|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02647 |
PLN02647 |
acyl-CoA thioesterase |
22-453 |
0e+00 |
|
acyl-CoA thioesterase
Pssm-ID: 215349 [Multi-domain] Cd Length: 437 Bit Score: 820.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569481 22 DGFWIPATRSQKMWNSTVPSDENPDQNSIDAGSSMRKPISLWPGMYHSPVTNALWEARRNMFEI---PTGDDASQSKLTA 98
Cdd:PLN02647 1 PEFASNSPRPIPVVSTFASPSLSPGNGSIDAGSSTRKPLSLWPGMYHSPVTNALWEARSSIFERlldPPKDAPPQSELLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569481 99 KSPSRSRTSILYKFSSDFVLREQYRNPWNEIRTGKLVEDLDALAGTISFKHCGG-DSSARSMILVTASVDRIIMKRPIRV 177
Cdd:PLN02647 81 KTPSQSRTSILYKFSSDFILREQYRNPWNEVRIGKLLEDLDALAGTISVKHCSDdDSTTRPLLLVTASVDKIVLKKPIRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569481 178 DTDLSIVGAVTWVGRSSMEMQLQVLQIQ-DTNNSSESVALEANFTFVARDAQTGKSAPINQVVPETEHEKFLWKEAEERN 256
Cdd:PLN02647 161 DVDLKIVGAVTWVGRSSMEIQLEVIQPTkDESNTSDSVALTANFTFVARDSKTGKSAPVNRLSPETEEEKLLFEEAEARN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569481 257 KLRKQKRAQGKEEHEKLkDLERLNELLAEGRVFLDMPALADRNSILIKDTSHENSLICQPQQRNIHGRIFGGFLMRKAFE 336
Cdd:PLN02647 241 KLRKKKRGEQKREFENG-EAERLEALLAEGRVFCDMPALADRNSILIRDTRLENSLICQPQQRNIHGRIFGGFLMRRAFE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569481 337 LAFSNAYTFAGVSPRFLEVDRVDFIKPVDVGNFLRFKSRVLYTEATSSAEPLINIEVVAHVTSPELRSSEVSNRFYFTFS 416
Cdd:PLN02647 320 LAFSTAYAFAGLRPYFLEVDHVDFLRPVDVGDFLRFKSCVLYTELENSEQPLINVEVVAHVTRPELRSSEVSNTFYFTFT 399
|
410 420 430
....*....|....*....|....*....|....*...
gi 42569481 417 VRPE-AMKDGLKIRNVVPATEEEARRVIERMDAERPIS 453
Cdd:PLN02647 400 VRPEaAMKNGFKIRNVVPATEEEARRILERMDAEHLVS 437
|
|
| BFIT_BACH |
cd03442 |
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ... |
110-236 |
6.22e-34 |
|
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, and brown adipose tissues. The archeal and eukaryotic members of this family have two tandem copies of the conserved hot dog fold, while most bacterial members have only one copy.
Pssm-ID: 239526 [Multi-domain] Cd Length: 123 Bit Score: 123.45 E-value: 6.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569481 110 YKFSSDFVLREQYRNPWNEIRTGKLVEDLDALAGTISFKHCGGdssarsmILVTASVDRIIMKRPIRVDTDLSIVGAVTW 189
Cdd:cd03442 6 TELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGG-------RVVTASVDRIDFLKPVRVGDVVELSARVVY 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 42569481 190 VGRSSMEMQLQVLQIqDTNNSSESVALEANFTFVARDAqTGKSAPIN 236
Cdd:cd03442 79 TGRTSMEVGVEVEAE-DPLTGERRLVTSAYFTFVALDE-DGKPRPVP 123
|
|
| YciA |
COG1607 |
Acyl-CoA hydrolase [Lipid transport and metabolism]; |
132-260 |
1.54e-25 |
|
Acyl-CoA hydrolase [Lipid transport and metabolism];
Pssm-ID: 441215 [Multi-domain] Cd Length: 146 Bit Score: 101.41 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569481 132 GKLVEDLDALAGTISFKHCGGdssarsmILVTASVDRIIMKRPIRVDTDLSIVGAVTWVGRSSMEMQLQVLqIQDTNNSS 211
Cdd:COG1607 27 GWLLSWMDEAAAIAAARHARG-------RVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSMEVGVEVW-AEDLRTGE 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 42569481 212 ESVALEANFTFVARDAQtGKSAPINQVVPETEHEKFLWKEAEERNKLRK 260
Cdd:COG1607 99 RRLVTEAYFTFVAVDED-GKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
|
|
| 4HBT |
pfam03061 |
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ... |
138-201 |
9.76e-05 |
|
Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters.
Pssm-ID: 427116 [Multi-domain] Cd Length: 79 Bit Score: 40.70 E-value: 9.76e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42569481 138 LDALAGTISFKHCGGDssarsmILVTASVDRIIMKRPIRVDTDLSIVGAVTWVGRSSMEMQLQV 201
Cdd:pfam03061 13 ADEAAGAAARRLGGSQ------QVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEV 70
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02647 |
PLN02647 |
acyl-CoA thioesterase |
22-453 |
0e+00 |
|
acyl-CoA thioesterase
Pssm-ID: 215349 [Multi-domain] Cd Length: 437 Bit Score: 820.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569481 22 DGFWIPATRSQKMWNSTVPSDENPDQNSIDAGSSMRKPISLWPGMYHSPVTNALWEARRNMFEI---PTGDDASQSKLTA 98
Cdd:PLN02647 1 PEFASNSPRPIPVVSTFASPSLSPGNGSIDAGSSTRKPLSLWPGMYHSPVTNALWEARSSIFERlldPPKDAPPQSELLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569481 99 KSPSRSRTSILYKFSSDFVLREQYRNPWNEIRTGKLVEDLDALAGTISFKHCGG-DSSARSMILVTASVDRIIMKRPIRV 177
Cdd:PLN02647 81 KTPSQSRTSILYKFSSDFILREQYRNPWNEVRIGKLLEDLDALAGTISVKHCSDdDSTTRPLLLVTASVDKIVLKKPIRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569481 178 DTDLSIVGAVTWVGRSSMEMQLQVLQIQ-DTNNSSESVALEANFTFVARDAQTGKSAPINQVVPETEHEKFLWKEAEERN 256
Cdd:PLN02647 161 DVDLKIVGAVTWVGRSSMEIQLEVIQPTkDESNTSDSVALTANFTFVARDSKTGKSAPVNRLSPETEEEKLLFEEAEARN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569481 257 KLRKQKRAQGKEEHEKLkDLERLNELLAEGRVFLDMPALADRNSILIKDTSHENSLICQPQQRNIHGRIFGGFLMRKAFE 336
Cdd:PLN02647 241 KLRKKKRGEQKREFENG-EAERLEALLAEGRVFCDMPALADRNSILIRDTRLENSLICQPQQRNIHGRIFGGFLMRRAFE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569481 337 LAFSNAYTFAGVSPRFLEVDRVDFIKPVDVGNFLRFKSRVLYTEATSSAEPLINIEVVAHVTSPELRSSEVSNRFYFTFS 416
Cdd:PLN02647 320 LAFSTAYAFAGLRPYFLEVDHVDFLRPVDVGDFLRFKSCVLYTELENSEQPLINVEVVAHVTRPELRSSEVSNTFYFTFT 399
|
410 420 430
....*....|....*....|....*....|....*...
gi 42569481 417 VRPE-AMKDGLKIRNVVPATEEEARRVIERMDAERPIS 453
Cdd:PLN02647 400 VRPEaAMKNGFKIRNVVPATEEEARRILERMDAEHLVS 437
|
|
| BFIT_BACH |
cd03442 |
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ... |
110-236 |
6.22e-34 |
|
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, and brown adipose tissues. The archeal and eukaryotic members of this family have two tandem copies of the conserved hot dog fold, while most bacterial members have only one copy.
Pssm-ID: 239526 [Multi-domain] Cd Length: 123 Bit Score: 123.45 E-value: 6.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569481 110 YKFSSDFVLREQYRNPWNEIRTGKLVEDLDALAGTISFKHCGGdssarsmILVTASVDRIIMKRPIRVDTDLSIVGAVTW 189
Cdd:cd03442 6 TELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGG-------RVVTASVDRIDFLKPVRVGDVVELSARVVY 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 42569481 190 VGRSSMEMQLQVLQIqDTNNSSESVALEANFTFVARDAqTGKSAPIN 236
Cdd:cd03442 79 TGRTSMEVGVEVEAE-DPLTGERRLVTSAYFTFVALDE-DGKPRPVP 123
|
|
| BFIT_BACH |
cd03442 |
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ... |
301-423 |
3.87e-33 |
|
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, and brown adipose tissues. The archeal and eukaryotic members of this family have two tandem copies of the conserved hot dog fold, while most bacterial members have only one copy.
Pssm-ID: 239526 [Multi-domain] Cd Length: 123 Bit Score: 121.52 E-value: 3.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569481 301 ILIKDTSHENSLICQPQQRNIHGRIFGGFLMRKAFELAFSNAYTFAGVSPRFLEVDRVDFIKPVDVGNFLRFKSRVLYTE 380
Cdd:cd03442 1 VPMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 42569481 381 ATSsaeplINIEVVAHVTSPELRSSEVSNRFYFTFSVRPEAMK 423
Cdd:cd03442 81 RTS-----MEVGVEVEAEDPLTGERRLVTSAYFTFVALDEDGK 118
|
|
| YciA |
COG1607 |
Acyl-CoA hydrolase [Lipid transport and metabolism]; |
132-260 |
1.54e-25 |
|
Acyl-CoA hydrolase [Lipid transport and metabolism];
Pssm-ID: 441215 [Multi-domain] Cd Length: 146 Bit Score: 101.41 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569481 132 GKLVEDLDALAGTISFKHCGGdssarsmILVTASVDRIIMKRPIRVDTDLSIVGAVTWVGRSSMEMQLQVLqIQDTNNSS 211
Cdd:COG1607 27 GWLLSWMDEAAAIAAARHARG-------RVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSMEVGVEVW-AEDLRTGE 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 42569481 212 ESVALEANFTFVARDAQtGKSAPINQVVPETEHEKFLWKEAEERNKLRK 260
Cdd:COG1607 99 RRLVTEAYFTFVAVDED-GKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
|
|
| YciA |
COG1607 |
Acyl-CoA hydrolase [Lipid transport and metabolism]; |
303-441 |
2.55e-14 |
|
Acyl-CoA hydrolase [Lipid transport and metabolism];
Pssm-ID: 441215 [Multi-domain] Cd Length: 146 Bit Score: 69.82 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569481 303 IKDTSHENSLICQPQQRNIHGRIFGGFLMRKAFELAFSNAYTFAG-----VSprfleVDRVDFIKPVDVGNFLRFKSRVL 377
Cdd:COG1607 2 LPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARgrvvtAS-----VDSVDFLRPVRVGDIVELYARVV 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42569481 378 YTEATSsaeplINIEVVAHVTSPELRSSEVSNRFYFTFsVrpeAMKDGLKIRNV---VPATEEEARR 441
Cdd:COG1607 77 RVGRTS-----MEVGVEVWAEDLRTGERRLVTEAYFTF-V---AVDEDGKPRPVpplIPETEEEKRL 134
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
112-223 |
1.01e-06 |
|
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.
Pssm-ID: 239524 [Multi-domain] Cd Length: 100 Bit Score: 47.08 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569481 112 FSSDFVLREQYRNPWNEIRTGKLVEDLDALAGTISFKHCGgdssaRSMILVTASVDrIIMKRPIRVDTDLSIVGAVTWVG 191
Cdd:cd03440 1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGG-----RGLGAVTLSLD-VRFLRPVRPGDTLTVEAEVVRVG 74
|
90 100 110
....*....|....*....|....*....|..
gi 42569481 192 RSSMEMQLQVLqiqdtnNSSESVALEANFTFV 223
Cdd:cd03440 75 RSSVTVEVEVR------NEDGKLVATATATFV 100
|
|
| FadM |
COG0824 |
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ... |
172-247 |
3.96e-05 |
|
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440586 [Multi-domain] Cd Length: 139 Bit Score: 43.35 E-value: 3.96e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42569481 172 KRPIRVDTDLSIVGAVTWVGRSSMEMQLQVlqiqdTNNSSESVALEANFTFVARDAQTGKSAPInqvvPETEHEKF 247
Cdd:COG0824 67 LRPARYGDELTVETRVVRLGGSSLTFEYEI-----FRADDGELLATGETVLVFVDLETGRPVPL----PDELRAAL 133
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
311-402 |
7.00e-05 |
|
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.
Pssm-ID: 239524 [Multi-domain] Cd Length: 100 Bit Score: 41.69 E-value: 7.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569481 311 SLICQPQQRNIHGRIFGGFLMRKAFELA--FSNAYTFAGVSPRFLEVDrVDFIKPVDVGNFLRFKSRVLYTEATSsaepl 388
Cdd:cd03440 4 RLTVTPEDIDGGGIVHGGLLLALADEAAgaAAARLGGRGLGAVTLSLD-VRFLRPVRPGDTLTVEAEVVRVGRSS----- 77
|
90
....*....|....
gi 42569481 389 INIEVVAHVTSPEL 402
Cdd:cd03440 78 VTVEVEVRNEDGKL 91
|
|
| 4HBT |
pfam03061 |
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ... |
138-201 |
9.76e-05 |
|
Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters.
Pssm-ID: 427116 [Multi-domain] Cd Length: 79 Bit Score: 40.70 E-value: 9.76e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42569481 138 LDALAGTISFKHCGGDssarsmILVTASVDRIIMKRPIRVDTDLSIVGAVTWVGRSSMEMQLQV 201
Cdd:pfam03061 13 ADEAAGAAARRLGGSQ------QVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEV 70
|
|
| PRK10694 |
PRK10694 |
acyl-CoA thioester hydrolase YciA; |
316-399 |
2.89e-03 |
|
acyl-CoA thioester hydrolase YciA;
Pssm-ID: 236736 [Multi-domain] Cd Length: 133 Bit Score: 37.92 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569481 316 PQQRNIHGRIFGGFLMRK--------AFELAFSNAYTfagvsprfLEVDRVDFIKPVDVGNFLRFKSRVLYTEATSSAep 387
Cdd:PRK10694 20 PADTNANGDIFGGWLMSQmdiggailAKEIAHGRVVT--------VRVEGMTFLRPVAVGDVVCCYARCVKTGTTSIS-- 89
|
90
....*....|...
gi 42569481 388 lINIEV-VAHVTS 399
Cdd:PRK10694 90 -INIEVwVKKVAS 101
|
|
| 4HBT |
pfam03061 |
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ... |
322-383 |
3.17e-03 |
|
Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters.
Pssm-ID: 427116 [Multi-domain] Cd Length: 79 Bit Score: 36.46 E-value: 3.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42569481 322 HGRIFGGFLMrKAFELAFSNAYTFAGVSPR--FLEVDRVDFIKPVDVGNFLRFKSRVLYTEATS 383
Cdd:pfam03061 1 GGVVHGGVYL-ALADEAAGAAARRLGGSQQvvVVVELSIDFLRPARLGDRLTVEARVVRLGRTS 63
|
|
| |
