|
Name |
Accession |
Description |
Interval |
E-value |
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
20-285 |
1.90e-104 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 305.26 E-value: 1.90e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 20 NIYRG-ISRNLVGKRVFGGQVLGQALRAASYT--TDRPAHSLHAYFLYGGDINAPIIYEVDRLRDGKSFVSRQVRAIQHG 96
Cdd:COG1946 17 GLFRGeISPDQGLRRVFGGQVAAQALRAARRTvpEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFSTRRVTAIQGG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 97 RVIFSAMVSFANPEEGLNYQHPEPDYPAPEALKSESELKegILNFVPenvRASFMRERHVEIRPIDPVNPFQPQPEAPFN 176
Cdd:COG1946 97 RVIFTATASFGVPEEGLEHQAPMPDVPPPEDLPSLPELL--IAGVLP---LRFFAFLRPFDIRPVEGPLPFAPPSGEPRQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 177 AHYIRTHDRIPkqlDDiSLHQAIVAFYSDFTLMTTALRPHGlsyiSPSLQCASIDHAIYFHRPLRADEWMLYDMEATVST 256
Cdd:COG1946 172 RVWMRARDPLP---DD-PLHAALLAYASDATPPATALLSWL----GPPLPAASLDHAMWFHRPFRADDWLLYDADSPSAS 243
|
250 260 270
....*....|....*....|....*....|
gi 1620984417 257 ASRGLNFGRMW-QNGQLVCSTVQEGLMRLR 285
Cdd:COG1946 244 GGRGLERGRIWdRDGRLVASSRQEGLVRGR 273
|
|
| PRK10526 |
PRK10526 |
acyl-CoA thioesterase II; Provisional |
21-286 |
3.99e-89 |
|
acyl-CoA thioesterase II; Provisional
Pssm-ID: 182519 [Multi-domain] Cd Length: 286 Bit Score: 267.00 E-value: 3.99e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 21 IYRGISRNLVGKRVFGGQVLGQALRAASYTT--DRPAHSLHAYFLYGGDINAPIIYEVDRLRDGKSFVSRQVRAIQHGRV 98
Cdd:PRK10526 21 LFRGQSEDLGLRQVFGGQVVGQALYAAKETVpeERLVHSFHSYFLRPGDSQKPIIYDVETLRDGNSFSARRVAAIQNGKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 99 IFSAMVSFANPEEGLNYQHPEPDYPAPEALKSESELKEGILNFVPENVRASFMRERHVEIRPIDPVNPFQPQPEAPFNAH 178
Cdd:PRK10526 101 IFYMTASFQAPEAGFEHQKTMPSAPAPDGLPSETDIAQSLAHLLPPVLKDKFICDRPLEIRPVEFHNPLKGHVAEPVRQV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 179 YIRTHDRIPkqlDDISLHQAIVAFYSDFTLMTTALRPHGLSYISPSLQCASIDHAIYFHRPLRADEWMLYDMEATVSTAS 258
Cdd:PRK10526 181 WIRANGSVP---DDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGMQIATIDHSMWFHRPFNLNEWLLYSVESTSASSA 257
|
250 260
....*....|....*....|....*....
gi 1620984417 259 RGLNFGRMW-QNGQLVCSTVQEGLMRLRE 286
Cdd:PRK10526 258 RGFVRGEFYtQDGVLVASTVQEGVMRNHN 286
|
|
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
20-283 |
3.70e-85 |
|
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. Physiological function is not known. Subunit: homotetramer. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 272951 [Multi-domain] Cd Length: 271 Bit Score: 256.13 E-value: 3.70e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 20 NIYRGISRNL---VGKRVFGGQVLGQALRAASYT--TDRPAHSLHAYFLYGGDINAPIIYEVDRLRDGKSFVSRQVRAIQ 94
Cdd:TIGR00189 6 NLFRGSHLSKgrqFLNRTFGGQVVGQALAAASKTvpEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRRVKAVQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 95 HGRVIFSAMVSFANPEEGLNYQHPEPDYPAPE-ALKSESELKEGILNFVPENVRASFMRERHVEIRPIDPVNPFQPQpEA 173
Cdd:TIGR00189 86 HGKTIFTLQASFQAEKSGIEHQSTMPKVPPPEsELPRENQLATKYPATLPRFLKHVVPFERPFEIRPVNLLNYLGGK-ED 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 174 PFNAHYIRTHDRIPkqlDDISLHQAIVAFYSDFTLMTTALRPHGLSYISPSlQCASIDHAIYFHRPLRADEWMLYDMEAT 253
Cdd:TIGR00189 165 PPQYVWRRARGSLP---DDPRLHQCALAYLSDLTLLPTALNPHNKAGFCHS-MAASLDHSIWFHRPFRADDWLLYKCSSP 240
|
250 260 270
....*....|....*....|....*....|.
gi 1620984417 254 VSTASRGLNFGRMW-QNGQLVCSTVQEGLMR 283
Cdd:TIGR00189 241 SAGGSRGLVEGKIFtRDGVLIASVVQEGLVR 271
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
31-282 |
1.47e-47 |
|
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally thioesterases. These enzymes are part of the Hotdog fold superfamily.
Pssm-ID: 463937 [Multi-domain] Cd Length: 246 Bit Score: 159.03 E-value: 1.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 31 GKRVFGGQVLGQALRAA-SYTTDRPAHSLHAYFLYGGDInAPIIYEVDRLRDGKSFVSRQVRAIQHGRVIFSAMVSFANP 109
Cdd:pfam13622 8 GRAPHGGYVAALLLRAAeRTVPPDPLHSLHVDFLRPVPP-GPVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 110 EEGLNYQHPE--PDYPAPEALKSESElkegilNFVPENVRASFMRERHVEIRPIDPVNPFQPQPEAPFnAHYIRthDRIP 187
Cdd:pfam13622 87 RSSEWELTPAapPPLPPPEDCPLAAD------EAPFPLFRRVPGFLDPFEPRFARGGGPFSPGGPGRV-RLWVR--LRDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 188 KQLDdislHQAIVAFYSDFTLMttalRPHGLSYISP-SLQCASIDHAIYFHRPLRADEWMLYDMEATVSTASRGLNFGRM 266
Cdd:pfam13622 158 GEPD----PLAALAYLADAFPP----RVLSLRLDPPaSGWFPTLDLTVYFHRRPPPGEWLLLRAETPVAGDGRGDVEARL 229
|
250
....*....|....*..
gi 1620984417 267 W-QNGQLVCSTVQEGLM 282
Cdd:pfam13622 230 WdEDGRLVATSRQEVLV 246
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
176-282 |
1.92e-40 |
|
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases (NRPSs) as well as modular polyketide synthases (PKSs) by hydrolyzing acetyl groups bound to the peptidyl carrier protein (PCP) and acyl carrier protein (ACP) domains, respectively. TEII has two tandem asymmetric hot dog folds that are structurally similar to one found in PaaI thioesterase, 4-hydroxybenzoyl-CoA thioesterase (4HBT) and beta-hydroxydecanoyl-ACP dehydratase and thus, the TEII monomer is equivalent to the homodimeric form of the latter three enzymes. Human TEII is expressed in T cells and has been shown to bind the product of the HIV-1 Nef gene.
Pssm-ID: 239528 [Multi-domain] Cd Length: 104 Bit Score: 136.22 E-value: 1.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 176 NAHYIRTHDRIPkqlDDISLHQAIVAFYSDFTLMTTALRPHGLSyISPSLQCASIDHAIYFHRPLRADEWMLYDMEATVS 255
Cdd:cd03444 1 LRVWVRARGPLP---DDPRLHAAALAYLSDSLLLGTALRPHGLP-LFDASASASLDHAIWFHRPFRADDWLLYEQRSPRA 76
|
90 100
....*....|....*....|....*...
gi 1620984417 256 TASRGLNFGRMW-QNGQLVCSTVQEGLM 282
Cdd:cd03444 77 GNGRGLVEGRIFtRDGELVASVAQEGLL 104
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
20-285 |
1.90e-104 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 305.26 E-value: 1.90e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 20 NIYRG-ISRNLVGKRVFGGQVLGQALRAASYT--TDRPAHSLHAYFLYGGDINAPIIYEVDRLRDGKSFVSRQVRAIQHG 96
Cdd:COG1946 17 GLFRGeISPDQGLRRVFGGQVAAQALRAARRTvpEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFSTRRVTAIQGG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 97 RVIFSAMVSFANPEEGLNYQHPEPDYPAPEALKSESELKegILNFVPenvRASFMRERHVEIRPIDPVNPFQPQPEAPFN 176
Cdd:COG1946 97 RVIFTATASFGVPEEGLEHQAPMPDVPPPEDLPSLPELL--IAGVLP---LRFFAFLRPFDIRPVEGPLPFAPPSGEPRQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 177 AHYIRTHDRIPkqlDDiSLHQAIVAFYSDFTLMTTALRPHGlsyiSPSLQCASIDHAIYFHRPLRADEWMLYDMEATVST 256
Cdd:COG1946 172 RVWMRARDPLP---DD-PLHAALLAYASDATPPATALLSWL----GPPLPAASLDHAMWFHRPFRADDWLLYDADSPSAS 243
|
250 260 270
....*....|....*....|....*....|
gi 1620984417 257 ASRGLNFGRMW-QNGQLVCSTVQEGLMRLR 285
Cdd:COG1946 244 GGRGLERGRIWdRDGRLVASSRQEGLVRGR 273
|
|
| PRK10526 |
PRK10526 |
acyl-CoA thioesterase II; Provisional |
21-286 |
3.99e-89 |
|
acyl-CoA thioesterase II; Provisional
Pssm-ID: 182519 [Multi-domain] Cd Length: 286 Bit Score: 267.00 E-value: 3.99e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 21 IYRGISRNLVGKRVFGGQVLGQALRAASYTT--DRPAHSLHAYFLYGGDINAPIIYEVDRLRDGKSFVSRQVRAIQHGRV 98
Cdd:PRK10526 21 LFRGQSEDLGLRQVFGGQVVGQALYAAKETVpeERLVHSFHSYFLRPGDSQKPIIYDVETLRDGNSFSARRVAAIQNGKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 99 IFSAMVSFANPEEGLNYQHPEPDYPAPEALKSESELKEGILNFVPENVRASFMRERHVEIRPIDPVNPFQPQPEAPFNAH 178
Cdd:PRK10526 101 IFYMTASFQAPEAGFEHQKTMPSAPAPDGLPSETDIAQSLAHLLPPVLKDKFICDRPLEIRPVEFHNPLKGHVAEPVRQV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 179 YIRTHDRIPkqlDDISLHQAIVAFYSDFTLMTTALRPHGLSYISPSLQCASIDHAIYFHRPLRADEWMLYDMEATVSTAS 258
Cdd:PRK10526 181 WIRANGSVP---DDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGMQIATIDHSMWFHRPFNLNEWLLYSVESTSASSA 257
|
250 260
....*....|....*....|....*....
gi 1620984417 259 RGLNFGRMW-QNGQLVCSTVQEGLMRLRE 286
Cdd:PRK10526 258 RGFVRGEFYtQDGVLVASTVQEGVMRNHN 286
|
|
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
20-283 |
3.70e-85 |
|
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. Physiological function is not known. Subunit: homotetramer. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 272951 [Multi-domain] Cd Length: 271 Bit Score: 256.13 E-value: 3.70e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 20 NIYRGISRNL---VGKRVFGGQVLGQALRAASYT--TDRPAHSLHAYFLYGGDINAPIIYEVDRLRDGKSFVSRQVRAIQ 94
Cdd:TIGR00189 6 NLFRGSHLSKgrqFLNRTFGGQVVGQALAAASKTvpEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRRVKAVQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 95 HGRVIFSAMVSFANPEEGLNYQHPEPDYPAPE-ALKSESELKEGILNFVPENVRASFMRERHVEIRPIDPVNPFQPQpEA 173
Cdd:TIGR00189 86 HGKTIFTLQASFQAEKSGIEHQSTMPKVPPPEsELPRENQLATKYPATLPRFLKHVVPFERPFEIRPVNLLNYLGGK-ED 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 174 PFNAHYIRTHDRIPkqlDDISLHQAIVAFYSDFTLMTTALRPHGLSYISPSlQCASIDHAIYFHRPLRADEWMLYDMEAT 253
Cdd:TIGR00189 165 PPQYVWRRARGSLP---DDPRLHQCALAYLSDLTLLPTALNPHNKAGFCHS-MAASLDHSIWFHRPFRADDWLLYKCSSP 240
|
250 260 270
....*....|....*....|....*....|.
gi 1620984417 254 VSTASRGLNFGRMW-QNGQLVCSTVQEGLMR 283
Cdd:TIGR00189 241 SAGGSRGLVEGKIFtRDGVLIASVVQEGLVR 271
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
20-282 |
1.83e-75 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 236.16 E-value: 1.83e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 20 NIYRGISR--NLVGKRVFGGQVLGQALRAASYTTDrPA---HSLHAYFLYGGDINAPIIYEVDRLRDGKSFVSRQVRAIQ 94
Cdd:PLN02868 144 DIFRGITLpdAPTFGKVFGGQLVGQALAAASKTVD-PLklvHSLHAYFLLVGDINLPIIYQVERIRDGHNFATRRVDAIQ 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 95 HGRVIFSAMVSFANPEEGLNYQHPE-PDYPAPEALKSESELKEGILN--FVPENVRASFMRERHV----EIRPIDPVNPF 167
Cdd:PLN02868 223 KGKVIFTLFASFQKEEQGFEHQESTmPHVPPPETLLSREELRERRLTdpRLPRSYRNKVAAKPFVpwpiEIRFCEPNNST 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 168 QPQPEAPFNAHYIRTHDRIPkqlDDISLHQAIVAFYSDFTLMTTALRPHGLSYISPSLqcASIDHAIYFHRPLRADEWML 247
Cdd:PLN02868 303 NQTKSPPRLRYWFRAKGKLS---DDQALHRCVAAYASDLIFLGTSLNPHRTKGLKFAA--LSLDHSMWFHRPFRADDWLL 377
|
250 260 270
....*....|....*....|....*....|....*.
gi 1620984417 248 YDMEATVSTASRGLNFGRMW-QNGQLVCSTVQEGLM 282
Cdd:PLN02868 378 FVIVSPAAHNGRGFATGHMFnRKGELVVSLTQEALL 413
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
31-282 |
1.47e-47 |
|
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally thioesterases. These enzymes are part of the Hotdog fold superfamily.
Pssm-ID: 463937 [Multi-domain] Cd Length: 246 Bit Score: 159.03 E-value: 1.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 31 GKRVFGGQVLGQALRAA-SYTTDRPAHSLHAYFLYGGDInAPIIYEVDRLRDGKSFVSRQVRAIQHGRVIFSAMVSFANP 109
Cdd:pfam13622 8 GRAPHGGYVAALLLRAAeRTVPPDPLHSLHVDFLRPVPP-GPVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 110 EEGLNYQHPE--PDYPAPEALKSESElkegilNFVPENVRASFMRERHVEIRPIDPVNPFQPQPEAPFnAHYIRthDRIP 187
Cdd:pfam13622 87 RSSEWELTPAapPPLPPPEDCPLAAD------EAPFPLFRRVPGFLDPFEPRFARGGGPFSPGGPGRV-RLWVR--LRDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 188 KQLDdislHQAIVAFYSDFTLMttalRPHGLSYISP-SLQCASIDHAIYFHRPLRADEWMLYDMEATVSTASRGLNFGRM 266
Cdd:pfam13622 158 GEPD----PLAALAYLADAFPP----RVLSLRLDPPaSGWFPTLDLTVYFHRRPPPGEWLLLRAETPVAGDGRGDVEARL 229
|
250
....*....|....*..
gi 1620984417 267 W-QNGQLVCSTVQEGLM 282
Cdd:pfam13622 230 WdEDGRLVATSRQEVLV 246
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
176-282 |
1.92e-40 |
|
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases (NRPSs) as well as modular polyketide synthases (PKSs) by hydrolyzing acetyl groups bound to the peptidyl carrier protein (PCP) and acyl carrier protein (ACP) domains, respectively. TEII has two tandem asymmetric hot dog folds that are structurally similar to one found in PaaI thioesterase, 4-hydroxybenzoyl-CoA thioesterase (4HBT) and beta-hydroxydecanoyl-ACP dehydratase and thus, the TEII monomer is equivalent to the homodimeric form of the latter three enzymes. Human TEII is expressed in T cells and has been shown to bind the product of the HIV-1 Nef gene.
Pssm-ID: 239528 [Multi-domain] Cd Length: 104 Bit Score: 136.22 E-value: 1.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 176 NAHYIRTHDRIPkqlDDISLHQAIVAFYSDFTLMTTALRPHGLSyISPSLQCASIDHAIYFHRPLRADEWMLYDMEATVS 255
Cdd:cd03444 1 LRVWVRARGPLP---DDPRLHAAALAYLSDSLLLGTALRPHGLP-LFDASASASLDHAIWFHRPFRADDWLLYEQRSPRA 76
|
90 100
....*....|....*....|....*...
gi 1620984417 256 TASRGLNFGRMW-QNGQLVCSTVQEGLM 282
Cdd:cd03444 77 GNGRGLVEGRIFtRDGELVASVAQEGLL 104
|
|
| Thioesterase_II_repeat2 |
cd03445 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
20-107 |
1.95e-38 |
|
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases (NRPSs) as well as modular polyketide synthases (PKSs) by hydrolyzing acetyl groups bound to the peptidyl carrier protein (PCP) and acyl carrier protein (ACP) domains, respectively. TEII has two tandem asymmetric hot dog folds that are structurally similar to one found in PaaI thioesterase, 4-hydroxybenzoyl-CoA thioesterase (4HBT) and beta-hydroxydecanoyl-ACP dehydratase and thus, the TEII monomer is equivalent to the homodimeric form of the latter three enzymes. Human TEII is expressed in T cells and has been shown to bind the product of the HIV-1 Nef gene.
Pssm-ID: 239529 [Multi-domain] Cd Length: 94 Bit Score: 130.43 E-value: 1.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 20 NIYRGIS---RNLVGKRVFGGQVLGQALRAASYTT--DRPAHSLHAYFLYGGDINAPIIYEVDRLRDGKSFVSRQVRAIQ 94
Cdd:cd03445 1 DRFRGVSppvPPGQGRGVFGGQVLAQALVAAARTVpdDRVPHSLHSYFLRPGDPDQPIEYEVERLRDGRSFATRRVRAVQ 80
|
90
....*....|...
gi 1620984417 95 HGRVIFSAMVSFA 107
Cdd:cd03445 81 NGKVIFTATASFQ 93
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
176-282 |
2.58e-28 |
|
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases (NRPSs) as well as modular polyketide synthases (PKSs) by hydrolyzing acetyl groups bound to the peptidyl carrier protein (PCP) and acyl carrier protein (ACP) domains, respectively. TEII has two tandem asymmetric hot dog folds that are structurally similar to one found in PaaI thioesterase, 4-hydroxybenzoyl-CoA thioesterase (4HBT) and beta-hydroxydecanoyl-ACP dehydratase and thus, the TEII monomer is equivalent to the homodimeric form of the latter three enzymes. Human TEII is expressed in T cells and has been shown to bind the product of the HIV-1 Nef gene.
Pssm-ID: 238311 [Multi-domain] Cd Length: 99 Bit Score: 104.35 E-value: 2.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 176 NAHYIRTHDRIPkqlDDISLHQAIVAFYSDFTLMTTALRPHGLSyispslQCASIDHAIYFHRPLRADEWMLYDMEATVS 255
Cdd:cd00556 1 DRFWGRAPGPLP---DDRRVFGGQLAAQSDLAALRTVPRPHGAS------GFASLDHHIYFHRPGDADEWLLYEVESLRD 71
|
90 100
....*....|....*....|....*...
gi 1620984417 256 TASRGLNFGRMWQN-GQLVCSTVQEGLM 282
Cdd:cd00556 72 GRSRALRRGRAYQRdGKLVASATQSFLV 99
|
|
| Acyl_CoA_thio |
pfam02551 |
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ... |
146-281 |
6.39e-26 |
|
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this domain are found in a number of acyl-CoA thioesterases.
Pssm-ID: 396894 Cd Length: 132 Bit Score: 99.24 E-value: 6.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 146 VRASFMRERHVEIRPIDPVNPFQPQpEAPFNAHYIRTHDRIPkqlDDISLHQAIVAFYSDFTLMTTALRPHGLSYISPSl 225
Cdd:pfam02551 2 ANDLFRGEYPVAVRPGELRRTFGGQ-VVAHQQSWVAALGTVP---DDPRLHSCALAYLSDLTLLLTALYPHGFLCDGIQ- 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1620984417 226 qcASIDHAIYFHRPLRADEWMLYDMEATVSTASRGLNFGRMW--QNGQLVCSTVQEGL 281
Cdd:pfam02551 77 --VSLDHSIYFHRPGDLNKWILYDVESPSASGGRGLRQGRNFstQSGKLIASVQQEGL 132
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
31-106 |
1.41e-22 |
|
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases (NRPSs) as well as modular polyketide synthases (PKSs) by hydrolyzing acetyl groups bound to the peptidyl carrier protein (PCP) and acyl carrier protein (ACP) domains, respectively. TEII has two tandem asymmetric hot dog folds that are structurally similar to one found in PaaI thioesterase, 4-hydroxybenzoyl-CoA thioesterase (4HBT) and beta-hydroxydecanoyl-ACP dehydratase and thus, the TEII monomer is equivalent to the homodimeric form of the latter three enzymes. Human TEII is expressed in T cells and has been shown to bind the product of the HIV-1 Nef gene.
Pssm-ID: 238311 [Multi-domain] Cd Length: 99 Bit Score: 89.33 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 31 GKRVFGGQVLGQALRAASYTTDRPA-------HSLHAYFLYGGDINAPIIYEVDRLRDGKSFVSRQVRAIQH-GRVIFSA 102
Cdd:cd00556 14 DRRVFGGQLAAQSDLAALRTVPRPHgasgfasLDHHIYFHRPGDADEWLLYEVESLRDGRSRALRRGRAYQRdGKLVASA 93
|
....
gi 1620984417 103 MVSF 106
Cdd:cd00556 94 TQSF 97
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
206-281 |
2.76e-04 |
|
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: 39.38 E-value: 2.76e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1620984417 206 FTLMTTALRPHGLSYISPSLQCASIDHAIYFHRPLRADEWMLYDMEATVSTASRGLNFGRMW-QNGQLVCSTVQEGL 281
Cdd:cd03440 24 LALADEAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRnEDGKLVATATATFV 100
|
|
| Acyl_CoA_thio |
pfam02551 |
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ... |
56-113 |
2.29e-03 |
|
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this domain are found in a number of acyl-CoA thioesterases.
Pssm-ID: 396894 Cd Length: 132 Bit Score: 37.61 E-value: 2.29e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620984417 56 HSLhaYFLYGGDINAPIIYEVDRLR--DGKSFVSRQVRAIQHGRVIFSAmvsfanPEEGL 113
Cdd:pfam02551 81 HSI--YFHRPGDLNKWILYDVESPSasGGRGLRQGRNFSTQSGKLIASV------QQEGL 132
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