06187 27 FDGRRTTYAELDERVNRLANALR-ALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVL---HPINIrlkPEEIAYILNDA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 137 NPKLAFTTPELAPKIAS-----SGISIVLerVEDTLRVPRGLKVVGNLTEMMKKEPSgQAVRNQVHKDDTAMLLYSSGTT 211
Cdd:PRK06187 103 EDRVVLVDSEFVPLLAAilpqlPTVRTVI--VEGDGPAAPLAPEVGEYEELLAAASD-TFDFPDIDENDAAAMLYTSGTT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 212 GRSKGVNSSHGNLIAHvARYIAEPFE-QPQQTFICTVPLFHTFGLLNFVLATLAlGTTVVILPRFDLGEMMAAVEKYRAT 290
Cdd:PRK06187 180 GHPKGVVLSHRNLFLH-SLAVCAWLKlSRDDVYLVIVPMFHVHAWGLPYLALMA-GAKQVIPRRFDPENLLDLIETERVT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 291 TLILVPPVLvTMINKADqIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYpTVDVYQGYALTESNGAGASI----ESVEE 366
Cdd:PRK06187 258 FFFAVPTIW-QMLLKAP-RAYFVDFSSLRLVIYGGAALPPALLREFKEKF-GIDLVQGYGMTETSPVVSVLppedQLPGQ 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 367 SRRYGAVGLLSCGVEARIVDPNtGQVM--GLNQTGELWLKGPSIAKGYFRNEEEiiTSE----GWLKTGDLCYIDNDGFL 440
Cdd:PRK06187 335 WTKRRSAGRPLPGVEARIVDDD-GDELppDGGEVGEIIVRGPWLMQGYWNRPEA--TAEtidgGWLHTGDVGYIDEDGYL 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063734905 441 FIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKVIDFISKQV 514
Cdd:PRK06187 412 YITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAKELRAFLRGRL 485
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
55-514 |
7.72e-82 |
|
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: 263.02 E-value: 7.72e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 55 AFIDAATDHRISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVlttANPLNTAS---EILR 131
Cdd:cd05926 5 ALVVPGSTPALTYADLAELVDDLAR-QLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAV---VAPLNPAYkkaEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 132 QIADSNPKLAFTTPELAPKIASSGISIVLERVEDTLRVPRGLKVVGN----LTEMMKKEPSGQAVrnqVHKDDTAMLLYS 207
Cdd:cd05926 81 YLADLGSKLVLTPKGELGPASRAASKLGLAILELALDVGVLIRAPSAeslsNLLADKKNAKSEGV---PLPDDLALILHT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 208 SGTTGRSKGVNSSHGNLIAHVaRYIAEPFE-QPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPRFDLGEMMAAVEK 286
Cdd:cd05926 158 SGTTGRPKGVPLTHRNLAASA-TNITNTYKlTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDVRD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 287 YRATTLILVPPVLVTMINKADQIMKKYDVSfLRTVRCGGAPLSKEVTQGFMKKYpTVDVYQGYALTESNGAGASIESVEE 366
Cdd:cd05926 237 YNATWYTAVPTIHQILLNRPEPNPESPPPK-LRFIRSCSASLPPAVLEALEATF-GAPVLEAYGMTEAAHQMTSNPLPPG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 367 SRRYGAVGLLScGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEEEIITS---EGWLKTGDLCYIDNDGFLFIV 443
Cdd:cd05926 315 PRKPGSVGKPV-GVEVRILDED-GEILPPGVVGEICLRGPNVTRGYLNNPEANAEAafkDGWFRTGDLGYLDADGYLFLT 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063734905 444 DRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKVIDFISKQV 514
Cdd:cd05926 393 GRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHL 463
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
64-498 |
1.37e-78 |
|
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: 252.40 E-value: 1.37e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 64 RISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLAFT 143
Cdd:cd05935 1 SLTYLELLEVVKKLAS-FLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 144 TPELapkiassgisivlervedtlrvprglkvvgnltemmkkepsgqavrnqvhkDDTAMLLYSSGTTGRSKGVNSSHGN 223
Cdd:cd05935 80 GSEL---------------------------------------------------DDLALIPYTSGTTGLPKGCMHTHFS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 224 LIAHVARYIAEPFEQPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPRFDLGEMMAAVEKYRATTLILVPPVLVTMI 303
Cdd:cd05935 109 AAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 304 NKADqiMKKYDVSFLRTVRCGGAPLSKEVTQGfMKKYPTVDVYQGYALTESNGAGASIESVEESRRygAVGLLSCGVEAR 383
Cdd:cd05935 189 ATPE--FKTRDLSSLKVLTGGGAPMPPAVAEK-LLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQ--CLGIP*FGVDAR 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 384 IVDPNTGQVMGLNQTGELWLKGPSIAKGYFRNEEEiiTSEGW--------LKTGDLCYIDNDGFLFIVDRLKELIKYKGY 455
Cdd:cd05935 264 VIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEE--TEESFieikgrrfFRTGDLGYMDEEGYFFFVDRVKRMINVSGF 341
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1063734905 456 QVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPE 498
Cdd:cd05935 342 KVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPE 384
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
51-514 |
1.69e-78 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 256.19 E-value: 1.69e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 51 RGKTAFI---DAATDHRISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTAS 127
Cdd:COG0365 23 GDKVALIwegEDGEERTLTYAELRREVNRFAN-ALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 128 EILRQIADSNPKLAFTTPE---------LAPKI--ASSGIS-----IVLERVEDTLRVPRGLkvvgNLTEMMKKEpSGQA 191
Cdd:COG0365 102 ALADRIEDAEAKVLITADGglrggkvidLKEKVdeALEELPslehvIVVGRTGADVPMEGDL----DWDELLAAA-SAEF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 192 VRNQVHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVARYIAEPFE-QPQQTFICTVPLFHTFGLLNFVLATLALGTTVV 270
Cdd:COG0365 177 EPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDlKPGDVFWCTADIGWATGHSYIVYGPLLNGATVV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 271 IL---PRF-DLGEMMAAVEKYRATTLILVPPVLVTMINKADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKY--PTVD 344
Cdd:COG0365 257 LYegrPDFpDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVgvPIVD 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 345 VYQGyalTESNG---AGASIESVeesrRYGAVGLLSCGVEARIVDPNtGQVMGLNQTGELWLKG--PSIAKGYFRNEEEI 419
Cdd:COG0365 337 GWGQ---TETGGifiSNLPGLPV----KPGSMGKPVPGYDVAVVDED-GNPVPPGEEGELVIKGpwPGMFRGYWNDPERY 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 420 I-----TSEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVA 494
Cdd:COG0365 409 RetyfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVV 488
|
490 500
....*....|....*....|...
gi 1063734905 495 RKPESNLCE---KKVIDFISKQV 514
Cdd:COG0365 489 LKPGVEPSDelaKELQAHVREEL 511
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
46-486 |
3.75e-70 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 234.51 E-value: 3.75e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 46 SSQTYRGKTA--FIDAATdhriSFSDLWMAVDRVADCLlHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPL 123
Cdd:PRK05605 41 AVARFGDRPAldFFGATT----TYAELGKQVRRAAAGL-RALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 124 NTASEILRQIADSNPKLAFTTPELAPkiassgisiVLERVEDTLRVPRGLKVvgNLTEMMKKE---------PSGQAVRN 194
Cdd:PRK05605 116 YTAHELEHPFEDHGARVAIVWDKVAP---------TVERLRRTTPLETIVSV--NMIAAMPLLqrlalrlpiPALRKARA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 195 QVH------------------------------KDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVAR---YIAEPFEQPQq 241
Cdd:PRK05605 185 ALTgpapgtvpwetlvdaaiggdgsdvshprptPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQgkaWVPGLGDGPE- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 242 TFICTVPLFHTFGL-LNFVLAtLALGTTVVILPRFDLGEMMAAVEKYRATTLILVPPVLVTMINKAdqimKKYDVSfLRT 320
Cdd:PRK05605 264 RVLAALPMFHAYGLtLCLTLA-VSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAA----EERGVD-LSG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 321 VR---CGGAPLS-------KEVTQGFMkkyptvdvYQGYALTESNGAgASIESVEESRRYGAVGLLSCGVEARIVDP-NT 389
Cdd:PRK05605 338 VRnafSGAMALPvstvelwEKLTGGLL--------VEGYGLTETSPI-IVGNPMSDDRRPGYVGVPFPDTEVRIVDPeDP 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 390 GQVMGLNQTGELWLKGPSIAKGYFRNEEEIITS--EGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLL 467
Cdd:PRK05605 409 DETMPDGEEGELLVRGPQVFKGYWNRPEETAKSflDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLR 488
|
490
....*....|....*....
gi 1063734905 468 NHPDILDAAVIPFPdKEAG 486
Cdd:PRK05605 489 EHPGVEDAAVVGLP-REDG 506
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
64-514 |
3.11e-67 |
|
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: 222.55 E-value: 3.11e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 64 RISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTtanPLNTA---SEILRQIADSNPKL 140
Cdd:cd05934 3 RWTYAELLRESARIAA-ALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLV---PINTAlrgDELAYIIDHSGAQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 141 AFTtpelapkiassgisivlervedtlrvprglkvvgnltemmkkepsgqavrnqvhkdDTAMLLYSSGTTGRSKGVNSS 220
Cdd:cd05934 79 VVV--------------------------------------------------------DPASILYTSGTTGPPKGVVIT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 221 HGNLiAHVARYIAEPFE-QPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPRFDLGEMMAAVEKYRATTLILVPpVL 299
Cdd:cd05934 103 HANL-TFAGYYSARRFGlGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLG-AM 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 300 VTMINKADQIMKKYDvsflRTVR-CGGAPLSKEVTQGFMKKYpTVDVYQGYALTEsnGAGASIESVEESRRYGAVGLLSC 378
Cdd:cd05934 181 LSYLLAQPPSPDDRA----HRLRaAYGAPNPPELHEEFEERF-GVRLLEGYGMTE--TIVGVIGPRDEPRRPGSIGRPAP 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 379 GVEARIVDPNTGQVmGLNQTGELWLK---GPSIAKGYFRNEEEIITS--EGWLKTGDLCYIDNDGFLFIVDRLKELIKYK 453
Cdd:cd05934 254 GYEVRIVDDDGQEL-PAGEPGELVIRglrGWGFFKGYYNMPEATAEAmrNGWFHTGDLGYRDADGFFYFVDRKKDMIRRR 332
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063734905 454 GYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKVIDFISKQV 514
Cdd:cd05934 333 GENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQL 393
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
53-498 |
7.46e-67 |
|
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: 222.17 E-value: 7.46e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 53 KTAFIDAatDHRISFSDLWMAVDRVADCLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVlttANPLNTAseilrq 132
Cdd:cd05941 2 RIAIVDD--GDSITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGV---AVPLNPS------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 133 iadsnpklaFTTPELAPKIASSGISIVLERvedtlrvprglkvvgnltemmkkepsgqavrnqvhkddtAMLLYSSGTTG 212
Cdd:cd05941 71 ---------YPLAELEYVITDSEPSLVLDP---------------------------------------ALILYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 213 RSKGVNSSHGNLIAHVaRYIAEPFE-QPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPRFDLGEMMAAVEKYRATT 291
Cdd:cd05941 103 RPKGVVLTHANLAANV-RALVDAWRwTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRLMPSITV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 292 LILVPPVLVTMI---NKADQIMKKYDVSFLRTVR---CGGAPLSKEVTQGFMKKYPTVdVYQGYALTE-----SNGAgas 360
Cdd:cd05941 182 FMGVPTIYTRLLqyyEAHFTDPQFARAAAAERLRlmvSGSAALPVPTLEEWEAITGHT-LLERYGMTEigmalSNPL--- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 361 iesvEESRRYGAVGLLSCGVEARIVDPNTGQVMGLNQTGELWLKGPSIAKGYFRNEE---EIITSEGWLKTGDLCYIDND 437
Cdd:cd05941 258 ----DGERRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEatkEEFTDDGWFKTGDLGVVDED 333
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063734905 438 GFLFIVDRLK-ELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPE 498
Cdd:cd05941 334 GYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAG 395
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
54-514 |
2.29e-66 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 225.60 E-value: 2.29e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 54 TAFIDAATDH---RISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSvmslGAVLTTANPLNTA---- 126
Cdd:PRK07529 45 SFLLDADPLDrpeTWTYAELLADVTRTAN-LLHSLGVGPGDVVAFLLPNLPETHFALWG----GEAAGIANPINPLlepe 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 127 --SEILRQiadSNPKL-----AFTTPELAPKIAS------SGISIVLERVEDTLRVPRGLKV----------VGNLTEMM 183
Cdd:PRK07529 120 qiAELLRA---AGAKVlvtlgPFPGTDIWQKVAEvlaalpELRTVVEVDLARYLPGPKRLAVplirrkaharILDFDAEL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 184 KKEPSGQAVR-NQVHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVARYIAEPFEQPQQTFICTVPLFHTFGLLNFVLAT 262
Cdd:PRK07529 197 ARQPGDRLFSgRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAP 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 263 LALGTTVVIL-------PRFdLGEMMAAVEKYRATTLILVPPVL-VTMINKADqimkKYDVSFLRTVRCGGAPLSKEVTQ 334
Cdd:PRK07529 277 LARGAHVVLAtpqgyrgPGV-IANFWKIVERYRINFLSGVPTVYaALLQVPVD----GHDISSLRYALCGAAPLPVEVFR 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 335 GFMKKypT-VDVYQGYALTESNgAGASIESVEESRRYGAVGLLSCGVEARIV--DPNTGQV--MGLNQTGELWLKGPSIA 409
Cdd:PRK07529 352 RFEAA--TgVRIVEGYGLTEAT-CVSSVNPPDGERRIGSVGLRLPYQRVRVVilDDAGRYLrdCAVDEVGVLCIAGPNVF 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 410 KGYFRNEEE--IITSEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQ 487
Cdd:PRK07529 429 SGYLEAAHNkgLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGE 508
|
490 500
....*....|....*....|....*..
gi 1063734905 488 FPMAYVARKPESNLCEKKVIDFISKQV 514
Cdd:PRK07529 509 LPVAYVQLKPGASATEAELLAFARDHI 535
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
66-512 |
1.49e-65 |
|
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: 218.47 E-value: 1.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 66 SFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLAFTTP 145
Cdd:TIGR01923 1 TWQDLDCEAAHLAK-ALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 146 ELApkiassgisivlERVEDTLrvprglkvvgNLTEMMKKEPSGQAVRNQVHKDDTAMLLYSSGTTGRSKGVNSSHGNLI 225
Cdd:TIGR01923 80 LLE------------EKDFQAD----------SLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 226 AHvARYIAEPFE-QPQQTFICTVPLFHTFGLlNFVLATLALGTTVVILPRF-DLGEMMAaveKYRATTLILVPPVLVTMi 303
Cdd:TIGR01923 138 AS-AVGSKENLGfTEDDNWLLSLPLYHISGL-SILFRWLIEGATLRIVDKFnQLLEMIA---NERVTHISLVPTQLNRL- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 304 nkADQIMKKYDvsfLRTVRCGGAPLSKEVTQgfMKKYPTVDVYQGYALTESNGAGASIEsVEESRRYGAVGLLSCGVEAR 383
Cdd:TIGR01923 212 --LDEGGHNEN---LRKILLGGSAIPAPLIE--EAQQYGLPIYLSYGMTETCSQVTTAT-PEMLHARPDVGRPLAGREIK 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 384 IvdpntgQVMGLNQTGELWLKGPSIAKGYFRNEE--EIITSEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAE 461
Cdd:TIGR01923 284 I------KVDNKEGHGEIMVKGANLMKGYLYQGEltPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEE 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1063734905 462 LEALLLNHPDILDAAVIPFPDKEAGQFPMAYVarKPESNLCEKKVIDFISK 512
Cdd:TIGR01923 358 IETVLYQHPGIQEAVVVPKPDAEWGQVPVAYI--VSESDISQAKLIAYLTE 406
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
53-509 |
2.22e-64 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 216.75 E-value: 2.22e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 53 KTAFIDAatDHRISFSDLWMAVDRVADCLLHdVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQ 132
Cdd:PRK03640 18 RTAIEFE--EKKVTFMELHEAVVSVAGKLAA-LGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 133 IADSNPKLAFTTPELAPKIaSSGISIVLErvedtlrvprglkvvgnltEMMKKEPSGQAVRNQVHKDDTAMLLYSSGTTG 212
Cdd:PRK03640 95 LDDAEVKCLITDDDFEAKL-IPGISVKFA-------------------ELMNGPKEEAEIQEEFDLDEVATIMYTSGTTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 213 RSKGVNSSHGNliaHVARYIAEPFE---QPQQTFICTVPLFHTFGLlNFVLATLALGTTVVILPRFDLGEMMAAVEKYRA 289
Cdd:PRK03640 155 KPKGVIQTYGN---HWWSAVGSALNlglTEDDCWLAAVPIFHISGL-SILMRSVIYGMRVVLVEKFDAEKINKLLQTGGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 290 TTLILVPPVLVTMINKADQimKKYDVSFlRTVRCGGAPLSK---EVTQgfMKKYPtvdVYQGYALTESNGAGASIESVEE 366
Cdd:PRK03640 231 TIISVVSTMLQRLLERLGE--GTYPSSF-RCMLLGGGPAPKpllEQCK--EKGIP---VYQSYGMTETASQIVTLSPEDA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 367 SRRYGAVG--LLSCGVeaRIVDpnTGQVMGLNQTGELWLKGPSIAKGYFRNEE---EIITSeGWLKTGDLCYIDNDGFLF 441
Cdd:PRK03640 303 LTKLGSAGkpLFPCEL--KIEK--DGVVVPPFEEGEIVVKGPNVTKGYLNREDatrETFQD-GWFKTGDIGYLDEEGFLY 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063734905 442 IVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARkpESNLCEKKVIDF 509
Cdd:PRK03640 378 VLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVTEEELRHF 443
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
65-515 |
9.45e-64 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 217.21 E-value: 9.45e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 65 ISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLAFTT 144
Cdd:PRK06710 50 ITFSVFHDKVKRFAN-YLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 145 PELAPKIASSGIS-----IVLERVEDTLRVPRGLkvvgnLTEMMKKEPSGQAVR----------NQVHKD---------- 199
Cdd:PRK06710 129 DLVFPRVTNVQSAtkiehVIVTRIADFLPFPKNL-----LYPFVQKKQSNLVVKvsesetihlwNSVEKEvntgvevpcd 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 200 ---DTAMLLYSSGTTGRSKGVNSSHGNLIAHVARYIAEPFE--QPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPR 274
Cdd:PRK06710 204 penDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNckEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPK 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 275 FDLGEMMAAVEKYRATTLILVPPVLVTMINKAdqIMKKYDVSFLRTVRCGGAPLSKEVTQGFmKKYPTVDVYQGYALTES 354
Cdd:PRK06710 284 FDMKMVFEAIKKHKVTLFPGAPTIYIALLNSP--LLKEYDISSIRACISGSAPLPVEVQEKF-ETVTGGKLVEGYGLTES 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 355 NGAGASiESVEESRRYGAVGLLSCGVEARIVDPNTGQVMGLNQTGELWLKGPSIAKGYFRNEEEI--ITSEGWLKTGDLC 432
Cdd:PRK06710 361 SPVTHS-NFLWEKRVPGSIGVPWPDTEAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETaaVLQDGWLHTGDVG 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 433 YIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKpESNLCEKKVIDFISK 512
Cdd:PRK06710 440 YMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLK-EGTECSEEELNQFAR 518
|
...
gi 1063734905 513 QVL 515
Cdd:PRK06710 519 KYL 521
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
199-511 |
1.27e-63 |
|
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: 210.98 E-value: 1.27e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 199 DDTAMLLYSSGTTGRSKGVNSSHGNLIAHvARYIAEPFEQPQQTFICT-VPLFHTFGLLNFVLATLALGTTVVIL-PRFD 276
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNN-GYFIGERLGLTEQDRLCIpVPLFHCFGSVLGVLACLTHGATMVFPsPSFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 277 LGEMMAAVEKYRATTLILVPPVLVTMINKADqiMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVDVYQGYALTESN- 355
Cdd:cd05917 81 PLAVLEAIEKEKCTALHGVPTMFIAELEHPD--FDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETSp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 356 -----GAGASIEsveesRRYGAVGLLSCGVEARIVDPNTGQVMGLNQTGELWLKGPSIAKGYFRNEE---EIITSEGWLK 427
Cdd:cd05917 159 vstqtRTDDSIE-----KRVNTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEktaEAIDGDGWLH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 428 TGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKVI 507
Cdd:cd05917 234 TGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIK 313
|
....
gi 1063734905 508 DFIS 511
Cdd:cd05917 314 AYCK 317
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
49-498 |
1.42e-63 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 215.31 E-value: 1.42e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 49 TYRGKTAFIDAATdhRISFSDLWMAVDRVADCLLhDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASE 128
Cdd:cd05959 16 GRGDKTAFIDDAG--SLTYAELEAEARRVAGALR-ALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 129 ILRQIADSNPKLAFTTPELAPKIASsgisiVLERVEDTLRV------PRGLKVVGNLTEMMKKEpSGQAVRNQVHKDDTA 202
Cdd:cd05959 93 YAYYLEDSRARVVVVSGELAPVLAA-----ALTKSEHTLVVlivsggAGPEAGALLLAELVAAE-AEQLKPAATHADDPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 203 MLLYSSGTTGRSKGVNSSHGNLIaHVARYIAEPFEQPQQTFIC--TVPLFHTFGLLNFVLATLALGTTVVILP-RFDLGE 279
Cdd:cd05959 167 FWLYSSGSTGRPKGVVHLHADIY-WTAELYARNVLGIREDDVCfsAAKLFFAYGLGNSLTFPLSVGATTVLMPeRPTPAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 280 MMAAVEKYRATTLILVPPVLVTMInkADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYpTVDVYQGYALTE------ 353
Cdd:cd05959 246 VFKRIRRYRPTVFFGVPTLYAAML--AAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARF-GLDILDGIGSTEmlhifl 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 354 SNGAGASiesveesrRYGAVGLLSCGVEARIVDPNTGQVMGlNQTGELWLKGPSIAKGYFRNEEEI-ITSEG-WLKTGDL 431
Cdd:cd05959 323 SNRPGRV--------RYGTTGKPVPGYEVELRDEDGGDVAD-GEPGELYVRGPSSATMYWNNRDKTrDTFQGeWTRTGDK 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063734905 432 CYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPE 498
Cdd:cd05959 394 YVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPG 460
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
65-512 |
4.20e-63 |
|
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: 211.44 E-value: 4.20e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 65 ISFSDLWMAVDRVADCLLHdVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLaftt 144
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAA-LGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 145 pelapkiassgisivlervedtlrvprglkvvgnltemmkkepsgqavrnqvhkDDTAMLLYSSGTTGRSKGVNSSHGNL 224
Cdd:cd05912 77 ------------------------------------------------------DDIATIMYTSGTTGKPKGVQQTFGNH 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 225 IAHvARYIAEPFEQPQQT-FICTVPLFHTFGLlNFVLATLALGTTVVILPRFDLGEMMAAVEKYRATTLILVPpvlvTMI 303
Cdd:cd05912 103 WWS-AIGSALNLGLTEDDnWLCALPLFHISGL-SILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVP----TML 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 304 NkadQIMKKYDVSFLRTVRC---GGAPLSKEV-TQGFMKKYPtvdVYQGYALTE--SNGAGASIESVEEsrRYGAVGLLS 377
Cdd:cd05912 177 Q---RLLEILGEGYPNNLRCillGGGPAPKPLlEQCKEKGIP---VYQSYGMTEtcSQIVTLSPEDALN--KIGSAGKPL 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 378 CGVEARIVDPNTGqvmgLNQTGELWLKGPSIAKGYFRNEE--EIITSEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGY 455
Cdd:cd05912 249 FPVELKIEDDGQP----PYEVGEILLKGPNVTKGYLNRPDatEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGE 324
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063734905 456 QVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARkpESNLCEKKVIDFISK 512
Cdd:cd05912 325 NIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVS--ERPISEEELIAYCSE 379
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
65-485 |
6.71e-63 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 215.73 E-value: 6.71e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 65 ISFSDLWMAVDRVAdCLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLAFT- 143
Cdd:COG1022 41 LTWAEFAERVRALA-AGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVe 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 144 TPELAPKIASSGISIV-LERV----EDTLRVPRGLKVVGNLTEMMKKEPSGQAV---RNQVHKDDTAMLLYSSGTTGRSK 215
Cdd:COG1022 120 DQEQLDKLLEVRDELPsLRHIvvldPRGLRDDPRLLSLDELLALGREVADPAELearRAAVKPDDLATIIYTSGTTGRPK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 216 GVNSSHGNLIAHVaRYIAEPFE-QPQQTFICTVPLFHTFGLLnFVLATLALGTTVVILPRFD-LGEMMAAVekyRATTLI 293
Cdd:COG1022 200 GVMLTHRNLLSNA-RALLERLPlGPGDRTLSFLPLAHVFERT-VSYYALAAGATVAFAESPDtLAEDLREV---KPTFML 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 294 LVPPVL-------VTMINKADQIMKK--------------------------------YDVSFLRTVR-----------C 323
Cdd:COG1022 275 AVPRVWekvyagiQAKAEEAGGLKRKlfrwalavgrryararlagkspslllrlkhalADKLVFSKLRealggrlrfavS 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 324 GGAPLSKEVTQ-----GfmkkyptVDVYQGYALTESnGAGASIeSVEESRRYGAVGLLSCGVEARIVDpntgqvmglnqT 398
Cdd:COG1022 355 GGAALGPELARffralG-------IPVLEGYGLTET-SPVITV-NRPGDNRIGTVGPPLPGVEVKIAE-----------D 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 399 GELWLKGPSIAKGYFRNEE---EIITSEGWLKTGDLCYIDNDGFLFIVDRLKELI-----KYkgyqVPPAELEALLLNHP 470
Cdd:COG1022 415 GEILVRGPNVMKGYYKNPEataEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIvtsggKN----VAPQPIENALKASP 490
|
490 500
....*....|....*....|....*
gi 1063734905 471 DILDAAVI----PF------PDKEA 485
Cdd:COG1022 491 LIEQAVVVgdgrPFlaalivPDFEA 515
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
63-501 |
6.72e-63 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 214.90 E-value: 6.72e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 63 HRISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLAF 142
Cdd:PRK06178 57 HVITYAELDELSDRFAA-LLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 143 TTPELAP------------KIASSGISIVLERvEDTLRVPRGLK----VVGNLTEMMKKEP--SGQAVRNQVHKDDTAML 204
Cdd:PRK06178 136 ALDQLAPvveqvraetslrHVIVTSLADVLPA-EPTLPLPDSLRaprlAAAGAIDLLPALRacTAPVPLPPPALDALAAL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 205 LYSSGTTGRSKGVNSSHGNLIAHVARY--IAEPFEQPQqTFICTVPLF----HTFGLLnfvlATLALGTTVVILPRFDLG 278
Cdd:PRK06178 215 NYTGGTTGMPKGCEHTQRDMVYTAAAAyaVAVVGGEDS-VFLSFLPEFwiagENFGLL----FPLFSGATLVLLARWDAV 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 279 EMMAAVEKYRATTLILVppvlvtmINKADQIM-----KKYDVSFLRTVRCggaplskevtQGFMKKYpTVDVYQ------ 347
Cdd:PRK06178 290 AFMAAVERYRVTRTVML-------VDNAVELMdhprfAEYDLSSLRQVRV----------VSFVKKL-NPDYRQrwralt 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 348 -------GYALTESNGA-----GASIESVEESRRYGAVGLLSCGVEARIVDPNTGQVMGLNQTGELWLKGPSIAKGYFRN 415
Cdd:PRK06178 352 gsvlaeaAWGMTETHTCdtftaGFQDDDFDLLSQPVFVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNK 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 416 EEeiITSE----GWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMA 491
Cdd:PRK06178 432 PE--ATAEalrdGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVA 509
|
490
....*....|
gi 1063734905 492 YVARKPESNL 501
Cdd:PRK06178 510 FVQLKPGADL 519
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
55-493 |
8.79e-63 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 213.23 E-value: 8.79e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 55 AFIDAATDHRISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIA 134
Cdd:PRK08276 2 AVIMAPSGEVVTYGELEARSNRLAH-GLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 135 DSNPKLAFTTPELAPkiassgisiVLERVEDTLrvPRGLKVVGnlteMMKKEPSG-----QAVRNQvhkDDT-------- 201
Cdd:PRK08276 81 DSGAKVLIVSAALAD---------TAAELAAEL--PAGVPLLL----VVAGPVPGfrsyeEALAAQ---PDTpiadetag 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 202 AMLLYSSGTTGRSKGV------NSSHGNLIAHVARYIAEPFEQPQQTFICTVPLFHTfGLLNFVLATLALGTTVVILPRF 275
Cdd:PRK08276 143 ADMLYSSGTTGRPKGIkrplpgLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHT-APLRFGMSALALGGTVVVMEKF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 276 DLGEMMAAVEKYRATTLILVPPVLVTMINKADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKY-PTVDVYqgYALTES 354
Cdd:PRK08276 222 DAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYDVSSLRVAIHAAAPCPVEVKRAMIDWWgPIIHEY--YASSEG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 355 NGAGAsIESVEESRRYGAVG--LLScgvEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEEEIITSE---GWLKTG 429
Cdd:PRK08276 300 GGVTV-ITSEDWLAHPGSVGkaVLG---EVRILDED-GNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARnphGWVTVG 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063734905 430 DLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYV 493
Cdd:PRK08276 375 DVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVV 438
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
59-514 |
3.58e-62 |
|
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: 211.72 E-value: 3.58e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 59 AATDHRISFSDLWMAVDRVADCLlHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNP 138
Cdd:cd12119 20 EGEVHRYTYAEVAERARRLANAL-RRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAED 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 139 KLAFTTPELAPkiassgisiVLERVEDTLrvPRGLKVVGNLTEMMKKEPSGQAVRN---------------QVHKDDTAM 203
Cdd:cd12119 99 RVVFVDRDFLP---------LLEAIAPRL--PTVEHVVVMTDDAAMPEPAGVGVLAyeellaaespeydwpDFDENTAAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 204 LLYSSGTTGRSKGVNSSHGNLIAH---VARYIAEPFEQpQQTFICTVPLFH--TFGLlnfVLATLALGTTVViLP-RFDL 277
Cdd:cd12119 168 ICYTSGTTGNPKGVVYSHRSLVLHamaALLTDGLGLSE-SDVVLPVVPMFHvnAWGL---PYAAAMVGAKLV-LPgPYLD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 278 GEMMAA-VEKYRATTLILVPPVLVTMINKADQimKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYptVDVYQGYALTESN- 355
Cdd:cd12119 243 PASLAElIEREGVTFAAGVPTVWQGLLDHLEA--NGRDLSSLRRVVIGGSAVPRSLIEAFEERG--VRVIHAWGMTETSp 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 356 -------GAGASIESVEESRRYGAV-GLLSCGVEARIVDPNtGQVM---GlNQTGELWLKGPSIAKGYFRNEEEII--TS 422
Cdd:cd12119 319 lgtvarpPSEHSNLSEDEQLALRAKqGRPVPGVELRIVDDD-GRELpwdG-KAVGELQVRGPWVTKSYYKNDEESEalTE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 423 EGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLC 502
Cdd:cd12119 397 DGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVT 476
|
490
....*....|..
gi 1063734905 503 EKKVIDFISKQV 514
Cdd:cd12119 477 AEELLEFLADKV 488
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
64-514 |
3.59e-62 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 212.71 E-value: 3.59e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 64 RISFSDLWMAVDRVADCLLHdVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLAFT 143
Cdd:PRK12583 45 RYTWRQLADAVDRLARGLLA-LGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVIC 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 144 TP------------ELAPKIASSGisivlervEDTLRVPRgLKVVGNLTEMMKKEPSG-------------------QAV 192
Cdd:PRK12583 124 ADafktsdyhamlqELLPGLAEGQ--------PGALACER-LPELRGVVSLAPAPPPGflawhelqargetvsrealAER 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 193 RNQVHKDDTAMLLYSSGTTGRSKGVNSSHGNlIAHVARYIAEPFEQPQQTFICT-VPLFHTFGLLNFVLATLALGTTVVI 271
Cdd:PRK12583 195 QASLDRDDPINIQYTSGTTGFPKGATLSHHN-ILNNGYFVAESLGLTEHDRLCVpVPLYHCFGMVLANLGCMTVGACLVY 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 272 lPR--FDLGEMMAAVEKYRATTLILVPPVLVTMINKADQimKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVDVYQGY 349
Cdd:PRK12583 274 -PNeaFDPLATLQAVEEERCTALYGVPTMFIAELDHPQR--GNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMAEVQIAY 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 350 ALTESN------GAGASIEsveesRRYGAVGLLSCGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEE---EII 420
Cdd:PRK12583 351 GMTETSpvslqtTAADDLE-----RRVETVGRTQPHLEVKVVDPD-GATVPRGEIGELCTRGYSVMKGYWNNPEataESI 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 421 TSEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESN 500
Cdd:PRK12583 425 DEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHA 504
|
490
....*....|....
gi 1063734905 501 LCEKKVIDFISKQV 514
Cdd:PRK12583 505 ASEEELREFCKARI 518
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
63-485 |
7.17e-62 |
|
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: 209.37 E-value: 7.17e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 63 HRISFSDLWMAVDRVADCLLHdVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLAF 142
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIA-LGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 143 ttpelapkiassgisivlerVEDtlrvprglkvvgnltemmkkepsgqavrnqvhKDDTAMLLYSSGTTGRSKGVNSSHG 222
Cdd:cd05907 83 --------------------VED--------------------------------PDDLATIIYTSGTTGRPKGVMLSHR 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 223 NlIAHVARYIAEPFEQ-PQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPRFDLGemMAAVEKYRATTLILVPPVLVT 301
Cdd:cd05907 111 N-ILSNALALAERLPAtEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETL--LDDLSEVRPTVFLAVPRVWEK 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 302 MINKADQI------MKKYDVSFLRTVR---CGGAPLSKEVTQgFMKKYpTVDVYQGYALTESNGAGASieSVEESRRYGA 372
Cdd:cd05907 188 VYAAIKVKavpglkRKLFDLAVGGRLRfaaSGGAPLPAELLH-FFRAL-GIPVYEGYGLTETSAVVTL--NPPGDNRIGT 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 373 VGLLSCGVEARIVDpntgqvmglnqTGELWLKGPSIAKGYFRNEE---EIITSEGWLKTGDLCYIDNDGFLFIVDRLKEL 449
Cdd:cd05907 264 VGKPLPGVEVRIAD-----------DGEILVRGPNVMLGYYKNPEataEALDADGWLHTGDLGEIDEDGFLHITGRKKDL 332
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1063734905 450 IKY-KGYQVPPAELEALLLNHPDILDAAVI----PF------PDKEA 485
Cdd:cd05907 333 IITsGGKNISPEPIENALKASPLISQAVVIgdgrPFlvalivPDPEA 379
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
55-509 |
3.98e-61 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 210.05 E-value: 3.98e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 55 AFIDAATDHRISFSDLWMAVDRVAdCLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASE---ILR 131
Cdd:PRK08315 34 ALVYRDQGLRWTYREFNEEVDALA-KGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSEleyALN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 132 Q-------IADSnpklaF-------TTPELAPKIASSGI----SIVLERVEDTLRV----PRGLKVVGNLTEMMKKEPSG 189
Cdd:PRK08315 113 QsgckaliAADG-----FkdsdyvaMLYELAPELATCEPgqlqSARLPELRRVIFLgdekHPGMLNFDELLALGRAVDDA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 190 Q--AVRNQVHKDDTAMLLYSSGTTGRSKGVNSSHGNlIAHVARYIAEPFEQPQQTFIC-TVPLFHTFGLLNFVLATLALG 266
Cdd:PRK08315 188 ElaARQATLDPDDPINIQYTSGTTGFPKGATLTHRN-ILNNGYFIGEAMKLTEEDRLCiPVPLYHCFGMVLGNLACVTHG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 267 TTVVI-LPRFDLGEMMAAVEKYRATTLILVPpvlvTM-INKADQIM-KKYDVSFLRTVRCGGAPLSKEVtqgfMKKyptV 343
Cdd:PRK08315 267 ATMVYpGEGFDPLATLAAVEEERCTALYGVP----TMfIAELDHPDfARFDLSSLRTGIMAGSPCPIEV----MKR---V 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 344 -------DVYQGYALTESN------GAGASIEsveesRRYGAVGLLSCGVEARIVDPNTGQVMGLNQTGELWLKGPSIAK 410
Cdd:PRK08315 336 idkmhmsEVTIAYGMTETSpvstqtRTDDPLE-----KRVTTVGRALPHLEVKIVDPETGETVPRGEQGELCTRGYSVMK 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 411 GYFRNEE---EIITSEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQ 487
Cdd:PRK08315 411 GYWNDPEktaEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGE 490
|
490 500
....*....|....*....|..
gi 1063734905 488 FPMAYVARKPESNLCEKKVIDF 509
Cdd:PRK08315 491 EVCAWIILRPGATLTEEDVRDF 512
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
46-509 |
1.26e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 207.86 E-value: 1.26e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 46 SSQTYRGKTAFIDAatDHRISFSDLWMAVDRVADCLLhDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNT 125
Cdd:PRK08316 20 SARRYPDKTALVFG--DRSWTYAELDAAVNRVAAALL-DLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 126 ASEILRQIADSNPKLAFTTPELAPKIASSGISIVLERVeDTLRVPRGLKVVGNLTEMMKKEPSGQAVRNQVHKDDT--AM 203
Cdd:PRK08316 97 GEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTL-ILSLVLGGREAPGGWLDFADWAEAGSVAEPDVELADDdlAQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 204 LLYSSGTTGRSKGVNSSHGNLIAHVARYIAEPFEQPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPRFDLGEMMAA 283
Cdd:PRK08316 176 ILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAPDPELILRT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 284 VEKYRATTLILVPPVLVTMINKADqiMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVDVYQGYALTESnGAGASIES 363
Cdd:PRK08316 256 IEAERITSFFAPPTVWISLLRHPD--FDTRDLSSLRKGYYGASIMPVEVLKELRERLPGLRFYNCYGQTEI-APLATVLG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 364 VEESRRYGAvgllSCG-----VEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEEEiiTSE----GWLKTGDLCYI 434
Cdd:PRK08316 333 PEEHLRRPG----SAGrpvlnVETRVVDDD-GNDVAPGEVGEIVHRSPQLMLGYWDDPEK--TAEafrgGWFHSGDLGVM 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063734905 435 DNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKVIDF 509
Cdd:PRK08316 406 DEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAH 480
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
64-513 |
1.46e-60 |
|
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: 205.31 E-value: 1.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 64 RISFSDLWMAVDRVADCLLhDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVlttANPL------NTASEILRqiaDSN 137
Cdd:cd05903 1 RLTYSELDTRADRLAAGLA-ALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAV---TNPIlpffreHELAFILR---RAK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 138 PKLAFTTPELapkiassgisivleRVEDTLRVPrglkvvgnltemmkkepsgqavrnqvhkDDTAMLLYSSGTTGRSKGV 217
Cdd:cd05903 74 AKVFVVPERF--------------RQFDPAAMP----------------------------DAVALLLFTSGTTGEPKGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 218 NSSHGNLIAHVARYIAEPFEQPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPRFDLGEMMAAVEKYRATTLILVPP 297
Cdd:cd05903 112 MHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 298 VLVTMINKADQIMKkyDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVdVYQGYALTESNGAGASIESVEESRRYGAVGLLS 377
Cdd:cd05903 192 FLTDLLNAVEEAGE--PLSRLRTFVCGGATVPRSLARRAAELLGAK-VCSAYGSTECPGAVTSITPAPEDRRLYTDGRPL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 378 CGVEARIVDpNTGQVMGLNQTGELWLKGPSIAKGYFRNEEEIIT--SEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGY 455
Cdd:cd05903 269 PGVEIKVVD-DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADaaPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGE 347
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063734905 456 QVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKVIDFISKQ 513
Cdd:cd05903 348 NIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQ 405
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
41-508 |
4.18e-60 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 205.86 E-value: 4.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 41 ITTFISSQTYRGKTAFIDAATDHRISFSDLWMAVDRVADCLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTA 120
Cdd:PRK06839 4 IAYWIEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 121 NPLNTASEILRQIADSNPKLAFTTPELAPKIASSGISIVLERVedtLRVPrglkvvgNLTEMMKKEPSGQAVRNQvhkDD 200
Cdd:PRK06839 84 NIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRV---ISIT-------SLKEIEDRKIDNFVEKNE---SA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 201 TAMLLYSSGTTGRSKGVNSSHGNLIAHVARYIAEPFEQPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPRFDLGEM 280
Cdd:PRK06839 151 SFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 281 MAAVEKYRATTLILVPPVLVTMINKADqiMKKYDVSFLRTVRCGGAPLSKEVTQGFMKK-YPtvdVYQGYALTESNGAGA 359
Cdd:PRK06839 231 LSMIEKHKVTVVMGVPTIHQALINCSK--FETTNLQSVRWFYNGGAPCPEELMREFIDRgFL---FGQGFGMTETSPTVF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 360 SIESVEESRRYGAVGLLSCGVEARIVDPNTGQVmGLNQTGELWLKGPSIAKGYFRNEEEIITS--EGWLKTGDLCYIDND 437
Cdd:PRK06839 306 MLSEEDARRKVGSIGKPVLFCDYELIDENKNKV-EVGEVGELLIRGPNVMKEYWNRPDATEETiqDGWLCTGDLARVDED 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063734905 438 GFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKVID 508
Cdd:PRK06839 385 GFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIE 455
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
81-509 |
1.27e-59 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 206.06 E-value: 1.27e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 81 LLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPK-------LAFTTPELAPKIAS 153
Cdd:PRK08974 65 LQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKaivivsnFAHTLEKVVFKTPV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 154 SgiSIVLERVEDTLRVPRG------LKVVGNLT------------EMMKKEPSGQAVRNQVHKDDTAMLLYSSGTTGRSK 215
Cdd:PRK08974 145 K--HVILTRMGDQLSTAKGtlvnfvVKYIKRLVpkyhlpdaisfrSALHKGRRMQYVKPELVPEDLAFLQYTGGTTGVAK 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 216 GVNSSHGNLIAHV--ARYIAEPFEQPQQTFICT-VPLFHTFGLLNFVLATLALGTTVVIL--PRfDLGEMMAAVEKYRAT 290
Cdd:PRK08974 223 GAMLTHRNMLANLeqAKAAYGPLLHPGKELVVTaLPLYHIFALTVNCLLFIELGGQNLLItnPR-DIPGFVKELKKYPFT 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 291 TLILVPPVLVTMINKADqiMKKYDVSFLRTVRCGGAPLSKEVTQGFmKKYPTVDVYQGYALTESNG--AGASIESVEESr 368
Cdd:PRK08974 302 AITGVNTLFNALLNNEE--FQELDFSSLKLSVGGGMAVQQAVAERW-VKLTGQYLLEGYGLTECSPlvSVNPYDLDYYS- 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 369 ryGAVGLLSCGVEARIVDpNTGQVMGLNQTGELWLKGPSIAKGYFRNEEEI--ITSEGWLKTGDLCYIDNDGFLFIVDRL 446
Cdd:PRK08974 378 --GSIGLPVPSTEIKLVD-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATdeVIKDGWLATGDIAVMDEEGFLRIVDRK 454
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063734905 447 KELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESnLCEKKVIDF 509
Cdd:PRK08974 455 KDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPS-LTEEELITH 516
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
46-514 |
7.25e-57 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 198.83 E-value: 7.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 46 SSQTYRGKTAFidAATDHRISFSDLWMAVDRVADCLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNT 125
Cdd:PRK05677 33 SCQRFADKPAF--SNLGKTLTYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 126 ASEILRQIADSNPK-------LAFTTPELAPKiasSGIS--IVLErVEDTLRVPRGLKVVGNLTEMMKKEPS-------- 188
Cdd:PRK05677 111 AREMEHQFNDSGAKalvclanMAHLAEKVLPK---TGVKhvIVTE-VADMLPPLKRLLINAVVKHVKKMVPAyhlpqavk 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 189 ---------GQAVRN-QVHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVAR---YIAEPFEQPQQTFICTVPLFHTFGL 255
Cdd:PRK05677 187 fndalakgaGQPVTEaNPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQcraLMGSNLNEGCEILIAPLPLYHIYAF 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 256 LNFVLATLALGTTVVIL--PRfDLGEMMAAVEKYRATTLILVPPVLVTMINKADqiMKKYDVSFLRTVRCGGAPLSKEVT 333
Cdd:PRK05677 267 TFHCMAMMLIGNHNILIsnPR-DLPAMVKELGKWKFSGFVGLNTLFVALCNNEA--FRKLDFSALKLTLSGGMALQLATA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 334 QGFmKKYPTVDVYQGYALTESngagASIESVE--ESRRYGAVGLLSCGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKG 411
Cdd:PRK05677 344 ERW-KEVTGCAICEGYGMTET----SPVVSVNpsQAIQVGTIGIPVPSTLCKVIDDD-GNELPLGEVGELCVKGPQVMKG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 412 YFRNEE---EIITSEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQF 488
Cdd:PRK05677 418 YWQRPEatdEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEA 497
|
490 500
....*....|....*....|....*.
gi 1063734905 489 PMAYVARKPESNLCEKKVIDFISKQV 514
Cdd:PRK05677 498 IKVFVVVKPGETLTKEQVMEHMRANL 523
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
48-510 |
9.28e-57 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 198.23 E-value: 9.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 48 QTYRGKTAFIDaatDH-RISFSDLWMAVDRVADCLLHDvGIRRGDVVLVLSPNTISIPIVCLSVMSLGA--VLttanpLN 124
Cdd:PRK07788 60 RRAPDRAALID---ERgTLTYAELDEQSNALARGLLAL-GVRAGDGVAVLARNHRGFVLALYAAGKVGAriIL-----LN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 125 TAseilrqiadsnpklaFTTPELAPKIASSGISIVL------ERVEDTL-RVPRGLKVVGNLTEMMKKEPSGQAVRNQVH 197
Cdd:PRK07788 131 TG---------------FSGPQLAEVAAREGVKALVyddeftDLLSALPpDLGRLRAWGGNPDDDEPSGSTDETLDDLIA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 198 KDDTAML----------LYSSGTTGRSKGVNSSHGNLIAHVARYIAE-PFEQpQQTFICTVPLFHTFGLLNFVLAtLALG 266
Cdd:PRK07788 196 GSSTAPLpkppkpggivILTSGTTGTPKGAPRPEPSPLAPLAGLLSRvPFRA-GETTLLPAPMFHATGWAHLTLA-MALG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 267 TTVVILPRFDLGEMMAAVEKYRATTLILVPPVLVTMINKADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVdVY 346
Cdd:PRK07788 274 STVVLRRRFDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPV-LY 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 347 QGYALTESngAGASIESVEESRRY-GAVGLLSCGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYF--RNEEEIitsE 423
Cdd:PRK07788 353 NLYGSTEV--AFATIATPEDLAEApGTVGRPPKGVTVKILDEN-GNEVPRGVVGRIFVGNGFPFEGYTdgRDKQII---D 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 424 GWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCE 503
Cdd:PRK07788 427 GLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDE 506
|
....*..
gi 1063734905 504 KKVIDFI 510
Cdd:PRK07788 507 DAIKDYV 513
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
62-501 |
3.00e-55 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 192.99 E-value: 3.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 62 DHRISFSDLWMAVDRVADCLlHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLA 141
Cdd:PRK12406 9 DRRRSFDELAQRAARAAGGL-AALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 142 FTTPELAPKIAS---SGISIVL----------ERVEDTLRVPRGLKVvgNLTEMMKKEPSGQAVRnqvhKDDTAMLLYSS 208
Cdd:PRK12406 88 IAHADLLHGLASalpAGVTVLSvptppeiaaaYRISPALLTPPAGAI--DWEGWLAQQEPYDGPP----VPQPQSMIYTS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 209 GTTGRSKGVNSSHGN--LIAHVARYIAEPFEQPQQT-FICTVPLFHT----FGLlnfvlATLALGTTVVILPRFDLGEMM 281
Cdd:PRK12406 162 GTTGHPKGVRRAAPTpeQAAAAEQMRALIYGLKPGIrALLTGPLYHSapnaYGL-----RAGRLGGVLVLQPRFDPEELL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 282 AAVEKYRATTLILVPPVLVTMINKADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVdVYQGYALTESnGAGASI 361
Cdd:PRK12406 237 QLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGPV-IYEYYGSTES-GAVTFA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 362 ESVEESRRYGAVGLLSCGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEEE---IITSEGWLKTGDLCYIDNDG 438
Cdd:PRK12406 315 TSEDALSHPGTVGKAAPGAELRFVDED-GRPLPQGEIGEIYSRIAGNPDFTYHNKPEkraEIDRGGFITSGDVGYLDADG 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063734905 439 FLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNL 501
Cdd:PRK12406 394 YLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATL 456
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
56-508 |
3.65e-55 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 192.78 E-value: 3.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 56 FIDAATDHRISFSDLWMAVDRVADcLLHDVGIRRGDVVLVL---SPNTIsipIVCLSVMSLGAVLTtanPLNTA---SEI 129
Cdd:PRK07514 20 FIETPDGLRYTYGDLDAASARLAN-LLVALGVKPGDRVAVQvekSPEAL---ALYLATLRAGAVFL---PLNTAytlAEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 130 LRQIADSNPKLAFTTPE----LAPKIASSGISIVLervedTLRVPRGlkvvGNLTEMMKKEPSG--QAVRNqvhKDDTAM 203
Cdd:PRK07514 93 DYFIGDAEPALVVCDPAnfawLSKIAAAAGAPHVE-----TLDADGT----GSLLEAAAAAPDDfeTVPRG---ADDLAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 204 LLYSSGTTGRSKGVNSSHGNLIAHvARYIAEPFE-QPQQTFICTVPLFHTFGLlnFVLA--TLALGTTVVILPRFDLGEM 280
Cdd:PRK07514 161 ILYTSGTTGRSKGAMLSHGNLLSN-ALTLVDYWRfTPDDVLIHALPIFHTHGL--FVATnvALLAGASMIFLPKFDPDAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 281 MAAVEkyRATTLILVPPVLVTMInkADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKyptvdvyQG------YALTES 354
Cdd:PRK07514 238 LALMP--RATVMMGVPTFYTRLL--QEPRLTREAAAHMRLFISGSAPLLAETHREFQER-------TGhailerYGMTET 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 355 NgagaSIES--VEESRRYGAVGLLSCGVEARIVDPNTGQVMGLNQTGELWLKGPSIAKGYFRNEE---EIITSEGWLKTG 429
Cdd:PRK07514 307 N----MNTSnpYDGERRAGTVGFPLPGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEktaEEFRADGFFITG 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063734905 430 DLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKVID 508
Cdd:PRK07514 383 DLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAILA 461
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
24-505 |
8.89e-55 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 193.11 E-value: 8.89e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 24 FYSKRKPLALPSkeSLDITTFISSQTY--RGKTAFIDaatdhRISFSDL-----WMAVDR----VADCLLHDVGIRRGDV 92
Cdd:PRK12492 5 FWNDKRPAGVPS--TIDLAAYKSVVEVfeRSCKKFAD-----RPAFSNLgvtlsYAELERhsaaFAAYLQQHTDLVPGDR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 93 VLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPK----LAFTTPELAPKIASSGISIVLE-RVEDTL 167
Cdd:PRK12492 78 IAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARalvyLNMFGKLVQEVLPDTGIEYLIEaKMGDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 168 RVPRGL---KVVGNLTEMMKKEPSGQAV---------RNQVHK------DDTAMLLYSSGTTGRSKGVNSSHGNLIAHVA 229
Cdd:PRK12492 158 PAAKGWlvnTVVDKVKKMVPAYHLPQAVpfkqalrqgRGLSLKpvpvglDDIAVLQYTGGTTGLAKGAMLTHGNLVANML 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 230 RYIA---------EP-FEQPQQTFICTVPLFHTFGLLNFVLATLALGTTVVIL--PRfDLGEMMAAVEKYRATTLILVPP 297
Cdd:PRK12492 238 QVRAclsqlgpdgQPlMKEGQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLItnPR-DIPGFIKELGKWRFSALLGLNT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 298 VLVTMINKADqiMKKYDVSFLRTVRCGGAPLSKEVTQGFmKKYPTVDVYQGYALTESNGAgASIESVEESRRYGAVGLLS 377
Cdd:PRK12492 317 LFVALMDHPG--FKDLDFSALKLTNSGGTALVKATAERW-EQLTGCTIVEGYGLTETSPV-ASTNPYGELARLGTVGIPV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 378 CGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEE---EIITSEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKG 454
Cdd:PRK12492 393 PGTALKVIDDD-GNELPLGERGELCIKGPQVMKGYWQQPEataEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSG 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1063734905 455 YQVPPAELEALLLNHPDILDAAVIPFPDKEAGQ-FPMAYVARKPESNLCEKK 505
Cdd:PRK12492 472 FNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEaVKLFVVARDPGLSVEELK 523
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
50-510 |
2.53e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 190.97 E-value: 2.53e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 50 YRGKTAFIDaaTDHRISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEI 129
Cdd:PRK06188 25 YPDRPALVL--GDTRLTYGQLADRISRYIQ-AFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 130 LRQIADSNPKLAFTTP--------ELAPKIASsgisivLERVEDTLRVPRGLkvvgNLTEMMKKEPSGQAVRNQVHkDDT 201
Cdd:PRK06188 102 AYVLEDAGISTLIVDPapfveralALLARVPS------LKHVLTLGPVPDGV----DLLAAAAKFGPAPLVAAALP-PDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 202 AMLLYSSGTTGRSKGVNSSHGNlIAHVARYIAEPFEQPQQT-FICTVPLFHTFGLlnFVLATLALGTTVVILPRFDLGEM 280
Cdd:PRK06188 171 AGLAYTGGTTGKPKGVMGTHRS-IATMAQIQLAEWEWPADPrFLMCTPLSHAGGA--FFLPTLLRGGTVIVLAKFDPAEV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 281 MAAVEKYRATTLILVPPVLVTMINKADqiMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVdVYQGYALTESNGAgAS 360
Cdd:PRK06188 248 LRAIEEQRITATFLVPTMIYALLDHPD--LRTRDLSSLETVYYGASPMSPVRLAEAIERFGPI-FAQYYGQTEAPMV-IT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 361 IESVEESRRYGAVGLLSCG-----VEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEEEiiTSE----GWLKTGDL 431
Cdd:PRK06188 324 YLRKRDHDPDDPKRLTSCGrptpgLRVALLDED-GREVAQGEVGEICVRGPLVMDGYWNRPEE--TAEafrdGWLHTGDV 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063734905 432 CYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKVIDFI 510
Cdd:PRK06188 401 AREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHV 479
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
48-487 |
1.30e-53 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 188.75 E-value: 1.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 48 QTYRGKTAFIDAATDHRISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTAS 127
Cdd:PRK13391 8 QTTPDKPAVIMASTGEVVTYRELDERSNRLAH-LFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 128 EILRQIADSNPKLAFTT-------PELAPKIASSGISIVLERVEDtlrVPRglkvVGNLTEMMKKEPSGQaVRNQVHKDD 200
Cdd:PRK13391 87 EAAYIVDDSGARALITSaakldvaRALLKQCPGVRHRLVLDGDGE---LEG----FVGYAEAVAGLPATP-IADESLGTD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 201 tamLLYSSGTTGRSKGVNS--SHGNLIAHVAryIAEPFEQ-----PQQTFICTVPLFHTfGLLNFVLATLALGTTVVILP 273
Cdd:PRK13391 159 ---MLYSSGTTGRPKGIKRplPEQPPDTPLP--LTAFLQRlwgfrSDMVYLSPAPLYHS-APQRAVMLVIRLGGTVIVME 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 274 RFDLGEMMAAVEKYRATTLILVPPVLVTMINKADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKY-PTVDVYqgYALT 352
Cdd:PRK13391 233 HFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWgPIIHEY--YAAT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 353 ESNGAGAsIESVEESRRYGAVGLLSCGVeARIVDPNtGQVMGLNQTGELWLKGPSIAKgYFRNEEEiiTSE------GWL 426
Cdd:PRK13391 311 EGLGFTA-CDSEEWLAHPGTVGRAMFGD-LHILDDD-GAELPPGEPGTIWFEGGRPFE-YLNDPAK--TAEarhpdgTWS 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063734905 427 KTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQ 487
Cdd:PRK13391 385 TVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGE 445
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
46-493 |
4.28e-52 |
|
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: 184.96 E-value: 4.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 46 SSQTYRGKTAFIDAatDHRISFSDLWMAVDRVAdCLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNT 125
Cdd:COG1021 34 RAERHPDRIAVVDG--ERRLSYAELDRRADRLA-AGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVFALPAHR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 126 ASEILRQIADSNPKlAFTTPELAPKIASSGIsivLERVEDTLRVPRGLKVVG------NLTEMMKKEPSGQAVRnqVHKD 199
Cdd:COG1021 111 RAEISHFAEQSEAV-AYIIPDRHRGFDYRAL---ARELQAEVPSLRHVLVVGdageftSLDALLAAPADLSEPR--PDPD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 200 DTAMLLYSSGTTGRSKGVNSSHgNLIAHVARYIAEPFE-QPQQTFICTVPLFHTFGLLNF-VLATLALGTTVVILPRFDL 277
Cdd:COG1021 185 DVAFFQLSGGTTGLPKLIPRTH-DDYLYSVRASAEICGlDADTVYLAALPAAHNFPLSSPgVLGVLYAGGTVVLAPDPSP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 278 GEMMAAVEKYRATTLILVPPVLVTMINKADQimKKYDVSFLRTVRCGGAPLS----KEVTQGFmkkyptvdvyqgyalte 353
Cdd:COG1021 264 DTAFPLIERERVTVTALVPPLALLWLDAAER--SRYDLSSLRVLQVGGAKLSpelaRRVRPAL----------------- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 354 sngaGASIESV---------------EESRRYGAVGL-LSCGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEE 417
Cdd:COG1021 325 ----GCTLQQVfgmaeglvnytrlddPEEVILTTQGRpISPDDEVRIVDED-GNPVPPGEVGELLTRGPYTIRGYYRAPE 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063734905 418 ---EIITSEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYV 493
Cdd:COG1021 400 hnaRAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFV 478
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
63-500 |
5.97e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 182.28 E-value: 5.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 63 HRISFSDLWMAVDRVADCLlHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVlttANPLN---TASEILRQIADSNPK 139
Cdd:PRK07786 41 NTTTWRELDDRVAALAGAL-SRRGVGFGDRVLILMLNRTEFVESVLAANMLGAI---AVPVNfrlTPPEIAFLVSDCGAH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 140 LAFTTPELAPKIA-----SSGISIVL---ERVEDTlrvprglkVVGNLTEMMKKEPSGQAVrnQVHKDDTAMLLYSSGTT 211
Cdd:PRK07786 117 VVVTEAALAPVATavrdiVPLLSTVVvagGSSDDS--------VLGYEDLLAEAGPAHAPV--DIPNDSPALIMYTSGTT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 212 GRSKGVNSSHGNLIAHVARYI-AEPFEQPQQTFICTVPLFHTFGLLNfVLATLALGTTVVILP--RFDLGEMMAAVEKYR 288
Cdd:PRK07786 187 GRPKGAVLTHANLTGQAMTCLrTNGADINSDVGFVGVPLFHIAGIGS-MLPGLLLGAPTVIYPlgAFDPGQLLDVLEAEK 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 289 ATTLILVPPVLVTMInkADQIMKKYDVSfLRTVRCGGAPLSKEVTQGFMKKYPTVDVYQGYALTESNGAGASIESVEESR 368
Cdd:PRK07786 266 VTGIFLVPAQWQAVC--AEQQARPRDLA-LRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSPVTCMLLGEDAIR 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 369 RYGAVGLLSCGVEARIVDPNTGQVmGLNQTGELWLKGPSIAKGYFRNEEEiiTSE----GWLKTGDLCYIDNDGFLFIVD 444
Cdd:PRK07786 343 KLGSVGKVIPTVAARVVDENMNDV-PVGEVGEIVYRAPTLMSGYWNNPEA--TAEafagGWFHSGDLVRQDEEGYVWVVD 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063734905 445 RLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESN 500
Cdd:PRK07786 420 RKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDA 475
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
82-509 |
6.95e-51 |
|
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: 180.96 E-value: 6.95e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 82 LHDVGIRRGDVVLVLSPNTisiPIVCLS---VMSLGAVLttaNPLNT---ASEILRQIADSNPKLAFTTPELA--PKIAS 153
Cdd:cd12118 46 LAALGISRGDTVAVLAPNT---PAMYELhfgVPMAGAVL---NALNTrldAEEIAFILRHSEAKVLFVDREFEyeDLLAE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 154 SGISIVLERVEDtlrvprglkvvgnltemmkkepsgqavrnqvhKDDTAMLLYSSGTTGRSKGVNSSH-GNLIAHVARYI 232
Cdd:cd12118 120 GDPDFEWIPPAD--------------------------------EWDPIALNYTSGTTGRPKGVVYHHrGAYLNALANIL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 233 AepFEQPQQT-FICTVPLFHTFGLlNFVLATLALGTTVVILPRFDLGEMMAAVEKYRATTLILVPPVLVTMINKADQIMK 311
Cdd:cd12118 168 E--WEMKQHPvYLWTLPMFHCNGW-CFPWTVAAVGGTNVCLRKVDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDAR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 312 KYDvsflRTVR--CGGAP-----LSKEVTQGFmkkyptvDVYQGYALTESNGAGASIESVEE------SRRYG-----AV 373
Cdd:cd12118 245 PLP----HRVHvmTAGAPppaavLAKMEELGF-------DVTHVYGLTETYGPATVCAWKPEwdelptEERARlkarqGV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 374 GLLSCGvEARIVDPNTGQ-VMGLNQT-GELWLKGPSIAKGYFRNEEEiiTSE----GWLKTGDLCYIDNDGFLFIVDRLK 447
Cdd:cd12118 314 RYVGLE-EVDVLDPETMKpVPRDGKTiGEIVFRGNIVMKGYLKNPEA--TAEafrgGWFHSGDLAVIHPDGYIEIKDRSK 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063734905 448 ELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKVIDF 509
Cdd:cd12118 391 DIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEEEIIAF 452
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
66-497 |
4.04e-50 |
|
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: 177.53 E-value: 4.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 66 SFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLAFTTp 145
Cdd:cd05972 2 SFRELKRESAKAAN-VLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 146 elapkiassgisivlervedtlrvprglkvvgnltemmkkepsgqavrnqvhKDDTAMLLYSSGTTGRSKGVNSSHGNLI 225
Cdd:cd05972 80 ----------------------------------------------------AEDPALIYFTSGTTGLPKGVLHTHSYPL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 226 AHVArYIAEPFE-QPQQTFICTVPLFHTFGLLNFVLATLALGTTVVI--LPRFDLGEMMAAVEKYRATTLILvPPVLVTM 302
Cdd:cd05972 108 GHIP-TAAYWLGlRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVyeGPRFDAERILELLERYGVTSFCG-PPTAYRM 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 303 INKADqiMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYpTVDVYQGYALTESNGAGASIESVEesRRYGAVGLLSCGVEA 382
Cdd:cd05972 186 LIKQD--LSSYKFSHLRLVVSAGEPLNPEVIEWWRAAT-GLPIRDGYGQTETGLTVGNFPDMP--VKPGSMGRPTPGYDV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 383 RIVDPNtGQVMGLNQTGELWLK--GPSIAKGYFRNEEEIITS--EGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVP 458
Cdd:cd05972 261 AIIDDD-GRELPPGEEGDIAIKlpPPGLFLGYVGDPEKTEASirGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIG 339
|
410 420 430
....*....|....*....|....*....|....*....
gi 1063734905 459 PAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKP 497
Cdd:cd05972 340 PFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTS 378
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
199-514 |
5.07e-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: 175.36 E-value: 5.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 199 DDTAMLLYSSGTTGRSKGVNSSHGNLIAHVARYIAEPFEQPQQTFICTVPLFHTFGLLNFVLATLALGTTVVIL------ 272
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAgpagyr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 273 -PRFdLGEMMAAVEKYRATTLILVPPVLVTMInkadQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKyPTVDVYQGYAL 351
Cdd:cd05944 82 nPGL-FDNFWKLVERYRITSLSTVPTVYAALL----QVPVNADISSLRFAMSGAAPLPVELRARFEDA-TGLPVVEGYGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 352 TESNgAGASIESVEESRRYGAVGLL--SCGVEARIVDPNTGQVM--GLNQTGELWLKGPSIAKGYFRNE--EEIITSEGW 425
Cdd:cd05944 156 TEAT-CLVAVNPPDGPKRPGSVGLRlpYARVRIKVLDGVGRLLRdcAPDEVGEICVAGPGVFGGYLYTEgnKNAFVADGW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 426 LKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKK 505
Cdd:cd05944 235 LNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEE 314
|
....*....
gi 1063734905 506 VIDFISKQV 514
Cdd:cd05944 315 LLAWARDHV 323
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
46-513 |
1.12e-49 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 179.06 E-value: 1.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 46 SSQTYRGKTAFIdaATDHRISFSDLwmavDRVADCL---LHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANP 122
Cdd:PRK07059 32 SFRQYADRPAFI--CMGKAITYGEL----DELSRALaawLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 123 LNTASEILRQIADSNPKLAFTTPELAPK----IASSGIS-IVLERVEDTLrvprGLK------VVGNLTEMMK------- 184
Cdd:PRK07059 106 LYTPRELEHQLKDSGAEAIVVLENFATTvqqvLAKTAVKhVVVASMGDLL----GFKghivnfVVRRVKKMVPawslpgh 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 185 -------KEPSGQAVRN-QVHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVAR---YIAEPFEQP----QQTFICTVPL 249
Cdd:PRK07059 182 vrfndalAEGARQTFKPvKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQmeaWLQPAFEKKprpdQLNFVCALPL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 250 FHTFGL-LNFVLATLALGTTVVIL-PRfDLGEMMAAVEKYRATTLILVPPVLVTMINKADqiMKKYDVSFLRTVRCGGAP 327
Cdd:PRK07059 262 YHIFALtVCGLLGMRTGGRNILIPnPR-DIPGFIKELKKYQVHIFPAVNTLYNALLNNPD--FDKLDFSKLIVANGGGMA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 328 LSKEVTQGFMKKYPTvDVYQGYALTESNGAgASIESVEESRRYGAVGLLSCGVEARIVDpNTGQVMGLNQTGELWLKGPS 407
Cdd:PRK07059 339 VQRPVAERWLEMTGC-PITEGYGLSETSPV-ATCNPVDATEFSGTIGLPLPSTEVSIRD-DDGNDLPLGEPGEICIRGPQ 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 408 IAKGYFRNEEE---IITSEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKE 484
Cdd:PRK07059 416 VMAGYWNRPDEtakVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEH 495
|
490 500
....*....|....*....|....*....
gi 1063734905 485 AGQFPMAYVARKpESNLCEKKVIDFISKQ 513
Cdd:PRK07059 496 SGEAVKLFVVKK-DPALTEEDVKAFCKER 523
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
62-501 |
1.13e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 177.77 E-value: 1.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 62 DHRISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLA 141
Cdd:PRK06145 25 DQEISYAEFHQRILQAAG-MLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 142 FTTPELAPKIASSGISIVLERV--EDTLRVPRGLKVVgnlTEMMKKEPsgqavrnqvhkDDTAMLLYSSGTTGRSKGVNS 219
Cdd:PRK06145 104 LVDEEFDAIVALETPKIVIDAAaqADSRRLAQGGLEI---PPQAAVAP-----------TDLVRLMYTSGTTDRPKGVMH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 220 SHGNLIAHVARYIAEPFEQPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPRFDLGEMMAAVEKYRATTLILVPPVL 299
Cdd:PRK06145 170 SYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLAAIERHRLTCAWMAPVML 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 300 VTMINKADQimKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVDVYQGYALTESNGAGASIESVEESRRYGAVGLLSCG 379
Cdd:PRK06145 250 SRVLTVPDR--DRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREIEKIGSTGRALAH 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 380 VEARIVDpNTGQVMGLNQTGELWLKGPSIAKGYFRNEEEIITS--EGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQV 457
Cdd:PRK06145 328 VEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAfyGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENI 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1063734905 458 PPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNL 501
Cdd:PRK06145 407 ASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATL 450
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
200-509 |
1.53e-49 |
|
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: 173.07 E-value: 1.53e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 200 DTAMLLYSSGTTGRSKGVNSSHGNLIAHVARYIAEPFEQPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPRFDLGE 279
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 280 MMAAVEKYRATTLILVPPVLVTMINKADQimKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVDVYQGYALTESNGA-- 357
Cdd:cd17638 81 ILEAIERERITVLPGPPTLFQSLLDHPGR--KKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGVAtm 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 358 ---GASIESVEESrrygaVGLLSCGVEARIVDPntgqvmglnqtGELWLKGPSIAKGYFRNEE---EIITSEGWLKTGDL 431
Cdd:cd17638 159 crpGDDAETVATT-----CGRACPGFEVRIADD-----------GEVLVRGYNVMQGYLDDPEataEAIDADGWLHTGDV 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063734905 432 CYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKVIDF 509
Cdd:cd17638 223 GELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAW 300
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
204-499 |
2.04e-49 |
|
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: 176.41 E-value: 2.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 204 LLYSSGTTGRSKGVNSSHGNLIAHVARYIAEPFEQP---QQTFICTVPLFHTFGLlNFVLATLALGTTVVILPRFDLGEM 280
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAALGFGpgaDSVYLSPAPLYHAAPF-RWSMTALFMGGTLVLMEKFDPEEF 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 281 MAAVEKYRATTLILVPPVLVTMINKADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVdVYQGYALTESNGAGAs 360
Cdd:cd05929 209 LRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPI-IWEYYGGTEGQGLTI- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 361 IESVEESRRYGAVGLLSCGvEARIVDPNtGQVMGLNQTGELWLKGPSiAKGYFRN---EEEIITSEGWLKTGDLCYIDND 437
Cdd:cd05929 287 INGEEWLTHPGSVGRAVLG-KVHILDED-GNEVPPGEIGEVYFANGP-GFEYTNDpekTAAARNEGGWSTLGDVGYLDED 363
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063734905 438 GFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPES 499
Cdd:cd05929 364 GYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGA 425
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
52-501 |
1.39e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 174.61 E-value: 1.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 52 GKTAFIDAATDHRISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTtanPLN---TASE 128
Cdd:PRK09088 10 QRLAAVDLALGRRWTYAELDALVGRLAA-VLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYV---PLNwrlSASE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 129 ILRQIADSNPKLAFTTPELApkiASSGISIVLERVEDTLrvprglkvvgnltemmkkEPSGQAVRNQVHKDDTAMLLYSS 208
Cdd:PRK09088 86 LDALLQDAEPRLLLGDDAVA---AGRTDVEDLAAFIASA------------------DALEPADTPSIPPERVSLILFTS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 209 GTTGRSKGVNSSHGNLIAHVARYIAEPFEQPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPRFD-------LGEMM 281
Cdd:PRK09088 145 GTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEpkrtlgrLGDPA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 282 AAVEKYrattlILVPPVLVTMINKADqimkkYDVSFLR---TVRCGGAPLSKEVTQGFMKK-YPTVDvyqGYALTESNGA 357
Cdd:PRK09088 225 LGITHY-----FCVPQMAQAFRAQPG-----FDAAALRhltALFTGGAPHAAEDILGWLDDgIPMVD---GFGMSEAGTV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 358 -GASIESVEESRRYGAVGLLSCGVEARIVDpNTGQVMGLNQTGELWLKGPSIAKGYFRNEEE---IITSEGWLKTGDLCY 433
Cdd:PRK09088 292 fGMSVDCDVIRAKAGAAGIPTPTVQTRVVD-DQGNDCPAGVPGELLLRGPNLSPGYWRRPQAtarAFTGDGWFRTGDIAR 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063734905 434 IDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNL 501
Cdd:PRK09088 371 RDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPL 438
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
71-514 |
2.98e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 174.46 E-value: 2.98e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 71 WMAVDRVADCL---LHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKL-----AF 142
Cdd:PRK07470 35 WREIDARVDALaaaLAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAmichaDF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 143 ttPELAPKIASSGISIvlervedTLRVPRGLKVVGNLTEMMKKEPSGQAVRN-QVHKDDTAMLLYSSGTTGRSKGVNSSH 221
Cdd:PRK07470 115 --PEHAAAVRAASPDL-------THVVAIGGARAGLDYEALVARHLGARVANaAVDHDDPCWFFFTSGTTGRPKAAVLTH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 222 GNLIAHVARYIAE--PFEQPQQTFICTVPLFHTFGLlnFVLATLALGTTVVILP--RFDLGEMMAAVEKYRATTLILVPP 297
Cdd:PRK07470 186 GQMAFVITNHLADlmPGTTEQDASLVVAPLSHGAGI--HQLCQVARGAATVLLPseRFDPAEVWALVERHRVTNLFTVPT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 298 VLVTMINkaDQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVDVyQGYALTESNGA----GASIESVEE--SRRYG 371
Cdd:PRK07470 264 ILKMLVE--HPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKVLV-QYFGLGEVTGNitvlPPALHDAEDgpDARIG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 372 AVGLLSCGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEEEIITS--EGWLKTGDLCYIDNDGFLFIVDRLKEL 449
Cdd:PRK07470 341 TCGFERTGMEVQIQDDE-GRELPPGETGEICVIGPAVFAGYYNNPEANAKAfrDGWFRTGDLGHLDARGFLYITGRASDM 419
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063734905 450 IKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKVIDFISKQV 514
Cdd:PRK07470 420 YISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAELLAWLDGKV 484
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
90-487 |
7.41e-48 |
|
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: 172.90 E-value: 7.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 90 GDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLAFTTPELAPKI-------ASSGISIV-LE 161
Cdd:cd05909 31 GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQFIEKLklhhlfdVEYDARIVyLE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 162 RVEDTLRVPRGLKVVGNLTeMMKKEPSGQAVRNQVHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHV--ARYIAEPfeQP 239
Cdd:cd05909 111 DLRAKISKADKCKAFLAGK-FPPKWLLRIFGVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVeqITAIFDP--NP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 240 QQTFICTVPLFHTFGLLNFVLATLALGTTVVILPR-FDLGEMMAAVEKYRATTLILVPPVLVTMINKAdqimKKYDVSFL 318
Cdd:cd05909 188 EDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNpLDYKKIPELIYDKKATILLGTPTFLRGYARAA----HPEDFSSL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 319 RTVRCGGAPLSKEVTQGFMKKYpTVDVYQGYALTESNgAGASIESVEESRRYGAVGLLSCGVEARIVDPNTGQVMGLNQT 398
Cdd:cd05909 264 RLVVAGAEKLKDTLRQEFQEKF-GIRILEGYGTTECS-PVISVNTPQSPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEG 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 399 GELWLKGPSIAKGYFRNEE--EIITSEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNH-PDILDA 475
Cdd:cd05909 342 GLLLVRGPNVMLGYLNEPEltSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEV 421
|
410
....*....|..
gi 1063734905 476 AVIPFPDKEAGQ 487
Cdd:cd05909 422 AVVSVPDGRKGE 433
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
73-477 |
8.40e-48 |
|
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: 170.52 E-value: 8.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 73 AVDRVADCLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTtanPLNTA--SEILRQI-ADSNPKLAFTTPELAP 149
Cdd:TIGR01733 8 RANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYV---PLDPAypAERLAFIlEDAGARLLLTDSALAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 150 KIASSGISIVLERVEDTLRVPRglkvvgnltemmkkEPSGQAVRNQVHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVA 229
Cdd:TIGR01733 85 RLAGLVLPVILLDPLELAALDD--------------APAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 230 RYIAEPFEQPQQTfictVPLFHTFGllnF------VLATLALGTTVVILP----RFDLGEMMAAVEKYRATTLILVPPVL 299
Cdd:TIGR01733 151 WLARRYGLDPDDR----VLQFASLS---FdasveeIFGALLAGATLVVPPedeeRDDAALLAALIAEHPVTVLNLTPSLL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 300 vTMINKADqimkKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVDVYQGYALTE-SNGAGASIESVEESRRYGAVGL--- 375
Cdd:TIGR01733 224 -ALLAAAL----PPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTEtTVWSTATLVDPDDAPRESPVPIgrp 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 376 LScGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEEEiiTSE-------------GWLKTGDLCYIDNDGFLFI 442
Cdd:TIGR01733 299 LA-NTRLYVLDDD-LRPVPVGVVGELYIGGPGVARGYLNRPEL--TAErfvpdpfaggdgaRLYRTGDLVRYLPDGNLEF 374
|
410 420 430
....*....|....*....|....*....|....*
gi 1063734905 443 VDRLKELIKYKGYQVPPAELEALLLNHPDILDAAV 477
Cdd:TIGR01733 375 LGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
53-513 |
1.08e-47 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 173.32 E-value: 1.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 53 KTAFIDAATDH----RISFSDLWMAVDRVADCLLhDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLttaNPLntaSE 128
Cdd:PRK13295 40 KTAVTAVRLGTgaprRFTYRELAALVDRVAVGLA-RLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVL---NPL---MP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 129 ILRQiadsnPKLAFTTpelapKIASSGISIV------------LERVEDTLRVPRGLKVVGN----------LTEMMKKE 186
Cdd:PRK13295 113 IFRE-----RELSFML-----KHAESKVLVVpktfrgfdhaamARRLRPELPALRHVVVVGGdgadsfeallITPAWEQE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 187 PSGQAV--RNQVHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVARYIAEPFEQPQQTFICTVPLFHTFGLLNFVLATLA 264
Cdd:PRK13295 183 PDAPAIlaRLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVM 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 265 LGTTVVILPRFDLGEMMAAVEKYRATTLILVPPVLVTMINKADQimKKYDVSFLRTVRCGGAP----LSKEVTQGFMKKy 340
Cdd:PRK13295 263 LGATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKE--SGRPVSSLRTFLCAGAPipgaLVERARAALGAK- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 341 ptvdVYQGYALTEsNGAGASIESVEESRRYGAV-GLLSCGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEEEI 419
Cdd:PRK13295 340 ----IVSAWGMTE-NGAVTLTKLDDPDERASTTdGCPLPGVEVRVVDAD-GAPLPAGQIGRLQVRGCSNFGGYLKRPQLN 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 420 ITS-EGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPE 498
Cdd:PRK13295 414 GTDaDGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPG 493
|
490
....*....|....*
gi 1063734905 499 SNLCEKKVIDFISKQ 513
Cdd:PRK13295 494 QSLDFEEMVEFLKAQ 508
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
66-497 |
1.45e-47 |
|
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: 170.76 E-value: 1.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 66 SFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVlttANPLNTA---SEILRQIADSNPKLAF 142
Cdd:cd05969 2 TFAQLKVLSARFAN-VLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAV---ICPLFSAfgpEAIRDRLENSEAKVLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 143 TTPELApkiassgisivlERVEdtlrvprglkvvgnltemmkkepsgqavrnqvhKDDTAMLLYSSGTTGRSKGVNSSHG 222
Cdd:cd05969 78 TTEELY------------ERTD---------------------------------PEDPTLLHYTSGTTGTPKGVLHVHD 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 223 NLIAH--VARYIAEpfEQPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILP-RFDLGEMMAAVEKYRATTLILVPPVL 299
Cdd:cd05969 113 AMIFYyfTGKYVLD--LHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEgRFDAESWYGIIERVKVTVWYTAPTAI 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 300 VTMINKADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYpTVDVYQGYALTESnGAGASIESVEESRRYGAVGLLSCG 379
Cdd:cd05969 191 RMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVF-GVPIHDTWWQTET-GSIMIANYPCMPIKPGSMGKPLPG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 380 VEARIVDPNtGQVMGLNQTGELWLKG--PSIAKGYFRNEEEIITS--EGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGY 455
Cdd:cd05969 269 VKAAVVDEN-GNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSfiDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGH 347
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1063734905 456 QVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKP 497
Cdd:cd05969 348 RVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKE 389
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
62-498 |
1.89e-47 |
|
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: 170.35 E-value: 1.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 62 DHRISFSDLWMAVDRVADCLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLntaseiLRQiadsnpkla 141
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPL------LRP--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 142 fttPELAPKIASSGISIVLervedtlrvprglkVVGNLTemmkkepsgqavrnqvHKDDTAMLLYSSGTTGRSKGVNSSH 221
Cdd:cd05958 73 ---KELAYILDKARITVAL--------------CAHALT----------------ASDDICILAFTSGTTGAPKATMHFH 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 222 GNLIAHVARY---IAEPfeQPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPRFDLGEMMAAVEKYRATTLILVPPV 298
Cdd:cd05958 120 RDPLASADRYavnVLRL--REDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYKPTVLFTAPTA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 299 LVTMINKADQimKKYDVSFLRTVRCGGAPLSKEVTQGFmKKYPTVDVYQGYALTESngAGASIESVEESRRYGAVGLLSC 378
Cdd:cd05958 198 YRAMLAHPDA--AGPDLSSLRKCVSAGEALPAALHRAW-KEATGIPIIDGIGSTEM--FHIFISARPGDARPGATGKPVP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 379 GVEARIVDpNTGQVMGLNQTGELWLKGPSIAKGYFRNEEEIITSEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVP 458
Cdd:cd05958 273 GYEAKVVD-DEGNPVPDGTIGRLAVRGPTGCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIA 351
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1063734905 459 PAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPE 498
Cdd:cd05958 352 PPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPG 391
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
53-499 |
6.18e-47 |
|
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: 169.18 E-value: 6.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 53 KTAFIDAatDHRISFSDLWMAVDRVADCLlHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQ 132
Cdd:cd05919 1 KTAFYAA--DRSVTYGQLHDGANRLGSAL-RNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 133 IADSNPKLAFTtpelapkiassgisivlervedtlrvprglkvvgnltemmkkepsgqavrnqvHKDDTAMLLYSSGTTG 212
Cdd:cd05919 78 ARDCEARLVVT-----------------------------------------------------SADDIAYLLYSSGTTG 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 213 RSKGVNSSHGNLIAHVARYIAEPFE-QPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPRFDLGE-MMAAVEKYRAT 290
Cdd:cd05919 105 PPKGVMHAHRDPLLFADAMAREALGlTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWPTAErVLATLARFRPT 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 291 TLILVPPVLVTMINKADqiMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYpTVDVYQGYALTE------SNGAGASiesv 364
Cdd:cd05919 185 VLYGVPTFYANLLDSCA--GSPDALRSLRLCVSAGEALPRGLGERWMEHF-GGPILDGIGATEvghiflSNRPGAW---- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 365 eesrRYGAVGLLSCGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEEEIITS--EGWLKTGDLCYIDNDGFLFI 442
Cdd:cd05919 258 ----RLGSTGRPVPGYEIRLVDEE-GHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATfnGGWYRTGDKFCRDADGWYTH 332
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063734905 443 VDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPES 499
Cdd:cd05919 333 AGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPA 389
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
64-497 |
1.67e-46 |
|
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: 167.99 E-value: 1.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 64 RISFSDLWMAVDRVADCLLhDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLntaseilrqiadsnpklaFT 143
Cdd:cd05971 6 KVTFKELKTASNRFANVLK-EIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFAL------------------FG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 144 TPELAPKIASSGISIVlerVEDTlrvprglkvvgnltemmkkepsgqavrnqvhKDDTAMLLYSSGTTGRSKGVNSSHGN 223
Cdd:cd05971 67 PEALEYRLSNSGASAL---VTDG-------------------------------SDDPALIIYTSGTTGPPKGALHAHRV 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 224 LIAHVARYiaepfEQPQQTFICTVPLFHT-------FGLLNFVLATLALGTTVVI--LPRFDLGEMMAAVEKYRATTLIL 294
Cdd:cd05971 113 LLGHLPGV-----QFPFNLFPRDGDLYWTpadwawiGGLLDVLLPSLYFGVPVLAhrMTKFDPKAALDLMSRYGVTTAFL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 295 vPPVLVTMINKADQIMKKYDVSfLRTVRCGGAPLSKEVTqGFMKKYPTVDVYQGYALTESN---GAGASIESVeesrRYG 371
Cdd:cd05971 188 -PPTALKMMRQQGEQLKHAQVK-LRAIATGGESLGEELL-GWAREQFGVEVNEFYGQTECNlviGNCSALFPI----KPG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 372 AVGLLSCGVEARIVDPNtGQVMGLNQTGELWLKGPSIAK--GYFRNEE--EIITSEGWLKTGDLCYIDNDGFLFIVDRLK 447
Cdd:cd05971 261 SMGKPIPGHRVAIVDDN-GTPLPPGEVGEIAVELPDPVAflGYWNNPSatEKKMAGDWLLTGDLGRKDSDGYFWYVGRDD 339
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1063734905 448 ELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKP 497
Cdd:cd05971 340 DVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNP 389
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
53-513 |
3.60e-46 |
|
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: 166.93 E-value: 3.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 53 KTAFIDAatDHRISFSDLWMAVDRVADCLLHdVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTtanPLNTASEILRQ 132
Cdd:cd05930 3 AVAVVDG--DQSLTYAELDARANRLARYLRE-RGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYV---PLDPSYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 133 ---IADSNPKLAFTTPelapkiassgisivlervedtlrvprglkvvgnltemmkkepsgqavrnqvhkDDTAMLLYSSG 209
Cdd:cd05930 77 ayiLEDSGAKLVLTDP-----------------------------------------------------DDLAYVIYTSG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 210 TTGRSKGVNSSHGNLIAHVARYIAEPFEQPQQTFICTVPLFHTFGLLNFvLATLALGTTVVILP---RFDLGEMMAAVEK 286
Cdd:cd05930 104 STGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEI-FGALLAGATLVVLPeevRKDPEALADLLAE 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 287 YRATTLILVPPVLVTMInkadQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVDVYQGYALTEsNGAGASIESVEE 366
Cdd:cd05930 183 EGITVLHLTPSLLRLLL----QELELAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTE-ATVDATYYRVPP 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 367 SRRYGA---VGLLSCGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEEEiiTSE----------GWL-KTGDLC 432
Cdd:cd05930 258 DDEEDGrvpIGRPIPNTRVYVLDEN-LRPVPPGVPGELYIGGAGLARGYLNRPEL--TAErfvpnpfgpgERMyRTGDLV 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 433 YIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKVIDFISK 512
Cdd:cd05930 335 RWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAE 414
|
.
gi 1063734905 513 Q 513
Cdd:cd05930 415 R 415
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
65-496 |
1.19e-45 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 168.13 E-value: 1.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 65 ISFSDLWMAVDRVADCLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLAF-- 142
Cdd:PRK08751 51 ITYREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVvi 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 143 ----TTPELApkIASSGISIVLER-VEDTLRVPRGLKVVGNLTEMMKKEPSGQ---AVR---------------NQVHKD 199
Cdd:PRK08751 131 dnfgTTVQQV--IADTPVKQVITTgLGDMLGFPKAALVNFVVKYVKKLVPEYRingAIRfrealalgrkhsmptLQIEPD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 200 DTAMLLYSSGTTGRSKGVNSSHGNLIAH---VARYIAE--PFEQPQQTFICTVPLFHTFGLLNFVLATLALG--TTVVIL 272
Cdd:PRK08751 209 DIAFLQYTGGTTGVAKGAMLTHRNLVANmqqAHQWLAGtgKLEEGCEVVITALPLYHIFALTANGLVFMKIGgcNHLISN 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 273 PRfDLGEMMAAVEKYRATTLILVPPVLVTMINKA--DQImkkyDVSFLRTVRCGGAPLSKEVTQGFmKKYPTVDVYQGYA 350
Cdd:PRK08751 289 PR-DMPGFVKELKKTRFTAFTGVNTLFNGLLNTPgfDQI----DFSSLKMTLGGGMAVQRSVAERW-KQVTGLTLVEAYG 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 351 LTESNGAgASIESVEESRRYGAVGLLSCGVEARIVDpNTGQVMGLNQTGELWLKGPSIAKGYFRNEEE---IITSEGWLK 427
Cdd:PRK08751 363 LTETSPA-ACINPLTLKEYNGSIGLPIPSTDACIKD-DAGTVLAIGEIGELCIKGPQVMKGYWKRPEEtakVMDADGWLH 440
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063734905 428 TGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARK 496
Cdd:PRK08751 441 TGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKK 509
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
47-509 |
2.08e-45 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 167.24 E-value: 2.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 47 SQTYRGKTAFIDAATdhRISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVlttANPLNTA 126
Cdd:PRK06155 31 AERYPDRPLLVFGGT--RWTYAEAARAAAAAAH-ALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAI---AVPINTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 127 S---EILRQIADSNPKLAFTTPELAPKIASSGISIV-LERV-----EDTLRVPRGLKVVGnltemmkKEPSGQAV-RNQV 196
Cdd:PRK06155 105 LrgpQLEHILRNSGARLLVVEAALLAALEAADPGDLpLPAVwlldaPASVSVPAGWSTAP-------LPPLDAPApAAAV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 197 HKDDTAMLLYSSGTTGRSKGVNSSHGNLIAhVARYIAEPFE-QPQQTFICTVPLFHTFGLLNFVLATLAlGTTVVILPRF 275
Cdd:PRK06155 178 QPGDTAAILYTSGTTGPSKGVCCPHAQFYW-WGRNSAEDLEiGADDVLYTTLPLFHTNALNAFFQALLA-GATYVLEPRF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 276 DLGEMMAAVEKYRATTLIL----VPPVLVTMINKADQImkkydvsflRTVRCGGAP-LSKEVTQGFMKKYpTVDVYQGYA 350
Cdd:PRK06155 256 SASGFWPAVRRHGATVTYLlgamVSILLSQPARESDRA---------HRVRVALGPgVPAALHAAFRERF-GVDLLDGYG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 351 LTESNgagASIESVEESRRYGAVGLLSCGVEARIVDPNtGQVMGLNQTGELWLKG--P-SIAKGYFRNEEEIITS--EGW 425
Cdd:PRK06155 326 STETN---FVIAVTHGSQRPGSMGRLAPGFEARVVDEH-DQELPDGEPGELLLRAdePfAFATGYFGMPEKTVEAwrNLW 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 426 LKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKK 505
Cdd:PRK06155 402 FHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVA 481
|
....
gi 1063734905 506 VIDF 509
Cdd:PRK06155 482 LVRH 485
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
58-514 |
3.37e-45 |
|
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: 166.65 E-value: 3.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 58 DAATDHRISFSDLWMAVDRVADCLLHdVGiRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTA---NPLNTASEILRQIA 134
Cdd:cd05931 18 EGGREETLTYAELDRRARAIAARLQA-VG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLpppTPGRHAERLAAILA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 135 DSNPKLAFTTPELAPKIAssgisivlERVEDTLRVPRGLKVVGNLTEmmkKEPSGQAVRNQVHKDDTAMLLYSSGTTGRS 214
Cdd:cd05931 96 DAGPRVVLTTAAALAAVR--------AFAASRPAAGTPRLLVVDLLP---DTSAADWPPPSPDPDDIAYLQYTSGSTGTP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 215 KGVNSSHGNLIAHVaRYIAEPFE-QPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILP---------RFdlgemMAAV 284
Cdd:cd05931 165 KGVVVTHRNLLANV-RQIRRAYGlDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSpaaflrrplRW-----LRLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 285 EKYRATTlILVP----PVLVTMINKADqiMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKY------PTVdVYQGYALTE- 353
Cdd:cd05931 239 SRYRATI-SAAPnfayDLCVRRVRDED--LEGLDLSSWRVALNGAEPVRPATLRRFAEAFapfgfrPEA-FRPSYGLAEa 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 354 ----SNGAGASIESVEESRRY--------------GAVGLLSCG-----VEARIVDPNTGQVMGLNQTGELWLKGPSIAK 410
Cdd:cd05931 315 tlfvSGGPPGTGPVVLRVDRDalagravavaaddpAARELVSCGrplpdQEVRIVDPETGRELPDGEVGEIWVRGPSVAS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 411 GYFRNEEEI---------ITSEGWLKTGDLCYIdNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILD---AAVI 478
Cdd:cd05931 395 GYWGRPEATaetfgalaaTDEGGWLRTGDLGFL-HDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRpgcVAAF 473
|
490 500 510
....*....|....*....|....*....|....*.
gi 1063734905 479 PFPDKEAGQFPMAYVARKPESNLCEKKVIDFISKQV 514
Cdd:cd05931 474 SVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAV 509
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
73-513 |
3.47e-45 |
|
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: 164.92 E-value: 3.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 73 AVDRVADcLLHDVGIRRGD-VVLVLSPNTISIPI---VCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLAFTTPELA 148
Cdd:cd05922 2 GVSAAAS-ALLEAGGVRGErVVLILPNRFTYIELsfaVAYAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 149 pkiassgisivlERVEDTLRVPRGLKVVGNLTEMMKKEPSGQAVRNQvhKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHv 228
Cdd:cd05922 81 ------------DRLRDALPASPDPGTVLDADGIRAARASAPAHEVS--HEDLALLLYTSGSTGSPKLVRLSHQNLLAN- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 229 ARYIAEPFE-QPQQTFICTVPLFHTFGLlNFVLATLALGTTVVILPRFDLGE-MMAAVEKYRATTLILVPPvLVTMINKA 306
Cdd:cd05922 146 ARSIAEYLGiTADDRALTVLPLSYDYGL-SVLNTHLLRGATLVLTNDGVLDDaFWEDLREHGATGLAGVPS-TYAMLTRL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 307 DqiMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVDVYQGYALTESNGAGASIESVEESRRYGAVGLLSCGVEARIVD 386
Cdd:cd05922 224 G--FDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPERILEKPGSIGLAIPGGEFEILD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 387 PNtGQVMGLNQTGELWLKGPSIAKGYFRNEEEII---TSEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELE 463
Cdd:cd05922 302 DD-GTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRkegRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIE 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1063734905 464 ALLLNHPDILDAAVIPFPDkEAGQFPMAYVARKPESNLceKKVIDFISKQ 513
Cdd:cd05922 381 AAARSIGLIIEAAAVGLPD-PLGEKLALFVTAPDKIDP--KDVLRSLAER 427
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
46-499 |
6.91e-45 |
|
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: 164.42 E-value: 6.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 46 SSQTYRGKTAFIDAatDHRISFSDLWMAVDRVAdCLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNT 125
Cdd:cd05920 24 SAARHPDRIAVVDG--DRRLTYRELDRRADRLA-AGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 126 ASEILRQIADSNPKLafttpelapkiassgisivlervedtLRVPRGLKVVgnltemmkkepSGQAVRNQVHKD--DTAM 203
Cdd:cd05920 101 RSELSAFCAHAEAVA--------------------------YIVPDRHAGF-----------DHRALARELAESipEVAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 204 LLYSSGTTGRSKGVNSSHgNLIAHVARYIAEPFEQPQQT-FICTVPLFHTFGLLN-FVLATLALGTTVVILPRFDLGEMM 281
Cdd:cd05920 144 FLLSGGTTGTPKLIPRTH-NDYAYNVRASAEVCGLDQDTvYLAVLPAAHNFPLACpGVLGTLLAGGRVVLAPDPSPDAAF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 282 AAVEKYRATTLILVPPVLVTMINKADQimKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYpTVDVYQGYALTES----NGA 357
Cdd:cd05920 223 PLIEREGVTVTALVPALVSLWLDAAAS--RRADLSSLRLLQVGGARLSPALARRVPPVL-GCTLQQVFGMAEGllnyTRL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 358 GASIESVEESRRYGavglLSCGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEEE---IITSEGWLKTGDLCYI 434
Cdd:cd05920 300 DDPDEVIIHTQGRP----MSPDDEIRVVDEE-GNPVPPGEEGELLTRGPYTIRGYYRAPEHnarAFTPDGFYRTGDLVRR 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063734905 435 DNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPES 499
Cdd:cd05920 375 TPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPP 439
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
65-484 |
1.62e-44 |
|
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: 163.00 E-value: 1.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 65 ISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLAFTT 144
Cdd:cd05914 8 LTYKDLADNIAKFAL-LLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 145 PElapkiassgisivlervedtlrvprglkvvgnltemmkkepsgqavrnqvhkDDTAMLLYSSGTTGRSKGVNSSHGNL 224
Cdd:cd05914 87 DE----------------------------------------------------DDVALINYTSGTTGNSKGVMLTYRNI 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 225 IAHVARYIAEPFEQPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPRF--DLGEMMAaveKYRATTLILVPPVLVTM 302
Cdd:cd05914 115 VSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIpsAKIIALA---FAQVTPTLGVPVPLVIE 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 303 -------INKAD------QIMKK-YDVSFLRTVR---------------CGGAPLSKEVTQGFMK-KYPtvdVYQGYALT 352
Cdd:cd05914 192 kifkmdiIPKLTlkkfkfKLAKKiNNRKIRKLAFkkvheafggnikefvIGGAKINPDVEEFLRTiGFP---YTIGYGMT 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 353 ESNGAGASieSVEESRRYGAVGLLSCGVEARIVDPNTGqvmglNQTGELWLKGPSIAKGYFRNEE---EIITSEGWLKTG 429
Cdd:cd05914 269 ETAPIISY--SPPNRIRLGSAGKVIDGVEVRIDSPDPA-----TGEGEIIVRGPNVMKGYYKNPEataEAFDKDGWFHTG 341
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063734905 430 DLCYIDNDGFLFIVDRLKELI-KYKGYQVPPAELEALLLNHPDILDAAVIPFPDKE 484
Cdd:cd05914 342 DLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKL 397
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
46-513 |
2.00e-44 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 164.54 E-value: 2.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 46 SSQTYRGKTAFIDaatDHRISFSdlWMAVDRVADCL---LHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANP 122
Cdd:PRK06087 32 TARAMPDKIAVVD---NHGASYT--YSALDHAASRLanwLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 123 LNTASEILRQIADSNPKlAFTTPELAPKIasSGISIVLERVEDtlrVPRGLKVVG-----------NLTEMMKKEPSGQA 191
Cdd:PRK06087 107 SWREAELVWVLNKCQAK-MFFAPTLFKQT--RPVDLILPLQNQ---LPQLQQIVGvdklapatsslSLSQIIADYEPLTT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 192 VRNqVHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVARYIAEPFEQPQQTFICTVPLFHTFGLLNFVLATLALGTTVVI 271
Cdd:PRK06087 181 AIT-THGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 272 LPRFDLGEMMAAVEKYRATTLILVPPVLVTMINKADQimKKYDVSFLRTVRCGGAPLSKEVTQgfmkkyptvDVYQ-GYA 350
Cdd:PRK06087 260 LDIFTPDACLALLEQQRCTCMLGATPFIYDLLNLLEK--QPADLSALRFFLCGGTTIPKKVAR---------ECQQrGIK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 351 LTESNGagaSIESVEE---------SRRYGAVGLLSCGVEARIVDPNTGQVMGLNQtGELWLKGPSIAKGYFRNEEE--- 418
Cdd:PRK06087 329 LLSVYG---STESSPHavvnlddplSRFMHTDGYAAAGVEIKVVDEARKTLPPGCE-GEEASRGPNVFMGYLDEPELtar 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 419 IITSEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVA-RKP 497
Cdd:PRK06087 405 ALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVlKAP 484
|
490
....*....|....*.
gi 1063734905 498 ESNLCEKKVIDFISKQ 513
Cdd:PRK06087 485 HHSLTLEEVVAFFSRK 500
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
61-487 |
3.65e-44 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 163.52 E-value: 3.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 61 TDHRI--SFSDLWMAVDRVADCLLHDvGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTtanPLNTASEILRQIADSnp 138
Cdd:PRK05852 38 TADRIaiSYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAASRADLVVV---PLDPALPIAEQRVRS-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 139 klafttpelapkiASSGISIVL-------ERVEDTLRVPRGLKVVGNLTEMMKK----------EPSGQAVRNQVHKDDT 201
Cdd:PRK05852 112 -------------QAAGARVVLidadgphDRAEPTTRWWPLTVNVGGDSGPSGGtlsvhldaatEPTPATSTPEGLRPDD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 202 AMLLYSSGTTGRSKGVNSSHGNLIAHVARYIAEPFEQPQQTFICTVPLFHTFGLLNFVLATLALGTTVvILP---RFDLG 278
Cdd:PRK05852 179 AMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAV-LLPargRFSAH 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 279 EMMAAVEKYRATTLILVPPVLVTMINKADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYpTVDVYQGYALTESNGAG 358
Cdd:PRK05852 258 TFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEF-AAPVVCAFGMTEATHQV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 359 AS--IESVEESRRYGA-VGLL--SCGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEEeiIT----SEGWLKTG 429
Cdd:PRK05852 337 TTtqIEGIGQTENPVVsTGLVgrSTGAQIRIVGSD-GLPLPAGAVGEVWLRGTTVVRGYLGDPT--ITaanfTDGWLRTG 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063734905 430 DLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQ 487
Cdd:PRK05852 414 DLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGE 471
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
200-510 |
4.42e-44 |
|
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: 158.59 E-value: 4.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 200 DTAMLLYSSGTTGRSKGVNSSHGNLIAHVARYIAEPFEQPQQTFICTVPLFHTFGLlNFVLATLALGTTVVILPRFDLGE 279
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGL-NLALATFHAGGANVVMEKFDPAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 280 MMAAVEKYRATTLILVPPVLVTMINKADQimKKYDVSFLRTVRCGGAPlskEVTQGFMKKYPTVdVYQGYALTESNGAgA 359
Cdd:cd17637 80 ALELIEEEKVTLMGSFPPILSNLLDAAEK--SGVDLSSLRHVLGLDAP---ETIQRFEETTGAT-FWSLYGQTETSGL-V 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 360 SIESVEEsrRYGAVGLLSCGVEARIVDPNTGQVmGLNQTGELWLKGPSIAKGYFRNEEEIITS--EGWLKTGDLCYIDND 437
Cdd:cd17637 153 TLSPYRE--RPGSAGRPGPLVRVRIVDDNDRPV-PAGETGEIVVRGPLVFQGYWNLPELTAYTfrNGWHHTGDLGRFDED 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063734905 438 GFLFIVDRL--KELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKVIDFI 510
Cdd:cd17637 230 GYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFV 304
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
53-497 |
6.70e-44 |
|
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: 163.52 E-value: 6.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 53 KTAFI----DAATDHRISFSDLWMAVDRVADCLLhDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASE 128
Cdd:cd17634 69 RTAIIyegdDTSQSRTISYRELHREVCRFAGTLL-DLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 129 ILRQIADSNPKLAFTTPE-----------------LAPKIASSGISIVLERVEdtlrVPRGLKVVGNL---TEMMKKEPS 188
Cdd:cd17634 148 VAGRIIDSSSRLLITADGgvragrsvplkknvddaLNPNVTSVEHVIVLKRTG----SDIDWQEGRDLwwrDLIAKASPE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 189 GQAVRnqVHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVARYIAEPFE-QPQQTFICTVPLFHTFGLLNFVLATLALGT 267
Cdd:cd17634 224 HQPEA--MNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDyGPGDIYWCTADVGWVTGHSYLLYGPLACGA 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 268 TVVIL---PRF-DLGEMMAAVEKYRATTLILVPPVLVTMINKADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKY--- 340
Cdd:cd17634 302 TTLLYegvPNWpTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIgke 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 341 --PTVDVYQGyalTESNGAGASIESVEESRRYGAVGLLSCGVEARIVDpNTGQVMGLNQTGELWLKG--PSIAKGYFRNE 416
Cdd:cd17634 382 kcPVVDTWWQ---TETGGFMITPLPGAIELKAGSATRPVFGVQPAVVD-NEGHPQPGGTEGNLVITDpwPGQTRTLFGDH 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 417 EEIITS-----EGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMA 491
Cdd:cd17634 458 ERFEQTyfstfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYA 537
|
....*.
gi 1063734905 492 YVARKP 497
Cdd:cd17634 538 YVVLNH 543
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
48-500 |
5.26e-43 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 158.56 E-value: 5.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 48 QTYRGKTAFIDaaTDHRISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAvltTANPLNTAS 127
Cdd:cd05945 2 AANPDRPAVVE--GGRTLTYRELKERADALAA-ALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGH---AYVPLDASS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 128 --EILRQIAD-SNPKLAFTTPelapkiassgisivlervedtlrvprglkvvgnltemmkkepsgqavrnqvhkDDTAML 204
Cdd:cd05945 76 paERIREILDaAKPALLIADG-----------------------------------------------------DDNAYI 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 205 LYSSGTTGRSKGVNSSHGNLIAHVARYIAEPFEQPQQTFICTVPLfhTFGLLNF-VLATLALGTTVVILPR---FDLGEM 280
Cdd:cd05945 103 IFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPF--SFDLSVMdLYPALASGATLVPVPRdatADPKQL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 281 MAAVEKYRATTLILVPPVLVTMINKADQIMKKYDVsfLRTVRCGGAPLSKEVTQGFMKKYPTVDVYQGYALTESNGAGAS 360
Cdd:cd05945 181 FRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLPS--LRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTY 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 361 IESVEES-RRYGAV--GLLSCGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEEE----IITSEG--WLKTGDL 431
Cdd:cd05945 259 IEVTPEVlDGYDRLpiGYAKPGAKLVILDED-GRPVPPGEKGELVISGPSVSKGYLNNPEKtaaaFFPDEGqrAYRTGDL 337
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063734905 432 CYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESN 500
Cdd:cd05945 338 VRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAE 406
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
51-499 |
1.07e-42 |
|
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: 158.83 E-value: 1.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 51 RGKTAFIDAATDHRISFSDLWMAVDRVAdCLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEIL 130
Cdd:cd05923 15 PDACAIADPARGLRLTYSELRARIEAVA-ARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 131 RQIADSNPKLAFTTP--ELAPKIASSGISIVLERVEDTLRVPrglKVVGNLTEMMKKEPsgqavrnqvhkDDTAMLLYSS 208
Cdd:cd05923 94 ELIERGEMTAAVIAVdaQVMDAIFQSGVRVLALSDLVGLGEP---ESAGPLIEDPPREP-----------EQPAFVFYTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 209 GTTGRSKGVnsshgnLIAHVARyiaepfeQPQQTFICTV---------------PLFHTFGLLNFVLATLALGTTVVILP 273
Cdd:cd05923 160 GTTGLPKGA------VIPQRAA-------ESRVLFMSTQaglrhgrhnvvlglmPLYHVIGFFAVLVAALALDGTYVVVE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 274 RFDLGEMMAAVEKYRATTLILVPPVLVTMINKADQIMKKydVSFLRTVRCGGAPLskevTQGFMKKY------PTVDVYq 347
Cdd:cd05923 227 EFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLK--LSSLRHVTFAGATM----PDAVLERVnqhlpgEKVNIY- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 348 gyALTESNGAGASIESVEESRryGAVGLLScgvEARIVDPNTGQVMGL--NQTGELWLKGPSIA--KGYFRNEEEIITS- 422
Cdd:cd05923 300 --GTTEAMNSLYMRDARTGTE--MRPGFFS---EVRIVRIGGSPDEALanGEEGELIVAAAADAafTGYLNQPEATAKKl 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063734905 423 -EGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPES 499
Cdd:cd05923 373 qDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGT 450
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
47-487 |
1.08e-41 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 155.94 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 47 SQTYRGKTAFIDAATDHRISFSDL---WMAVDRVadclLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPL 123
Cdd:PRK13390 7 AQIAPDRPAVIVAETGEQVSYRQLdddSAALARV----LYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 124 NTASEILRQIADSNPKLAFTTPELAPKIASSGISIVLE-----RVEDTLRVPRGLKVVG-NLTEmmkkEPSGqavrnqvh 197
Cdd:PRK13390 83 LTAPEADYIVGDSGARVLVASAALDGLAAKVGADLPLRlsfggEIDGFGSFEAALAGAGpRLTE----QPCG-------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 198 kddtAMLLYSSGTTGRSKGVN--------SSHGNLIAHVARYIAEPFEQpqQTFICTVPLFHTfGLLNFVLATLALGTTV 269
Cdd:PRK13390 151 ----AVMLYSSGTTGFPKGIQpdlpgrdvDAPGDPIVAIARAFYDISES--DIYYSSAPIYHA-APLRWCSMVHALGGTV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 270 VILPRFDLGEMMAAVEKYRATTLILVPPVLVTMINKADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVdVYQGY 349
Cdd:PRK13390 224 VLAKRFDAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPI-VYEYY 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 350 ALTESNGAgASIESVEESRRYGAVGLLSCGvEARIVDpNTGQVMGLNQTGELWLKGPSIAKGYFRNEEEIITSEG----- 424
Cdd:PRK13390 303 SSTEAHGM-TFIDSPDWLAHPGSVGRSVLG-DLHICD-DDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHpahpf 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063734905 425 WLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQ 487
Cdd:PRK13390 380 WTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGE 442
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
50-512 |
3.43e-41 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 154.84 E-value: 3.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 50 YRGKTAFI--DAATDHR-ISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIpIVCL-SVMSLGAVLTtanPLNT 125
Cdd:PRK08008 20 YGHKTALIfeSSGGVVRrYSYLELNEEINRTAN-LFYSLGIRKGDKVALHLDNCPEF-IFCWfGLAKIGAIMV---PINA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 126 ------ASEILRQiadSNPKLAFTTPELAP---KIASSGIS----IVLERVEDTLRVPrglkvVGNLTEMMKKEPSGQAV 192
Cdd:PRK08008 95 rllreeSAWILQN---SQASLLVTSAQFYPmyrQIQQEDATplrhICLTRVALPADDG-----VSSFTQLKAQQPATLCY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 193 RNQVHKDDTAMLLYSSGTTGRSKGVNSSHGNLIaHVARYIA-EPFEQPQQTFICTVPLFHTFGLLNFVLATLALGTTVVI 271
Cdd:PRK08008 167 APPLSTDDTAEILFTSGTTSRPKGVVITHYNLR-FAGYYSAwQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 272 LPRFDLGEMMAAVEKYRATTLILVPPVLVT-MINKA---DQIMKKYDVSFLrtvrcggAPLSKEVTQGFMKKYpTVDVYQ 347
Cdd:PRK08008 246 LEKYSARAFWGQVCKYRATITECIPMMIRTlMVQPPsanDRQHCLREVMFY-------LNLSDQEKDAFEERF-GVRLLT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 348 GYALTESNGaGASIESVEESRRYGAVGLLSCGVEARIVDPNtGQVMGLNQTGELWLKG---PSIAKGYFRNEE---EIIT 421
Cdd:PRK08008 318 SYGMTETIV-GIIGDRPGDKRRWPSIGRPGFCYEAEIRDDH-NRPLPAGEIGEICIKGvpgKTIFKEYYLDPKataKVLE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 422 SEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNL 501
Cdd:PRK08008 396 ADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETL 475
|
490
....*....|.
gi 1063734905 502 CEKKVIDFISK 512
Cdd:PRK08008 476 SEEEFFAFCEQ 486
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
71-506 |
1.65e-39 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 150.68 E-value: 1.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 71 WMAVDRVADCL---LHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGA--VLttanpLNTAseilrqiadsnpklaFTTP 145
Cdd:PRK13382 71 WRELDERSDALaaaLQALPIGEPRVVGIMCRNHRGFVEALLAANRIGAdiLL-----LNTS---------------FAGP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 146 ELAPKIASSGISIVLERVEDTLRVPRGLKVVGNLT--------------EMMKKEPSGQAVRNQVHKDDTAMLlySSGTT 211
Cdd:PRK13382 131 ALAEVVTREGVDTVIYDEEFSATVDRALADCPQATrivawtdedhdltvEVLIAAHAGQRPEPTGRKGRVILL--TSGTT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 212 GRSKGVNSShGNLIAHVARYIAE--PFEQPQQTFIcTVPLFHTFGLLNFVLAtLALGTTVVILPRFDLGEMMAAVEKYRA 289
Cdd:PRK13382 209 GTPKGARRS-GPGGIGTLKAILDrtPWRAEEPTVI-VAPMFHAWGFSQLVLA-ASLACTIVTRRRFDPEATLDLIDRHRA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 290 TTLILVPPVLVTMINKADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVdVYQGYALTEsngAG-ASIESVEESR 368
Cdd:PRK13382 286 TGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDV-IYNNYNATE---AGmIATATPADLR 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 369 RY-GAVGLLSCGVEARIVDPN-----TGQVmglnqtGELWLKGPSIAKGYFRNEEEIItSEGWLKTGDLCYIDNDGFLFI 442
Cdd:PRK13382 362 AApDTAGRPAEGTEIRILDQDfrevpTGEV------GTIFVRNDTQFDGYTSGSTKDF-HDGFMASGDVGYLDENGRLFV 434
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063734905 443 VDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKV 506
Cdd:PRK13382 435 VGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETL 498
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
51-497 |
3.16e-39 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 150.05 E-value: 3.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 51 RGKTA--FIDAATDHRISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTtanPLNTA-- 126
Cdd:PRK04319 58 KDKVAlrYLDASRKEKYTYKELKELSNKFAN-VLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVG---PLFEAfm 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 127 SEILRQ-IADSNPKLAFTTPELAPKIASSGIS----IVLerVEDTLRVPRGLKvvgNLTEMMKKEPSGQAVRNqVHKDDT 201
Cdd:PRK04319 134 EEAVRDrLEDSEAKVLITTPALLERKPADDLPslkhVLL--VGEDVEEGPGTL---DFNALMEQASDEFDIEW-TDREDG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 202 AMLLYSSGTTGRSKGVNSSHGNLIAH--VARYIAEpfEQPQQTFICTV-PLFHT---FGllnfVLATLALGTTVVIL-PR 274
Cdd:PRK04319 208 AILHYTSGSTGKPKGVLHVHNAMLQHyqTGKYVLD--LHEDDVYWCTAdPGWVTgtsYG----IFAPWLNGATNVIDgGR 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 275 FDLGEMMAAVEKYRATTLILVPPVLVTMINKADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKY--PtvdVYQGYALT 352
Cdd:PRK04319 282 FSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDLSSLRHILSVGEPLNPEVVRWGMKVFglP---IHDNWWMT 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 353 E------SNGAGASIesveesrRYGAVGLLSCGVEARIVDpNTGQVMGLNQTGELWLKG--PSIAKGYFRNEE--EIITS 422
Cdd:PRK04319 359 EtggimiANYPAMDI-------KPGSMGKPLPGIEAAIVD-DQGNELPPNRMGNLAIKKgwPSMMRGIWNNPEkyESYFA 430
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063734905 423 EGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKP 497
Cdd:PRK04319 431 GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRP 505
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
196-467 |
5.81e-39 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 152.00 E-value: 5.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 196 VHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVARyIAEPFEQPQQTFICTV-PLFHTFGLLNFVLATLALGTTVVILPR 274
Cdd:PRK08633 779 FKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQ-ISDVFNLRNDDVILSSlPFFHSFGLTVTLWLPLLEGIKVVYHPD 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 275 FDLGEMMA-AVEKYRATTLILVPPVLVTMI--NKADQIMkkydVSFLRTVRCGGAPLSKEVTQGFMKKYpTVDVYQGYAL 351
Cdd:PRK08633 858 PTDALGIAkLVAKHRATILLGTPTFLRLYLrnKKLHPLM----FASLRLVVAGAEKLKPEVADAFEEKF-GIRILEGYGA 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 352 TESNG-AGASIESVEESR-------RYGAVGLLSCGVEARIVDPNTGQVMGLNQTGELWLKGPSIAKGYFRNEEEiiTSE 423
Cdd:PRK08633 933 TETSPvASVNLPDVLAADfkrqtgsKEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEK--TAE 1010
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1063734905 424 --------GWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLL 467
Cdd:PRK08633 1011 vikdidgiGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELA 1062
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
200-497 |
6.92e-39 |
|
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: 144.40 E-value: 6.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 200 DTAMLLYSSGTTGRSKGVNSSHGNLIAHvARYIAEPFEQ-PQQTFICTVPLFHTFGLLnFVLATLALGTTVVIL-PRFDL 277
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLAS-AAGLHSRLGFgGGDSWLLSLPLYHVGGLA-ILVRSLLAGAELVLLeRNQAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 278 GEMMAAvekYRATTLILVPPVLVTMInkaDQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKypTVDVYQGYALTESNGA 357
Cdd:cd17630 79 AEDLAP---PGVTHVSLVPTQLQRLL---DSGQGPAALKSLRAVLLGGAPIPPELLERAADR--GIPLYTTYGMTETASQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 358 GASIESVEESRRYgaVGLLSCGVEARIVDPntgqvmglnqtGELWLKGPSIAKGYFRNE-EEIITSEGWLKTGDLCYIDN 436
Cdd:cd17630 151 VATKRPDGFGRGG--VGVLLPGRELRIVED-----------GEIWVGGASLAMGYLRGQlVPEFNEDGWFTTKDLGELHA 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063734905 437 DGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMA-YVARKP 497
Cdd:cd17630 218 DGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAvIVGRGP 279
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
64-515 |
2.82e-37 |
|
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: 143.27 E-value: 2.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 64 RISFSDLWMAVDRVAdCLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVlttanplntasEILRQiADSnpklafT 143
Cdd:cd17640 5 RITYKDLYQEILDFA-AGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAV-----------DVVRG-SDS------S 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 144 TPELAPKIASSGISIVlervedtlrvprglkVVGNltemmkkepsgqavrnqvHKDDTAMLLYSSGTTGRSKGVNSSHGN 223
Cdd:cd17640 66 VEELLYILNHSESVAL---------------VVEN------------------DSDDLATIIYTSGTTGNPKGVMLTHAN 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 224 LIaHVARYIAEpFEQPQ--QTFICTVPLFHTFG-LLNFVLATLALG---TTVVILPRfDLgemmaavEKYRATTLILVPP 297
Cdd:cd17640 113 LL-HQIRSLSD-IVPPQpgDRFLSILPIWHSYErSAEYFIFACGCSqayTSIRTLKD-DL-------KRVKPHYIVSVPR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 298 VLVTMINKA-DQI-----MKKYDVSFL------RTVRCGGAPLSKEVTQGFmkKYPTVDVYQGYALTESNGAGASIESVE 365
Cdd:cd17640 183 LWESLYSGIqKQVsksspIKQFLFLFFlsggifKFGISGGGALPPHVDTFF--EAIGIEVLNGYGLTETSPVVSARRLKC 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 366 ESRryGAVGLLSCGVEARIVDPNTGQVMGLNQTGELWLKGPSIAKGYFRNEE---EIITSEGWLKTGDLCYIDNDGFLFI 442
Cdd:cd17640 261 NVR--GSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEatsKVLDSDGWFNTGDLGWLTCGGELVL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 443 VDRLKELIKYK-GYQVPPAELEALLLNHPDI------------LDAAVIPFPD------KEAGQFpmayVARKPESNLCE 503
Cdd:cd17640 339 TGRAKDTIVLSnGENVEPQPIEEALMRSPFIeqimvvgqdqkrLGALIVPNFEelekwaKESGVK----LANDRSQLLAS 414
|
490
....*....|..
gi 1063734905 504 KKVIDFISKQVL 515
Cdd:cd17640 415 KKVLKLYKNEIK 426
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
64-499 |
7.17e-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: 142.48 E-value: 7.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 64 RISFSDLwmavDRVADCLLHDV---GIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKL 140
Cdd:cd17651 20 RLTYAEL----DRRANRLAHRLrarGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 141 AFTTPELAPKIASsgisivlERVEDTLRVPRGLKvvgnltemmkkEPSGQAVRNQVHKDDTAMLLYSSGTTGRSKGVNSS 220
Cdd:cd17651 96 VLTHPALAGELAV-------ELVAVTLLDQPGAA-----------AGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 221 HG---NLIA-HVARYIAEPFEQPQQtfictvplfhtFGLLNF------VLATLALGTTVVILP---RFDLGEMMAAVEKY 287
Cdd:cd17651 158 HRslaNLVAwQARASSLGPGARTLQ-----------FAGLGFdvsvqeIFSTLCAGATLVLPPeevRTDPPALAAWLDEQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 288 RATTLILVPPVLVTMINKADQIMKKydVSFLRTVRCGGAPLS-KEVTQGFMKKYPTVDVYQGYALTESNGAGASIESVEE 366
Cdd:cd17651 227 RISRVFLPTVALRALAEHGRPLGVR--LAALRYLLTGGEQLVlTEDLREFCAGLPGLRLHNHYGPTETHVVTALSLPGDP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 367 SRRYGA--VGLLSCGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEEeiITSEGWL-----------KTGDLCY 433
Cdd:cd17651 305 AAWPAPppIGRPIDNTRVYVLDAA-LRPVPPGVPGELYIGGAGLARGYLNRPE--LTAERFVpdpfvpgarmyRTGDLAR 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063734905 434 IDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPES 499
Cdd:cd17651 382 WLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEA 447
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
58-512 |
1.93e-36 |
|
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: 141.86 E-value: 1.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 58 DAATDHRISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSN 137
Cdd:cd05970 41 DAGEERIFTFAELADYSDKTAN-FFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESAD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 138 PKLafttpelapkIASSGISIVLERVEDTL----RVPRGLKVVGNLTE--------MMKKEPSGQAVRNQVHK--DDTAM 203
Cdd:cd05970 120 IKM----------IVAIAEDNIPEEIEKAApecpSKPKLVWVGDPVPEgwidfrklIKNASPDFERPTANSYPcgEDILL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 204 LLYSSGTTGRSKGVNSSHGNLIAHvaryiaepfeqpqqtfICTVPLFHTF--GLLNFVLATLALGTT------------- 268
Cdd:cd05970 190 VYFSSGTTGMPKMVEHDFTYPLGH----------------IVTAKYWQNVreGGLHLTVADTGWGKAvwgkiygqwiaga 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 269 ---VVILPRFDLGEMMAAVEKYRATTLIlVPPVLVTMINKADqiMKKYDVSFLRTVRCGGAPLSKEVTQGFmKKYPTVDV 345
Cdd:cd05970 254 avfVYDYDKFDPKALLEKLSKYGVTTFC-APPTIYRFLIRED--LSRYDLSSLRYCTTAGEALNPEVFNTF-KEKTGIKL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 346 YQGYALTESNGAGASIESVEEsrRYGAVGLLSCGVEARIVDPNtGQVMGLNQTGELWL---KGPSIA--KGYFRNEEEii 420
Cdd:cd05970 330 MEGFGQTETTLTIATFPWMEP--KPGSMGKPAPGYEIDLIDRE-GRSCEAGEEGEIVIrtsKGKPVGlfGGYYKDAEK-- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 421 TSEGW----LKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVA-- 494
Cdd:cd05970 405 TAEVWhdgyYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVla 484
|
490 500
....*....|....*....|
gi 1063734905 495 --RKPESNLcEKKVIDFISK 512
Cdd:cd05970 485 kgYEPSEEL-KKELQDHVKK 503
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
62-494 |
2.96e-36 |
|
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: 143.84 E-value: 2.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 62 DHRISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAV---LTTANPlntASEILRQIADSNP 138
Cdd:COG1020 499 DQSLTYAELNARANRLAH-HLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAyvpLDPAYP---AERLAYMLEDAGA 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 139 KLAFTTPELAPKIASSGISIVLErveDTLRVPRGlkvvgnltemmkkepSGQAVRNQVHKDDTAMLLYSSGTTGRSKGVN 218
Cdd:COG1020 575 RLVLTQSALAARLPELGVPVLAL---DALALAAE---------------PATNPPVPVTPDDLAYVIYTSGSTGRPKGVM 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 219 SSHGNLIAHVArYIAEPFEQPQQTficTVPLFHTFGllnF------VLATLALGTTVVILP---RFDLGEMMAAVEKYRA 289
Cdd:COG1020 637 VEHRALVNLLA-WMQRRYGLGPGD---RVLQFASLS---FdasvweIFGALLSGATLVLAPpeaRRDPAALAELLARHRV 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 290 TTLILVPPVLVTMINKADQimkkyDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVDVYQGYALTEsNGAGASIESVEESRR 369
Cdd:COG1020 710 TVLNLTPSLLRALLDAAPE-----ALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTE-TTVDSTYYEVTPPDA 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 370 YGA---VGL-LScGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEEeiITSE----------G--WLKTGDLCY 433
Cdd:COG1020 784 DGGsvpIGRpIA-NTRVYVLDAH-LQPVPVGVPGELYIGGAGLARGYLNRPE--LTAErfvadpfgfpGarLYRTGDLAR 859
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063734905 434 IDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVA 494
Cdd:COG1020 860 WLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVV 920
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
31-513 |
4.99e-36 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 141.31 E-value: 4.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 31 LALPSKESLDIT--TFI--SSQTYRGKTAFIDAATdhRISFSDLWMAVDRVADCLLhDVGIRRGDVVLVLSPNTISIPIV 106
Cdd:PLN03102 4 LALCEANNVPLTpiTFLkrASECYPNRTSIIYGKT--RFTWPQTYDRCCRLAASLI-SLNITKNDVVSVLAPNTPAMYEM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 107 CLSVMSLGAVLttaNPLNT---ASEILRQIADSNPKLAFTTPELAP------KIASSGIS------IVLERVEDTLRVPR 171
Cdd:PLN03102 81 HFAVPMAGAVL---NPINTrldATSIAAILRHAKPKILFVDRSFEPlarevlHLLSSEDSnlnlpvIFIHEIDFPKRPSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 172 GLKVVGNLTEMMKKEPSGQAVRNQVHKD-DTAMLLYSSGTTGRSKGVNSSH-GNLIAHVARYIA-EPFEQPqqTFICTVP 248
Cdd:PLN03102 158 EELDYECLIQRGEPTPSLVARMFRIQDEhDPISLNYTSGTTADPKGVVISHrGAYLSTLSAIIGwEMGTCP--VYLWTLP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 249 LFHTFGLlNFVLATLALGTTVVILPRFDLGEMMAAVEKYRATTLILVPPVLVTMI--NKADQIMKKYDVSFLrtvrCGGA 326
Cdd:PLN03102 236 MFHCNGW-TFTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLkgNSLDLSPRSGPVHVL----TGGS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 327 P----LSKEVTQ-GFmkkyptvDVYQGYALTESNGAGASIE------------SVEESRRYGAVGLLSCGVEARIVD--- 386
Cdd:PLN03102 311 PppaaLVKKVQRlGF-------QVMHAYGLTEATGPVLFCEwqdewnrlpenqQMELKARQGVSILGLADVDVKNKEtqe 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 387 --PNTGQVMGlnqtgELWLKGPSIAKGYFRNEEEiiTSE----GWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPA 460
Cdd:PLN03102 384 svPRDGKTMG-----EIVIKGSSIMKGYLKNPKA--TSEafkhGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSV 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1063734905 461 ELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKVIDFISKQ 513
Cdd:PLN03102 457 EVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKLVTRE 509
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
198-507 |
7.51e-36 |
|
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: 139.66 E-value: 7.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 198 KDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVA--RYIAEPFEQPQQTFICTVPLFHTFGL--LNFVL---ATLALGTTVV 270
Cdd:cd17639 87 PDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAglGDRVPELLGPDDRYLAYLPLAHIFELaaENVCLyrgGTIGYGSPRT 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 271 IL------PRFDLGEmmaavekYRATTLILVPPVLVTM-------INKADQIMKK----------------YDVSF---- 317
Cdd:cd17639 167 LTdkskrgCKGDLTE-------FKPTLMVGVPAIWDTIrkgvlakLNPMGGLKRTlfwtayqsklkalkegPGTPLldel 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 318 ------------LRTVRCGGAPLSKEvTQGFMKKYpTVDVYQGYALTESNGAGASIESveESRRYGAVGLLSCGVEARIV 385
Cdd:cd17639 240 vfkkvraalggrLRYMLSGGAPLSAD-TQEFLNIV-LCPVIQGYGLTETCAGGTVQDP--GDLETGRVGPPLPCCEIKLV 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 386 D-PNTGQVM-GLNQTGELWLKGPSIAKGYFRNEE---EIITSEGWLKTGDLCYIDNDGFLFIVDRLKELIKYK-GYQVPP 459
Cdd:cd17639 316 DwEEGGYSTdKPPPRGEILIRGPNVFKGYYKNPEktkEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIAL 395
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063734905 460 AELEALLLNHPDILDAAVIPFPDKeagQFPMAYV----------ARK---PES---NLCEKKVI 507
Cdd:cd17639 396 EKLESIYRSNPLVNNICVYADPDK---SYPVAIVvpnekhltklAEKhgvINSeweELCEDKKL 456
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
45-514 |
1.00e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 139.75 E-value: 1.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 45 ISSQTYRGKTAFIDaaTDHRISFSDLWMAVDRVADCLLHDvGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLN 124
Cdd:PRK13383 43 VTAARWPGRTAIID--DDGALSYRELQRATESLARRLTRD-GVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 125 TASEILRQIADSNPKLAFTTPELAPKIASSGISI-VLERVEDTLRVPRGLKVVGnltemmkkePSGQAVrnqvhkddtam 203
Cdd:PRK13383 120 RSDALAAALRAHHISTVVADNEFAERIAGADDAVaVIDPATAGAEESGGRPAVA---------APGRIV----------- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 204 lLYSSGTTGRSKGV------NSSHGNLIAHVARYIAepfeQPQQTFICTVPLFHTFGLLNFVLaTLALGTTVVILPRFDL 277
Cdd:PRK13383 180 -LLTSGTTGKPKGVprapqlRSAVGVWVTILDRTRL----RTGSRISVAMPMFHGLGLGMLML-TIALGGTVLTHRHFDA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 278 GEMMAAVEKYRATTLILVPPVLVTMINKADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVdVYQGYALTESnGA 357
Cdd:PRK13383 254 EAALAQASLHRADAFTAVPVVLARILELPPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDI-LYNGYGSTEV-GI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 358 GASIESVEESRRYGAVGLLSCGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEEEIITsEGWLKTGDLCYIDND 437
Cdd:PRK13383 332 GALATPADLRDAPETVGKPVAGCPVRILDRN-NRPVGPRVTGRIFVGGELAGTRYTDGGGKAVV-DGMTSTGDMGYLDNA 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063734905 438 GFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKVIDFISKQV 514
Cdd:PRK13383 410 GRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRV 486
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
62-513 |
6.07e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 136.66 E-value: 6.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 62 DHRISFSDLWMAVDRVADcllhdvGIRRGDVVLVLSPNTISipiVCLSVmsLGAVL--TTANPLNtaseilrqiADSNPK 139
Cdd:PRK07787 23 GRVLSRSDLAGAATAVAE------RVAGARRVAVLATPTLA---TVLAV--VGALIagVPVVPVP---------PDSGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 140 lafttpELAPKIASSGISIVLERVEDTL----RVPRGLKVVGNLTEmmkKEPSGQAvrnqvhkddTAMLLYSSGTTGRSK 215
Cdd:PRK07787 83 ------ERRHILADSGAQAWLGPAPDDPaglpHVPVRLHARSWHRY---PEPDPDA---------PALIVYTSGTTGPPK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 216 GVNSSHgNLIAHVARYIAEPFE-QPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPRFDlGEMMAAVEKYRATTLIL 294
Cdd:PRK07787 145 GVVLSR-RAIAADLDALAEAWQwTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPT-PEAYAQALSEGGTLYFG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 295 VPpvlvTMINK--ADQIMKKYdvsfLRTVR---CGGAPLSKEVTQGFmKKYPTVDVYQGYALTES---NGAGASIEsvee 366
Cdd:PRK07787 223 VP----TVWSRiaADPEAARA----LRGARllvSGSAALPVPVFDRL-AALTGHRPVERYGMTETlitLSTRADGE---- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 367 sRRYGAVGLLSCGVEARIVDPNTGQVMGLNQT-GELWLKGPSIAKGYFRNEE---EIITSEGWLKTGDLCYIDNDGFLFI 442
Cdd:PRK07787 290 -RRPGWVGLPLAGVETRLVDEDGGPVPHDGETvGELQVRGPTLFDGYLNRPDataAAFTADGWFRTGDVAVVDPDGMHRI 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063734905 443 VDRLK-ELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNlcEKKVIDFISKQ 513
Cdd:PRK07787 369 VGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVA--ADELIDFVAQQ 438
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
206-493 |
2.72e-34 |
|
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: 131.37 E-value: 2.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 206 YSSGTTGRSKGVNSSHGNLIAhvaryiaepfeqpqqTFICTV---------------PLFHTfGLLNFVLATLALGTTVV 270
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIE---------------SFVCNEdlfnisgedailapgPLSHS-LFLYGAISALYLGGTFI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 271 ILPRFDLGEMMAAVEKYRATTLILVPPVLvtminkaDQIMKKYD-VSFLRTVRCGGAPLSKEVTQGFMKKYPTVDVYQGY 349
Cdd:cd17633 71 GQRKFNPKSWIRKINQYNATVIYLVPTML-------QALARTLEpESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 350 ALTESNGAGASieSVEESRRYGAVGLLSCGVEARIVDPNTGQVmglnqtGELWLKGPSIAKGYFRneEEIITSEGWLKTG 429
Cdd:cd17633 144 GTSELSFITYN--FNQESRPPNSVGRPFPNVEIEIRNADGGEI------GKIFVKSEMVFSGYVR--GGFSNPDGWMSVG 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063734905 430 DLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYV 493
Cdd:cd17633 214 DIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALY 277
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
200-506 |
4.19e-34 |
|
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: 131.61 E-value: 4.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 200 DTAMLLYSSGTTGRSKGVNSSHGNLIAHVARYIAEPFEQP-QQTFICTVPLFHTFGLLNFVLATLALGTTVVILPRFDLG 278
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVvGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 279 EMMAAVEKYRATTLILVPPV---LVTMINKADQIMKKydvsfLRTVRCGGA-PLSKEVTqgFMKKYPTVDVYQGYALTES 354
Cdd:cd17635 82 SLFKILTTNAVTTTCLVPTLlskLVSELKSANATVPS-----LRLIGYGGSrAIAADVR--FIEATGLTNTAQVYGLSET 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 355 nGAGASIESVEESRRYGAVGLLSCGVEARIVDpNTGQVMGLNQTGELWLKGPSIAKGYFRNEEEI--ITSEGWLKTGDLC 432
Cdd:cd17635 155 -GTALCLPTDDDSIEINAVGRPYPGVDVYLAA-TDGIAGPSASFGTIWIKSPANMLGYWNNPERTaeVLIDGWVNTGDLG 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063734905 433 YIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPEsnLCEKKV 506
Cdd:cd17635 233 ERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAE--LDENAI 304
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
43-509 |
9.10e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 134.30 E-value: 9.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 43 TFI--SSQTYRGKTAFIDAATdhRISFSDLWMAVDRVADCLLHdVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLtta 120
Cdd:PRK08162 22 SFLerAAEVYPDRPAVIHGDR--RRTWAETYARCRRLASALAR-RGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVL--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 121 NPLNT---ASEILRQIADSNPKLAFTTPELAPkiassgisiVLERVEDTLRVPRGLKVVGNLTEMMKKEPSG----QAVR 193
Cdd:PRK08162 96 NTLNTrldAASIAFMLRHGEAKVLIVDTEFAE---------VAREALALLPGPKPLVIDVDDPEYPGGRFIGaldyEAFL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 194 NQVHKD----------DTAMLLYSSGTTGRSKGVNSSH-GNLIAHVARYIAepFEQPQQ-TFICTVPLFHTFGLLnFVLA 261
Cdd:PRK08162 167 ASGDPDfawtlpadewDAIALNYTSGTTGNPKGVVYHHrGAYLNALSNILA--WGMPKHpVYLWTLPMFHCNGWC-FPWT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 262 TLALGTTVVILPRFDLGEMMAAVEKYRATTLILVPPVLVTMINKADQIMKKYD--VSFLrtvrCGGAPLSKEVTQGfMKK 339
Cdd:PRK08162 244 VAARAGTNVCLRKVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDhpVHAM----VAGAAPPAAVIAK-MEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 340 YpTVDVYQGYALTESNGAgASI-------------ESVEESRRYGAVGLLSCGVeaRIVDPNTGQ-VMGLNQT-GELWLK 404
Cdd:PRK08162 319 I-GFDLTHVYGLTETYGP-ATVcawqpewdalpldERAQLKARQGVRYPLQEGV--TVLDPDTMQpVPADGETiGEIMFR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 405 GPSIAKGYFRNEEEiiTSE----GWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPF 480
Cdd:PRK08162 395 GNIVMKGYLKNPKA--TEEafagGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAK 472
|
490 500
....*....|....*....|....*....
gi 1063734905 481 PDKEAGQFPMAYVARKPESNLCEKKVIDF 509
Cdd:PRK08162 473 PDPKWGEVPCAFVELKDGASATEEEIIAH 501
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
54-478 |
2.02e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 133.33 E-value: 2.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 54 TAFIDAATDhrISFSDLWMAVDRVAdCLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQI 133
Cdd:PRK06164 27 VALIDEDRP--LSRAELRALVDRLA-AWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHIL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 134 ADSNPKLAFttpeLAPKIASSGISIVLERVEDTLRVP-RGLKVVGN---------------LTEMMKKEPSGQAVRNQVH 197
Cdd:PRK06164 104 GRGRARWLV----VWPGFKGIDFAAILAAVPPDALPPlRAIAVVDDaadatpapapgarvqLFALPDPAPPAAAGERAAD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 198 KDDTAMLLYSSGTTGRSKGVNSSHGNLIAHvARYIAEPFE-QPQQTFICTVPLFHTFGLlNFVLATLALGTTVVILPRFD 276
Cdd:PRK06164 180 PDAGALLFTTSGTTSGPKLVLHRQATLLRH-ARAIARAYGyDPGAVLLAALPFCGVFGF-STLLGALAGGAPLVCEPVFD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 277 LGEMMAAVEKYRATTLILVPPVLVTMINKADQimkKYDVSFLRtvRCGGA---PLSKEV-----TQGFmkkyPTVDVY-- 346
Cdd:PRK06164 258 AARTARALRRHRVTHTFGNDEMLRRILDTAGE---RADFPSAR--LFGFAsfaPALGELaalarARGV----PLTGLYgs 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 347 -QGYALTesngAGASIESVEESRRYGAVGLLSCGVEARIVDPNTGQVMGLNQTGELWLKGPSIAKGYFRNEE---EIITS 422
Cdd:PRK06164 329 sEVQALV----ALQPATDPVSVRIEGGGRPASPEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDataRALTD 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063734905 423 EGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVI 478
Cdd:PRK06164 405 DGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVV 460
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
74-493 |
2.78e-33 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 133.00 E-value: 2.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 74 VDRV---ADCLLHdVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTtanPLN------TASEILRQIADSNPKLAFTT 144
Cdd:PLN02860 39 VDGVlslAAGLLR-LGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVA---PLNyrwsfeEAKSAMLLVRPVMLVTDETC 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 145 PELAPKIASSGISIVLERV---EDTLRVPRGLKVVGNlTEMMKKEPSGQAVRNQV-HKDDTAMLLYSSGTTGRSKGVNSS 220
Cdd:PLN02860 115 SSWYEELQNDRLPSLMWQVfleSPSSSVFIFLNSFLT-TEMLKQRALGTTELDYAwAPDDAVLICFTSGTTGRPKGVTIS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 221 HGNLIAHVARYIAEPFEQPQQTFICTVPLFHtFGLLNFVLATLALGTTVVILPRFDLGEMMAAVEKYRATTLILVPPVLV 300
Cdd:PLN02860 194 HSALIVQSLAKIAIVGYGEDDVYLHTAPLCH-IGGLSSALAMLMVGACHVLLPKFDAKAALQAIKQHNVTSMITVPAMMA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 301 TMINKADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVDVYQGYALTES------------NGAGASIESVEESR 368
Cdd:PLN02860 273 DLISLTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEAcssltfmtlhdpTLESPKQTLQTVNQ 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 369 RYGAVGLLSCG---------VEARIVDPNTGQVmglnqtGELWLKGPSIAKGYFRN---EEEIITSEGWLKTGDLCYIDN 436
Cdd:PLN02860 353 TKSSSVHQPQGvcvgkpaphVELKIGLDESSRV------GRILTRGPHVMLGYWGQnseTASVLSNDGWLDTGDIGWIDK 426
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063734905 437 DGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYV 493
Cdd:PLN02860 427 AGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACV 483
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
59-493 |
4.67e-33 |
|
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: 131.63 E-value: 4.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 59 AATDHRISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNP 138
Cdd:cd17646 18 VDEGRTLTYRELDERANRLAH-LLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 139 KLAFTTPELAPKIASSGISIVLERVEDTLRVPRGLKVVgnltemmkkepsgqavrnqVHKDDTAMLLYSSGTTGRSKGVn 218
Cdd:cd17646 97 AVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLVP-------------------PRPDNLAYVIYTSGSTGRPKGV- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 219 sshgnLIAHVAryIAEPFEQPQQTFICT---VPLFHT-FGL---LNFVLATLALGTTVVILP---RFDLGEMMAAVEKYR 288
Cdd:cd17646 157 -----MVTHAG--IVNRLLWMQDEYPLGpgdRVLQKTpLSFdvsVWELFWPLVAGARLVVARpggHRDPAYLAALIREHG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 289 ATTLILVPPVLVTMINKADqimkKYDVSFLRTVRCGGAPLSKEVTQGFMKKyPTVDVYQGYALTEsngagASIESV---- 364
Cdd:cd17646 230 VTTCHFVPSMLRVFLAEPA----AGSCASLRRVFCSGEALPPELAARFLAL-PGAELHNLYGPTE-----AAIDVThwpv 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 365 --EESRRYGAVGLLSCGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEEEiiTSEGWL-----------KTGDL 431
Cdd:cd17646 300 rgPAETPSVPIGRPVPNTRLYVLDDA-LRPVPVGVPGELYLGGVQLARGYLGRPAL--TAERFVpdpfgpgsrmyRTGDL 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063734905 432 CYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYV 493
Cdd:cd17646 377 ARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYV 438
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
200-508 |
5.47e-33 |
|
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: 128.19 E-value: 5.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 200 DTAMLLYSSGTTGRSKGVNSSHGNLIAH--VARYIAEPFEQPqqTFICTVPLFHtFGLLNFVLATLALGTTVVILPRFDL 277
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQalVLAVLQAIDEGT--VFLNSGPLFH-IGTLMFTLATFHAGGTNVFVRRVDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 278 GEMMAAVEKYRATTLILVPPVLvtminkaDQIMK-----KYDVSFLRTVRcgGAPLSKEV----TQGFMKKYPtvdvyqG 348
Cdd:cd17636 78 EEVLELIEAERCTHAFLLPPTI-------DQIVElnadgLYDLSSLRSSP--AAPEWNDMatvdTSPWGRKPG------G 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 349 YALTESNG----AGASIESVeesrryGAVGLLSCGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEEEII--TS 422
Cdd:cd17636 143 YGQTEVMGlatfAALGGGAI------GGAGRPSPLVQVRILDED-GREVPDGEVGEIVARGPTVMAGYWNRPEVNArrTR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 423 EGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLC 502
Cdd:cd17636 216 GGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVT 295
|
....*.
gi 1063734905 503 EKKVID 508
Cdd:cd17636 296 EAELIE 301
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
154-510 |
6.99e-33 |
|
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: 131.57 E-value: 6.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 154 SGISIVLervedtlrVPRGLKVVgNLTEMMKKEPSGQAVRNQVHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVARYIA 233
Cdd:cd05927 78 AEISIVF--------CDAGVKVY-SLEEFEKLGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 234 EPFEQ----PQQTFICTVPLFHTFGLLNfVLATLALGTTVVILpRFDLGEMMAAVEKYRATTLILVP------------- 296
Cdd:cd05927 149 ILEILnkinPTDVYISYLPLAHIFERVV-EALFLYHGAKIGFY-SGDIRLLLDDIKALKPTVFPGVPrvlnriydkifnk 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 297 -----PVLVTMINKA-------------------DQIM-KKYDVSFLRTVR---CGGAPLSKEVTQgFMKKYPTVDVYQG 348
Cdd:cd05927 227 vqakgPLKRKLFNFAlnyklaelrsgvvraspfwDKLVfNKIKQALGGNVRlmlTGSAPLSPEVLE-FLRVALGCPVLEG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 349 YALTESNGAGASieSVEESRRYGAVG-LLSCgVEARIVD-PNTG-QVMGLNQTGELWLKGPSIAKGYFRNEE---EIITS 422
Cdd:cd05927 306 YGQTECTAGATL--TLPGDTSVGHVGgPLPC-AEVKLVDvPEMNyDAKDPNPRGEVCIRGPNVFSGYYKDPEktaEALDE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 423 EGWLKTGDLCYIDNDGFLFIVDRLKELIKY-KGYQVPPAELEALLLNHPDI-------------LDAAVIPFPD------ 482
Cdd:cd05927 383 DGWLHTGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSPFVaqifvygdslksfLVAIVVPDPDvlkewa 462
|
410 420
....*....|....*....|....*....
gi 1063734905 483 KEAGQFPMAYvarkpeSNLCE-KKVIDFI 510
Cdd:cd05927 463 ASKGGGTGSF------EELCKnPEVKKAI 485
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
61-514 |
1.34e-32 |
|
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: 131.67 E-value: 1.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 61 TDHRISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPntiSIP---IVCLSVMSLGAVLTTANPLNTASEILRQIADSN 137
Cdd:cd05967 79 TERTYTYAELLDEVSRLAG-VLRKLGVVKGDRVIIYMP---MIPeaaIAMLACARIGAIHSVVFGGFAAKELASRIDDAK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 138 PKLAFT-------------TPELAPKIASSGIS----IVLERVEDTLRVPRGLKVVGNLTEMMKKEPSGQAvrnQVHKDD 200
Cdd:cd05967 155 PKLIVTascgiepgkvvpyKPLLDKALELSGHKphhvLVLNRPQVPADLTKPGRDLDWSELLAKAEPVDCV---PVAATD 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 201 TAMLLYSSGTTGRSKGV---NSSHGNLIAHVARYIAEPfeQPQQTFICTVPLFHTFGLLNFVLATLALGTTVVIL----- 272
Cdd:cd05967 232 PLYILYTSGTTGKPKGVvrdNGGHAVALNWSMRNIYGI--KPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYegkpv 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 273 --PrfDLGEMMAAVEKYRATTLILVPPVLvTMINKAD---QIMKKYDVSFLRTVRCGGAPLSKEvTQGFMKKYPTVDVYQ 347
Cdd:cd05967 310 gtP--DPGAFWRVIEKYQVNALFTAPTAI-RAIRKEDpdgKYIKKYDLSSLRTLFLAGERLDPP-TLEWAENTLGVPVID 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 348 GYALTESNGAGASIESVEESR--RYGAVGLLSCGVEARIVDPNtGQVMGLNQTGELWLKGP---SIAKGYFRNEEEIIT- 421
Cdd:cd05967 386 HWWQTETGWPITANPVGLEPLpiKAGSPGKPVPGYQVQVLDED-GEPVGPNELGNIVIKLPlppGCLLTLWKNDERFKKl 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 422 ----SEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKP 497
Cdd:cd05967 465 ylskFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKE 544
|
490
....*....|....*..
gi 1063734905 498 ESNLCEKKVIDFISKQV 514
Cdd:cd05967 545 GVKITAEELEKELVALV 561
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
63-510 |
1.42e-32 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 130.64 E-value: 1.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 63 HRISFSDLWMAVDRVADCLLHDvGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLAF 142
Cdd:PRK06018 38 VRTTYAQIHDRALKVSQALDRD-GIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 143 TTPELAPKIAssGISIVLERVE------DTLRVPRglKVVGNLT--EMMKKEPSGQAVRNQVHKDDTAMLLYSSGTTGRS 214
Cdd:PRK06018 117 TDLTFVPILE--KIADKLPSVEryvvltDAAHMPQ--TTLKNAVayEEWIAEADGDFAWKTFDENTAAGMCYTSGTTGDP 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 215 KGVNSSHGNLIAH--VARYIAEPFEQPQQTFICTVPLFH--TFGLlnfVLATLALGTTVVIL-PRFDLGEMMAAVEKYRA 289
Cdd:PRK06018 193 KGVLYSHRSNVLHalMANNGDALGTSAADTMLPVVPLFHanSWGI---AFSAPSMGTKLVMPgAKLDGASVYELLDTEKV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 290 TTLILVPPVLVTMInkadQIMKKYDVSF--LRTVRCGGAPLSKEVTQGFMKKypTVDVYQGYALTESNGAG--------- 358
Cdd:PRK06018 270 TFTAGVPTVWLMLL----QYMEKEGLKLphLKMVVCGGSAMPRSMIKAFEDM--GVEVRHAWGMTEMSPLGtlaalkppf 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 359 ASIESVEESRRYGAVGLLSCGVEARIVDPNTGQVMGLNQT-GELWLKGPSIAKGYFRNEEEIITSEGWLKTGDLCYIDND 437
Cdd:PRK06018 344 SKLPGDARLDVLQKQGYPPFGVEMKITDDAGKELPWDGKTfGRLKVRGPAVAAAYYRVDGEILDDDGFFDTGDVATIDAY 423
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063734905 438 GFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKVIDFI 510
Cdd:PRK06018 424 GYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEILKYM 496
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
82-514 |
2.87e-32 |
|
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: 129.47 E-value: 2.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 82 LHDVGIRRGDVVLVLSPNtisIPIVC---LSVMSLGAVLTTANPLNTASEILRQIADSNPKLAFTTPELApKIASSGISI 158
Cdd:cd05915 41 LRALGVGVGDRVATLGFN---HFRHLeayFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPNLL-PLVEAIRGE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 159 VLERVEdtlrvprglkvvgNLTEMMKKE----------PSGQAVRnQVHKDDTAMLLYSSGTTGRSKGVNSSH--GNLIA 226
Cdd:cd05915 117 LKTVQH-------------FVVMDEKAPegylayeealGEEADPV-RVPERAACGMAYTTGTTGLPKGVVYSHraLVLHS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 227 HVARYIAEPFEQPQQTFICTVPLFHTFGLLnFVLATLALGTTVVILPRFDLGEMM-AAVEKYRATTLILVPPVLVTMINK 305
Cdd:cd05915 183 LAASLVDGTALSEKDVVLPVVPMFHVNAWC-LPYAATLVGAKQVLPGPRLDPASLvELFDGEGVTFTAGVPTVWLALADY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 306 ADQIMKkydvSFLRTVRCGGAPLSKEVTQGFMKKYPTVDVYQGYALTESNGAGASI------ESV--EESRRYGAVGLLS 377
Cdd:cd05915 262 LESTGH----RLKTLRRLVVGGSAAPRSLIARFERMGVEVRQGYGLTETSPVVVQNfvkshlESLseEEKLTLKAKTGLP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 378 CGVEA-RIVDPNTGQVMGLNQTGE-LWLKGPSIAKGYFRNEEEIITSE---GWLKTGDLCYIDNDGFLFIVDRLKELIKY 452
Cdd:cd05915 338 IPLVRlRVADEEGRPVPKDGKALGeVQLKGPWITGGYYGNEEATRSALtpdGFFRTGDIAVWDEEGYVEIKDRLKDLIKS 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063734905 453 KGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKpESNLCEKKVIDFISKQV 514
Cdd:cd05915 418 GGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPR-GEKPTPEELNEHLLKAG 478
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
50-466 |
4.06e-32 |
|
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: 129.32 E-value: 4.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 50 YRGKTAFIDAATDHRISFSDLWMAVDRVADCLLHDvGIRRGD-VVLVLSPNTISIP----------IVCLSvmSLGAVLT 118
Cdd:cd05906 25 TKGITYIDADGSEEFQSYQDLLEDARRLAAGLRQL-GLRPGDsVILQFDDNEDFIPafwacvlagfVPAPL--TVPPTYD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 119 TANPLNTASEILRQIADSnPKLaFTTPELAPKIAssgisivlervedTLRVPRGLKVVGNLTEMMKKEPSGQAVRNQVHK 198
Cdd:cd05906 102 EPNARLRKLRHIWQLLGS-PVV-LTDAELVAEFA-------------GLETLSGLPGIRVLSIEELLDTAADHDLPQSRP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 199 DDTAMLLYSSGTTGRSKGVNSSHGNLIAHVARYIAEPFEQPQQTFICTVPLFHTFGLLNFVLATLALGT------TVVIL 272
Cdd:cd05906 167 DDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCqqvhvpTEEIL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 273 ---PRF-DLgemmaaVEKYRAtTLILVPPVLVTMINkaDQIMK----KYDVSFLRTVRCGGAPLSKEVTQGFM---KKY- 340
Cdd:cd05906 247 adpLRWlDL------IDRYRV-TITWAPNFAFALLN--DLLEEiedgTWDLSSLRYLVNAGEAVVAKTIRRLLrllEPYg 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 341 --PTVdVYQGYALTESnGAGAsIESV--EESRRYGAVGLLSC-----GVEARIVDPNtGQVMGLNQTGELWLKGPSIAKG 411
Cdd:cd05906 318 lpPDA-IRPAFGMTET-CSGV-IYSRsfPTYDHSQALEFVSLgrpipGVSMRIVDDE-GQLLPEGEVGRLQVRGPVVTKG 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063734905 412 YFRNEE---EIITSEGWLKTGDLCYIDNdGFLFIVDRLKELIKYKGYQVPPAELEALL 466
Cdd:cd05906 394 YYNNPEanaEAFTEDGWFRTGDLGFLDN-GNLTITGRTKDTIIVNGVNYYSHEIEAAV 450
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
48-514 |
4.12e-32 |
|
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: 129.99 E-value: 4.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 48 QTYRGKTAFI----DAATDHRISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPL 123
Cdd:cd05966 64 KERGDKVAIIwegdEPDQSRTITYRELLREVCRFAN-VLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 124 NTASEILRQIADSNPKLAFTTP----------------ELAPKIASSGISIVLERVEDTLRVPRGLKVVGNltEMMKKEP 187
Cdd:cd05966 143 FSAESLADRINDAQCKLVITADggyrggkviplkeivdEALEKCPSVEKVLVVKRTGGEVPMTEGRDLWWH--DLMAKQS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 188 SGQAVRnQVHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVA---RYIaepFE-QPQQTFICTVPLF----HTFGllnfV 259
Cdd:cd05966 221 PECEPE-WMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAAttfKYV---FDyHPDDIYWCTADIGwitgHSYI----V 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 260 LATLALGTTVVIL---PRF-DLGEMMAAVEKYRATTLILVPPVLVTMINKADQIMKKYDVSFLRTVRCGGAPLSKEVTQG 335
Cdd:cd05966 293 YGPLANGATTVMFegtPTYpDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMW 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 336 FMK-----KYPTVDVY-QgyalTESNG------AGASiesveeSRRYGAVGLLSCGVEARIVDPNTGQVmGLNQTGELWL 403
Cdd:cd05966 373 YYEvigkeRCPIVDTWwQ----TETGGimitplPGAT------PLKPGSATRPFFGIEPAILDEEGNEV-EGEVEGYLVI 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 404 KG--PSIAKGYFRNEEEIITS-----EGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAA 476
Cdd:cd05966 442 KRpwPGMARTIYGDHERYEDTyfskfPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAA 521
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1063734905 477 VIPFPDKEAGQFPMAYVA----RKPESNLcEKKVIDFISKQV 514
Cdd:cd05966 522 VVGRPHDIKGEAIYAFVTlkdgEEPSDEL-RKELRKHVRKEI 562
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
65-514 |
1.01e-31 |
|
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: 129.15 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 65 ISFSDLWMAVDRVADCLLHdVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTtanPLNT--ASEILR-QIADSNPKLA 141
Cdd:cd05968 92 LTYGELLYEVKRLANGLRA-LGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVV---PIFSgfGKEAAAtRLQDAEAKAL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 142 FTT------------PELAPKIASSGISIVLERVEDTLRVPRGLKVVGNL--TEMMKKEPSGQAvrnQVHKDDTAMLLYS 207
Cdd:cd05968 168 ITAdgftrrgrevnlKEEADKACAQCPTVEKVVVVRHLGNDFTPAKGRDLsyDEEKETAGDGAE---RTESEDPLMIIYT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 208 SGTTGRSKGVNSSHGNLIAHVARYIAEPFEQPQQTficTVPLFHTFGLLN---FVLATLALGTTVVI---LPRFD-LGEM 280
Cdd:cd05968 245 SGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGD---LLTWFTDLGWMMgpwLIFGGLILGATMVLydgAPDHPkADRL 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 281 MAAVEKYRATTLILVPPVLVTMINKADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMK-----KYPTVDvYQGYalTESN 355
Cdd:cd05968 322 WRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFEtvgkgRNPIIN-YSGG--TEIS 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 356 GA---GASIESVEESRRYGAVGllscGVEARIVDPNTGQVMGlnQTGELWLKGP--SIAKGYFRNEEEIITS-----EGW 425
Cdd:cd05968 399 GGilgNVLIKPIKPSSFNGPVP----GMKADVLDESGKPARP--EVGELVLLAPwpGMTRGFWRDEDRYLETywsrfDNV 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 426 LKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKP---ESNLC 502
Cdd:cd05968 473 WVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPgvtPTEAL 552
|
490
....*....|..
gi 1063734905 503 EKKVIDFISKQV 514
Cdd:cd05968 553 AEELMERVADEL 564
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
65-493 |
2.24e-31 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 127.59 E-value: 2.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 65 ISFSDLWMAVDRVADCLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLttaNPLNTA---SEILRQIADSNPKLA 141
Cdd:PRK05620 39 TTFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVF---NPLNKQlmnDQIVHIINHAEDEVI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 142 FTTPELAPKIAS--------SGISIVLERVEDTLRV--PRGLKVVGnlTEMMKKEPSGQAVRNQVHKDDTAMLLYSSGTT 211
Cdd:PRK05620 116 VADPRLAEQLGEilkecpcvRAVVFIGPSDADSAAAhmPEGIKVYS--YEALLDGRSTVYDWPELDETTAAAICYSTGTT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 212 GRSKGVNSSHGNLIAH-VARYIAEPFE-QPQQTFICTVPLFH--TFGLlnfVLATLALGTTVViLPRFDL-GEMMAAVek 286
Cdd:PRK05620 194 GAPKGVVYSHRSLYLQsLSLRTTDSLAvTHGESFLCCVPIYHvlSWGV---PLAAFMSGTPLV-FPGPDLsAPTLAKI-- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 287 yRATTLIL----VPPVLVtminkadQIMKKY-----DVSFLRTVRCGGAPLSKEVTQGFMKKYpTVDVYQGYALTESNG- 356
Cdd:PRK05620 268 -IATAMPRvahgVPTLWI-------QLMVHYlknppERMSLQEIYVGGSAVPPILIKAWEERY-GVDVVHVWGMTETSPv 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 357 -------AGASIESVEESRRygAVGLLSCGVEARIVdpNTGQVMGLN--QTGELWLKGPSIAKGY--------------F 413
Cdd:PRK05620 339 gtvarppSGVSGEARWAYRV--SQGRFPASLEYRIV--NDGQVMESTdrNEGEIQVRGNWVTASYyhspteegggaastF 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 414 RNEE-----EIITSEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQF 488
Cdd:PRK05620 415 RGEDvedanDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGER 494
|
....*
gi 1063734905 489 PMAYV 493
Cdd:PRK05620 495 PLAVT 499
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
62-513 |
2.50e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 126.92 E-value: 2.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 62 DHRISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLA 141
Cdd:PRK07798 26 DRRLTYAELEERANRLAH-YLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 142 FTTPELAPKIASsgisiVLERVEDtLRVprgLKVVGNltemmkkePSGQAVRNQVHKDDTA------------------M 203
Cdd:PRK07798 105 VYEREFAPRVAE-----VLPRLPK-LRT---LVVVED--------GSGNDLLPGAVDYEDAlaagsperdfgerspddlY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 204 LLYSSGTTGRSKGVNSSHGNL-------IAHV-ARYIAEPFEQ-------PQQTFICTVPLFHTFGLLNfVLATLALGTT 268
Cdd:PRK07798 168 LLYTGGTTGMPKGVMWRQEDIfrvllggRDFAtGEPIEDEEELakraaagPGMRRFPAPPLMHGAGQWA-AFAALFSGQT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 269 VVILP--RFDLGEMMAAVEKYRATTLILVPPVLVTMINKADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVDVY 346
Cdd:PRK07798 247 VVLLPdvRFDADEVWRTIEREKVNVITIVGDAMARPLLDALEARGPYDLSSLFAIASGGALFSPSVKEALLELLPNVVLT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 347 QGYALTESnGAGASIESVEESRRYGA--VGLlscGVEARIVDPNTGQVM-GLNQTGelWL-KGPSIAKGYFRNEEE---- 418
Cdd:PRK07798 327 DSIGSSET-GFGGSGTVAKGAVHTGGprFTI---GPRTVVLDEDGNPVEpGSGEIG--WIaRRGHIPLGYYKDPEKtaet 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 419 --IITSEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARK 496
Cdd:PRK07798 401 fpTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLR 480
|
490
....*....|....*..
gi 1063734905 497 PESNLCEKKVIDFISKQ 513
Cdd:PRK07798 481 EGARPDLAELRAHCRSS 497
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
93-513 |
1.07e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 125.18 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 93 VLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLAFTTPELAPKIAS--SGISIVlerVEDTLRvp 170
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGldPGVRVI---NVDSPA-- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 171 rglkvvgnLTEMMKKEPSGQAVRNQVHKDDTAMLLYSSGTTGRSKGVNSSHGNlIAHVARYIAEPFE-QPQQTFICTVPL 249
Cdd:PRK07867 132 --------WADELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRK-VASAGVMLAQRFGlGPDDVCYVSMPL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 250 FHTfgllNFVLA----TLALGTTVVILPRFDLGEMMAAVEKYRATTLILV-PP---VLVT--MINKADqimkkydvSFLR 319
Cdd:PRK07867 203 FHS----NAVMAgwavALAAGASIALRRKFSASGFLPDVRRYGATYANYVgKPlsyVLATpeRPDDAD--------NPLR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 320 TV--RCGGAPLSKEvtqgFMKKYPTVdVYQGYALTEsngAGASIESvEESRRYGAVGLLSCGVEarIVDPNTGQ------ 391
Cdd:PRK07867 271 IVygNEGAPGDIAR----FARRFGCV-VVDGFGSTE---GGVAITR-TPDTPPGALGPLPPGVA--IVDPDTGTecppae 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 392 ------VMGLNQTGELW-LKGPSIAKGYFRNEE---EIItSEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAE 461
Cdd:PRK07867 340 dadgrlLNADEAIGELVnTAGPGGFEGYYNDPEadaERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAP 418
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1063734905 462 LEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKVIDFISKQ 513
Cdd:PRK07867 419 IERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLAAQ 470
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
62-496 |
2.29e-30 |
|
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: 123.56 E-value: 2.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 62 DHRISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTtanPLNTAS--EILRQI-ADSNP 138
Cdd:cd12116 10 DRSLSYAELDERANRLAA-RLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYV---PLDPDYpaDRLRYIlEDAEP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 139 KLAFTTPELAPKIAssGISIVLERVEDTLRVPrglkvvgnltemmkkepsGQAVRNQVHKDDTAMLLYSSGTTGRSKGVN 218
Cdd:cd12116 86 ALVLTDDALPDRLP--AGLPVLLLALAAAAAA------------------PAAPRTPVSPDDLAYVIYTSGSTGRPKGVV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 219 SSHGNLIAHVARYIAEPFEQPQQTFIC-TVPLFhTFGLLNFVLATLAlGTTVVILPR---FDLGEMMAAVEKYRATTLIL 294
Cdd:cd12116 146 VSHRNLVNFLHSMRERLGLGPGDRLLAvTTYAF-DISLLELLLPLLA-GARVVIAPRetqRDPEALARLIEAHSITVMQA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 295 VPPVLvtminkadQIMKKYDVSFLRTVR--CGGAPLSKEVTQGFMKKypTVDVYQGYALTESNgAGASIESVEESRRYGA 372
Cdd:cd12116 224 TPATW--------RMLLDAGWQGRAGLTalCGGEALPPDLAARLLSR--VGSLWNLYGPTETT-IWSTAARVTAAAGPIP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 373 VGLLSCGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEEeiITSEG------------WLKTGDLCYIDNDGFL 440
Cdd:cd12116 293 IGRPLANTQVYVLDAA-LRPVPPGVPGELYIGGDGVAQGYLGRPA--LTAERfvpdpfagpgsrLYRTGDLVRRRADGRL 369
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063734905 441 FIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFpMAYVARK 496
Cdd:cd12116 370 EYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRL-VAYVVLK 424
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
65-493 |
3.72e-30 |
|
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: 122.29 E-value: 3.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 65 ISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEiLRQiadsnpklaftt 144
Cdd:cd05974 1 VSFAEMSARSSRVAN-FLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDD-LRD------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 145 pelapkiassgisivlervedtlRVPRGLKVVGnltemmkkepsgqAVRNQVHKDDTAMLLYSSGTTGRSKGVNSSHGNL 224
Cdd:cd05974 67 -----------------------RVDRGGAVYA-------------AVDENTHADDPMLLYFTSGTTSKPKLVEHTHRSY 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 225 -IAHVARYIAEPFEQPQQTFICTVPLFHTFGLLNFvLATLALGTTVVIL--PRFDLGEMMAAVEKYRATTLIlVPPVLVT 301
Cdd:cd05974 111 pVGHLSTMYWIGLKPGDVHWNISSPGWAKHAWSCF-FAPWNAGATVFLFnyARFDAKRVLAALVRYGVTTLC-APPTVWR 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 302 MINKADqiMKKYDVSfLRTVRCGGAPLSKEVTQGFMKKYpTVDVYQGYALTE-----SNGAGASIESveesrryGAVGLL 376
Cdd:cd05974 189 MLIQQD--LASFDVK-LREVVGAGEPLNPEVIEQVRRAW-GLTIRDGYGQTEttalvGNSPGQPVKA-------GSMGRP 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 377 SCGVEARIVDPNTGQVmglnQTGELWL-----KGPSIAKGYFRNEEEI--ITSEGWLKTGDLCYIDNDGFLFIVDRLKEL 449
Cdd:cd05974 258 LPGYRVALLDPDGAPA----TEGEVALdlgdtRPVGLMKGYAGDPDKTahAMRGGYYRTGDIAMRDEDGYLTYVGRADDV 333
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1063734905 450 IKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYV 493
Cdd:cd05974 334 FKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFI 377
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
62-498 |
2.28e-29 |
|
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: 120.77 E-value: 2.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 62 DHRISFSDLWMAVDRVADCLLHDvGIRRGDVVLVLSPNTISIPIVCLSVMSLGAV---LTTANPLNTASEILrqiADSNP 138
Cdd:cd12117 20 DRSLTYAELNERANRLARRLRAA-GVGPGDVVGVLAERSPELVVALLAVLKAGAAyvpLDPELPAERLAFML---ADAGA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 139 KLAFTTPELApkiassgisivlerVEDTLRVPRGLKVVGNLTEmmkkepSGQAVRNQVHKDDTAMLLYSSGTTGRSKGVN 218
Cdd:cd12117 96 KVLLTDRSLA--------------GRAGGLEVAVVIDEALDAG------PAGNPAVPVSPDDLAYVMYTSGSTGRPKGVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 219 SSHGNLI--AHVARYIAEpfeQPQQTFICTVPL------FHTFG-LLNfvlatlalGTTVVILPR---FDLGEMMAAVEK 286
Cdd:cd12117 156 VTHRGVVrlVKNTNYVTL---GPDDRVLQTSPLafdastFEIWGaLLN--------GARLVLAPKgtlLDPDALGALIAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 287 YRATTLILVPPVLVTMinkADQimkkyDVSFLRTVRC---GGAPLSKEVTQGFMKKYPTVDVYQGYALTESNGAGASIES 363
Cdd:cd12117 225 EGVTVLWLTAALFNQL---ADE-----DPECFAGLRElltGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 364 VEESRRYGAV--GLLSCGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEEEiiTSEG-----------WLKTGD 430
Cdd:cd12117 297 TELDEVAGSIpiGRPIANTRVYVLDED-GRPVPPGVPGELYVGGDGLALGYLNRPAL--TAERfvadpfgpgerLYRTGD 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063734905 431 LCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPE 498
Cdd:cd12117 374 LARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGA 441
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
81-498 |
5.25e-29 |
|
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: 119.74 E-value: 5.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 81 LLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAV---LTTANPLNTASEILRqiaDSNPKLAFTTPELAPKIASSGIS 157
Cdd:cd17655 38 TLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAylpIDPDYPEERIQYILE---DSGADILLTQSHLQPPIAFIGLI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 158 IVLErvEDTLRVPRGlkvvGNLtemmkkEPSGQAvrnqvhkDDTAMLLYSSGTTGRSKGVNSSH---GNLIAHVARYIAe 234
Cdd:cd17655 115 DLLD--EDTIYHEES----ENL------EPVSKS-------DDLAYVIYTSGSTGKPKGVMIEHrgvVNLVEWANKVIY- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 235 pfeQPQQTficTVPLFHTFGLLNFV---LATLALGTTVVILPRFDLGEMMAAVEKYR--ATTLILVPPVLVTMINKADqi 309
Cdd:cd17655 175 ---QGEHL---RVALFASISFDASVteiFASLLSGNTLYIVRKETVLDGQALTQYIRqnRITIIDLTPAHLKLLDAAD-- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 310 mkKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPT-VDVYQGYALTESNgAGASIESVEESRRYGA---VGLLSCGVEARIV 385
Cdd:cd17655 247 --DSEGLSLKHLIVGGEALSTELAKKIIELFGTnPTITNAYGPTETT-VDASIYQYEPETDQQVsvpIGKPLGNTRIYIL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 386 DPNtGQVMGLNQTGELWLKGPSIAKGYFRNEEeiITSEGWL-----------KTGDLCYIDNDGFLFIVDRLKELIKYKG 454
Cdd:cd17655 324 DQY-GRPQPVGVAGELYIGGEGVARGYLNRPE--LTAEKFVddpfvpgermyRTGDLARWLPDGNIEFLGRIDHQVKIRG 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1063734905 455 YQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPE 498
Cdd:cd17655 401 YRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKE 444
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
81-478 |
6.33e-29 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 120.91 E-value: 6.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 81 LLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLAFTTPELAPKIASSGISIVL 160
Cdd:PRK06060 46 VLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRFQPSRVAEAA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 161 ERVEDTLRVprglkvvgnltemmkkEPSGQAVrnqVHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVARYIAEPFE-QP 239
Cdd:PRK06060 126 ELMSEAARV----------------APGGYEP---MGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKALRlTP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 240 QQTFICTVPLFHTFGLLNFVLATLALGTTVVILPrFDLGEMMAAVEKYRattliLVPPVLVTMINKADQIMKKYDVSFLR 319
Cdd:PRK06060 187 EDTGLCSARMYFAYGLGNSVWFPLATGGSAVINS-APVTPEAAAILSAR-----FGPSVLYGVPNFFARVIDSCSPDSFR 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 320 TVRC---GGAPLSKEVTQGFMKKYPTVDVYQGYALTESNGAGASiESVEEsRRYGAVGLLSCGVEARIVDPNtGQVMGLN 396
Cdd:PRK06060 261 SLRCvvsAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTFVS-NRVDE-WRLGTLGRVLPPYEIRVVAPD-GTTAGPG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 397 QTGELWLKGPSIAKGYFRNEEEIITSEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAA 476
Cdd:PRK06060 338 VEGDLWVRGPAIAKGYWNRPDSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAA 417
|
..
gi 1063734905 477 VI 478
Cdd:PRK06060 418 VV 419
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
181-470 |
6.40e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 120.85 E-value: 6.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 181 EMMKKEPSGQAVRNQVHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHV---ARYIAE---PFEqPQQTFICTVPLFHT-- 252
Cdd:PTZ00216 246 AKGHSAGSHHPLNIPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGIlalEDRLNDligPPE-EDETYCSYLPLAHIme 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 253 FGLLNFVLATLAL---GTTVVIL-----PRFDLGEmmaavekYRATTLILVPPVLVTM------------------INKA 306
Cdd:PTZ00216 325 FGVTNIFLARGALigfGSPRTLTdtfarPHGDLTE-------FRPVFLIGVPRIFDTIkkaveaklppvgslkrrvFDHA 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 307 DQ-----IMKKYDVSF----------------LRTVRCGGAPLSkEVTQGFMkkypTV---DVYQGYALTESNGAGA--- 359
Cdd:PTZ00216 398 YQsrlraLKEGKDTPYwnekvfsapravlggrVRAMLSGGGPLS-AATQEFV----NVvfgMVIQGWGLTETVCCGGiqr 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 360 --SIEsveesrrYGAVGLLSCGVEARIVDpntgqVMGLNQT------GELWLKGPSIAKGYFRNEE---EIITSEGWLKT 428
Cdd:PTZ00216 473 tgDLE-------PNAVGQLLKGVEMKLLD-----TEEYKHTdtpeprGEILLRGPFLFKGYYKQEEltrEVLDEDGWFHT 540
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1063734905 429 GDLCYIDNDGFLFIVDRLKELIK-YKGYQVPPAELEALLLNHP 470
Cdd:PTZ00216 541 GDVGSIAANGTLRIIGRVKALAKnCLGEYIALEALEALYGQNE 583
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
55-487 |
1.14e-28 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 120.84 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 55 AFIDAATDH-------------RISFSDLWMAVDRVADCLLHdvGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLT--- 118
Cdd:PRK06814 636 ALIEAAKIHgfkklavedpvngPLTYRKLLTGAFVLGRKLKK--NTPPGENVGVMLPNANGAAVTFFALQSAGRVPAmin 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 119 -TANPLNT-----ASEIlRQIADSNpklAFTTP-ELAPKIA--SSGISIV-LERVEDTLRVprGLKVVGNLTEMMKKEPs 188
Cdd:PRK06814 714 fSAGIANIlsackAAQV-KTVLTSR---AFIEKaRLGPLIEalEFGIRIIyLEDVRAQIGL--ADKIKGLLAGRFPLVY- 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 189 gqavRNQVHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVARYIAE-PFeQPQQTFICTVPLFHTFGLL-NFVLATLAlG 266
Cdd:PRK06814 787 ----FCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARiDF-SPEDKVFNALPVFHSFGLTgGLVLPLLS-G 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 267 TTVVILP-----RFdLGEMMAAVEkyrATTLILVPPVLVTMINKADqimkKYDVSFLRTVRCGGAPLSKEVTQGFMKKYp 341
Cdd:PRK06814 861 VKVFLYPsplhyRI-IPELIYDTN---ATILFGTDTFLNGYARYAH----PYDFRSLRYVFAGAEKVKEETRQTWMEKF- 931
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 342 TVDVYQGYALTESngagASIESVEE--SRRYGAVGLLSCGVEARiVDPntgqVMGLNQTGELWLKGPSIAKGYFRNE--- 416
Cdd:PRK06814 932 GIRILEGYGVTET----APVIALNTpmHNKAGTVGRLLPGIEYR-LEP----VPGIDEGGRLFVRGPNVMLGYLRAEnpg 1002
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063734905 417 --EEIitSEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLN-HPDILDAAViPFPDKEAGQ 487
Cdd:PRK06814 1003 vlEPP--ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAElWPDALHAAV-SIPDARKGE 1073
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
64-498 |
2.06e-28 |
|
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: 118.34 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 64 RISFSDLWMAVDRVADCLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLAFT 143
Cdd:cd05928 41 KWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 144 TPELAPKIASsgISIVLERVEDTLRV-PRGLKVVGNLTEMMKkEPSGQAVRNQVHKDDTAMLLYSSGTTGRSKGVNSSHG 222
Cdd:cd05928 121 SDELAPEVDS--VASECPSLKTKLLVsEKSRDGWLNFKELLN-EASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 223 NL---IAHVARYIAEPfeQPQQTFICTVPLFHTFGLLNFVLATLALGTTVVI--LPRFDLGEMMAAVEKYRATTLILVPP 297
Cdd:cd05928 198 SLglgLKVNGRYWLDL--TASDIMWNTSDTGWIKSAWSSLFEPWIQGACVFVhhLPRFDPLVILKTLSSYPITTFCGAPT 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 298 VLvTMINKADqiMKKYDVSFLRTVRCGGAPLSKEVTQGFmKKYPTVDVYQGYALTES-----NGAGASIESveesrryGA 372
Cdd:cd05928 276 VY-RMLVQQD--LSSYKFPSLQHCVTGGEPLNPEVLEKW-KAQTGLDIYEGYGQTETglicaNFKGMKIKP-------GS 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 373 VGLLSCGVEARIVDPNtGQVMGLNQTGELWLK-GP----SIAKGYFRNEE---EIITSEGWLkTGDLCYIDNDGFLFIVD 444
Cdd:cd05928 345 MGKASPPYDVQIIDDN-GNVLPPGTEGDIGIRvKPirpfGLFSGYVDNPEktaATIRGDFYL-TGDRGIMDEDGYFWFMG 422
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1063734905 445 RLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPE 498
Cdd:cd05928 423 RADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQ 476
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
147-493 |
2.51e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 120.06 E-value: 2.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 147 LAPKIASSGISIVL--ERVEDTLRVPRGLKVVgnLTEMMKKEPSGQAVRN---QVHKDDTAMLLYSSGTTGRSKGVNSSH 221
Cdd:PRK12316 600 LAYMLEDSGVQLLLsqSHLGRKLPLAAGVQVL--DLDRPAAWLEGYSEENpgtELNPENLAYVIYTSGSTGKPKGAGNRH 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 222 GNLIAHVaRYIAEPFEQP-QQTFICTVPLFHTFGLLNFVLaTLALGTTVVILP---RFDLGEMMAAVEKYRATTLILVPP 297
Cdd:PRK12316 678 RALSNRL-CWMQQAYGLGvGDTVLQKTPFSFDVSVWEFFW-PLMSGARLVVAApgdHRDPAKLVELINREGVDTLHFVPS 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 298 VLVTMINKADQImkkyDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVDVYQGYALTESNGAGASIESVEESRRYGAVGLLS 377
Cdd:PRK12316 756 MLQAFLQDEDVA----SCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGGDSVPIGRPI 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 378 CGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFR----NEEEIITS-----EGWLKTGDLCYIDNDGFLFIVDRLKE 448
Cdd:PRK12316 832 ANLACYILDAN-LEPVPVGVLGELYLAGRGLARGYHGrpglTAERFVPSpfvagERMYRTGDLARYRADGVIEYAGRIDH 910
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1063734905 449 LIKYKGYQVPPAELEALLLNHPDILDAAVIpfpdKEAGQFPMAYV 493
Cdd:PRK12316 911 QVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGKQLVGYV 951
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
133-473 |
7.89e-28 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 118.73 E-value: 7.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 133 IADSNPKLAFTTPELAPKIASSGisivlERVEDTLrvPRGLKVvgnltEMMKKEPSGQAVRNQVHKDDTAMLLYSSGTTG 212
Cdd:PRK05691 112 IADAEPRLLLTVADLRDSLLQME-----ELAAANA--PELLCV-----DTLDPALAEAWQEPALQPDDIAFLQYTSGSTA 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 213 RSKGVNSSHGNLIAHvARYIAEPF---EQPQQTFICTVPLFHTFGLLNFVLATLALGTTVVIL-PRFDLGE---MMAAVE 285
Cdd:PRK05691 180 LPKGVQVSHGNLVAN-EQLIRHGFgidLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMsPAYFLERplrWLEAIS 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 286 KYRATtlILVPPVLVTMI---NKADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTV-----DVYQGYALTESN-- 355
Cdd:PRK05691 259 EYGGT--ISGGPDFAYRLcseRVSESALERLDLSRWRVAYSGSEPIRQDSLERFAEKFAACgfdpdSFFASYGLAEATlf 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 356 ------GAGASIESVEE---SRRYGAVG----LLSCGV-----EARIVDPNTGQVMGLNQTGELWLKGPSIAKGYFRNEE 417
Cdd:PRK05691 337 vsggrrGQGIPALELDAealARNRAEPGtgsvLMSCGRsqpghAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPE 416
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063734905 418 E----IITSEG--WLKTGDLCYIdNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDIL 473
Cdd:PRK05691 417 AsaktFVEHDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVV 477
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
158-487 |
1.52e-27 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 116.73 E-value: 1.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 158 IVLERVEDTLRVPRGLKVVGNL----TEMMKKEPsgqavrnqvhkDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVA--RY 231
Cdd:PRK08043 331 VYLEDLKDDVTTADKLWIFAHLlmprLAQVKQQP-----------EDAALILFTSGSEGHPKGVVHSHKSLLANVEqiKT 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 232 IAEpFeQPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPrfdlgemmaAVEKYRattlilVPPVLV----------- 300
Cdd:PRK08043 400 IAD-F-TPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYP---------SPLHYR------IVPELVydrnctvlfgt 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 301 -TMINKADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYpTVDVYQGYALTESngagASIES--VEESRRYGAVGLLS 377
Cdd:PRK08043 463 sTFLGNYARFANPYDFARLRYVVAGAEKLQESTKQLWQDKF-GLRILEGYGVTEC----APVVSinVPMAAKPGTVGRIL 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 378 CGVEARIVdpntgQVMGLNQTGELWLKGPSIAKGYFRNE------------EEIITSEGWLKTGDLCYIDNDGFLFIVDR 445
Cdd:PRK08043 538 PGMDARLL-----SVPGIEQGGRLQLKGPNIMNGYLRVEkpgvlevptaenARGEMERGWYDTGDIVRFDEQGFVQIQGR 612
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1063734905 446 LKELIKYKGYQVPPAELEALLLN-HPDILDAAVIPfPDKEAGQ 487
Cdd:PRK08043 613 AKRFAKIAGEMVSLEMVEQLALGvSPDKQHATAIK-SDASKGE 654
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
62-491 |
2.10e-27 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 116.13 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 62 DHRISFSDLWMAVDRVADCLLhDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVlttANPLNTAseiLRQ------IAD 135
Cdd:PRK08279 60 DQSISYAELNARANRYAHWAA-ARGVGKGDVVALLMENRPEYLAAWLGLAKLGAV---VALLNTQ---QRGavlahsLNL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 136 SNPKLAFTTPELAPKIASSGISIVLERV-----EDTLRVPRGLKvvgNLTEMMKKEPSG-QAVRNQVHKDDTAMLLYSSG 209
Cdd:PRK08279 133 VDAKHLIVGEELVEAFEEARADLARPPRlwvagGDTLDDPEGYE---DLAAAAAGAPTTnPASRSGVTAKDTAFYIYTSG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 210 TTGRSKGVNSSH------GNLIAHVARYiaepfeQPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPRFDLGEMMAA 283
Cdd:PRK08279 210 TTGLPKAAVMSHmrwlkaMGGFGGLLRL------TPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFWDD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 284 VEKYRATT----------LILVPPvlvtminKADQimkkydvsflR--TVRCG-GAPLSKEVTQGFMKKYPTVDVYQGYA 350
Cdd:PRK08279 284 VRRYRATAfqyigelcryLLNQPP-------KPTD----------RdhRLRLMiGNGLRPDIWDEFQQRFGIPRILEFYA 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 351 LTESNGAGASIESVEesrryGAVG--LLSCGVEARIV--DPNTG----------QVMGLNQTGELwlkgpsIAK------ 410
Cdd:PRK08279 347 ASEGNVGFINVFNFD-----GTVGrvPLWLAHPYAIVkyDVDTGepvrdadgrcIKVKPGEVGLL------IGRitdrgp 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 411 --GYFR---NEEEIIT---SEG--WLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAV--- 477
Cdd:PRK08279 416 fdGYTDpeaSEKKILRdvfKKGdaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVygv 495
|
490
....*....|....*
gi 1063734905 478 -IPFPDKEAGqfpMA 491
Cdd:PRK08279 496 eVPGTDGRAG---MA 507
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
114-513 |
8.38e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 113.97 E-value: 8.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 114 GAVLTTANPLNTASEILRQIADSNPKLAFTTPELAPKIASSGISIVLERVEDTLRVPRGLKVVGNLTEMMKKEPsgqavr 193
Cdd:PRK13388 76 GYVLVGLNTTRRGAALAADIRRADCQLLVTDAEHRPLLDGLDLPGVRVLDVDTPAYAELVAAAGALTPHREVDA------ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 194 nqvhkDDTAMLLYSSGTTGRSKGVNSSHGNLiAHVARYIAEPFE-QPQQTFICTVPLFHTfgllNFVLA----TLALGTT 268
Cdd:PRK13388 150 -----MDPFMLIFTSGTTGAPKAVRCSHGRL-AFAGRALTERFGlTRDDVCYVSMPLFHS----NAVMAgwapAVASGAA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 269 VVILPRFDLGEMMAAVEKYRAT---------TLILVPPvlvtmiNKADQIMKKYDVSFlrtvrcgGAPLSKEVTQGFMKK 339
Cdd:PRK13388 220 VALPAKFSASGFLDDVRRYGATyfnyvgkplAYILATP------ERPDDADNPLRVAF-------GNEASPRDIAEFSRR 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 340 YpTVDVYQGYALTEsngaGASIESVEESRRYGAVGLLSCGVEarIVDPNTGQ---VMGLNQTGELW-----------LKG 405
Cdd:PRK13388 287 F-GCQVEDGYGSSE----GAVIVVREPGTPPGSIGRGAPGVA--IYNPETLTecaVARFDAHGALLnadeaigelvnTAG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 406 PSIAKGYFRNEEEiiTSE----GWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFP 481
Cdd:PRK13388 360 AGFFEGYYNNPEA--TAErmrhGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVP 437
|
410 420 430
....*....|....*....|....*....|..
gi 1063734905 482 DKEAGQFPMAYVARKPESNLCEKKVIDFISKQ 513
Cdd:PRK13388 438 DERVGDQVMAALVLRDGATFDPDAFAAFLAAQ 469
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
202-463 |
5.29e-26 |
|
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: 111.68 E-value: 5.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 202 AMLLYSSGTTGRSKGVNSSHGNlIAHVARYIAE-----PFEQPQQTFICTVPLFHTFG-LLNFVLATLALGTTVVILPRF 275
Cdd:cd05933 153 CTLIYTSGTTGMPKGVMLSHDN-ITWTAKAASQhmdlrPATVGQESVVSYLPLSHIAAqILDIWLPIKVGGQVYFAQPDA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 276 DLGEMMAAVEKYRATTLILVPPV-------LVTMINKADQIMKKYDV--------------------------------- 315
Cdd:cd05933 232 LKGTLVKTLREVRPTAFMGVPRVwekiqekMKAVGAKSGTLKRKIASwakgvgletnlklmggespsplfyrlakklvfk 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 316 ---SFLRTVRC-----GGAPLSKEVTQGFMKKYptVDVYQGYALTESngAGASIESVEESRRYGAVGLLSCGVEARIVDP 387
Cdd:cd05933 312 kvrKALGLDRCqkfftGAAPISRETLEFFLSLN--IPIMELYGMSET--SGPHTISNPQAYRLLSCGKALPGCKTKIHNP 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 388 NTgqvmglNQTGELWLKGPSIAKGYFRNE---EEIITSEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQ-VPPAELE 463
Cdd:cd05933 388 DA------DGIGEICFWGRHVFMGYLNMEdktEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGEnVPPVPIE 461
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
200-514 |
1.30e-25 |
|
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: 107.85 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 200 DTAMLLYSSGTTGRSKGVNSSHGNL---IAHVARYIAEPFEQ-----------PQQTFICTVPLFHTFGLLNFVLATLAL 265
Cdd:cd05924 4 DDLYILYTGGTTGMPKGVMWRQEDIfrmLMGGADFGTGEFTPsedahkaaaaaAGTVMFPAPPLMHGTGSWTAFGGLLGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 266 GTTVVILPRFDLGEMMAAVEKYRATTLILVPPVLVTMINKADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVDV 345
Cdd:cd05924 84 QTVVLPDDRFDPEEVWRTIEKHKVTSMTIVGDAMARPLIDALRDAGPYDLSSLFAISSGGALLSPEVKQGLLELVPNITL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 346 YQGYALTES--NGAGASIESVEESRRYGAVGLLSCgvearIVDPNTGQVMGLNQTGELWLKGPSIAKGYFRNEEE----I 419
Cdd:cd05924 164 VDAFGSSETgfTGSGHSAGSGPETGPFTRANPDTV-----VLDDDGRVVPPGSGGVGWIARRGHIPLGYYGDEAKtaetF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 420 ITSEG--WLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKP 497
Cdd:cd05924 239 PEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLRE 318
|
330
....*....|....*..
gi 1063734905 498 ESNLCEKKVIDFISKQV 514
Cdd:cd05924 319 GAGVDLEELREHCRTRI 335
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
82-478 |
1.43e-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: 110.21 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 82 LHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVlttanPLNTaseilrqIADSNPklafttPELAPKIASSGISIVL- 160
Cdd:cd17641 28 LLALGVGRGDVVAILGDNRPEWVWAELAAQAIGAL-----SLGI-------YQDSMA------EEVAYLLNYTGARVVIa 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 161 ---ERVEDTLRV--------------PRGL------------KVVGNLTEMMKKEPS-GQAVRNQVHKDDTAMLLYSSGT 210
Cdd:cd17641 90 edeEQVDKLLEIadripsvryviycdPRGMrkyddprlisfeDVVALGRALDRRDPGlYEREVAAGKGEDVAVLCTTSGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 211 TGRSKGVNSSHGNLIAHVARYIAEPFEQPQQTFICTVPL-------------FHTFGLLNFV--LATL-----ALGTTVV 270
Cdd:cd17641 170 TGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLpwigeqmysvgqaLVCGFIVNFPeePETMmedlrEIGPTFV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 271 IL-PR-----------------------FDLGemMAAVEKYRATTLILVPPVLVTMINK--ADQIMKK-----YDVSFLR 319
Cdd:cd17641 250 LLpPRvwegiaadvrarmmdatpfkrfmFELG--MKLGLRALDRGKRGRPVSLWLRLASwlADALLFRplrdrLGFSRLR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 320 TVRCGGAPLSKEVTQGFMKKypTVDVYQGYALTESngAGASIESVEESRRYGAVGLLSCGVEARIvdpntgqvmglNQTG 399
Cdd:cd17641 328 SAATGGAALGPDTFRFFHAI--GVPLKQLYGQTEL--AGAYTVHRDGDVDPDTVGVPFPGTEVRI-----------DEVG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 400 ELWLKGPSIAKGYFRNEE---EIITSEGWLKTGDLCYIDNDGFLFIVDRLKELIK-YKGYQVPPAELEALLLNHPDILDA 475
Cdd:cd17641 393 EILVRSPGVFVGYYKNPEataEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTtSDGTRFSPQFIENKLKFSPYIAEA 472
|
...
gi 1063734905 476 AVI 478
Cdd:cd17641 473 VVL 475
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
60-499 |
1.51e-25 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 109.55 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 60 ATDHRISFSDLWMAVDRVAdCLLHDVGIRRGDVVLVL---SPNTIsipIVCLSVMSLGAV---LTTANPLNTASEILRqi 133
Cdd:cd05918 20 AWDGSLTYAELDRLSSRLA-HHLRSLGVGPGVFVPLCfekSKWAV---VAMLAVLKAGGAfvpLDPSHPLQRLQEILQ-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 134 aDSNPKLAFTTpelapkiassgisivlervedtlrvprglkvvgnltemmkkepsgqavrnqvHKDDTAMLLYSSGTTGR 213
Cdd:cd05918 94 -DTGAKVVLTS----------------------------------------------------SPSDAAYVIFTSGSTGK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 214 SKGVNSSHGNlIAHVARYIAEPFEQPQQTficTVPLF--HTFGL-LNFVLATLALGTTVVILPRFD-LGEMMAAVEKYRA 289
Cdd:cd05918 121 PKGVVIEHRA-LSTSALAHGRALGLTSES---RVLQFasYTFDVsILEIFTTLAAGGCLCIPSEEDrLNDLAGFINRLRV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 290 TTLILVPPVlvtminkADQIMKKyDVSFLRTVRCGGAPLSKEVTQGFMKKyptVDVYQGYALTES--NGAGASIESVEES 367
Cdd:cd05918 197 TWAFLTPSV-------ARLLDPE-DVPSLRTLVLGGEALTQSDVDTWADR---VRLINAYGPAECtiAATVSPVVPSTDP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 368 RRYGavglLSCGVEARIVDP-NTGQVMGLNQTGELWLKGPSIAKGYFRNEEE----IITSEGWL------------KTGD 430
Cdd:cd05918 266 RNIG----RPLGATCWVVDPdNHDRLVPIGAVGELLIEGPILARGYLNDPEKtaaaFIEDPAWLkqegsgrgrrlyRTGD 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063734905 431 LCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILD---AAVIPFPDKEAGQFPMAYVARKPES 499
Cdd:cd05918 342 LVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKevvVEVVKPKDGSSSPQLVAFVVLDGSS 413
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
53-509 |
2.29e-25 |
|
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: 108.56 E-value: 2.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 53 KTAFIDAatDHRISFSDLWMAVDRVADCLLHDvGIRRGDVVLVLSPNTISIPIVCLSVMSLGAV---LTTANPlntaSEI 129
Cdd:cd12115 15 AIALVCG--DESLTYAELNRRANRLAARLRAA-GVGPESRVGVCLERTPDLVVALLAVLKAGAAyvpLDPAYP----PER 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 130 LRQIA-DSNPKLAFTTPelapkiassgisivlervedtlrvprglkvvgnltemmkkepsgqavrnqvhkDDTAMLLYSS 208
Cdd:cd12115 88 LRFILeDAQARLVLTDP-----------------------------------------------------DDLAYVIYTS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 209 GTTGRSKGVNSSHGNLIAHVaRYIAEPF--EQPQQTFICTVPlfhTFGLLNFVL-ATLALGTTVVILPR-FDLGEMMAAV 284
Cdd:cd12115 115 GSTGRPKGVAIEHRNAAAFL-QWAAAAFsaEELAGVLASTSI---CFDLSVFELfGPLATGGKVVLADNvLALPDLPAAA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 285 EkyraTTLILVPPVLVTMINKADQImkkydVSFLRTVRCGGAPLSKEVTQGFMKKYPTVDVYQGYALTESNGAGASIESV 364
Cdd:cd12115 191 E----VTLINTVPSAAAELLRHDAL-----PASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVP 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 365 EESRRYGAVGLLSCGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEEeiITSEGWL-----------KTGDLCY 433
Cdd:cd12115 262 PGASGEVSIGRPLANTQAYVLDRA-LQPVPLGVPGELYIGGAGVARGYLGRPG--LTAERFLpdpfgpgarlyRTGDLVR 338
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063734905 434 IDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKVIDF 509
Cdd:cd12115 339 WRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRH 414
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
74-472 |
3.06e-25 |
|
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: 108.71 E-value: 3.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 74 VDRVADCLLHdVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPlNTASEILRQIAD-SNPKLAFTT-----PEL 147
Cdd:cd05932 16 ARRLAAALRA-LGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYP-TLNPDTIRYVLEhSESKALFVGklddwKAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 148 APKIASSGISIVLErVEDTLRVPRGLKVVGNltemmKKEPSGQAVRNQvhKDDTAMLLYSSGTTGRSKGVNSSHGNLIAH 227
Cdd:cd05932 94 APGVPEGLISISLP-PPSAANCQYQWDDLIA-----QHPPLEERPTRF--PEQLATLIYTSGTTGQPKGVMLTFGSFAWA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 228 VARYIAEPFEQPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPRFDlgEMMAAVEKYRATTLILVP----------- 296
Cdd:cd05932 166 AQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLD--TFVEDVQRARPTLFFSVPrlwtkfqqgvq 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 297 --------------PVLVTMINKadQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKypTVDVYQGYALTESngAGASIE 362
Cdd:cd05932 244 dkipqqklnlllkiPVVNSLVKR--KVLKGLGLDQCRLAGCGSAPVPPALLEWYRSL--GLNILEAYGMTEN--FAYSHL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 363 SVEESRRYGAVGLLSCGVEARIVDpntgqvmglnqTGELWLKGPSIAKGYFRNEE---EIITSEGWLKTGDLCYIDNDGF 439
Cdd:cd05932 318 NYPGRDKIGTVGNAGPGVEVRISE-----------DGEILVRSPALMMGYYKDPEataEAFTADGFLRTGDKGELDADGN 386
|
410 420 430
....*....|....*....|....*....|....
gi 1063734905 440 LFIVDRLKELIKY-KGYQVPPAELEALLLNHPDI 472
Cdd:cd05932 387 LTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRV 420
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
62-500 |
3.67e-25 |
|
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: 107.72 E-value: 3.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 62 DHRISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLA 141
Cdd:cd17652 10 DETLTYAELNARANRLAR-LLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 142 FTTPelapkiassgisivlervedtlrvprglkvvgnltemmkkepsgqavrnqvhkDDTAMLLYSSGTTGRSKGVNSSH 221
Cdd:cd17652 89 LTTP-----------------------------------------------------DNLAYVIYTSGSTGRPKGVVVTH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 222 GNLIAHVARYIAEPFEQPQQTfictVPLFHTFG----LLNFVLATLAlGTTVVILPRFDL--GEMMAAV-EKYRATTLIL 294
Cdd:cd17652 116 RGLANLAAAQIAAFDVGPGSR----VLQFASPSfdasVWELLMALLA-GATLVLAPAEELlpGEPLADLlREHRITHVTL 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 295 VPPVLVTMinKADQIMKkydvsfLRTVRCGGAPLSKEVTQgfmKKYPTVDVYQGYALTESNgAGASIESVEESRRYGAVG 374
Cdd:cd17652 191 PPAALAAL--PPDDLPD------LRTLVVAGEACPAELVD---RWAPGRRMINAYGPTETT-VCATMAGPLPGGGVPPIG 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 375 LLSCGVEARIVDPNTGQV-MGLnqTGELWLKGPSIAKGYFRNEEeiITSEGWL------------KTGDLCYIDNDGFLF 441
Cdd:cd17652 259 RPVPGTRVYVLDARLRPVpPGV--PGELYIAGAGLARGYLNRPG--LTAERFVadpfgapgsrmyRTGDLARWRADGQLE 334
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063734905 442 IVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESN 500
Cdd:cd17652 335 FLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAA 393
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
58-493 |
4.63e-25 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 109.22 E-value: 4.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 58 DAATDHRISFSDLWMAVDRVADCLLhDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSN 137
Cdd:PLN02654 114 EPGFDASLTYSELLDRVCQLANYLK-DVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 138 PKLAFTTPelAPKIASSGISIVlERVEDTL--RVPRGLKVVGNLT----EMMKKEPS----GQAVRNQ------------ 195
Cdd:PLN02654 193 PKVVITCN--AVKRGPKTINLK-DIVDAALdeSAKNGVSVGICLTyenqLAMKREDTkwqeGRDVWWQdvvpnyptkcev 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 196 --VHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVARYIAEPFE-QPQQTFICTVPL-------FHTFG-LLNfvlatla 264
Cdd:PLN02654 270 ewVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDyKPTDVYWCTADCgwitghsYVTYGpMLN------- 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 265 lGTTVVIL---PRF-DLGEMMAAVEKYRATTLILVPPVLVTMINKADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMK-- 338
Cdd:PLN02654 343 -GATVLVFegaPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNvv 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 339 ---KYPTVDVY-----QGYALTESNGAGasiesveeSRRYGAVGLLSCGVEARIVDPNTGQVMGlNQTGELWLKG--PSI 408
Cdd:PLN02654 422 gdsRCPISDTWwqtetGGFMITPLPGAW--------PQKPGSATFPFFGVQPVIVDEKGKEIEG-ECSGYLCVKKswPGA 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 409 AKGYFRNEEEIITS-----EGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDK 483
Cdd:PLN02654 493 FRTLYGDHERYETTyfkpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHE 572
|
490
....*....|
gi 1063734905 484 EAGQFPMAYV 493
Cdd:PLN02654 573 VKGQGIYAFV 582
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
64-472 |
5.74e-25 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 108.45 E-value: 5.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 64 RISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNtiSIPIVCLSV--MSLGAVLTTANPLNTASEILRQIADSNPKlA 141
Cdd:PRK09274 41 ELSFAELDARSDAIAH-GLNAAGIGRGMRAVLMVTP--SLEFFALTFalFKAGAVPVLVDPGMGIKNLKQCLAEAQPD-A 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 142 FTTPELApKIASsgisIVLERVEDTLRVprgLKVVGN--------LTEMMKKEPSGQAVRNQVHKDDTAMLLYSSGTTGR 213
Cdd:PRK09274 117 FIGIPKA-HLAR----RLFGWGKPSVRR---LVTVGGrllwggttLATLLRDGAAAPFPMADLAPDDMAAILFTSGSTGT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 214 SKGVNSSHGNLIAHV----ARYIAEPFEQPQQTFictvPLFHTFGllnfvlatLALGTTVVIlPRFDLG--------EMM 281
Cdd:PRK09274 189 PKGVVYTHGMFEAQIealrEDYGIEPGEIDLPTF----PLFALFG--------PALGMTSVI-PDMDPTrpatvdpaKLF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 282 AAVEKYRATTLILVPpvlvTMINKADQIMKKYDVSF--LRTVRCGGAPLSKEVTQGFMKKYP-TVDVYQGYALTESNGAg 358
Cdd:PRK09274 256 AAIERYGVTNLFGSP----ALLERLGRYGEANGIKLpsLRRVISAGAPVPIAVIERFRAMLPpDAEILTPYGATEALPI- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 359 ASIESVE---ESRRY---GA---VGLLSCGVEARIVDPNTG--------QVMGLNQTGELWLKGPSIAKGYFRNEEE--- 418
Cdd:PRK09274 331 SSIESREilfATRAAtdnGAgicVGRPVDGVEVRIIAISDApipewddaLRLATGEIGEIVVAGPMVTRSYYNRPEAtrl 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063734905 419 --IITSEG--WLKTGDLCYIDNDGFLFIVDRLKELIKYKG---YQVPpaeLEALLLNHPDI 472
Cdd:PRK09274 411 akIPDGQGdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGgtlYTIP---CERIFNTHPGV 468
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
71-463 |
6.16e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 108.16 E-value: 6.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 71 WMAVDRVADCL---LHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSnpklafttpel 147
Cdd:PRK07768 32 WGEVHERARRIaggLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWAEDT----------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 148 APKIASSGISIVL-----ERVEDTLRvPRGLKVVgNLTEMMKKEPsgqAVRNQVHKDDTAMLLYSSGTTGRSKGVNSSHG 222
Cdd:PRK07768 101 LRVIGMIGAKAVVvgepfLAAAPVLE-EKGIRVL-TVADLLAADP---IDPVETGEDDLALMQLTSGSTGSPKAVQITHG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 223 NLIAHV-ARYIAEPFEQPQQTFICTVPLFHTFGLLNFVLATLALGTTVV-ILPRFDLGE---MMAAVEKYRATtlILVPP 297
Cdd:PRK07768 176 NLYANAeAMFVAAEFDVETDVMVSWLPLFHDMGMVGFLTVPMYFGAELVkVTPMDFLRDpllWAELISKYRGT--MTAAP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 298 -----VLVTMINKADQiMKKYDVSFLRTVRCGGAPLSKEVTQGF--------MKkyPTVdVYQGYALTESN--------G 356
Cdd:PRK07768 254 nfayaLLARRLRRQAK-PGAFDLSSLRFALNGAEPIDPADVEDLldagarfgLR--PEA-ILPAYGMAEATlavsfspcG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 357 AGASIESVE----------------ESRRYGAVGLLSCGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEEEII 420
Cdd:PRK07768 330 AGLVVDEVDadllaalrravpatkgNTRRLATLGPPLPGLEVRVVDED-GQVLPPRGVGVIELRGESVTPGYLTMDGFIP 408
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1063734905 421 TSE--GWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELE 463
Cdd:PRK07768 409 AQDadGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE 453
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
82-514 |
8.80e-25 |
|
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: 8.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 82 LHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLAFTTPELAPKIASSGISIVLE 161
Cdd:cd17656 30 LREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLTQRHLKSKLSFNKSTILLE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 162 RVEDTlrvprglkvvgnltemmkkEPSGQAVRNQVHKDDTAMLLYSSGTTGRSKGVNSSHGNLiahvARYIAEPFEQPQQ 241
Cdd:cd17656 110 DPSIS-------------------QEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNM----VNLLHFEREKTNI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 242 TFICTVPLFHTFGL---LNFVLATLALGTTVVILP---RFDLGEMMAAVEKYRATTLILvPPVLVTMINKadqiMKKYDV 315
Cdd:cd17656 167 NFSDKVLQFATCSFdvcYQEIFSTLLSGGTLYIIReetKRDVEQLFDLVKRHNIEVVFL-PVAFLKFIFS----EREFIN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 316 SFLRTVR---CGGAPL--SKEVTQGFMKKypTVDVYQGYALTESNGAGA-SIESVEESRRYGAVGLLSCGVEARIVDPNt 389
Cdd:cd17656 242 RFPTCVKhiiTAGEQLviTNEFKEMLHEH--NVHLHNHYGPSETHVVTTyTINPEAEIPELPPIGKPISNTWIYILDQE- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 390 GQVMGLNQTGELWLKGPSIAKGYFRNEEeiITSEGWL-----------KTGDLCYIDNDGFLFIVDRLKELIKYKGYQVP 458
Cdd:cd17656 319 QQLQPQGIVGELYISGASVARGYLNRQE--LTAEKFFpdpfdpnermyRTGDLARYLPDGNIEFLGRADHQVKIRGYRIE 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063734905 459 PAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVArkPESNLCEKKVIDFISKQV 514
Cdd:cd17656 397 LGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV--MEQELNISQLREYLAKQL 450
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
65-493 |
1.85e-24 |
|
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: 105.68 E-value: 1.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 65 ISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTtanPLNTAseilrqiadsnpklaFTT 144
Cdd:cd05973 1 LTFGELRALSARFAN-ALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQ---PLFTA---------------FGP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 145 PELAPKIASSGISIVLERVEdtlrvprglkvvgnltemmkkepsgqavrnQVHK--DDTAMLLYSSGTTGRSKGVNSSHG 222
Cdd:cd05973 62 KAIEHRLRTSGARLVVTDAA------------------------------NRHKldSDPFVMMFTSGTTGLPKGVPVPLR 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 223 NLIAHVArYIAEPFE-QPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPR-FDLGEMMAAVEKYRATTLILVPPVLV 300
Cdd:cd05973 112 ALAAFGA-YLRDAVDlRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGgFSVESTWRVIERLGVTNLAGSPTAYR 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 301 TMINKADQIMKKYDVSfLRTVRCGGAPLSKEVTQGFMKKYpTVDVYQGYALTESNGAGASIESVEESRRYGAVGLLSCGV 380
Cdd:cd05973 191 LLMAAGAEVPARPKGR-LRRVSSAGEPLTPEVIRWFDAAL-GVPIHDHYGQTELGMVLANHHALEHPVHAGSAGRAMPGW 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 381 EARIVDPNTGQVmGLNQTGELWL---KGPSIAKGYFRNEEEIITSEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQV 457
Cdd:cd05973 269 RVAVLDDDGDEL-GPGEPGRLAIdiaNSPLMWFRGYQLPDTPAIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRI 347
|
410 420 430
....*....|....*....|....*....|....*.
gi 1063734905 458 PPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYV 493
Cdd:cd05973 348 GPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFV 383
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
52-493 |
2.10e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 106.02 E-value: 2.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 52 GKTAFIDaaTDHRISFSDLWMAVDRVADCLLHDVGirRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILR 131
Cdd:PRK07638 16 NKIAIKE--NDRVLTYKDWFESVCKVANWLNEKES--KNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 132 QIADSNPKLAFTTPELAPKIASSGISIVLERvedtlrvprglkvvgNLTEMMKKE-PSGQAVRNQVHkdDTAMLLYSSGT 210
Cdd:PRK07638 92 RLAISNADMIVTERYKLNDLPDEEGRVIEID---------------EWKRMIEKYlPTYAPIENVQN--APFYMGFTSGS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 211 TGRSKGVNSSHGNLIaHVARYIAEPFE-QPQQTFICTVPLFHTFGLLNFVlATLALGTTVVILPRFDLGEMMAAVEKYRA 289
Cdd:PRK07638 155 TGKPKAFLRAQQSWL-HSFDCNVHDFHmKREDSVLIAGTLVHSLFLYGAI-STLYVGQTVHLMRKFIPNQVLDKLETENI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 290 TTLILVPpvlvTMIN---KADQIMKKYDvsflrTVRCGGAPLSKEVTQGFMKKYPTVDVYQGYALTESNGAGASIESvEE 366
Cdd:PRK07638 233 SVMYTVP----TMLEslyKENRVIENKM-----KIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSFVTALVDE-ES 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 367 SRRYGAVGLLSCGVEARIVDPnTGQVMGLNQTGELWLKGPSIAKGYFRN--EEEIITSEGWLKTGDLCYIDNDGFLFIVD 444
Cdd:PRK07638 303 ERRPNSVGRPFHNVQVRICNE-AGEEVQKGEIGTVYVKSPQFFMGYIIGgvLARELNADGWMTVRDVGYEDEEGFIYIVG 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1063734905 445 RLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYV 493
Cdd:PRK07638 382 REKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII 430
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
64-493 |
2.56e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 107.94 E-value: 2.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 64 RISFSDLWMAVDRVADCLLhDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLAFT 143
Cdd:PRK12467 537 VLSYAELNRQANRLAHVLI-AAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLT 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 144 TPELApkiassgisivlerveDTLRVPRGLKVVgnLTEMMKKEPSGQAVRN---QVHKDDTAMLLYSSGTTGRSKGVNSS 220
Cdd:PRK12467 616 QSHLL----------------AQLPVPAGLRSL--CLDEPADLLCGYSGHNpevALDPDNLAYVIYTSGSTGQPKGVAIS 677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 221 HGNLiahvARYIAEPFEQPQQTFICTVPLFHTFGLLNFVL---ATLALGTTVVILPR---FDLGEMMAAVEKYRATTLIL 294
Cdd:PRK12467 678 HGAL----ANYVCVIAERLQLAADDSMLMVSTFAFDLGVTelfGALASGATLHLLPPdcaRDAEAFAALMADQGVTVLKI 753
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 295 VPPVLVTMInkadQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVDVYQGYALTESNGAGASIESVEESRRYGAVG 374
Cdd:PRK12467 754 VPSHLQALL----QASRVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYELSDEERDFGNVP 829
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 375 LLS--CGVEARIVD----PNTGQVMglnqtGELWLKGPSIAKGYFRNEEeiITSEGWL------------KTGDLCYIDN 436
Cdd:PRK12467 830 IGQplANLGLYILDhylnPVPVGVV-----GELYIGGAGLARGYHRRPA--LTAERFVpdpfgadggrlyRTGDLARYRA 902
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063734905 437 DGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFpMAYV 493
Cdd:PRK12467 903 DGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQL-VAYL 958
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
62-493 |
8.47e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 106.40 E-value: 8.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 62 DHRISFSDLWMAVDRVADCLL-HDVGIRRgdVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKL 140
Cdd:PRK12467 3118 DQQLSYAELNRRANRLAHRLIaIGVGPDV--LVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKL 3195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 141 AFTTPELapkiassgisivLERvedtLRVPRGLKVV----GNLTEMMKKEPSgqavrNQVHKDDTAMLLYSSGTTGRSKG 216
Cdd:PRK12467 3196 LLTQAHL------------LEQ----LPAPAGDTALtldrLDLNGYSENNPS-----TRVMGENLAYVIYTSGSTGKPKG 3254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 217 VNSSHGNLIAHVaRYIAEPFEQPQQTficTVPLFHTFGLLNFV---LATLALGTTVVILP--RFDLGEMMAAVEKYRATT 291
Cdd:PRK12467 3255 VGVRHGALANHL-CWIAEAYELDAND---RVLLFMSFSFDGAQerfLWTLICGGCLVVRDndLWDPEELWQAIHAHRISI 3330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 292 LILVPpvlvTMINKADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVDVYQGYALTESNGAGASIESVEESR--- 368
Cdd:PRK12467 3331 ACFPP----AYLQQFAEDAGGADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAVcea 3406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 369 RYGAVGLLSCGVEARIVDPNTGQVmGLNQTGELWLKGPSIAKGYFR----NEEEIITS------EGWLKTGDLCYIDNDG 438
Cdd:PRK12467 3407 PYAPIGRPVAGRSIYVLDGQLNPV-PVGVAGELYIGGVGLARGYHQrpslTAERFVADpfsgsgGRLYRTGDLARYRADG 3485
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1063734905 439 FLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFpDKEAGQFPMAYV 493
Cdd:PRK12467 3486 VIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYV 3539
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
44-493 |
1.02e-23 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 105.03 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 44 FISSQTYRGKTafidaatdhrISFSDLWMAVDRVADCLLhDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLT----- 118
Cdd:PRK10524 74 AVSTETDEERT----------YTFRQLHDEVNRMAAMLR-SLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSvvfgg 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 119 -TANPLNTaseilrQIADSNPKLAFTTP------ELAP--KIASSGISIVLERVEDTLRVPRGLkvvgnlTEMMKKEPSG 189
Cdd:PRK10524 143 fASHSLAA------RIDDAKPVLIVSADagsrggKVVPykPLLDEAIALAQHKPRHVLLVDRGL------APMARVAGRD 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 190 Q--AVRNQVHKD-----------DTAMLLYSSGTTGRSKGVNSSHGNLIAHVA---RYIaepFE-QPQQTFICTVPLFHT 252
Cdd:PRK10524 211 VdyATLRAQHLGarvpvewlesnEPSYILYTSGTTGKPKGVQRDTGGYAVALAtsmDTI---FGgKAGETFFCASDIGWV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 253 FGLLNFVLATLALGTTVVI---LP-RFDLGEMMAAVEKYRATTLiLVPPVLVTMINKAD-QIMKKYDVSFLRTVRCGGAP 327
Cdd:PRK10524 288 VGHSYIVYAPLLAGMATIMyegLPtRPDAGIWWRIVEKYKVNRM-FSAPTAIRVLKKQDpALLRKHDLSSLRALFLAGEP 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 328 LSKEVTQGFMK--KYPTVDVY-QgyalTESNGAGASIESVEESR--RYGAVGLLSCGVEARIVDPNTGQVMGLNQTGELW 402
Cdd:PRK10524 367 LDEPTASWISEalGVPVIDNYwQ----TETGWPILAIARGVEDRptRLGSPGVPMYGYNVKLLNEVTGEPCGPNEKGVLV 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 403 LKGP--------------SIAKGYFRNEEEIITSegwlkTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLN 468
Cdd:PRK10524 443 IEGPlppgcmqtvwgdddRFVKTYWSLFGRQVYS-----TFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISS 517
|
490 500
....*....|....*....|....*
gi 1063734905 469 HPDILDAAVIPFPDKEAGQFPMAYV 493
Cdd:PRK10524 518 HPAVAEVAVVGVKDALKGQVAVAFV 542
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
129-493 |
1.25e-23 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 104.32 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 129 ILRQIADSNPKLAFTTPELAPKIASSGISivlervedtlrvpRGLKVVGNLTEMMKkEPSGQAVRNQVHKDDTAMLLYSS 208
Cdd:PRK09192 120 LRGMLASAQPAAIITPDELLPWVNEATHG-------------NPLLHVLSHAWFKA-LPEADVALPRPTPDDIAYLQYSS 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 209 GTTGRSKGVNSSHG----NLIAHVARYIAEpfeQPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPR---------- 274
Cdd:PRK09192 186 GSTRFPRGVIITHRalmaNLRAISHDGLKV---RPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTrdfarrplqw 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 275 FDLgemmaaVEKYRATtlILVPPVL--------VTMINKADqimkkYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVdvy 346
Cdd:PRK09192 263 LDL------ISRNRGT--ISYSPPFgyelcarrVNSKDLAE-----LDLSCWRVAGIGADMIRPDVLHQFAEAFAPA--- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 347 qG---------YALTESN--------GAGASIESVEESRRYG---AVGLLS----------CGV-----EARIVDPNtGQ 391
Cdd:PRK09192 327 -GfddkafmpsYGLAEATlavsfsplGSGIVVEEVDRDRLEYqgkAVAPGAetrrvrtfvnCGKalpghEIEIRNEA-GM 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 392 VMGLNQTGELWLKGPSIAKGYFRNEE--EIITSEGWLKTGDLCYIdNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNH 469
Cdd:PRK09192 405 PLPERVVGHICVRGPSLMSGYFRDEEsqDVLAADGWLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQE 483
|
410 420
....*....|....*....|....*
gi 1063734905 470 PDILDAAVIPFP-DKEAGQFPMAYV 493
Cdd:PRK09192 484 PELRSGDAAAFSiAQENGEKIVLLV 508
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
62-494 |
1.44e-23 |
|
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: 103.16 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 62 DHRISFSDLWMAVDRVADCLlHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLA 141
Cdd:cd17643 10 DRRLTYGELDARANRLARTL-RAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 142 FTTPelapkiassgisivlervedtlrvprglkvvgnltemmkkepsgqavrnqvhkDDTAMLLYSSGTTGRSKGVNSSH 221
Cdd:cd17643 89 LTDP-----------------------------------------------------DDLAYVIYTSGSTGRPKGVVVSH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 222 GNLIAHVA--RYIAEPFEQPQQTfictvpLFHTFGLlNF----VLATLALGTTVVILPRfdlgEMMAAVEKYRAttliLV 295
Cdd:cd17643 116 ANVLALFAatQRWFGFNEDDVWT------LFHSYAF-DFsvweIWGALLHGGRLVVVPY----EVARSPEDFAR----LL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 296 PPVLVTMINK----------ADQIMKKyDVSFLRTVRCGGAPLSKEVTQGFMKKYPTV--DVYQGYALTESNGAGASIES 363
Cdd:cd17643 181 RDEGVTVLNQtpsafyqlveAADRDGR-DPLALRYVIFGGEALEAAMLRPWAGRFGLDrpQLVNMYGITETTVHVTFRPL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 364 VEESRRYGAVGLLSC---GVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEEEiiTSEGWL------------KT 428
Cdd:cd17643 260 DAADLPAAAASPIGRplpGLRVYVLDAD-GRPVPPGVVGELYVSGAGVARGYLGRPEL--TAERFVanpfggpgsrmyRT 336
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063734905 429 GDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVA 494
Cdd:cd17643 337 GDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVV 402
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
28-493 |
1.65e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 105.42 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 28 RKPLALPSkeSLDITTFISSQTYRGKTAFIDAATDHRISFSDLWMAVDRVADCLLhDVGIRRGDVVLVLSPNTISIPIVC 107
Cdd:PRK12316 1994 RTPEAYPR--GPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLR-ARGVGPEVRVAIAAERSFELVVAL 2070
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 108 LSVMSLGAVLTtanPLNTAseilrqiadsnpklaFTTPELAPKIASSGISIVL--ERVEDTLRVPRGLKVVGNLTEMMKK 185
Cdd:PRK12316 2071 LAVLKAGGAYV---PLDPN---------------YPAERLAYMLEDSGAALLLtqRHLLERLPLPAGVARLPLDRDAEWA 2132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 186 EPSGQAVRNQVHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHV----ARYIAEPFEQPQQtfictvplFHTFGLLNFV-- 259
Cdd:PRK12316 2133 DYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCqaagERYELSPADCELQ--------FMSFSFDGAHeq 2204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 260 -LATLALGTTVVILP--RFDLGEMMAAVEKYRATTLILVPPVLVTMINKADQIMKKYDVsflRTVRCGGAPLSKEVTQGF 336
Cdd:PRK12316 2205 wFHPLLNGARVLIRDdeLWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPAV---RVYCFGGEAVPAASLRLA 2281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 337 MKKYPTVDVYQGYALTESngagASIESVEESRR-------YGAVGLLSCGVEARIVDPNTgQVMGLNQTGELWLKGPSIA 409
Cdd:PRK12316 2282 WEALRPVYLFNGYGPTEA----VVTPLLWKCRPqdpcgaaYVPIGRALGNRRAYILDADL-NLLAPGMAGELYLGGEGLA 2356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 410 KGYFrnEEEIITSEGWL------------KTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAV 477
Cdd:PRK12316 2357 RGYL--NRPGLTAERFVpdpfsasgerlyRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVV 2434
|
490
....*....|....*.
gi 1063734905 478 IPFpDKEAGQFPMAYV 493
Cdd:PRK12316 2435 VAQ-DGASGKQLVAYV 2449
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
82-500 |
2.46e-23 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 103.39 E-value: 2.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 82 LHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLAFTTPELAPkIASSGISIVLE 161
Cdd:PLN02479 62 LAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQEFFT-LAEEALKILAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 162 RVEDTLRVPRgLKVVGNltEMMKKEPSGQAVRN------------------QVHKD--DTAMLLYSSGTTGRSKGVNSSH 221
Cdd:PLN02479 141 KKKSSFKPPL-LIVIGD--PTCDPKSLQYALGKgaieyekfletgdpefawKPPADewQSIALGYTSGTTASPKGVVLHH 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 222 -GNLIAHVARYIAepFEQPQ-QTFICTVPLFHTFGLLnFVLATLALGTTVVILPRFDLGEMMAAVEKYRATTLILVPPVL 299
Cdd:PLN02479 218 rGAYLMALSNALI--WGMNEgAVYLWTLPMFHCNGWC-FTWTLAALCGTNICLRQVTAKAIYSAIANYGVTHFCAAPVVL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 300 VTMIN--KADQIMKKYDVSFLRTVrcGGAP----LSKEVTQGFMkkyptvdVYQGYALTESNGAGA---------SIESV 364
Cdd:PLN02479 295 NTIVNapKSETILPLPRVVHVMTA--GAAPppsvLFAMSEKGFR-------VTHTYGLSETYGPSTvcawkpewdSLPPE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 365 EESRRYGAVGLLSCGVEA-RIVDPNTGQVMGLNQT--GELWLKGPSIAKGYFRNEE--EIITSEGWLKTGDLCYIDNDGF 439
Cdd:PLN02479 366 EQARLNARQGVRYIGLEGlDVVDTKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKanEEAFANGWFHSGDLGVKHPDGY 445
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063734905 440 LFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESN 500
Cdd:PLN02479 446 IEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVD 506
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
62-501 |
3.66e-23 |
|
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: 102.05 E-value: 3.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 62 DHRISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANpLNTASEILRQIADsnpkla 141
Cdd:cd05940 1 DEALTYAELDAMANRYAR-WLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALIN-YNLRGESLAHCLN------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 142 fttpelapkIASSGISIVlervedtlrvprglkvvgnltemmkkepsgqavrnqvhkdDTAMLLYSSGTTGRSKGVNSSH 221
Cdd:cd05940 73 ---------VSSAKHLVV----------------------------------------DAALYIYTSGTTGLPKAAIISH 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 222 GNLIAHVARYIAEPFEQPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPRFDLGEMMAAVEKYRATTLILVPPVLVT 301
Cdd:cd05940 104 RRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATIFQYIGELCRY 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 302 MINkadQIMKKYDVSFLRTVRCGGApLSKEVTQGFMKKYPTVDVYQGYALTESNgagasIESVEESRRYGAVG----LLS 377
Cdd:cd05940 184 LLN---QPPKPTERKHKVRMIFGNG-LRPDIWEEFKERFGVPRIAEFYAATEGN-----SGFINFFGKPGAIGrnpsLLR 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 378 CGVEARIV--DPNTGQVM----------GLNQTGELWLKgpsIAK-----GYFRN---EEEIITS-----EGWLKTGDLC 432
Cdd:cd05940 255 KVAPLALVkyDLESGEPIrdaegrcikvPRGEPGLLISR---INPlepfdGYTDPaatEKKILRDvfkkgDAWFNTGDLM 331
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063734905 433 YIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAV----IPFPDKEAGqfpMAYVARKPESNL 501
Cdd:cd05940 332 RLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygvqVPGTDGRAG---MAAIVLQPNEEF 401
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
197-494 |
3.93e-23 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 102.06 E-value: 3.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 197 HKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHvARYIAEPFE-QPQQtfiCTVPlfhtFGLLNF------VLATLALGTTV 269
Cdd:cd17649 92 HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAH-CQATAERYGlTPGD---RELQ----FASFNFdgaheqLLPPLICGACV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 270 VILPR---FDLGEMMAAVEKYRATTLILVPPVLVTMINKADQIMKKYDVSfLRTVRCGGAPLSKE-VTQGFMKKyptVDV 345
Cdd:cd17649 164 VLRPDelwASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDGRPPS-LRLYIFGGEALSPElLRRWLKAP---VRL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 346 YQGYALTESNGAGASIESVEESRRYGA---VGLLSCGVEARIVDPNTGQVMgLNQTGELWLKGPSIAKGYF--------R 414
Cdd:cd17649 240 FNAYGPTEATVTPLVWKCEAGAARAGAsmpIGRPLGGRSAYILDADLNPVP-VGVTGELYIGGEGLARGYLgrpeltaeR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 415 NEEEIITSEG--WLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFpMAY 492
Cdd:cd17649 319 FVPDPFGAPGsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQL-VAY 397
|
..
gi 1063734905 493 VA 494
Cdd:cd17649 398 VV 399
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
64-493 |
5.01e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 103.88 E-value: 5.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 64 RISFSDLWMAVDRVADCLL-HDVGirrGDVVLVLS-PNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLA 141
Cdd:PRK12316 4576 KLTYAELNRRANRLAHALIaRGVG---PEVLVGIAmERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALL 4652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 142 FTTPELAPKI-ASSGI-SIVLERVEDTLRVPrglkvvgnltemmKKEPSgqavrNQVHKDDTAMLLYSSGTTGRSKGVNS 219
Cdd:PRK12316 4653 LTQSHLLQRLpIPDGLaSLALDRDEDWEGFP-------------AHDPA-----VRLHPDNLAYVIYTSGSTGRPKGVAV 4714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 220 SHGNLIAHVARYIAEPFEQPQQtficTVPLFHTFGLLNFVLA---TLALGTTVVILP--RFDLGEMMAAVEKYRATTLIL 294
Cdd:PRK12316 4715 SHGSLVNHLHATGERYELTPDD----RVLQFMSFSFDGSHEGlyhPLINGASVVIRDdsLWDPERLYAEIHEHRVTVLVF 4790
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 295 VPPVLVTMINKADqimKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVDVYQGYALTESN---GAGASIESVEESRRYG 371
Cdd:PRK12316 4791 PPVYLQQLAEHAE---RDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTvtvLLWKARDGDACGAAYM 4867
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 372 AVGLLSCGVEARIVDpNTGQVMGLNQTGELWLKGPSIAKGYFRNEEeiITSEGWL------------KTGDLCYIDNDGF 439
Cdd:PRK12316 4868 PIGTPLGNRSGYVLD-GQLNPLPVGVAGELYLGGEGVARGYLERPA--LTAERFVpdpfgapggrlyRTGDLARYRADGV 4944
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1063734905 440 LFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPfPDKEAGQFPMAYV 493
Cdd:PRK12316 4945 IDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIA-QEGAVGKQLVGYV 4997
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
204-509 |
1.11e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 101.32 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 204 LLYSSGTTGRSKGVNSSHGNLIAHvARYIAEPFE---QPQQTFICTVPLFHT--FGLLnfVLATLALGTTVVILPRFDLG 278
Cdd:PRK07008 181 LCYTSGTTGNPKGALYSHRSTVLH-AYGAALPDAmglSARDAVLPVVPMFHVnaWGLP--YSAPLTGAKLVLPGPDLDGK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 279 EMMAAVEKYRATTLILVPPVLVTMINKADQIMKKYDvSFLRTVrCGGAPLSKEVTQGFMKKYpTVDVYQGYALTESNGAG 358
Cdd:PRK07008 258 SLYELIEAERVTFSAGVPTVWLGLLNHMREAGLRFS-TLRRTV-IGGSACPPAMIRTFEDEY-GVEVIHAWGMTEMSPLG 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 359 -------ASIESVEESRRY--GAVGLLSCGVEARIVDPNTGQVMGLNQT-GELWLKGPSIAKGYFRNEEEIItSEGWLKT 428
Cdd:PRK07008 335 tlcklkwKHSQLPLDEQRKllEKQGRVIYGVDMKIVGDDGRELPWDGKAfGDLQVRGPWVIDRYFRGDASPL-VDGWFPT 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 429 GDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKVID 508
Cdd:PRK07008 414 GDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELLA 493
|
.
gi 1063734905 509 F 509
Cdd:PRK07008 494 F 494
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
39-497 |
1.94e-22 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 100.45 E-value: 1.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 39 LDITTFISSQTYRGKTAFIDAatDHRISFSDLWMAVDRVAdCLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVlt 118
Cdd:PRK10946 25 LPLTDILTRHAASDAIAVICG--ERQFSYRELNQASDNLA-CSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 119 tanPLNT-----ASEIL---RQI------ADSNPKLaFTTPELAP--KIASSGISIVLERVEDTLRvprglkvvgNLTEM 182
Cdd:PRK10946 100 ---PVNAlfshqRSELNayaSQIepalliADRQHAL-FSDDDFLNtlVAEHSSLRVVLLLNDDGEH---------SLDDA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 183 MKkEPSGQAVRNQVHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVaRYIAEPFEQPQQT-FICTVPLFHTF-----GLL 256
Cdd:PRK10946 167 IN-HPAEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYYYSV-RRSVEICGFTPQTrYLCALPAAHNYpmsspGAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 257 NFVLAtlalGTTVVILPRFDLGEMMAAVEKYRATTLILVPPVLVTMINKADQIMKKYDVSFLRTVRCGGAPLSKEVTqgf 336
Cdd:PRK10946 245 GVFLA----GGTVVLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKLLQVGGARLSETLA--- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 337 mKKYPTVdvyqgyaltesngAGASIESVeesrrYG-AVGL--------------------LSCGVEARIVDPNtGQVMGL 395
Cdd:PRK10946 318 -RRIPAE-------------LGCQLQQV-----FGmAEGLvnytrlddsderifttqgrpMSPDDEVWVADAD-GNPLPQ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 396 NQTGELWLKGPSIAKGYFRNEE---EIITSEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDI 472
Cdd:PRK10946 378 GEVGRLMTRGPYTFRGYYKSPQhnaSAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAV 457
|
490 500
....*....|....*....|....*.
gi 1063734905 473 LDAAVIPFPDKEAGQFPMAY-VARKP 497
Cdd:PRK10946 458 IHAALVSMEDELMGEKSCAFlVVKEP 483
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
199-498 |
2.96e-22 |
|
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: 99.17 E-value: 2.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 199 DDTAMLLYSSGTTGRSKGVNSSHGNLIaHVARYIAEPFEQPQQTficTVPLFHTFGLLNFVL---ATLALGTTVVILP-- 273
Cdd:cd17645 104 DDLAYVIYTSGSTGLPKGVMIEHHNLV-NLCEWHRPYFGVTPAD---KSLVYASFSFDASAWeifPHLTAGAALHVVPse 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 274 -RFDLGEMMAAVEKYRATTLILVPPVlvtminkADQIMKKYDVSFlRTVRCGGAPLSKEVTQGFmkkyptvDVYQGYALT 352
Cdd:cd17645 180 rRLDLDALNDYFNQEGITISFLPTGA-------AEQFMQLDNQSL-RVLLTGGDKLKKIERKGY-------KLVNNYGPT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 353 ESNGAGASIEsVEESRRYGAVGLLSCGVEARIVDPNTgQVMGLNQTGELWLKGPSIAKGYFRNEEEI---------ITSE 423
Cdd:cd17645 245 ENTVVATSFE-IDKPYANIPIGKPIDNTRVYILDEAL-QLQPIGVAGELCIAGEGLARGYLNRPELTaekfivhpfVPGE 322
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063734905 424 GWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPE 498
Cdd:cd17645 323 RMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEE 397
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
82-510 |
5.36e-22 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 99.82 E-value: 5.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 82 LHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGA---VLTTANPLNTASEILRQIadsNPKLAFT-------------TP 145
Cdd:PTZ00237 109 LLNLNISKNDNVLIYMANTLEPLIAMLSCARIGAthcVLFDGYSVKSLIDRIETI---TPKLIITtnygilndeiitfTP 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 146 ELAPKIASSGIS----IVLERVEDTLRvpRGLKVVGNLT----------EMMK-KEpsgqavRNQ--------VHKDDTA 202
Cdd:PTZ00237 186 NLKEAIELSTFKpsnvITLFRNDITSE--SDLKKIETIPtipntlswydEIKKiKE------NNQspfyeyvpVESSHPL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 203 MLLYSSGTTGRSKGV---NSSHGNLIAHVARYIAEpfeqpqqTFICTVPLFHT-FGLL---NFVLATLALGTTVV----- 270
Cdd:PTZ00237 258 YILYTSGTTGNSKAVvrsNGPHLVGLKYYWRSIIE-------KDIPTVVFSHSsIGWVsfhGFLYGSLSLGNTFVmfegg 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 271 -ILPRFDLGEMMAAVEKYRATTLILVPPVLVTMIN---KADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYpTVDVY 346
Cdd:PTZ00237 331 iIKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKtdpEATIIRSKYDLSNLKEIWCGGEVIEESIPEYIENKL-KIKSS 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 347 QGYALTESnGAGASIESVEESRRYGAVGLLSCGVEARIVDPNtGQVMGLNQTGELWLK---GPSIAKGYFRNEE---EII 420
Cdd:PTZ00237 410 RGYGQTEI-GITYLYCYGHINIPYNATGVPSIFIKPSILSED-GKELNVNEIGEVAFKlpmPPSFATTFYKNDEkfkQLF 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 421 TS-EGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPES 499
Cdd:PTZ00237 488 SKfPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQ 567
|
490
....*....|.
gi 1063734905 500 nlcEKKVIDFI 510
Cdd:PTZ00237 568 ---SNQSIDLN 575
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
171-463 |
9.34e-22 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 99.02 E-value: 9.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 171 RGLKVVGNLTEMMKKEPSGQAVR--------NQVHKD----------DTAMLLYSSGTTGRSKGVNSSHGNLIAHVARYI 232
Cdd:PLN02736 175 RLIVVVGGADEPLPSLPSGTGVEivtyskllAQGRSSpqpfrppkpeDVATICYTSGTTGTPKGVVLTHGNLIANVAGSS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 233 AEPFEQPQQTFICTVPLFHTFGLLNfVLATLALGTTVVILpRFDLGEMMAAVEKYRATTLILVPPVL------VTMINKA 306
Cdd:PLN02736 255 LSTKFYPSDVHISYLPLAHIYERVN-QIVMLHYGVAVGFY-QGDNLKLMDDLAALRPTIFCSVPRLYnriydgITNAVKE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 307 DQIMKK--YDVSF--------------------------------LRTVRCGGAPLSKEVTQgFMKKYPTVDVYQGYALT 352
Cdd:PLN02736 333 SGGLKErlFNAAYnakkqalengknpspmwdrlvfnkikaklggrVRFMSSGASPLSPDVME-FLRICFGGRVLEGYGMT 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 353 ESNgagASIESVEES-RRYGAVGLLSCGVEARIVDpntgqVMGLNQT--------GELWLKGPSIAKGYFRNEE---EII 420
Cdd:PLN02736 412 ETS---CVISGMDEGdNLSGHVGSPNPACEVKLVD-----VPEMNYTsedqpyprGEICVRGPIIFKGYYKDEVqtrEVI 483
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1063734905 421 TSEGWLKTGDLCYIDNDGFLFIVDRLKELIKY-KGYQVPPAELE 463
Cdd:PLN02736 484 DEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIE 527
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
196-469 |
9.90e-22 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 98.35 E-value: 9.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 196 VHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHvaRYIAEPFEQPQQT--FICTVPLFHTFGLLNFVLATLALGTTVVI-- 271
Cdd:PRK06334 180 KDPEDVAVILFTSGTEKLPKGVPLTHANLLAN--QRACLKFFSPKEDdvMMSFLPPFHAYGFNSCTLFPLLSGVPVVFay 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 272 --LPRFDLGEMmaaVEKYRATTLILVPPVLVTMINKAdqimKKYDVSF--LRTVRCGGAPLSKEVTQGFMKKYPTVDVYQ 347
Cdd:PRK06334 258 npLYPKKIVEM---IDEAKVTFLGSTPVFFDYILKTA----KKQESCLpsLRFVVIGGDAFKDSLYQEALKTFPHIQLRQ 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 348 GYALTESNGAgASIESVEESRRYGAVGLLSCGVEARIVDPNTGQVMGLNQTGELWLKGPSIAKGYFRNEEEI----ITSE 423
Cdd:PRK06334 331 GYGTTECSPV-ITINTVNSPKHESCVGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLGEDFGQgfveLGGE 409
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1063734905 424 GWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNH 469
Cdd:PRK06334 410 TWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
52-508 |
2.93e-21 |
|
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: 96.57 E-value: 2.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 52 GKTAFIDAatDHRISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTtanPLNTASEILR 131
Cdd:cd12114 2 DATAVICG--DGTLTYGELAERARRVAG-ALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYV---PVDIDQPAAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 132 qiadsnpklafttpeLAPKIASSGISIVL-ERVEDTLRVPRGLKVVGNLTemmKKEPSGQAVRNQVHKDDTAMLLYSSGT 210
Cdd:cd12114 76 ---------------REAILADAGARLVLtDGPDAQLDVAVFDVLILDLD---ALAAPAPPPPVDVAPDDLAYVIFTSGS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 211 TGRSKGVNSSHGNLIahvaryiaepfeqpqQTFICTVPLFH------TFGL--LNF------VLATLALGTTVVILPRFD 276
Cdd:cd12114 138 TGTPKGVMISHRAAL---------------NTILDINRRFAvgpddrVLALssLSFdlsvydIFGALSAGATLVLPDEAR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 277 LGE---MMAAVEKYRATTLILVPPVLVTMINKADQIMKkyDVSFLRTVRCGG--APLSKEvtqgfmkkyPTVDVYQGYAL 351
Cdd:cd12114 203 RRDpahWAELIERHGVTLWNSVPALLEMLLDVLEAAQA--LLPSLRLVLLSGdwIPLDLP---------ARLRALAPDAR 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 352 TESNGaGA----------SIESVEESRR---YGaVGLlsCGVEARIVDPNtGQ-----VMGlnqtgELWLKGPSIAKGYF 413
Cdd:cd12114 272 LISLG-GAteasiwsiyhPIDEVPPDWRsipYG-RPL--ANQRYRVLDPR-GRdcpdwVPG-----ELWIGGRGVALGYL 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 414 RNEE-------EIITSEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAG 486
Cdd:cd12114 342 GDPEltaarfvTHPDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGK 421
|
490 500
....*....|....*....|..
gi 1063734905 487 QFpMAYVARKPESNLCEKKVID 508
Cdd:cd12114 422 RL-AAFVVPDNDGTPIAPDALR 442
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
62-511 |
3.25e-21 |
|
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: 96.98 E-value: 3.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 62 DHRISFSDLWMAVDRVADCLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLA 141
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 142 FTTPELA-------PKIASSGISIVLERVEDTlrvPRGlkvVGNLTEMMKKEPSG---QAVRNQVHKDDTAMLLYSSGTT 211
Cdd:cd05938 83 VVAPELQeaveevlPALRADGVSVWYLSHTSN---TEG---VISLLDKVDAASDEpvpASLRAHVTIKSPALYIYTSGTT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 212 GRSKGVNSSHGNLIAHVARYIAEPFEQPQQTFICtVPLFHTFGLLNFVLATLALGTTVVILPRFDLGEMMAAVEKYRATT 291
Cdd:cd05938 157 GLPKAARISHLRVLQCSGFLSLCGVTADDVIYIT-LPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKHNVTV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 292 LILVPPVLVTMIN----KADQIMKkydvsflrtVRCG-GAPLSKEVTQGFMKKYPTVDVYQGYALTESNgagasIESVEE 366
Cdd:cd05938 236 IQYIGELLRYLCNqpqsPNDRDHK---------VRLAiGNGLRADVWREFLRRFGPIRIREFYGSTEGN-----IGFFNY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 367 SRRYGAVG-------------LLSCGVE-ARIVDPNTGQVM--GLNQTGELwlkgpsIAK--------GYFRNEEEiitS 422
Cdd:cd05938 302 TGKIGAVGrvsylykllfpfeLIKFDVEkEEPVRDAQGFCIpvAKGEPGLL------VAKitqqspflGYAGDKEQ---T 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 423 EG------------WLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAV--IPFPDKEaGQF 488
Cdd:cd05938 373 EKkllrdvfkkgdvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVygVTVPGHE-GRI 451
|
490 500
....*....|....*....|...
gi 1063734905 489 PMAYVARKPESNLCEKKVIDFIS 511
Cdd:cd05938 452 GMAAVKLKPGHEFDGKKLYQHVR 474
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
65-486 |
4.78e-21 |
|
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: 96.37 E-value: 4.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 65 ISFSDLWMAVDRVADCLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVlttANPL--NTASEILRQI-ADSNPK-L 140
Cdd:cd17632 68 ITYAELWERVGAVAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAV---SVPLqaGASAAQLAPIlAETEPRlL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 141 AFTTPELAPKIASSGISIVLERV--------EDTLR------------VPRGLKVVGNLTEMMKKEPSGQAVRNQVHKDD 200
Cdd:cd17632 145 AVSAEHLDLAVEAVLEGGTPPRLvvfdhrpeVDAHRaalesarerlaaVGIPVTTLTLIAVRGRDLPPAPLFRPEPDDDP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 201 TAMLLYSSGTTGRSKGVNSSHgNLIAHVARyIAEPFEQPQQTFICTV---PLFHTFGlLNFVLATLALGTTVVILPRFDL 277
Cdd:cd17632 225 LALLIYTSGSTGTPKGAMYTE-RLVATFWL-KVSSIQDIRPPASITLnfmPMSHIAG-RISLYGTLARGGTAYFAAASDM 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 278 GEMMAAVEKYRATTLILVPPV--------LVTMINK----ADQIMKKYDV-SFLR---------TVRCGGAPLSKEVtQG 335
Cdd:cd17632 302 STLFDDLALVRPTELFLVPRVcdmlfqryQAELDRRsvagADAETLAERVkAELRervlggrllAAVCGSAPLSAEM-KA 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 336 FMKKYPTVDVYQGYALTEsngAGASIESVEESRRygAVgllscgVEARIVD-PNtgqvMGLNQT------GELWLKGPSI 408
Cdd:cd17632 381 FMESLLDLDLHDGYGSTE---AGAVILDGVIVRP--PV------LDYKLVDvPE----LGYFRTdrphprGELLVKTDTL 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 409 AKGYFRNEE---EIITSEGWLKTGDLCYIDNDGFLFIVDRLKELIKY-KGYQVPPAELEALLLNHPDI------------ 472
Cdd:cd17632 446 FPGYYKRPEvtaEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVrqifvygnsera 525
|
490
....*....|....*
gi 1063734905 473 -LDAAVIPFPDKEAG 486
Cdd:cd17632 526 yLLAVVVPTQDALAG 540
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
147-493 |
2.25e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 95.61 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 147 LAPKIASSGISIVLERVEDTLRVPRGLKVVGNLTEMMKKEPSGQAVRN---QVHKDDTAMLLYSSGTTGRSKGVNSSHGN 223
Cdd:PRK12467 1663 LAYMIEDSGIELLLTQSHLQARLPLPDGLRSLVLDQEDDWLEGYSDSNpavNLAPQNLAYVIYTSGSTGRPKGAGNRHGA 1742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 224 LIAHvaryiaepFEQPQQTFICT----VPLFHTFGLLNFV---LATLALGTTVVILP---RFDLGEMMAAVEKYRATTLI 293
Cdd:PRK12467 1743 LVNR--------LCATQEAYQLSaadvVLQFTSFAFDVSVwelFWPLINGARLVIAPpgaHRDPEQLIQLIERQQVTTLH 1814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 294 LVPPVLVTMINKADQIMKKYDvsfLRTVRCGGAPLSKEVTQGFMKKYPTVDVYQGYALTEsngagASIE--------SVE 365
Cdd:PRK12467 1815 FVPSMLQQLLQMDEQVEHPLS---LRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTE-----TAVDvthwtcrrKDL 1886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 366 ESRRYGAVGLLSCGVEARIVDpNTGQVMGLNQTGELWLKGPSIAKGYFRNEEeiITSEGWL------------KTGDLCY 433
Cdd:PRK12467 1887 EGRDSVPIGQPIANLSTYILD-ASLNPVPIGVAGELYLGGVGLARGYLNRPA--LTAERFVadpfgtvgsrlyRTGDLAR 1963
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 434 IDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPfPDKEAGQFPMAYV 493
Cdd:PRK12467 1964 YRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIA-QDGANGKQLVAYV 2022
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
62-493 |
2.66e-20 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 93.81 E-value: 2.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 62 DHRISFSDLWMAVDRVAdCLLHDVGIRRGDVVLV---LSPNTIsipivclsVMSLGAVLTTAN--PLNT--ASEILRQIA 134
Cdd:PRK04813 25 GEKLTYGQLKEDSDALA-AFIDSLKLPDKSPIIVfghMSPEML--------ATFLGAVKAGHAyiPVDVssPAERIEMII 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 135 D-SNPKLAFTTPELAPKIasSGISIVlervedtlrvprglkVVGNLTEMMKKEPSGQAvRNQVHKDDTAMLLYSSGTTGR 213
Cdd:PRK04813 96 EvAKPSLIIATEELPLEI--LGIPVI---------------TLDELKDIFATGNPYDF-DHAVKGDDNYYIIFTSGTTGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 214 SKGVNSSHGNLIAHVaRYIAEPFEQPQ-QTFICTVPLfhTFGLLNFVLA-TLALGTTVVILPRfdlgemmaavekyratT 291
Cdd:PRK04813 158 PKGVQISHDNLVSFT-NWMLEDFALPEgPQFLNQAPY--SFDLSVMDLYpTLASGGTLVALPK----------------D 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 292 LILVPPVLVTMINK------------ADqiMKKYDVSF-------LRT-VRCGGApLSKEVTQGFMKKYPTVDVYQGYAL 351
Cdd:PRK04813 219 MTANFKQLFETLPQlpinvwvstpsfAD--MCLLDPSFneehlpnLTHfLFCGEE-LPHKTAKKLLERFPSATIYNTYGP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 352 TESNGAGASIESVEES-RRYGA--VGLLSCGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFRNEEE----IITSEG 424
Cdd:PRK04813 296 TEATVAVTSIEITDEMlDQYKRlpIGYAKPDSPLLIIDEE-GTKLPDGEQGEIVISGPSVSKGYLNNPEKtaeaFFTFDG 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063734905 425 W--LKTGDLCYIDnDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYV 493
Cdd:PRK04813 375 QpaYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYV 444
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
64-478 |
3.09e-20 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 93.14 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 64 RISFSDLWMAVDRVAdCLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTtanPLNTASEILRqiadsnpklaft 143
Cdd:cd17653 22 SLTYGELDAASNALA-NRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYV---PLDAKLPSAR------------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 144 tpelapkiassgISIVLERVEDTLRVPrglkvvgnltemmkkePSGQavrnqvhkDDTAMLLYSSGTTGRSKGVNSSHGN 223
Cdd:cd17653 86 ------------IQAILRTSGATLLLT----------------TDSP--------DDLAYIIFTSGSTGIPKGVMVPHRG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 224 LIAHVARYIAEPFEQPQQtficTVPLFHTFGL---LNFVLATLALGTTVVIL-PRFDLGEMMAAVekyraTTLILVPPVL 299
Cdd:cd17653 130 VLNYVSQPPARLDVGPGS----RVAQVLSIAFdacIGEIFSTLCNGGTLVLAdPSDPFAHVARTV-----DALMSTPSIL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 300 VTminkadqiMKKYDVSFLRTVRCGGAPlskeVTQGFMKKY-PTVDVYQGYALTESNgAGASIESVEESRRYgAVGLLSC 378
Cdd:cd17653 201 ST--------LSPQDFPNLKTIFLGGEA----VPPSLLDRWsPGRRLYNAYGPTECT-ISSTMTELLPGQPV-TIGKPIP 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 379 GVEARIVDPNTGQV-MGlnQTGELWLKGPSIAKGYFRNEEEIITS-------EGWL--KTGDLCYIDNDGFLFIVDRLKE 448
Cdd:cd17653 267 NSTCYILDADLQPVpEG--VVGEICISGVQVARGYLGNPALTASKfvpdpfwPGSRmyRTGDYGRWTEDGGLEFLGREDN 344
|
410 420 430
....*....|....*....|....*....|.
gi 1063734905 449 LIKYKGYQVP-PAELEALLLNHPDILDAAVI 478
Cdd:cd17653 345 QVKVRGFRINlEEIEEVVLQSQPEVTQAAAI 375
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
66-486 |
3.81e-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: 93.27 E-value: 3.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 66 SFSDLWMAVDRVADCLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLAFTTP 145
Cdd:cd05937 7 TYSETYDLVLRYAHWLHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVIVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 146 elapkiassgisivlervedtlrvprglkvvgnltemmkkepsgqavrnqvhkDDTAMLLYSSGTTGRSKGV------NS 219
Cdd:cd05937 87 -----------------------------------------------------DDPAILIYTSGTTGLPKAAaiswrrTL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 220 SHGNLIAHVARyiaepFEQPQQTFICtVPLFH-TFGLLNFVlATLALGTTVVILPRFDLGEMMAAVEKYRATTLILVPPV 298
Cdd:cd05937 114 VTSNLLSHDLN-----LKNGDRTYTC-MPLYHgTAAFLGAC-NCLMSGGTLALSRKFSASQFWKDVRDSGATIIQYVGEL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 299 ----LVTMINKADQIMKkydvsflrtVRCG-GAPLSKEVTQGFMKKYPTVDVYQGYALTEsnGAGASIesveeSRRYGAV 373
Cdd:cd05937 187 crylLSTPPSPYDRDHK---------VRVAwGNGLRPDIWERFRERFNVPEIGEFYAATE--GVFALT-----NHNVGDF 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 374 GLLSCGVEARI-------------VDPNTGQVMGLNQTG---------------ELWLKGPSIAKGYFRNEEE----IIT 421
Cdd:cd05937 251 GAGAIGHHGLIrrwkfenqvvlvkMDPETDDPIRDPKTGfcvrapvgepgemlgRVPFKNREAFQGYLHNEDAteskLVR 330
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063734905 422 S-----EGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAV----IPFPDKEAG 486
Cdd:cd05937 331 DvfrkgDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygvkVPGHDGRAG 404
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
62-515 |
4.77e-20 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 92.63 E-value: 4.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 62 DHRISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNtiSIPIVC--LSVMSLGAVLTTANPLNTASeiLRQiadsnpk 139
Cdd:PRK09029 26 DEVLTWQQLCARIDQLAA-GFAQQGVVEGSGVALRGKN--SPETLLayLALLQCGARVLPLNPQLPQP--LLE------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 140 lafttpELAPKIassGISIVLervedtlrVPRGLKVVGNLTEMMKKEPSG-QAVRNQVHKDDTAMLlySSGTTGRSKGVN 218
Cdd:PRK09029 94 ------ELLPSL---TLDFAL--------VLEGENTFSALTSLHLQLVEGaHAVAWQPQRLATMTL--TSGSTGLPKAAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 219 SSHGnliAHVARyiAE------PFEQpQQTFICTVPLFHTFGLlNFVLATLALGTTVVILPRFDLGEMMAAVekyraTTL 292
Cdd:PRK09029 155 HTAQ---AHLAS--AEgvlslmPFTA-QDSWLLSLPLFHVSGQ-GIVWRWLYAGATLVVRDKQPLEQALAGC-----THA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 293 ILVPPVLVTMINKADQIMKkydvsfLRTVRCGGAPLSKEVTQGFMKKypTVDVYQGYALTESngagASIESVEESRRYGA 372
Cdd:PRK09029 223 SLVPTQLWRLLDNRSEPLS------LKAVLLGGAAIPVELTEQAEQQ--GIRCWCGYGLTEM----ASTVCAKRADGLAG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 373 VGLLSCGVEARIVDpntgqvmglnqtGELWLKGPSIAKGYFRNEEeIIT---SEGWLKTGDLCYIdNDGFLFIVDRLKEL 449
Cdd:PRK09029 291 VGSPLPGREVKLVD------------GEIWLRGASLALGYWRQGQ-LVPlvnDEGWFATRDRGEW-QNGELTILGRLDNL 356
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063734905 450 IKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAyvarkpesnlcekkVIDFISKQVL 515
Cdd:PRK09029 357 FFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVA--------------VVESDSEAAV 408
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
45-499 |
9.73e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 93.48 E-value: 9.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 45 ISSQTYRGKTAFIDAATDHRISFSDLWMAVDRVADCLLhDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLN 124
Cdd:PRK12316 3063 FEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLI-ERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEY 3141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 125 TASEILRQIADSNPKLAFTTPELAPKIASSGISIVLERVEDTLrvprglkvvgnltemmkkepSGQAVRNQVHKDDTAML 204
Cdd:PRK12316 3142 PEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDENY--------------------AEANPAIRTMPENLAYV 3201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 205 LYSSGTTGRSKGVNSSHGNLIAHvARYIAEPFEQPQQTficTVPLFHTFGLLNFVL---ATLALGTTVVILPRFDLGEMM 281
Cdd:PRK12316 3202 IYTSGSTGKPKGVGIRHSALSNH-LCWMQQAYGLGVGD---RVLQFTTFSFDVFVEelfWPLMSGARVVLAGPEDWRDPA 3277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 282 AAVEKYRATTlILVPPVLVTMINKADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPtvdVYQGYALTESNGAGASI 361
Cdd:PRK12316 3278 LLVELINSEG-VDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLP---LYNLYGPTEATITVTHW 3353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 362 ESVEESRRYGAVGLLSCGVEARIVDPNtGQVMGLNQTGELWLKGPSIAKGYFrnEEEIITSEGWL-----------KTGD 430
Cdd:PRK12316 3354 QCVEEGKDAVPIGRPIANRACYILDGS-LEPVPVGALGELYLGGEGLARGYH--NRPGLTAERFVpdpfvpgerlyRTGD 3430
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063734905 431 LCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPfpdkEAGQFPMAYVARKPES 499
Cdd:PRK12316 3431 LARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVPEDEA 3495
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
198-463 |
1.66e-19 |
|
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: 91.40 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 198 KDDTAMLLYSSGTTGRSKGVNSSHGNLIaHVARYIAEPFE-QPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILP--- 273
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLV-HNMFAILNSTEwKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPtrl 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 274 ---RFDLgeMMAAVEKYRATtlILVPP-----VLVTMINkaDQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMK-----KY 340
Cdd:cd05908 184 firRPIL--WLKKASEHKAT--IVSSPnfgykYFLKTLK--PEKANDWDLSSIRMILNGAEPIDYELCHEFLDhmskyGL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 341 PTVDVYQGYALTEsNGAGASIESVEES-------RRYGAVG---------------LLSCG-----VEARIVDpNTGQVM 393
Cdd:cd05908 258 KRNAILPVYGLAE-ASVGASLPKAQSPfktitlgRRHVTHGepepevdkkdsecltFVEVGkpideTDIRICD-EDNKIL 335
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063734905 394 GLNQTGELWLKGPSIAKGYFRNEEE---IITSEGWLKTGDLCYIDNdGFLFIVDRLKELIKYKGYQVPPAELE 463
Cdd:cd05908 336 PDGYIGHIQIRGKNVTPGYYNNPEAtakVFTDDGWLKTGDLGFIRN-GRLVITGREKDIIFVNGQNVYPHDIE 407
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
199-499 |
1.60e-18 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 87.02 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 199 DDTAMLLYSSGTTGRSKGVNSSHGNLIAHvARYIAEPFEQPQQtFICTVPLFHTFGLLNFVLATLAlGTTVVIL--PR-F 275
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTAS-ADATHDRLGGPGQ-WLLALPAHHIAGLQVLVRSVIA-GSEPVELdvSAgF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 276 DLGEMMAAVEKY----RATTLilVPPVLVTMINKADQI--MKKYDvsflrTVRCGGAPLSKEVTQGfmKKYPTVDVYQGY 349
Cdd:PRK07824 112 DPTALPRAVAELgggrRYTSL--VPMQLAKALDDPAATaaLAELD-----AVLVGGGPAPAPVLDA--AAAAGINVVRTY 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 350 ALTESNGagasiesveesrryGAV--GLLSCGVEARIVDpntgqvmglnqtGELWLKGPSIAKGYfRNEEE--IITSEGW 425
Cdd:PRK07824 183 GMSETSG--------------GCVydGVPLDGVRVRVED------------GRIALGGPTLAKGY-RNPVDpdPFAEPGW 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063734905 426 LKTGDLCYIDnDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPES 499
Cdd:PRK07824 236 FRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGP 308
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
64-497 |
2.37e-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: 87.52 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 64 RISFSDLWMAVDRVADCLLhDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKlAFt 143
Cdd:cd05910 2 RLSFRELDERSDRIAQGLT-AYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPD-AF- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 144 tpelapkiassgisivlervedtLRVPRGlkvvgnltemmkkepsgqavrnqvhkDDTAMLLYSSGTTGRSKGVNSSHGN 223
Cdd:cd05910 79 -----------------------IGIPKA--------------------------DEPAAILFTSGSTGTPKGVVYRHGT 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 224 LIAHVARyIAEPFE-QPQQTFICTVPLFHTFGllnfvlatLALGTTVVILP-------RFDLGEMMAAVEKYRATTLILV 295
Cdd:cd05910 110 FAAQIDA-LRQLYGiRPGEVDLATFPLFALFG--------PALGLTSVIPDmdptrpaRADPQKLVGAIRQYGVSIVFGS 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 296 PPVLVTMINKADQIMKKydVSFLRTVRCGGAPLSKEVTQGFMKK-YPTVDVYQGYALTESNGAgASIES--VEESRRYGA 372
Cdd:cd05910 181 PALLERVARYCAQHGIT--LPSLRRVLSAGAPVPIALAARLRKMlSDEAEILTPYGATEALPV-SSIGSreLLATTTAAT 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 373 -------VGLLSCGVEARIVDPNTGQVMGLNQT--------GELWLKGPSIAKGYF-RNEEEIIT-----SEG-WLKTGD 430
Cdd:cd05910 258 sggagtcVGRPIPGVRVRIIEIDDEPIAEWDDTlelprgeiGEITVTGPTVTPTYVnRPVATALAkiddnSEGfWHRMGD 337
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063734905 431 LCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFpDKEAGQFPMAYVARKP 497
Cdd:cd05910 338 LGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV-GKPGCQLPVLCVEPLP 403
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
199-503 |
6.13e-18 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 86.37 E-value: 6.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 199 DDTAMLLYSSGTTGRSKGVNSSHGNlIAHVA-----RYIAEPFeQPQQTFICTVPLFHTFGllNFVLATLAlGTTVVILP 273
Cdd:cd17650 93 EDLAYVIYTSGTTGKPKGVMVEHRN-VAHAAhawrrEYELDSF-PVRLLQMASFSFDVFAG--DFARSLLN-GGTLVICP 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 274 ---RFDLGEMMAAVEKYRATTLILVPPVLVTMINKADQimKKYDVSFLRTVRCGG----APLSKEVTQGFMKKYPTVDvy 346
Cdd:cd17650 168 devKLDPAALYDLILKSRITLMESTPALIRPVMAYVYR--NGLDLSAMRLLIVGSdgckAQDFKTLAARFGQGMRIIN-- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 347 qGYALTEsngagASIESV--EESR-RYGAVGLLSCG-----VEARIVDPnTGQVMGLNQTGELWLKGPSIAKGYFRNEEe 418
Cdd:cd17650 244 -SYGVTE-----ATIDSTyyEEGRdPLGDSANVPIGrplpnTAMYVLDE-RLQPQPVGVAGELYIGGAGVARGYLNRPE- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 419 iITSEGWL-----------KTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQ 487
Cdd:cd17650 316 -LTAERFVenpfapgermyRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEA 394
|
330
....*....|....*.
gi 1063734905 488 FPMAYVARKPESNLCE 503
Cdd:cd17650 395 RLCAYVVAAATLNTAE 410
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
65-486 |
1.19e-17 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 85.83 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 65 ISFSDLWMAVDRVAdCLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLAFTT 144
Cdd:PRK05857 42 LRYRELVAEVGGLA-ADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 145 PElaPKIASSGISIVLERVEdTLRVPRGLKVVGNLTEMMKKEPSGQAvrnQVHKDDTAMLLYSSGTTGRSKGVNSSHGNL 224
Cdd:PRK05857 121 PG--SKMASSAVPEALHSIP-VIAVDIAAVTRESEHSLDAASLAGNA---DQGSEDPLAMIFTSGTTGEPKAVLLANRTF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 225 IAHVARYIAEPFEQ----PQQTFICTVPLFHTFGLLnFVLATLALGTTVVILPRFDLGEMMAAVEKYRATTlILVPPVLV 300
Cdd:PRK05857 195 FAVPDILQKEGLNWvtwvVGETTYSPLPATHIGGLW-WILTCLMHGGLCVTGGENTTSLLEILTTNAVATT-CLVPTLLS 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 301 TMINKADqiMKKYDVSFLRTVRCGGA-PLSKEVTqgFMKKyPTVDVYQGYALTES----------NGAGASIESveesrr 369
Cdd:PRK05857 273 KLVSELK--SANATVPSLRLVGYGGSrAIAADVR--FIEA-TGVRTAQVYGLSETgctalclptdDGSIVKIEA------ 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 370 yGAVGLLSCGVEARIVDPNTG--QVMGLNQT---GELWLKGPSIAKGYFRNEEEI--ITSEGWLKTGDLCYIDNDGFLFI 442
Cdd:PRK05857 342 -GAVGRPYPGVDVYLAATDGIgpTAPGAGPSasfGTLWIKSPANMLGYWNNPERTaeVLIDGWVNTGDLLERREDGFFYI 420
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1063734905 443 VDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAG 486
Cdd:PRK05857 421 KGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFG 464
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
182-477 |
2.91e-17 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 84.87 E-value: 2.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 182 MMKKEPSGQavrNQVHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHV--ARYIAEPFEQPQQT---FICTVPLFHTFGLL 256
Cdd:PLN02430 206 MGKENPSET---NPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVrgVDLFMEQFEDKMTHddvYLSFLPLAHILDRM 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 257 N---FVLATLALGTTvvilpRFDLGEMMAAVEKYRATTLILVPPVLVTM---INKADQ-----------IMKKYDVSF-- 317
Cdd:PLN02430 283 IeeyFFRKGASVGYY-----HGDLNALRDDLMELKPTLLAGVPRVFERIhegIQKALQelnprrrlifnALYKYKLAWmn 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 318 ---------------------------LRTVRCGGAPLSKEVTQgFMKKYPTVDVYQGYALTESNGaGASIESVEESRRY 370
Cdd:PLN02430 358 rgyshkkaspmadflafrkvkaklggrLRLLISGGAPLSTEIEE-FLRVTSCAFVVQGYGLTETLG-PTTLGFPDEMCML 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 371 GAVGLLSCGVEARIVD-PNTG-QVMGLNQTGELWLKGPSIAKGYFRNEE--EIITSEGWLKTGDLCYIDNDGFLFIVDRL 446
Cdd:PLN02430 436 GTVGAPAVYNELRLEEvPEMGyDPLGEPPRGEICVRGKCLFSGYYKNPEltEEVMKDGWFHTGDIGEILPNGVLKIIDRK 515
|
330 340 350
....*....|....*....|....*....|..
gi 1063734905 447 KELIKY-KGYQVPPAELEALLLNHPDILDAAV 477
Cdd:PLN02430 516 KNLIKLsQGEYVALEYLENVYGQNPIVEDIWV 547
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
59-477 |
3.89e-17 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 84.32 E-value: 3.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 59 AATDHRISFSDLWMAVDRVADCLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNP 138
Cdd:cd05905 9 GKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 139 KLAFTTpELAPKIASSGISIVLERVE--DTLRVPRGLKVVGNLTE-MMKKEPSGQAVRNQvhKDDTAMLLYSSGTTGRSK 215
Cdd:cd05905 89 RVALTV-EACLKGLPKKLLKSKTAAEiaKKKGWPKILDFVKIPKSkRSKLKKWGPHPPTR--DGDTAYIEYSFSSDGSLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 216 GVNSSHGNLIAHvARYIAEPFE-QPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPRFDL----GEMMAAVEKYRAT 290
Cdd:cd05905 166 GVAVSHSSLLAH-CRALKEACElYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMktnpLLWLQTLSQYKVR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 291 TLILVPPVLVTMINKADQIM---KKYDVSF--LRT--VRCGGAPlSKEVTQGFMKKYPTVDVYQGYALTE---------S 354
Cdd:cd05905 245 DAYVKLRTLHWCLKDLSSTLaslKNRDVNLssLRMcmVPCENRP-RISSCDSFLKLFQTLGLSPRAVSTEfgtrvnpfiC 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 355 NGAGASIESVE-----ESRRYGAV----------------GLLSCGVEARIVDPNTGQVMGLNQTGELWLKGPSIAKGYF 413
Cdd:cd05905 324 WQGTSGPEPSRvyldmRALRHGVVrlderdkpnslplqdsGKVLPGAQVAIVNPETKGLCKDGEIGEIWVNSPANASGYF 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 414 R---------------NEEEIITSEGWLKTGDLCYI----------DNDGFLFIVDRLKELIKYKGYQVPPAELEA-LLL 467
Cdd:cd05905 404 LldgetndtfkvfpstRLSTGITNNSYARTGLLGFLrptkctdlnvEEHDLLFVVGSIDETLEVRGLRHHPSDIEAtVMR 483
|
490
....*....|
gi 1063734905 468 NHPDILDAAV 477
Cdd:cd05905 484 VHPYRGRCAV 493
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
198-470 |
5.21e-17 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 84.01 E-value: 5.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 198 KDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVARYIAE-PFEQPQQTFICTVPLFHTFGLL--NFVLAT---------LAL 265
Cdd:PLN02387 249 PNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVvPKLGKNDVYLAYLPLAHILELAaeSVMAAVgaaigygspLTL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 266 GTTVVILPRFDLGEmmaaVEKYRATTLILVPPVL-------VTMINKADQIMKK-------------------------- 312
Cdd:PLN02387 329 TDTSNKIKKGTKGD----ASALKPTLMTAVPAILdrvrdgvRKKVDAKGGLAKKlfdiaykrrlaaiegswfgawglekl 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 313 -YDVSFLRTVR-----------CGGAPLSKEvTQGFMKKYPTVDVYQGYALTESnGAGASIESVEESRrYGAVG--LLSC 378
Cdd:PLN02387 405 lWDALVFKKIRavlggrirfmlSGGAPLSGD-TQRFINICLGAPIGQGYGLTET-CAGATFSEWDDTS-VGRVGppLPCC 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 379 GVeaRIVDPNTGQVMGLNQT---GELWLKGPSIAKGYFRNEEEiiTSE---------GWLKTGDLCYIDNDGFLFIVDRL 446
Cdd:PLN02387 482 YV--KLVSWEEGGYLISDKPmprGEIVIGGPSVTLGYFKNQEK--TDEvykvdergmRWFYTGDIGQFHPDGCLEIIDRK 557
|
330 340
....*....|....*....|....*
gi 1063734905 447 KELIKYK-GYQVPPAELEALLLNHP 470
Cdd:PLN02387 558 KDIVKLQhGEYVSLGKVEAALSVSP 582
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
55-479 |
2.04e-16 |
|
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: 82.32 E-value: 2.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 55 AFIDAATDH---RISFSDLWMAVDRVADCLLHdVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANP---LNTASE 128
Cdd:cd05943 86 AAIYAAEDGertEVTWAELRRRVARLAAALRA-LGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPdfgVPGVLD 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 129 ILRQIAdsnPKLAFTTP----------------ELAPKIASSGISIVLERV--EDTLRVPRGLKVVGnLTEMMKKEPSGQ 190
Cdd:cd05943 165 RFGQIE---PKVLFAVDaytyngkrhdvrekvaELVKGLPSLLAVVVVPYTvaAGQPDLSKIAKALT-LEDFLATGAAGE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 191 AVRNQVHKDDTAMLLYSSGTTGRSKG-VNSSHGNLIAHVARYIAEPFEQPQQTFICtvplFHTFG--LLNFVLATLALGT 267
Cdd:cd05943 241 LEFEPLPFDHPLYILYSSGTTGLPKCiVHGAGGTLLQHLKEHILHCDLRPGDRLFY----YTTCGwmMWNWLVSGLAVGA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 268 TVVIL---PRF-DLGEMMAAVEKYRAtTLILVPPVLVTMINKADQIMKK-YDVSFLRTVRCGGAPLSKE----------- 331
Cdd:cd05943 317 TIVLYdgsPFYpDTNALWDLADEEGI-TVFGTSAKYLDALEKAGLKPAEtHDLSSLRTILSTGSPLKPEsfdyvydhikp 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 332 ------------VTQGFMKKYPTVDVYQGYAltESNGAGASIESVEESRR--YGAVGLLSCgveariVDPNTGQ-VMGLN 396
Cdd:cd05943 396 dvllasisggtdIISCFVGGNPLLPVYRGEI--QCRGLGMAVEAFDEEGKpvWGEKGELVC------TKPFPSMpVGFWN 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 397 QTGelwlkGPSIAKGYFRneeeiiTSEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAA 476
Cdd:cd05943 468 DPD-----GSRYRAAYFA------KYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSL 536
|
...
gi 1063734905 477 VIP 479
Cdd:cd05943 537 VVG 539
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
192-464 |
4.37e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 81.31 E-value: 4.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 192 VRNQVHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVARYIaEPFEQPQQTFICT-VPLFHTFGLLNFVLATLaLGTTVV 270
Cdd:PRK07769 173 VPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVI-DALEGQEGDRGVSwLPFFHDMGLITVLLPAL-LGHYIT 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 271 IL--------PRFDLGEMmAAVEKYRATTLILVPpvlvtmiNKAdqimkkYDVSFLRTV-RCGGAPL-----------SK 330
Cdd:PRK07769 251 FMspaafvrrPGRWIREL-ARKPGGTGGTFSAAP-------NFA------FEHAAARGLpKDGEPPLdlsnvkgllngSE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 331 EVTQGFMKKY---------PTVDVYQGYALTESNGAGASIESVEESR-----RY---------------GAVGLLSCGVE 381
Cdd:PRK07769 317 PVSPASMRKFneafapyglPPTAIKPSYGMAEATLFVSTTPMDEEPTviyvdRDelnagrfvevpadapNAVAQVSAGKV 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 382 AR-----IVDPNTGQVMGLNQTGELWLKGPSIAKGYFRNEEEIIT--------------SEG------WLKTGDL-CYID 435
Cdd:PRK07769 397 GVsewavIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAAtfqnilksrlseshAEGapddalWVRTGDYgVYFD 476
|
330 340
....*....|....*....|....*....
gi 1063734905 436 NDgfLFIVDRLKELIKYKGYQVPPAELEA 464
Cdd:PRK07769 477 GE--LYITGRVKDLVIIDGRNHYPQDLEY 503
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
202-504 |
8.63e-16 |
|
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: 79.79 E-value: 8.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 202 AMLLYSSGTTGRSKGVNSSHGNLIAHVARYIAEPFE-QPQQTFIctvplfhtFGLLNF------VLATLALGTTVVILP- 273
Cdd:cd17644 109 AYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGItSSDRVLQ--------FASIAFdvaaeeIYVTLLSGATLVLRPe 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 274 --RFDLGEMMAAVEKYRATTLILVPPVLVTMINKADQIMKKYDvSFLRTVRCGG-APLSKEVTQGFMKKYPTVDVYQGYA 350
Cdd:cd17644 181 emRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLP-SSLRLVIVGGeAVQPELVRQWQKNVGNFIQLINVYG 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 351 LTEsngagASIESV--------EESRRYGAVGLLSCGVEARIVDPNTGQV-MGLnqTGELWLKGPSIAKGYFRNEEeiIT 421
Cdd:cd17644 260 PTE-----ATIAATvcrltqltERNITSVPIGRPIANTQVYILDENLQPVpVGV--PGELHIGGVGLARGYLNRPE--LT 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 422 SEGWL-------------KTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQF 488
Cdd:cd17644 331 AEKFIshpfnsseserlyKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKR 410
|
330
....*....|....*..
gi 1063734905 489 PMAY-VARKPESNLCEK 504
Cdd:cd17644 411 LVAYiVPHYEESPSTVE 427
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
53-493 |
2.61e-15 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 78.64 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 53 KTAFI----DAATDHRISFSDLWMAVDRVAdCLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLT------TANP 122
Cdd:PRK00174 83 KVAIIwegdDPGDSRKITYRELHREVCRFA-NALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSvvfggfSAEA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 123 LNTaseilrQIADSNPKLAFTTPE------LAP--KIASSGISIVlERVEDTLRVPR-GLKVvgNLT--------EMMKK 185
Cdd:PRK00174 162 LAD------RIIDAGAKLVITADEgvrggkPIPlkANVDEALANC-PSVEKVIVVRRtGGDV--DWVegrdlwwhELVAG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 186 EPSG-QAVRnqVHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVA---RYIaepFE-QPQQTFICTVPLF----HTFgll 256
Cdd:PRK00174 233 ASDEcEPEP--MDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAmtmKYV---FDyKDGDVYWCTADVGwvtgHSY--- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 257 nFVLATLALGTTVVIL---PRF-DLGEMMAAVEKYRATTLILVPPVLVTMINKADQIMKKYDVSFLR---TVrcgGAPLS 329
Cdd:PRK00174 305 -IVYGPLANGATTLMFegvPNYpDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSSLRllgSV---GEPIN 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 330 KE--------VTQGfmkKYPTVDVY-QgyalTESNG------AGASiesveeSRRYGAVGLLSCGVEARIVDpNTGQVMG 394
Cdd:PRK00174 381 PEawewyykvVGGE---RCPIVDTWwQ----TETGGimitplPGAT------PLKPGSATRPLPGIQPAVVD-EEGNPLE 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 395 LNQTGELWLKG--PSIAKGYFRNEEEIITS-----EGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLL 467
Cdd:PRK00174 447 GGEGGNLVIKDpwPGMMRTIYGDHERFVKTyfstfKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALV 526
|
490 500
....*....|....*....|....*.
gi 1063734905 468 NHPDILDAAVIPFPDKEAGQFPMAYV 493
Cdd:PRK00174 527 AHPKVAEAAVVGRPDDIKGQGIYAFV 552
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
63-437 |
5.67e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 77.78 E-value: 5.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 63 HRISFSDLWMAVDRVADCLLhDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANP----LNTASEILRQIADS-N 137
Cdd:PRK12582 79 RKVTYGEAKRAVDALAQALL-DLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPayslMSHDHAKLKHLFDLvK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 138 PKLAFTT--PELAPKIAS---SGISIVLervedTLRVPRGLKVVGnLTEMMKKEPSGQ--AVRNQVHKDDTAMLLYSSGT 210
Cdd:PRK12582 158 PRVVFAQsgAPFARALAAldlLDVTVVH-----VTGPGEGIASIA-FADLAATPPTAAvaAAIAAITPDTVAKYLFTSGS 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 211 TGRSKGVNSSHGNLIAHVARYIA----EPFEQPQQTfICTVPLFHTFG---LLNFVLATlalGTTVVI-----LPRFdLG 278
Cdd:PRK12582 232 TGMPKAVINTQRMMCANIAMQEQlrprEPDPPPPVS-LDWMPWNHTMGgnaNFNGLLWG---GGTLYIddgkpLPGM-FE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 279 EMMAAVEKYRATTLILVP---PVLVTMINKADQIMKKYdVSFLRTVRCGGAPLSKEVTQGfMKKYPT------VDVYQGY 349
Cdd:PRK12582 307 ETIRNLREISPTVYGNVPagyAMLAEAMEKDDALRRSF-FKNLRLMAYGGATLSDDLYER-MQALAVrttghrIPFYTGY 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 350 ALTESngAGASIESVEESRRYGAVGLLSCGVEARIVdPNtGQVMglnqtgELWLKGPSIAKGYFRNEE---EIITSEGWL 426
Cdd:PRK12582 385 GATET--APTTTGTHWDTERVGLIGLPLPGVELKLA-PV-GDKY------EVRVKGPNVTPGYHKDPEltaAAFDEEGFY 454
|
410
....*....|..
gi 1063734905 427 KTGDLC-YIDND 437
Cdd:PRK12582 455 RLGDAArFVDPD 466
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
147-478 |
6.15e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 78.29 E-value: 6.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 147 LAPKIASSGISIVL--ERVEDTLRVPRGLKVVGNLTEMMKKEPSgQAVRNQVHKDDTAMLLYSSGTTGRSKGVNSSHGNL 224
Cdd:PRK05691 1220 LAYMLADSGVELLLtqSHLLERLPQAEGVSAIALDSLHLDSWPS-QAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAAL 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 225 iahvaryiAEPfeqpqqtfictvplfhtfglLNFVLATLALGTTVVILPR----FDL--------------------GE- 279
Cdd:PRK05691 1299 --------AER--------------------LQWMQATYALDDSDVLMQKapisFDVsvwecfwplitgcrlvlagpGEh 1350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 280 -----MMAAVEKYRATTLILVPPVLVTMINKADQImkkyDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVDVYQGYALTEs 354
Cdd:PRK05691 1351 rdpqrIAELVQQYGVTTLHFVPPLLQLFIDEPLAA----ACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTE- 1425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 355 ngagASIE------SVEESRRyGAVGLLSCGVEARIVDPNTGQVMGlNQTGELWLKGPSIAKGYFRNEEeiITSEGWL-- 426
Cdd:PRK05691 1426 ----TAINvthwqcQAEDGER-SPIGRPLGNVLCRVLDAELNLLPP-GVAGELCIGGAGLARGYLGRPA--LTAERFVpd 1497
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063734905 427 ----------KTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVI 478
Cdd:PRK05691 1498 plgedgarlyRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL 1559
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
150-463 |
3.11e-14 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 75.19 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 150 KIASSGISIVLE--RVEDTLRVPRGLKVVGNLTEMMKKEPSgqAVRNQVHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAH 227
Cdd:PRK05851 103 RFAGIGVRTVLShgSHLERLRAVDSSVTVHDLATAAHTNRS--ASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 228 VARYIAEPFEQPQQTFICT-VPLFHTFGLlNFVLATLALGTTVVILPRfdlGEMMAAVEKY-------RATtLILVPPVL 299
Cdd:PRK05851 181 LRGLNARVGLDAATDVGCSwLPLYHDMGL-AFLLTAALAGAPLWLAPT---TAFSASPFRWlswlsdsRAT-LTAAPNFA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 300 VTMINKADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVDVYQG-----YALTESN--------GAGASIESVEE 366
Cdd:PRK05851 256 YNLIGKYARRVSDVDLGALRVALNGGEPVDCDGFERFATAMAPFGFDAGaaapsYGLAESTcavtvpvpGIGLRVDEVTT 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 367 S-----RRYGAVGLLSCGVEARIVDPNTGQVMGLNQTGELWLKGPSIAKGYFrnEEEIITSEGWLKTGDLCYIDNDGfLF 441
Cdd:PRK05851 336 DdgsgaRRHAVLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYL--GQAPIDPDDWFPTGDLGYLVDGG-LV 412
|
330 340
....*....|....*....|..
gi 1063734905 442 IVDRLKELIKYKGYQVPPAELE 463
Cdd:PRK05851 413 VCGRAKELITVAGRNIFPTEIE 434
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
64-430 |
3.15e-14 |
|
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: 75.16 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 64 RISFSDLWMAVDRVADCLLhDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAvltTANPLNTASEILRQIADsnpKLAFT 143
Cdd:cd05921 25 RVTYAEALRQVRAIAQGLL-DLGLSAERPLLILSGNSIEHALMALAAMYAGV---PAAPVSPAYSLMSQDLA---KLKHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 144 TPELAPKI--ASSG--ISIVLERVED-------TLRVPRGLKVVgNLTEMMKKEPSGQ--AVRNQVHKDDTAMLLYSSGT 210
Cdd:cd05921 98 FELLKPGLvfAQDAapFARALAAIFPlgtplvvSRNAVAGRGAI-SFAELAATPPTAAvdAAFAAVGPDTVAKFLFTSGS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 211 TGRSKGVNSSHGNL---IAHVARYIAEPFEQPQQtFICTVPLFHTFGLLNFVLATLALGTTVVIlprfDLGEMMAAV--E 285
Cdd:cd05921 177 TGLPKAVINTQRMLcanQAMLEQTYPFFGEEPPV-LVDWLPWNHTFGGNHNFNLVLYNGGTLYI----DDGKPMPGGfeE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 286 KYR-----ATTLILVPPVLVTMINKA---DQIMKKydvSFLRTVRC---GGAPLSKEV----------TQGFmkkypTVD 344
Cdd:cd05921 252 TLRnlreiSPTVYFNVPAGWEMLVAAlekDEALRR---RFFKRLKLmfyAGAGLSQDVwdrlqalavaTVGE-----RIP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 345 VYQGYALTESngAGASIESVEESRRYGAVGLLSCGVEARIVdPNTGQVmglnqtgELWLKGPSIAKGYFRNEE---EIIT 421
Cdd:cd05921 324 MMAGLGATET--APTATFTHWPTERSGLIGLPAPGTELKLV-PSGGKY-------EVRVKGPNVTPGYWRQPEltaQAFD 393
|
....*....
gi 1063734905 422 SEGWLKTGD 430
Cdd:cd05921 394 EEGFYCLGD 402
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
200-487 |
3.70e-14 |
|
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: 74.36 E-value: 3.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 200 DTAMLLYSSGTTGRSKGVNSSHG---NLIAHVAR-----------------YIAEPF-EQpqqtfictvplfHTFGLLNf 258
Cdd:cd17648 95 DLAYAIYTSGTTGKPKGVLVEHGsvvNLRTSLSEryfgrdngdeavlffsnYVFDFFvEQ------------MTLALLN- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 259 vlatlalGTTVVILP---RFDLGEMMAAVEKYRATTLILVPPVLvtminkadqimKKYDVS---FLRTVRCGGAPLSKEV 332
Cdd:cd17648 162 -------GQKLVVPPdemRFDPDRFYAYINREKVTYLSGTPSVL-----------QQYDLArlpHLKRVDAAGEEFTAPV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 333 TQGFMKKYPTVdVYQGYALTESNGAGASIESVEESRRYGAVGLLSCGVEARIVDPNTgQVMGLNQTGELWLKGPSIAKGY 412
Cdd:cd17648 224 FEKLRSRFAGL-IINAYGPTETTVTNHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAM-KRVPVGAVGELYLGGDGVARGY 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 413 FRNEEeiITSEGWL-------------------KTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDIL 473
Cdd:cd17648 302 LNRPE--LTAERFLpnpfqteqerargrnarlyKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVR 379
|
330
....*....|....
gi 1063734905 474 DAAVIPFPDKEAGQ 487
Cdd:cd17648 380 ECAVVAKEDASQAQ 393
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
187-450 |
5.01e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 74.59 E-value: 5.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 187 PSGQAVRNQVHkDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVARYIAEPFEQ------PQQTFICTVPLFHTFGLLNFVL 260
Cdd:PRK05850 149 PRGSDARPRDL-PSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDYFGDtggvppPDTTVVSWLPFYHDMGLVLGVC 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 261 ATLALGTTVVI------LPR----------------------FDLgemmaAVekyRATTlilvppvlvtminkaDQIMKK 312
Cdd:PRK05850 228 APILGGCPAVLtspvafLQRparwmqllasnphafsaapnfaFEL-----AV---RKTS---------------DDDMAG 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 313 YDVSFLRTVRCGgaplSKEVTQGFMKKY----------PTVdVYQGYALTE------SNGAGASIESV------------ 364
Cdd:PRK05850 285 LDLGGVLGIISG----SERVHPATLKRFadrfapfnlrETA-IRPSYGLAEatvyvaTREPGQPPESVrfdyeklsagha 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 365 EESRRYGAVGLLSCGV----EARIVDPNTGQVMGLNQTGELWLKGPSIAKGYFRNEEE--------II-----TSEG-WL 426
Cdd:PRK05850 360 KRCETGGGTPLVSYGSprspTVRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEEtertfgatLVdpspgTPEGpWL 439
|
330 340
....*....|....*....|....
gi 1063734905 427 KTGDLCYIDnDGFLFIVDRLKELI 450
Cdd:PRK05850 440 RTGDLGFIS-EGELFIVGRIKDLL 462
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
197-451 |
1.13e-13 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 73.72 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 197 HKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVA----------RYIAEpfeqpQQTFICTVPLFHTFgllNFVLATLALG 266
Cdd:PLN02861 218 QKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLstdhllkvtdRVATE-----EDSYFSYLPLAHVY---DQVIETYCIS 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 267 TTVVI-LPRFDLGEMMAAVEKYRATTLILVPPV-------LVTMINKADQIMKK-YDVSF-------------------- 317
Cdd:PLN02861 290 KGASIgFWQGDIRYLMEDVQALKPTIFCGVPRVydriytgIMQKISSGGMLRKKlFDFAYnyklgnlrkglkqeeasprl 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 318 ---------------LRTVRCGGAPLSKEVTQgFMKKYPTVDVYQGYALTESNGaGASIESVEESRRYGAVGLLSCGVEA 382
Cdd:PLN02861 370 drlvfdkikeglggrVRLLLSGAAPLPRHVEE-FLRVTSCSVLSQGYGLTESCG-GCFTSIANVFSMVGTVGVPMTTIEA 447
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063734905 383 RIVD-PNTG-QVMGLNQTGELWLKGPSIAKGYFRNEE--EIITSEGWLKTGDLCYIDNDGFLFIVDRLKELIK 451
Cdd:PLN02861 448 RLESvPEMGyDALSDVPRGEICLRGNTLFSGYHKRQDltEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFK 520
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
198-451 |
1.64e-13 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 73.13 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 198 KDDTAMLLYSSGTTGRSKGV---NSSHGNLIAHVARYIAEPFE--QPQQTFICTVPLFHTFGLL---NFVLATLALGttv 269
Cdd:PLN02614 222 KSDICTIMYTSGTTGDPKGVmisNESIVTLIAGVIRLLKSANAalTVKDVYLSYLPLAHIFDRVieeCFIQHGAAIG--- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 270 viLPRFDLGEMMAAVEKYRATTLILVPPVLVTMINKADQ------IMKK--YDVSF------------------------ 317
Cdd:PLN02614 299 --FWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKklsdggFLKKfvFDSAFsykfgnmkkgqshveasplcdklv 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 318 -----------LRTVRCGGAPLSKEVtQGFMKKYPTVDVYQGYALTESnGAGASIESVEESRRYGAVGLLSCGVEARI-- 384
Cdd:PLN02614 377 fnkvkqglggnVRIILSGAAPLASHV-ESFLRVVACCHVLQGYGLTES-CAGTFVSLPDELDMLGTVGPPVPNVDIRLes 454
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063734905 385 VDPNTGQVMGLNQTGELWLKGPSIAKGYFRNEEeiITSE----GWLKTGDLCYIDNDGFLFIVDRLKELIK 451
Cdd:PLN02614 455 VPEMEYDALASTPRGEICIRGKTLFSGYYKRED--LTKEvlidGWLHTGDVGEWQPNGSMKIIDRKKNIFK 523
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
236-501 |
2.99e-13 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 71.56 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 236 FEQPQQTFICTVPLFHTFGLLNFVLATLAlGTTVVILPRFDLGEMMAAVEKYRATTLILVPPVLVTMINKADQIMKKYdv 315
Cdd:PRK07445 156 FQLQQVNSFCVLPLYHVSGLMQFMRSFLT-GGKLVILPYKRLKSGQELPPNPSDFFLSLVPTQLQRLLQLRPQWLAQF-- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 316 sflRTVRCGGAP----LSKEVTQGFMKKYPTvdvyqgYALTESngaGASIESVEESrrygavgllscgvEARIVDPNTGQ 391
Cdd:PRK07445 233 ---RTILLGGAPawpsLLEQARQLQLRLAPT------YGMTET---ASQIATLKPD-------------DFLAGNNSSGQ 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 392 VM-------GLNQTGELWLKGPSIAKGYFRNeeeIITSEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEA 464
Cdd:PRK07445 288 VLphaqitiPANQTGNITIQAQSLALGYYPQ---ILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEA 364
|
250 260 270
....*....|....*....|....*....|....*...
gi 1063734905 465 LLLNHPDILDAAVIPFPDKEAGQFPMA-YVARKPESNL 501
Cdd:PRK07445 365 AILATGLVQDVCVLGLPDPHWGEVVTAiYVPKDPSISL 402
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
181-451 |
3.17e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 72.44 E-value: 3.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 181 EMMKKEPSGQAVRNQvHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVA----RYIAEPFeqPQQTFICTVPLFHTFGLL 256
Cdd:PTZ00342 287 DMTKNKTTNYKIQNE-DPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVplckHSIFKKY--NPKTHLSYLPISHIYERV 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 257 NFVLAtLALGTTVVILPRfDL-----------GEMMAAVEKY--RATTLIL-----VPPVLVTMINKADQIMK-KYDVSF 317
Cdd:PTZ00342 364 IAYLS-FMLGGTINIWSK-DInyfskdiynskGNILAGVPKVfnRIYTNIMteinnLPPLKRFLVKKILSLRKsNNNGGF 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 318 ---------------------LRTVRCGGAPLSKEVTQGFmKKYPTVDVYQGYALTESNGA-------GASIESVEesrr 369
Cdd:PTZ00342 442 skflegithisskikdkvnpnLEVILNGGGKLSPKIAEEL-SVLLNVNYYQGYGLTETTGPifvqhadDNNTESIG---- 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 370 ygavGLLSCGVEARIVDPNTGQVMGLNQTGELWLKGPSIAKGYFRNEEEI---ITSEGWLKTGDLCYIDNDGFLFIVDRL 446
Cdd:PTZ00342 517 ----GPISPNTKYKVRTWETYKATDTLPKGELLIKSDSIFSGYFLEKEQTknaFTEDGYFKTGDIVQINKNGSLTFLDRS 592
|
....*
gi 1063734905 447 KELIK 451
Cdd:PTZ00342 593 KGLVK 597
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
202-494 |
6.83e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 71.74 E-value: 6.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 202 AMLLYSSGTTGRSKGVNSSHGNLIAHVARYIAEPFEQPQQtfiCTVplfHtFGLLNF------VLATLALGTTVVILPR- 274
Cdd:PRK05691 2336 AYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADD---CEL---H-FYSINFdaaserLLVPLLCGARVVLRAQg 2408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 275 -FDLGEMMAAVEKYRATTLILVPPVLVTMinkADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVDVYQGYALTE 353
Cdd:PRK05691 2409 qWGAEEICQLIREQQVSILGFTPSYGSQL---AQWLAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTE 2485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 354 S---NGAGASIESVEESRRYGAVGLLSCGVEARIVDPNtgqVMGLNQ--TGELWLKGPSIAKGYFRNEEeiITSEGWL-- 426
Cdd:PRK05691 2486 TvvmPLACLAPEQLEEGAASVPIGRVVGARVAYILDAD---LALVPQgaTGELYVGGAGLAQGYHDRPG--LTAERFVad 2560
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063734905 427 ----------KTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFpDKEAGQFPMAYVA 494
Cdd:PRK05691 2561 pfaadggrlyRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGYLV 2637
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
62-501 |
1.62e-12 |
|
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: 69.38 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 62 DHRISFSDLWMAVDRVADcLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANplntaseilrqiadSNPKLa 141
Cdd:cd05939 1 DRHWTFRELNEYSNKVAN-FFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALIN--------------SNLRL- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 142 fttPELAPKIASSGISIVLERVEDTlrvprglkvvgnLTEMMKKEPSGQAVRNQvhkDDTAMLLYSSGTTGRSKGVNSSH 221
Cdd:cd05939 65 ---ESLLHCITVSKAKALIFNLLDP------------LLTQSSTEPPSQDDVNF---RDKLFYIYTSGTTGLPKAAVIVH 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 222 GNLIaHVARYIAEPFE-QPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPRFDLGEMMAAVEKYRATTLILVPPV-- 298
Cdd:cd05939 127 SRYY-RIAAGAYYAFGmRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEIcr 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 299 --LVTMINKADQimkKYDVSFLRtvrcgGAPLSKEVTQGFMKKYPTVDVYQGYALTESNgagASIESVEesrryGAVGll 376
Cdd:cd05939 206 ylLAQPPSEEEQ---KHNVRLAV-----GNGLRPQIWEQFVRRFGIPQIGEFYGATEGN---SSLVNID-----NHVG-- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 377 SCGVEARI-----------VDPNTGQVM----GL------NQTGElwLKGPSIAK-------GYFR---NEEEIITSEgw 425
Cdd:cd05939 268 ACGFNSRIlpsvypirlikVDEDTGELIrdsdGLcipcqpGEPGL--LVGKIIQNdplrrfdGYVNegaTNKKIARDV-- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 426 LKTGDLCYIDND-------GFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAV----IPFPDKEAGqfpMAYVA 494
Cdd:cd05939 344 FKKGDSAFLSGDvlvmdelGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygveVPGVEGRAG---MAAIV 420
|
....*..
gi 1063734905 495 RkPESNL 501
Cdd:cd05939 421 D-PERKV 426
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
203-497 |
2.71e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 68.52 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 203 MLLYSSGTTGRSKGVNSSHGNLIAHVARYIAEpFEQPQ-QTFICTVPLFHTFGLLNFVLATLALGTTVVIL----PRFDL 277
Cdd:PRK08308 105 LLQYSSGTTGEPKLIRRSWTEIDREIEAYNEA-LNCEQdETPIVACPVTHSYGLICGVLAALTRGSKPVIItnknPKFAL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 278 gemmAAVEKYRATTLILVPPVLVTMINkadqiMKKYDVSFLRtVRCGGAPLSKEVtqgFMK-KYPTVDVYQGYALTESnG 356
Cdd:PRK08308 184 ----NILRNTPQHILYAVPLMLHILGR-----LLPGTFQFHA-VMTSGTPLPEAW---FYKlRERTTYMMQQYGCSEA-G 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 357 AGASIESVEESrrygavglLSCGVEARIVDPNTGQvmGLNQTGELWLKgpsiakgyfRNEEEIitsegwlKTGDLCYIDN 436
Cdd:PRK08308 250 CVSICPDMKSH--------LDLGNPLPHVSVSAGS--DENAPEEIVVK---------MGDKEI-------FTKDLGYKSE 303
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063734905 437 DGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQ-FPMAYVARKP 497
Cdd:PRK08308 304 RGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGErVKAKVISHEE 365
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
64-430 |
1.06e-11 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 67.21 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 64 RISFSDLWMAVDRVADCLLhDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANP----LNTASEILRQIADS-NP 138
Cdd:PRK08180 69 RLTYAEALERVRAIAQALL-DRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPayslVSQDFGKLRHVLELlTP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 139 KLAFTT--PELAPKIASsgisIVLERVED-TLRVPRGLKVVGNLTEMMKKEPSG--QAVRNQVHKDDTAMLLYSSGTTGR 213
Cdd:PRK08180 148 GLVFADdgAAFARALAA----VVPADVEVvAVRGAVPGRAATPFAALLATPPTAavDAAHAAVGPDTIAKFLFTSGSTGL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 214 SKGVNSSHGNLIAhVARYIAE--PF--EQPQqTFICTVPLFHTFG-LLNFVLAtLALGTTVVIlprfDLGEMMAA----- 283
Cdd:PRK08180 224 PKAVINTHRMLCA-NQQMLAQtfPFlaEEPP-VLVDWLPWNHTFGgNHNLGIV-LYNGGTLYI----DDGKPTPGgfdet 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 284 VEKYR--ATTLIL-VP---PVLVTMInKADQIMKKydvSFLRTVRC---GGAPLSKEV----------TQG----FMKky 340
Cdd:PRK08180 297 LRNLReiSPTVYFnVPkgwEMLVPAL-ERDAALRR---RFFSRLKLlfyAGAALSQDVwdrldrvaeaTCGerirMMT-- 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 341 ptvdvyqGYALTESngAGASIESVEESRRYGAVGLLSCGVEARIVdPNTGQVmglnqtgELWLKGPSIAKGYFRNEE--- 417
Cdd:PRK08180 371 -------GLGMTET--APSATFTTGPLSRAGNIGLPAPGCEVKLV-PVGGKL-------EVRVKGPNVTPGYWRAPElta 433
|
410
....*....|...
gi 1063734905 418 EIITSEGWLKTGD 430
Cdd:PRK08180 434 EAFDEEGYYRSGD 446
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
81-479 |
1.26e-11 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 67.38 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 81 LLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTtanPLNTA---SEILRQIADSNPKLAFTTPELAPKIASSGIS 157
Cdd:PRK10252 499 LLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWL---PLDTGypdDRLKMMLEDARPSLLITTADQLPRFADVPDL 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 158 IVLervedTLRVPRGlkvvgnltemmkkePSGQAVRNQVHKDDTAMLLYSSGTTGRSKGVnsshgnLIAHVA-------- 229
Cdd:PRK10252 576 TSL-----CYNAPLA--------------PQGAAPLQLSQPHHTAYIIFTSGSTGRPKGV------MVGQTAivnrllwm 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 230 --RYIAEPFEQPQQTFICT--VPLFHtfgllnFVLATLAlGTTVVILP----RfDLGEMMAAVEKYRATTLILVPPVLVT 301
Cdd:PRK10252 631 qnHYPLTADDVVLQKTPCSfdVSVWE------FFWPFIA-GAKLVMAEpeahR-DPLAMQQFFAEYGVTTTHFVPSMLAA 702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 302 MINKADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKY---------PT---VDV--YQGYALTESNGAGASIesvees 367
Cdd:PRK10252 703 FVASLTPEGARQSCASLRQVFCSGEALPADLCREWQQLTgaplhnlygPTeaaVDVswYPAFGEELAAVRGSSV------ 776
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 368 rrygAVGLLSCGVEARIVDpNTGQVMGLNQTGELWLKGPSIAKGYFRNEEeiITSEGWL-----------KTGDLCYIDN 436
Cdd:PRK10252 777 ----PIGYPVWNTGLRILD-ARMRPVPPGVAGDLYLTGIQLAQGYLGRPD--LTASRFIadpfapgermyRTGDVARWLD 849
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1063734905 437 DGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIP 479
Cdd:PRK10252 850 DGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHA 892
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
372-464 |
2.61e-11 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 65.92 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 372 AVGLLSCGVEAR-----IVDPNTGQVMGLNQTGELWLKGPSIAKGYF-RNEEEIIT---------SEG-----------W 425
Cdd:PRK12476 398 AVAHVSCGQVARsqwavIVDPDTGAELPDGEVGEIWLHGDNIGRGYWgRPEETERTfgaklqsrlAEGshadgaaddgtW 477
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1063734905 426 LKTGDL-CYIdnDGFLFIVDRLKELIKYKGYQVPPAELEA 464
Cdd:PRK12476 478 LRTGDLgVYL--DGELYITGRIADLIVIDGRNHYPQDIEA 515
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
65-477 |
1.09e-10 |
|
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: 63.65 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 65 ISFSDLWMAVDRVADCLLHDVGIRRGDVVLVLSPnTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSnpklaftt 144
Cdd:cd17654 17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDR-GTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKC-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 145 pelapkiassGISIVLERvedtlrvprglKVVGNLTEMMKKEPSGQAVRnqvHKDDTAMLLYSSGTTGRSKGVnsshgnL 224
Cdd:cd17654 88 ----------HVSYLLQN-----------KELDNAPLSFTPEHRHFNIR---TDECLAYVIHTSGTTGTPKIV------A 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 225 IAHvaRYIAEPFEQPQQTFICT------VPLFHTF--GLLNFVLAtLALGTTVVILP---RFDLGEMMAAVEKYRATTLI 293
Cdd:cd17654 138 VPH--KCILPNIQHFRSLFNITsedilfLTSPLTFdpSVVEIFLS-LSSGATLLIVPtsvKVLPSKLADILFKRHRITVL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 294 LVPPVLVTMINKA---DQIMKKydVSFLRTVRCGGAPL-SKEVTQGFMKKYPTVDVYQGYALTE-SNGAGASIESVEESR 368
Cdd:cd17654 215 QATPTLFRRFGSQsikSTVLSA--TSSLRVLALGGEPFpSLVILSSWRGKGNRTRIFNIYGITEvSCWALAYKVPEEDSP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 369 RYGAVGLLSCGVEARivdpntgQVMGLNQTGELWLKGpsIAKGYFRNEEEIITSEGWLKTGDLCYIdNDGFLFIVDRLKE 448
Cdd:cd17654 293 VQLGSPLLGTVIEVR-------DQNGSEGTGQVFLGG--LNRVCILDDEVTVPKGTMRATGDFVTV-KDGELFFLGRKDS 362
|
410 420
....*....|....*....|....*....
gi 1063734905 449 LIKYKGYQVPPAELEALLLNHPDILDAAV 477
Cdd:cd17654 363 QIKRRGKRINLDLIQQVIESCLGVESCAV 391
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
461-514 |
1.19e-10 |
|
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: 57.55 E-value: 1.19e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1063734905 461 ELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKVIDFISKQV 514
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREEL 54
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
207-478 |
7.56e-10 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 60.93 E-value: 7.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 207 SSGTTGRSKGVNSSHgNLIAHVARYIAEPFE----QPQQTFICTVPlFHTF-GLLNFVLATLALGTTVVilpRFDLG--- 278
Cdd:COG1541 91 SSGTTGKPTVVGYTR-KDLDRWAELFARSLRaagvRPGDRVQNAFG-YGLFtGGLGLHYGAERLGATVI---PAGGGnte 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 279 ---EMMaavEKYRATTLILVPPVLVTMINKADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPtVDVYQGYALTESn 355
Cdd:COG1541 166 rqlRLM---QDFGPTVLVGTPSYLLYLAEVAEEEGIDPRDLSLKKGIFGGEPWSEEMRKEIEERWG-IKAYDIYGLTEV- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 356 GAGASIESVE-------ESRRYgavgllscgVEarIVDPNTGQVMGLNQTGELwlkgpsiakgyfrneeeIITS---EGW 425
Cdd:COG1541 241 GPGVAYECEAqdglhiwEDHFL---------VE--IIDPETGEPVPEGEEGEL-----------------VVTTltkEAM 292
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063734905 426 ----LKTGDLCYIDND----G-----FLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVI 478
Cdd:COG1541 293 plirYRTGDLTRLLPEpcpcGrthprIGRILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQI 358
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
64-332 |
1.22e-09 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 60.58 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 64 RISFSDLWMAVDRVADCLLhDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANP---LNTASEILRQIAdsnPKL 140
Cdd:PRK03584 114 ELSWAELRRQVAALAAALR-ALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPdfgVQGVLDRFGQIE---PKV 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 141 AFTTP----------------ELAPKIASSGISIVLERVEDTLRVPRGLKVVGnLTEMMKKEPSGQAVRNQVHKDDTAML 204
Cdd:PRK03584 190 LIAVDgyryggkafdrrakvaELRAALPSLEHVVVVPYLGPAAAAAALPGALL-WEDFLAPAEAAELEFEPVPFDHPLWI 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 205 LYSSGTTGRSKGVNSSHGN-LIAHVAryiaepfE-------QPQQTFIctvpLFHTFG--LLNFVLATLALGTTVVIlpr 274
Cdd:PRK03584 269 LYSSGTTGLPKCIVHGHGGiLLEHLK-------ElglhcdlGPGDRFF----WYTTCGwmMWNWLVSGLLVGATLVL--- 334
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063734905 275 FD-------LGEMMAAVEKYRATTLILVPPVLvTMINKAD-QIMKKYDVSFLRTVRCGGAPLSKEV 332
Cdd:PRK03584 335 YDgspfypdPNVLWDLAAEEGVTVFGTSAKYL-DACEKAGlVPGETHDLSALRTIGSTGSPLPPEG 399
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
199-478 |
2.89e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 60.18 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 199 DDTAMLLYSSGTTGRSKGV------------------NSSHGNLIAHVAryiaepfeqpQQTFICTVPLFhtfgllnfvL 260
Cdd:PRK05691 3869 DNLAYVIYTSGSTGLPKGVmveqrgmlnnqlskvpylALSEADVIAQTA----------SQSFDISVWQF---------L 3929
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 261 ATLALGTTVVILPR---FDLGEMMAAVEKYRATTLILVPPVLVTMINKADQIMkkydvSFLRTVRCGGAPLSKEVTQGFM 337
Cdd:PRK05691 3930 AAPLFGARVEIVPNaiaHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQAL-----DGLRWMLPTGEAMPPELARQWL 4004
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 338 KKYPTVDVYQGYALTESNGAGASIESVEESRR--YGAVGLLScgvearivDPNTGQVMG-------LNQTGELWLKGPSI 408
Cdd:PRK05691 4005 QRYPQIGLVNAYGPAECSDDVAFFRVDLASTRgsYLPIGSPT--------DNNRLYLLDealelvpLGAVGELCVAGTGV 4076
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 409 AKGYFRNEEEIITS----------EGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVI 478
Cdd:PRK05691 4077 GRGYVGDPLRTALAfvphpfgapgERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVA 4156
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
207-471 |
2.38e-04 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 43.38 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 207 SSGTTGRSKGVNSSHGNL---IAHVARYI----AEPFEQPQQTFIctvplFHTF-GLLNFVLATLALGTTVVilPRFDLG 278
Cdd:cd05913 86 SSGTTGKPTVVGYTKNDLdvwAELVARCLdaagVTPGDRVQNAYG-----YGLFtGGLGFHYGAERLGALVI--PAGGGN 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 279 -EMM-AAVEKYRATTLILVPPVLVTMINKADQIMKKYDVSFLRTVRCGGAPLSkEVTQGFMKKYPTVDVYQGYALTESNG 356
Cdd:cd05913 159 tERQlQLIKDFGPTVLCCTPSYALYLAEEAEEEGIDPRELSLKVGIFGAEPWT-EEMRKRIERRLGIKAYDIYGLTEIIG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734905 357 AGASIESVEEsrryGAVGLLSCGVEARIVDPNTGQVMGLNQTGELwlkgpsiakgyfrneeeIITS---EGWL----KTG 429
Cdd:cd05913 238 PGVAFECEEK----DGLHIWEDHFIPEIIDPETGEPVPPGEVGEL-----------------VFTTltkEAMPliryRTR 296
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1063734905 430 DL---------CYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPD 471
Cdd:cd05913 297 DItrllpgpcpCGRTHRRIDRITGRSDDMLIIRGVNVFPSQIEDVLLKIPG 347
|
|
| |
