|
Name |
Accession |
Description |
Interval |
E-value |
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
32-256 |
2.57e-102 |
|
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: 298.89 E-value: 2.57e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966161 32 ISSGDPNVPVLYQVERTRTGSSFSVRSVKAVQHGKPIFICQASFQqAQPSPMQHQFSMPTVPPPEElldcetlidQYLRD 111
Cdd:TIGR00189 54 VRAGDPKKPIIYDVERLRDGRSFITRRVKAVQHGKTIFTLQASFQ-AEKSGIEHQSTMPKVPPPES---------ELPRE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966161 112 PNLQKRYPVALNRIAAQEVP----IEIKPINPSPLSQLQRMePKQMFWVRARGYIGEgDMKMHCCVAAYISDYAFLGTAV 187
Cdd:TIGR00189 124 NQLATKYPATLPRFLKHVVPferpFEIRPVNLLNYLGGKED-PPQYVWRRARGSLPD-DPRLHQCALAYLSDLTLLPTAL 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966161 188 LPHQWQHKVHFMV-SLDHSMWFHTPFRADHWMLYECESPWAGGSRGLVHGRLWRQDGVLAVTCAQEGVIR 256
Cdd:TIGR00189 202 NPHNKAGFCHSMAaSLDHSIWFHRPFRADDWLLYKCSSPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
35-258 |
2.70e-73 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 225.14 E-value: 2.70e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966161 35 GDPNVPVLYQVERTRTGSSFSVRSVKAVQHGKPIFICQASFQQAQPSPmQHQFSMPTVPPPEELLDcetlidqyLRDPNL 114
Cdd:COG1946 66 GDPDGPIEYEVERLRDGRSFSTRRVTAIQGGRVIFTATASFGVPEEGL-EHQAPMPDVPPPEDLPS--------LPELLI 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966161 115 QKRYPValnRIAAQEVPIEIKPINPSPLSQLQRMEPKQMFWVRARGyiGEGDMKMHCCVAAYISDYAFLGTAVLPhqWQH 194
Cdd:COG1946 137 AGVLPL---RFFAFLRPFDIRPVEGPLPFAPPSGEPRQRVWMRARD--PLPDDPLHAALLAYASDATPPATALLS--WLG 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966966161 195 KVHFMVSLDHSMWFHTPFRADHWMLYECESPWAGGSRGLVHGRLWRQDGVLAVTCAQEGVIRVK 258
Cdd:COG1946 210 PPLPAASLDHAMWFHRPFRADDWLLYDADSPSASGGRGLERGRIWDRDGRLVASSRQEGLVRGR 273
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
34-255 |
2.44e-72 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 227.30 E-value: 2.44e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966161 34 SGDPNVPVLYQVERTRTGSSFSVRSVKAVQHGKPIFICQASFQQAQPSpMQHQFS-MPTVPPPEELLDCETLIDQYLRDP 112
Cdd:PLN02868 193 VGDINLPIIYQVERIRDGHNFATRRVDAIQKGKVIFTLFASFQKEEQG-FEHQEStMPHVPPPETLLSREELRERRLTDP 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966161 113 NLQKRYPvalNRIAAQEV---PIEIKPINPSPLSQLQRMEPKQMFWVRARGYIGEgDMKMHCCVAAYISDYAFLGTAVLP 189
Cdd:PLN02868 272 RLPRSYR---NKVAAKPFvpwPIEIRFCEPNNSTNQTKSPPRLRYWFRAKGKLSD-DQALHRCVAAYASDLIFLGTSLNP 347
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966966161 190 HQWQHKVHFMVSLDHSMWFHTPFRADHWMLYECESPWAGGSRGLVHGRLWRQDGVLAVTCAQEGVI 255
Cdd:PLN02868 348 HRTKGLKFAALSLDHSMWFHRPFRADDWLLFVIVSPAAHNGRGFATGHMFNRKGELVVSLTQEALL 413
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
152-255 |
7.58e-47 |
|
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: 151.63 E-value: 7.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966161 152 QMFWVRARGYIGEgDMKMHCCVAAYISDYAFLGTAVLPHQWQHKVH-FMVSLDHSMWFHTPFRADHWMLYECESPWAGGS 230
Cdd:cd03444 1 LRVWVRARGPLPD-DPRLHAAALAYLSDSLLLGTALRPHGLPLFDAsASASLDHAIWFHRPFRADDWLLYEQRSPRAGNG 79
|
90 100
....*....|....*....|....*
gi 966966161 231 RGLVHGRLWRQDGVLAVTCAQEGVI 255
Cdd:cd03444 80 RGLVEGRIFTRDGELVASVAQEGLL 104
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
40-255 |
2.13e-42 |
|
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: 145.17 E-value: 2.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966161 40 PVLYQVERTRTGSSFSVRSVKAVQHGKPIFICQASFQQAQPSPMQ-HQFSMPTVPPPEElldcetlidqylrDPNLQKRY 118
Cdd:pfam13622 48 PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRLRSSEWElTPAAPPPLPPPED-------------CPLAADEA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966161 119 PVALNRIAAQEV-PIEIKPINPSPLSQlQRMEPKQMFWVRARgyigEGDMKMHCCVAAYISDyAFLGTAVLPHQWQHKVH 197
Cdd:pfam13622 115 PFPLFRRVPGFLdPFEPRFARGGGPFS-PGGPGRVRLWVRLR----DGGEPDPLAALAYLAD-AFPPRVLSLRLDPPASG 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 966966161 198 FMVSLDHSMWFHTPFRADHWMLYECESPWAGGSRGLVHGRLWRQDGVLAVTCAQEGVI 255
Cdd:pfam13622 189 WFPTLDLTVYFHRRPPPGEWLLLRAETPVAGDGRGDVEARLWDEDGRLVATSRQEVLV 246
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
32-256 |
2.57e-102 |
|
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: 298.89 E-value: 2.57e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966161 32 ISSGDPNVPVLYQVERTRTGSSFSVRSVKAVQHGKPIFICQASFQqAQPSPMQHQFSMPTVPPPEElldcetlidQYLRD 111
Cdd:TIGR00189 54 VRAGDPKKPIIYDVERLRDGRSFITRRVKAVQHGKTIFTLQASFQ-AEKSGIEHQSTMPKVPPPES---------ELPRE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966161 112 PNLQKRYPVALNRIAAQEVP----IEIKPINPSPLSQLQRMePKQMFWVRARGYIGEgDMKMHCCVAAYISDYAFLGTAV 187
Cdd:TIGR00189 124 NQLATKYPATLPRFLKHVVPferpFEIRPVNLLNYLGGKED-PPQYVWRRARGSLPD-DPRLHQCALAYLSDLTLLPTAL 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966161 188 LPHQWQHKVHFMV-SLDHSMWFHTPFRADHWMLYECESPWAGGSRGLVHGRLWRQDGVLAVTCAQEGVIR 256
Cdd:TIGR00189 202 NPHNKAGFCHSMAaSLDHSIWFHRPFRADDWLLYKCSSPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
35-258 |
2.70e-73 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 225.14 E-value: 2.70e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966161 35 GDPNVPVLYQVERTRTGSSFSVRSVKAVQHGKPIFICQASFQQAQPSPmQHQFSMPTVPPPEELLDcetlidqyLRDPNL 114
Cdd:COG1946 66 GDPDGPIEYEVERLRDGRSFSTRRVTAIQGGRVIFTATASFGVPEEGL-EHQAPMPDVPPPEDLPS--------LPELLI 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966161 115 QKRYPValnRIAAQEVPIEIKPINPSPLSQLQRMEPKQMFWVRARGyiGEGDMKMHCCVAAYISDYAFLGTAVLPhqWQH 194
Cdd:COG1946 137 AGVLPL---RFFAFLRPFDIRPVEGPLPFAPPSGEPRQRVWMRARD--PLPDDPLHAALLAYASDATPPATALLS--WLG 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966966161 195 KVHFMVSLDHSMWFHTPFRADHWMLYECESPWAGGSRGLVHGRLWRQDGVLAVTCAQEGVIRVK 258
Cdd:COG1946 210 PPLPAASLDHAMWFHRPFRADDWLLYDADSPSASGGRGLERGRIWDRDGRLVASSRQEGLVRGR 273
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
34-255 |
2.44e-72 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 227.30 E-value: 2.44e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966161 34 SGDPNVPVLYQVERTRTGSSFSVRSVKAVQHGKPIFICQASFQQAQPSpMQHQFS-MPTVPPPEELLDCETLIDQYLRDP 112
Cdd:PLN02868 193 VGDINLPIIYQVERIRDGHNFATRRVDAIQKGKVIFTLFASFQKEEQG-FEHQEStMPHVPPPETLLSREELRERRLTDP 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966161 113 NLQKRYPvalNRIAAQEV---PIEIKPINPSPLSQLQRMEPKQMFWVRARGYIGEgDMKMHCCVAAYISDYAFLGTAVLP 189
Cdd:PLN02868 272 RLPRSYR---NKVAAKPFvpwPIEIRFCEPNNSTNQTKSPPRLRYWFRAKGKLSD-DQALHRCVAAYASDLIFLGTSLNP 347
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966966161 190 HQWQHKVHFMVSLDHSMWFHTPFRADHWMLYECESPWAGGSRGLVHGRLWRQDGVLAVTCAQEGVI 255
Cdd:PLN02868 348 HRTKGLKFAALSLDHSMWFHRPFRADDWLLFVIVSPAAHNGRGFATGHMFNRKGELVVSLTQEALL 413
|
|
| PRK10526 |
PRK10526 |
acyl-CoA thioesterase II; Provisional |
35-259 |
4.04e-57 |
|
acyl-CoA thioesterase II; Provisional
Pssm-ID: 182519 [Multi-domain] Cd Length: 286 Bit Score: 184.18 E-value: 4.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966161 35 GDPNVPVLYQVERTRTGSSFSVRSVKAVQHGKPIFICQASFQqAQPSPMQHQFSMPTVPPPEELLDcETLIDQylrdpNL 114
Cdd:PRK10526 68 GDSQKPIIYDVETLRDGNSFSARRVAAIQNGKPIFYMTASFQ-APEAGFEHQKTMPSAPAPDGLPS-ETDIAQ-----SL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966161 115 QKRYPVALNRIAAQEVPIEIKPIN-PSPLsQLQRMEPKQMFWVRARGYIGEgDMKMHCCVAAYISDYAFLGTAVLPHqwq 193
Cdd:PRK10526 141 AHLLPPVLKDKFICDRPLEIRPVEfHNPL-KGHVAEPVRQVWIRANGSVPD-DLRVHQYLLGYASDLNFLPVALQPH--- 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966966161 194 hKVHFM------VSLDHSMWFHTPFRADHWMLYECESPWAGGSRGLVHGRLWRQDGVLAVTCAQEGVIRVKP 259
Cdd:PRK10526 216 -GIGFLepgmqiATIDHSMWFHRPFNLNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMRNHN 286
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
152-255 |
7.58e-47 |
|
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: 151.63 E-value: 7.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966161 152 QMFWVRARGYIGEgDMKMHCCVAAYISDYAFLGTAVLPHQWQHKVH-FMVSLDHSMWFHTPFRADHWMLYECESPWAGGS 230
Cdd:cd03444 1 LRVWVRARGPLPD-DPRLHAAALAYLSDSLLLGTALRPHGLPLFDAsASASLDHAIWFHRPFRADDWLLYEQRSPRAGNG 79
|
90 100
....*....|....*....|....*
gi 966966161 231 RGLVHGRLWRQDGVLAVTCAQEGVI 255
Cdd:cd03444 80 RGLVEGRIFTRDGELVASVAQEGLL 104
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
40-255 |
2.13e-42 |
|
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: 145.17 E-value: 2.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966161 40 PVLYQVERTRTGSSFSVRSVKAVQHGKPIFICQASFQQAQPSPMQ-HQFSMPTVPPPEElldcetlidqylrDPNLQKRY 118
Cdd:pfam13622 48 PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRLRSSEWElTPAAPPPLPPPED-------------CPLAADEA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966161 119 PVALNRIAAQEV-PIEIKPINPSPLSQlQRMEPKQMFWVRARgyigEGDMKMHCCVAAYISDyAFLGTAVLPHQWQHKVH 197
Cdd:pfam13622 115 PFPLFRRVPGFLdPFEPRFARGGGPFS-PGGPGRVRLWVRLR----DGGEPDPLAALAYLAD-AFPPRVLSLRLDPPASG 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 966966161 198 FMVSLDHSMWFHTPFRADHWMLYECESPWAGGSRGLVHGRLWRQDGVLAVTCAQEGVI 255
Cdd:pfam13622 189 WFPTLDLTVYFHRRPPPGEWLLLRAETPVAGDGRGDVEARLWDEDGRLVATSRQEVLV 246
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
152-255 |
1.51e-35 |
|
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: 122.45 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966161 152 QMFWVRARGYIGeGDMKMHCCVAAYISDYAFLGTAVLPHqwqhKVHFMVSLDHSMWFHTPFRADHWMLYECESPWAGGSR 231
Cdd:cd00556 1 DRFWGRAPGPLP-DDRRVFGGQLAAQSDLAALRTVPRPH----GASGFASLDHHIYFHRPGDADEWLLYEVESLRDGRSR 75
|
90 100
....*....|....*....|....
gi 966966161 232 GLVHGRLWRQDGVLAVTCAQEGVI 255
Cdd:cd00556 76 ALRRGRAYQRDGKLVASATQSFLV 99
|
|
| Acyl_CoA_thio |
pfam02551 |
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ... |
146-254 |
6.51e-25 |
|
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: 96.16 E-value: 6.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966161 146 QRMEPKQMfWVRARGYIGEgDMKMHCCVAAYISDYAFLGTAVLPHQWQHKvHFMVSLDHSMWFHTPFRADHWMLYECESP 225
Cdd:pfam02551 26 QVVAHQQS-WVAALGTVPD-DPRLHSCALAYLSDLTLLLTALYPHGFLCD-GIQVSLDHSIYFHRPGDLNKWILYDVESP 102
|
90 100 110
....*....|....*....|....*....|
gi 966966161 226 WAGGSRGLVHGRLWR-QDGVLAVTCAQEGV 254
Cdd:pfam02551 103 SASGGRGLRQGRNFStQSGKLIASVQQEGL 132
|
|
| Thioesterase_II_repeat2 |
cd03445 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
35-77 |
2.61e-16 |
|
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: 72.27 E-value: 2.61e-16
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 966966161 35 GDPNVPVLYQVERTRTGSSFSVRSVKAVQHGKPIFICQASFQQ 77
Cdd:cd03445 52 GDPDQPIEYEVERLRDGRSFATRRVRAVQNGKVIFTATASFQR 94
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
154-254 |
1.07e-09 |
|
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: 54.40 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966161 154 FWVRARGYIGEGDMKMHCCVAAYISDYAFLGTAVLPHqwqHKVHFMVSLDHSMWFHTPFRADHWMLYECESPWAGGSRGL 233
Cdd:cd03440 3 LRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLG---GRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVT 79
|
90 100
....*....|....*....|.
gi 966966161 234 VHGRLWRQDGVLAVTCAQEGV 254
Cdd:cd03440 80 VEVEVRNEDGKLVATATATFV 100
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
35-76 |
1.51e-08 |
|
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: 51.19 E-value: 1.51e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 966966161 35 GDPNVPVLYQVERTRTGSSFSVRSVKAVQH-GKPIFICQASFQ 76
Cdd:cd00556 56 GDADEWLLYEVESLRDGRSRALRRGRAYQRdGKLVASATQSFL 98
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