|
Name |
Accession |
Description |
Interval |
E-value |
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
21-536 |
0e+00 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 829.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 21 LPKDPNTSLVSFLFrnSSSYPSKLAIADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVT 100
Cdd:cd05904 1 LPTDLPLDSVSFLF--ASAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 101 AIGGVFTTANPLYTVNEVSKQIKDSNPKIIISVNQLFDKIKGFDLPVVLLGSKDTVEIPPGSNSKIlsfdnvmelsEPVS 180
Cdd:cd05904 79 SLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLASLALPVVLLDSAEFDSLSFSDLLFE----------ADEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 181 EYPFVEIKQSDTAALLYSSGTTGTSKGVELTHGNFIAASLMVTMDQDLMGEYHGVFLCFLPMFHVFGLAVITYSQLQRGN 260
Cdd:cd05904 149 EPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 261 ALVSMARFELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECGRNIPNVLLMQGY 340
Cdd:cd05904 229 TVVVMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 341 GMTETCGIVSVEDPRLGKR-NSGSAGMLAPGVEAQIVSVETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKSW 419
Cdd:cd05904 309 GMTESTGVVAMCFAPEKDRaKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGW 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 420 VHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQD 499
Cdd:cd05904 389 LHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDE 468
|
490 500 510
....*....|....*....|....*....|....*..
gi 15234634 500 IQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:cd05904 469 IMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
45-532 |
0e+00 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 577.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 45 AIADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKD 124
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 125 SNPKIIISVNQLFDKIKGFdlpVVLLGSKDTVEIPPGSNSKILSFDNVMELSEPVSEYPFVEIKQ---SDTAALLYSSGT 201
Cdd:cd05911 81 SKPKVIFTDPDGLEKVKEA---AKELGPKDKIIVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKdgkDDTAAILYSSGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 202 TGTSKGVELTHGNFIAASLMVTMDQDLMGEYHGVFLCFLPMFHVFGLaVITYSQLQRGNALVSMARFELELVLKNIEKFR 281
Cdd:cd05911 158 TGLPKGVCLSHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYHIYGL-FTTLASLLNGATVIIMPKFDSELFLDLIEKYK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 282 VTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECGRNIPNVLLMQGYGMTETCGIVSVedPRLGKRNS 361
Cdd:cd05911 237 ITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTV--NPDGDDKP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 362 GSAGMLAPGVEAQIVSVETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKSWVHTGDLGYFNEDGNLYVVDRIK 441
Cdd:cd05911 315 GSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 442 ELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQKFIAKQVAPYKRLR-RVSFI 520
Cdd:cd05911 395 ELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYKQLRgGVVFV 474
|
490
....*....|..
gi 15234634 521 SLVPKSAAGKIL 532
Cdd:cd05911 475 DEIPKSASGKIL 486
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
11-544 |
0e+00 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 552.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 11 IYRSLRPTLVLPKdpNTSLVSFLFRNSSSYPSKLAIADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSY 90
Cdd:PLN02246 9 IFRSKLPDIYIPN--HLPLHDYCFERLSEFSDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 91 QFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIIISVNQLFDKIKGF----DLPVVllgskdTVEIPPgsnSKI 166
Cdd:PLN02246 87 EFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLaeddGVTVV------TIDDPP---EGC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 167 LSFDNVMELSEpvSEYPFVEIKQSDTAALLYSSGTTGTSKGVELTHGnfiaaSLMVTMDQDLMGE-----YHG--VFLCF 239
Cdd:PLN02246 158 LHFSELTQADE--NELPEVEISPDDVVALPYSSGTTGLPKGVMLTHK-----GLVTSVAQQVDGEnpnlyFHSddVILCV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 240 LPMFHVFGLAVITYSQLQRGNALVSMARFELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPL 319
Cdd:PLN02246 231 LPMFHIYSLNSVLLCGLRVGAAILIMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 320 GKDLMEECGRNIPNVLLMQGYGMTETCGIVSV-----EDPRLGKrnSGSAGMLAPGVEAQIVSVETGKSQPPNQQGEIWV 394
Cdd:PLN02246 311 GKELEDAFRAKLPNAVLGQGYGMTEAGPVLAMclafaKEPFPVK--SGSCGTVVRNAELKIVDPETGASLPRNQPGEICI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 395 RGPNMMKGYLNNPQATKETIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPF 474
Cdd:PLN02246 389 RGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPM 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 475 PDEEAGEVPIAFVVRSPNSSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRRELvqqvRSKM 544
Cdd:PLN02246 469 KDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDL----RAKL 534
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
10-536 |
3.90e-171 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 495.90 E-value: 3.90e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 10 GIYRSLRPTLVLPKDPNTSLVSFLFrNSSSYPSKLAIADSDTGDSLTFSQLKSAVARLAHGFHR-LGIRKNDVVLIFAPN 88
Cdd:PLN02574 23 GIYSSKHPPVPLPSDPNLDAVSFIF-SHHNHNGDTALIDSSTGFSISYSELQPLVKSMAAGLYHvMGVRQGDVVLLLLPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 89 SYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIIISVNQLFDKIKGFDLPVVLL---GSKDTVEIPPGSNSK 165
Cdd:PLN02574 102 SVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSPLGVPVIGVpenYDFDSKRIEFPKFYE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 166 ILSFDnvmelSEPVSEYPfveIKQSDTAALLYSSGTTGTSKGVELTHGNFIAA-SLMVTMDQDLMgEYHG---VFLCFLP 241
Cdd:PLN02574 182 LIKED-----FDFVPKPV---IKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMvELFVRFEASQY-EYPGsdnVYLAALP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 242 MFHVFGLAVITYSQLQRGNALVSMARFELELVLKNIEKFRVTHLWVVPPVFLALSKQS-IVKKFDLSSLKYIGSGAAPLG 320
Cdd:PLN02574 253 MFHIYGLSLFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAkGVCGEVLKSLKQVSCGAAPLS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 321 KDLMEECGRNIPNVLLMQGYGMTETCGIVSVEDPRLGKRNSGSAGMLAPGVEAQIVSVETGKSQPPNQQGEIWVRGPNMM 400
Cdd:PLN02574 333 GKFIQDFVQTLPHVDFIQGYGMTESTAVGTRGFNTEKLSKYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVM 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 401 KGYLNNPQATKETIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAG 480
Cdd:PLN02574 413 KGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECG 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15234634 481 EVPIAFVVRSPNSSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:PLN02574 493 EIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRREL 548
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
29-543 |
1.60e-159 |
|
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: 461.97 E-value: 1.60e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 29 LVSFLFRNSSSYPSKLAIADSDTgdSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTT 108
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGR--RLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 109 ANPLYTVNEVSKQIKDSNPKIIIsvnqlfdkikgfdlpvvllgskdtveippgsnskilsfdnvmelsepvseypfveik 188
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALV--------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 189 qsdTAALLYSSGTTGTSKGVELTHGNFIAASLMVTMDQDLmgEYHGVFLCFLPMFHVFGLAVITYSQLQRGNALVSMARF 268
Cdd:COG0318 102 ---TALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGL--TPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRF 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 269 ELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECgRNIPNVLLMQGYGMTETCGI 348
Cdd:COG0318 177 DPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERF-EERFGVRIVEGYGLTETSPV 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 349 VSVEDPRLGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIdKKSWVHTGDLGYF 428
Cdd:COG0318 256 VTVNPEDPGERRPGSVGRPLPGVEVRIVD-EDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRL 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 429 NEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQKFIAKQV 508
Cdd:COG0318 334 DEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERL 413
|
490 500 510
....*....|....*....|....*....|....*
gi 15234634 509 APYKRLRRVSFISLVPKSAAGKILRRELVQQVRSK 543
Cdd:COG0318 414 ARYKVPRRVEFVDELPRTASGKIDRRALRERYAAG 448
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
11-544 |
1.35e-149 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 440.18 E-value: 1.35e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 11 IYRSLRPTLVLPKDpnTSLVSFLFRNSSSYPSKLAIADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSY 90
Cdd:PLN02330 14 IFRSRYPSVPVPDK--LTLPDFVLQDAELYADKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 91 QFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIIISVNQLFDKIKGFDLPVVLLGSKdtveippgSNSKILSFD 170
Cdd:PLN02330 92 EYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGLGLPVIVLGEE--------KIEGAVNWK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 171 NVMELSEPVSE-YPFVEIKQSDTAALLYSSGTTGTSKGVELTHGNFIA--ASLMVTMDQDLMGEYhgVFLCFLPMFHVFG 247
Cdd:PLN02330 164 ELLEAADRAGDtSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVAnlCSSLFSVGPEMIGQV--VTLGLIPFFHIYG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 248 LAVITYSQLQRGNALVSMARFELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKY--IGSGAAPLGKDLME 325
Cdd:PLN02330 242 ITGICCATLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLqaIMTAAAPLAPELLT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 326 ECGRNIPNVLLMQGYGMTE-TCGIVSVEDPRLG----KRNSgsAGMLAPGVEAQIVSVETGKSQPPNQQGEIWVRGPNMM 400
Cdd:PLN02330 322 AFEAKFPGVQVQEAYGLTEhSCITLTHGDPEKGhgiaKKNS--VGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVM 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 401 KGYLNNPQATKETIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAG 480
Cdd:PLN02330 400 QGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAG 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15234634 481 EVPIAFVVRSPNSSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRRELVQQVRSKM 544
Cdd:PLN02330 480 EIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLSIN 543
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
29-537 |
2.38e-141 |
|
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: 416.19 E-value: 2.38e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 29 LVSFLFRNSSSYPSKLAIadSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTT 108
Cdd:cd05936 1 LADLLEEAARRFPDKTAL--IFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 109 ANPLYTVNEVSKQIKDSNPKIIISvnqlfdkikgfdlpvvllgskdtveippgsnskILSFDNVMELSEPVSEYPfvEIK 188
Cdd:cd05936 79 LNPLYTPRELEHILNDSGAKALIV---------------------------------AVSFTDLLAAGAPLGERV--ALT 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 189 QSDTAALLYSSGTTGTSKGVELTHGNFIAASLMVTMDQDLMGEYHGVFLCFLPMFHVFGLAVITYSQLQRGNALVSMARF 268
Cdd:cd05936 124 PEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRF 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 269 ELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECGRnIPNVLLMQGYGMTETCGI 348
Cdd:cd05936 204 RPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEE-LTGVPIVEGYGLTETSPV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 349 VSVeDPRLGKRNSGSAGMLAPGVEAQIVSVEtGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIdKKSWVHTGDLGYF 428
Cdd:cd05936 283 VAV-NPLDGPRKPGSIGIPLPGTEVKIVDDD-GEELPPGEVGELWVRGPQVMKGYWNRPEETAEAF-VDGWLRTGDIGYM 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 429 NEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQKFIAKQV 508
Cdd:cd05936 360 DEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQL 439
|
490 500
....*....|....*....|....*....
gi 15234634 509 APYKRLRRVSFISLVPKSAAGKILRRELV 537
Cdd:cd05936 440 AGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
25-540 |
4.51e-136 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 404.57 E-value: 4.51e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 25 PNTsLVSFLFRNSSSYPSKLAIadSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGG 104
Cdd:PRK06187 5 PLT-IGRILRHGARKHPDKEAV--YFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 105 VFTTANPLYTVNEVSKQIKDSNPKIIIsVNQ----LFDKIKGfDLP----VVLLGSKDTVEIPPGSnskiLSFDNVMElS 176
Cdd:PRK06187 82 VLHPINIRLKPEEIAYILNDAEDRVVL-VDSefvpLLAAILP-QLPtvrtVIVEGDGPAAPLAPEV----GEYEELLA-A 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 177 EPvSEYPFVEIKQSDTAALLYSSGTTGTSKGVELTHGNFIAASLMVTM-----DQDlmgeyhgVFLCFLPMFHVFGLAVi 251
Cdd:PRK06187 155 AS-DTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAwlklsRDD-------VYLVIVPMFHVHAWGL- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 252 TYSQLQRGNALVSMARFELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECGR-- 329
Cdd:PRK06187 226 PYLALMAGAKQVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEkf 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 330 NIPnvlLMQGYGMTETCGIVSV--EDPRLGKRNS--GSAGMLAPGVEAQIVSvETGKSQPPN--QQGEIWVRGPNMMKGY 403
Cdd:PRK06187 306 GID---LVQGYGMTETSPVVSVlpPEDQLPGQWTkrRSAGRPLPGVEARIVD-DDGDELPPDggEVGEIIVRGPWLMQGY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 404 LNNPQATKETIDKkSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVP 483
Cdd:PRK06187 382 WNRPEATAETIDG-GWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERP 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15234634 484 IAFVVRSPNSSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRRELVQQV 540
Cdd:PRK06187 461 VAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQY 517
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
33-533 |
4.33e-129 |
|
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: 383.88 E-value: 4.33e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 33 LFRNSSSYPSKLAIADSDTgdSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPL 112
Cdd:cd17631 1 LRRRARRHPDRTALVFGGR--SLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 113 YTVNEVSKQIKDSNPKIIISvnqlfdkikgfdlpvvllgskdtveippgsnskilsfdnvmelsepvseypfveikqsDT 192
Cdd:cd17631 79 LTPPEVAYILADSGAKVLFD----------------------------------------------------------DL 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 193 AALLYSSGTTGTSKGVELTHGNFIAASLMVTMDQDLmgEYHGVFLCFLPMFHVFGLAVITYSQLQRGNALVSMARFELEL 272
Cdd:cd17631 101 ALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDL--GPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPET 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 273 VLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECGRNipNVLLMQGYGMTETCGIVSVE 352
Cdd:cd17631 179 VLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQAR--GVKFVQGYGMTETSPGVTFL 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 353 DPRLGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIdKKSWVHTGDLGYFNEDG 432
Cdd:cd17631 257 SPEDHRRKLGSAGRPVFFVEVRIVD-PDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 433 NLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQKFIAKQVAPYK 512
Cdd:cd17631 335 YLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLARYK 414
|
490 500
....*....|....*....|.
gi 15234634 513 RLRRVSFISLVPKSAAGKILR 533
Cdd:cd17631 415 IPKSVEFVDALPRNATGKILK 435
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
28-536 |
7.57e-128 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 383.49 E-value: 7.57e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 28 SLVSFLFRNSSSYPSKLAIADSDTgdSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFT 107
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGDQ--RLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 108 TANPLYTVNEVSKQIKDSNPKIIISVNQLFDKIKGFDLPVVLLGSKDTVEIPPG--SNSKILSFDNVMELSEPvsEYPFV 185
Cdd:PRK07656 84 PLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICETEEDdpHTEKMKTFTDFLAAGDP--AERAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 186 EIKQSDTAALLYSSGTTGTSKGVELTHGNFIAASlmvtmdqDLMGEYHGV-----FLCFLPMFHVFGLAVITYSQLQRGN 260
Cdd:PRK07656 162 EVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNA-------ADWAEYLGLtegdrYLAANPFFHVFGYKAGVNAPLMRGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 261 ALVSMARFELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECGRNIPNVLLMQGY 340
Cdd:PRK07656 235 TILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVLTGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 341 GMTETCGIVSV---EDPRlgKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKK 417
Cdd:PRK07656 315 GLSEASGVTTFnrlDDDR--KTVAGTIGTAIAGVENKIVN-ELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDAD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 418 SWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITE 497
Cdd:PRK07656 392 GWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTE 471
|
490 500 510
....*....|....*....|....*....|....*....
gi 15234634 498 QDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:PRK07656 472 EELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
33-447 |
6.17e-127 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 377.42 E-value: 6.17e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 33 LFRNSSSYPSKLAIaDSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPL 112
Cdd:pfam00501 1 LERQAARTPDKTAL-EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 113 YTVNEVSKQIKDSNPK-IIISVNQLFDKIKGFDLPVVLLGSKDTVEIPPGSNSKILSFdnvMELSEPVSEYPFVEIKQSD 191
Cdd:pfam00501 80 LPAEELAYILEDSGAKvLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPE---EAKPADVPPPPPPPPDPDD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 192 TAALLYSSGTTGTSKGVELTHGNFIA-ASLMVTMDQDLMGEY-HGVFLCFLPMFHVFGLAVITYSQLQRGNALVSMARFE 269
Cdd:pfam00501 157 LAYIIYTSGTTGKPKGVMLTHRNLVAnVLSIKRVRPRGFGLGpDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 270 L---ELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECgRNIPNVLLMQGYGMTETC 346
Cdd:pfam00501 237 AldpAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRF-RELFGGALVNGYGLTETT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 347 GIVSVEDPRLGKRNS-GSAGMLAPGVEAQIVSVETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKSWVHTGDL 425
Cdd:pfam00501 316 GVVTTPLPLDEDLRSlGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDL 395
|
410 420
....*....|....*....|..
gi 15234634 426 GYFNEDGNLYVVDRIKELIKYK 447
Cdd:pfam00501 396 GRRDEDGYLEIVGRKKDQIKLG 417
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
38-538 |
1.06e-126 |
|
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: 381.10 E-value: 1.06e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 38 SSYPSKLAIADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNE 117
Cdd:cd17642 28 ASVPGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 118 VSKQIKDSNPKIIISVNQLFDKIkgfdlpvvlLGSKDTVEIPpgsnSKILSFDNVMELSEPVSEYPFVEI---------- 187
Cdd:cd17642 108 LDHSLNISKPTIVFCSKKGLQKV---------LNVQKKLKII----KTIIILDSKEDYKGYQCLYTFITQnlppgfneyd 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 188 -------KQSDTAALLYSSGTTGTSKGVELTHGNFIA---ASLMVTMDQDLMGEYhgVFLCFLPMFHVFG-LAVITYsqL 256
Cdd:cd17642 175 fkppsfdRDEQVALIMNSSGSTGLPKGVQLTHKNIVArfsHARDPIFGNQIIPDT--AILTVIPFHHGFGmFTTLGY--L 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 257 QRGNALVSMARFELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECGRNIPNVLL 336
Cdd:cd17642 251 ICGFRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 337 MQGYGMTETCGIVSVEDPrlGKRNSGSAGMLAPGVEAQIVSVETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDK 416
Cdd:cd17642 331 RQGYGLTETTSAILITPE--GDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 417 KSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSIT 496
Cdd:cd17642 409 DGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMT 488
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 15234634 497 EQDIQKFIAKQVAPYKRLR-RVSFISLVPKSAAGKILRRELVQ 538
Cdd:cd17642 489 EKEVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
191-532 |
1.16e-121 |
|
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: 361.22 E-value: 1.16e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 191 DTAALLYSSGTTGTSKGVELTHGNFIAASLMvtMDQDLMGEYHGVFLCFLPMFHVFGLAVITYSqLQRGNALVSMARFEL 270
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAA--LAASGGLTEGDVFLSTLPLFHIGGLFGLLGA-LLAGGTVVLLPKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 271 ELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECgRNIPNVLLMQGYGMTETCGIVS 350
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERF-EEAPGIKLVNGYGLTETGGTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 351 VEDPRLGKRNSGSAGMLAPGVEAQIVSVETGKsQPPNQQGEIWVRGPNMMKGYLNNPQATKETiDKKSWVHTGDLGYFNE 430
Cdd:cd04433 157 TGPPDDDARKPGSVGRPVPGVEVRIVDPDGGE-LPPGEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 431 DGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQKFIAKQVAP 510
Cdd:cd04433 235 DGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAP 314
|
330 340
....*....|....*....|..
gi 15234634 511 YKRLRRVSFISLVPKSAAGKIL 532
Cdd:cd04433 315 YKVPRRVVFVDALPRTASGKID 336
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
41-538 |
5.76e-110 |
|
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: 336.59 E-value: 5.76e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 41 PSKLAIADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSK 120
Cdd:cd05926 1 PDAPALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 121 QIKDSNPKIIISVNQLFDKI----KGFDLPVVLLGSKDTVEIPPGSNSKI--LSFDNVMELSEPVSeypfveiKQSDTAA 194
Cdd:cd05926 81 YLADLGSKLVLTPKGELGPAsraaSKLGLAILELALDVGVLIRAPSAESLsnLLADKKNAKSEGVP-------LPDDLAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 195 LLYSSGTTGTSKGVELTHGNFIAASLMVTmdqdlmGEYHGVF----LCFLPMFHVFGLAVITYSQLQRGNALVSMARFEL 270
Cdd:cd05926 154 ILHTSGTTGRPKGVPLTHRNLAASATNIT------NTYKLTPddrtLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 271 ELVLKNIEKFRVTHLWVVPP---VFLALSKQSIVKKfdLSSLKYIGSGAAPLGKDLMEECGR--NIPnVLlmQGYGMTET 345
Cdd:cd05926 228 STFWPDVRDYNATWYTAVPTihqILLNRPEPNPESP--PPKLRFIRSCSASLPPAVLEALEAtfGAP-VL--EAYGMTEA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 346 CGIVSVEDPRLGKRNSGSAGmLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKSWVHTGDL 425
Cdd:cd05926 303 AHQMTSNPLPPGPRKPGSVG-KPVGVEVRILD-EDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 426 GYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQKFIA 505
Cdd:cd05926 381 GYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCR 460
|
490 500 510
....*....|....*....|....*....|...
gi 15234634 506 KQVAPYKRLRRVSFISLVPKSAAGKILRRELVQ 538
Cdd:cd05926 461 KHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
32-536 |
7.16e-110 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 338.62 E-value: 7.16e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 32 FLFRNSSSYPSKLA-IADSDTGD--SLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTT 108
Cdd:COG0365 14 CLDRHAEGRGDKVAlIWEGEDGEerTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 109 ANPLYTVNEVSKQIKDSNPKIIISVNQLFDKIKGFDLP---------------VVLLGSKDTVEIPPGsnskILSFDNVM 173
Cdd:COG0365 94 VFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKekvdealeelpslehVIVVGRTGADVPMEG----DLDWDELL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 174 ELSEPvsEYPFVEIKQSDTAALLYSSGTTGTSKGVELTHGNFIAASLMvtmdqdlMGEYH------GVFLCFLPMFHVFG 247
Cdd:COG0365 170 AAASA--EFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAAT-------TAKYVldlkpgDVFWCTADIGWATG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 248 LAVITYSQLQRGNALV----SMARFELELVLKNIEKFRVTHLWVVPPVFLALSKQ--SIVKKFDLSSLKYIGSGAAPLGK 321
Cdd:COG0365 241 HSYIVYGPLLNGATVVlyegRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAgdEPLKKYDLSSLRLLGSAGEPLNP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 322 DLMEECGRNIpNVLLMQGYGMTETCGIVS----VEDPRLgkrnsGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRG- 396
Cdd:COG0365 321 EVWEWWYEAV-GVPIVDGWGQTETGGIFIsnlpGLPVKP-----GSMGKPVPGYDVAVVD-EDGNPVPPGEEGELVIKGp 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 397 -PNMMKGYLNNPQATKETI--DKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIP 473
Cdd:COG0365 394 wPGMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVG 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15234634 474 FPDEEAGEVPIAFVVRSPNSSITE---QDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:COG0365 474 VPDEIRGQVVKAFVVLKPGVEPSDelaKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
54-536 |
3.16e-107 |
|
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: 327.51 E-value: 3.16e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 54 SLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKiiisv 133
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAK----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 134 nqlfdkikgfdlpVVLLGSKdtveippgsnskilsfdnvmelsepvseypfveikQSDTAALLYSSGTTGTSKGVELTHG 213
Cdd:cd05935 76 -------------VAVVGSE-----------------------------------LDDLALIPYTSGTTGLPKGCMHTHF 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 214 NFIAASLMVTMDQDLMGEyhGVFLCFLPMFHVFGLAVITYSQLQRGNALVSMARFELELVLKNIEKFRVTHLWVVPPVFL 293
Cdd:cd05935 108 SAAANALQSAVWTGLTPS--DVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 294 ALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECgRNIPNVLLMQGYGMTETCGIVSVEDPRLGKRNSgsAGMLAPGVEA 373
Cdd:cd05935 186 DLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKL-LKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQC--LGIP*FGVDA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 374 QIVSVETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKE---TIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQ 450
Cdd:cd05935 263 RVIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEEsfiEIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFK 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 451 VAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSP--NSSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAA 528
Cdd:cd05935 343 VWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPeyRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSAS 422
|
....*...
gi 15234634 529 GKILRREL 536
Cdd:cd05935 423 GKILWRLL 430
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
21-544 |
2.32e-101 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 316.13 E-value: 2.32e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 21 LPKD---PNTSLVSFLFRNSSSYPSKLAIADSDTgdSLTFSQLKSAVARLAhGF--HRLGIRKNDVVLIFAPNSYQFPLC 95
Cdd:PRK08314 1 LPKSltlPETSLFHNLEVSARRYPDKTAIVFYGR--AISYRELLEEAERLA-GYlqQECGVRKGDRVLLYMQNSPQFVIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 96 FLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIIISVNQLFDKIK----GFDLPVVLLGS-------KDTVEIPPGSNS 164
Cdd:PRK08314 78 YYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVApavgNLRLRHVIVAQysdylpaEPEIAVPAWLRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 165 KI----LSFDNVMELSEPVSEY---PFVEIKQSDTAALLYSSGTTGTSKGVELTHG----NFIAASLMVTMDQDlmgeyh 233
Cdd:PRK08314 158 EPplqaLAPGGVVAWKEALAAGlapPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRtvmaNAVGSVLWSNSTPE------ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 234 GVFLCFLPMFHVFGLAVITYSQLQRGNALVSMARFELELVLKNIEKFRVTHlWVVPPV----FLAlskQSIVKKFDLSSL 309
Cdd:PRK08314 232 SVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMPRWDREAAARLIERYRVTH-WTNIPTmvvdFLA---SPGLAERDLSSL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 310 KYIGSGAAPL----GKDLMEECGrnipnVLLMQGYGMTETCGIVSVEDPRLGKRNSgsAGMLAPGVEAQIVSVETGKSQP 385
Cdd:PRK08314 308 RYIGGGGAAMpeavAERLKELTG-----LDYVEGYGLTETMAQTHSNPPDRPKLQC--LGIPTFGVDARVIDPETLEELP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 386 PNQQGEIWVRGPNMMKGYLNNPQATKE---TIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVS 462
Cdd:PRK08314 381 PGEVGEIVVHGPQVFKGYWNRPEATAEafiEIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYK 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 463 HPDILDAVVIPFPDEEAGEVPIAFVVRSPNS--SITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRRELVQQV 540
Cdd:PRK08314 461 HPAIQEACVIATPDPRRGETVKAVVVLRPEArgKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQE 540
|
....
gi 15234634 541 RSKM 544
Cdd:PRK08314 541 KARA 544
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
24-479 |
1.07e-98 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 310.88 E-value: 1.07e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 24 DPNTSLVSFLFRNSSSYPSKLAIADSDTGD--SLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTA 101
Cdd:COG1022 8 PPADTLPDLLRRRAARFPDRVALREKEDGIwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 102 IGGVFTtanPLY---TVNEVSKQIKDSNPKIIISVNQ-LFDKIKGF--DLP----VVLLGskdtvEIPPGSNSKILSFDN 171
Cdd:COG1022 88 AGAVTV---PIYptsSAEEVAYILNDSGAKVLFVEDQeQLDKLLEVrdELPslrhIVVLD-----PRGLRDDPRLLSLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 172 VMELSEPVSEYPFVE-----IKQSDTAALLYSSGTTGTSKGVELTHGNFIAASLMVtMDQDLMGEyHGVFLCFLPMFHVF 246
Cdd:COG1022 160 LLALGREVADPAELEarraaVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARAL-LERLPLGP-GDRTLSFLPLAHVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 247 GLaVITYSQLQRGnALVSMARfELELVLKNIEKFRVTHLWVVPPVF--------LALSKQSIVKK--FDL---------- 306
Cdd:COG1022 238 ER-TVSYYALAAG-ATVAFAE-SPDTLAEDLREVKPTFMLAVPRVWekvyagiqAKAEEAGGLKRklFRWalavgrryar 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 307 --------------------------------SSLKYIGSGAAPLGKDLmEECGRNIpNVLLMQGYGMTETCGIVSVEdp 354
Cdd:COG1022 315 arlagkspslllrlkhaladklvfsklrealgGRLRFAVSGGAALGPEL-ARFFRAL-GIPVLEGYGLTETSPVITVN-- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 355 RLGKRNSGSAGMLAPGVEAQIvsvetgksqppNQQGEIWVRGPNMMKGYLNNPQATKETIDKKSWVHTGDLGYFNEDGNL 434
Cdd:COG1022 391 RPGDNRIGTVGPPLPGVEVKI-----------AEDGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFL 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 435 YVVDRIKELI-----KYkgfqVAPAELEGLLVSHPDILDAVVI----PF------PDEEA 479
Cdd:COG1022 460 RITGRKKDLIvtsggKN----VAPQPIENALKASPLIEQAVVVgdgrPFlaalivPDFEA 515
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
32-543 |
3.02e-93 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 295.79 E-value: 3.02e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 32 FLFRNSSSYPSKLAIadSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANP 111
Cdd:PRK06710 29 YVEQMASRYPEKKAL--HFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 112 LYTVNEVSKQIKDSNPKIIISVNQLFDKIKGFDLP-----VVLLGSKDTVEIP-----PGSNSKILSFDNVMELSEPVSE 181
Cdd:PRK06710 107 LYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSAtkiehVIVTRIADFLPFPknllyPFVQKKQSNLVVKVSESETIHL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 182 YPFVEIK-----------QSDTAALLYSSGTTGTSKGVELTHGNFIAASLMVTMDQDLMGEYHGVFLCFLPMFHVFGLAV 250
Cdd:PRK06710 187 WNSVEKEvntgvevpcdpENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEEVVLGVLPFFHVYGMTA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 251 ITYSQLQRGNALVSMARFELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECGRn 330
Cdd:PRK06710 267 VMNLSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFET- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 331 IPNVLLMQGYGMTETCGiVSVEDPRLGKRNSGSAGMLAPGVEAQIVSVETGKSQPPNQQGEIWVRGPNMMKGYLNNPQAT 410
Cdd:PRK06710 346 VTGGKLVEGYGLTESSP-VTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEET 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 411 KETIdKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRS 490
Cdd:PRK06710 425 AAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLK 503
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 15234634 491 PNSSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRRELVQQVRSK 543
Cdd:PRK06710 504 EGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEKRK 556
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
41-541 |
3.92e-92 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 290.33 E-value: 3.92e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 41 PSKLAIADSDTgdSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSK 120
Cdd:PRK03640 16 PDRTAIEFEEK--KVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLW 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 121 QIKDSNPKIIISVNQLFDKIKGfdlpvvlLGSKDTVEIPPGSNSKIlsfdnvmelsEPVSEYPFveikqSDTAALLYSSG 200
Cdd:PRK03640 94 QLDDAEVKCLITDDDFEAKLIP-------GISVKFAELMNGPKEEA----------EIQEEFDL-----DEVATIMYTSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 201 TTGTSKGVELTHGN--FIAASLMVTM---DQDlmgeyhgVFLCFLPMFHVFGLAVITYSqLQRGNALVSMARFELELVLK 275
Cdd:PRK03640 152 TTGKPKGVIQTYGNhwWSAVGSALNLgltEDD-------CWLAAVPIFHISGLSILMRS-VIYGMRVVLVEKFDAEKINK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 276 NIEKFRVTHLWVVPpVFLalskQSIVKKFDL----SSLKYIGSGAAPLGKDLMEECG-RNIPnvlLMQGYGMTETCGIVS 350
Cdd:PRK03640 224 LLQTGGVTIISVVS-TML----QRLLERLGEgtypSSFRCMLLGGGPAPKPLLEQCKeKGIP---VYQSYGMTETASQIV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 351 VEDPRLGKRNSGSAGmlAPGVEAQIVSVETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIdKKSWVHTGDLGYFNE 430
Cdd:PRK03640 296 TLSPEDALTKLGSAG--KPLFPCELKIEKDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 431 DGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSpnSSITEQDIQKFIAKQVAP 510
Cdd:PRK03640 373 EGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKS--GEVTEEELRHFCEEKLAK 450
|
490 500 510
....*....|....*....|....*....|.
gi 15234634 511 YKRLRRVSFISLVPKSAAGKILRRELVQQVR 541
Cdd:PRK03640 451 YKVPKRFYFVEELPRNASGKLLRHELKQLVE 481
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
25-539 |
2.11e-91 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 291.13 E-value: 2.11e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 25 PNTSLVSFLFRNSSSYPSKLAIadSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGG 104
Cdd:PRK05605 30 GDTTLVDLYDNAVARFGDRPAL--DFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 105 VFTTANPLYTVNEVSKQIKDSNPKIIIsvnqLFDKIKGF------DLPVVLLGSKDTVE-------------IPP----- 160
Cdd:PRK05605 108 VVVEHNPLYTAHELEHPFEDHGARVAI----VWDKVAPTverlrrTTPLETIVSVNMIAampllqrlalrlpIPAlrkar 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 161 ----GSNSKILSFDNVMELSEP----VSEYPfvEIKQSDTAALLYSSGTTGTSKGVELTHGNFIAASLMVTMDQDLMGEY 232
Cdd:PRK05605 184 aaltGPAPGTVPWETLVDAAIGgdgsDVSHP--RPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVPGLGDG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 233 HGVFLCFLPMFHVFGLA-VITYSQLQRGnALVSMARFELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKY 311
Cdd:PRK05605 262 PERVLAALPMFHAYGLTlCLTLAVSIGG-ELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRN 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 312 IGSGAAPLGKDLMEECgRNIPNVLLMQGYGMTETCGIVsVEDPRLGKRNSGSAGMLAPGVEAQIVSVET-GKSQPPNQQG 390
Cdd:PRK05605 341 AFSGAMALPVSTVELW-EKLTGGLLVEGYGLTETSPII-VGNPMSDDRRPGYVGVPFPDTEVRIVDPEDpDETMPDGEEG 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 391 EIWVRGPNMMKGYLNNPQATKETIdKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAV 470
Cdd:PRK05605 419 ELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAA 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15234634 471 VIPFPDEEAGEVPIAFVVRSPNSSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRRElVQQ 539
Cdd:PRK05605 498 VVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRRE-VRE 565
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
54-538 |
1.88e-90 |
|
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: 283.47 E-value: 1.88e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 54 SLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSnpkiiisv 133
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDS-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 134 nqlfdkikgfdlpvvllgskdtveippgsnskilsfdnvmelsepvseypfvEIKQSDTAALLYSSGTTGTSKGVELTHG 213
Cdd:cd05912 73 ----------------------------------------------------DVKLDDIATIMYTSGTTGKPKGVQQTFG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 214 N--FIAASLMVTM---DQDlmgeyhgVFLCFLPMFHVFGLAVITYSqLQRGNALVSMARFELELVLKNIEKFRVTHLWVV 288
Cdd:cd05912 101 NhwWSAIGSALNLgltEDD-------NWLCALPLFHISGLSILMRS-VIYGMTVYLVDKFDAEQVLHLINSGKVTIISVV 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 289 PPVFlalskQSIVKKFDL---SSLKYIGSGAAPLGKDLMEECG-RNIPnvlLMQGYGMTETCGIVSVEDPRLGKRNSGSA 364
Cdd:cd05912 173 PTML-----QRLLEILGEgypNNLRCILLGGGPAPKPLLEQCKeKGIP---VYQSYGMTETCSQIVTLSPEDALNKIGSA 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 365 GMLAPGVEAQIVSvetgKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIdKKSWVHTGDLGYFNEDGNLYVVDRIKELI 444
Cdd:cd05912 245 GKPLFPVELKIED----DGQPPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLI 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 445 KYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRspNSSITEQDIQKFIAKQVAPYKRLRRVSFISLVP 524
Cdd:cd05912 320 ISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVS--ERPISEEELIAYCSEKLAKYKVPKKIYFVDELP 397
|
490
....*....|....
gi 15234634 525 KSAAGKILRRELVQ 538
Cdd:cd05912 398 RTASGKLLRHELKQ 411
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
24-539 |
6.19e-89 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 283.36 E-value: 6.19e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 24 DPNTSLVSFLFRNSSS-YPSKLAIADSDTgdSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAI 102
Cdd:PRK08316 7 RARRQTIGDILRRSARrYPDKTALVFGDR--SWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 103 GGVFTTANPLYTVNEVSKQIKDSNPKIIISVNQLFDKIKG--FDLPVVLLGSkDTVEIPPGSNSKILSFDNvMELSEPVS 180
Cdd:PRK08316 85 GAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAalALLPVDTLIL-SLVLGGREAPGGWLDFAD-WAEAGSVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 181 EyPFVEIKQSDTAALLYSSGTTGTSKGVELTHGNFIA--ASLMVTMDqdlMGEyHGVFLCFLPMFHVFGLAVITYSQLQR 258
Cdd:PRK08316 163 E-PDVELADDDLAQILYTSGTESLPKGAMLTHRALIAeyVSCIVAGD---MSA-DDIPLHALPLYHCAQLDVFLGPYLYV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 259 GNALVSMARFELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECGRNIPNVLLMQ 338
Cdd:PRK08316 238 GATNVILDAPDPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERLPGLRFYN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 339 GYGMTETCGIVSVEDPRLGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIdKKS 418
Cdd:PRK08316 318 CYGQTEIAPLATVLGPEEHLRRPGSAGRPVLNVETRVVD-DDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF-RGG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 419 WVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQ 498
Cdd:PRK08316 396 WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTED 475
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 15234634 499 DIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRRELVQQ 539
Cdd:PRK08316 476 ELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRER 516
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
32-531 |
7.66e-85 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 273.61 E-value: 7.66e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 32 FLFRNSSSYPSKLAIADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANP 111
Cdd:PRK08315 21 LLDRTAARYPDREALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 112 LYTVNEVSKQIKDSNPKIIISVNQLFD--------------------KIKGFDLP----VVLLGSkdtvEIPPGsnskIL 167
Cdd:PRK08315 101 AYRLSELEYALNQSGCKALIAADGFKDsdyvamlyelapelatcepgQLQSARLPelrrVIFLGD----EKHPG----ML 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 168 SFDNVMELSEPVSEYPFVEIKQS----DTAALLYSSGTTGTSKGVELTHGN------FIAASLMVTmDQDLmgeyhgvfL 237
Cdd:PRK08315 173 NFDELLALGRAVDDAELAARQATldpdDPINIQYTSGTTGFPKGATLTHRNilnngyFIGEAMKLT-EEDR--------L 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 238 CF-LPMFHVFG-----LAVITysqlqRGNALVSMA-RFELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLK 310
Cdd:PRK08315 244 CIpVPLYHCFGmvlgnLACVT-----HGATMVYPGeGFDPLATLAAVEEERCTALYGVPTMFIAELDHPDFARFDLSSLR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 311 Y-IGSGA---APLGKDLMEECgrNIPNVLLmqGYGMTETCGIV---SVEDPrLGKRNSgSAGMLAPGVEAQIVSVETGKS 383
Cdd:PRK08315 319 TgIMAGSpcpIEVMKRVIDKM--HMSEVTI--AYGMTETSPVStqtRTDDP-LEKRVT-TVGRALPHLEVKIVDPETGET 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 384 QPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSH 463
Cdd:PRK08315 393 VPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTH 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15234634 464 PDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKI 531
Cdd:PRK08315 473 PKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKI 540
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
56-536 |
2.82e-84 |
|
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: 271.04 E-value: 2.82e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 56 TFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIII---S 132
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFvdrD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 133 VNQLFDKIKGfDLP----VVLLGSKDtvEIPPGSNSKILSFDNVMELSEPvsEYPFVEIKQSDTAALLYSSGTTGTSKGV 208
Cdd:cd12119 107 FLPLLEAIAP-RLPtvehVVVMTDDA--AMPEPAGVGVLAYEELLAAESP--EYDWPDFDENTAAAICYTSGTTGNPKGV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 209 ELTHGNFIAASLMVTMdQDLMGEYHG-VFLCFLPMFHV--FGLAvitYSQLQRGNALVSMARF-ELELVLKNIEKFRVTH 284
Cdd:cd12119 182 VYSHRSLVLHAMAALL-TDGLGLSESdVVLPVVPMFHVnaWGLP---YAAAMVGAKLVLPGPYlDPASLAELIEREGVTF 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 285 LWVVPPVFLALSKQSIVKKFDLSSLK--YIGSGAAPLGkdLMEECGRNIpnVLLMQGYGMTETCGIVSVEDPRLGKRNSG 362
Cdd:cd12119 258 AAGVPTVWQGLLDHLEANGRDLSSLRrvVIGGSAVPRS--LIEAFEERG--VRVIHAWGMTETSPLGTVARPPSEHSNLS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 363 ---------SAGMLAPGVEAQIVSVEtGKSQP--PNQQGEIWVRGPNMMKGYLNNPQATKEtIDKKSWVHTGDLGYFNED 431
Cdd:cd12119 334 edeqlalraKQGRPVPGVELRIVDDD-GRELPwdGKAVGELQVRGPWVTKSYYKNDEESEA-LTEDGWLRTGDVATIDED 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 432 GNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQKFIAKQVAPY 511
Cdd:cd12119 412 GYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLADKVAKW 491
|
490 500
....*....|....*....|....*
gi 15234634 512 KRLRRVSFISLVPKSAAGKILRREL 536
Cdd:cd12119 492 WLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
41-543 |
8.53e-83 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 266.34 E-value: 8.53e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 41 PSKLAIADSDtgDSLTFSQLKSAVARLAHGF-HRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVS 119
Cdd:PRK06839 16 PDRIAIITEE--EEMTYKQLHEYVSKVAAYLiYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 120 KQIKDSNPKIIISVnqlfdkiKGFDLPVVLLGSKDTVEIPpgsnskiLSFDNVMELSEpVSEYPFVEIKQSDTAALLYSS 199
Cdd:PRK06839 94 FQLKDSGTTVLFVE-------KTFQNMALSMQKVSYVQRV-------ISITSLKEIED-RKIDNFVEKNESASFIICYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 200 GTTGTSKGVELTHGNFIAASLMVTMDQDLMGeyHGVFLCFLPMFHVFGLAVITYSQLQRGNALVSMARFELELVLKNIEK 279
Cdd:PRK06839 159 GTTGKPKGAVLTQENMFWNALNNTFAIDLTM--HDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTKALSMIEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 280 FRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECGRNipNVLLMQGYGMTETCGIV---SVEDPRl 356
Cdd:PRK06839 237 HKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDR--GFLFGQGFGMTETSPTVfmlSEEDAR- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 357 gkRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIdKKSWVHTGDLGYFNEDGNLYV 436
Cdd:PRK06839 314 --RKVGSIGKPVLFCDYELID-ENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 437 VDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQKFIAKQVAPYKRLRR 516
Cdd:PRK06839 390 VGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKE 469
|
490 500
....*....|....*....|....*..
gi 15234634 517 VSFISLVPKSAAGKILRRELVQQVRSK 543
Cdd:PRK06839 470 IVFLKELPKNATGKIQKAQLVNQLKSR 496
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
45-538 |
3.20e-80 |
|
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: 257.99 E-value: 3.20e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 45 AIADSDTGDSLTFSQLKSAVARLAHGFHRLG-IRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIK 123
Cdd:cd05941 2 RIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 124 DSNPKIIIsvnqlfdkikgfdlpvvllgskdtveippgsnskilsfdnvmelsepvseypfveikqsDTAALLYSSGTTG 203
Cdd:cd05941 82 DSEPSLVL-----------------------------------------------------------DPALILYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 204 TSKGVELTHGNfIAAslMVTMDQDLMgEY--HGVFLCFLPMFHVFGLAVITYSQLQRGNALVSMARFELELVLKNIEKFR 281
Cdd:cd05941 103 RPKGVVLTHAN-LAA--NVRALVDAW-RWteDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRLMPS 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 282 VTHLWVVPPVFLALSKQ--------SIVKKFDLSSLKYIGSGAAPLGKDLMEECGRNIPNVLLmQGYGMTETCGIVSVed 353
Cdd:cd05941 179 ITVFMGVPTIYTRLLQYyeahftdpQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLL-ERYGMTEIGMALSN-- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 354 PRLGKRNSGSAGMLAPGVEAQIVSVETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKSWVHTGDLGYFNEDGN 433
Cdd:cd05941 256 PLDGERRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGY 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 434 LYVVDRIK-ELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNS-SITEQDIQKFIAKQVAPY 511
Cdd:cd05941 336 YWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAaALSLEELKEWAKQRLAPY 415
|
490 500
....*....|....*....|....*..
gi 15234634 512 KRLRRVSFISLVPKSAAGKILRRELVQ 538
Cdd:cd05941 416 KRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
52-539 |
4.17e-80 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 261.51 E-value: 4.17e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 52 GDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIII 131
Cdd:PRK06178 56 GHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 132 SVNQLfdkikgfdLPVV-------------------LLGSKDTVEIPPGSNSKILSFDNVMEL----SEPVSEYPFVEIK 188
Cdd:PRK06178 136 ALDQL--------APVVeqvraetslrhvivtsladVLPAEPTLPLPDSLRAPRLAAAGAIDLlpalRACTAPVPLPPPA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 189 QSDTAALLYSSGTTGTSKGVELTHGNFI---AASLMVTmdqdLMGEYHGVFLCFLPMFHV----FGLAVITYSqlqrGNA 261
Cdd:PRK06178 208 LDALAALNYTGGTTGMPKGCEHTQRDMVytaAAAYAVA----VVGGEDSVFLSFLPEFWIagenFGLLFPLFS----GAT 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 262 LVSMARFELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIG--SGAAPLGKDLMEECgRNIPNVLLMQG 339
Cdd:PRK06178 280 LVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQVRvvSFVKKLNPDYRQRW-RALTGSVLAEA 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 340 -YGMTET-------CGIvSVEDPRLgKRNSGSAGMLAPGVEAQIVSVETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATK 411
Cdd:PRK06178 359 aWGMTEThtcdtftAGF-QDDDFDL-LSQPVFVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATA 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 412 ETIdKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSP 491
Cdd:PRK06178 437 EAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKP 515
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 15234634 492 NSSITEQDIQKFIAKQVAPYKrLRRVSFISLVPKSAAGKILRRELVQQ 539
Cdd:PRK06178 516 GADLTAAALQAWCRENMAVYK-VPEIRIVDALPMTATGKVRKQDLQAL 562
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
52-542 |
5.60e-80 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 260.48 E-value: 5.60e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 52 GDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIII 131
Cdd:PRK07786 40 GNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 132 SVNQLFDKIKGFDLPVVLLgskDTVEIPPG-SNSKILSFDNVmeLSEPVSEYPFVEIKQSDTAALLYSSGTTGTSKGVEL 210
Cdd:PRK07786 120 TEAALAPVATAVRDIVPLL---STVVVAGGsSDDSVLGYEDL--LAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 211 THGNFIAASLMV--TMDQDLMgeyHGVFLCFLPMFHVFGL-AVITYSQLQRGNALVSMARFELELVLKNIEKFRVTHLWV 287
Cdd:PRK07786 195 THANLTGQAMTClrTNGADIN---SDVGFVGVPLFHIAGIgSMLPGLLLGAPTVIYPLGAFDPGQLLDVLEAEKVTGIFL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 288 VPPVFLALSKQSIVKKFDLSsLKYIGSGAAPLGKDLMEECGRNIPNVLLMQGYGMTETCGIVSVEDPRLGKRNSGSAGML 367
Cdd:PRK07786 272 VPAQWQAVCAEQQARPRDLA-LRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSPVTCMLLGEDAIRKLGSVGKV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 368 APGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKkSWVHTGDLGYFNEDGNLYVVDRIKELIKYK 447
Cdd:PRK07786 351 IPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMIISG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 448 GFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFV-VRSPNSSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKS 526
Cdd:PRK07786 429 GENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAaVRNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRN 508
|
490
....*....|....*.
gi 15234634 527 AAGKILRRELVQQVRS 542
Cdd:PRK07786 509 PAGKVLKTELRERYGA 524
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
24-543 |
1.35e-77 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 254.59 E-value: 1.35e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 24 DPNTSLVSfLFRNS-SSYPSKLAIADsdTGDSLTFSQL----KSAVARLAHGfhrLGIRKNDVVLIFAPNSYQFPLCFLA 98
Cdd:PRK08974 20 DRYQSLVD-MFEQAvARYADQPAFIN--MGEVMTFRKLeersRAFAAYLQNG---LGLKKGDRVALMMPNLLQYPIALFG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 99 VTAIGGVFTTANPLYTVNEVSKQIKDSNPKIIISVNQL---FDKIKgFDLP---VVLLGSKDTVEIPPG----------- 161
Cdd:PRK08974 94 ILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFahtLEKVV-FKTPvkhVILTRMGDQLSTAKGtlvnfvvkyik 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 162 ------------SNSKILSFDNVMELSEPvseypfvEIKQSDTAALLYSSGTTGTSKGVELTHGNFIA--------ASLM 221
Cdd:PRK08974 173 rlvpkyhlpdaiSFRSALHKGRRMQYVKP-------ELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLAnleqakaaYGPL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 222 VTMDQDLMgeyhgvfLCFLPMFHVFGLAV--ITYSQLQRGNALVSMARfELELVLKNIEKFRVTHLWVVPPVFLALSKQS 299
Cdd:PRK08974 246 LHPGKELV-------VTALPLYHIFALTVncLLFIELGGQNLLITNPR-DIPGFVKELKKYPFTAITGVNTLFNALLNNE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 300 IVKKFDLSSLKYIGSGAAPLGKDLMEECgRNIPNVLLMQGYGMTETCGIVSVeDPRLGKRNSGSAGMLAPGVEAQIVSvE 379
Cdd:PRK08974 318 EFQELDFSSLKLSVGGGMAVQQAVAERW-VKLTGQYLLEGYGLTECSPLVSV-NPYDLDYYSGSIGLPVPSTEIKLVD-D 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 380 TGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIdKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGL 459
Cdd:PRK08974 395 DGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 460 LVSHPDILDAVVIPFPDEEAGEVPIAFVVRSpNSSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRRELVQQ 539
Cdd:PRK08974 474 VMLHPKVLEVAAVGVPSEVSGEAVKIFVVKK-DPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
|
....
gi 15234634 540 VRSK 543
Cdd:PRK08974 553 ARAK 556
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
40-531 |
1.22e-76 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 252.00 E-value: 1.22e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 40 YPSKLAIADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVS 119
Cdd:PRK12583 31 FPDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 120 KQIKDSNPKIIIS---------VNQLFDKIKGF-----------DLP----VVLLGSKDtveiPPGsnskILSFDNVMEL 175
Cdd:PRK12583 111 YALGQSGVRWVICadafktsdyHAMLQELLPGLaegqpgalaceRLPelrgVVSLAPAP----PPG----FLAWHELQAR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 176 SEPVSEYPFVEIKQS----DTAALLYSSGTTGTSKGVELTHGNFIAASLMVTmdqDLMGEYHGVFLCF-LPMFHVFGLAV 250
Cdd:PRK12583 183 GETVSREALAERQASldrdDPINIQYTSGTTGFPKGATLSHHNILNNGYFVA---ESLGLTEHDRLCVpVPLYHCFGMVL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 251 ITYSQLQRGNALVSMA-RFELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAP----LGKDLME 325
Cdd:PRK12583 260 ANLGCMTVGACLVYPNeAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPcpieVMRRVMD 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 326 ECgrNIPNVLLmqGYGMTETCGIV---SVEDPrLGKRNSgSAGMLAPGVEAQIVSVEtGKSQPPNQQGEIWVRGPNMMKG 402
Cdd:PRK12583 340 EM--HMAEVQI--AYGMTETSPVSlqtTAADD-LERRVE-TVGRTQPHLEVKVVDPD-GATVPRGEIGELCTRGYSVMKG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 403 YLNNPQATKETIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEV 482
Cdd:PRK12583 413 YWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEE 492
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 15234634 483 PIAFVVRSPNSSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKI 531
Cdd:PRK12583 493 IVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKV 541
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
21-536 |
6.49e-76 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 250.32 E-value: 6.49e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 21 LPKDPNTSLVSFLFRNSSSYPSKLAIadSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVT 100
Cdd:PRK07059 17 IDASQYPSLADLLEESFRQYADRPAF--ICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 101 AIGGVFTTANPLYTVNEVSKQIKDSNPKIII-------SVNQLFDKIkgfDLPVV-------LLGSKDTV---------- 156
Cdd:PRK07059 95 RAGYVVVNVNPLYTPRELEHQLKDSGAEAIVvlenfatTVQQVLAKT---AVKHVvvasmgdLLGFKGHIvnfvvrrvkk 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 157 EIPPGSNSKILSFDNVMELSEPVSEYPfVEIKQSDTAALLYSSGTTGTSKGVELTHGNFIAAslMVTMDQDLMGEY---- 232
Cdd:PRK07059 172 MVPAWSLPGHVRFNDALAEGARQTFKP-VKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVAN--VLQMEAWLQPAFekkp 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 233 ---HGVFLCFLPMFHVFGLAVITYSQLQRG--NALVSMARfELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLS 307
Cdd:PRK07059 249 rpdQLNFVCALPLYHIFALTVCGLLGMRTGgrNILIPNPR-DIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 308 SLKY-IGSGAA---PLGKDLMEECGRNIpnvllMQGYGMTETCGIVSVeDPRLGKRNSGSAGMLAPGVEAQIVSvETGKS 383
Cdd:PRK07059 328 KLIVaNGGGMAvqrPVAERWLEMTGCPI-----TEGYGLSETSPVATC-NPVDATEFSGTIGLPLPSTEVSIRD-DDGND 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 384 QPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSH 463
Cdd:PRK07059 401 LPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASH 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15234634 464 PDILDAVVIPFPDEEAGEVPIAFVVRSpNSSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:PRK07059 481 PGVLEVAAVGVPDEHSGEAVKLFVVKK-DPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
54-479 |
2.56e-75 |
|
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: 245.58 E-value: 2.56e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 54 SLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTtanPLYTVNEVSKQ---IKDSNPKII 130
Cdd:cd05907 5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPV---PIYPTSSAEQIayiLNDSEAKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 131 IsvnqlfdkikgfdlpvvllgskdtVEIPpgsnskilsfdnvmelsepvseypfveikqSDTAALLYSSGTTGTSKGVEL 210
Cdd:cd05907 82 F------------------------VEDP------------------------------DDLATIIYTSGTTGRPKGVML 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 211 THGNFIAASL-MVTMDQDLMGEyhgVFLCFLPMFHVFGLAVITYSQLQRGnALVSMArFELELVLKNIEKFRVTHLWVVP 289
Cdd:cd05907 108 SHRNILSNALaLAERLPATEGD---RHLSFLPLAHVFERRAGLYVPLLAG-ARIYFA-SSAETLLDDLSEVRPTVFLAVP 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 290 PVFLALSKQSIVKK--------FDL---SSLKYIGSGAAPLGKDLMEEC-GRNIPnvlLMQGYGMTETCGIVSVEDPrlG 357
Cdd:cd05907 183 RVWEKVYAAIKVKAvpglkrklFDLavgGRLRFAASGGAPLPAELLHFFrALGIP---VYEGYGLTETSAVVTLNPP--G 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 358 KRNSGSAGMLAPGVEAQIVSvetgksqppnqQGEIWVRGPNMMKGYLNNPQATKETIDKKSWVHTGDLGYFNEDGNLYVV 437
Cdd:cd05907 258 DNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHIT 326
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 15234634 438 DRIKELIKY-KGFQVAPAELEGLLVSHPDILDAVVI----PF------PDEEA 479
Cdd:cd05907 327 GRKKDLIITsGGKNISPEPIENALKASPLISQAVVIgdgrPFlvalivPDPEA 379
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
22-536 |
3.12e-75 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 250.26 E-value: 3.12e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 22 PKDPNTSLVSFLFRNSSSYPSKLAI------ADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLC 95
Cdd:PRK07529 20 ARDLPASTYELLSRAAARHPDAPALsflldaDPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 96 FLAVTAIGGVFTTaNPLYTVNEVSKQIKDSNPKIII------------SVNQLFDKIKGFDlPVVLLGSKDTVEIP---- 159
Cdd:PRK07529 100 LWGGEAAGIANPI-NPLLEPEQIAELLRAAGAKVLVtlgpfpgtdiwqKVAEVLAALPELR-TVVEVDLARYLPGPkrla 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 160 -----PGSNSKILSFDNVMElSEPVSEYPFVE-IKQSDTAALLYSSGTTGTSKGVELTHGNFIAASLMVTMDQDLMGEyh 233
Cdd:PRK07529 178 vplirRKAHARILDFDAELA-RQPGDRLFSGRpIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPG-- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 234 GVFLCFLPMFHVFGLAVITYSQLQRGNALV--SMARFELELVLKN----IEKFRVTHLWVVPPVFLALSkQSIVKKFDLS 307
Cdd:PRK07529 255 DTVFCGLPLFHVNALLVTGLAPLARGAHVVlaTPQGYRGPGVIANfwkiVERYRINFLSGVPTVYAALL-QVPVDGHDIS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 308 SLKYIGSGAAPL----GKDLMEECGrnipnVLLMQGYGMTETCGIVSVeDPRLGKRNSGSAGMLAPGVEAQIVSV-ETGK 382
Cdd:PRK07529 334 SLRYALCGAAPLpvevFRRFEAATG-----VRIVEGYGLTEATCVSSV-NPPDGERRIGSVGLRLPYQRVRVVILdDAGR 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 383 SQ---PPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKsWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGL 459
Cdd:PRK07529 408 YLrdcAVDEVGVLCIAGPNVFSGYLEAAHNKGLWLEDG-WLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEA 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 460 LVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQKFIAKQVA-----PykrlRRVSFISLVPKSAAGKILRR 534
Cdd:PRK07529 487 LLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAELLAFARDHIAeraavP----KHVRILDALPKTAVGKIFKP 562
|
..
gi 15234634 535 EL 536
Cdd:PRK07529 563 AL 564
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
197-536 |
1.02e-74 |
|
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: 240.64 E-value: 1.02e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 197 YSSGTTGTSKGVELTHGNFIAASLMVTmdqDLMGEYHGVFLCF-LPMFHVFGLAVITYSQLQRGNALVSMAR-FELELVL 274
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIG---ERLGLTEQDRLCIpVPLFHCFGSVLGVLACLTHGATMVFPSPsFDPLAVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 275 KNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMeecgRNIPNVLLMQ----GYGMTET---CG 347
Cdd:cd05917 86 EAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELM----KRVIEVMNMKdvtiAYGMTETspvST 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 348 IVSVEDPrLGKRnSGSAGMLAPGVEAQIVSVETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKSWVHTGDLGY 427
Cdd:cd05917 162 QTRTDDS-IEKR-VNTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 428 FNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQKFIAKQ 507
Cdd:cd05917 240 MDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKAYCKGK 319
|
330 340
....*....|....*....|....*....
gi 15234634 508 VAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:cd05917 320 IAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
47-536 |
1.63e-74 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 246.60 E-value: 1.63e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 47 ADSDTGDSLTFSQLKsavaRLAHGF-----HRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQ 121
Cdd:PRK05677 42 AFSNLGKTLTYGELY----KLSGAFaawlqQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 122 IKDSNPK------------------------IIISVNQLFDKIKGFDLPVVLLGSKDTVeiPPGSNSKILSFDNVMELS- 176
Cdd:PRK05677 118 FNDSGAKalvclanmahlaekvlpktgvkhvIVTEVADMLPPLKRLLINAVVKHVKKMV--PAYHLPQAVKFNDALAKGa 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 177 -EPVSEypfVEIKQSDTAALLYSSGTTGTSKGVELTHGNFIAASLMV-TMDQDLMGEYHGVFLCFLPMFHVFGLAVITYS 254
Cdd:PRK05677 196 gQPVTE---ANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCrALMGSNLNEGCEILIAPLPLYHIYAFTFHCMA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 255 QLQRGN--ALVSMARfELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDlMEECGRNIP 332
Cdd:PRK05677 273 MMLIGNhnILISNPR-DLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMALQLA-TAERWKEVT 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 333 NVLLMQGYGMTETCGIVSVeDPRLGKRnSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKE 412
Cdd:PRK05677 351 GCAICEGYGMTETSPVVSV-NPSQAIQ-VGTIGIPVPSTLCKVID-DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 413 TIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPN 492
Cdd:PRK05677 428 ILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPG 507
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 15234634 493 SSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:PRK05677 508 ETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
31-536 |
5.71e-73 |
|
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: 240.28 E-value: 5.71e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 31 SFLFRNSSSYPSKLAIADSDTgdSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTAN 110
Cdd:cd12118 8 SFLERAAAVYPDRTSIVYGDR--RYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 111 PLYTVNEVSKQIKDSNPKIIIsVNQLFDKIKgfdlpVVLLGSKDTVEIPPgsnskilsfdnvmelsepVSEYpfveikqs 190
Cdd:cd12118 86 TRLDAEEIAFILRHSEAKVLF-VDREFEYED-----LLAEGDPDFEWIPP------------------ADEW-------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 191 DTAALLYSSGTTGTSKGVELTHG----NFIAASLMVTMDQdlmgeyHGVFLCFLPMFHVFGLAvITYSQLQRGNALVSMA 266
Cdd:cd12118 134 DPIALNYTSGTTGRPKGVVYHHRgaylNALANILEWEMKQ------HPVYLWTLPMFHCNGWC-FPWTVAAVGGTNVCLR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 267 RFELELVLKNIEKFRVTHLWVVPPVF--LALSKQSIVKKFDlSSLKYIGSGAAP----LGKdlMEECGRNIpnvllMQGY 340
Cdd:cd12118 207 KVDAKAIYDLIEKHKVTHFCGAPTVLnmLANAPPSDARPLP-HRVHVMTAGAPPpaavLAK--MEELGFDV-----THVY 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 341 GMTETCGIVSV-------------EDPRLgKRNSGSAGMLAPGVEaqIVSVETGKSQPPNQQ--GEIWVRGPNMMKGYLN 405
Cdd:cd12118 279 GLTETYGPATVcawkpewdelpteERARL-KARQGVRYVGLEEVD--VLDPETMKPVPRDGKtiGEIVFRGNIVMKGYLK 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 406 NPQATKETIdKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIA 485
Cdd:cd12118 356 NPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCA 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 15234634 486 FVVRSPNSSITEQDIQKFIAKQVAPYKRLRRVSFISLvPKSAAGKILRREL 536
Cdd:cd12118 435 FVELKEGAKVTEEEIIAFCREHLAGFMVPKTVVFGEL-PKTSTGKIQKFVL 484
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
56-536 |
6.57e-73 |
|
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: 238.35 E-value: 6.57e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 56 TFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIIISvnq 135
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 136 lfdkikgfdlpvvllgskdtveippgsnskilsfdnvmelsepvseypfveikqsDTAALLYSSGTTGTSKGVELTHGNF 215
Cdd:cd05934 82 -------------------------------------------------------DPASILYTSGTTGPPKGVVITHANL 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 216 I-----AASLMVTMDQDlmgeyhgVFLCFLPMFHVFGLAVITYSQLQRGNALVSMARFELELVLKNIEKFRVTHLWVVPP 290
Cdd:cd05934 107 TfagyySARRFGLGEDD-------VYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGA 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 291 VFLALSKQSIVKKFDLSSLKYIGSGAAPlgKDLMEECGRNIpNVLLMQGYGMTETCGIVSVedPRLGKRNSGSAGMLAPG 370
Cdd:cd05934 180 MLSYLLAQPPSPDDRAHRLRAAYGAPNP--PELHEEFEERF-GVRLLEGYGMTETIVGVIG--PRDEPRRPGSIGRPAPG 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 371 VEAQIVSvETGKSQPPNQQGEIWVR---GPNMMKGYLNNPQATKETIdKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYK 447
Cdd:cd05934 255 YEVRIVD-DDGQELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRR 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 448 GFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSA 527
Cdd:cd05934 333 GENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTP 412
|
....*....
gi 15234634 528 AGKILRREL 536
Cdd:cd05934 413 TEKVAKAQL 421
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
191-533 |
8.62e-72 |
|
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: 232.39 E-value: 8.62e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 191 DTAALLYSSGTTGTSKGVELTHGNFIAASLM------VTMDQDlmgeyhgvFLCFLPMFHVFGLAVITYSQLQRGNALVS 264
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAwadcadLTEDDR--------YLIINPFFHTFGYKAGIVACLLTGATVVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 265 MARFELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECGRNIPNVLLMQGYGMTE 344
Cdd:cd17638 73 VAVFDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 345 tCGIVSV----EDPRLGKRNSGSAgmlAPGVEAQIVSvetgksqppnqQGEIWVRGPNMMKGYLNNPQATKETIDKKSWV 420
Cdd:cd17638 153 -AGVATMcrpgDDAETVATTCGRA---CPGFEVRIAD-----------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 421 HTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDI 500
Cdd:cd17638 218 HTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDV 297
|
330 340 350
....*....|....*....|....*....|...
gi 15234634 501 QKFIAKQVAPYKRLRRVSFISLVPKSAAGKILR 533
Cdd:cd17638 298 IAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
55-536 |
1.01e-71 |
|
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: 235.31 E-value: 1.01e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 55 LTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIIISvn 134
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 135 qlfdkikgfdlpvvllgskdtveippgsnskilsfdnvmelsepvseypfveiKQSDTAALLYSSGTTGTSKGVELTHGN 214
Cdd:cd05972 79 -----------------------------------------------------DAEDPALIYFTSGTTGLPKGVLHTHSY 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 215 FIAAslMVTM-------DQDLM------GEYHGVFLCFL-PMFHvfGLAVITYSqlqrgnalvsMARFELELVLKNIEKF 280
Cdd:cd05972 106 PLGH--IPTAaywlglrPDDIHwniadpGWAKGAWSSFFgPWLL--GATVFVYE----------GPRFDAERILELLERY 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 281 RVTHLWVVPPVFLALSKQSIvKKFDLSSLKYIGSGAAPLGK---DLMEECGrNIPnvlLMQGYGMTET---CGIVSVEDP 354
Cdd:cd05972 172 GVTSFCGPPTAYRMLIKQDL-SSYKFSHLRLVVSAGEPLNPeviEWWRAAT-GLP---IRDGYGQTETgltVGNFPDMPV 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 355 RlgkrnSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVR--GPNMMKGYLNNPQATKETIdKKSWVHTGDLGYFNEDG 432
Cdd:cd05972 247 K-----PGSMGRPTPGYDVAIID-DDGRELPPGEEGDIAIKlpPPGLFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 433 NLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITE---QDIQKFIAKQVA 509
Cdd:cd05972 320 YFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEelaEELQGHVKKVLA 399
|
490 500
....*....|....*....|....*..
gi 15234634 510 PYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:cd05972 400 PYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
40-536 |
4.40e-71 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 236.42 E-value: 4.40e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 40 YPSKLAIADSDTgdSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVS 119
Cdd:PRK06188 25 YPDRPALVLGDT--RLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 120 KQIKDSNPKIIIsvnqlFDKIKGFDLPVVLLGSKDTVEippgsnsKILSFDNV------MELSEPVSEYPFVEIKQS-DT 192
Cdd:PRK06188 103 YVLEDAGISTLI-----VDPAPFVERALALLARVPSLK-------HVLTLGPVpdgvdlLAAAAKFGPAPLVAAALPpDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 193 AALLYSSGTTGTSKGVELTHGNfiaaslMVTMDQDLMGEY----HGVFLCFLPMFHVFGLAVitYSQLQRGNALVSMARF 268
Cdd:PRK06188 171 AGLAYTGGTTGKPKGVMGTHRS------IATMAQIQLAEWewpaDPRFLMCTPLSHAGGAFF--LPTLLRGGTVIVLAKF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 269 ELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECGRNIPNVLlMQGYGMTETCGI 348
Cdd:PRK06188 243 DPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGPIF-AQYYGQTEAPMV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 349 VSV--------EDPRLgkrnSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIdKKSWV 420
Cdd:PRK06188 322 ITYlrkrdhdpDDPKR----LTSCGRPTPGLRVALLD-EDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-RDGWL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 421 HTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDI 500
Cdd:PRK06188 396 HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAEL 475
|
490 500 510
....*....|....*....|....*....|....*.
gi 15234634 501 QKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:PRK06188 476 QAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
31-541 |
1.53e-68 |
|
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: 230.03 E-value: 1.53e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 31 SFLFRNSSSYPSKLAIADSDTgdSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTAN 110
Cdd:COG1021 29 DLLRRRAERHPDRIAVVDGER--RLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVFAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 111 PLYTVNEVSKQIKDSNPK-IIISvnqlfDKIKGFDL---------------PVVLLGSKDTVeippgsnskiLSFDNVME 174
Cdd:COG1021 107 PAHRRAEISHFAEQSEAVaYIIP-----DRHRGFDYralarelqaevpslrHVLVVGDAGEF----------TSLDALLA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 175 lsEPVSEYPFvEIKQSDTAALLYSSGTTGTSKGVELTHG----NFIAASLMVTMDQDlmgeyhGVFLCFLPMFHVFGLAV 250
Cdd:COG1021 172 --APADLSEP-RPDPDDVAFFQLSGGTTGLPKLIPRTHDdylySVRASAEICGLDAD------TVYLAALPAAHNFPLSS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 251 ITY-SQLQRGnALVSMAR-------FELelvlknIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGkd 322
Cdd:COG1021 243 PGVlGVLYAG-GTVVLAPdpspdtaFPL------IERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLS-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 323 lmEECGRNIPNVL---LMQGYGMTEtcGIVS---VEDPRL------GKrnsgsagMLAPGVEAQIVSvETGKSQPPNQQG 390
Cdd:COG1021 314 --PELARRVRPALgctLQQVFGMAE--GLVNytrLDDPEEvilttqGR-------PISPDDEVRIVD-EDGNPVPPGEVG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 391 EIWVRGPNMMKGYLNNPQATKETIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAV 470
Cdd:COG1021 382 ELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAA 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15234634 471 VIPFPDEEAGEVPIAFVVrSPNSSITEQDIQKFI-AKQVAPYKRLRRVSFISLVPKSAAGKILRRELVQQVR 541
Cdd:COG1021 462 VVAMPDEYLGERSCAFVV-PRGEPLTLAELRRFLrERGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
26-544 |
1.47e-67 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 227.71 E-value: 1.47e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 26 NTSLVSFLFRNSSSYPSKLAIADsDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGV 105
Cdd:PRK06087 22 DASLADYWQQTARAMPDKIAVVD-NHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 106 FTTANPLYTVNEVSKQIKDSNPKIIIsVNQLFDKIKGFDLPVVLLGSKDTVE-------IPPGSNSkiLSFDNVMELSEP 178
Cdd:PRK06087 101 SVPLLPSWREAELVWVLNKCQAKMFF-APTLFKQTRPVDLILPLQNQLPQLQqivgvdkLAPATSS--LSLSQIIADYEP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 179 VSEypFVEIKQSDTAALLYSSGTTGTSKGVELTHGNFIA------ASLMVTMDqDLM----------GEYHGVFLCFLPm 242
Cdd:PRK06087 178 LTT--AITTHGDELAAVLFTSGTEGLPKGVMLTHNNILAseraycARLNLTWQ-DVFmmpaplghatGFLHGVTAPFLI- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 243 fhvfglavitysqlqrGNALVSMARFELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKD 322
Cdd:PRK06087 254 ----------------GARSVLLDIFTPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 323 LMEECGRNipNVLLMQGYGMTETC--GIVSVEDPRlgKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMM 400
Cdd:PRK06087 318 VARECQQR--GIKLLSVYGSTESSphAVVNLDDPL--SRFMHTDGYAAAGVEIKVVD-EARKTLPPGCEGEEASRGPNVF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 401 KGYLNNPQATKETIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAG 480
Cdd:PRK06087 393 MGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLG 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 481 EVPIAFVV-RSPNSSITEQDIQKFIAKQ-VAPYKRLRRVSFISLVPKSAAGKI----LRRELVQQVRSKM 544
Cdd:PRK06087 473 ERSCAYVVlKAPHHSLTLEEVVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKIqkflLRKDIMRRLTQDV 542
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
51-536 |
1.82e-67 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 226.32 E-value: 1.82e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 51 TGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQ-FPLCFLAVTAiGGVFTTANPLYTVNEVSKQIKDSNPKI 129
Cdd:PRK08276 8 SGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEfFEVYWAARRS-GLYYTPINWHLTAAEIAYIVDDSGAKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 130 IISVNQLFDKIKG------FDLPVVLLGSKDtveiPPGsnskilsfdnVMELSEPVSEYPFVEIK-QSDTAALLYSSGTT 202
Cdd:PRK08276 87 LIVSAALADTAAElaaelpAGVPLLLVVAGP----VPG----------FRSYEEALAAQPDTPIAdETAGADMLYSSGTT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 203 GTSKGV--ELTHGNFIAASLMVT--MDQDLMGEYHGVFLCFLPMFHVfglAVITYSQ--LQRGNALVSMARFELELVLKN 276
Cdd:PRK08276 153 GRPKGIkrPLPGLDPDEAPGMMLalLGFGMYGGPDSVYLSPAPLYHT---APLRFGMsaLALGGTVVVMEKFDAEEALAL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 277 IEKFRVTHLWVVPPVF---LALSkQSIVKKFDLSSLKYIGSGAAP----LGKDLMEECGrniPnvLLMQGYGMTETCGiV 349
Cdd:PRK08276 230 IERYRVTHSQLVPTMFvrmLKLP-EEVRARYDVSSLRVAIHAAAPcpveVKRAMIDWWG---P--IIHEYYASSEGGG-V 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 350 SVEDPRLGKRNSGSAGMLAPGvEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKSWVHTGDLGYFN 429
Cdd:PRK08276 303 TVITSEDWLAHPGSVGKAVLG-EVRILD-EDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVGYLD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 430 EDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITE---QDIQKFIAK 506
Cdd:PRK08276 381 EDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDalaAELIAWLRG 460
|
490 500 510
....*....|....*....|....*....|
gi 15234634 507 QVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:PRK08276 461 RLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
47-536 |
4.15e-67 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 227.01 E-value: 4.15e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 47 ADSDTGDSLTFSQLKSAVARLAHGF-HRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDS 125
Cdd:PRK12492 42 AFSNLGVTLSYAELERHSAAFAAYLqQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 126 NPKIIISVNqLFDK-------------------------IKGFDLPVVLLGSKDTVeiPPGSNSKILSFDNVMELSEPVS 180
Cdd:PRK12492 122 GARALVYLN-MFGKlvqevlpdtgieylieakmgdllpaAKGWLVNTVVDKVKKMV--PAYHLPQAVPFKQALRQGRGLS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 181 EYPfVEIKQSDTAALLYSSGTTGTSKGVELTHGNFIAASLMV--TMDQD------LMGEYHGVFLCFLPMFHVFGLAVIT 252
Cdd:PRK12492 199 LKP-VPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVraCLSQLgpdgqpLMKEGQEVMIAPLPLYHIYAFTANC 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 253 YSQLQRGN--ALVSMARfELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECgRN 330
Cdd:PRK12492 278 MCMMVSGNhnVLITNPR-DIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKDLDFSALKLTNSGGTALVKATAERW-EQ 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 331 IPNVLLMQGYGMTETCGIVSVeDPRLGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQAT 410
Cdd:PRK12492 356 LTGCTIVEGYGLTETSPVAST-NPYGELARLGTVGIPVPGTALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEAT 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 411 KETIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVV-R 489
Cdd:PRK12492 434 AEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVaR 513
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15234634 490 SPNSSITEqdIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:PRK12492 514 DPGLSVEE--LKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
35-536 |
1.03e-66 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 224.31 E-value: 1.03e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 35 RNSSSYPSKLAIADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYT 114
Cdd:cd05923 9 RAASRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 115 VNEVSKQIKdsnpkiiisvnqlFDKIKGfdlpVVLLGSKDTVEIPPGSNSKILSFDNVMELSEPVSEYPFVEIKQ---SD 191
Cdd:cd05923 89 AAELAELIE-------------RGEMTA----AVIAVDAQVMDAIFQSGVRVLALSDLVGLGEPESAGPLIEDPPrepEQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 192 TAALLYSSGTTGTSKGVELTHGNfiAAS---LMVTMDQDLMGEyHGVFLCFLPMFHVFGLAVITYSQLQRGNALVSMARF 268
Cdd:cd05923 152 PAFVFYTSGTTGLPKGAVIPQRA--AESrvlFMSTQAGLRHGR-HNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 269 ELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECGRNIPNvLLMQGYGMTETCGI 348
Cdd:cd05923 229 DPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPG-EKVNIYGTTEAMNS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 349 VSVEDPRLGKRnsgsagmLAPGV--EAQIVSVETGKSQ--PPNQQGEIWVR--GPNMMKGYLNNPQATKETIdKKSWVHT 422
Cdd:cd05923 308 LYMRDARTGTE-------MRPGFfsEVRIVRIGGSPDEalANGEEGELIVAaaADAAFTGYLNQPEATAKKL-QDGWYRT 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 423 GDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPnSSITEQDIQK 502
Cdd:cd05923 380 GDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPRE-GTLSADELDQ 458
|
490 500 510
....*....|....*....|....*....|....*
gi 15234634 503 F-IAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:cd05923 459 FcRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
54-539 |
4.28e-66 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 223.04 E-value: 4.28e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 54 SLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIIISV 133
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 134 NQLFDKIKGfDLP--VVLLgskdTVEIPP--GSNSKI-----------LSFDNVMELSEPvSEYPFVEIKQSdtaaLLYS 198
Cdd:PRK12406 91 ADLLHGLAS-ALPagVTVL----SVPTPPeiAAAYRIspalltppagaIDWEGWLAQQEP-YDGPPVPQPQS----MIYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 199 SGTTGTSKGVELTHGNFIAASLMVTMDQDLMGEYHGV-FLCFLPMFH----VFGLAVITYsqlqrGNALVSMARFELELV 273
Cdd:PRK12406 161 SGTTGHPKGVRRAAPTPEQAAAAEQMRALIYGLKPGIrALLTGPLYHsapnAYGLRAGRL-----GGVLVLQPRFDPEEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 274 LKNIEKFRVTHLWVVPPVFLALSK--QSIVKKFDLSSLKYIGSGAAPLGKD----LMEECGRNIpnvllMQGYGMTETcG 347
Cdd:PRK12406 236 LQLIERHRITHMHMVPTMFIRLLKlpEEVRAKYDVSSLRHVIHAAAPCPADvkraMIEWWGPVI-----YEYYGSTES-G 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 348 IVSVEDPRLGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMK-GYLNNPQATKEtIDKKSWVHTGDLG 426
Cdd:PRK12406 310 AVTFATSEDALSHPGTVGKAAPGAELRFVD-EDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAE-IDRGGFITSGDVG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 427 YFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQKFIAK 506
Cdd:PRK12406 388 YLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKA 467
|
490 500 510
....*....|....*....|....*....|...
gi 15234634 507 QVAPYKRLRRVSFISLVPKSAAGKILRRELVQQ 539
Cdd:PRK12406 468 RLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
33-539 |
5.25e-66 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 222.44 E-value: 5.25e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 33 LFRNSSSYPSKLAIADSDtGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPL 112
Cdd:PRK07514 8 ALRAAFADRDAPFIETPD-GLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 113 YTVNEVSKQIKDSNPKIIISVNQLFDKIKGFDLP-----VVLLGSKDTveippGSnskilsfdnVMELSEPVSE-YPFVE 186
Cdd:PRK07514 87 YTLAELDYFIGDAEPALVVCDPANFAWLSKIAAAagaphVETLDADGT-----GS---------LLEAAAAAPDdFETVP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 187 IKQSDTAALLYSSGTTGTSKGVELTHGNFIAASLMVTmdqdlmgEYHG-----VFLCFLPMFHVFGLAVITYSQLQRGNA 261
Cdd:PRK07514 153 RGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLV-------DYWRftpddVLIHALPIFHTHGLFVATNVALLAGAS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 262 LVSMARFELELVLKNIEkfRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEE----CGRNIpnvllM 337
Cdd:PRK07514 226 MIFLPKFDPDAVLALMP--RATVMMGVPTFYTRLLQEPRLTREAAAHMRLFISGSAPLLAETHREfqerTGHAI-----L 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 338 QGYGMTETCGIVSveDPRLGKRNSGSAGMLAPGVEAQIVSVETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKK 417
Cdd:PRK07514 299 ERYGMTETNMNTS--NPYDGERRAGTVGFPLPGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRAD 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 418 SWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVI--PFPDeeAGEVPIAFVVRSPNSSI 495
Cdd:PRK07514 377 GFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIgvPHPD--FGEGVTAVVVPKPGAAL 454
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 15234634 496 TEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRRELVQQ 539
Cdd:PRK07514 455 DEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
191-533 |
8.76e-66 |
|
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: 216.75 E-value: 8.76e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 191 DTAALLYSSGTTGTSKGVELTHGNFIAASLMVtmdQDLMG-EYHGVFLCFLPMFHVFGLAvITYSQLQRGNALVSMARFE 269
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQL---IHAMGlTEADVYLNMLPLFHIAGLN-LALATFHAGGANVVMEKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 270 LELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECGrnipNVLLMQGYGMTETCGIV 349
Cdd:cd17637 77 PAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVLGLDAPETIQRFEETT----GATFWSLYGQTETSGLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 350 SVEDPRlgkRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIdKKSWVHTGDLGYFN 429
Cdd:cd17637 153 TLSPYR---ERPGSAGRPGPLVRVRIVD-DNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDLGRFD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 430 EDGNLYVVDRI--KELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQKFIAKQ 507
Cdd:cd17637 228 EDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFVGSR 307
|
330 340
....*....|....*....|....*.
gi 15234634 508 VAPYKRLRRVSFISLVPKSAAGKILR 533
Cdd:cd17637 308 IARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
54-536 |
2.08e-65 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 219.17 E-value: 2.08e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 54 SLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIIIsV 133
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 134 NQLFdkikgfdlpvvllGSKDTVEIPpgsnskilsfdnvmelsepvseypfveikqSDTAALLYSSGTTGTSKGVELTHG 213
Cdd:cd05903 80 PERF-------------RQFDPAAMP------------------------------DAVALLLFTSGTTGEPKGVMHSHN 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 214 NFIAASLMVTmdQDLMGEYHGVFLCFLPMFHVFGLAVITYSQLQRGNALVSMARFELELVLKNIEKFRVTHLWVVPPVFL 293
Cdd:cd05903 117 TLSASIRQYA--ERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPFLT 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 294 ALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECGRNIPNVLLmQGYGMTETCGIVSVEDPRLGKRNSGSAGMLAPGVEA 373
Cdd:cd05903 195 DLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVC-SAYGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 374 QIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETiDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAP 453
Cdd:cd05903 274 KVVD-DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADA-APEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPV 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 454 AELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQKFI-AKQVAPYKRLRRVSFISLVPKSAAGKIL 532
Cdd:cd05903 352 LEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKVQ 431
|
....
gi 15234634 533 RREL 536
Cdd:cd05903 432 KFRL 435
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
47-536 |
6.43e-65 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 221.29 E-value: 6.43e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 47 ADSDTGDSLTFSQLKSAVARLA-HGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDS 125
Cdd:PRK08751 43 AYHSFGKTITYREADQLVEQFAaYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 126 NPKIIISVNQLFDKIKGF--DLP---VVLLGSKDTVEIPPGSnskILSFdNVMELSEPVSEY------------------ 182
Cdd:PRK08751 123 GASVLVVIDNFGTTVQQViaDTPvkqVITTGLGDMLGFPKAA---LVNF-VVKYVKKLVPEYringairfrealalgrkh 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 183 --PFVEIKQSDTAALLYSSGTTGTSKGVELTHGNFIAAslMVTMDQDLMG-----EYHGVFLCFLPMFHVFGLAV--ITY 253
Cdd:PRK08751 199 smPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVAN--MQQAHQWLAGtgkleEGCEVVITALPLYHIFALTAngLVF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 254 SQLQRGNALVSMARfELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECgRNIPN 333
Cdd:PRK08751 277 MKIGGCNHLISNPR-DMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERW-KQVTG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 334 VLLMQGYGMTETCGIVSVeDPRLGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKET 413
Cdd:PRK08751 355 LTLVEAYGLTETSPAACI-NPLTLKEYNGSIGLPIPSTDACIKD-DAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKV 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 414 IDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGE-VPIAFVVRSPN 492
Cdd:PRK08751 433 MDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEiVKVVIVKKDPA 512
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 15234634 493 ssITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:PRK08751 513 --LTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
40-536 |
2.75e-64 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 219.03 E-value: 2.75e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 40 YPSKLAIADsDTGdSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGvfttanPLYTVN-EV 118
Cdd:PRK07788 62 APDRAALID-ERG-TLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGA------RIILLNtGF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 119 SK-QIKDS----NPKIIIsVNQLFDKIKGF---DLPVVLLGSKDTVEIPPgSNSKILSFDNVMELSEPVseyPFVEIKQS 190
Cdd:PRK07788 134 SGpQLAEVaareGVKALV-YDDEFTDLLSAlppDLGRLRAWGGNPDDDEP-SGSTDETLDDLIAGSSTA---PLPKPPKP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 191 DTAALLySSGTTGTSKGVELTHGNfIAASLMVTMDQDLMGEyHGVFLCFLPMFHVFGLAVITYSqLQRGNALVSMARFEL 270
Cdd:PRK07788 209 GGIVIL-TSGTTGTPKGAPRPEPS-PLAPLAGLLSRVPFRA-GETTLLPAPMFHATGWAHLTLA-MALGSTVVLRRRFDP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 271 ELVLKNIEKFRVTHLwVVPPVFLalskQSIVK-------KFDLSSLKYIGSGAAPLGKDL----MEECGRNIPNVllmqg 339
Cdd:PRK07788 285 EATLEDIAKHKATAL-VVVPVML----SRILDlgpevlaKYDTSSLKIIFVSGSALSPELatraLEAFGPVLYNL----- 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 340 YGMTEtCGIVSVEDPRLGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPqaTKETIDkkSW 419
Cdd:PRK07788 355 YGSTE-VAFATIATPEDLAEAPGTVGRPPKGVTVKILD-ENGNEVPRGVVGRIFVGNGFPFEGYTDGR--DKQIID--GL 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 420 VHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQD 499
Cdd:PRK07788 429 LSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDA 508
|
490 500 510
....*....|....*....|....*....|....*..
gi 15234634 500 IQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:PRK07788 509 IKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKREL 545
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
28-536 |
5.77e-64 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 217.06 E-value: 5.77e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 28 SLVSFLFRNSSSYPSKLAIADSDtgDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFT 107
Cdd:PRK06145 3 NLSASIAFHARRTPDRAALVYRD--QEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 108 TANPLYTVNEVSKQIKDSNPKIIIsVNQLFDKIKGFDLPVVLLGS---KDTVEIPPGSnskilsfdnvmelsEPVSeyPF 184
Cdd:PRK06145 81 PINYRLAADEVAYILGDAGAKLLL-VDEEFDAIVALETPKIVIDAaaqADSRRLAQGG--------------LEIP--PQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 185 VEIKQSDTAALLYSSGTTGTSKGVELTHGNFI------AASLMVTMDQDLM--GEYHGVFLCFLPmfhvfGLAVitysqL 256
Cdd:PRK06145 144 AAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHwksidhVIALGLTASERLLvvGPLYHVGAFDLP-----GIAV-----L 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 257 QRGNALVSMARFELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECGRNIPNVLL 336
Cdd:PRK06145 214 WVGGTLRIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 337 MQGYGMTETCGIVSVEDPRLGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIdK 416
Cdd:PRK06145 294 IDAYGLTETCSGDTLMEAGREIEKIGSTGRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-Y 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 417 KSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSIT 496
Cdd:PRK06145 372 GDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLT 451
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15234634 497 EQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:PRK06145 452 LEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
40-539 |
7.35e-64 |
|
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: 217.75 E-value: 7.35e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 40 YPSKLAIA-DSDTGDS--LTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVN 116
Cdd:cd05970 30 YPDKLALVwCDDAGEEriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 117 EVSKQIKDSNPKIIISVNQ--LFDKIKGF--DLPVVLLGSKDTVEIPPGsnskILSFDNVMELSEPVSEYPF--VEIKQS 190
Cdd:cd05970 110 DIVYRIESADIKMIVAIAEdnIPEEIEKAapECPSKPKLVWVGDPVPEG----WIDFRKLIKNASPDFERPTanSYPCGE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 191 DTAALLYSSGTTGTSKGVELTH----GNFIAASLMVTMDQD--------------LMGEYHGVFLCflpmfhvfGLAVIT 252
Cdd:cd05970 186 DILLVYFSSGTTGMPKMVEHDFtyplGHIVTAKYWQNVREGglhltvadtgwgkaVWGKIYGQWIA--------GAAVFV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 253 YSqlqrgnalvsMARFELELVLKNIEKFRVTHLWVVPPVFLALSKQSIvKKFDLSSLKYIGSGAAPLGKDLMEECgRNIP 332
Cdd:cd05970 258 YD----------YDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDL-SRYDLSSLRYCTTAGEALNPEVFNTF-KEKT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 333 NVLLMQGYGMTETcgIVSVEDPRLGKRNSGSAGMLAPGVEAQIVSVEtGKSQPPNQQGEIWVRGPN-----MMKGYLNNP 407
Cdd:cd05970 326 GIKLMEGFGQTET--TLTIATFPWMEPKPGSMGKPAPGYEIDLIDRE-GRSCEAGEEGEIVIRTSKgkpvgLFGGYYKDA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 408 QATKETIdKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFV 487
Cdd:cd05970 403 EKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATI 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15234634 488 VRSPN---SSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRRELVQQ 539
Cdd:cd05970 482 VLAKGyepSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRER 536
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
29-539 |
2.22e-62 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 213.36 E-value: 2.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 29 LVSFLFRNSSSYPSKLAIADSDtgDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTT 108
Cdd:PRK07470 9 LAHFLRQAARRFPDRIALVWGD--RSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 109 ANPLYTVNEVSKQIKDSNPKIIISVNQLFDKIKGFDLPVVLLGSKDTVEIPPGSnskiLSFDNVM--ELSEPVSEypfVE 186
Cdd:PRK07470 87 TNFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTHVVAIGGARAG----LDYEALVarHLGARVAN---AA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 187 IKQSDTAALLYSSGTTGTSKGVELTHGN--FIAASLMVtmdqDLM--GEYHGVFLCFLPMFHvfGLAVITYSQLQRGNAL 262
Cdd:PRK07470 160 VDHDDPCWFFFTSGTTGRPKAAVLTHGQmaFVITNHLA----DLMpgTTEQDASLVVAPLSH--GAGIHQLCQVARGAAT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 263 VSMA--RFELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECGRNIPNVLLmQGY 340
Cdd:PRK07470 234 VLLPseRFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKVLV-QYF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 341 GMTETCGIVSVEDPRLGKR------NSGSAGMLAPGVEAQIVSVEtGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETI 414
Cdd:PRK07470 313 GLGEVTGNITVLPPALHDAedgpdaRIGTCGFERTGMEVQIQDDE-GRELPPGETGEICVIGPAVFAGYYNNPEANAKAF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 415 dKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSS 494
Cdd:PRK07470 392 -RDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAP 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 15234634 495 ITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKI----LRRELVQQ 539
Cdd:PRK07470 471 VDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKItkkmVREELEER 519
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
56-538 |
4.71e-62 |
|
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: 210.37 E-value: 4.71e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 56 TFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIIISvnq 135
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 136 lfdkikgfDLPvvllgskdtveippgsnskilsfdnvmelsepvseypfveikqSDTAALLYSSGTTGTSKGVELTH--- 212
Cdd:cd05971 85 --------DGS-------------------------------------------DDPALIIYTSGTTGPPKGALHAHrvl 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 213 -GNFIAASL---MVTMDQDLM------GEYHGVFLCFLPMFHvFGLAVITYSqlqrgnalvsMARFELELVLKNIEKFRV 282
Cdd:cd05971 114 lGHLPGVQFpfnLFPRDGDLYwtpadwAWIGGLLDVLLPSLY-FGVPVLAHR----------MTKFDPKAALDLMSRYGV 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 283 THLWVvPPVFLALSKQ--SIVKKFDLSsLKYIGSGAAPLGKDLMEeCGRNIPNVLLMQGYGMTEtCGIVSVEDPRLGKRN 360
Cdd:cd05971 183 TTAFL-PPTALKMMRQqgEQLKHAQVK-LRAIATGGESLGEELLG-WAREQFGVEVNEFYGQTE-CNLVIGNCSALFPIK 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 361 SGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPN--MMKGYLNNPQATKETIdKKSWVHTGDLGYFNEDGNLYVVD 438
Cdd:cd05971 259 PGSMGKPIPGHRVAIVD-DNGTPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKM-AGDWLLTGDLGRKDSDGYFWYVG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 439 RIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQ---DIQKFIAKQVAPYKRLR 515
Cdd:cd05971 337 RDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDAlarEIQELVKTRLAAHEYPR 416
|
490 500
....*....|....*....|...
gi 15234634 516 RVSFISLVPKSAAGKILRRELVQ 538
Cdd:cd05971 417 EIEFVNELPRTATGKIRRRELRA 439
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
29-536 |
8.52e-62 |
|
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: 211.46 E-value: 8.52e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 29 LVSFLFRNSSS-YPSKLAIadSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFT 107
Cdd:cd05959 5 AATLVDLNLNEgRGDKTAF--IDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 108 TANPLYTVNEVSKQIKDSNPKIIISVNQLFDKIKgfdlpVVLLGSKDTVEI-----PPGSNSKILSFDNVM----ELSEP 178
Cdd:cd05959 83 PVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLA-----AALTKSEHTLVVlivsgGAGPEAGALLLAELVaaeaEQLKP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 179 VSEYPfveikqSDTAALLYSSGTTGTSKGVELTHGNFIAASlmVTMDQDLMGEYHG-VFLCFLPMFHVFGLAVITYSQLQ 257
Cdd:cd05959 158 AATHA------DDPAFWLYSSGSTGRPKGVVHLHADIYWTA--ELYARNVLGIREDdVCFSAAKLFFAYGLGNSLTFPLS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 258 RGNALVSMA-RFELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECgRNIPNVLL 336
Cdd:cd05959 230 VGATTVLMPeRPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERW-KARFGLDI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 337 MQGYGMTETCGIVSVEDPrlGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIdK 416
Cdd:cd05959 309 LDGIGSTEMLHIFLSNRP--GRVRYGTTGKPVPGYEVELRD-EDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF-Q 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 417 KSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSP---NS 493
Cdd:cd05959 385 GEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPgyeDS 464
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 15234634 494 SITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:cd05959 465 EALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
41-536 |
8.49e-61 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 208.12 E-value: 8.49e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 41 PSKLAIADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSK 120
Cdd:PRK09088 9 PQRLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 121 QIKDSNPKIIISVNQLFD------KIKGFDLPVVLLGSKDTVEIPPGSNSKILsfdnvmelsepvseypfveikqsdtaa 194
Cdd:PRK09088 89 LLQDAEPRLLLGDDAVAAgrtdveDLAAFIASADALEPADTPSIPPERVSLIL--------------------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 195 llYSSGTTGTSKGVELTHGNFIAASLmvtmDQDLMG--EYHGVFLCFLPMFHVFGLAVITYSQLQRGNALVSMARFELEL 272
Cdd:PRK09088 142 --FTSGTSGQPKGVMLSERNLQQTAH----NFGVLGrvDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 273 VLKNI--EKFRVTHLWVVPPVFLALSKQSivkKFDLSSLKY---IGSGAAP-LGKDLMEECGRNIPNVllmQGYGMTETC 346
Cdd:PRK09088 216 TLGRLgdPALGITHYFCVPQMAQAFRAQP---GFDAAALRHltaLFTGGAPhAAEDILGWLDDGIPMV---DGFGMSEAG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 347 GIVSVE-DPRLGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKSWVHTGDL 425
Cdd:PRK09088 290 TVFGMSvDCDVIRAKAGAAGIPTPTVQTRVVD-DQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 426 GYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQKFIA 505
Cdd:PRK09088 369 ARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLS 448
|
490 500 510
....*....|....*....|....*....|.
gi 15234634 506 KQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:PRK09088 449 TRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
41-543 |
2.39e-59 |
|
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: 207.17 E-value: 2.39e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 41 PSKLA-IADS---DTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVN 116
Cdd:cd05967 65 GDQIAlIYDSpvtGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 117 EVSKQIKDSNPKIIISVN------------QLFDK---IKGFDLPVVLLGSKDTVEIPPGSNSKILSFDNVMELSEPVse 181
Cdd:cd05967 145 ELASRIDDAKPKLIVTAScgiepgkvvpykPLLDKaleLSGHKPHHVLVLNRPQVPADLTKPGRDLDWSELLAKAEPV-- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 182 yPFVEIKQSDTAALLYSSGTTGTSKGVELTHGNFiAASLMVTMdQDLMGEYHG-VFLCFLPMFHVFGLAVITYSQLQRGN 260
Cdd:cd05967 223 -DCVPVAATDPLYILYTSGTTGKPKGVVRDNGGH-AVALNWSM-RNIYGIKPGdVWWAASDVGWVVGHSYIVYGPLLHGA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 261 ALVSmarFELELV--------LKNIEKFRVTHLWVVPPVFLALSKQ----SIVKKFDLSSLKYIGSGAAPLGKDLMEeCG 328
Cdd:cd05967 300 TTVL---YEGKPVgtpdpgafWRVIEKYQVNALFTAPTAIRAIRKEdpdgKYIKKYDLSSLRTLFLAGERLDPPTLE-WA 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 329 RNIPNVLLMQGYGMTETCGIVSVEDPRLGKR--NSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGP---NMMKGY 403
Cdd:cd05967 376 ENTLGVPVIDHWWQTETGWPITANPVGLEPLpiKAGSPGKPVPGYQVQVLD-EDGEPVGPNELGNIVIKLPlppGCLLTL 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 404 LNNPQATKETIDKKS--WVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGE 481
Cdd:cd05967 455 WKNDERFKKLYLSKFpgYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQ 534
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15234634 482 VPIAFVVRSPNSSITEQDIQKFIAK----QVAPYKRLRRVSFISLVPKSAAGKILRRELVQQVRSK 543
Cdd:cd05967 535 VPLGLVVLKEGVKITAEELEKELVAlvreQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGE 600
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
41-539 |
1.08e-58 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 203.38 E-value: 1.08e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 41 PSKLAIADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSK 120
Cdd:PRK13391 11 PDKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 121 QIKDSNPKIIISVNQLFDKIKGF--DLPVVLLgskDTVEIPPGSNSKILSFdnvmelSEPVSEYPFVEIK-QSDTAALLY 197
Cdd:PRK13391 91 IVDDSGARALITSAAKLDVARALlkQCPGVRH---RLVLDGDGELEGFVGY------AEAVAGLPATPIAdESLGTDMLY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 198 SSGTTGTSKGV--ELTHGNFIAASLMVTMDQDLMGEYHG-VFLCFLPMFHVFGLAVITYSQLQRGNALVsMARFELELVL 274
Cdd:PRK13391 162 SSGTTGRPKGIkrPLPEQPPDTPLPLTAFLQRLWGFRSDmVYLSPAPLYHSAPQRAVMLVIRLGGTVIV-MEHFDAEQYL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 275 KNIEKFRVTHLWVVPPVFLALSK--QSIVKKFDLSSLKYIGSGAAP----LGKDLMEECGRNIpnvllMQGYGMTETCGi 348
Cdd:PRK13391 241 ALIEEYGVTHTQLVPTMFSRMLKlpEEVRDKYDLSSLEVAIHAAAPcppqVKEQMIDWWGPII-----HEYYAATEGLG- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 349 VSVEDPRLGKRNSGSAGMLAPGVeAQIVSvETGKSQPPNQQGEIWVRGPNMMKgYLNNPQATKETID-KKSWVHTGDLGY 427
Cdd:PRK13391 315 FTACDSEEWLAHPGTVGRAMFGD-LHILD-DDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHpDGTWSTVGDIGY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 428 FNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITE---QDIQKFI 504
Cdd:PRK13391 392 VDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPalaAELIAFC 471
|
490 500 510
....*....|....*....|....*....|....*
gi 15234634 505 AKQVAPYKRLRRVSFISLVPKSAAGKILRRELVQQ 539
Cdd:PRK13391 472 RQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDR 506
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
46-536 |
3.11e-58 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 202.22 E-value: 3.11e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 46 IADSDTGD--SLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIK 123
Cdd:PRK08008 27 IFESSGGVvrRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 124 DSNPKIIISVNQ---LFDKI---KGFDLPVVLLGSKDTVEIPPGSNSKILSFDNVMELSEPVSeypfveIKQSDTAALLY 197
Cdd:PRK08008 107 NSQASLLVTSAQfypMYRQIqqeDATPLRHICLTRVALPADDGVSSFTQLKAQQPATLCYAPP------LSTDDTAEILF 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 198 SSGTTGTSKGVELTHGNFIAASLMVTMDQDLmgEYHGVFLCFLPMFHV-----FGLAVITYsqlqrGNALVSMARFELEL 272
Cdd:PRK08008 181 TSGTTSRPKGVVITHYNLRFAGYYSAWQCAL--RDDDVYLTVMPAFHIdcqctAAMAAFSA-----GATFVLLEKYSARA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 273 VLKNIEKFR--VTH--------LWVVPPV-------------FLALSKQSivkkfdlsslkyigsgaaplgKDLMEEcgR 329
Cdd:PRK08008 254 FWGQVCKYRatITEcipmmirtLMVQPPSandrqhclrevmfYLNLSDQE---------------------KDAFEE--R 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 330 NipNVLLMQGYGMTETcgIVSV-EDPRLGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRG---PNMMKGYLN 405
Cdd:PRK08008 311 F--GVRLLTSYGMTET--IVGIiGDRPGDKRRWPSIGRPGFCYEAEIRD-DHNRPLPAGEIGEICIKGvpgKTIFKEYYL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 406 NPQATKETIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIA 485
Cdd:PRK08008 386 DPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKA 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 15234634 486 FVVRSPNSSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:PRK08008 466 FVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
55-487 |
6.88e-58 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 202.34 E-value: 6.88e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 55 LTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIII--- 131
Cdd:PLN02860 33 RTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVtde 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 132 SVNQLFDKIKGFDLPV----VLLGSkDTVEIPPGSNSkILSFDNVME--LSEPVSEYPFVeikqSDTAALL-YSSGTTGT 204
Cdd:PLN02860 113 TCSSWYEELQNDRLPSlmwqVFLES-PSSSVFIFLNS-FLTTEMLKQraLGTTELDYAWA----PDDAVLIcFTSGTTGR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 205 SKGVELTHGNFIAASL----MVTMDQDlmgeyhGVFLCFLPMFHVFGLAVITySQLQRGNALVSMARFELELVLKNIEKF 280
Cdd:PLN02860 187 PKGVTISHSALIVQSLakiaIVGYGED------DVYLHTAPLCHIGGLSSAL-AMLMVGACHVLLPKFDAKAALQAIKQH 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 281 RVTHLWVVPPV---FLALSKQSIVKKfDLSSLKYIGSGAAPLGKDLMEECGRNIPNVLLMQGYGMTETCG---IVSVEDP 354
Cdd:PLN02860 260 NVTSMITVPAMmadLISLTRKSMTWK-VFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEACSsltFMTLHDP 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 355 RL----------GKRNSGSAGML--------APGVEAQIVSVETGKSqppnqqGEIWVRGPNMMKGYLNNPQATKETIDK 416
Cdd:PLN02860 339 TLespkqtlqtvNQTKSSSVHQPqgvcvgkpAPHVELKIGLDESSRV------GRILTRGPHVMLGYWGQNSETASVLSN 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15234634 417 KSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFV 487
Cdd:PLN02860 413 DGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACV 483
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
28-536 |
7.54e-58 |
|
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: 200.25 E-value: 7.54e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 28 SLVSFLFRNSSSYPSKLAIADSDTgdSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFT 107
Cdd:cd05920 16 PLGDLLARSAARHPDRIAVVDGDR--RLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 108 TANPLYTVNEVSKQIKDSNPKIIIsvnqLFDKIKGFDlpvvllgskdtveippgsnskilSFDNVMELSEpvseypfvei 187
Cdd:cd05920 94 LALPSHRRSELSAFCAHAEAVAYI----VPDRHAGFD-----------------------HRALARELAE---------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 188 KQSDTAALLYSSGTTGTSKGVELTHGNFiaaSLMVTMDQDLMG-EYHGVFLCFLPMFHVFGLA---VItySQLQRGNALV 263
Cdd:cd05920 137 SIPEVALFLLSGGTTGTPKLIPRTHNDY---AYNVRASAEVCGlDQDTVYLAVLPAAHNFPLAcpgVL--GTLLAGGRVV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 264 SMARFELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGkdlmEECGRNIPNVL---LMQGY 340
Cdd:cd05920 212 LAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLS----PALARRVPPVLgctLQQVF 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 341 GMTEtcGIVS---VEDPrlGKRNSGSAGM-LAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDK 416
Cdd:cd05920 288 GMAE--GLLNytrLDDP--DEVIIHTQGRpMSPDDEIRVVD-EEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 417 KSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPnSSIT 496
Cdd:cd05920 363 DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRD-PPPS 441
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 15234634 497 EQDIQKFI-AKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:cd05920 442 AAQLRRFLrERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
41-536 |
1.25e-57 |
|
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: 198.52 E-value: 1.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 41 PSKLAIADSDTgdSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSK 120
Cdd:cd05930 1 PDAVAVVDGDQ--SLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 121 QIKDSNPKIIISvnqlfdkikgfdlpvvllgskdtveippgsnskilsfdnvmelsepvseypfveiKQSDTAALLYSSG 200
Cdd:cd05930 79 ILEDSGAKLVLT-------------------------------------------------------DPDDLAYVIYTSG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 201 TTGTSKGVELTHGNFiaASLMVTMDQDLMGEYHGVFLCFlpMFHVFGLAVI-TYSQLQRGNALV---SMARFELELVLKN 276
Cdd:cd05930 104 STGKPKGVMVEHRGL--VNLLLWMQEAYPLTPGDRVLQF--TSFSFDVSVWeIFGALLAGATLVvlpEEVRKDPEALADL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 277 IEKFRVTHLWVVPPVFLALSKQSIVKkfDLSSLKYIGSGAAPLGKDLMEECGRNIPNVLLMQGYGMTETCGIVSVEDPRL 356
Cdd:cd05930 180 LAEEGITVLHLTPSLLRLLLQELELA--ALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPP 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 357 GKRNSGSA--GMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKSWVH------TGDLGYF 428
Cdd:cd05930 258 DDEEDGRVpiGRPIPNTRVYVLD-ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPgermyrTGDLVRW 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 429 NEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQKFIAKQV 508
Cdd:cd05930 337 LPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERL 416
|
490 500
....*....|....*....|....*...
gi 15234634 509 APYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:cd05930 417 PDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
63-537 |
4.54e-57 |
|
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: 197.66 E-value: 4.54e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 63 AVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGG----VFTTANPLYTVNEVSKQIKDSNPKIIISVNQLFD 138
Cdd:cd05922 2 GVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGrlglVFVPLNPTLKESVLRYLVADAGGRIVLADAGAAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 139 KIKgFDLPVvlLGSKDTVeippgsnskiLSFDnvmELSEPVSEYPFVEIKQSDTAALLYSSGTTGTSKGVELTHGNFIAA 218
Cdd:cd05922 82 RLR-DALPA--SPDPGTV----------LDAD---GIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLAN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 219 SLMVTMDQDLMGEyhGVFLCFLPMFHVFGLAVITySQLQRGNALVSMARFEL-ELVLKNIEKFRVTHLWVVPPVFlALSK 297
Cdd:cd05922 146 ARSIAEYLGITAD--DRALTVLPLSYDYGLSVLN-THLLRGATLVLTNDGVLdDAFWEDLREHGATGLAGVPSTY-AMLT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 298 QSIVKKFDLSSLKYIGSGAAPLGKDLMEECGRNIP--NVLLMqgYGMTETCGIVSVEDPRLGKRNSGSAGMLAPGVEAQI 375
Cdd:cd05922 222 RLGFDPAKLPSLRYLTQAGGRLPQETIARLRELLPgaQVYVM--YGQTEATRRMTYLPPERILEKPGSIGLAIPGGEFEI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 376 VSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAE 455
Cdd:cd05922 300 LD-DDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 456 LEGLLVSHPDILDAVVIPFPDeEAGEVPIAFVVRSPnsSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRRE 535
Cdd:cd05922 379 IEAAARSIGLIIEAAAVGLPD-PLGEKLALFVTAPD--KIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAA 455
|
..
gi 15234634 536 LV 537
Cdd:cd05922 456 LR 457
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
19-536 |
4.57e-57 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 200.63 E-value: 4.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 19 LVLPKDPNTSL--VSFLFRNSSSYPSKLAIADSDTgdSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCF 96
Cdd:PLN03102 4 LALCEANNVPLtpITFLKRASECYPNRTSIIYGKT--RFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 97 LAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIIIsVNQLFDKI------------KGFDLPVVLLGSKDTveiPPGSNS 164
Cdd:PLN03102 82 FAVPMAGAVLNPINTRLDATSIAAILRHAKPKILF-VDRSFEPLarevlhllssedSNLNLPVIFIHEIDF---PKRPSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 165 KILSFDNVMELSEP---VSEYPFVEIKQSDTAALLYSSGTTGTSKGVELTH-GNFIAA-SLMVTMDqdlMGEYhGVFLCF 239
Cdd:PLN03102 158 EELDYECLIQRGEPtpsLVARMFRIQDEHDPISLNYTSGTTADPKGVVISHrGAYLSTlSAIIGWE---MGTC-PVYLWT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 240 LPMFHVFGLAvITYSQLQRGNALVSMARFELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPL 319
Cdd:PLN03102 234 LPMFHCNGWT-FTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 320 GKDLMEECGRniPNVLLMQGYGMTETCGIV-------------SVEDPRLGKRNSGSAGMLApgvEAQIVSVETGKSQPP 386
Cdd:PLN03102 313 PAALVKKVQR--LGFQVMHAYGLTEATGPVlfcewqdewnrlpENQQMELKARQGVSILGLA---DVDVKNKETQESVPR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 387 NQQ--GEIWVRGPNMMKGYLNNPQATKETIdKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHP 464
Cdd:PLN03102 388 DGKtmGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 465 DILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQKFIAKQ--VAPYKRL--------RRVSFISLVPKSAAGKILRR 534
Cdd:PLN03102 467 KVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKLVTRErdLIEYCREnlphfmcpRKVVFLQELPKNGNGKILKP 546
|
..
gi 15234634 535 EL 536
Cdd:PLN03102 547 KL 548
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
55-536 |
1.34e-56 |
|
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: 195.80 E-value: 1.34e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 55 LTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSyqfPLCFLAVTAIGGVFTTANPLYTV---NEVSKQIKDSNPKIII 131
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRS---PELYFSMLGIGKIGAVICPLFSAfgpEAIRDRLENSEAKVLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 132 SVNQLFDKikgfdlpvvllgskdtveippgsnskilsfdnvMELSEPvseypfveikqsdtAALLYSSGTTGTSKGVELT 211
Cdd:cd05969 78 TTEELYER---------------------------------TDPEDP--------------TLLHYTSGTTGTPKGVLHV 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 212 HGNFIAASLMVTMDQDLMGEyhGVFLCFLPMFHVFGLAVITYSQLQRGNALVSM-ARFELELVLKNIEKFRVTHLWVVPP 290
Cdd:cd05969 111 HDAMIFYYFTGKYVLDLHPD--DIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYeGRFDAESWYGIIERVKVTVWYTAPT 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 291 VFLALSKQSI--VKKFDLSSLKYIGSGAAPLGKDLMEeCGRNIPNVLLMQGYGMTETCGIVSVEDPRLgKRNSGSAGMLA 368
Cdd:cd05969 189 AIRMLMKEGDelARKYDLSSLRFIHSVGEPLNPEAIR-WGMEVFGVPIHDTWWQTETGSIMIANYPCM-PIKPGSMGKPL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 369 PGVEAQIVSvETGKSQPPNQQGEIWVRG--PNMMKGYLNNPQATKETIdKKSWVHTGDLGYFNEDGNLYVVDRIKELIKY 446
Cdd:cd05969 267 PGVKAAVVD-ENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADDIIKT 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 447 KGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQ---DIQKFIAKQVAPYKRLRRVSFISLV 523
Cdd:cd05969 345 SGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDElkeEIINFVRQKLGAHVAPREIEFVDNL 424
|
490
....*....|...
gi 15234634 524 PKSAAGKILRREL 536
Cdd:cd05969 425 PKTRSGKIMRRVL 437
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
43-536 |
4.68e-56 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 197.43 E-value: 4.68e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 43 KLAI--ADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTtanPLYTV---NE 117
Cdd:PRK04319 60 KVALryLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVG---PLFEAfmeEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 118 VSKQIKDSNPKIIISVNQLFDKIKGFDLP----VVLLGskDTVEIPPGsnskILSFDNVMElsEPVSEYPFVEIKQSDTA 193
Cdd:PRK04319 137 VRDRLEDSEAKVLITTPALLERKPADDLPslkhVLLVG--EDVEEGPG----TLDFNALME--QASDEFDIEWTDREDGA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 194 ALLYSSGTTGTSKGVELTHGNFIAASLMVTMDQDLMGEyhGVFLC--------------FLPMFHvfGLAVItysqlqrg 259
Cdd:PRK04319 209 ILHYTSGSTGKPKGVLHVHNAMLQHYQTGKYVLDLHED--DVYWCtadpgwvtgtsygiFAPWLN--GATNV-------- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 260 nalVSMARFELELVLKNIEKFRVTHLWVVPPVFLALSKQS--IVKKFDLSSLKYIGSGAAPLGKDL----MEECGRNIPN 333
Cdd:PRK04319 277 ---IDGGRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGddLVKKYDLSSLRHILSVGEPLNPEVvrwgMKVFGLPIHD 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 334 vllmqGYGMTETCGIVSVEDPRLGKRnSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRG--PNMMKGYLNNPQATK 411
Cdd:PRK04319 354 -----NWWMTETGGIMIANYPAMDIK-PGSMGKPLPGIEAAIVD-DQGNELPPNRMGNLAIKKgwPSMMRGIWNNPEKYE 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 412 ETIdKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSP 491
Cdd:PRK04319 427 SYF-AGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRP 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 15234634 492 NSSITEQ---DIQKFIAK----QVAPykrlRRVSFISLVPKSAAGKILRREL 536
Cdd:PRK04319 506 GYEPSEElkeEIRGFVKKglgaHAAP----REIEFKDKLPKTRSGKIMRRVL 553
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
31-542 |
9.20e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 195.94 E-value: 9.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 31 SFLFRNSSSYPSKLAIADSDTgdSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTAN 110
Cdd:PRK08162 22 SFLERAAEVYPDRPAVIHGDR--RRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 111 PLYTVNEVSKQIKDSNPKIIIS-------VNQLFDKIKGFDLPVVllgskDTVEIPPGSNSKILSFDNVMELSEPVSEYP 183
Cdd:PRK08162 100 TRLDAASIAFMLRHGEAKVLIVdtefaevAREALALLPGPKPLVI-----DVDDPEYPGGRFIGALDYEAFLASGDPDFA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 184 FVEIKQS-DTAALLYSSGTTGTSKGVELTH-GNFI-AASLMVTMDqdlMGEyHGVFLCFLPMFHVFG------LAVitys 254
Cdd:PRK08162 175 WTLPADEwDAIALNYTSGTTGNPKGVVYHHrGAYLnALSNILAWG---MPK-HPVYLWTLPMFHCNGwcfpwtVAA---- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 255 qlqRGNALVSMARFELELVLKNIEKFRVTHLWVVPPVFLAL------SKQSIVKKfdlssLKYIGSGAAP----LGKdlM 324
Cdd:PRK08162 247 ---RAGTNVCLRKVDPKLIFDLIREHGVTHYCGAPIVLSALinapaeWRAGIDHP-----VHAMVAGAAPpaavIAK--M 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 325 EECGRNIPNVllmqgYGMTETCGIVSV-------------EDPRLGKRNsgsaGMLAPGVEAqiVSV---ETGKSQPPNQ 388
Cdd:PRK08162 317 EEIGFDLTHV-----YGLTETYGPATVcawqpewdalpldERAQLKARQ----GVRYPLQEG--VTVldpDTMQPVPADG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 389 Q--GEIWVRGPNMMKGYLNNPQATKETIdKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDI 466
Cdd:PRK08162 386 EtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAV 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15234634 467 LDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQKFIAKQVAPYKRLRRVSFISLvPKSAAGKILRRELVQQVRS 542
Cdd:PRK08162 465 LVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKAVVFGEL-PKTSTGKIQKFVLREQAKS 539
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
55-515 |
1.21e-55 |
|
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: 194.11 E-value: 1.21e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 55 LTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGgvfttanplytvnevskqikdsnpkiiisvn 134
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALG------------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 135 qlfdkikgfdlpvvllgskdTVEIPPGSNSKILSFDNVMELSEPVSeyPFVEIKQSDTAALLYSSGTTGTSKGVELTHGN 214
Cdd:cd17640 55 --------------------AVDVVRGSDSSVEELLYILNHSESVA--LVVENDSDDLATIIYTSGTTGNPKGVMLTHAN 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 215 FIaaSLMVTMDQDLMGEYHGVFLCFLPMFHVFGLAVITYSqLQRGnalVSMARFELELVLKNIEKFRVTHLWVVPPVFLA 294
Cdd:cd17640 113 LL--HQIRSLSDIVPPQPGDRFLSILPIWHSYERSAEYFI-FACG---CSQAYTSIRTLKDDLKRVKPHYIVSVPRLWES 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 295 L--------SKQSIVKKFDLSSLKYI--------GSGAAPLGKDLMEEcgrnIPNVLLMQGYGMTETCGIVSVEdpRLGK 358
Cdd:cd17640 187 LysgiqkqvSKSSPIKQFLFLFFLSGgifkfgisGGGALPPHVDTFFE----AIGIEVLNGYGLTETSPVVSAR--RLKC 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 359 RNSGSAGMLAPGVEAQIVSVETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKSWVHTGDLGYFNEDGNLYVVD 438
Cdd:cd17640 261 NVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 439 RIKELIKYK-GFQVAPAELEGLLVSHPDI------------LDAVVIPFPD--EEAGEVPIAFVVRSPNSSITEQDIQKF 503
Cdd:cd17640 341 RAKDTIVLSnGENVEPQPIEEALMRSPFIeqimvvgqdqkrLGALIVPNFEelEKWAKESGVKLANDRSQLLASKKVLKL 420
|
490
....*....|..
gi 15234634 504 IAKQVAPYKRLR 515
Cdd:cd17640 421 YKNEIKDEISNR 432
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
25-539 |
2.71e-55 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 194.89 E-value: 2.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 25 PNTSLVSFLFRNSSSYPSKLAIAD--SDTGDS--LTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVT 100
Cdd:PRK13295 22 HDRTINDDLDACVASCPDKTAVTAvrLGTGAPrrFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 101 AIGGVFTTANPLYTVNEVSKQIKDSNPKIIIsVNQLFdkiKGFDLPVVLLGSKDtvEIPPGSNSKIL------SFDNVme 174
Cdd:PRK13295 102 RIGAVLNPLMPIFRERELSFMLKHAESKVLV-VPKTF---RGFDHAAMARRLRP--ELPALRHVVVVggdgadSFEAL-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 175 LSEPVSEY------PFVEIKQS--DTAALLYSSGTTGTSKGVELTHGNFIAASLMVTMDQDLMGEyhGVFLCFLPMFHVF 246
Cdd:PRK13295 174 LITPAWEQepdapaILARLRPGpdDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGAD--DVILMASPMAHQT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 247 GLAVITYSQLQRGNALVSMARFELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEE 326
Cdd:PRK13295 252 GFMYGLMMPVMLGATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVER 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 327 cGRNIPNVLLMQGYGMTEtCGIVSVEDP-RLGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLN 405
Cdd:PRK13295 332 -ARAALGAKIVSAWGMTE-NGAVTLTKLdDPDERASTTDGCPLPGVEVRVVD-ADGAPLPAGQIGRLQVRGCSNFGGYLK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 406 NPQATKEtiDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIA 485
Cdd:PRK13295 409 RPQLNGT--DADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACA 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15234634 486 FVVRSPNSSITEQDIQKF-----IAKQVAPykrlRRVSFISLVPKSAAGKI----LRRELVQQ 539
Cdd:PRK13295 487 FVVPRPGQSLDFEEMVEFlkaqkVAKQYIP----ERLVVRDALPRTPSGKIqkfrLREMLRGE 545
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
190-537 |
5.10e-55 |
|
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: 192.21 E-value: 5.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 190 SDTAALLYSSGTTGTSKGVE--LTHGNFIAASLMvtMDQDLMGEYHG-VFLCFLPMFHVFGLAViTYSQLQRGNALVSMA 266
Cdd:cd05929 125 AAGWKMLYSGGTTGRPKGIKrgLPGGPPDNDTLM--AAALGFGPGADsVYLSPAPLYHAAPFRW-SMTALFMGGTLVLME 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 267 RFELELVLKNIEKFRVTHLWVVPPVFLALSK--QSIVKKFDLSSLKYIGSGAAP---LGKDLMEECGRNIpnvlLMQGYG 341
Cdd:cd05929 202 KFDPEEFLRLIERYRVTFAQFVPTMFVRLLKlpEAVRNAYDLSSLKRVIHAAAPcppWVKEQWIDWGGPI----IWEYYG 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 342 MTETCG--IVSVEDpRLGKRnsGSAGMLAPGvEAQIVSvETGKSQPPNQQGEIWVRGPNMmKGYLNNPQATKETIDKKSW 419
Cdd:cd05929 278 GTEGQGltIINGEE-WLTHP--GSVGRAVLG-KVHILD-EDGNEVPPGEIGEVYFANGPG-FEYTNDPEKTAAARNEGGW 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 420 VHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQD 499
Cdd:cd05929 352 STLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTAL 431
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 15234634 500 IQKFIA---KQVAPYKRLRRVSFISLVPKSAAGKILRRELV 537
Cdd:cd05929 432 AEELIAflrDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
54-536 |
6.77e-55 |
|
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: 191.14 E-value: 6.77e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 54 SLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIIIsv 133
Cdd:cd05919 10 SVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVV-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 134 nqlfdkikgfdlpvvllgskdtveippgsnskilsfdnvmelsepvseypfveIKQSDTAALLYSSGTTGTSKGVELTHG 213
Cdd:cd05919 88 -----------------------------------------------------TSADDIAYLLYSSGTTGPPKGVMHAHR 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 214 NFIAASlmvtmdqDLMG-EYHG-----VFLCFLPMFHVFGLAVITYSQLQRG-NALVSMARFELELVLKNIEKFRVTHLW 286
Cdd:cd05919 115 DPLLFA-------DAMArEALGltpgdRVFSSAKMFFGYGLGNSLWFPLAVGaSAVLNPGWPTAERVLATLARFRPTVLY 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 287 VVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPL----GKDLMEECGRNIpnvllMQGYGMTETcGIVSVEDpRLGKRNSG 362
Cdd:cd05919 188 GVPTFYANLLDSCAGSPDALRSLRLCVSAGEALprglGERWMEHFGGPI-----LDGIGATEV-GHIFLSN-RPGAWRLG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 363 SAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIdKKSWVHTGDLGYFNEDGNLYVVDRIKE 442
Cdd:cd05919 261 STGRPVPGYEIRLVD-EEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGRADD 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 443 LIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITE---QDIQKFIAKQVAPYKRLRRVSF 519
Cdd:cd05919 339 MLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQEslaRDIHRHLLERLSAHKVPRRIAF 418
|
490
....*....|....*..
gi 15234634 520 ISLVPKSAAGKILRREL 536
Cdd:cd05919 419 VDELPRTATGKLQRFKL 435
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
192-540 |
1.33e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 191.36 E-value: 1.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 192 TAALLYSSGTTGTSKGVELTHgNFIAASLMVTMD------QDLMGeyHGvflcfLPMFHVFGLAVITYSQLQRGNALVSM 265
Cdd:PRK07787 130 PALIVYTSGTTGPPKGVVLSR-RAIAADLDALAEawqwtaDDVLV--HG-----LPLFHVHGLVLGVLGPLRIGNRFVHT 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 266 ARFELELVLKNIEkFRVTHLWVVPPVFLALSKQSIVKKfDLSSLKYIGSGAAPL----GKDLMEECGRNIpnvllMQGYG 341
Cdd:PRK07787 202 GRPTPEAYAQALS-EGGTLYFGVPTVWSRIAADPEAAR-ALRGARLLVSGSAALpvpvFDRLAALTGHRP-----VERYG 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 342 MTETCGIVSVE-DprlGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQ--GEIWVRGPNMMKGYLNNPQATKETIDKKS 418
Cdd:PRK07787 275 MTETLITLSTRaD---GERRPGWVGLPLAGVETRLVD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADG 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 419 WVHTGDLGYFNEDGNLYVVDRIK-ELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVrsPNSSITE 497
Cdd:PRK07787 351 WFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV--GADDVAA 428
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 15234634 498 QDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRRELVQQV 540
Cdd:PRK07787 429 DELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSEG 471
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
45-539 |
4.65e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 191.50 E-value: 4.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 45 AIADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKD 124
Cdd:PRK06164 26 AVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 125 SNPKIIIsvnqLFDKIKGFDLPVVLLGSKDTVEIP-------PGSNSKI---LSFDNVMELSEPVSEYP---FVEIKQSD 191
Cdd:PRK06164 106 GRARWLV----VWPGFKGIDFAAILAAVPPDALPPlraiavvDDAADATpapAPGARVQLFALPDPAPPaaaGERAADPD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 192 TAALLYS-SGTTGTSKGVE------LTHGNFIAASLmvTMDQDlmgeyhGVFLCFLPMFHVFGLAVITySQLQRGNALVS 264
Cdd:PRK06164 182 AGALLFTtSGTTSGPKLVLhrqatlLRHARAIARAY--GYDPG------AVLLAALPFCGVFGFSTLL-GALAGGAPLVC 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 265 MARFELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKfDLSSLKYIGSGA-APLGKDLMEE-CGRNIPNVLLmqgYGM 342
Cdd:PRK06164 253 EPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERA-DFPSARLFGFASfAPALGELAALaRARGVPLTGL---YGS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 343 TETCGIVS---VEDPRLGKRNSGsaGMLA-PGVEAQIVSVETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKS 418
Cdd:PRK06164 329 SEVQALVAlqpATDPVSVRIEGG--GRPAsPEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 419 WVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFpDEEAGEVPIAFVVRSPNSSITEQ 498
Cdd:PRK06164 407 YFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA-TRDGKTVPVAFVIPTDGASPDEA 485
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 15234634 499 DIQKFIAKQVAPYKRLRRVSFISLVPKSAAG---KILRRELVQQ 539
Cdd:PRK06164 486 GLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREM 529
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
55-476 |
7.44e-53 |
|
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: 188.19 E-value: 7.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 55 LTFSQLKSAVARLAHGFHRLGIR--KNDVVLIFAPNSYQFPLCFLAVTAIGGVFTtanPLY---TVNEVSKQIKDSNPKI 129
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTV---PLYdtlGPEAIEYILNHAEISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 130 IIsvnqlFDKikgfdlpvvllgskdtveippgsNSKILSFDNVMELSEPvSEYPFVEIKQSDTAALLYSSGTTGTSKGVE 209
Cdd:cd05927 83 VF-----CDA-----------------------GVKVYSLEEFEKLGKK-NKVPPPPPKPEDLATICYTSGTTGNPKGVM 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 210 LTHGNFIA--ASLMVTMDQDLMGEYHGVFLCFLPMFHVFGLAVITYSqLQRGnALVSMARFELELVLKNIEKFRVTHLWV 287
Cdd:cd05927 134 LTHGNIVSnvAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALF-LYHG-AKIGFYSGDIRLLLDDIKALKPTVFPG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 288 VPPVF--------LALSKQSIVKKF-----------DLSS------------------------LKYIGSGAAPLGKDLM 324
Cdd:cd05927 212 VPRVLnriydkifNKVQAKGPLKRKlfnfalnyklaELRSgvvraspfwdklvfnkikqalggnVRLMLTGSAPLSPEVL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 325 EECgRNIPNVLLMQGYGMTETCGIVSVEDPrlGKRNSGSAGMLAPGVEAQIVSV-ETG-KSQPPNQQGEIWVRGPNMMKG 402
Cdd:cd05927 292 EFL-RVALGCPVLEGYGQTECTAGATLTLP--GDTSVGHVGGPLPCAEVKLVDVpEMNyDAKDPNPRGEVCIRGPNVFSG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 403 YLNNPQATKETIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKY-KGFQVAPAELEGLLVSHPDI-------------LD 468
Cdd:cd05927 369 YYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSPFVaqifvygdslksfLV 448
|
....*...
gi 15234634 469 AVVIPFPD 476
Cdd:cd05927 449 AIVVPDPD 456
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
28-536 |
1.25e-52 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 187.66 E-value: 1.25e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 28 SLVSFLFRNSSSYPSKLAIADSDTgdSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFT 107
Cdd:PRK06155 22 TLPAMLARQAERYPDRPLLVFGGT--RWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 108 TANPLYTVNEVSKQIKDSNPKIIISVNQLFDKIKGFDLP------VVLLGSKDTVEIPPGsnskiLSFDNVMELSEPVse 181
Cdd:PRK06155 100 PINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGdlplpaVWLLDAPASVSVPAG-----WSTAPLPPLDAPA-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 182 yPFVEIKQSDTAALLYSSGTTGTSKGVELTHGNF------IAASLMVTMDQdlmgeyhgVFLCFLPMFHVFGLAviTYSQ 255
Cdd:PRK06155 173 -PAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFywwgrnSAEDLEIGADD--------VLYTTLPLFHTNALN--AFFQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 256 lqrgnALVSMARFELElvlkniEKFRVTHLWVvppvflALSKQSIVKKFDLSSLKYI--------------------GSG 315
Cdd:PRK06155 242 -----ALLAGATYVLE------PRFSASGFWP------AVRRHGATVTYLLGAMVSIllsqparesdrahrvrvalgPGV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 316 AAPLGKDLMEECGrnipnVLLMQGYGMTETCGIVSVedpRLGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVR 395
Cdd:PRK06155 305 PAALHAAFRERFG-----VDLLDGYGSTETNFVIAV---THGSQRPGSMGRLAPGFEARVVD-EHDQELPDGEPGELLLR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 396 GPN---MMKGYLNNPQATKETIdKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVI 472
Cdd:PRK06155 376 ADEpfaFATGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVF 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15234634 473 PFPDEEAG-EVPIAFVVRsPNSSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:PRK06155 455 PVPSELGEdEVMAAVVLR-DGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
191-538 |
1.90e-52 |
|
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: 181.38 E-value: 1.90e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 191 DTAALLYSSGTTGTSKGVELTHGNFIAASLMVtmdQDLMGEY-HGVFLCFLPMFHVFGLAVITYSQLQrGNALVSMARfe 269
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGL---HSRLGFGgGDSWLLSLPLYHVGGLAILVRSLLA-GAELVLLER-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 270 LELVLKNIEKFRVTHLWVVPPVFLAL--SKQSIVkkfDLSSLKYIGSGAAPLGKDLMEEC-GRNIPnvlLMQGYGMTETC 346
Cdd:cd17630 75 NQALAEDLAPPGVTHVSLVPTQLQRLldSGQGPA---ALKSLRAVLLGGAPIPPELLERAaDRGIP---LYTTYGMTETA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 347 GIVSVEDPRLGKRnsGSAGMLAPGVEAQIVsvetgksqppnQQGEIWVRGPNMMKGYLNNPqaTKETIDKKSWVHTGDLG 426
Cdd:cd17630 149 SQVATKRPDGFGR--GGVGVLLPGRELRIV-----------EDGEIWVGGASLAMGYLRGQ--LVPEFNEDGWFTTKDLG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 427 YFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVrsPNSSITEQDIQKFIAK 506
Cdd:cd17630 214 ELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIV--GRGPADPAELRAWLKD 291
|
330 340 350
....*....|....*....|....*....|..
gi 15234634 507 QVAPYKRLRRVSFISLVPKSAAGKILRRELVQ 538
Cdd:cd17630 292 KLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
41-536 |
3.52e-52 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 186.12 E-value: 3.52e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 41 PSKLAIADsDTGdSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSK 120
Cdd:PRK13382 57 PDRPGLID-ELG-TLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 121 QIKDSNPKIIIsVNQLFDKIkgfdLPVVLLGSKDTVEIPPGSNSKILSFDNVMeLSEPVSEYPFVEIKQSDTaaLLYSSG 200
Cdd:PRK13382 135 VVTREGVDTVI-YDEEFSAT----VDRALADCPQATRIVAWTDEDHDLTVEVL-IAAHAGQRPEPTGRKGRV--ILLTSG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 201 TTGTSKGVELThGNFIAASLMVTMDQDLMgEYHGVFLCFLPMFHVFGLAVITYSQLQRgNALVSMARFELELVLKNIEKF 280
Cdd:PRK13382 207 TTGTPKGARRS-GPGGIGTLKAILDRTPW-RAEEPTVIVAPMFHAWGFSQLVLAASLA-CTIVTRRRFDPEATLDLIDRH 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 281 RVTHLWVVPPVF---LALSKQsIVKKFDLSSLKYIGSGAAPLGKDL----MEECGRNIPNvllmqGYGMTETcGIVSVED 353
Cdd:PRK13382 284 RATGLAVVPVMFdriMDLPAE-VRNRYSGRSLRFAAASGSRMRPDVviafMDQFGDVIYN-----NYNATEA-GMIATAT 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 354 PRLGKRNSGSAGMLAPGVEAQIVSVEtGKSQPPNQQGEIWVRGPNMMKGYlnNPQATKETIDkkSWVHTGDLGYFNEDGN 433
Cdd:PRK13382 357 PADLRAAPDTAGRPAEGTEIRILDQD-FREVPTGEVGTIFVRNDTQFDGY--TSGSTKDFHD--GFMASGDVGYLDENGR 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 434 LYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQKFIAKQVAPYKR 513
Cdd:PRK13382 432 LFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDNLANYKV 511
|
490 500
....*....|....*....|...
gi 15234634 514 LRRVSFISLVPKSAAGKILRREL 536
Cdd:PRK13382 512 PRDIVVLDELPRGATGKILRREL 534
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
56-471 |
5.48e-52 |
|
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: 182.47 E-value: 5.48e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 56 TFSQLKSAVARLAHGFH-RLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIIISVN 134
Cdd:TIGR01733 1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 135 QLFDKIKGFDLPVVLLGSKDTVEIPPgsnskilsfdnvmelsEPVSEYPFVEIKQSDTAALLYSSGTTGTSKGVELTHGN 214
Cdd:TIGR01733 81 ALASRLAGLVLPVILLDPLELAALDD----------------APAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 215 fIAASLMVTMDQDLMGEYHgVFLCFLPmfHVFGLAVI-TYSQLQRGNALV----SMARFELELVLKNIEKFRVTHLWVVP 289
Cdd:TIGR01733 145 -LVNLLAWLARRYGLDPDD-RVLQFAS--LSFDASVEeIFGALLAGATLVvppeDEERDDAALLAALIAEHPVTVLNLTP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 290 PVFLALSKQSIvkkFDLSSLKYIGSGAAPLGKDLMEECGRNIPNVLLMQGYGMTET---CGIVSVEDPRLGKRNSGSAGM 366
Cdd:TIGR01733 221 SLLALLAAALP---PALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETtvwSTATLVDPDDAPRESPVPIGR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 367 LAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKE--------TIDKKSWVHTGDLGYFNEDGNLYVVD 438
Cdd:TIGR01733 298 PLANTRLYVLD-DDLRPVPVGVVGELYIGGPGVARGYLNRPELTAErfvpdpfaGGDGARLYRTGDLVRYLPDGNLEFLG 376
|
410 420 430
....*....|....*....|....*....|...
gi 15234634 439 RIKELIKYKGFQVAPAELEGLLVSHPDILDAVV 471
Cdd:TIGR01733 377 RIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
52-533 |
2.36e-51 |
|
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: 182.26 E-value: 2.36e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 52 GDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIIi 131
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 132 svnqlfdkikgfdlpvvllgskdtveippgsnskilsfdnvmelsepvseypFVEiKQSDTAALLYSSGTTGTSKGVELT 211
Cdd:cd05914 84 ----------------------------------------------------FVS-DEDDVALINYTSGTTGNSKGVMLT 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 212 HGNfIAASLMVTMDQDLMGEyHGVFLCFLPMFHVFGLAVITYSQLQRGNALVSMARFELELVLKnIEKFRVT------HL 285
Cdd:cd05914 111 YRN-IVSNVDGVKEVVLLGK-GDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAKIIA-LAFAQVTptlgvpVP 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 286 WVV---------PPVFLALSKQSIVKK-FDLS---------------SLKYIGSGAAPLGKDLmEECGRNIpNVLLMQGY 340
Cdd:cd05914 188 LVIekifkmdiiPKLTLKKFKFKLAKKiNNRKirklafkkvheafggNIKEFVIGGAKINPDV-EEFLRTI-GFPYTIGY 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 341 GMTETCGIVSVEDPrlGKRNSGSAGMLAPGVEAQIVSvetgkSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKSWV 420
Cdd:cd05914 266 GMTETAPIISYSPP--NRIRLGSAGKVIDGVEVRIDS-----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWF 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 421 HTGDLGYFNEDGNLYVVDRIKELI-KYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPI--------AFVVRSP 491
Cdd:cd05914 339 HTGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLVALAYIdpdfldvkALKQRNI 418
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 15234634 492 NSSITEQDIQKfIAKQVAPYKRLRRVSFISL-VPKSAAGKILR 533
Cdd:cd05914 419 IDAIKWEVRDK-VNQKVPNYKKISKVKIVKEeFEKTPKGKIKR 460
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
190-536 |
3.04e-51 |
|
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: 179.21 E-value: 3.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 190 SDTAALLYSSGTTGTSKGVELTHGNFIAASLMvtMDQDLMGEYHGVFLCFLPMFHVFGLAVITYSQLQRGNALV--SMAR 267
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWM--LALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVlaGPAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 268 FELELVLKN----IEKFRVTHLWVVPPVFLALSKQSIvkKFDLSSLKYIGSGAAPLGKDLmeecGRNIPN---VLLMQGY 340
Cdd:cd05944 80 YRNPGLFDNfwklVERYRITSLSTVPTVYAALLQVPV--NADISSLRFAMSGAAPLPVEL----RARFEDatgLPVVEGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 341 GMTETCGIVSVeDPRLGKRNSGSAGMLAPGVEAQIVsVETGKSQP-----PNQQGEIWVRGPNMMKGYLNNPQATKETID 415
Cdd:cd05944 154 GLTEATCLVAV-NPPDGPKRPGSVGLRLPYARVRIK-VLDGVGRLlrdcaPDEVGEICVAGPGVFGGYLYTEGNKNAFVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 416 KKsWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSI 495
Cdd:cd05944 232 DG-WLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVV 310
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 15234634 496 TEQDIQKFIAKQVAPYKRL-RRVSFISLVPKSAAGKILRREL 536
Cdd:cd05944 311 EEEELLAWARDHVPERAAVpKHIEVLEELPVTAVGKVFKPAL 352
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
45-536 |
4.61e-51 |
|
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: 181.29 E-value: 4.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 45 AIADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKD 124
Cdd:cd05945 7 RPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 125 SNPKIIISVnqlfdkikgfdlpvvllgskdtveippgsnskilsfdnvmelsepvseypfveikQSDTAALLYSSGTTGT 204
Cdd:cd05945 87 AKPALLIAD-------------------------------------------------------GDDNAYIIFTSGSTGR 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 205 SKGVELTHGN---FIAAslmvtMDQDLMGEYHGVFLCFLPmFHvFGLAVIT-YSQLQRGNALVS----MARFELELVlKN 276
Cdd:cd05945 112 PKGVQISHDNlvsFTNW-----MLSDFPLGPGDVFLNQAP-FS-FDLSVMDlYPALASGATLVPvprdATADPKQLF-RF 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 277 IEKFRVTHlWVVPPVFLALSKQSivKKFD---LSSLKYIGSGAAPLGKDLMEECGRNIPNVLLMQGYGMTETCGIVSVED 353
Cdd:cd05945 184 LAEHGITV-WVSTPSFAAMCLLS--PTFTpesLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIE 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 354 PR---LGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKE---TIDKKSWVHTGDLGY 427
Cdd:cd05945 261 VTpevLDGYDRLPIGYAKPGAKLVILD-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAaffPDEGQRAYRTGDLVR 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 428 FNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSIT-EQDIQKFIAK 506
Cdd:cd05945 340 LEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGlTKAIKAELAE 419
|
490 500 510
....*....|....*....|....*....|
gi 15234634 507 QVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:cd05945 420 RLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
51-531 |
1.75e-50 |
|
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: 180.61 E-value: 1.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 51 TGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFaPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKII 130
Cdd:cd05909 4 LGTSLTYRKLLTGAIALARKLAKMTKEGENVGVML-PPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 131 ISVNQLFDKIKGFDLPVVLLGSK----DTVEIPPGSNSKILSFDNVMELSEPVSEYPFVEIKQS-DTAALLYSSGTTGTS 205
Cdd:cd05909 83 LTSKQFIEKLKLHHLFDVEYDARivylEDLRAKISKADKCKAFLAGKFPPKWLLRIFGVAPVQPdDPAVILFTSGSEGLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 206 KGVELTHGNFIAASLMVTMDQDLMGEyhGVFLCFLPMFHVFGLAVITYSQLQRGNALVSMAR-FELELVLKNIEKFRVTH 284
Cdd:cd05909 163 KGVVLSHKNLLANVEQITAIFDPNPE--DVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNpLDYKKIPELIYDKKATI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 285 LWVVPPVFLALSKQsiVKKFDLSSLKYIGSGAAPLGKDLMEECgRNIPNVLLMQGYGMTETCGIVSVEDPRLGKRnSGSA 364
Cdd:cd05909 241 LLGTPTFLRGYARA--AHPEDFSSLRLVVAGAEKLKDTLRQEF-QEKFGIRILEGYGTTECSPVISVNTPQSPNK-EGTV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 365 GMLAPGVEAQIVSVETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIdKKSWVHTGDLGYFNEDGNLYVVDRIKELI 444
Cdd:cd05909 317 GRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 445 KYKGFQVAPAELEGLL--VSHPDILDAVVIpFPDEEAGEVPIAFVVRSPNSSITEQDIQKfiAKQVAPYKRLRRVSFISL 522
Cdd:cd05909 396 KIAGEMVSLEAIEDILseILPEDNEVAVVS-VPDGRKGEKIVLLTTTTDTDPSSLNDILK--NAGISNLAKPSYIHQVEE 472
|
....*....
gi 15234634 523 VPKSAAGKI 531
Cdd:cd05909 473 IPLLGTGKP 481
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
48-541 |
2.35e-50 |
|
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: 181.28 E-value: 2.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 48 DSDTGDSLTFSQLKSAVARLAHGFHRLGiRKNDVVLIFAPNSYQFPLCFLAVTAIGGVfttANPLY------TVNEVSKQ 121
Cdd:cd05931 18 EGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAI---AVPLPpptpgrHAERLAAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 122 IKDSNPKIIISVNQLFDKIKGFdlpvvllgskdTVEIPPGSNSKILSFDNVMelSEPVSEYPFVEIKQSDTAALLYSSGT 201
Cdd:cd05931 94 LADAGPRVVLTTAAALAAVRAF-----------AASRPAAGTPRLLVVDLLP--DTSAADWPPPSPDPDDIAYLQYTSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 202 TGTSKGVELTHGNFIAAslMVTMDQDLMGEYHGVFLCFLPMFHVFGLAVITYSQLQRGNALVSMA---------RFelel 272
Cdd:cd05931 161 TGTPKGVVVTHRNLLAN--VRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSpaaflrrplRW---- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 273 vLKNIEKFRVTHlwVVPPVF---LALSKQSIVKK--FDLSSLKYIGSGAAPLGKDLMEE-------CGrnIPNVLLMQGY 340
Cdd:cd05931 235 -LRLISRYRATI--SAAPNFaydLCVRRVRDEDLegLDLSSWRVALNGAEPVRPATLRRfaeafapFG--FRPEAFRPSY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 341 GMTETCGIVS------------VEDPRLGKRNSG------------SAGMLAPGVEAQIVSVETGKSQPPNQQGEIWVRG 396
Cdd:cd05931 310 GLAEATLFVSggppgtgpvvlrVDRDALAGRAVAvaaddpaarelvSCGRPLPDQEVRIVDPETGRELPDGEVGEIWVRG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 397 PNMMKGYLNNPQATKET------IDKKSWVHTGDLGYFNeDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILD-- 468
Cdd:cd05931 390 PSVASGYWGRPEATAETfgalaaTDEGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRpg 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 469 ---AVVIPFPDEEAGEVPIAfVVRSPNSSIT---EQDIQKFIAKQ--VAPykrlRRVSFISL--VPKSAAGKILRRELVQ 538
Cdd:cd05931 469 cvaAFSVPDDGEERLVVVAE-VERGADPADLaaiAAAIRAAVAREhgVAP----ADVVLVRPgsIPRTSSGKIQRRACRA 543
|
...
gi 15234634 539 QVR 541
Cdd:cd05931 544 AYL 546
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
28-531 |
3.85e-50 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 185.90 E-value: 3.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 28 SLVSFLFRNSSSYPSKLAIADSdTGDSLTFSQLKSAVARLAHGFHRLgIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVft 107
Cdd:PRK08633 616 PLAEAWIDTAKRNWSRLAVADS-TGGELSYGKALTGALALARLLKRE-LKDEENVGILLPPSVAGALANLALLLAGKV-- 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 108 TANPLYTVNEVSKQ--IKDSNPKIIISVNQLFDKIKG------FDLPVVLLGSKDTVEiPPGSNSKILSFDNVMEL-SEP 178
Cdd:PRK08633 692 PVNLNYTASEAALKsaIEQAQIKTVITSRKFLEKLKNkgfdleLPENVKVIYLEDLKA-KISKVDKLTALLAARLLpARL 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 179 VSEYPFVEIKQSDTAALLYSSGTTGTSKGVELTHGNFIAASLmvTMDQDLMGEYHGVFLCFLPMFHVFGLAVITYSQLQR 258
Cdd:PRK08633 771 LKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIE--QISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLE 848
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 259 GNALVSMAR-FELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECgRNIPNVLLM 337
Cdd:PRK08633 849 GIKVVYHPDpTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADAF-EEKFGIRIL 927
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 338 QGYGMTETCGIVSV--------EDPRLGKRNSGSAGMLAPGVEAQIVSVETGKSQPPNQQGEIWVRGPNMMKGYLNNPQA 409
Cdd:PRK08633 928 EGYGATETSPVASVnlpdvlaaDFKRQTGSKEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEK 1007
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 410 TKE---TIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLL--VSHPDILDAVVIPFPDEEAGEvpi 484
Cdd:PRK08633 1008 TAEvikDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELakALGGEEVVFAVTAVPDEKKGE--- 1084
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15234634 485 AFVVRSPNSSITEQDIQKFIAKQVAPykRLRRVSFISLV---PKSAAGKI 531
Cdd:PRK08633 1085 KLVVLHTCGAEDVEELKRAIKESGLP--NLWKPSRYFKVealPLLGSGKL 1132
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
18-542 |
6.15e-50 |
|
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: 180.17 E-value: 6.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 18 TLVLPKDPNTSLVSFLFRNSSSYPSK--LAIADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLC 95
Cdd:cd05906 1 PLHRPEGAPRTLLELLLRAAERGPTKgiTYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 96 FLAVTAIGGVFTTANPLYTVNEVSKQIKDsnpkiIISVNQLFDKikgfdlPVVLLGSKDTVEIPP---GSNSKILSFDNV 172
Cdd:cd05906 81 FWACVLAGFVPAPLTVPPTYDEPNARLRK-----LRHIWQLLGS------PVVLTDAELVAEFAGletLSGLPGIRVLSI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 173 MELSEPVSEYPFVEIKQSDTAALLYSSGTTGTSKGVELTHGNFIAASLMVTMDQDLMGEyhGVFLCFLPMFHVfglAVIT 252
Cdd:cd05906 150 EELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQ--DVFLNWVPLDHV---GGLV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 253 YSQLQRGNALVSMARFELELVLKN-------IEKFRVTHLWVvPPVFLALSKQSIVK----KFDLSSLKYIGSGA----A 317
Cdd:cd05906 225 ELHLRAVYLGCQQVHVPTEEILADplrwldlIDRYRVTITWA-PNFAFALLNDLLEEiedgTWDLSSLRYLVNAGeavvA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 318 PLGKDLM---EECGRNiPNVLlMQGYGMTETCG--IVSVEDPRLGKRNSG---SAGMLAPGVEAQIVSvETGKSQPPNQQ 389
Cdd:cd05906 304 KTIRRLLrllEPYGLP-PDAI-RPAFGMTETCSgvIYSRSFPTYDHSQALefvSLGRPIPGVSMRIVD-DEGQLLPEGEV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 390 GEIWVRGPNMMKGYLNNPQATKETIDKKSWVHTGDLGYFnEDGNLYVVDRIKELIKYKGFQVAPAELEgllvshpdildA 469
Cdd:cd05906 381 GRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFL-DNGNLTITGRTKDTIIVNGVNYYSHEIE-----------A 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 470 VVipfpdEEAGEVPI----AFVVRSPNSSiTEQDIQKFIAKQVAPYKRLRRVSFI--------------------SLVPK 525
Cdd:cd05906 449 AV-----EEVPGVEPsftaAFAVRDPGAE-TEELAIFFVPEYDLQDALSETLRAIrsvvsrevgvspayliplpkEEIPK 522
|
570
....*....|....*..
gi 15234634 526 SAAGKILRRELVQQVRS 542
Cdd:cd05906 523 TSLGKIQRSKLKAAFEA 539
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
55-541 |
1.23e-48 |
|
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: 175.87 E-value: 1.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 55 LTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPnsyqfplcflavtaiggvfTTANPLYTVNEVSKQikdsnpkiiisvn 134
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAE-------------------TRAEWLITALGCWSQ------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 135 qlfdkikgfDLPVVllgskdTVeippgsnskilsFDNVME------LSEPVSEYPFVEIKQSDTAALLYSSGTTGTSKGV 208
Cdd:cd17639 54 ---------NIPIV------TV------------YATLGEdalihsLNETECSAIFTDGKPDDLACIMYTSGSTGNPKGV 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 209 ELTHGNFIAAslMVTMDQDLmGEYHG---VFLCFLPMFHVFGLAViTYSQLQRGNAL-VSMARFELELVLKN----IEKF 280
Cdd:cd17639 107 MLTHGNLVAG--IAGLGDRV-PELLGpddRYLAYLPLAHIFELAA-ENVCLYRGGTIgYGSPRTLTDKSKRGckgdLTEF 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 281 RVTHLWVVPPVF-------LA-LSKQSIVKK--FDLS-------------------------------SLKYIGSGAAPL 319
Cdd:cd17639 183 KPTLMVGVPAIWdtirkgvLAkLNPMGGLKRtlFWTAyqsklkalkegpgtplldelvfkkvraalggRLRYMLSGGAPL 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 320 GKDLMEecgrnIPNVLL---MQGYGMTETCGIVSVEDPrlGKRNSGSAGMLAPGVEAQIVSVETGKSQP--PNQQGEIWV 394
Cdd:cd17639 263 SADTQE-----FLNIVLcpvIQGYGLTETCAGGTVQDP--GDLETGRVGPPLPCCEIKLVDWEEGGYSTdkPPPRGEILI 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 395 RGPNMMKGYLNNPQATKETIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYK-GFQVAPAELEGLLVSHPDILDAVVIP 473
Cdd:cd17639 336 RGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYA 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15234634 474 FPDEEAgevPIAFVVrsPNssitEQDIQKFIAKQVAPY---------KRLRRVSFISLVPKSAAGKILRRELVQQVR 541
Cdd:cd17639 416 DPDKSY---PVAIVV--PN----EKHLTKLAEKHGVINseweelcedKKLQKAVLKSLAETARAAGLEKFEIPQGVV 483
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
50-539 |
2.21e-48 |
|
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: 175.73 E-value: 2.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 50 DTGDSL--TFSQLKSAVARLAHGFHRL-GIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSN 126
Cdd:cd05928 35 GKGDEVkwSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 127 PKIIISVNQLFDKIKGFDLPVVLLGSKDTVEipPGSNSKILSFDNVMELSEPvsEYPFVEIKQSDTAALLYSSGTTGTSK 206
Cdd:cd05928 115 AKCIVTSDELAPEVDSVASECPSLKTKLLVS--EKSRDGWLNFKELLNEAST--EHHCVETGSQEPMAIYFTSGTTGSPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 207 GVELTHGNFiaaSLMVTMDqdlmgeyhGVFLCFLPMFHVF------GLAVITYSQL----QRGNALV--SMARFELELVL 274
Cdd:cd05928 191 MAEHSHSSL---GLGLKVN--------GRYWLDLTASDIMwntsdtGWIKSAWSSLfepwIQGACVFvhHLPRFDPLVIL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 275 KNIEKFRVTHLWVVPPVFLALSKQSIvKKFDLSSLKYIGSGAAPLGKDLMEECgRNIPNVLLMQGYGMTETCGIVSVedP 354
Cdd:cd05928 260 KTLSSYPITTFCGAPTVYRMLVQQDL-SSYKFPSLQHCVTGGEPLNPEVLEKW-KAQTGLDIYEGYGQTETGLICAN--F 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 355 RLGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVR-GPN----MMKGYLNNPQATKETIDKKSWVhTGDLGYFN 429
Cdd:cd05928 336 KGMKIKPGSMGKASPPYDVQIID-DNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIRGDFYL-TGDRGIMD 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 430 EDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSP--NSSITEQ---DIQKFI 504
Cdd:cd05928 414 EDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPqfLSHDPEQltkELQQHV 493
|
490 500 510
....*....|....*....|....*....|....*
gi 15234634 505 AKQVAPYKRLRRVSFISLVPKSAAGKILRRELVQQ 539
Cdd:cd05928 494 KSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
191-529 |
5.68e-48 |
|
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: 169.40 E-value: 5.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 191 DTAALLYSSGTTGTSKGVELTHGNFIAASLMVTMDQDLMGEYhgVFLCFLPMFHV----FGLAVitysqLQRGNALVSMA 266
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGT--VFLNSGPLFHIgtlmFTLAT-----FHAGGTNVFVR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 267 RFELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLkYIGSGAAPLGKDLMEEcgrNIPNVLLMQGYGMTETC 346
Cdd:cd17636 74 RVDAEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSL-RSSPAAPEWNDMATVD---TSPWGRKPGGYGQTEVM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 347 GIVSVedPRLGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIdKKSWVHTGDLG 426
Cdd:cd17636 150 GLATF--AALGGGAIGGAGRPSPLVQVRILD-EDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT-RGGWHHTNDLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 427 YFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQKFIAK 506
Cdd:cd17636 226 RREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRA 305
|
330 340
....*....|....*....|...
gi 15234634 507 QVAPYKRLRRVSFISLVPKSAAG 529
Cdd:cd17636 306 RIASYKKPKSVEFADALPRTAGG 328
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
54-536 |
4.95e-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: 169.97 E-value: 4.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 54 SLTFSQLKSAVARLAHGF-HRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIIIS 132
Cdd:cd05958 10 EWTYRDLLALANRIANVLvGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVALC 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 133 VNQLfdkikgfdlpvvllgskDTVEippgsnskilsfdnvmelsepvseypfveikqsDTAALLYSSGTTGTSKGVELTH 212
Cdd:cd05958 90 AHAL-----------------TASD---------------------------------DICILAFTSGTTGAPKATMHFH 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 213 GNFIAASLMVTMdQDLMGEYHGVFLCFLPMFHVFGLAVITYSQLQRGNALVSMARFELELVLKNIEKFRVTHLWVVPPVF 292
Cdd:cd05958 120 RDPLASADRYAV-NVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYKPTVLFTAPTAY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 293 LALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECgRNIPNVLLMQGYGMTETCGIVSVEDPrlGKRNSGSAGMLAPGVE 372
Cdd:cd05958 199 RAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAW-KEATGIPIIDGIGSTEMFHIFISARP--GDARPGATGKPVPGYE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 373 AQIVSvETGKSQPPNQQGEIWVRGPNmmkGYLNNPQATKETIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVA 452
Cdd:cd05958 276 AKVVD-DEGNPVPDGTIGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 453 PAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQ---DIQKFIAKQVAPYKRLRRVSFISLVPKSAAG 529
Cdd:cd05958 352 PPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVlarELQDHAKAHIAPYKYPRAIEFVTELPRTATG 431
|
....*..
gi 15234634 530 KILRREL 536
Cdd:cd05958 432 KLQRFAL 438
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
41-532 |
1.03e-45 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 169.29 E-value: 1.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 41 PSKLAI----ADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVN 116
Cdd:cd17634 67 GDRTAIiyegDDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 117 EVSKQIKDSNPKIIISVNQLFDKIKGFDL-------------PV--VLLGSKDTVEIPpGSNSKILSFDNVMELSEPvsE 181
Cdd:cd17634 147 AVAGRIIDSSSRLLITADGGVRAGRSVPLkknvddalnpnvtSVehVIVLKRTGSDID-WQEGRDLWWRDLIAKASP--E 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 182 YPFVEIKQSDTAALLYSSGTTGTSKGVELTHGNFIAASlmvTMDQDLMGEYHG--VFLCFLPMFHVFGLAVITYSQLQRG 259
Cdd:cd17634 224 HQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYA---ATTMKYVFDYGPgdIYWCTADVGWVTGHSYLLYGPLACG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 260 NALV---------SMARFelelvLKNIEKFRVTHLWVVPPVFLALSKQ--SIVKKFDLSSLKYIGSGAAPLGKDLMEECG 328
Cdd:cd17634 301 ATTLlyegvpnwpTPARM-----WQVVDKHGVNILYTAPTAIRALMAAgdDAIEGTDRSSLRILGSVGEPINPEAYEWYW 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 329 RNIPNVL--LMQGYGMTETCGIVSVEDPRLGKRNSGSAGMLAPGVEAQIVSVEtGKSQPPNQQGEIWVRG--PNMMKGYL 404
Cdd:cd17634 376 KKIGKEKcpVVDTWWQTETGGFMITPLPGAIELKAGSATRPVFGVQPAVVDNE-GHPQPGGTEGNLVITDpwPGQTRTLF 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 405 NNPQATKETI---DKKSWVHtGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGE 481
Cdd:cd17634 455 GDHERFEQTYfstFKGMYFS-GDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQ 533
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 15234634 482 VPIAFVVRSPN---SSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKIL 532
Cdd:cd17634 534 APYAYVVLNHGvepSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
41-539 |
2.40e-45 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 167.37 E-value: 2.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 41 PSKLAIADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSK 120
Cdd:PRK05852 30 PEAPALVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 121 QIKDSNPKIIisvnqLFDKIKGFD--------LPVVLLGSKDTveiPPGSNSKILSFDNVMELSePVSEYPfvEIKQSDT 192
Cdd:PRK05852 110 RSQAAGARVV-----LIDADGPHDraepttrwWPLTVNVGGDS---GPSGGTLSVHLDAATEPT-PATSTP--EGLRPDD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 193 AALLYSSGTTGTSKGVELTHGNfIAASLMVTMDQDLMGEYHGVfLCFLPMFHVFGLAVITYSQLQRGNA--LVSMARFEL 270
Cdd:PRK05852 179 AMIMFTGGTTGLPKMVPWTHAN-IASSVRAIITGYRLSPRDAT-VAVMPLYHGHGLIAALLATLASGGAvlLPARGRFSA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 271 ELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDL--SSLKYIGSGAAPLGKDLMEECGRNIPNVLLmQGYGMTETC-- 346
Cdd:PRK05852 257 HTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRkpAALRFIRSCSAPLTAETAQALQTEFAAPVV-CAFGMTEAThq 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 347 -------GIVSVEDPRLgkrNSGSAGMlAPGVEAQIVSVEtGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIdKKSW 419
Cdd:PRK05852 336 vtttqieGIGQTENPVV---STGLVGR-STGAQIRIVGSD-GLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANF-TDGW 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 420 VHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQD 499
Cdd:PRK05852 410 LRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEE 489
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15234634 500 IQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRRELVQQ 539
Cdd:PRK05852 490 LVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQ 529
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
190-533 |
4.13e-45 |
|
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: 162.04 E-value: 4.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 190 SDTAALLYSSGTTGTSKGVELTHGNFIAAsLMVTMDQDLMGEYHGVFLCFLPMFHVFGLAVITYSQLQRGNALVSMARFE 269
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAV-PDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 270 LELVLKNIEKFRVTHLWVVPPvflALSKQSIVKKFDLS---SLKYIGSGAA-PLGKDLmeecgRNI---PNVLLMQGYGM 342
Cdd:cd17635 80 YKSLFKILTTNAVTTTCLVPT---LLSKLVSELKSANAtvpSLRLIGYGGSrAIAADV-----RFIeatGLTNTAQVYGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 343 TETCGIVSVEDPRlGKRNSGSAGMLAPGVEAQIVSVEtGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIdKKSWVHT 422
Cdd:cd17635 152 SETGTALCLPTDD-DSIEINAVGRPYPGVDVYLAATD-GIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 423 GDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSP---NSSITEQD 499
Cdd:cd17635 229 GDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAeldENAIRALK 308
|
330 340 350
....*....|....*....|....*....|....
gi 15234634 500 IQkfIAKQVAPYKRLRRVSFISLVPKSAAGKILR 533
Cdd:cd17635 309 HT--IRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
35-536 |
6.84e-45 |
|
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: 167.35 E-value: 6.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 35 RNSSSYPSKLAIA----DSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTAN 110
Cdd:cd05966 61 RHLKERGDKVAIIwegdEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 111 PLYTVNEVSKQIKDSNPKIIISVNQLFDKIKGFDL-PVVllgsKDTVEIPPG---------SNSKI-------LSFDNVM 173
Cdd:cd05966 141 AGFSAESLADRINDAQCKLVITADGGYRGGKVIPLkEIV----DEALEKCPSvekvlvvkrTGGEVpmtegrdLWWHDLM 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 174 ELSEPvsEYPFVEIKQSDTAALLYSSGTTGTSKGVELTHGNFI---AASLMVTMDqdlmgeYH--GVFLCFLPMFHVFGL 248
Cdd:cd05966 217 AKQSP--ECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLlyaATTFKYVFD------YHpdDIYWCTADIGWITGH 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 249 AVITYSQLQRGNALV---------SMARFelelvLKNIEKFRVTHLWVVPPVFLALSKQ--SIVKKFDLSSLKYIGSGAA 317
Cdd:cd05966 289 SYIVYGPLANGATTVmfegtptypDPGRY-----WDIVEKHKVTIFYTAPTAIRALMKFgdEWVKKHDLSSLRVLGSVGE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 318 PLGKD----LMEECGRNipNVLLMQGYGMTETCGIVSVEDPRLGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIW 393
Cdd:cd05966 364 PINPEawmwYYEVIGKE--RCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPFFGIEPAILD-EEGNEVEGEVEGYLV 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 394 VRG--PNMMKGYLNNPQATKETIDKKSWVH--TGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDA 469
Cdd:cd05966 441 IKRpwPGMARTIYGDHERYEDTYFSKFPGYyfTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEA 520
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 470 VVIPFPDEEAGEVPIAFVVRSPNSSIT---EQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:cd05966 521 AVVGRPHDIKGEAIYAFVTLKDGEEPSdelRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRIL 590
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
45-536 |
1.76e-44 |
|
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: 169.27 E-value: 1.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 45 AIADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTtanPL---YTVNEVSKQ 121
Cdd:COG1020 492 AVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYV---PLdpaYPAERLAYM 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 122 IKDSNPKIIISVNQLFDKIKGFDLPVVLLgskDTVEIPPGSnskilsfdnvmelsepvSEYPFVEIKQSDTAALLYSSGT 201
Cdd:COG1020 569 LEDAGARLVLTQSALAARLPELGVPVLAL---DALALAAEP-----------------ATNPPVPVTPDDLAYVIYTSGS 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 202 TGTSKGVELTHGNfiAASLMVTMDQDLMGEYHGVFLCFLPMfhVFGLAVI-TYSQLQRGNALV---SMARFELELVLKNI 277
Cdd:COG1020 629 TGRPKGVMVEHRA--LVNLLAWMQRRYGLGPGDRVLQFASL--SFDASVWeIFGALLSGATLVlapPEARRDPAALAELL 704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 278 EKFRVTHLWVVPPVFLALSKQSIvkkFDLSSLKYIGSGAAPLGKDLMEECGRNIPNVLLMQGYGMTETCGIVSVEDPRLG 357
Cdd:COG1020 705 ARHRVTVLNLTPSLLRALLDAAP---EALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPP 781
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 358 KRNSGSA--GMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKE-------TIDKKSWVHTGDLGYF 428
Cdd:COG1020 782 DADGGSVpiGRPIANTRVYVLD-AHLQPVPVGVPGELYIGGAGLARGYLNRPELTAErfvadpfGFPGARLYRTGDLARW 860
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 429 NEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQKFIAKQV 508
Cdd:COG1020 861 LPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLL 940
|
490 500
....*....|....*....|....*...
gi 15234634 509 APYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:COG1020 941 PPYMVPAAVVLLLPLPLTGNGKLDRLAL 968
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
21-536 |
1.32e-42 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 160.40 E-value: 1.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 21 LPKDPN--TSLVS--FLFRNSSSYPSKLAIADSDTgdSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCF 96
Cdd:PLN02479 10 LPKNAAnyTALTPlwFLERAAVVHPTRKSVVHGSV--RYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 97 LAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIIIsVNQLF------------DKIKG-FDLPVVLLGSKDTVEipPGSN 163
Cdd:PLN02479 88 FGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVM-VDQEFftlaeealkilaEKKKSsFKPPLLIVIGDPTCD--PKSL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 164 SKILS-----FDNVMELSEPvsEYPFVEIKQS-DTAALLYSSGTTGTSKGVELTH-GNFIAA---SLMVTMDQDlmgeyh 233
Cdd:PLN02479 165 QYALGkgaieYEKFLETGDP--EFAWKPPADEwQSIALGYTSGTTASPKGVVLHHrGAYLMAlsnALIWGMNEG------ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 234 GVFLCFLPMFHVFGLAvITYSQLQRGNALVSMARFELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKF-DLSSLKYI 312
Cdd:PLN02479 237 AVYLWTLPMFHCNGWC-FTWTLAALCGTNICLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETIlPLPRVVHV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 313 -GSGAAPLGKDL--MEECGRNIPNVllmqgYGMTETCGIVSV-------------EDPRLGKRNsgsaGMLAPGVEA-QI 375
Cdd:PLN02479 316 mTAGAAPPPSVLfaMSEKGFRVTHT-----YGLSETYGPSTVcawkpewdslppeEQARLNARQ----GVRYIGLEGlDV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 376 VSVETGKSQPPNQQ--GEIWVRGPNMMKGYLNNPQATKETIdKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAP 453
Cdd:PLN02479 387 VDTKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 454 AELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFV-----VRSPNSSITEQDIQKFIAKQVAPYKRLRRVSFISLvPKSAA 528
Cdd:PLN02479 466 LEVENVVYTHPAVLEASVVARPDERWGESPCAFVtlkpgVDKSDEAALAEDIMKFCRERLPAYWVPKSVVFGPL-PKTAT 544
|
....*...
gi 15234634 529 GKILRREL 536
Cdd:PLN02479 545 GKIQKHVL 552
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
55-530 |
1.56e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 159.67 E-value: 1.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 55 LTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIIISVN 134
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVYER 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 135 QLFDKIKGF--DLP----VVLLGSKDTVEIPPGSnskiLSFDNVMELSEPvsEYPFVEiKQSDTAALLYSSGTTGTSKGV 208
Cdd:PRK07798 109 EFAPRVAEVlpRLPklrtLVVVEDGSGNDLLPGA----VDYEDALAAGSP--ERDFGE-RSPDDLYLLYTGGTTGMPKGV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 209 ELTHGNfIAASLMVTMD----QDLMGEYH----------GVFLCFLPMFHVFGLAViTYSQLQRGNALV--SMARFELEL 272
Cdd:PRK07798 182 MWRQED-IFRVLLGGRDfatgEPIEDEEElakraaagpgMRRFPAPPLMHGAGQWA-AFAALFSGQTVVllPDVRFDADE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 273 VLKNIEKFRVTHLWVVPPVFL-----ALSKQsivKKFDLSSLKYIGSGAAPLGKDLMEECGRNIPNVLLMQGYGMTET-- 345
Cdd:PRK07798 260 VWRTIEREKVNVITIVGDAMArplldALEAR---GPYDLSSLFAIASGGALFSPSVKEALLELLPNVVLTDSIGSSETgf 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 346 CGIVSVEDprlGKRNSGSAgMLAPGVEAQIVSVETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKET---IDKKSWVHT 422
Cdd:PRK07798 337 GGSGTVAK---GAVHTGGP-RFTIGPRTVVLDEDGNPVEPGSGEIGWIARRGHIPLGYYKDPEKTAETfptIDGVRYAIP 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 423 GDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQK 502
Cdd:PRK07798 413 GDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLAELRA 492
|
490 500
....*....|....*....|....*...
gi 15234634 503 FIAKQVAPYKRLRRVSFISLVPKSAAGK 530
Cdd:PRK07798 493 HCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
41-536 |
6.11e-42 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 157.48 E-value: 6.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 41 PSKLAIADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSK 120
Cdd:PRK13390 11 PDRPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 121 QIKDSNPKIIISVNQLfdkikgfDLPVVLLGSKDTVEIPPGSN-SKILSFDNVMELSEPvseyPFVEikQSDTAALLYSS 199
Cdd:PRK13390 91 IVGDSGARVLVASAAL-------DGLAAKVGADLPLRLSFGGEiDGFGSFEAALAGAGP----RLTE--QPCGAVMLYSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 200 GTTGTSKGV--ELTHGNF---------IAASLMVTMDQDLMGE----YHGVFLCFLPMFHVFGLAVitysqlqrgnalVS 264
Cdd:PRK13390 158 GTTGFPKGIqpDLPGRDVdapgdpivaIARAFYDISESDIYYSsapiYHAAPLRWCSMVHALGGTV------------VL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 265 MARFELELVLKNIEKFRVTHLWVVPPVFLALSK--QSIVKKFDLSSLKYIGSGAAPLGKDLmEECGRNIPNVLLMQGYGM 342
Cdd:PRK13390 226 AKRFDAQATLGHVERYRITVTQMVPTMFVRLLKldADVRTRYDVSSLRAVIHAAAPCPVDV-KHAMIDWLGPIVYEYYSS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 343 TETCGIVSVEDPRLgKRNSGSAGMLAPGvEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKS--WV 420
Cdd:PRK13390 305 TEAHGMTFIDSPDW-LAHPGSVGRSVLG-DLHICD-DDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 421 HTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDI 500
Cdd:PRK13390 382 TVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELA 461
|
490 500 510
....*....|....*....|....*....|....*....
gi 15234634 501 QKFI---AKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:PRK13390 462 RELIdytRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
54-534 |
7.78e-42 |
|
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: 158.81 E-value: 7.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 54 SLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIIISV 133
Cdd:cd05968 91 TLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 134 NQLFDKIKGFDLP----------------VVLLGSKDTVeipPGSNSKILSFDNVMELSEPVSEypfvEIKQSDTAALLY 197
Cdd:cd05968 171 DGFTRRGREVNLKeeadkacaqcptvekvVVVRHLGNDF---TPAKGRDLSYDEEKETAGDGAE----RTESEDPLMIIY 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 198 SSGTTGTSKGVELTHGNF---IAASLMVTMD---QDL------MGEYHGVFLCFLPMfhVFGLAVITYSQLQRGNALVSM 265
Cdd:cd05968 244 TSGTTGKPKGTVHVHAGFplkAAQDMYFQFDlkpGDLltwftdLGWMMGPWLIFGGL--ILGATMVLYDGAPDHPKADRL 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 266 ARFelelvlknIEKFRVTHLWVVPPVFLALS--KQSIVKKFDLSSLKYIGSGAAPLGKD----LMEECGrnIPNVLLMQG 339
Cdd:cd05968 322 WRM--------VEDHEITHLGLSPTLIRALKprGDAPVNAHDLSSLRVLGSTGEPWNPEpwnwLFETVG--KGRNPIINY 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 340 YGMTETCG-IVSVEDPRLGKRNSGSAGMlaPGVEAQIVSvETGKSQPPnQQGEIWVRGP--NMMKGYLNNPQATKETIDK 416
Cdd:cd05968 392 SGGTEISGgILGNVLIKPIKPSSFNGPV--PGMKADVLD-ESGKPARP-EVGELVLLAPwpGMTRGFWRDEDRYLETYWS 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 417 K---SWVHtGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPN- 492
Cdd:cd05968 468 RfdnVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGv 546
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 15234634 493 --SSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRR 534
Cdd:cd05968 547 tpTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRR 590
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
55-472 |
5.82e-41 |
|
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: 154.55 E-value: 5.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 55 LTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGV----FTTANPlYTVNEVskqIKDSNPKII 130
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHIsvplYPTLNP-DTIRYV---LEHSESKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 131 IsVNQLFDKIkgfDLPVVLLGSKDTVEIPPGSNSKIL-SFDNVMELSEPVSEYPFVEIKQsdTAALLYSSGTTGTSKGVE 209
Cdd:cd05932 83 F-VGKLDDWK---AMAPGVPEGLISISLPPPSAANCQyQWDDLIAQHPPLEERPTRFPEQ--LATLIYTSGTTGQPKGVM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 210 LTHGNF-IAASLMV----TMDQDLMgeyhgvfLCFLPMFHVFGLAVITYSQLqRGNALVSMARfELELVLKNIEK----- 279
Cdd:cd05932 157 LTFGSFaWAAQAGIehigTEENDRM-------LSYLPLAHVTERVFVEGGSL-YGGVLVAFAE-SLDTFVEDVQRarptl 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 280 -FRVTHLWV---------VP----------PVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLME---ECGRNIpnvll 336
Cdd:cd05932 228 fFSVPRLWTkfqqgvqdkIPqqklnlllkiPVVNSLVKRKVLKGLGLDQCRLAGCGSAPVPPALLEwyrSLGLNI----- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 337 MQGYGMTETCGIVSVEDPrlGKRNSGSAGMLAPGVEAQIvsvetgksqppNQQGEIWVRGPNMMKGYLNNPQATKETIDK 416
Cdd:cd05932 303 LEAYGMTENFAYSHLNYP--GRDKIGTVGNAGPGVEVRI-----------SEDGEILVRSPALMMGYYKDPEATAEAFTA 369
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 15234634 417 KSWVHTGDLGYFNEDGNLYVVDRIKELIKY-KGFQVAPAELEGLLVSHPDILDAVVI 472
Cdd:cd05932 370 DGFLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVI 426
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
35-544 |
1.26e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 153.40 E-value: 1.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 35 RNSSSYPSKLAIADSDtgDSLTFSQLKSAVARLAHGFHRLGiRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYT 114
Cdd:PRK07638 9 KHASLQPNKIAIKEND--RVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 115 VNEVSKQIKDSNPKIIISVNQLFDKIKGFDLPVVLLgskdtveippgsnskilsfDNVMEL-SEPVSEYPFVEIKQSDTA 193
Cdd:PRK07638 86 QDELKERLAISNADMIVTERYKLNDLPDEEGRVIEI-------------------DEWKRMiEKYLPTYAPIENVQNAPF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 194 ALLYSSGTTGTSKGVELTHGNF--------------------IAASLMvtmdqdlmgeyHGVFLcflpmfhvFGlAVity 253
Cdd:PRK07638 147 YMGFTSGSTGKPKAFLRAQQSWlhsfdcnvhdfhmkredsvlIAGTLV-----------HSLFL--------YG-AI--- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 254 SQLQRGNALVSMARFELELVLKNIEKFRVTHLWVVPPVFLALSKqsiVKKFDLSSLKYIGSGAApLGKDLMEECGRNIPN 333
Cdd:PRK07638 204 STLYVGQTVHLMRKFIPNQVLDKLETENISVMYTVPTMLESLYK---ENRVIENKMKIISSGAK-WEAEAKEKIKNIFPY 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 334 VLLMQGYGMTETcGIVSVEDPRLGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKEt 413
Cdd:PRK07638 280 AKLYEFYGASEL-SFVTALVDEESERRPNSVGRPFHNVQVRICN-EAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARE- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 414 IDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNS 493
Cdd:PRK07638 357 LNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSATK 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 15234634 494 siteQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRRELVQQVRSKM 544
Cdd:PRK07638 437 ----QQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQE 483
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
41-536 |
2.02e-40 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 152.74 E-value: 2.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 41 PSKLAIADSDTgdSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSK 120
Cdd:cd12117 11 PDAVAVVYGDR--SLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 121 QIKDSNPKIIISVNQLFDKIKGFDLPVVLLGSKDTVEIPPgsnskilsfdnvmeLSEPVSEypfveikqSDTAALLYSSG 200
Cdd:cd12117 89 MLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGN--------------PAVPVSP--------DDLAYVMYTSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 201 TTGTSKGVELTHgnfiAASLMVTMDQDLMGEY-HGVFLCFLP------MFHVFGlavitysqlqrgnALVSMARFEL--E 271
Cdd:cd12117 147 STGRPKGVAVTH----RGVVRLVKNTNYVTLGpDDRVLQTSPlafdasTFEIWG-------------ALLNGARLVLapK 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 272 LVLKNIEKFR-------VTHLWVVPPVFLALSKQsivkkfD---LSSLKYIGSGAAPLGKDLMEECGRNIPNVLLMQGYG 341
Cdd:cd12117 210 GTLLDPDALGaliaeegVTVLWLTAALFNQLADE------DpecFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 342 MTE-----TCGIVSVEDPRLGKRNSGSAgmlAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKET--- 413
Cdd:cd12117 284 PTEnttftTSHVVTELDEVAGSIPIGRP---IANTRVYVLD-EDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERfva 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 414 ---IDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVrs 490
Cdd:cd12117 360 dpfGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVV-- 437
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 15234634 491 PNSSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:cd12117 438 AEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
195-530 |
2.15e-40 |
|
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: 149.84 E-value: 2.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 195 LLYSSGTTGTSKGVELTHGNFIAASLMV--------TMDQDLMGEYHG----VFLCFLPMFHVFGLAVITYSQLQRGNAL 262
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIFRMLMGGadfgtgefTPSEDAHKAAAAaagtVMFPAPPLMHGTGSWTAFGGLLGGQTVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 263 VSMARFELELVLKNIEKFRVTHLWVVPPVFL-----ALSKQsivKKFDLSSLKYIGSGAAPLGKDLMEECGRNIPNVLLM 337
Cdd:cd05924 88 LPDDRFDPEEVWRTIEKHKVTSMTIVGDAMArplidALRDA---GPYDLSSLFAISSGGALLSPEVKQGLLELVPNITLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 338 QGYGMTETcGIVSVEDPRLGKRNSGSAGMLAPGVeaqIVSVETGKSQPPNQQGEIWV--RGpNMMKGYLNNPQATKET-- 413
Cdd:cd05924 165 DAFGSSET-GFTGSGHSAGSGPETGPFTRANPDT---VVLDDDGRVVPPGSGGVGWIarRG-HIPLGYYGDEAKTAETfp 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 414 -IDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPN 492
Cdd:cd05924 240 eVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREG 319
|
330 340 350
....*....|....*....|....*....|....*...
gi 15234634 493 SSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGK 530
Cdd:cd05924 320 AGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
56-541 |
2.44e-40 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 153.37 E-value: 2.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 56 TFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIIIS--- 132
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITdlt 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 133 ----VNQLFDKIKGFDLPVVLlgsKDTVEIPPGSNSKILSFDNVmeLSEPVSEYPFVEIKQSDTAALLYSSGTTGTSKGV 208
Cdd:PRK06018 121 fvpiLEKIADKLPSVERYVVL---TDAAHMPQTTLKNAVAYEEW--IAEADGDFAWKTFDENTAAGMCYTSGTTGDPKGV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 209 ELTH-GNFIAAslMVTMDQDLMG-EYHGVFLCFLPMFHV--FGLAvitYSQLQRGNALVsM--ARFELELVLKNIEKFRV 282
Cdd:PRK06018 196 LYSHrSNVLHA--LMANNGDALGtSAADTMLPVVPLFHAnsWGIA---FSAPSMGTKLV-MpgAKLDGASVYELLDTEKV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 283 THLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLM---EECGrnipnVLLMQGYGMTETC--GIVSVEDPRLG 357
Cdd:PRK06018 270 TFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIkafEDMG-----VEVRHAWGMTEMSplGTLAALKPPFS 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 358 KRnSGSAGM-------LAP-GVEAQIVSvETGKSQPPNQQ--GEIWVRGPNMMKGYLnnpQATKETIDKKSWVHTGDLGY 427
Cdd:PRK06018 345 KL-PGDARLdvlqkqgYPPfGVEMKITD-DAGKELPWDGKtfGRLKVRGPAVAAAYY---RVDGEILDDDGFFDTGDVAT 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 428 FNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQKFIAKQ 507
Cdd:PRK06018 420 IDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEILKYMDGK 499
|
490 500 510
....*....|....*....|....*....|....
gi 15234634 508 VAPYKRLRRVSFISLVPKSAAGKILRRELVQQVR 541
Cdd:PRK06018 500 IAKWWMPDDVAFVDAIPHTATGKILKTALREQFK 533
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
55-457 |
7.39e-40 |
|
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: 152.90 E-value: 7.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 55 LTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSyqfPLCFLAvtAIGGVFT--TANPLYTVN--EVSKQIKDSNPKII 130
Cdd:cd05933 9 LTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNS---PEWFIA--AVGAIFAggIAVGIYTTNspEACQYVAETSEANI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 131 ISVN---QLfDKIKGFD--LP----VVLLGskdtvEIPPGSNSKILSFDNVMELSEPVSEYPFVEI----KQSDTAALLY 197
Cdd:cd05933 84 LVVEnqkQL-QKILQIQdkLPhlkaIIQYK-----EPLKEKEPNLYSWDEFMELGRSIPDEQLDAIissqKPNQCCTLIY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 198 SSGTTGTSKGVELTHGN--FIAASLMVTMDQDLMGEYHGVFLCFLPMFHV------------FGlAVITYSQLQRGN-AL 262
Cdd:cd05933 158 TSGTTGMPKGVMLSHDNitWTAKAASQHMDLRPATVGQESVVSYLPLSHIaaqildiwlpikVG-GQVYFAQPDALKgTL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 263 VSMAR-------------FE--LELVLKNIEKF----RVTHLWVV----------------PPVFLALSKQSIVKK---- 303
Cdd:cd05933 237 VKTLRevrptafmgvprvWEkiQEKMKAVGAKSgtlkRKIASWAKgvgletnlklmggespSPLFYRLAKKLVFKKvrka 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 304 FDLSSLKYIGSGAAPLGKDLMEE-CGRNIPnvlLMQGYGMTETCGIVSVEDPrlGKRNSGSAGMLAPGVEAQIVSvetgk 382
Cdd:cd05933 317 LGLDRCQKFFTGAAPISRETLEFfLSLNIP---IMELYGMSETSGPHTISNP--QAYRLLSCGKALPGCKTKIHN----- 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15234634 383 sQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQ-VAPAELE 457
Cdd:cd05933 387 -PDADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGEnVPPVPIE 461
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
45-536 |
2.94e-39 |
|
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: 149.42 E-value: 2.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 45 AIADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKD 124
Cdd:cd17651 11 APALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLAD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 125 SNPKIIISVNQLFDKIKGFDLPVVLLGSKDTVEIPPGSnskilsfdnvmelsepvseyPFVEIKQSDTAALLYSSGTTGT 204
Cdd:cd17651 91 AGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADAE--------------------PDPALDADDLAYVIYTSGSTGR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 205 SKGVELTHG---NFIAAslmvtmdqdlmgeyHGVFLCFLPMFHVFGLAVITY--------SQLQRGNALV---SMARFEL 270
Cdd:cd17651 151 PKGVVMPHRslaNLVAW--------------QARASSLGPGARTLQFAGLGFdvsvqeifSTLCAGATLVlppEEVRTDP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 271 ELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSG--AAPLGKDLMEECGRnIPNVLLMQGYGMTE---- 344
Cdd:cd17651 217 PALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGgeQLVLTEDLREFCAG-LPGLRLHNHYGPTEthvv 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 345 TCGIVSVEDPRLGKRNSgsAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKSWV---- 420
Cdd:cd17651 296 TALSLPGDPAAWPAPPP--IGRPIDNTRVYVLD-AALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgar 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 421 --HTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQ 498
Cdd:cd17651 373 myRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAA 452
|
490 500 510
....*....|....*....|....*....|....*...
gi 15234634 499 DIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:cd17651 453 ELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
45-543 |
1.15e-38 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 148.60 E-value: 1.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 45 AIADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVftTANPLYT-----VNEVS 119
Cdd:PRK10946 39 AIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNALFShqrseLNAYA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 120 KQIKdsnPKIIISVNQ--LF---DKIKGF-----DLPVVLLGSKDTveippgsnskILSFDNVMElsEPVSEYPFVEIKQ 189
Cdd:PRK10946 117 SQIE---PALLIADRQhaLFsddDFLNTLvaehsSLRVVLLLNDDG----------EHSLDDAIN--HPAEDFTATPSPA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 190 SDTAALLYSSGTTGTSKGVELTHGNF---IAASLMVT-MDQdlmgeyHGVFLCFLPMFHVF------GLAVitysqLQRG 259
Cdd:PRK10946 182 DEVAFFQLSGGSTGTPKLIPRTHNDYyysVRRSVEICgFTP------QTRYLCALPAAHNYpmsspgALGV-----FLAG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 260 NALVsMAR-------FELelvlknIEKFRVTHLWVVPP-VFLALSK-QSIVKKFDLSSLKYIGSGAAPLGkdlmEECGRN 330
Cdd:PRK10946 251 GTVV-LAPdpsatlcFPL------IEKHQVNVTALVPPaVSLWLQAiAEGGSRAQLASLKLLQVGGARLS----ETLARR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 331 IPNVL---LMQGYGMTEtcGIVS---VEDPRlgKRNSGSAGM-LAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGY 403
Cdd:PRK10946 320 IPAELgcqLQQVFGMAE--GLVNytrLDDSD--ERIFTTQGRpMSPDDEVWVAD-ADGNPLPQGEVGRLMTRGPYTFRGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 404 LNNPQATKETIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVP 483
Cdd:PRK10946 395 YKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKS 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15234634 484 IAF-VVRSPNSSITeqdIQKFIAKQ-VAPYKRLRRVSFISLVPKSAAGKILRRELVQQVRSK 543
Cdd:PRK10946 475 CAFlVVKEPLKAVQ---LRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLASR 533
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
55-536 |
4.17e-38 |
|
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: 145.40 E-value: 4.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 55 LTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVskqikdsnpkiiisvn 134
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDL---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 135 qlfdkikgfdlpvvllgsKDTVEIPPGSNSKIlsfdnvmelsepvseypfVEIKQSDTAALLY-SSGTTGTSKGVELTHG 213
Cdd:cd05974 65 ------------------RDRVDRGGAVYAAV------------------DENTHADDPMLLYfTSGTTSKPKLVEHTHR 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 214 NFIAASLMVTMDQDLM-GEYH----------GVFLCFLPMFHVfGLAVITYSQlqrgnalvsmARFELELVLKNIEKFRV 282
Cdd:cd05974 109 SYPVGHLSTMYWIGLKpGDVHwnisspgwakHAWSCFFAPWNA-GATVFLFNY----------ARFDAKRVLAALVRYGV 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 283 THLWVVPPVFLALSKQSIVKkFDLSSLKYIGSGAaPLGKDLMEECgRNIPNVLLMQGYGMTETCGIVSVEDPRLGKrnSG 362
Cdd:cd05974 178 TTLCAPPTVWRMLIQQDLAS-FDVKLREVVGAGE-PLNPEVIEQV-RRAWGLTIRDGYGQTETTALVGNSPGQPVK--AG 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 363 SAGMLAPGVEAQIVSVETGksqpPNQQGEIWV-----RGPNMMKGYLNNPQATKETIdKKSWVHTGDLGYFNEDGNLYVV 437
Cdd:cd05974 253 SMGRPLPGYRVALLDPDGA----PATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYV 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 438 DRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVV------RSPNssiTEQDIQKFIAKQVAPY 511
Cdd:cd05974 328 GRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVlragyePSPE---TALEIFRFSRERLAPY 404
|
490 500
....*....|....*....|....*
gi 15234634 512 KRLRRVSFISLvPKSAAGKILRREL 536
Cdd:cd05974 405 KRIRRLEFAEL-PKTISGKIRRVEL 428
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
197-533 |
1.09e-37 |
|
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: 141.39 E-value: 1.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 197 YSSGTTGTSKGVELTHGNFIAAslMVTMDQDLMGEYHGVFLCFLPMFHVFGLAVITYSqLQRGNALVSMARFELELVLKN 276
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIES--FVCNEDLFNISGEDAILAPGPLSHSLFLYGAISA-LYLGGTFIGQRKFNPKSWIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 277 IEKFRVTHLWVVPPVFLALSKQsivkKFDLSSLKYIGSGAAPLGKDLMEECGRNIPNVLLMQGYGMTETCGIVSVEDPRL 356
Cdd:cd17633 84 INQYNATVIYLVPTMLQALART----LEPESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYNFNQES 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 357 GKRNSgsAGMLAPGVEAQIVSVETGKsqppnqQGEIWVRGPNMMKGYLnnpqaTKETIDKKSWVHTGDLGYFNEDGNLYV 436
Cdd:cd17633 160 RPPNS--VGRPFPNVEIEIRNADGGE------IGKIFVKSEMVFSGYV-----RGGFSNPDGWMSVGDIGYVDEEGYLYL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 437 VDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVrspNSSITEQDIQKFIAKQVAPYKRLRR 516
Cdd:cd17633 227 VGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS---GDKLTYKQLKRFLKQKLSRYEIPKK 303
|
330
....*....|....*..
gi 15234634 517 VSFISLVPKSAAGKILR 533
Cdd:cd17633 304 IIFVDSLPYTSSGKIAR 320
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
2-457 |
1.18e-37 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 147.17 E-value: 1.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 2 EKSGYGRDGIYRSLR-PTLVLPKDPNTSLVSFLFRNSSSYPSKLA--------IADSDT-GDS--LTFSQLKSAVARLAH 69
Cdd:PLN02736 14 EKLQTGKWNVYRSARsPLKLVSRFPDHPEIGTLHDNFVYAVETFRdykylgtrIRVDGTvGEYkwMTYGEAGTARTAIGS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 70 GFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVfttANPLY----------TVNEVSKQIKDSNPKIIISVNQLFDK 139
Cdd:PLN02736 94 GLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYV---SVPLYdtlgpdavkfIVNHAEVAAIFCVPQTLNTLLSCLSE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 140 IKGFDLPVVLLGSKDTV-EIPPGSNSKILSFDNVMELSEpVSEYPFVEIKQSDTAALLYSSGTTGTSKGVELTHGNFIAA 218
Cdd:PLN02736 171 IPSVRLIVVVGGADEPLpSLPSGTGVEIVTYSKLLAQGR-SSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIAN 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 219 SLMVTMDQDLmgeYHG-VFLCFLPMFHV-----------FGLAVITYsqlqRGNALVSMarfelelvlKNIEKFRVTHLW 286
Cdd:PLN02736 250 VAGSSLSTKF---YPSdVHISYLPLAHIyervnqivmlhYGVAVGFY----QGDNLKLM---------DDLAALRPTIFC 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 287 VVPPVF-------------------------LALSKQSIVKKFDLSSL-----------------KYIGSGAAPLGKDLM 324
Cdd:PLN02736 314 SVPRLYnriydgitnavkesgglkerlfnaaYNAKKQALENGKNPSPMwdrlvfnkikaklggrvRFMSSGASPLSPDVM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 325 EECgRNIPNVLLMQGYGMTETCGIVSVEDPrlGKRNSGSAGMLAPGVEAQIVSVE----TGKSQP-PnqQGEIWVRGPNM 399
Cdd:PLN02736 394 EFL-RICFGGRVLEGYGMTETSCVISGMDE--GDNLSGHVGSPNPACEVKLVDVPemnyTSEDQPyP--RGEICVRGPII 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15234634 400 MKGYLNNPQATKETIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKY-KGFQVAPAELE 457
Cdd:PLN02736 469 FKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIE 527
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
48-541 |
1.30e-37 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 146.08 E-value: 1.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 48 DSDTGDSLTFSQLKSAVARLAHGFH-RLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSN 126
Cdd:PRK05620 32 GGAEQEQTTFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 127 PKIIISVNQLFDKIKGF--DLP----VVLLG--SKDTVEIPPGSNSKILSFDNvmELSEPVSEYPFVEIKQSDTAALLYS 198
Cdd:PRK05620 112 DEVIVADPRLAEQLGEIlkECPcvraVVFIGpsDADSAAAHMPEGIKVYSYEA--LLDGRSTVYDWPELDETTAAAICYS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 199 SGTTGTSKGVELTHGNFIAASLMVtMDQDLMGEYHGV-FLCFLPMFHVFGLAViTYSQLQRGNALVSMAR-FELELVLKN 276
Cdd:PRK05620 190 TGTTGAPKGVVYSHRSLYLQSLSL-RTTDSLAVTHGEsFLCCVPIYHVLSWGV-PLAAFMSGTPLVFPGPdLSAPTLAKI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 277 IEKF--RVTHlwVVPPVFLALSKQSIVKKFDLSSLKYI---GSGAAPLGKDLMEE-CGRNIPNVllmqgYGMTETCGIVS 350
Cdd:PRK05620 268 IATAmpRVAH--GVPTLWIQLMVHYLKNPPERMSLQEIyvgGSAVPPILIKAWEErYGVDVVHV-----WGMTETSPVGT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 351 VEDPRLGKrnSGSA--------GMLAPGVEAQIVSVETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATK---------ET 413
Cdd:PRK05620 341 VARPPSGV--SGEArwayrvsqGRFPASLEYRIVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPTEEGggaastfrgED 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 414 IDKKS-------WVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAF 486
Cdd:PRK05620 419 VEDANdrftadgWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAV 498
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15234634 487 VVRSPN---SSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRRELVQQVR 541
Cdd:PRK05620 499 TVLAPGiepTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHLA 556
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
28-536 |
1.36e-37 |
|
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: 145.27 E-value: 1.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 28 SLVSFLFRNSSSYPSKlaiadsDTGD-SLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVF 106
Cdd:cd05915 3 RAAALFGRKEVVSRLH------TGEVhRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 107 TTANPLYTVNEVSKQIKDSNPKIIIsVNQLFDKIKGFDLPVVllgskDTVEIPPGSNSKILSFDNVMELSEPvSEYPFVE 186
Cdd:cd05915 77 HTANPRLSPKEIAYILNHAEDKVLL-FDPNLLPLVEAIRGEL-----KTVQHFVVMDEKAPEGYLAYEEALG-EEADPVR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 187 IKQSDTAALLYSSGTTGTSKGVELTH-GNFIAASLMVTMDQdLMGEYHGVFLCFLPMFHVFGLAVItYSQLQRGNALVSM 265
Cdd:cd05915 150 VPERAACGMAYTTGTTGLPKGVVYSHrALVLHSLAASLVDG-TALSEKDVVLPVVPMFHVNAWCLP-YAATLVGAKQVLP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 266 ARFEL-ELVLKNIEKFRVTHLWVVPPVF--LALSKQSIVKKFDLSsLKYIGSGAAPlgKDLMEECgRNIPNVLLMQGYGM 342
Cdd:cd05915 228 GPRLDpASLVELFDGEGVTFTAGVPTVWlaLADYLESTGHRLKTL-RRLVVGGSAA--PRSLIAR-FERMGVEVRQGYGL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 343 TETCGIVSV-------------EDPRLGKRNSgsagmLAPGVEAQIVSVETGKSQPPNQQG--EIWVRGPNMMKGYLNNP 407
Cdd:cd05915 304 TETSPVVVQnfvkshleslseeEKLTLKAKTG-----LPIPLVRLRVADEEGRPVPKDGKAlgEVQLKGPWITGGYYGNE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 408 QATKETIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFv 487
Cdd:cd05915 379 EATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAV- 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15234634 488 VRSPNSSITEQDIQKFIAKQVAPYKRL-RRVSFISLVPKSAAGKILRREL 536
Cdd:cd05915 458 VVPRGEKPTPEELNEHLLKAGFAKWQLpDAYVFAEEIPRTSAGKFLKRAL 507
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
27-536 |
3.89e-37 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 143.98 E-value: 3.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 27 TSLVSFLFRNSSSYPSKLAIADSDtgDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVF 106
Cdd:PRK13383 35 TNPYTLLAVTAARWPGRTAIIDDD--GALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 107 TTANPLYTVNEVSKQIKDSNPKIIISVNQLFDKIKGFDLPVVLLGSKDTVEIPPGSNSKILSFDNVmelsepvseypfve 186
Cdd:PRK13383 113 VPISTEFRSDALAAALRAHHISTVVADNEFAERIAGADDAVAVIDPATAGAEESGGRPAVAAPGRI-------------- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 187 ikqsdtaaLLYSSGTTGTSKGVELTHGNFIAASLMVTMDQDLMGEYHGVFLCFLPMFHVFGLAVITYSqLQRGNALVSMA 266
Cdd:PRK13383 179 --------VLLTSGTTGKPKGVPRAPQLRSAVGVWVTILDRTRLRTGSRISVAMPMFHGLGLGMLMLT-IALGGTVLTHR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 267 RFELELVLKNIEKFRVTHLWVVPPVF---LALSKQsIVKKFDLSSLKYIGSGA----APLGKDLMEECGRnipnvLLMQG 339
Cdd:PRK13383 250 HFDAEAALAQASLHRADAFTAVPVVLariLELPPR-VRARNPLPQLRVVMSSGdrldPTLGQRFMDTYGD-----ILYNG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 340 YGMTETcGIVSVEDPRLGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNpqATKETIDKKSw 419
Cdd:PRK13383 324 YGSTEV-GIGALATPADLRDAPETVGKPVAGCPVRILD-RNNRPVGPRVTGRIFVGGELAGTRYTDG--GGKAVVDGMT- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 420 vHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQD 499
Cdd:PRK13383 399 -STGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQ 477
|
490 500 510
....*....|....*....|....*....|....*..
gi 15234634 500 IQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:PRK13383 478 LRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
56-472 |
2.67e-36 |
|
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: 142.56 E-value: 2.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 56 TFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVfttANPLYT---VNEVSKQIKDSNPKIIIS 132
Cdd:cd17641 13 TWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGAL---SLGIYQdsmAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 133 VNQ-LFDKI--KGFDLPVVLlgsKDTVEIPPG----SNSKILSFDNVMEL------SEP-VSEYPFVEIKQSDTAALLYS 198
Cdd:cd17641 90 EDEeQVDKLleIADRIPSVR---YVIYCDPRGmrkyDDPRLISFEDVVALgraldrRDPgLYEREVAAGKGEDVAVLCTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 199 SGTTGTSKGVELTHGNFI---AASLMVtmDQDLMGEYhgvFLCFLPmfhvfgLAVITYSQLQRGNALVSmaRF------E 269
Cdd:cd17641 167 SGTTGKPKLAMLSHGNFLghcAAYLAA--DPLGPGDE---YVSVLP------LPWIGEQMYSVGQALVC--GFivnfpeE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 270 LELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFD-------------------------------------------- 305
Cdd:cd17641 234 PETMMEDLREIGPTFVLLPPRVWEGIAADVRARMMDatpfkrfmfelgmklglraldrgkrgrpvslwlrlaswladall 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 306 ---------LSSLKYIGSGAAPLGKD---LMEECGRNipnvlLMQGYGMTETCGIVSVEdpRLGKRNSGSAGMLAPGVEA 373
Cdd:cd17641 314 frplrdrlgFSRLRSAATGGAALGPDtfrFFHAIGVP-----LKQLYGQTELAGAYTVH--RDGDVDPDTVGVPFPGTEV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 374 QIVSVetgksqppnqqGEIWVRGPNMMKGYLNNPQATKETIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIK-YKGFQVA 452
Cdd:cd17641 387 RIDEV-----------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTtSDGTRFS 455
|
490 500
....*....|....*....|
gi 15234634 453 PAELEGLLVSHPDILDAVVI 472
Cdd:cd17641 456 PQFIENKLKFSPYIAEAVVL 475
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
45-536 |
7.73e-36 |
|
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: 139.37 E-value: 7.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 45 AIADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKD 124
Cdd:cd17643 3 AVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 125 SNPKIIisvnqlfdkikgfdlpvvllgskdtveippgsnskilsfdnvmeLSEPvseypfveikqSDTAALLYSSGTTGT 204
Cdd:cd17643 83 SGPSLL--------------------------------------------LTDP-----------DDLAYVIYTSGSTGR 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 205 SKGVELTHGNFIAaslMVTMDQDLMGEYHG-VFLcflpMFH--VFGLAVI-TYSQLQRGNALV------SMARFELELVL 274
Cdd:cd17643 108 PKGVVVSHANVLA---LFAATQRWFGFNEDdVWT----LFHsyAFDFSVWeIWGALLHGGRLVvvpyevARSPEDFARLL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 275 KnieKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECGRNIPNV--LLMQGYGMTETCGIVSVE 352
Cdd:cd17643 181 R---DEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLDrpQLVNMYGITETTVHVTFR 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 353 --DPR-LGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKE-------TIDKKSWVHT 422
Cdd:cd17643 258 plDAAdLPAAAASPIGRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRT 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 423 GDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQK 502
Cdd:cd17643 337 GDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRA 416
|
490 500 510
....*....|....*....|....*....|....
gi 15234634 503 FIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:cd17643 417 LLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
45-536 |
2.20e-35 |
|
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: 138.56 E-value: 2.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 45 AIADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKD 124
Cdd:cd17646 14 APAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLAD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 125 SNPKIIISVNQLFDKIKGfDLPVVLLGSKDTVEIPPGSnskilsfdnvmelsepvseyPFVEIKQSDTAALLYSSGTTGT 204
Cdd:cd17646 94 AGPAVVLTTADLAARLPA-GGDVALLGDEALAAPPATP--------------------PLVPPRPDNLAYVIYTSGSTGR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 205 SKGVELTHGNFiaASLMVTMdQDLMGEYHG-VFLCFLPM-FHV----FGLAVITysqlqrGNALVsMARFELE----LVL 274
Cdd:cd17646 153 PKGVMVTHAGI--VNRLLWM-QDEYPLGPGdRVLQKTPLsFDVsvweLFWPLVA------GARLV-VARPGGHrdpaYLA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 275 KNIEKFRVTHLWVVP---PVFLALSKQSivkkfDLSSLKYIGSGAAPLGKDLMEECgRNIPNVLLMQGYGMTETC-GIVS 350
Cdd:cd17646 223 ALIREHGVTTCHFVPsmlRVFLAEPAAG-----SCASLRRVFCSGEALPPELAARF-LALPGAELHNLYGPTEAAiDVTH 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 351 VEDPRLGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKSWVH------TGD 424
Cdd:cd17646 297 WPVRGPAETPSVPIGRPVPNTRLYVLD-DALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 425 LGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSP-NSSITEQDIQKF 503
Cdd:cd17646 376 LARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAgAAGPDTAALRAH 455
|
490 500 510
....*....|....*....|....*....|...
gi 15234634 504 IAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:cd17646 456 LAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
35-542 |
3.41e-35 |
|
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: 138.06 E-value: 3.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 35 RNSSSYPSKLAIADSDTgdSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYT 114
Cdd:cd05918 7 ERARSQPDAPAVCAWDG--SLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 115 VNEVSKQIKDSNPKIIISvnqlfdkikgfdlpvvllgskdtveippgsnskilsfdnvmelSEPvseypfveikqSDTAA 194
Cdd:cd05918 85 LQRLQEILQDTGAKVVLT-------------------------------------------SSP-----------SDAAY 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 195 LLYSSGTTGTSKGVELTHGNFiAASLMVtmdqdlMGEYHGV-----FLCF---------LPMFH--VFGLAVITYSQLQR 258
Cdd:cd05918 111 VIFTSGSTGKPKGVVIEHRAL-STSALA------HGRALGLtsesrVLQFasytfdvsiLEIFTtlAAGGCLCIPSEEDR 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 259 GNALvsmARFelelvlknIEKFRVTHLWVVPPVFLALSKQsivkkfDLSSLKYIGSGAAPLGKDLMEECGrniPNVLLMQ 338
Cdd:cd05918 184 LNDL---AGF--------INRLRVTWAFLTPSVARLLDPE------DVPSLRTLVLGGEALTQSDVDTWA---DRVRLIN 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 339 GYGMTETC------GIVSVEDPR-LGKRNSGSAGMLAPGVEAQIVsvetgksqPPNQQGEIWVRGPNMMKGYLNNPQATK 411
Cdd:cd05918 244 AYGPAECTiaatvsPVVPSTDPRnIGRPLGATCWVVDPDNHDRLV--------PIGAVGELLIEGPILARGYLNDPEKTA 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 412 ET-IDKKSWVH------------TGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSH-PDILDAVV--IPFP 475
Cdd:cd05918 316 AAfIEDPAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSlPGAKEVVVevVKPK 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 476 DEEAGEVPIAFVVRSPNSSITEQDIQKFIAKQVAPYKRLRRVS---------------FISL--VPKSAAGKILRRELVQ 538
Cdd:cd05918 396 DGSSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDEFRALVAELRsklrqrlpsymvpsvFLPLshLPLTASGKIDRRALRE 475
|
....
gi 15234634 539 QVRS 542
Cdd:cd05918 476 LAES 479
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
55-464 |
9.28e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 138.96 E-value: 9.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 55 LTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTT--ANP-----LYTVNEVSKQIKDSNP 127
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATvyANLgedalAYALRETECKAIVCNG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 128 KIIISVNQLFDKIKGFDLPVVLLGSkdtveIPPGSNSK---ILSFDNVMELSEP-VSEYPF-VEIKQSDTAALLYSSGTT 202
Cdd:PTZ00216 202 KNVPNLLRLMKSGGMPNTTIIYLDS-----LPASVDTEgcrLVAWTDVVAKGHSaGSHHPLnIPENNDDLALIMYTSGTT 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 203 GTSKGVELTHGNfIAASLMvTMDQ---DLMGEYHG--VFLCFLPMFHVFGLAViTYSQLQRGnALV----------SMAR 267
Cdd:PTZ00216 277 GDPKGVMHTHGS-LTAGIL-ALEDrlnDLIGPPEEdeTYCSYLPLAHIMEFGV-TNIFLARG-ALIgfgsprtltdTFAR 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 268 FELELVlknieKFRVTHLWVVPPVFLALSKQ---------SIVKK-FD---LSSLKYIGSG-----------AAP---LG 320
Cdd:PTZ00216 353 PHGDLT-----EFRPVFLIGVPRIFDTIKKAveaklppvgSLKRRvFDhayQSRLRALKEGkdtpywnekvfSAPravLG 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 321 KDLMEECGRNIP---------NVLL---MQGYGMTETCGIVSVEdpRLGKRNSGSAGMLAPGVEAQIVSVETGK-SQPPN 387
Cdd:PTZ00216 428 GRVRAMLSGGGPlsaatqefvNVVFgmvIQGWGLTETVCCGGIQ--RTGDLEPNAVGQLLKGVEMKLLDTEEYKhTDTPE 505
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15234634 388 QQGEIWVRGPNMMKGYLNNPQATKETIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIK-YKGFQVAPAELEGLLVSHP 464
Cdd:PTZ00216 506 PRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKnCLGEYIALEALEALYGQNE 583
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
55-533 |
1.15e-33 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 135.25 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 55 LTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIIISVN 134
Cdd:PTZ00237 93 LTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTN 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 135 Q--LFDKIKGF--DLP------------VVLLGSKDTVE---------IPPGSNSkiLSFDNVMELSEPVSEYPFVE--- 186
Cdd:PTZ00237 173 YgiLNDEIITFtpNLKeaielstfkpsnVITLFRNDITSesdlkkietIPTIPNT--LSWYDEIKKIKENNQSPFYEyvp 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 187 IKQSDTAALLYSSGTTGTSKGVELTHGNFIAA-----SLMVTMDQDLMGEYH----GVflcflpMFHVFglaviTYSQLQ 257
Cdd:PTZ00237 251 VESSHPLYILYTSGTTGNSKAVVRSNGPHLVGlkyywRSIIEKDIPTVVFSHssigWV------SFHGF-----LYGSLS 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 258 RGNALVS-----MARFELELVLKN-IEKFRVTHLWVVPPVFLALSK-----QSIVKKFDLSSLKYIGSGAAPLGKDLMEE 326
Cdd:PTZ00237 320 LGNTFVMfeggiIKNKHIEDDLWNtIEKHKVTHTLTLPKTIRYLIKtdpeaTIIRSKYDLSNLKEIWCGGEVIEESIPEY 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 327 CGRNIpNVLLMQGYGMTETcGIVSVEDPRLGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVR---GPNMMKGY 403
Cdd:PTZ00237 400 IENKL-KIKSSRGYGQTEI-GITYLYCYGHINIPYNATGVPSIFIKPSILS-EDGKELNVNEIGEVAFKlpmPPSFATTF 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 404 LNNPQATKETIDK-KSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEV 482
Cdd:PTZ00237 477 YKNDEKFKQLFSKfPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNV 556
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15234634 483 PIAFVVRSPNSSITEQD-------IQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILR 533
Cdd:PTZ00237 557 PIGLLVLKQDQSNQSIDlnklkneINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
55-533 |
2.77e-33 |
|
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: 131.87 E-value: 2.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 55 LTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTtanPLYTVnevskqikdSNPKIIISvn 134
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQ---PLFTA---------FGPKAIEH-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 135 qlfdKIKGFDLPVVllgskdtveippgsnskILSFDNVMELSEPvseyPFVEikqsdtaalLYSSGTTGTSKGVE----- 209
Cdd:cd05973 67 ----RLRTSGARLV-----------------VTDAANRHKLDSD----PFVM---------MFTSGTTGLPKGVPvplra 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 210 -LTHGNFIAASLMVTMDQdlmgeyhgVFLCFLPMFHVFGLAVITYSQLQRGNA-LVSMARFELELVLKNIEKFRVTHLWV 287
Cdd:cd05973 113 lAAFGAYLRDAVDLRPED--------SFWNAADPGWAYGLYYAITGPLALGHPtILLEGGFSVESTWRVIERLGVTNLAG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 288 VPPVFLALSKQSIVKKFDLS-SLKYIGSGAAPLGKDLMEECGRNIpNVLLMQGYGMTETcGIV-----SVEDPRlgkrNS 361
Cdd:cd05973 185 SPTAYRLLMAAGAEVPARPKgRLRRVSSAGEPLTPEVIRWFDAAL-GVPIHDHYGQTEL-GMVlanhhALEHPV----HA 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 362 GSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWV---RGPNM-MKGYLNNPQATketIDKKsWVHTGDLGYFNEDGNLYVV 437
Cdd:cd05973 259 GSAGRAMPGWRVAVLD-DDGDELGPGEPGRLAIdiaNSPLMwFRGYQLPDTPA---IDGG-YYLTGDTVEFDPDGSFSFI 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 438 DRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQ---DIQKFIAKQVAPYKRL 514
Cdd:cd05973 334 GRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPAladELQLHVKKRLSAHAYP 413
|
490
....*....|....*....
gi 15234634 515 RRVSFISLVPKSAAGKILR 533
Cdd:cd05973 414 RTIHFVDELPKTPSGKIQR 432
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
54-537 |
5.39e-33 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 133.15 E-value: 5.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 54 SLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIIISV 133
Cdd:PRK10524 84 TYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPVLIVSA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 134 N------------QLFDKikgfdlpvvllgSKDTVEIPPgsnSKILSFDNVMELSEPVSEY----------------PFV 185
Cdd:PRK10524 164 DagsrggkvvpykPLLDE------------AIALAQHKP---RHVLLVDRGLAPMARVAGRdvdyatlraqhlgarvPVE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 186 EIKQSDTAALLYSSGTTGTSKGVELTHGNFiAASLMVTMDQDLMGEYHGVFLCFLPMFHVFGLAVITYSQLqrgnaLVSM 265
Cdd:PRK10524 229 WLESNEPSYILYTSGTTGKPKGVQRDTGGY-AVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPL-----LAGM 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 266 ARFELE-------------LVlkniEKFRVTHLWVVPPVFLALSKQ--SIVKKFDLSSLKYIGSGAAPLGkdlmEECGRN 330
Cdd:PRK10524 303 ATIMYEglptrpdagiwwrIV----EKYKVNRMFSAPTAIRVLKKQdpALLRKHDLSSLRALFLAGEPLD----EPTASW 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 331 IPNVL---LMQGYGMTETcG--IVSVEdPRLGKRNS--GSAGMLAPGVEAQIVSVETGKSQPPNQQGEIWVRGPNmmkgy 403
Cdd:PRK10524 375 ISEALgvpVIDNYWQTET-GwpILAIA-RGVEDRPTrlGSPGVPMYGYNVKLLNEVTGEPCGPNEKGVLVIEGPL----- 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 404 lnnPQATKETI--DKKSWVHT------------GDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDA 469
Cdd:PRK10524 448 ---PPGCMQTVwgDDDRFVKTywslfgrqvystFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEV 524
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15234634 470 VVIPFPDEEAGEVPIAFVVRSPNSSIT--------EQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRRELV 537
Cdd:PRK10524 525 AVVGVKDALKGQVAVAFVVPKDSDSLAdrearlalEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQ 600
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
180-539 |
6.63e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 132.11 E-value: 6.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 180 SEYPFVEIKQSDTAALLYSSGTTGTSKGVELTHGNFIAASLMVTmDQDLMGEYHGVFLCfLPMFH----VFGLAVitysQ 255
Cdd:PRK07867 142 AEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLA-QRFGLGPDDVCYVS-MPLFHsnavMAGWAV----A 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 256 LQRGNALVSMARFELELVLKNIEKFRVTHL-WVVPPVFLALSKQSIVKKFDlSSLKYI-GSGAAPlgKDLmEECGRNIpN 333
Cdd:PRK07867 216 LAAGASIALRRKFSASGFLPDVRRYGATYAnYVGKPLSYVLATPERPDDAD-NPLRIVyGNEGAP--GDI-ARFARRF-G 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 334 VLLMQGYGMTEtcGIVSVEdpRLGKRNSGSAGMLAPGVeaQIVSVETGKSQPPNQQ------------GEIW-VRGPNMM 400
Cdd:PRK07867 291 CVVVDGFGSTE--GGVAIT--RTPDTPPGALGPLPPGV--AIVDPDTGTECPPAEDadgrllnadeaiGELVnTAGPGGF 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 401 KGYLNNPQATKETIdKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAG 480
Cdd:PRK07867 365 EGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVG 443
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15234634 481 EVPIAFVVRSPNSSITEQDIQKFIAKQ--VAPYKRLRRVSFISLVPKSAAGKILRRELVQQ 539
Cdd:PRK07867 444 DQVMAALVLAPGAKFDPDAFAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQLSAE 504
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
23-442 |
1.64e-32 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 131.17 E-value: 1.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 23 KDPNTSLVSFLFRNSSSYPSKLAIADSDTGDS--------LTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQF-P 93
Cdd:PRK09274 2 MASMANIARHLPRAAQERPDQLAVAVPGGRGAdgklaydeLSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFfA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 94 LCFlAVTAIGGVFTTANPLYTVNEVSKQIKDSNPK--IIISVNQLFDKIKGFDLPVVLlgSKDTVEIPPGSNSKILSfdn 171
Cdd:PRK09274 82 LTF-ALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDafIGIPKAHLARRLFGWGKPSVR--RLVTVGGRLLWGGTTLA--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 172 VMELSEPVSEYPFVEIKQSDTAALLYSSGTTGTSKGVELTHGNFIAaslMVTMDQDLMGEYHG-VFLCFLPMFHVFGLA- 249
Cdd:PRK09274 156 TLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEA---QIEALREDYGIEPGeIDLPTFPLFALFGPAl 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 250 ----VITYSQLQRgNALVSMARfelelVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLME 325
Cdd:PRK09274 233 gmtsVIPDMDPTR-PATVDPAK-----LFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 326 ECGRNIPN-VLLMQGYGMTETCGIVSVE-DPRLGKRNSGSA-------GMLAPGVEAQIVSVETG--------KSQPPNQ 388
Cdd:PRK09274 307 RFRAMLPPdAEILTPYGATEALPISSIEsREILFATRAATDngagicvGRPVDGVEVRIIAISDApipewddaLRLATGE 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 15234634 389 QGEIWVRGPNMMKGYLNNPQATKET--IDKKS--WVHTGDLGYFNEDGNLYVVDRIKE 442
Cdd:PRK09274 387 IGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLGYLDAQGRLWFCGRKAH 444
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
175-539 |
2.12e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 130.53 E-value: 2.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 175 LSEPVSEYPFVEIKQSDTAALLYSSGTTGTSKGVELTHGN--FIAASLMvtmdqdlmgEYHG-----VFLCFLPMFH--- 244
Cdd:PRK13388 135 VAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRlaFAGRALT---------ERFGltrddVCYVSMPLFHsna 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 245 -VFGLAVItysqLQRGNALVSMARFELELVLKNIEKFRVTHL-WVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPlgKD 322
Cdd:PRK13388 206 vMAGWAPA----VASGAAVALPAKFSASGFLDDVRRYGATYFnYVGKPLAYILATPERPDDADNPLRVAFGNEASP--RD 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 323 lMEECGRNIpNVLLMQGYGMTETCGIVSVED--PRlgkrnsGSAGMLAPGVEaqIVSVETGKSQPPNQ------------ 388
Cdd:PRK13388 280 -IAEFSRRF-GCQVEDGYGSSEGAVIVVREPgtPP------GSIGRGAPGVA--IYNPETLTECAVARfdahgallnade 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 389 -QGEIWVR-GPNMMKGYLNNPQATKETIdKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDI 466
Cdd:PRK13388 350 aIGELVNTaGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAI 428
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15234634 467 LDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQKFIAKQ------VAPykRLRRVSfiSLVPKSAAGKILRRELVQQ 539
Cdd:PRK13388 429 NRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAFLAAQpdlgtkAWP--RYVRIA--ADLPSTATNKVLKRELIAQ 503
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
41-536 |
2.68e-32 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 129.76 E-value: 2.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 41 PSKLAIADSDtgDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSK 120
Cdd:cd17655 11 PDHTAVVFED--QTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 121 QIKDSNPKIIISVNQLFDKIKGFDLpvVLLGSKDTVEIPPGSNSKilsfdnvmelsepvseypfVEIKQSDTAALLYSSG 200
Cdd:cd17655 89 ILEDSGADILLTQSHLQPPIAFIGL--IDLLDEDTIYHEESENLE-------------------PVSKSDDLAYVIYTSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 201 TTGTSKGVELTHGNFIaaSLMVTMDQDLMGEYHGVFLCFLPMfhVFGLAVIT-YSQLQRGNALVSMARFEL---ELVLKN 276
Cdd:cd17655 148 STGKPKGVMIEHRGVV--NLVEWANKVIYQGEHLRVALFASI--SFDASVTEiFASLLSGNTLYIVRKETVldgQALTQY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 277 IEKFRVTHLwVVPPVFLALSKQsiVKKFDLSSLKYIGSGAAPLGKDLMEE-CGRNIPNVLLMQGYGMTETCGIVSVEDPR 355
Cdd:cd17655 224 IRQNRITII-DLTPAHLKLLDA--ADDSEGLSLKHLIVGGEALSTELAKKiIELFGTNPTITNAYGPTETTVDASIYQYE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 356 LGKRNSGSAGMLAPGVEAQIVSVET-GKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKSWV------HTGDLGYF 428
Cdd:cd17655 301 PETDQQVSVPIGKPLGNTRIYILDQyGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARW 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 429 NEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNssITEQDIQKFIAKQV 508
Cdd:cd17655 381 LPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKE--LPVAQLREFLAREL 458
|
490 500 510
....*....|....*....|....*....|
gi 15234634 509 APYkrLRRVSFISL--VPKSAAGKILRREL 536
Cdd:cd17655 459 PDY--MIPSYFIKLdeIPLTPNGKVDRKAL 486
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
56-541 |
3.68e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 129.83 E-value: 3.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 56 TFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANP-------LYTVNEVSKQIKDSNPK 128
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPrlfpeqiAYIVNHAEDRYVLFDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 129 IIISVNQLFDK---IKGFdlpvVLLGSKDTVeipPGSNSKILSFDNVMELSEPVSEYPfvEIKQSDTAALLYSSGTTGTS 205
Cdd:PRK07008 121 FLPLVDALAPQcpnVKGW----VAMTDAAHL---PAGSTPLLCYETLVGAQDGDYDWP--RFDENQASSLCYTSGTTGNP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 206 KGVELTHGNFI----AASLmvtmdQDLMG-EYHGVFLCFLPMFHV--FGL---AVITYSQLQ-RGNALVSMARFELelvl 274
Cdd:PRK07008 192 KGALYSHRSTVlhayGAAL-----PDAMGlSARDAVLPVVPMFHVnaWGLpysAPLTGAKLVlPGPDLDGKSLYEL---- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 275 knIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLK--YIGSGAAP--LGKDLMEECGrnipnVLLMQGYGMTE------ 344
Cdd:PRK07008 263 --IEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRrtVIGGSACPpaMIRTFEDEYG-----VEVIHAWGMTEmsplgt 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 345 TCGIVSVEDPR--------LGKRnsgsaGMLAPGVEAQIVSvETGKSQPPN--QQGEIWVRGPNMMKGYLNNPQATkeTI 414
Cdd:PRK07008 336 LCKLKWKHSQLpldeqrklLEKQ-----GRVIYGVDMKIVG-DDGRELPWDgkAFGDLQVRGPWVIDRYFRGDASP--LV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 415 DkkSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSS 494
Cdd:PRK07008 408 D--GWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAE 485
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15234634 495 ITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRRELVQQVR 541
Cdd:PRK07008 486 VTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQFR 532
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
52-541 |
4.73e-32 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 129.24 E-value: 4.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 52 GDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIG------GVFTTANPLYTVNEVSKqikds 125
Cdd:PRK04813 25 GEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGhayipvDVSSPAERIEMIIEVAK----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 126 nPKIIISVNqlfdkikgfDLPVVLLgskdtveippgsNSKILSFDNVMELSEPVSEYPFVE-IKQSDTAALLYSSGTTGT 204
Cdd:PRK04813 100 -PSLIIATE---------ELPLEIL------------GIPVITLDELKDIFATGNPYDFDHaVKGDDNYYIIFTSGTTGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 205 SKGVELTHGNFIaaSLMVTMDQDLMGEYHGVFLCFLPmfHVFGLAVIT-YSQLQRGNALVSM-----ARFELelVLKNIE 278
Cdd:PRK04813 158 PKGVQISHDNLV--SFTNWMLEDFALPEGPQFLNQAP--YSFDLSVMDlYPTLASGGTLVALpkdmtANFKQ--LFETLP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 279 KFRVThLWVVPPVF--LALskqsIVKKFD---LSSLKYIgsgaapL--GKDLMEECGRNI----PNVLLMQGYGMTETCG 347
Cdd:PRK04813 232 QLPIN-VWVSTPSFadMCL----LDPSFNeehLPNLTHF------LfcGEELPHKTAKKLlerfPSATIYNTYGPTEATV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 348 IVS---VEDPRLGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKE---TIDKKSWVH 421
Cdd:PRK04813 301 AVTsieITDEMLDQYKRLPIGYAKPDSPLLIID-EEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEaffTFDGQPAYH 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 422 TGDLGYFnEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQ 501
Cdd:PRK04813 380 TGDAGYL-EDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDFEREFELT 458
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 15234634 502 KFIAKQVA----PYKRLRRVSFISLVPKSAAGKILRRELVQQVR 541
Cdd:PRK04813 459 KAIKKELKerlmEYMIPRKFIYRDSLPLTPNGKIDRKALIEEVN 502
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
172-542 |
5.01e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 129.73 E-value: 5.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 172 VMELSEPVSEYPF--VEIKQSDTAALLYSSGTTGTSKGVELTHGNFIA--ASLMVTMDQDlmgEYHGVFLCFLPMFHVFG 247
Cdd:PRK07768 132 VLTVADLLAADPIdpVETGEDDLALMQLTSGSTGSPKAVQITHGNLYAnaEAMFVAAEFD---VETDVMVSWLPLFHDMG 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 248 LAVITYSQLQRGNALVSM--ARFELELVL--KNIEKFRVTHLwvVPPVF----LA--LSKQSIVKKFDLSSLKYIGSGAA 317
Cdd:PRK07768 209 MVGFLTVPMYFGAELVKVtpMDFLRDPLLwaELISKYRGTMT--AAPNFayalLArrLRRQAKPGAFDLSSLRFALNGAE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 318 PLG----KDLMEECGR-NIPNVLLMQGYGMTETCGIVSVEDPRLGKR------------------NSGSA------GMLA 368
Cdd:PRK07768 287 PIDpadvEDLLDAGARfGLRPEAILPAYGMAEATLAVSFSPCGAGLVvdevdadllaalrravpaTKGNTrrlatlGPPL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 369 PGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLnNPQATKETIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKG 448
Cdd:PRK07768 367 PGLEVRVVD-EDGQVLPPRGVGVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAG 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 449 FQVAPAELEGLLVSHPDIL--DAVVIPFPDEEAGEvPIAFVVRSPNSSitEQDIQKFIAKQVAPYKR----LRRVSFISL 522
Cdd:PRK07768 445 RNIYPTDIERAAARVEGVRpgNAVAVRLDAGHSRE-GFAVAVESNAFE--DPAEVRRIRHQVAHEVVaevgVRPRNVVVL 521
|
410 420
....*....|....*....|....
gi 15234634 523 ----VPKSAAGKILRRELVQQVRS 542
Cdd:PRK07768 522 gpgsIPKTPSGKLRRANAAELVTP 545
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
33-538 |
2.92e-31 |
|
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: 125.88 E-value: 2.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 33 LFRNS-SSYPSKLAIadSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANP 111
Cdd:cd17653 2 AFERIaAAHPDAVAV--ESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 112 LYTVNEVSKQIKDSNPKIIISVNqlfdkikgfdlpvvllgskdtveippgsnskilsfdnvmelsepvseypfveiKQSD 191
Cdd:cd17653 80 KLPSARIQAILRTSGATLLLTTD-----------------------------------------------------SPDD 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 192 TAALLYSSGTTGTSKGVELTHGNFIAAslmVTMDQDLMGEYHG--VFLCFLPMFHVFgLAVItYSQLQRGNALV---SMA 266
Cdd:cd17653 107 LAYIIFTSGSTGIPKGVMVPHRGVLNY---VSQPPARLDVGPGsrVAQVLSIAFDAC-IGEI-FSTLCNGGTLVladPSD 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 267 RFelELVLKNIEKFRVThlwvvpPVFLalskqSIVKKFDLSSLKYIGSGAAPLGKDLMEECGrniPNVLLMQGYGMTETC 346
Cdd:cd17653 182 PF--AHVARTVDALMST------PSIL-----STLSPQDFPNLKTIFLGGEAVPPSLLDRWS---PGRRLYNAYGPTECT 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 347 GIVSVEDPRLGKRNsgSAGMLAPGVEAQIvsVETGKSQPP-NQQGEIWVRGPNMMKGYLNNPQATKETIDKKSWVH---- 421
Cdd:cd17653 246 ISSTMTELLPGQPV--TIGKPIPNSTCYI--LDADLQPVPeGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPgsrm 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 422 --TGDLGYFNEDGNLYVVDRIKELIKYKGFQVA-PAELEGLLVSHPDILDAVVIpfpdeEAGEVPIAFVVrsPnSSITEQ 498
Cdd:cd17653 322 yrTGDYGRWTEDGGLEFLGREDNQVKVRGFRINlEEIEEVVLQSQPEVTQAAAI-----VVNGRLVAFVT--P-ETVDVD 393
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 15234634 499 DIQKFIAKQVAPYKRLRRvsFISL--VPKSAAGKILRRELVQ 538
Cdd:cd17653 394 GLRSELAKHLPSYAVPDR--IIALdsFPLTANGKVDRKALRE 433
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
45-536 |
1.05e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 125.07 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 45 AIADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKD 124
Cdd:PRK12316 2019 AIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLED 2098
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 125 SNPKIIISVNQLFDKIkgfdlpvvllgskdtveiPPGSNSKILSFDNVMELSEPVSEYPFVEIKQSDTAALLYSSGTTGT 204
Cdd:PRK12316 2099 SGAALLLTQRHLLERL------------------PLPAGVARLPLDRDAEWADYPDTAPAVQLAGENLAYVIYTSGSTGL 2160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 205 SKGVELTHGNFIA-------ASLMVTMDQDLM-------GEYHGvflCFLPMFHvfGLAVITysqlqRGNALvsmarFEL 270
Cdd:PRK12316 2161 PKGVAVSHGALVAhcqaageRYELSPADCELQfmsfsfdGAHEQ---WFHPLLN--GARVLI-----RDDEL-----WDP 2225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 271 ELVLKNIEKFRVThLWVVPPVFL-ALSKQSIVKKFDLSSLKYIGSGAApLGKDLMEECGRNIPNVLLMQGYGMTETCGIV 349
Cdd:PRK12316 2226 EQLYDEMERHGVT-ILDFPPVYLqQLAEHAERDGRPPAVRVYCFGGEA-VPAASLRLAWEALRPVYLFNGYGPTEAVVTP 2303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 350 SVEDPRlgkRNSGSAGMLAP-----GVEAQIVSVETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKSWVH--- 421
Cdd:PRK12316 2304 LLWKCR---PQDPCGAAYVPigralGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSAsge 2380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 422 ----TGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFpDEEAGEVPIAFVVRSPNSSITE 497
Cdd:PRK12316 2381 rlyrTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAAEDLL 2459
|
490 500 510
....*....|....*....|....*....|....*....
gi 15234634 498 QDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:PRK12316 2460 AELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
55-464 |
1.82e-29 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 122.92 E-value: 1.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 55 LTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPL----CF---LAVTAIGGVFTTANPLYTVNE--VSKQIKDS 125
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIalqgCFrqnITVVTIYASLGEEALCHSLNEteVTTVICDS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 126 NP-KIIISVNQLFDKIKGfdlpVVLL---GSKDTVEIPPGSNSKILSFDNVMELSEPVSEYPFVEIKqSDTAALLYSSGT 201
Cdd:PLN02387 187 KQlKKLIDISSQLETVKR----VIYMddeGVDSDSSLSGSSNWTVSSFSEVEKLGKENPVDPDLPSP-NDIAVIMYTSGS 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 202 TGTSKGVELTHGNFIA--ASLMvTMDQDLmgEYHGVFLCFLPMFHVFGLAV----------ITY----------SQLQRG 259
Cdd:PLN02387 262 TGLPKGVMMTHGNIVAtvAGVM-TVVPKL--GKNDVYLAYLPLAHILELAAesvmaavgaaIGYgspltltdtsNKIKKG 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 260 N-ALVSMARFEL------------ELVLKNIEkfrvthlwvvppvflalSKQSIVKK-FDLS------------------ 307
Cdd:PLN02387 339 TkGDASALKPTLmtavpaildrvrDGVRKKVD-----------------AKGGLAKKlFDIAykrrlaaiegswfgawgl 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 308 -------------------SLKYIGSGAAPLGKDLMeecgRNIpNVLL----MQGYGMTETC--GIVS-VEDPRLGKrns 361
Cdd:PLN02387 402 ekllwdalvfkkiravlggRIRFMLSGGAPLSGDTQ----RFI-NICLgapiGQGYGLTETCagATFSeWDDTSVGR--- 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 362 gsAGMLAPGVEAQIVSVETGK---SQPPNQQGEIWVRGPNMMKGYLNNPQATKET--IDKKS--WVHTGDLGYFNEDGNL 434
Cdd:PLN02387 474 --VGPPLPCCYVKLVSWEEGGyliSDKPMPRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCL 551
|
490 500 510
....*....|....*....|....*....|.
gi 15234634 435 YVVDRIKELIKYK-GFQVAPAELEGLLVSHP 464
Cdd:PLN02387 552 EIIDRKKDIVKLQhGEYVSLGKVEAALSVSP 582
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
41-536 |
1.83e-29 |
|
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: 121.04 E-value: 1.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 41 PSKLAIADSDTgdSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSK 120
Cdd:cd17650 1 PDAIAVSDATR--QLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 121 QIKDSNPKIIisvnqlfdkikgfdlpvvllgskdtveippgsnskilsfdnvmeLSEPvseypfveikqSDTAALLYSSG 200
Cdd:cd17650 79 MLEDSGAKLL--------------------------------------------LTQP-----------EDLAYVIYTSG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 201 TTGTSKGVELTHGNFIAASLmvTMDQdlmgEYHgvflcfLPMFHVFGLAVITYS----------QLQRGNALVSM---AR 267
Cdd:cd17650 104 TTGKPKGVMVEHRNVAHAAH--AWRR----EYE------LDSFPVRLLQMASFSfdvfagdfarSLLNGGTLVICpdeVK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 268 FELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKY--IGSGAAPLgKDLMEECGRNIPNVLLMQGYGMTET 345
Cdd:cd17650 172 LDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLliVGSDGCKA-QDFKTLAARFGQGMRIINSYGVTEA 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 346 C---GIVSVEDPRLGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKSWV-- 420
Cdd:cd17650 251 TidsTYYEEGRDPLGDSANVPIGRPLPNTAMYVLD-ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFApg 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 421 ----HTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVrsPNSSIT 496
Cdd:cd17650 330 ermyRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVV--AAATLN 407
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 15234634 497 EQDIQKFIAKQVAPYkrLRRVSFISLV--PKSAAGKILRREL 536
Cdd:cd17650 408 TAELRAFLAKELPSY--MIPSYYVQLDalPLTPNGKVDRRAL 447
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
43-536 |
1.91e-29 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 122.56 E-value: 1.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 43 KLAI---ADsDTGDS--LTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFT------TANP 111
Cdd:PRK00174 83 KVAIiweGD-DPGDSrkITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSvvfggfSAEA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 112 LYTvnevskQIKDSNPKIIISVNQLFDKIKgfdlPVVLlgsKDTV----EIPPgsnskilSFDNVM-------------- 173
Cdd:PRK00174 162 LAD------RIIDAGAKLVITADEGVRGGK----PIPL---KANVdealANCP-------SVEKVIvvrrtggdvdwveg 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 174 ------ELSEPVSEY-PFVEIKQSDTAALLYSSGTTGTSKGVELTHGNFIAASLMvTM-------DQDlmgeyhgVFLCF 239
Cdd:PRK00174 222 rdlwwhELVAGASDEcEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAM-TMkyvfdykDGD-------VYWCT 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 240 LPMFHVFGLAVITYSQLQRGNALV---------SMARFelelvLKNIEKFRVTHLWVVPPVFLALSKQ--SIVKKFDLSS 308
Cdd:PRK00174 294 ADVGWVTGHSYIVYGPLANGATTLmfegvpnypDPGRF-----WEVIDKHKVTIFYTAPTAIRALMKEgdEHPKKYDLSS 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 309 LKYIGSGAAP------------LGKdlmEECgrniPNVllmQGYGMTETCGIVSVEDPRLGKRNSGSAGMLAPGVEAQIV 376
Cdd:PRK00174 369 LRLLGSVGEPinpeawewyykvVGG---ERC----PIV---DTWWQTETGGIMITPLPGATPLKPGSATRPLPGIQPAVV 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 377 SvETGKSQPPNQQG-----EIWvrgPNMMKGYLNNPQATKETIdkksWVH------TGDLGYFNEDGNLYVVDRIKELIK 445
Cdd:PRK00174 439 D-EEGNPLEGGEGGnlvikDPW---PGMMRTIYGDHERFVKTY----FSTfkgmyfTGDGARRDEDGYYWITGRVDDVLN 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 446 YKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVV----RSPNSSITeQDIQKFIAKQVAPYKRLRRVSFIS 521
Cdd:PRK00174 511 VSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTlkggEEPSDELR-KELRNWVRKEIGPIAKPDVIQFAP 589
|
570
....*....|....*
gi 15234634 522 LVPKSAAGKILRREL 536
Cdd:PRK00174 590 GLPKTRSGKIMRRIL 604
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
41-536 |
4.24e-29 |
|
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: 120.07 E-value: 4.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 41 PSKLAIADSDtgDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSK 120
Cdd:cd12114 1 PDATAVICGD--GTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 121 QIKDSNPKIIISVnqlfdkikgfDLPVVLLGSKDTVEIPPGSnskilsfdnvmeLSEPVSEYPFVEIKQSDTAALLYSSG 200
Cdd:cd12114 79 ILADAGARLVLTD----------GPDAQLDVAVFDVLILDLD------------ALAAPAPPPPVDVAPDDLAYVIFTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 201 TTGTSKGVELTHgnfiaASLMVTMDQdlMGEYHGV----------FLCF-LPMFHVFGL-----AVITYSQLQRGNALvS 264
Cdd:cd12114 137 STGTPKGVMISH-----RAALNTILD--INRRFAVgpddrvlalsSLSFdLSVYDIFGAlsagaTLVLPDEARRRDPA-H 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 265 MARFelelvlknIEKFRVThLWV-VPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECGRNIPNVLLMQGYGMT 343
Cdd:cd12114 209 WAEL--------IERHGVT-LWNsVPALLEMLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGAT 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 344 ETcGIVSVEDPrLGKrnsgsagmlapgVEAQIVSVETGKsqP-PNQQ----------------GEIWVRGPNMMKGYLNN 406
Cdd:cd12114 280 EA-SIWSIYHP-IDE------------VPPDWRSIPYGR--PlANQRyrvldprgrdcpdwvpGELWIGGRGVALGYLGD 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 407 PQATKET----IDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEV 482
Cdd:cd12114 344 PELTAARfvthPDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRL 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15234634 483 pIAFVV-RSPNSSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:cd12114 424 -AAFVVpDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
41-536 |
1.35e-28 |
|
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: 118.19 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 41 PSKLAIADSDtgDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSK 120
Cdd:cd12115 13 PDAIALVCGD--ESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 121 QIKDSNPKIIisvnqlfdkikgfdlpvvllgskdtveippgsnskilsfdnvmeLSEPvseypfveikqSDTAALLYSSG 200
Cdd:cd12115 91 ILEDAQARLV--------------------------------------------LTDP-----------DDLAYVIYTSG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 201 TTGTSKGVELTHGNfiAASLMVTMDQDLMGEY-HGVF----LCF-LPMFHVFG-LAVitysqlqrgNALVSMARFELELV 273
Cdd:cd12115 116 STGRPKGVAIEHRN--AAAFLQWAAAAFSAEElAGVLastsICFdLSVFELFGpLAT---------GGKVVLADNVLALP 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 274 LKNIEKfRVTHLWVVPPVFLALSKQSIVKKfdlsSLKYIGSGAAPLGKDLMEECGRNIPNVLLMQGYGMTETCGIVSVED 353
Cdd:cd12115 185 DLPAAA-EVTLINTVPSAAAELLRHDALPA----SVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAP 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 354 PRLGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETI------DKKSWVHTGDLGY 427
Cdd:cd12115 260 VPPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFlpdpfgPGARLYRTGDLVR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 428 FNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQKFIAKQ 507
Cdd:cd12115 339 WRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTR 418
|
490 500
....*....|....*....|....*....
gi 15234634 508 VAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:cd12115 419 LPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
23-478 |
2.39e-28 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 118.77 E-value: 2.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 23 KDPNTSLVSFLfRNSSSYPSKLAIADSDTGdSLTFSQLKSAVARLAHgfhRLGIRKNDVVLIFAPNSYQFPLCFLAVTAI 102
Cdd:PRK06334 16 RSGKTVLESFL-KLCSEMTTATVCWDEQLG-KLSYNQVRKAVIALAT---KVSKYPDQHIGIMMPASAGAYIAYFATLLS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 103 GGVFTTANPLYTVNEVSKQIKDSNPKIIISVNQLFDK---IKGFDL--PVVLLGSKDTveippgsnSKILSFDNVMELSE 177
Cdd:PRK06334 91 GKIPVMINWSQGLREVTACANLVGVTHVLTSKQLMQHlaqTHGEDAeyPFSLIYMEEV--------RKELSFWEKCRIGI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 178 PVS-EYPFV-------EIKQSDTAALLYSSGTTGTSKGVELTHGNFIA---ASL--MVTMDQDLMgeyhgvfLCFLPMFH 244
Cdd:PRK06334 163 YMSiPFEWLmrwfgvsDKDPEDVAVILFTSGTEKLPKGVPLTHANLLAnqrACLkfFSPKEDDVM-------MSFLPPFH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 245 VFGLAVITYSQLQRGNALV-SMARFELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDL 323
Cdd:PRK06334 236 AYGFNSCTLFPLLSGVPVVfAYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 324 MEECGRNIPNVLLMQGYGMTETCGIVSVEDPRlGKRNSGSAGMLAPGVEAQIVSVETGKSQPPNQQGEIWVRGPNMMKGY 403
Cdd:PRK06334 316 YQEALKTFPHIQLRQGYGTTECSPVITINTVN-SPKHESCVGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 404 L-NNPQATKETIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSH------PDILDAVVIPFPD 476
Cdd:PRK06334 395 LgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGfgqnaaDHAGPLVVCGLPG 474
|
..
gi 15234634 477 EE 478
Cdd:PRK06334 475 EK 476
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
25-536 |
2.63e-28 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 118.57 E-value: 2.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 25 PNTSLVSFLfRNSSSYPSKLAIADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGG 104
Cdd:PRK05857 13 PSTVLDRVF-EQARQQPEAIALRRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 105 VFTTAN---PLYTVNEVSkQIKDsnPKIIISVNQlfDKIKGFDLPVVLLG-SKDTVEIPPGSNSKILSFDNVMELSEPvs 180
Cdd:PRK05857 92 IAVMADgnlPIAAIERFC-QITD--PAAALVAPG--SKMASSAVPEALHSiPVIAVDIAAVTRESEHSLDAASLAGNA-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 181 eypfvEIKQSDTAALLYSSGTTGTSKGVELTHGNFIAASlmvtmdqDLMGEYHGVFLCF---------LPMFHVFGLAVI 251
Cdd:PRK05857 165 -----DQGSEDPLAMIFTSGTTGEPKAVLLANRTFFAVP-------DILQKEGLNWVTWvvgettyspLPATHIGGLWWI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 252 tYSQLQRGNALVSMARFELELV-LKNIEKFRVTHLwvVPPVFLALSKQSIVKKFDLSSLKYIGSGAA-PLGKDL--MEEC 327
Cdd:PRK05857 233 -LTCLMHGGLCVTGGENTTSLLeILTTNAVATTCL--VPTLLSKLVSELKSANATVPSLRLVGYGGSrAIAADVrfIEAT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 328 GrnipnVLLMQGYGMTET-CGIVSV--EDPRLGKRNSGSAGMLAPGVEAQIVSVETGKSQPPNQQ-----GEIWVRGPNM 399
Cdd:PRK05857 310 G-----VRTAQVYGLSETgCTALCLptDDGSIVKIEAGAVGRPYPGVDVYLAATDGIGPTAPGAGpsasfGTLWIKSPAN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 400 MKGYLNNPQATKETIdKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEA 479
Cdd:PRK05857 385 MLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEF 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15234634 480 GE-VPIAFVVRSPNSSITEQDIQKFIAkqvAPYKR----LRRVSFISLV---PKSAAGKILRREL 536
Cdd:PRK05857 464 GAlVGLAVVASAELDESAARALKHTIA---ARFRResepMARPSTIVIVtdiPRTQSGKVMRASL 525
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
41-536 |
3.61e-28 |
|
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: 117.58 E-value: 3.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 41 PSKLAIADSDtgDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSK 120
Cdd:cd17656 2 PDAVAVVFEN--QKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 121 QIKDSNPKIIISVNQLFDKIKgFDLPVVLLGSKDtveIPPGSNSKILSFDNvmelsepvseypfveikQSDTAALLYSSG 200
Cdd:cd17656 80 IMLDSGVRVVLTQRHLKSKLS-FNKSTILLEDPS---ISQEDTSNIDYINN-----------------SDDLLYIIYTSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 201 TTGTSKGVELTHGNfIAASLMVTMDQDLMGEYHGVFLCFLPMFHVFGLAVitYSQLQRGNALvSMARFELELVLKNIEKF 280
Cdd:cd17656 139 TTGKPKGVQLEHKN-MVNLLHFEREKTNINFSDKVLQFATCSFDVCYQEI--FSTLLSGGTL-YIIREETKRDVEQLFDL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 281 RVTH---LWVVPPVFLAL--SKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECGRNiPNVLLMQGYGMTETcGIVSV---- 351
Cdd:cd17656 215 VKRHnieVVFLPVAFLKFifSEREFINRFPTCVKHIITAGEQLVITNEFKEMLHE-HNVHLHNHYGPSET-HVVTTytin 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 352 ------EDPRLGKrnsgsagmlaPGVEAQIVSV-ETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETI------DKKS 418
Cdd:cd17656 293 peaeipELPPIGK----------PISNTWIYILdQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFfpdpfdPNER 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 419 WVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVrsPNSSITEQ 498
Cdd:cd17656 363 MYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV--MEQELNIS 440
|
490 500 510
....*....|....*....|....*....|....*...
gi 15234634 499 DIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:cd17656 441 QLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
37-513 |
4.68e-28 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 116.89 E-value: 4.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 37 SSSYPSKLAIADSDtgDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVn 116
Cdd:PRK09029 13 AQVRPQAIALRLND--EVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQ- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 117 EVSKQIKDSNPKIIISVNQLFDKIKGFDLPVVLlgskdtveippgsnskilsfdnvmelsePVSEYPFVEIKQSDTAALL 196
Cdd:PRK09029 90 PLLEELLPSLTLDFALVLEGENTFSALTSLHLQ----------------------------LVEGAHAVAWQPQRLATMT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 197 YSSGTTGTSKGVELTHGNFIAA-----SLMVTMDQDlmgeyhgVFLCFLPMFHVFGLAvITYSQLQRGnalvsmARfele 271
Cdd:PRK09029 142 LTSGSTGLPKAAVHTAQAHLASaegvlSLMPFTAQD-------SWLLSLPLFHVSGQG-IVWRWLYAG------AT---- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 272 LVLKNIEKF-----RVTHLWVVPPVFLALSKQSIVKkfdlSSLKYI--GsGAAplgkdlmeecgrnIPNVLLMQ------ 338
Cdd:PRK09029 204 LVVRDKQPLeqalaGCTHASLVPTQLWRLLDNRSEP----LSLKAVllG-GAA-------------IPVELTEQaeqqgi 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 339 ----GYGMTETCGIVSVedprlgKRNSGSA--GMLAPGVEAQIVSvetgksqppnqqGEIWVRGPNMMKGYLNNPQATKE 412
Cdd:PRK09029 266 rcwcGYGLTEMASTVCA------KRADGLAgvGSPLPGREVKLVD------------GEIWLRGASLALGYWRQGQLVPL 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 413 TiDKKSWVHTGDLGYFNeDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAfVVRSpN 492
Cdd:PRK09029 328 V-NDEGWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVA-VVES-D 403
|
490 500
....*....|....*....|.
gi 15234634 493 SSITEQDIQKFIAKQVAPYKR 513
Cdd:PRK09029 404 SEAAVVNLAEWLQDKLARFQQ 424
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
45-536 |
2.17e-27 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 114.66 E-value: 2.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 45 AIADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKD 124
Cdd:cd17652 3 APAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 125 SNPKIIisvnqlfdkikgfdlpvvllgskdtveippgsnskilsfdnvmeLSEPvseypfveikqSDTAALLYSSGTTGT 204
Cdd:cd17652 83 ARPALL--------------------------------------------LTTP-----------DNLAYVIYTSGSTGR 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 205 SKGVELTHGNfiAASLMVTMDQDLMGEYHGVFLCFL-PMFHVF------------GLAVITYSQLQRGNALVSMARFEle 271
Cdd:cd17652 108 PKGVVVTHRG--LANLAAAQIAAFDVGPGSRVLQFAsPSFDASvwellmallagaTLVLAPAEELLPGEPLADLLREH-- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 272 lvlkniekfRVTHLWVVPPVFLALSKQsivkkfDLSSLKYIGSGAAPLGKDLMEE--CGRNIPNvllmqGYGMTETCGIV 349
Cdd:cd17652 184 ---------RITHVTLPPAALAALPPD------DLPDLRTLVVAGEACPAELVDRwaPGRRMIN-----AYGPTETTVCA 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 350 SVEDPrLGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKEtidkkSWV--------- 420
Cdd:cd17652 244 TMAGP-LPGGGVPPIGRPVPGTRVYVLD-ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAE-----RFVadpfgapgs 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 421 ---HTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITE 497
Cdd:cd17652 317 rmyRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTA 396
|
490 500 510
....*....|....*....|....*....|....*....
gi 15234634 498 QDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:cd17652 397 AELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
35-488 |
5.08e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 116.60 E-value: 5.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 35 RNSSSYPSKL---------------AIADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAV 99
Cdd:PRK12316 4542 RTDAGYPATRcvhqlvaerarmtpdAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAV 4621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 100 TAIGGVFTTANPLYTVNEVSKQIKDSNPKIIISVNQLFDKikgfdLPvvllgskdtveIPPGSNSkiLSFDNVMELSEPV 179
Cdd:PRK12316 4622 LKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQR-----LP-----------IPDGLAS--LALDRDEDWEGFP 4683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 180 SEYPFVEIKQSDTAALLYSSGTTGTSKGVELTHGNFIAASLMvtmdqdlMGEYHGV-----FLCFLPM-FHVFGLAVitY 253
Cdd:PRK12316 4684 AHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHA-------TGERYELtpddrVLQFMSFsFDGSHEGL--Y 4754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 254 SQLQRGNALVsMARFEL---ELVLKNIEKFRVTHLwVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECGRN 330
Cdd:PRK12316 4755 HPLINGASVV-IRDDSLwdpERLYAEIHEHRVTVL-VFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLAWRA 4832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 331 IPNVLLMQGYGMTETCGIVSVEDPRLGKRNSGSA---GMLAPGVEAQIVSVEtGKSQPPNQQGEIWVRGPNMMKGYLNNP 407
Cdd:PRK12316 4833 LKPVYLFNGYGPTETTVTVLLWKARDGDACGAAYmpiGTPLGNRSGYVLDGQ-LNPLPVGVAGELYLGGEGVARGYLERP 4911
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 408 QATKETI------DKKSWVH-TGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDeEAG 480
Cdd:PRK12316 4912 ALTAERFvpdpfgAPGGRLYrTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEG-AVG 4990
|
....*...
gi 15234634 481 EVPIAFVV 488
Cdd:PRK12316 4991 KQLVGYVV 4998
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
188-476 |
1.02e-26 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 114.53 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 188 KQSDTAALLYSSGTTGTSKGVELTHGNfiAASLMVTMD------QDLMgEYHGVFLCFLPMFHVFGLAVITYsqLQRGNA 261
Cdd:PLN02430 218 KPLDICTIMYTSGTSGDPKGVVLTHEA--VATFVRGVDlfmeqfEDKM-THDDVYLSFLPLAHILDRMIEEY--FFRKGA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 262 LVSMARFELELVLKNIEKFRVTHLWVVPPVF--------LALSKQSIVKKFDLSSL-KY--------------------- 311
Cdd:PLN02430 293 SVGYYHGDLNALRDDLMELKPTLLAGVPRVFerihegiqKALQELNPRRRLIFNALyKYklawmnrgyshkkaspmadfl 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 312 ---------------IGSGAAPLGKDLmEECGRNIPNVLLMQGYGMTETCGIVSVEDPRlGKRNSGSAGMLAPGVEAQIV 376
Cdd:PLN02430 373 afrkvkaklggrlrlLISGGAPLSTEI-EEFLRVTSCAFVVQGYGLTETLGPTTLGFPD-EMCMLGTVGAPAVYNELRLE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 377 SV-ETGKS---QPPnqQGEIWVRGPNMMKGYLNNPQATKETIdKKSWVHTGDLGYFNEDGNLYVVDRIKELIKY-KGFQV 451
Cdd:PLN02430 451 EVpEMGYDplgEPP--RGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLsQGEYV 527
|
330 340 350
....*....|....*....|....*....|....*...
gi 15234634 452 APAELEGLLVSHP---DI----------LDAVVIPFPD 476
Cdd:PLN02430 528 ALEYLENVYGQNPiveDIwvygdsfksmLVAVVVPNEE 565
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
41-536 |
1.10e-26 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 113.16 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 41 PSKLAIadSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSK 120
Cdd:cd12116 1 PDATAV--RDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 121 QIKDSNPKIIISVNQLFDKIKGfDLPVVLLGSKDTVEIPPgsnskilsfdnvmELSEPVSEypfveikqSDTAALLYSSG 200
Cdd:cd12116 79 ILEDAEPALVLTDDALPDRLPA-GLPVLLLALAAAAAAPA-------------APRTPVSP--------DDLAYVIYTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 201 TTGTSKGVELTHGNFiaASLMVTMDQDL-MGeyhgvflcflPMFHVfgLAVITYS----------QLQRGnALVSMARFE 269
Cdd:cd12116 137 STGRPKGVVVSHRNL--VNFLHSMRERLgLG----------PGDRL--LAVTTYAfdisllelllPLLAG-ARVVIAPRE 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 270 L----ELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLkyigSGAAPLGKDLMEEC---GRNIPNVllmqgYGM 342
Cdd:cd12116 202 TqrdpEALARLIEAHSITVMQATPATWRMLLDAGWQGRAGLTAL----CGGEALPPDLAARLlsrVGSLWNL-----YGP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 343 TET-----CGIVSVED--PRLGKRnsgsagmlAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETI- 414
Cdd:cd12116 273 TETtiwstAARVTAAAgpIPIGRP--------LANTQVYVLD-AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFv 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 415 ------DKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVpIAFVV 488
Cdd:cd12116 344 pdpfagPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRL-VAYVV 422
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 15234634 489 RSPNSSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:cd12116 423 LKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
55-466 |
2.82e-26 |
|
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: 111.78 E-value: 2.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 55 LTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIIISVn 134
Cdd:cd05910 3 LSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFIGI- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 135 qlfdkikgfdlpvvllgskdtveippgsnskilsfdnvmelsePVSEYPfveikqsdtAALLYSSGTTGTSKGVELTHGN 214
Cdd:cd05910 82 -------------------------------------------PKADEP---------AAILFTSGSTGTPKGVVYRHGT 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 215 FIAaslMVTMDQDLMGEYHG-VFLCFLPMFHVFGLAVITYSQLQRGNALVSmARFELELVLKNIEKFRVTHLWVVPPVFL 293
Cdd:cd05910 110 FAA---QIDALRQLYGIRPGeVDLATFPLFALFGPALGLTSVIPDMDPTRP-ARADPQKLVGAIRQYGVSIVFGSPALLE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 294 ALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECGRNI-PNVLLMQGYGMTETCGIVSVEDPRL----GKRNSGSAGMLA 368
Cdd:cd05910 186 RVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLsDEAEILTPYGATEALPVSSIGSRELlattTAATSGGAGTCV 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 369 ----PGVEAQIVSVETG--------KSQPPNQQGEIWVRGPNMMKGYLNNPQATK----ETIDKKSWVHTGDLGYFNEDG 432
Cdd:cd05910 266 grpiPGVRVRIIEIDDEpiaewddtLELPRGEIGEITVTGPTVTPTYVNRPVATAlakiDDNSEGFWHRMGDLGYLDDEG 345
|
410 420 430
....*....|....*....|....*....|....
gi 15234634 433 NLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDI 466
Cdd:cd05910 346 RLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGV 379
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
55-536 |
1.71e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 111.79 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 55 LTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIIISVN 134
Cdd:PRK12467 1600 LTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQS 1679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 135 QLFDkikgfdlpvvllgskdtvEIPPGSNSKILSFDNVMELSEPVSEY-PFVEIKQSDTAALLYSSGTTGTSKGVELTHG 213
Cdd:PRK12467 1680 HLQA------------------RLPLPDGLRSLVLDQEDDWLEGYSDSnPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHG 1741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 214 NFIAASlmvtmdqDLMGEYHG-----VFLCFLPM---FHVFGLavitYSQLQRGNALVsMARFEL----ELVLKNIEKFR 281
Cdd:PRK12467 1742 ALVNRL-------CATQEAYQlsaadVVLQFTSFafdVSVWEL----FWPLINGARLV-IAPPGAhrdpEQLIQLIERQQ 1809
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 282 VTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAApLGKDLMEECGRNIPNVLLMQGYGMTETCGIVSVEDPRLGK--- 358
Cdd:PRK12467 1810 VTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEA-LEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCRRKDleg 1888
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 359 RNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKE--------TIDKKSWvHTGDLGYFNE 430
Cdd:PRK12467 1889 RDSVPIGQPIANLSTYILD-ASLNPVPIGVAGELYLGGVGLARGYLNRPALTAErfvadpfgTVGSRLY-RTGDLARYRA 1966
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 431 DGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPfPDEEAGEVPIAFVVrsPN-SSITEQDIqkfiaKQVA 509
Cdd:PRK12467 1967 DGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIA-QDGANGKQLVAYVV--PTdPGLVDDDE-----AQVA 2038
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 15234634 510 PYKRLRR--------------VSFISLVPKSAAGKILRREL 536
Cdd:PRK12467 2039 LRAILKNhlkaslpeymvpahLVFLARMPLTPNGKLDRKAL 2079
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
53-536 |
2.39e-25 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 110.37 E-value: 2.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 53 DSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIIIS 132
Cdd:PLN02654 119 ASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVIT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 133 VNQLFDKIKGFDLpvvllgsKDTVEIPPGSNSK-------ILSFDNVMELS---------------EPVSEYPF---VE- 186
Cdd:PLN02654 199 CNAVKRGPKTINL-------KDIVDAALDESAKngvsvgiCLTYENQLAMKredtkwqegrdvwwqDVVPNYPTkceVEw 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 187 IKQSDTAALLYSSGTTGTSKGVELTHGNFI---AASLMVTMDqdlmgeYH--GVFLCFLPMFHVFGLAVITYSQLQRGNA 261
Cdd:PLN02654 272 VDAEDPLFLLYTSGSTGKPKGVLHTTGGYMvytATTFKYAFD------YKptDVYWCTADCGWITGHSYVTYGPMLNGAT 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 262 LVSmarFE-----------LELVlkniEKFRVTHLWVVPPVFLALSKQ--SIVKKFDLSSLKYIGSgaapLGKDLMEECG 328
Cdd:PLN02654 346 VLV---FEgapnypdsgrcWDIV----DKYKVTIFYTAPTLVRSLMRDgdEYVTRHSRKSLRVLGS----VGEPINPSAW 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 329 RNIPNVL------LMQGYGMTETCGIVSVEDPRLGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRG--PNMM 400
Cdd:PLN02654 415 RWFFNVVgdsrcpISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVD-EKGKEIEGECSGYLCVKKswPGAF 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 401 KGYLNNPQATKETIDK--KSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEE 478
Cdd:PLN02654 494 RTLYGDHERYETTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEV 573
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15234634 479 AGEVPIAFVVRSPNSSITEQDIQKFIA---KQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:PLN02654 574 KGQGIYAFVTLVEGVPYSEELRKSLILtvrNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
41-536 |
2.42e-25 |
|
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: 108.99 E-value: 2.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 41 PSKLAIADSDtgDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSK 120
Cdd:cd17649 1 PDAVALVFGD--QSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 121 QIKDSNPKIIISvnqlfdkikgfdlpvvllgskdtveippgsnskilsfdnvmelsepvseypfveiKQSDTAA-LLYSS 199
Cdd:cd17649 79 MLEDSGAGLLLT-------------------------------------------------------HHPRQLAyVIYTS 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 200 GTTGTSKGVELTHGNfIAASLMVTMDQDLMGEyHGVFLCFLPM-FHVF----------GLAVITysqlqRGNALVSMARF 268
Cdd:cd17649 104 GSTGTPKGVAVSHGP-LAAHCQATAERYGLTP-GDRELQFASFnFDGAheqllpplicGACVVL-----RPDELWASADE 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 269 ELELvlknIEKFRVTHLwVVPPVFLALSKQSIVKKFDLS--SLKYIGSGAAPLGKDLMEECGRNipNVLLMQGYGMTETC 346
Cdd:cd17649 177 LAEM----VRELGVTVL-DLPPAYLQQLAEEADRTGDGRppSLRLYIFGGEALSPELLRRWLKA--PVRLFNAYGPTEAT 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 347 GIVSVEDPRLGKRNSGSA---GMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETI--DKKS--- 418
Cdd:cd17649 250 VTPLVWKCEAGAARAGASmpiGRPLGGRSAYILD-ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFvpDPFGapg 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 419 --WVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDeEAGEVPIAFVVRSPNSSIT 496
Cdd:cd17649 329 srLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDG-AGGKQLVAYVVLRAAAAQP 407
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 15234634 497 E--QDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:cd17649 408 ElrAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKAL 449
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
33-510 |
2.49e-25 |
|
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: 110.05 E-value: 2.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 33 LFRNSSSyPSKLAIADSDTG--DSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTAN 110
Cdd:cd05943 76 LLRHADA-DDPAAIYAAEDGerTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCS 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 111 PLYTVNEVS---KQIKdsnPKIIISVNQLFDKIKGFD-LPVV------LLGSKDTVEIP---PGSNSKILSFDNVMELSE 177
Cdd:cd05943 155 PDFGVPGVLdrfGQIE---PKVLFAVDAYTYNGKRHDvREKVaelvkgLPSLLAVVVVPytvAAGQPDLSKIAKALTLED 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 178 PVSEYP-----FVEIKQSDTAALLYSSGTTGTSKGVELTHGnfiaASLMVTMDQ-----DLmgEYHGVFLCFLP----MF 243
Cdd:cd05943 232 FLATGAageleFEPLPFDHPLYILYSSGTTGLPKCIVHGAG----GTLLQHLKEhilhcDL--RPGDRLFYYTTcgwmMW 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 244 H--VFGLAVitysqlqrGNALV----SMARFELELVLKNIEKFRVTHLWVVPPVFLALSKQSIV--KKFDLSSLKYIGSG 315
Cdd:cd05943 306 NwlVSGLAV--------GATIVlydgSPFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKpaETHDLSSLRTILST 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 316 AAPLGKDLMEECGRNI-PNVLLMQGYGMTETCGIVSVEDPRL----GKRNSGSAGMlapgveAQIVSVETGKSQpPNQQG 390
Cdd:cd05943 378 GSPLKPESFDYVYDHIkPDVLLASISGGTDIISCFVGGNPLLpvyrGEIQCRGLGM------AVEAFDEEGKPV-WGEKG 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 391 EIWVRG--PNMMKGYLNNPQATKEtidKKS--------WVHtGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLL 460
Cdd:cd05943 451 ELVCTKpfPSMPVGFWNDPDGSRY---RAAyfakypgvWAH-GDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVV 526
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 15234634 461 VSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITE---QDIQKFIAKQVAP 510
Cdd:cd05943 527 EKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDelrKRIRSTIRSALSP 579
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
27-533 |
3.98e-25 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 110.64 E-value: 3.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 27 TSLVSFLFRNSSSYPSKLAI----ADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFaPNSYQFPLCFLAVTAI 102
Cdd:PRK05691 9 LTLVQALQRRAAQTPDRLALrflaDDPGEGVVLSYRDLDLRARTIAAALQARASFGDRAVLLF-PSGPDYVAAFFGCLYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 103 GGVFTTANPLYTVNEVSKQ-----IKDSNPKIIISVNQLFDKIKGFDlpvvllgskdtvEIPPGSNSKILSFDNVmeLSE 177
Cdd:PRK05691 88 GVIAVPAYPPESARRHHQErllsiIADAEPRLLLTVADLRDSLLQME------------ELAAANAPELLCVDTL--DPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 178 PVSEYPFVEIKQSDTAALLYSSGTTGTSKGVELTHGNFIAASLMVTMDQDLMGEYHGVFLCFLPMFHVFGLAVITYSQLQ 257
Cdd:PRK05691 154 LAEAWQEPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPDDVIVSWLPLYHDMGLIGGLLQPIF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 258 RGNALVSMA-RFELELVLKNIEK---------------FRVTHLWVvppvflalsKQSIVKKFDLSSLKYIGSGAAPLGK 321
Cdd:PRK05691 234 SGVPCVLMSpAYFLERPLRWLEAiseyggtisggpdfaYRLCSERV---------SESALERLDLSRWRVAYSGSEPIRQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 322 DLMEE-------CGRNIPNvlLMQGYGMTETC----------GIVSVE-DPRLGKRNSG---------SAGMLAPGVEAQ 374
Cdd:PRK05691 305 DSLERfaekfaaCGFDPDS--FFASYGLAEATlfvsggrrgqGIPALElDAEALARNRAepgtgsvlmSCGRSQPGHAVL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 375 IVSVETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETI---DKKSWVHTGDLGyFNEDGNLYVVDRIKELIKYKGFQV 451
Cdd:PRK05691 383 IVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFvehDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 452 APAELEGLLVSHPDIL-DAVVIPFPDEEAGEVPI---AFVVRSPNSSITEQDIQKFIAKQVAPYKRLRRVSFISL----V 523
Cdd:PRK05691 462 YPQDIEKTVEREVEVVrKGRVAAFAVNHQGEEGIgiaAEISRSVQKILPPQALIKSIRQAVAEACQEAPSVVLLLnpgaL 541
|
570
....*....|
gi 15234634 524 PKSAAGKILR 533
Cdd:PRK05691 542 PKTSSGKLQR 551
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
53-543 |
6.62e-25 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 108.97 E-value: 6.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 53 DSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIIIS 132
Cdd:PRK06060 29 DVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 133 VNQLFDKIKGfdlpvvllgskdtveippgsnskilsfDNVMELSEPVSEYPFV-----EIKQSDTAAL-LYSSGTTGTSK 206
Cdd:PRK06060 109 SDALRDRFQP---------------------------SRVAEAAELMSEAARVapggyEPMGGDALAYaTYTSGTTGPPK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 207 GVELTHGN---FIAA----SLMVTmDQDlmgeyhgVFLCFLPMFHVFGLAVITYSQLQRG-NALVSMARFELELVLKNIE 278
Cdd:PRK06060 162 AAIHRHADpltFVDAmcrkALRLT-PED-------TGLCSARMYFAYGLGNSVWFPLATGgSAVINSAPVTPEAAAILSA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 279 KFRVTHLWVVPPVFLALSKQSIVKKFdlSSLKYIGSGAAPLGKDLMEECGRNIPNVLLMQGYGMTE---TCGIVSVEDPR 355
Cdd:PRK06060 234 RFGPSVLYGVPNFFARVIDSCSPDSF--RSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEvgqTFVSNRVDEWR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 356 LGkrnsgSAGMLAPGVEAQIVSVEtGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDkksWVHTGDLGYFNEDGNLY 435
Cdd:PRK06060 312 LG-----TLGRVLPPYEIRVVAPD-GTTAGPGVEGDLWVRGPAIAKGYWNRPDSPVANEG---WLDTRDRVCIDSDGWVT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 436 VVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITE---QDIQKFIAKQVAPYK 512
Cdd:PRK06060 383 YRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGsvmRDLHRGLLNRLSAFK 462
|
490 500 510
....*....|....*....|....*....|.
gi 15234634 513 RLRRVSFISLVPKSAAGKILRRELVQQVRSK 543
Cdd:PRK06060 463 VPHRFAVVDRLPRTPNGKLVRGALRKQSPTK 493
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
10-480 |
1.53e-24 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 107.65 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 10 GIYRSLRPTLVLPKDPNTSLVSFLFRNSSSYPSKLAIADSDTgdSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNS 89
Cdd:PRK08279 20 GILRGLKRTALITPDSKRSLGDVFEEAAARHPDRPALLFEDQ--SISYAELNARANRYAHWAAARGVGKGDVVALLMENR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 90 YQFPLCFLAVTAIGGVftTAnpLYTVNEVSK----QIKDSNPKIII---SVNQLFDKIKGFDL--PVVLLGSKDTVEIPP 160
Cdd:PRK08279 98 PEYLAAWLGLAKLGAV--VA--LLNTQQRGAvlahSLNLVDAKHLIvgeELVEAFEEARADLArpPRLWVAGGDTLDDPE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 161 GsnskilsFDNVMELSEPVSEYPFVEIKQS---DTAALLYSSGTTGTSKGVELTHGNFIAA----SLMVTMDQDlmgeyh 233
Cdd:PRK08279 174 G-------YEDLAAAAAGAPTTNPASRSGVtakDTAFYIYTSGTTGLPKAAVMSHMRWLKAmggfGGLLRLTPD------ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 234 GVFLCFLPMFHVFGLAVITysqlqrGNALVSMARfeleLVLKniEKFRVTHLWvvppvflalskqSIVKKFDLSSLKYIG 313
Cdd:PRK08279 241 DVLYCCLPLYHNTGGTVAW------SSVLAAGAT----LALR--RKFSASRFW------------DDVRRYRATAFQYIG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 314 --------SGAAPLGKD----LMeeCGRN--------------IPNVLlmQGYGMTE-------------TCGIVsvedP 354
Cdd:PRK08279 297 elcryllnQPPKPTDRDhrlrLM--IGNGlrpdiwdefqqrfgIPRIL--EFYAASEgnvgfinvfnfdgTVGRV----P 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 355 RLGKRNsgsagmlapgveAQIVSVETGKSQP------------PNQQGE----IWVRGPnmMKGYlNNPQATKETI--D- 415
Cdd:PRK08279 369 LWLAHP------------YAIVKYDVDTGEPvrdadgrcikvkPGEVGLligrITDRGP--FDGY-TDPEASEKKIlrDv 433
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15234634 416 -KK--SWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVV----IPFPDEEAG 480
Cdd:PRK08279 434 fKKgdAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVygveVPGTDGRAG 505
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
41-531 |
1.88e-24 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 108.13 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 41 PSKLAIADSDTGdSLTFSQL--KSAV--ARLAHGFHrlgirKNDVVLIFAPNSYQFPLCFLAVTAIGGV-----FTTAnp 111
Cdd:PRK06814 646 FKKLAVEDPVNG-PLTYRKLltGAFVlgRKLKKNTP-----PGENVGVMLPNANGAAVTFFALQSAGRVpaminFSAG-- 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 112 lyTVNeVSKQIKDSNPKIIISVNQLFDKIK--------GFDLPVVLLgskDTVEIPPGSNSKILSFdnvMELSEPvsEYP 183
Cdd:PRK06814 718 --IAN-ILSACKAAQVKTVLTSRAFIEKARlgpliealEFGIRIIYL---EDVRAQIGLADKIKGL---LAGRFP--LVY 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 184 FVEIKQSDTAALLYSSGTTGTSKGVELTHGNFIAASLMVTMDQDLMGEyHGVFLCfLPMFHVFGLAVitysqlqrgnalv 263
Cdd:PRK06814 787 FCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPE-DKVFNA-LPVFHSFGLTG------------- 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 264 smarfelELVLKNIEKFRV------THLWVVPPV--------------FLALSKQSiVKKFDLSSLKYIGSGAAPLgKD- 322
Cdd:PRK06814 852 -------GLVLPLLSGVKVflypspLHYRIIPELiydtnatilfgtdtFLNGYARY-AHPYDFRSLRYVFAGAEKV-KEe 922
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 323 ----LMEECGRNIpnvllMQGYGMTETCGIVSVEDPRLGKrnSGSAGMLAPGVEAQIVSVETgksqpPNQQGEIWVRGPN 398
Cdd:PRK06814 923 trqtWMEKFGIRI-----LEGYGVTETAPVIALNTPMHNK--AGTVGRLLPGIEYRLEPVPG-----IDEGGRLFVRGPN 990
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 399 MMKGYL--NNPQATKETIDkkSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVS-HPDILDAVViPFP 475
Cdd:PRK06814 991 VMLGYLraENPGVLEPPAD--GWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAElWPDALHAAV-SIP 1067
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15234634 476 DEEAGEVPIAFVVRspnSSITEQDIQKFIAKQVAPYKRL-RRVSFISLVPKSAAGKI 531
Cdd:PRK06814 1068 DARKGERIILLTTA---SDATRAAFLAHAKAAGASELMVpAEIITIDEIPLLGTGKI 1121
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
53-487 |
3.96e-24 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 106.24 E-value: 3.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 53 DSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVfTTANPLYT--------VNEVSKQIKD 124
Cdd:PRK09192 48 EALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLV-PVPLPLPMgfggresyIAQLRGMLAS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 125 SNPKIIISVnqlfDKIKGFdlpvvllgskdTVEIPPGSNSK-ILSFDNVMELSEPVSEYPfvEIKQSDTAALLYSSGTTG 203
Cdd:PRK09192 127 AQPAAIITP----DELLPW-----------VNEATHGNPLLhVLSHAWFKALPEADVALP--RPTPDDIAYLQYSSGSTR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 204 TSKGVELTHGnfiaaSLMVtmdqDLMG-EYHGVFL-----CF--LPMFHVFGL-----AVITySQLQrgnalVSM----- 265
Cdd:PRK09192 190 FPRGVIITHR-----ALMA----NLRAiSHDGLKVrpgdrCVswLPFYHDMGLvgfllTPVA-TQLS-----VDYlptrd 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 266 -ARFELeLVLKNIEKFRVThLWVVPPVFLAL-----SKQSIVKkFDLSSLKYIGSGAAPLGKDLME---EC--GRNIPNV 334
Cdd:PRK09192 255 fARRPL-QWLDLISRNRGT-ISYSPPFGYELcarrvNSKDLAE-LDLSCWRVAGIGADMIRPDVLHqfaEAfaPAGFDDK 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 335 LLMQGYGMTET----------CGIVS--VEDPRLGKR-----------------NSGSAgmlAPGVEAQIVSvETGKSQP 385
Cdd:PRK09192 332 AFMPSYGLAEAtlavsfsplgSGIVVeeVDRDRLEYQgkavapgaetrrvrtfvNCGKA---LPGHEIEIRN-EAGMPLP 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 386 PNQQGEIWVRGPNMMKGYLNNPQATKeTIDKKSWVHTGDLGYFnEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPD 465
Cdd:PRK09192 408 ERVVGHICVRGPSLMSGYFRDEESQD-VLAADGWLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPE 485
|
490 500
....*....|....*....|...
gi 15234634 466 ILDAVVIPFP-DEEAGEVPIAFV 487
Cdd:PRK09192 486 LRSGDAAAFSiAQENGEKIVLLV 508
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
190-539 |
4.34e-24 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 103.59 E-value: 4.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 190 SDTAALLYSSGTTGTSKGVELTHGNFIAaSLMVTMDQdLMGEyhGVFLCFLPMFHVFGLAVITYSqLQRGNALVSM---A 266
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTA-SADATHDR-LGGP--GQWLLALPAHHIAGLQVLVRS-VIAGSEPVELdvsA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 267 RFElelvlknIEKF-RVTHLWVVPPVFLALSKQSIVKKFD-------LSSLKYIGSGAAPLGKDLME---ECGRNIpnvl 335
Cdd:PRK07824 110 GFD-------PTALpRAVAELGGGRRYTSLVPMQLAKALDdpaataaLAELDAVLVGGGPAPAPVLDaaaAAGINV---- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 336 lMQGYGMTETCGiVSVEDprlgkrnsgsaGMLAPGVEAQIVsvetgksqppnqQGEIWVRGPNMMKGYLNNPQatKETID 415
Cdd:PRK07824 179 -VRTYGMSETSG-GCVYD-----------GVPLDGVRVRVE------------DGRIALGGPTLAKGYRNPVD--PDPFA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 416 KKSWVHTGDLGYFNeDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSI 495
Cdd:PRK07824 232 EPGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAP 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 15234634 496 TEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRRELVQQ 539
Cdd:PRK07824 311 TLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRR 354
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
237-538 |
7.95e-24 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 104.31 E-value: 7.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 237 LCFLPMFHVFGLAVITYSQLQRGN-ALVSMARFEL--ELVLKNIEKFrvthLWVVPP---VFLALSKQSivkkfdLSSLK 310
Cdd:PRK07445 164 FCVLPLYHVSGLMQFMRSFLTGGKlVILPYKRLKSgqELPPNPSDFF----LSLVPTqlqRLLQLRPQW------LAQFR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 311 YIGSGAAPLGKDLMEECGR-NIPnvlLMQGYGMTETCGIVSVEDP---RLGKRNSGSagmLAPGVEAQIVsvetgksqpP 386
Cdd:PRK07445 234 TILLGGAPAWPSLLEQARQlQLR---LAPTYGMTETASQIATLKPddfLAGNNSSGQ---VLPHAQITIP---------A 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 387 NQQGEIWVRGPNMMKGYLnnPQatkeTIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDI 466
Cdd:PRK07445 299 NQTGNITIQAQSLALGYY--PQ----ILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLV 372
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15234634 467 LDAVVIPFPDEEAGEVPIAFVVrsPN-SSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRRELVQ 538
Cdd:PRK07445 373 QDVCVLGLPDPHWGEVVTAIYV--PKdPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
41-536 |
3.74e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 104.65 E-value: 3.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 41 PSKLAIADSDTgdSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSK 120
Cdd:PRK12316 525 PEAPALAFGEE--TLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAY 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 121 QIKDSNPKIIISVNQLFDKikgfdLPVvllgskdtveippGSNSKILSFDNV-MELSEPVSEYPFVEIKQSDTAALLYSS 199
Cdd:PRK12316 603 MLEDSGVQLLLSQSHLGRK-----LPL-------------AAGVQVLDLDRPaAWLEGYSEENPGTELNPENLAYVIYTS 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 200 GTTGTSKGVELTHGNFiaASLMVTMDQDLMGEYHGVFLCFLPMfhVFGLAVIT-YSQLQRGNALVSMA---RFELELVLK 275
Cdd:PRK12316 665 GSTGKPKGAGNRHRAL--SNRLCWMQQAYGLGVGDTVLQKTPF--SFDVSVWEfFWPLMSGARLVVAApgdHRDPAKLVE 740
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 276 NIEKFRVTHLWVVPPVFLALSKQSIVKkfDLSSLKYIGSGAAPLGKDLMEECGRNIPNVLLMQGYGMTETCGIVSVEDPR 355
Cdd:PRK12316 741 LINREGVDTLHFVPSMLQAFLQDEDVA--SCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCV 818
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 356 LGKRNSGSAGMLAPGVEAQIVSVEtGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKET------IDKKSWVHTGDLGYFN 429
Cdd:PRK12316 819 EEGGDSVPIGRPIANLACYILDAN-LEPVPVGVLGELYLAGRGLARGYHGRPGLTAERfvpspfVAGERMYRTGDLARYR 897
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 430 EDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPfpdeEAGEVPIAFVVRSPNSSITEQDIQKFIAKQVA 509
Cdd:PRK12316 898 ADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLESEGGDWREALKAHLAASLP 973
|
490 500
....*....|....*....|....*..
gi 15234634 510 PYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:PRK12316 974 EYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
25-457 |
4.51e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 103.27 E-value: 4.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 25 PNTSLVSFLFRNSSSYPSKLA--IADSDTGD-----SLTFSQ----LKSAVARLAHGFHRlgirkNDVVLIFAPNSYQFP 93
Cdd:PRK07769 19 PNTNLVRHVERWAKVRGDKLAyrFLDFSTERdgvarDLTWSQfgarNRAVGARLQQVTKP-----GDRVAILAPQNLDYL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 94 LCFLAVTAIGGVfttANPLYTVNE------VSKQIKDSNPKIII-------SVNQLFDKIKGFDLPVVLlgskdTVEIPP 160
Cdd:PRK07769 94 IAFFGALYAGRI---AVPLFDPAEpghvgrLHAVLDDCTPSAILtttdsaeGVRKFFRARPAKERPRVI-----AVDAVP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 161 gsnskilsfDNVMELSEPVseypfvEIKQSDTAALLYSSGTTGTSKGVELTHGNfiAASLMVTMDQDLMGEYHGVFLCFL 240
Cdd:PRK07769 166 ---------DEVGATWVPP------EANEDTIAYLQYTSGSTRIPAGVQITHLN--LPTNVLQVIDALEGQEGDRGVSWL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 241 PMFHVFGLAVITYSQLQrGNALVSMA---------RFELELVLKNIEKFRVthlWVVPPVF-LALSKQSIVKK-----FD 305
Cdd:PRK07769 229 PFFHDMGLITVLLPALL-GHYITFMSpaafvrrpgRWIRELARKPGGTGGT---FSAAPNFaFEHAAARGLPKdgeppLD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 306 LSSLKYIGSGAAPLGKDLMEECGR-----NIPNVLLMQGYGMTETCGIVSV----EDPRL-----GKRNSG--------- 362
Cdd:PRK07769 305 LSNVKGLLNGSEPVSPASMRKFNEafapyGLPPTAIKPSYGMAEATLFVSTtpmdEEPTViyvdrDELNAGrfvevpada 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 363 -------SAGMLAPGVEAQIVSVETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETI-----------------DKKS 418
Cdd:PRK07769 385 pnavaqvSAGKVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrlseshaegapDDAL 464
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15234634 419 WVHTGDLG-YFneDGNLYVVDRIKELIKYKGFQVAPAELE 457
Cdd:PRK07769 465 WVRTGDYGvYF--DGELYITGRVKDLVIIDGRNHYPQDLE 502
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
41-536 |
8.18e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 103.32 E-value: 8.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 41 PSKLAIAdSDtGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSK 120
Cdd:PRK12467 526 PERPALV-FG-EQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAY 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 121 QIKDSNPKIIISVNQLFDKikgfdLPVvllgskdtveipPGSNSKILSFDNVMELSEPVSEYPFVEIKQSDTAALLYSSG 200
Cdd:PRK12467 604 MLDDSGVRLLLTQSHLLAQ-----LPV------------PAGLRSLCLDEPADLLCGYSGHNPEVALDPDNLAYVIYTSG 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 201 TTGTSKGVELTHGNF------IAASLMVTMDqDLMGEYHGvflcflPMFHVFGLAVitYSQLQRGNALVSMAR---FELE 271
Cdd:PRK12467 667 STGQPKGVAISHGALanyvcvIAERLQLAAD-DSMLMVST------FAFDLGVTEL--FGALASGATLHLLPPdcaRDAE 737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 272 LVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKfdLSSLKYIGSGAAPLGKDLMEECGRNIPNVLLMQGYGMTETCGIVSV 351
Cdd:PRK12467 738 AFAALMADQGVTVLKIVPSHLQALLQASRVAL--PRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVST 815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 352 EDPRLGKRNSGSA--GMLAPGVEAQIVSVETGKSqPPNQQGEIWVRGPNMMKGYLNNPQATKETI-------DKKSWVHT 422
Cdd:PRK12467 816 YELSDEERDFGNVpiGQPLANLGLYILDHYLNPV-PVGVVGELYIGGAGLARGYHRRPALTAERFvpdpfgaDGGRLYRT 894
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 423 GDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPdEEAGEVPIAFVVRSPNSSITEQ---- 498
Cdd:PRK12467 895 GDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQP-GDAGLQLVAYLVPAAVADGAEHqatr 973
|
490 500 510
....*....|....*....|....*....|....*....
gi 15234634 499 -DIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:PRK12467 974 dELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
197-542 |
9.40e-23 |
|
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: 101.41 E-value: 9.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 197 YSSGTTGTSKGVELTHGNFIAASLMVTMDQDLMGEyhGVFLCFLPMFHVFGLAVITYSQLQRG--NALVSMARFELE--L 272
Cdd:cd05908 113 FSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTK--DRILSWMPLTHDMGLIAFHLAPLIAGmnQYLMPTRLFIRRpiL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 273 VLKNIEKFRVTHlwVVPP-----VFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECGRNipnvllMQGYGMTETC- 346
Cdd:cd05908 191 WLKKASEHKATI--VSSPnfgykYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDH------MSKYGLKRNAi 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 347 --------GIVSVEDPRLGK--------RNSGSAGMLAPGVE------AQIVSV-------------ETGKSQPPNQQGE 391
Cdd:cd05908 263 lpvyglaeASVGASLPKAQSpfktitlgRRHVTHGEPEPEVDkkdsecLTFVEVgkpidetdiricdEDNKILPDGYIGH 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 392 IWVRGPNMMKGYLNNPQATKETIDKKSWVHTGDLGyFNEDGNLYVVDRIKELIKYKGFQVAPAELEgllvshpdildAVV 471
Cdd:cd05908 343 IQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIE-----------RIA 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 472 IPFPDEEAGEVPIAFVVrspNSSITEQDIQKFIAK-----QVAPYK-------------RLRRVSFISLVPKSAAGKILR 533
Cdd:cd05908 411 EELEGVELGRVVACGVN---NSNTRNEEIFCFIEHrksedDFYPLGkkikkhlnkrggwQINEVLPIRRIPKTTSGKVKR 487
|
....*....
gi 15234634 534 RELVQQVRS 542
Cdd:cd05908 488 YELAQRYQS 496
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
28-542 |
1.41e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 101.56 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 28 SLVSFLFRNSSSYPSKLAIA----DSDTG---DSLTFSQLKSAVARLAHGFHRLGiRKNDVVLIFAPNSYQFPLCFLAVT 100
Cdd:PRK05850 2 SVPSLLRERASLQPDDAAFTfidyEQDPAgvaETLTWSQLYRRTLNVAEELRRHG-STGDRAVILAPQGLEYIVAFLGAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 101 AIGGVfttANPL----YTVNE--VSKQIKDSNPKIIISVNQLFDKIKgfdlpvvllgskDTVEIPPGSNS-KILSFDnVM 173
Cdd:PRK05850 81 QAGLI---AVPLsvpqGGAHDerVSAVLRDTSPSVVLTTSAVVDDVT------------EYVAPQPGQSApPVIEVD-LL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 174 ELSEPvSEYPFVEIKQSDTAALLYSSGTTGTSKGVELTHGNfiaasLMVTMDQ---DLMGEYHGV------FLCFLPMFH 244
Cdd:PRK05850 145 DLDSP-RGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRN-----VIANFEQlmsDYFGDTGGVpppdttVVSWLPFYH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 245 VFGL-------------AVIT--YSQLQRGnalvsmARFeLELVLKNiekfrvTHLWVVPPVF---LALSKQSI--VKKF 304
Cdd:PRK05850 219 DMGLvlgvcapilggcpAVLTspVAFLQRP------ARW-MQLLASN------PHAFSAAPNFafeLAVRKTSDddMAGL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 305 DLSSLKYIGSGA-----APLgKDLMEECGR-NIPNVLLMQGYGMTEtcGIVSVEDPRLG-----------KRNSGSAGML 367
Cdd:PRK05850 286 DLGGVLGIISGServhpATL-KRFADRFAPfNLRETAIRPSYGLAE--ATVYVATREPGqppesvrfdyeKLSAGHAKRC 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 368 APGVEAQ-------------IVSVETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKET----IDKKS-------WVHTG 423
Cdd:PRK05850 363 ETGGGTPlvsygsprsptvrIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTfgatLVDPSpgtpegpWLRTG 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 424 DLGYFNeDGNLYVVDRIKELIKYKGfqvapaelegllVSH-PDILDAVV----------IPFPDEEAGE-VPIAFVVRSP 491
Cdd:PRK05850 443 DLGFIS-EGELFIVGRIKDLLIVDG------------RNHyPDDIEATIqeitggrvaaISVPDDGTEKlVAIIELKKRG 509
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 15234634 492 NSSITEQDIQKFIAKQV-APYKRLRRVSFISLV-------PKSAAGKILRRELVQQVRS 542
Cdd:PRK05850 510 DSDEEAMDRLRTVKREVtSAISKSHGLSVADLVlvapgsiPITTSGKIRRAACVEQYRQ 568
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
29-541 |
1.67e-22 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 102.55 E-value: 1.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 29 LVSFLFRNSSSYPSKLAIADSdtGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTT 108
Cdd:PRK05691 1133 LPELLNEQARQTPERIALVWD--GGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVP 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 109 ANPLYTVNEVSKQIKDSNPKIIISVNQLFDKIkgfdlpvvllgskdtveiPPGSNSKILSFDNVMELSEPVSEyPFVEIK 188
Cdd:PRK05691 1211 LDPDYPAERLAYMLADSGVELLLTQSHLLERL------------------PQAEGVSAIALDSLHLDSWPSQA-PGLHLH 1271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 189 QSDTAALLYSSGTTGTSKGVELTHG------NFIAASLMVTMDQDLMGEYH-----GVFLCFLPMfhvfglavITysqlq 257
Cdd:PRK05691 1272 GDNLAYVIYTSGSTGQPKGVGNTHAalaerlQWMQATYALDDSDVLMQKAPisfdvSVWECFWPL--------IT----- 1338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 258 rGNALVSMARFE-------LELVlkniEKFRVTHLWVVPPVFLALSKQSIVKkfDLSSLKYIGSGAAPLGKDLMEECGRN 330
Cdd:PRK05691 1339 -GCRLVLAGPGEhrdpqriAELV----QQYGVTTLHFVPPLLQLFIDEPLAA--ACTSLRRLFSGGEALPAELRNRVLQR 1411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 331 IPNVLLMQGYGMTETCGIV-----SVEDprlGKRNSgsAGMLAPGVEAQIVSVETGKSqPPNQQGEIWVRGPNMMKGYLN 405
Cdd:PRK05691 1412 LPQVQLHNRYGPTETAINVthwqcQAED---GERSP--IGRPLGNVLCRVLDAELNLL-PPGVAGELCIGGAGLARGYLG 1485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 406 NPQATKETI-------DKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIpFPDEE 478
Cdd:PRK05691 1486 RPALTAERFvpdplgeDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-VREGA 1564
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15234634 479 AGEVPIAFVVRSPNSSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL---VQQVR 541
Cdd:PRK05691 1565 AGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALpepVWQQR 1630
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
9-428 |
2.11e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 101.28 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 9 DG--IYRSLRPtlvlPKDPNTSLVSFLFRNSSSYPSKLAIADSDTGD----SLTFSQLKSAVARLAHGFHRLGIRKNDVV 82
Cdd:PRK12582 33 DGsiVIKSRHP----LGPYPRSIPHLLAKWAAEAPDRPWLAQREPGHgqwrKVTYGEAKRAVDALAQALLDLGLDPGRPV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 83 LIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVneVS------KQIKDS-NPKIIISVN-QLFDK----IKGFDLPVVLL 150
Cdd:PRK12582 109 MILSGNSIEHALMTLAAMQAGVPAAPVSPAYSL--MShdhaklKHLFDLvKPRVVFAQSgAPFARalaaLDLLDVTVVHV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 151 GskdtveiPPGSNSKILSFDNVmeLSEPVSEypfvEIKQS------DTAA-LLYSSGTTGTSKGVELTHGNFIAASLMvt 223
Cdd:PRK12582 187 T-------GPGEGIASIAFADL--AATPPTA----AVAAAiaaitpDTVAkYLFTSGSTGMPKAVINTQRMMCANIAM-- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 224 MDQ---DLMGEYHGVFLCFLPMFHVFGlavitysqlqrGNALVSMARFE---------------LELVLKNIEKFRVTHL 285
Cdd:PRK12582 252 QEQlrpREPDPPPPVSLDWMPWNHTMG-----------GNANFNGLLWGggtlyiddgkplpgmFEETIRNLREISPTVY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 286 WVVPPVFLALSK-----QSIVKKFdLSSLKYIGSGAAPLGKDLME--------ECGRNIPnvlLMQGYGMTETCGI-VSV 351
Cdd:PRK12582 321 GNVPAGYAMLAEamekdDALRRSF-FKNLRLMAYGGATLSDDLYErmqalavrTTGHRIP---FYTGYGATETAPTtTGT 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15234634 352 E-DPRlgkrNSGSAGMLAPGVEAQIVsvetgksqPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKSWVHTGDLGYF 428
Cdd:PRK12582 397 HwDTE----RVGLIGLPLPGVELKLA--------PVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARF 462
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
45-536 |
4.17e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 101.19 E-value: 4.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 45 AIADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKD 124
Cdd:PRK12316 3073 AVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLED 3152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 125 SNpkiiisvnqlfdkikgfdlpVVLLGSKDTVEIPPGSNSKILSFDNVMElsEPVSEYPFVEIKQSDTAALLYSSGTTGT 204
Cdd:PRK12316 3153 SG--------------------AQLLLSQSHLRLPLAQGVQVLDLDRGDE--NYAEANPAIRTMPENLAYVIYTSGSTGK 3210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 205 SKGVELTHGNFIAASLMVtmdQDLMGEYHGVFLCFLPMFHVFGLAVITYSQLQRGNALVSMARFELELVLKNIEKFRVTH 284
Cdd:PRK12316 3211 PKGVGIRHSALSNHLCWM---QQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEG 3287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 285 LWVVPPVFLALSKQ-SIVKKFDLSSLKYIGSGAAPLGKDLMEECGRNIPnvlLMQGYGMTETCGIVSVEDPRLGKRNSGS 363
Cdd:PRK12316 3288 VDVLHAYPSMLQAFlEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLP---LYNLYGPTEATITVTHWQCVEEGKDAVP 3364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 364 AGMLAPGVEAQIVSVeTGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKSWV------HTGDLGYFNEDGNLYVV 437
Cdd:PRK12316 3365 IGRPIANRACYILDG-SLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVpgerlyRTGDLARYRADGVIEYI 3443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 438 DRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIpfpdEEAGEVPIAFVVRSPNSSITEQDIQKFIAKQVAPYKRLRRV 517
Cdd:PRK12316 3444 GRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHL 3519
|
490
....*....|....*....
gi 15234634 518 SFISLVPKSAAGKILRREL 536
Cdd:PRK12316 3520 LFLERMPLTPNGKLDRKAL 3538
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
195-536 |
4.76e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 98.57 E-value: 4.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 195 LLYSSGTTGTSKGVELTHGNF---IAA--SLMvTMDQDLMGeyhgVFLCflPMFHVFGLAVITYSQLQRGNALVSMARFE 269
Cdd:PRK08308 106 LQYSSGTTGEPKLIRRSWTEIdreIEAynEAL-NCEQDETP----IVAC--PVTHSYGLICGVLAALTRGSKPVIITNKN 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 270 LELVLKNIEKFRVTHLWVVPPVFLALSKQS-IVKKFDlsslKYIGSGA---APLGKDLMEECGRnipnvlLMQGYGMTET 345
Cdd:PRK08308 179 PKFALNILRNTPQHILYAVPLMLHILGRLLpGTFQFH----AVMTSGTplpEAWFYKLRERTTY------MMQQYGCSEA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 346 cGIVSVedprlgkrnsgSAGMLAP---GVEAQIVSVETGKSqpPNQQGEIWVRgpnmmkgylnnpqATKETIdkkswvHT 422
Cdd:PRK08308 249 -GCVSI-----------CPDMKSHldlGNPLPHVSVSAGSD--ENAPEEIVVK-------------MGDKEI------FT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 423 GDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGE-VPIAFVVRSPnssITEQDIQ 501
Cdd:PRK08308 296 KDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGErVKAKVISHEE---IDPVQLR 372
|
330 340 350
....*....|....*....|....*....|....*
gi 15234634 502 KFIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:PRK08308 373 EWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
1-498 |
6.73e-22 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 99.71 E-value: 6.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 1 MEKSGYGRDG------IYRSLRPTLVLPkDPNTSLVSF--LFRNS-SSYPS-----KLAIADSDTGDSL--TFSQLKSAV 64
Cdd:PLN02614 11 VEEGKEGSDGrpsvgpVYRSIFAKDGFP-NPIEGMDSCwdVFRMSvEKYPNnpmlgRREIVDGKPGKYVwqTYQEVYDIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 65 ARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAiGGVFTTanPLYTV---NEVSKQIKDSNPKIII----SVNQLF 137
Cdd:PLN02614 90 IKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNA-HGLYCV--PLYDTlgaGAVEFIISHSEVSIVFveekKISELF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 138 DKIKG---FDLPVVLLG--SKDTVEIPPGSNSKILSFDNVMELSEPvSEYPFVEIKQSDTAALLYSSGTTGTSKGVELTH 212
Cdd:PLN02614 167 KTCPNsteYMKTVVSFGgvSREQKEEAETFGLVIYAWDEFLKLGEG-KQYDLPIKKKSDICTIMYTSGTTGDPKGVMISN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 213 GNFIAaslMVTMDQDLMGEYHG------VFLCFLPMFHVFGlAVITYSQLQRGNAlVSMARFELELVLKNIEKFRVTHLW 286
Cdd:PLN02614 246 ESIVT---LIAGVIRLLKSANAaltvkdVYLSYLPLAHIFD-RVIEECFIQHGAA-IGFWRGDVKLLIEDLGELKPTIFC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 287 VVPPVF--------LALSKQSIVKKFDLSS-------------------------------------LKYIGSGAAPLGK 321
Cdd:PLN02614 321 AVPRVLdrvysglqKKLSDGGFLKKFVFDSafsykfgnmkkgqshveasplcdklvfnkvkqglggnVRIILSGAAPLAS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 322 DLmEECGRNIPNVLLMQGYGMTETCGIVSVEDP-RLGKRnsGSAGMLAPGVEAQIVSVETGK--SQPPNQQGEIWVRGPN 398
Cdd:PLN02614 401 HV-ESFLRVVACCHVLQGYGLTESCAGTFVSLPdELDML--GTVGPPVPNVDIRLESVPEMEydALASTPRGEICIRGKT 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 399 MMKGYLNNPQATKET-IDkkSWVHTGDLGYFNEDGNLYVVDRIKELIKY-KGFQVAPAELEGLLvSHPDILDAVVIPFPD 476
Cdd:PLN02614 478 LFSGYYKREDLTKEVlID--GWLHTGDVGEWQPNGSMKIIDRKKNIFKLsQGEYVAVENIENIY-GEVQAVDSVWVYGNS 554
|
570 580
....*....|....*....|..
gi 15234634 477 EEAGEVPIAfvvrSPNSSITEQ 498
Cdd:PLN02614 555 FESFLVAIA----NPNQQILER 572
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
55-536 |
6.86e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 100.62 E-value: 6.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 55 LTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIIISVN 134
Cdd:PRK12467 3121 LSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQA 3200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 135 QLFDKikgfdLPVVllgskdtveippgSNSKILSFDNVMELSEPvSEYPFVEIKQSDTAALLYSSGTTGTSKGVELTHGN 214
Cdd:PRK12467 3201 HLLEQ-----LPAP-------------AGDTALTLDRLDLNGYS-ENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGA 3261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 215 FiaaslmvTMDQDLMGEYHGV-----FLCFLPMfhVFGLAVI-TYSQLQRGNALVSMA--RFELELVLKNIEKFRVTHLW 286
Cdd:PRK12467 3262 L-------ANHLCWIAEAYELdandrVLLFMSF--SFDGAQErFLWTLICGGCLVVRDndLWDPEELWQAIHAHRISIAC 3332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 287 VVPPVFLALSKQSIVKkfDLSSLKYIGSGAAPLGKDLMEECGRNIPNVLLMQGYGMTETCGIVSVEDPRLGKRNSGSAGM 366
Cdd:PRK12467 3333 FPPAYLQQFAEDAGGA--DCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAVCEAPYAP 3410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 367 LAPGVEAQIVSVETGKSQP-P-NQQGEIWVRGPNMMKGYLNNPQATKETIDKKSWV-------HTGDLGYFNEDGNLYVV 437
Cdd:PRK12467 3411 IGRPVAGRSIYVLDGQLNPvPvGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgsggrlyRTGDLARYRADGVIEYL 3490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 438 DRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFpDEEAGEVPIAFVV-RSPNSSITEQdIQKFIAKQVAPYKRLRR 516
Cdd:PRK12467 3491 GRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVpADPQGDWRET-LRDHLAASLPDYMVPAQ 3568
|
490 500
....*....|....*....|
gi 15234634 517 VSFISLVPKSAAGKILRREL 536
Cdd:PRK12467 3569 LLVLAAMPLGPNGKVDRKAL 3588
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
188-473 |
7.80e-22 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 99.53 E-value: 7.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 188 KQSDTAALLYSSGTTGTSKGVELTHGNFIAASLmvTMDQ-----DLMGEYHGVFLCFLPMFHVFGLAVITYSqLQRGnAL 262
Cdd:PLN02861 218 QKTDICTIMYTSGTTGEPKGVILTNRAIIAEVL--STDHllkvtDRVATEEDSYFSYLPLAHVYDQVIETYC-ISKG-AS 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 263 VSMARFELELVLKNIEKFRVTHLWVVPPVF--------LALSKQSIVKK--FDLS------------------------- 307
Cdd:PLN02861 294 IGFWQGDIRYLMEDVQALKPTIFCGVPRVYdriytgimQKISSGGMLRKklFDFAynyklgnlrkglkqeeasprldrlv 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 308 ----------SLKYIGSGAAPLGKDLmEECGRNIPNVLLMQGYGMTETCG--IVSVED--PRLGkrnsgSAGMLAPGVEA 373
Cdd:PLN02861 374 fdkikeglggRVRLLLSGAAPLPRHV-EEFLRVTSCSVLSQGYGLTESCGgcFTSIANvfSMVG-----TVGVPMTTIEA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 374 QIVSV-ETGKSQPPN-QQGEIWVRGPNMMKGYLNNPQATKETIdKKSWVHTGDLGYFNEDGNLYVVDRIKELIKY-KGFQ 450
Cdd:PLN02861 448 RLESVpEMGYDALSDvPRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLsQGEY 526
|
330 340 350
....*....|....*....|....*....|....*.
gi 15234634 451 VAPAELEGLLVSHPDI-------------LDAVVIP 473
Cdd:PLN02861 527 VAVENLENTYSRCPLIasiwvygnsfesfLVAVVVP 562
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
53-481 |
1.41e-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: 98.30 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 53 DSLTFSQLKSAVARLAHGFH-RLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVfttANPLYT---VNEVSKQIKDSNPK 128
Cdd:cd17632 66 ETITYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAV---SVPLQAgasAAQLAPILAETEPR 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 129 II-ISVNQLFDKIK----GFDLP-VVLLGSKDTVEI-------------PPGSNSKILSFDNVMELSEPVSEYPFVEIKQ 189
Cdd:cd17632 143 LLaVSAEHLDLAVEavleGGTPPrLVVFDHRPEVDAhraalesarerlaAVGIPVTTLTLIAVRGRDLPPAPLFRPEPDD 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 190 SDTAALLYSSGTTGTSKGVELTHGNFIAASLMVTMDQDLMgEYHGVFLCFLPMFHVFGLAVItYSQLQRGNALVSMARFE 269
Cdd:cd17632 223 DPLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIR-PPASITLNFMPMSHIAGRISL-YGTLARGGTAYFAAASD 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 270 LELVLKNIEKFRVTHLWVVPPV-------FLALSKQSIVKKFDLSSL----------KYIG-------SGAAPLGKDL-- 323
Cdd:cd17632 301 MSTLFDDLALVRPTELFLVPRVcdmlfqrYQAELDRRSVAGADAETLaervkaelreRVLGgrllaavCGSAPLSAEMka 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 324 -MEECgrniPNVLLMQGYGMTETcGIVSVeDPRLgKRnsgsagmlAPGVEAQIVSV-ETG--KSQPPNQQGEIWVRGPNM 399
Cdd:cd17632 381 fMESL----LDLDLHDGYGSTEA-GAVIL-DGVI-VR--------PPVLDYKLVDVpELGyfRTDRPHPRGELLVKTDTL 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 400 MKGYLNNPQATKETIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKY-KGFQVAPAELEGLLVSHPDI------------ 466
Cdd:cd17632 446 FPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVrqifvygnsera 525
|
490
....*....|....*.
gi 15234634 467 -LDAVVIPFPDEEAGE 481
Cdd:cd17632 526 yLLAVVVPTQDALAGE 541
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
56-471 |
1.92e-21 |
|
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: 97.89 E-value: 1.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 56 TFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYT--------VNEVSKQIKdsnP 127
Cdd:cd05921 27 TYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSlmsqdlakLKHLFELLK---P 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 128 KIIISVN-----QLFDKIKGFDLPVVLLGSkdtveipPGSNSKILSFDNVMElSEPVSEYP--FVEIKQSDTAALLYSSG 200
Cdd:cd05921 104 GLVFAQDaapfaRALAAIFPLGTPLVVSRN-------AVAGRGAISFAELAA-TPPTAAVDaaFAAVGPDTVAKFLFTSG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 201 TTGTSKGVELTHGNFIAASLMVTMDQDLMGEYHGVFLCFLPMFHVFGLAVITYSQLQRGNALV------SMARFELelVL 274
Cdd:cd05921 176 STGLPKAVINTQRMLCANQAMLEQTYPFFGEEPPVLVDWLPWNHTFGGNHNFNLVLYNGGTLYiddgkpMPGGFEE--TL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 275 KNIEKFRVTHLWVVPPVFLAL-----SKQSIVKKFdLSSLKYIGSGAAPLGKDL--------MEECGRNIPnvlLMQGYG 341
Cdd:cd05921 254 RNLREISPTVYFNVPAGWEMLvaaleKDEALRRRF-FKRLKLMFYAGAGLSQDVwdrlqalaVATVGERIP---MMAGLG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 342 MTETCGIVSVEDPRLGKrnSGSAGMLAPGVEAQIVsvetgksqPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKSWVH 421
Cdd:cd05921 330 ATETAPTATFTHWPTER--SGLIGLPAPGTELKLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYC 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 15234634 422 TGDLGYFNEDGN----LYVVDRIKELIKYKG---FQVAPAELEGLLVSHPDILDAVV 471
Cdd:cd05921 400 LGDAAKLADPDDpakgLVFDGRVAEDFKLASgtwVSVGPLRARAVAACAPLVHDAVV 456
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
18-534 |
2.25e-21 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 97.89 E-value: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 18 TLVLPkdPNTSLVSFLFRNSSSYPSKLAIADSD-TGDS------LTFSQLKSAVARLAHGFHRLgIRKNDVVLIFAPNSY 90
Cdd:PRK12476 27 NIALP--PGTTLISLIERNIANVGDTVAYRYLDhSHSAagcaveLTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 91 QFPLCFLAVTAIGgvfTTANPLYT------VNEVSKQIKDSNPKIII-------SVNQLFDKIKGFDLPVVLLgskdTVE 157
Cdd:PRK12476 104 DYVAGFFAAIKAG---TIAVPLFApelpghAERLDTALRDAEPTVVLtttaaaeAVEGFLRNLPRLRRPRVIA----IDA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 158 IPpgsnskilsfDNVMELSEPVseypfvEIKQSDTAALLYSSGTTGTSKGVELTHGNFIAASLMVTMDQDLMG-EYHGVf 236
Cdd:PRK12476 177 IP----------DSAGESFVPV------ELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLLDrNTHGV- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 237 lCFLPMFHVFGLAVITYSQLQRGNA-LVSMARFelelvlkniekFRVTHLWVVP--------PVFLA-------LSKQSI 300
Cdd:PRK12476 240 -SWLPLYHDMGLSMIGFPAVYGGHStLMSPTAF-----------VRRPQRWIKAlsegsrtgRVVTAapnfayeWAAQRG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 301 VKK----FDLSSLKYIgSGAAPLGKDLMEECGR-----NIPNVLLMQGYGMTETCGIVSVEDPR-------LGKRNSG-- 362
Cdd:PRK12476 308 LPAegddIDLSNVVLI-IGSEPVSIDAVTTFNKafapyGLPRTAFKPSYGIAEATLFVATIAPDaepsvvyLDREQLGag 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 363 ----------------SAGMLAPGVEAQIVSVETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETI------------ 414
Cdd:PRK12476 387 ravrvaadapnavahvSCGQVARSQWAVIVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegs 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 415 ------DKKSWVHTGDLGYFnEDGNLYVVDRIKELIKYKGFQVAPAELEGLLV-SHPDILDAVVIPF--PDEEAGEVPIA 485
Cdd:PRK12476 467 hadgaaDDGTWLRTGDLGVY-LDGELYITGRIADLIVIDGRNHYPQDIEATVAeASPMVRRGYVTAFtvPAEDNERLVIV 545
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 15234634 486 fVVRSPNSSITE-QDIQKFIAKQVAPYKRLrRVSFISLV-----PKSAAGKILRR 534
Cdd:PRK12476 546 -AERAAGTSRADpAPAIDAIRAAVSRRHGL-AVADVRLVpagaiPRTTSGKLARR 598
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
9-428 |
6.14e-21 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 96.49 E-value: 6.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 9 DG--IYRSLRPtlvlPKDPNTSLVSFLFRNSSSYPSKLAIADSDTGD---SLTFSQLKSAVARLAHGFHRLGIRKNDVVL 83
Cdd:PRK08180 23 DGtiYLRSAEP----LGDYPRRLTDRLVHWAQEAPDRVFLAERGADGgwrRLTYAEALERVRAIAQALLDRGLSAERPLM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 84 IFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVneVSKQ-------IKDSNPKIII-SVNQLFDK----IKGFDLPVVLLG 151
Cdd:PRK08180 99 ILSGNSIEHALLALAAMYAGVPYAPVSPAYSL--VSQDfgklrhvLELLTPGLVFaDDGAAFARalaaVVPADVEVVAVR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 152 SkdtveIPPGSnsKILSFDNVMELSEPVS-EYPFVEIKQSDTAALLYSSGTTGTSKGVELTHGNFIAASLMVTMDQDLMG 230
Cdd:PRK08180 177 G-----AVPGR--AATPFAALLATPPTAAvDAAHAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 231 EYHGVFLCFLPMFHVFGlavitysqlqrGNALVSM-----------------ARFELelVLKNIEKFRVTHLWVVPPVFL 293
Cdd:PRK08180 250 EEPPVLVDWLPWNHTFG-----------GNHNLGIvlynggtlyiddgkptpGGFDE--TLRNLREISPTVYFNVPKGWE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 294 ALSK-----QSIVKKFdLSSLKYIGSGAAPLGKDL--------MEECGRNIPnvlLMQGYGMTETCG-IVSVEDPRLGkr 359
Cdd:PRK08180 317 MLVPalerdAALRRRF-FSRLKLLFYAGAALSQDVwdrldrvaEATCGERIR---MMTGLGMTETAPsATFTTGPLSR-- 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15234634 360 nSGSAGMLAPGVEAQIVSVEtGKSqppnqqgEIWVRGPNMMKGYLNNPQATKETIDKKSWVHTGDLGYF 428
Cdd:PRK08180 391 -AGNIGLPAPGCEVKLVPVG-GKL-------EVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRF 450
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
45-536 |
7.03e-21 |
|
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: 95.58 E-value: 7.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 45 AIADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKD 124
Cdd:cd17644 16 AVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYILED 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 125 SNPKIIISvnqlfdkikgfdlpvvllgskdtveippgsnskilsfdnvmelsepvseypfveiKQSDTAALLYSSGTTGT 204
Cdd:cd17644 96 AQISVLLT-------------------------------------------------------QPENLAYVIYTSGSTGK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 205 SKGVELTHGNFIAASLMVTMDQDLMGEYH-GVFLCFlpmfhVFGLAVIT-YSQLQRGNALV---SMARFELELVLKNIEK 279
Cdd:cd17644 121 PKGVMIEHQSLVNLSHGLIKEYGITSSDRvLQFASI-----AFDVAAEEiYVTLLSGATLVlrpEEMRSSLEDFVQYIQQ 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 280 FRVThLWVVPPVFL-----ALSKQSIVKkfdLSSLKYIGSGAAPLGKDLMEECGRNI-PNVLLMQGYGMTE---TCGIVS 350
Cdd:cd17644 196 WQLT-VLSLPPAYWhllvlELLLSTIDL---PSSLRLVIVGGEAVQPELVRQWQKNVgNFIQLINVYGPTEatiAATVCR 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 351 VEDPRLGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKSWVH--------T 422
Cdd:cd17644 272 LTQLTERNITSVPIGRPIANTQVYILD-ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykT 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 423 GDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQK 502
Cdd:cd17644 351 GDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVELRQ 430
|
490 500 510
....*....|....*....|....*....|....
gi 15234634 503 FIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:cd17644 431 FLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
52-524 |
1.48e-20 |
|
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: 94.34 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 52 GDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIII 131
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 132 SvnqlfdkikgfdlpvvllgskdtveippgsnskilsfdnvmelsepvseypfveikqsDTAALLYSSGTTGTSKGVELT 211
Cdd:cd05940 81 V----------------------------------------------------------DAALYIYTSGTTGLPKAAIIS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 212 H-----GNFIAASLMVTMDQDLMgeyhgvFLCfLPMFHVFGLAVITYSQLQRGNALVSMARFELELVLKNIEKFRVThlw 286
Cdd:cd05940 103 HrrawrGGAFFAGSGGALPSDVL------YTC-LPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQAT--- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 287 VVPPV-----FLALSKQSIVKKfDLSSLKYIGSGAAPlgkDLMEECGR--NIPNVLlmQGYGMTE-TCGIVSVEdprlgk 358
Cdd:cd05940 173 IFQYIgelcrYLLNQPPKPTER-KHKVRMIFGNGLRP---DIWEEFKErfGVPRIA--EFYAATEgNSGFINFF------ 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 359 RNSGSAG----MLAPGVEAQIVSV----------------ETGKSQPPNQQGEIWVRGPnmMKGYLNnPQATKETI---- 414
Cdd:cd05940 241 GKPGAIGrnpsLLRKVAPLALVKYdlesgepirdaegrciKVPRGEPGLLISRINPLEP--FDGYTD-PAATEKKIlrdv 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 415 --DKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVV--IPFPDEEaGEVPIAFVVRS 490
Cdd:cd05940 318 fkKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPGTD-GRAGMAAIVLQ 396
|
490 500 510
....*....|....*....|....*....|....
gi 15234634 491 PNSSITEQDIQKFIAKQVAPYKRLRrvsFISLVP 524
Cdd:cd05940 397 PNEEFDLSALAAHLEKNLPGYARPL---FLRLQP 427
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
46-536 |
2.51e-20 |
|
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: 93.77 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 46 IADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDS 125
Cdd:cd17645 15 VAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 126 NPKIIISvnqlfdkikgfdlpvvllgskdtveippgsnskilsfdnvmelsepvseypfveiKQSDTAALLYSSGTTGTS 205
Cdd:cd17645 95 SAKILLT-------------------------------------------------------NPDDLAYVIYTSGSTGLP 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 206 KGVELTHGNFI-------AASLMVTMDQDLMgeYHGVflcflpMFHVFGLAVITYsqLQRGNAL---VSMARFELELVLK 275
Cdd:cd17645 120 KGVMIEHHNLVnlcewhrPYFGVTPADKSLV--YASF------SFDASAWEIFPH--LTAGAALhvvPSERRLDLDALND 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 276 NIEKFRVTHLWVVPPV---FLALSKQSivkkfdlssLKYIGSGAAPLGKdlMEECGRNIPNvllmqGYGMTEtCGIVSVE 352
Cdd:cd17645 190 YFNQEGITISFLPTGAaeqFMQLDNQS---------LRVLLTGGDKLKK--IERKGYKLVN-----NYGPTE-NTVVATS 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 353 DPRLGKRNSGSAGMLAPGVEAQIVSvETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKSWV------HTGDLG 426
Cdd:cd17645 253 FEIDKPYANIPIGKPIDNTRVYILD-EALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLA 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 427 YFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVrsPNSSITEQDIQKFIAK 506
Cdd:cd17645 332 KFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVT--APEEIPHEELREWLKN 409
|
490 500 510
....*....|....*....|....*....|..
gi 15234634 507 QVAPYkrLRRVSFISL--VPKSAAGKILRREL 536
Cdd:cd17645 410 DLPDY--MIPTYFVHLkaLPLTANGKVDRKAL 439
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
455-530 |
5.73e-20 |
|
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: 84.13 E-value: 5.73e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15234634 455 ELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGK 530
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
188-502 |
3.98e-18 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 87.84 E-value: 3.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 188 KQSDTAAL-LYSSGTTGTSKGVELTHgnfiaASLMVTMDQ-----DLMGEYHgvFLCFLPMFHVFGLAVITYSQLQRGnA 261
Cdd:PRK08043 362 QQPEDAALiLFTSGSEGHPKGVVHSH-----KSLLANVEQiktiaDFTPNDR--FMSALPLFHSFGLTVGLFTPLLTG-A 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 262 LVSMARFELelvlkniekfrvtHLWVVPPV--------------FLAlSKQSIVKKFDLSSLKYIGSGAAPLGKDL---- 323
Cdd:PRK08043 434 EVFLYPSPL-------------HYRIVPELvydrnctvlfgtstFLG-NYARFANPYDFARLRYVVAGAEKLQESTkqlw 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 324 MEECGRNIpnvllMQGYGMTETCGIVSVEDPRLGKRnsGSAGMLAPGVEAQIVSVetgksQPPNQQGEIWVRGPNMMKGY 403
Cdd:PRK08043 500 QDKFGLRI-----LEGYGVTECAPVVSINVPMAAKP--GTVGRILPGMDARLLSV-----PGIEQGGRLQLKGPNIMNGY 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 404 --------LNNPQA-TKETIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGL-LVSHPDILDAVVIP 473
Cdd:PRK08043 568 lrvekpgvLEVPTAeNARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLaLGVSPDKQHATAIK 647
|
330 340
....*....|....*....|....*....
gi 15234634 474 fPDEEAGEvpiAFVVRSPNSSITEQDIQK 502
Cdd:PRK08043 648 -SDASKGE---ALVLFTTDSELTREKLQQ 672
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
183-539 |
2.54e-17 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 84.82 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 183 PFVEIKQSDTAALLYSSGTTGTSKGVELTHGNFIAaSLMVTMDQDLMGEYHGVFLCFLPMFHVFGLAVitysqlqrgnaL 262
Cdd:PRK05851 145 SLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLS-NLRGLNARVGLDAATDVGCSWLPLYHDMGLAF-----------L 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 263 VSMARFELELVLKNIEKFRVTHL-WVVppvFLALSKQSI-----------------VKKFDLSSLKYIGSGAAPLGKDLM 324
Cdd:PRK05851 213 LTAALAGAPLWLAPTTAFSASPFrWLS---WLSDSRATLtaapnfaynligkyarrVSDVDLGALRVALNGGEPVDCDGF 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 325 EECGRNIPNV-----LLMQGYGMTETCGIVSVEDPRLGKR-------NSGSAGMLA------PGVEAQIVSVETGKSQPP 386
Cdd:PRK05851 290 ERFATAMAPFgfdagAAAPSYGLAESTCAVTVPVPGIGLRvdevttdDGSGARRHAvlgnpiPGMEVRISPGDGAAGVAG 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 387 NQQGEIWVRGPNMMKGYLNNPqatkeTIDKKSWVHTGDLGYFNeDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDI 466
Cdd:PRK05851 370 REIGEIEIRGASMMSGYLGQA-----PIDPDDWFPTGDLGYLV-DGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGV 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 467 LDAVVIPFPDEEAGEVP---IAFVVRSPNSSITEQDIQKFIAKQ--VAPYKrlrrVSFIS--LVPKSAAGKiLRRELVQQ 539
Cdd:PRK05851 444 REGAVVAVGTGEGSARPglvIAAEFRGPDEAGARSEVVQRVASEcgVVPSD----VVFVApgSLPRTSSGK-LRRLAVKR 518
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
41-536 |
4.73e-17 |
|
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: 83.60 E-value: 4.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 41 PSKLAIADSDTgdSLTFSQLKSAVARLAHGFHRLG-IRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVS 119
Cdd:cd17648 1 PDRVAVVYGDK--RLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 120 KQIKDSNPKIIISvnqlfdkikgfdlpvvllgskdtveippgsNSKilsfdnvmelsepvseypfveikqsDTAALLYSS 199
Cdd:cd17648 79 FILEDTGARVVIT------------------------------NST-------------------------DLAYAIYTS 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 200 GTTGTSKGVELTHGNfiaaslMVTMDQDLMGEYHG---------VFLCFLPMFHV--FGLAVITysqlqrGNALVSM--- 265
Cdd:cd17648 104 GTTGKPKGVLVEHGS------VVNLRTSLSERYFGrdngdeavlFFSNYVFDFFVeqMTLALLN------GQKLVVPpde 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 266 ARFELELVLKNIEKFRVTHLWVVPpvflalskqSIVKKFDLSSLKYIGSGAApLGKDLMEECGRNIPNV---LLMQGYGM 342
Cdd:cd17648 172 MRFDPDRFYAYINREKVTYLSGTP---------SVLQQYDLARLPHLKRVDA-AGEEFTAPVFEKLRSRfagLIINAYGP 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 343 TETcGIVSVEDPRLG-KRNSGSAGMLAPGVEAQIVSVETgKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETI------- 414
Cdd:cd17648 242 TET-TVTNHKRFFPGdQRFDKSLGRPVRNTKCYVLNDAM-KRVPVGAVGELYLGGDGVARGYLNRPELTAERFlpnpfqt 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 415 --DKKSWVH-----TGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPI--- 484
Cdd:cd17648 320 eqERARGRNarlykTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSRIqky 399
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 15234634 485 --AFVVRSPnSSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:cd17648 400 lvGYYLPEP-GHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
165-445 |
4.01e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 81.69 E-value: 4.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 165 KILSFDNVMElsepvSEYPFVEIKQSD---TAALLYSSGTTGTSKGVELTHGNFIAASLMVTmDQDLMGEYH-GVFLCFL 240
Cdd:PTZ00342 281 SIILFDDMTK-----NKTTNYKIQNEDpdfITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLC-KHSIFKKYNpKTHLSYL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 241 PMFHVFGlAVITYSQLQRGNALVSMARfELELVLKNIEKFRVTHLWVVPPVF-------------LALSKQSIVKK---- 303
Cdd:PTZ00342 355 PISHIYE-RVIAYLSFMLGGTINIWSK-DINYFSKDIYNSKGNILAGVPKVFnriytnimteinnLPPLKRFLVKKilsl 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 304 ----------------FDLSS---------LKYIGSGAAPLGKDLMEECgRNIPNVLLMQGYGMTETCGIVSVEDpRLGK 358
Cdd:PTZ00342 433 rksnnnggfskflegiTHISSkikdkvnpnLEVILNGGGKLSPKIAEEL-SVLLNVNYYQGYGLTETTGPIFVQH-ADDN 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 359 RNSGSAGMLAPGVEAQIVSVETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKSWVHTGDLGYFNEDGNLYVVD 438
Cdd:PTZ00342 511 NTESIGGPISPNTKYKVRTWETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLD 590
|
....*..
gi 15234634 439 RIKELIK 445
Cdd:PTZ00342 591 RSKGLVK 597
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
45-536 |
4.48e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 82.14 E-value: 4.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 45 AIADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKD 124
Cdd:PRK05691 2204 APALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIED 2283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 125 SNPKIIISVNQLFDKikgfdlpvvlLGskdtvEIPPGSNSKILSFDNVMELSEPVSEYPFVEIKQSDtAALLYSSGTTGT 204
Cdd:PRK05691 2284 SGIGLLLSDRALFEA----------LG-----ELPAGVARWCLEDDAAALAAYSDAPLPFLSLPQHQ-AYLIYTSGSTGK 2347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 205 SKGVELTHGNF-------IAASLMVTMDQDLmgeyHgvflcflpmFHVFGLAVITYSQLQrgnALVSMARFEL------- 270
Cdd:PRK05691 2348 PKGVVVSHGEIamhcqavIERFGMRADDCEL----H---------FYSINFDAASERLLV---PLLCGARVVLraqgqwg 2411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 271 -ELVLKNIEKFRVTHLWVVPPVFLALSkQSIVKKFDLSSLKYIGSGAAPLGKDLMEECGRNIPNVLLMQGYGMTETcgiv 349
Cdd:PRK05691 2412 aEEICQLIREQQVSILGFTPSYGSQLA-QWLAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTET---- 2486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 350 sVEDPrlgkrnsgsAGMLAP-GVEAQIVSVETGKS---------------QPPNQQGEIWVRGPNMMKGYLNNPQATKE- 412
Cdd:PRK05691 2487 -VVMP---------LACLAPeQLEEGAASVPIGRVvgarvayildadlalVPQGATGELYVGGAGLAQGYHDRPGLTAEr 2556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 413 ------TIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFpDEEAGEVPIAF 486
Cdd:PRK05691 2557 fvadpfAADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGY 2635
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15234634 487 VVRSPNSSITEQDIQ-----KFIAKQVAP-YKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:PRK05691 2636 LVSAVAGQDDEAQAAlrealKAHLKQQLPdYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
25-536 |
5.21e-16 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 81.63 E-value: 5.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 25 PNTSLVSFLFRNSSSYPSKLAIADSdtGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGG 104
Cdd:PRK10252 456 PETTLSALVAQQAAKTPDAPALADA--RYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGA 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 105 VFTTANPLYTVNEVSKQIKDSNPKIIISVNQLFDKIKgfDLPVVLLGSKDTVEIPPGSNSKILSfdnvmelsepvseypf 184
Cdd:PRK10252 534 AWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFA--DVPDLTSLCYNAPLAPQGAAPLQLS---------------- 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 185 veiKQSDTAALLYSSGTTGTSKGVELTHgNFIAASLMvtmdqdLMGEYHG------------------VFLCFLPMFhVF 246
Cdd:PRK10252 596 ---QPHHTAYIIFTSGSTGRPKGVMVGQ-TAIVNRLL------WMQNHYPltaddvvlqktpcsfdvsVWEFFWPFI-AG 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 247 GLAVITYSQLQRGNAlvSMARFelelvlknIEKFRVTHLWVVPPV---FLA-LSKQSIVKKfdLSSLKYI-GSGAApLGK 321
Cdd:PRK10252 665 AKLVMAEPEAHRDPL--AMQQF--------FAEYGVTTTHFVPSMlaaFVAsLTPEGARQS--CASLRQVfCSGEA-LPA 731
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 322 DLMEECGRNIpNVLLMQGYGMTETCGIVSvedprlGKRNSGSAGMLAPGVEAQI----------VSVETGKSQPPNQQGE 391
Cdd:PRK10252 732 DLCREWQQLT-GAPLHNLYGPTEAAVDVS------WYPAFGEELAAVRGSSVPIgypvwntglrILDARMRPVPPGVAGD 804
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 392 IWVRGPNMMKGYLNNPQATKETIDKKSWV------HTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPD 465
Cdd:PRK10252 805 LYLTGIQLAQGYLGRPDLTASRFIADPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPD 884
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15234634 466 I----LDAVVIPFPDEEAGEVP--IAFVVRSPNSSITEQDIQKFIAKQVAPYkrLRRVSFISL--VPKSAAGKILRREL 536
Cdd:PRK10252 885 VeqavTHACVINQAAATGGDARqlVGYLVSQSGLPLDTSALQAQLRERLPPH--MVPVVLLQLdqLPLSANGKLDRKAL 961
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
33-319 |
9.92e-16 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 80.22 E-value: 9.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 33 LFRNSSsyPSKLAI-ADSDTGD--SLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTA 109
Cdd:PRK03584 92 LLRHRR--DDRPAIiFRGEDGPrrELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSC 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 110 NPLYTVNEVS---KQIKdsnPKIIISVNQLFDKIKGFD-LPVV------LLGSKDTVEIP-------PGSNSKILSFDNV 172
Cdd:PRK03584 170 SPDFGVQGVLdrfGQIE---PKVLIAVDGYRYGGKAFDrRAKVaelraaLPSLEHVVVVPylgpaaaAAALPGALLWEDF 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 173 MELSEPVS-EY---PFveikqSDTAALLYSSGTTGTSK-------GVELTHgnfiAASLMVTMD---QDlmgeyhgVFLC 238
Cdd:PRK03584 247 LAPAEAAElEFepvPF-----DHPLWILYSSGTTGLPKcivhghgGILLEH----LKELGLHCDlgpGD-------RFFW 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 239 FLP----M--FHVFGLAVitysqlqrGNALV----SMARFELELVLKNIEKFRVTHLWVVPPVFLALSKQSIV--KKFDL 306
Cdd:PRK03584 311 YTTcgwmMwnWLVSGLLV--------GATLVlydgSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVpgETHDL 382
|
330
....*....|...
gi 15234634 307 SSLKYIGSGAAPL 319
Cdd:PRK03584 383 SALRTIGSTGSPL 395
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
196-536 |
2.77e-14 |
|
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: 75.20 E-value: 2.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 196 LYSSGTTGTSKGVELTHG----NFIAASLMVTMDQDLmgeyhgvfLCFLPMFHVFGLAVITYS-QLQRGNALVS---MAR 267
Cdd:cd17654 124 IHTSGTTGTPKIVAVPHKcilpNIQHFRSLFNITSED--------ILFLTSPLTFDPSVVEIFlSLSSGATLLIvptSVK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 268 FELELVLKNI-EKFRVTHLWVVPPVFLALSKQSIvKKFDLS---SLKYIGSGAAPLGKDLMEECGRNIPNVL-LMQGYGM 342
Cdd:cd17654 196 VLPSKLADILfKRHRITVLQATPTLFRRFGSQSI-KSTVLSatsSLRVLALGGEPFPSLVILSSWRGKGNRTrIFNIYGI 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 343 TETCGIVSVEdpRLGKRNSGSAGmlapGVEAQIVSVETGKSQPPNQQGEIWVRGPN---MMKGYLNNPQATketidkksW 419
Cdd:cd17654 275 TEVSCWALAY--KVPEEDSPVQL----GSPLLGTVIEVRDQNGSEGTGQVFLGGLNrvcILDDEVTVPKGT--------M 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 420 VHTGDLgYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAgevpIAFVVRSPNSSITEQD 499
Cdd:cd17654 341 RATGDF-VTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQRL----IAFIVGESSSSRIHKE 415
|
330 340 350
....*....|....*....|....*....|....*..
gi 15234634 500 IQKFiakQVAPYKRLRRVSFISLVPKSAAGKILRREL 536
Cdd:cd17654 416 LQLT---LLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
52-539 |
1.07e-13 |
|
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: 73.24 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 52 GDSLTFSQLKSAVARLAHGFH-RLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVftTAnplytvnevskqikdsnpkiI 130
Cdd:cd05937 3 GKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA--PA--------------------F 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 131 ISVNqlfdkikgfdlpvvlLGSKDTVEIPPGSNSKilsfdnvmelsepvseypFVEIKQSDTAALLYSSGTTGTSKGV-- 208
Cdd:cd05937 61 INYN---------------LSGDPLIHCLKLSGSR------------------FVIVDPDDPAILIYTSGTTGLPKAAai 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 209 ----ELTHGNFIAaSLMVTMDQDLMgeyhgvFLCfLPMFHVFGLAVITYSQLQRGNALVSMARFELELVLKNIEKFRVTH 284
Cdd:cd05937 108 swrrTLVTSNLLS-HDLNLKNGDRT------YTC-MPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATI 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 285 LWVVPPV--FLALSKQSIVKKFDLSSLKYiGSGAAPlgkDLMEECGR--NIPNVllMQGYGMTEtcGIVSvedprLGKRN 360
Cdd:cd05937 180 IQYVGELcrYLLSTPPSPYDRDHKVRVAW-GNGLRP---DIWERFRErfNVPEI--GEFYAATE--GVFA-----LTNHN 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 361 SGSAGMLAPG---------VEAQIVSV----ETG-----------KSQPPNQQGEIWVRGPNMMK----GYLNNPQATKE 412
Cdd:cd05937 247 VGDFGAGAIGhhglirrwkFENQVVLVkmdpETDdpirdpktgfcVRAPVGEPGEMLGRVPFKNReafqGYLHNEDATES 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 413 TIDKK------SWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVV--IPFPDEEaGEVPI 484
Cdd:cd05937 327 KLVRDvfrkgdIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygVKVPGHD-GRAGC 405
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15234634 485 AFVVRSPNSsiteQDIQKFIAKQVAPYKRLRRVS-----FISLVPKSAAG---KILRRELVQQ 539
Cdd:cd05937 406 AAITLEESS----AVPTEFTKSLLASLARKNLPSyavplFLRLTEEVATTdnhKQQKGVLRDE 464
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
52-539 |
2.18e-13 |
|
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: 72.46 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 52 GDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIII 131
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 132 svnqlfdkikgFDLPVVLLgsKDTVEIPPgsNSKILSFDNVMelsepvseypfveikqsdtaALLYSSGTTGTSKGVELT 211
Cdd:cd05939 81 -----------FNLLDPLL--TQSSTEPP--SQDDVNFRDKL--------------------FYIYTSGTTGLPKAAVIV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 212 HGN--FIAASLMVTMDqdlMGEYHGVFLCfLPMFHVFGLAVITYSQLQRGNALVSMARFELELVLKNIEKFRVT------ 283
Cdd:cd05939 126 HSRyyRIAAGAYYAFG---MRPEDVVYDC-LPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCTivqyig 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 284 ----HLWVVPP--------VFLALS---KQSIVKKF-DLSSLKYIGS--GAAplgkdlmeECGRNIPNVllmqgYGMTET 345
Cdd:cd05939 202 eicrYLLAQPPseeeqkhnVRLAVGnglRPQIWEQFvRRFGIPQIGEfyGAT--------EGNSSLVNI-----DNHVGA 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 346 CGIVSVEDP-----RLGKRNS-------GSAGML---APGVEAQIVsvetgksqppnqqGEIWVRGP-NMMKGYLNNpQA 409
Cdd:cd05939 269 CGFNSRILPsvypiRLIKVDEdtgelirDSDGLCipcQPGEPGLLV-------------GKIIQNDPlRRFDGYVNE-GA 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 410 TKETIDKKSWVH------TGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVV----IPFPDEEA 479
Cdd:cd05939 335 TNKKIARDVFKKgdsaflSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygveVPGVEGRA 414
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15234634 480 GEVPIAFVVRspnssitEQDIQKF---IAKQVAPYKRLRRVSFISLVPKSAAGKILRRELVQQ 539
Cdd:cd05939 415 GMAAIVDPER-------KVDLDRFsavLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKE 470
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
52-522 |
6.68e-12 |
|
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: 67.70 E-value: 6.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 52 GDSLTFSQLKSAVARLAHGFHR-LGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKII 130
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 131 ISVNQLFDKIKgfdlPVVLLGSKDTVEI---PPGSNSK-ILSFDNVM--ELSEPVSEYPFVEIKQSDTAALLYSSGTTGT 204
Cdd:cd05938 83 VVAPELQEAVE----EVLPALRADGVSVwylSHTSNTEgVISLLDKVdaASDEPVPASLRAHVTIKSPALYIYTSGTTGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 205 SKGVELTHGNFIAASLMvtmdQDLMGEYHG--VFLCfLPMFHVFGLAVITYSQLQRGNALVSMARFELELVLKNIEKFRV 282
Cdd:cd05938 159 PKAARISHLRVLQCSGF----LSLCGVTADdvIYIT-LPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKHNV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 283 T----------HLWVVPPvflalSKQSIVKKFDLSslkyIGSGAAPlgkDLMEECGRNIPNVLLMQGYGMTE-------- 344
Cdd:cd05938 234 TviqyigellrYLCNQPQ-----SPNDRDHKVRLA----IGNGLRA---DVWREFLRRFGPIRIREFYGSTEgnigffny 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 345 --TCGIVSvedprlgkRNSGSAGMLAP------GVE-------AQIVSVETGKSQPPNQQGEIWVRGPnmMKGYLNNPQA 409
Cdd:cd05938 302 tgKIGAVG--------RVSYLYKLLFPfelikfDVEkeepvrdAQGFCIPVAKGEPGLLVAKITQQSP--FLGYAGDKEQ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 410 TKetiDKK---------SWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVV--IPFPDEE 478
Cdd:cd05938 372 TE---KKLlrdvfkkgdVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVygVTVPGHE 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 15234634 479 aGEVPIAFVVRSPNSSITEQDIQKFIAKQVAPYKRLRrvsFISL 522
Cdd:cd05938 449 -GRIGMAAVKLKPGHEFDGKKLYQHVREYLPAYARPR---FLRI 488
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
51-471 |
1.63e-10 |
|
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: 63.52 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 51 TGDSLTFSQLKSAVARLAHGF-HRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLytvnEVSKQIKDSNPKI 129
Cdd:cd05905 11 EATTLTWGKLLSRAEKIAAVLqKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPP----DISQQLGFLLGTC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 130 IISVNQLFDKI-KGFdlPVVLLGSKDTVEIP-----PgsnsKILSFDNVmELSEPVSEYPFVEIK---QSDTAALLYSSG 200
Cdd:cd05905 87 KVRVALTVEAClKGL--PKKLLKSKTAAEIAkkkgwP----KILDFVKI-PKSKRSKLKKWGPHPptrDGDTAYIEYSFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 201 TTGTSKGVELTHGNFIAASLMVTMDQDL---------------MGEYHGVFLCFLPMFHVFglaVITYSQLQRGNALVSM 265
Cdd:cd05905 160 SDGSLSGVAVSHSSLLAHCRALKEACELyesrplvtvldfksgLGLWHGCLLSVYSGHHTI---LIPPELMKTNPLLWLQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 266 ARFELElVLKNIEKFRVTHLWVV-PPVFLALSKQSIVkkfDLSSLK-------------YIGSGAAPLG-KDLMEEC--- 327
Cdd:cd05905 237 TLSQYK-VRDAYVKLRTLHWCLKdLSSTLASLKNRDV---NLSSLRmcmvpcenrprisSCDSFLKLFQtLGLSPRAvst 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 328 ---GRNIPNVLLMQGYGMTETCGIVSVED-----PRLGKRNSGSA------GMLAPGVEAQIVSVETGKSQPPNQQGEIW 393
Cdd:cd05905 313 efgTRVNPFICWQGTSGPEPSRVYLDMRAlrhgvVRLDERDKPNSlplqdsGKVLPGAQVAIVNPETKGLCKDGEIGEIW 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 394 VRGPNMMKGYLNNPQATKET------------IDKKSWVHTGDLGYF----------NEDGNLYVVDRIKELIKYKGFQV 451
Cdd:cd05905 393 VNSPANASGYFLLDGETNDTfkvfpstrlstgITNNSYARTGLLGFLrptkctdlnvEEHDLLFVVGSIDETLEVRGLRH 472
|
490 500
....*....|....*....|.
gi 15234634 452 APAELEG-LLVSHPDILDAVV 471
Cdd:cd05905 473 HPSDIEAtVMRVHPYRGRCAV 493
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
36-212 |
2.65e-07 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 53.54 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 36 NSSSYPSKLAIADSDTGD------SLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTA 109
Cdd:PLN03052 184 KPSKTDDSIAIIWRDEGSddlpvnRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSI 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 110 NPLYTVNEVSKQIKDSNPKIIISvnQLFDKIKGFDLP----VVLLGSKDTVEIPP-GSNSKI------LSFDNVMELSEP 178
Cdd:PLN03052 264 ADSFAPSEIATRLKISKAKAIFT--QDVIVRGGKSIPlysrVVEAKAPKAIVLPAdGKSVRVklregdMSWDDFLARANG 341
|
170 180 190
....*....|....*....|....*....|....*..
gi 15234634 179 VS---EYPFVEIKQSDTAALLYSSGTTGTSKGVELTH 212
Cdd:PLN03052 342 LRrpdEYKAVEQPVEAFTNILFSSGTTGEPKAIPWTQ 378
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
40-497 |
7.52e-07 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 51.75 E-value: 7.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 40 YPSKLAIADSDTGDS-----LTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYT 114
Cdd:cd17647 1 FPERTCVVETPSLNSsktrsFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 115 VnevSKQIkdsnpkIIISVNqlfdKIKGFdlpVVLlgSKDTVEIPPGSNSKiLSFdnvmelsepvseypfveikqsdtaa 194
Cdd:cd17647 81 P---ARQN------IYLGVA----KPRGL---IVI--RAAGVVVGPDSNPT-LSF------------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 195 llySSGTTGTSKGVELTHG------NFIAASLMVTMDQD---LMGEYHGVFL--CFLPMFHVFGLAVITYSQLQRGNALV 263
Cdd:cd17647 117 ---TSGSEGIPKGVLGRHFslayyfPWMAKRFNLSENDKftmLSGIAHDPIQrdMFTPLFLGAQLLVPTQDDIGTPGRLA 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 264 S-MARFelelvlknieKFRVTHLwvVPPVFLALSKQSIVKKFDLSSLKYIGsgaaplgkDLM--EECGRN---IPNVLLM 337
Cdd:cd17647 194 EwMAKY----------GATVTHL--TPAMGQLLTAQATTPFPKLHHAFFVG--------DILtkRDCLRLqtlAENVRIV 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 338 QGYGMTETCGIVSV-------EDPRLGKRNS----GSAGMLapGVEAQIVS-VETGKSQPPNQQGEIWVRGPNMMKGYLN 405
Cdd:cd17647 254 NMYGTTETQRAVSYfevpsrsSDPTFLKNLKdvmpAGRGML--NVQLLVVNrNDRTQICGIGEVGEIYVRAGGLAEGYRG 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 406 NPQATKET------IDKKSWVH----------------------TGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELE 457
Cdd:cd17647 332 LPELNKEKfvnnwfVEPDHWNYldkdnnepwrqfwlgprdrlyrTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEID 411
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15234634 458 GLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITE 497
Cdd:cd17647 412 THISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPDDE 451
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
390-494 |
2.12e-05 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 47.37 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 390 GEIWVRGPNMMKGYLNNPQATKET------IDKKSWVH----------------------TGDLGYFNEDGNLYVVDRIK 441
Cdd:TIGR03443 622 GEIYVRAGGLAEGYLGLPELNAEKfvnnwfVDPSHWIDldkennkperefwlgprdrlyrTGDLGRYLPDGNVECCGRAD 701
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 15234634 442 ELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSS 494
Cdd:TIGR03443 702 DQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVPQDKSD 754
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
390-472 |
2.51e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.39 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234634 390 GEIWVRGPNMMKGYLNNPQATKETIDKKSW-------VHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVS 462
Cdd:PRK05691 4067 GELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHE 4146
|
90
....*....|
gi 15234634 463 HPDILDAVVI 472
Cdd:PRK05691 4147 QAEVREAAVA 4156
|
|
| |
