|
Name |
Accession |
Description |
Interval |
E-value |
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
3-227 |
9.99e-95 |
|
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: 278.47 E-value: 9.99e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915605 3 ISTGDPKVPVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQmQPSPLQHQFSMPSVPPPEDlldhealidQYLRD 82
Cdd:TIGR00189 54 VRAGDPKKPIIYDVERLRDGRSFITRRVKAVQHGKTIFTLQASFQA-EKSGIEHQSTMPKVPPPES---------ELPRE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915605 83 PNLHKKYRVGLNRVAAQEVP----IEIKVVNPPTLTQLQALePKQMFWVRARGYIGEgDIKMHCCVAAYISDYAFLGTAL 158
Cdd:TIGR00189 124 NQLATKYPATLPRFLKHVVPferpFEIRPVNLLNYLGGKED-PPQYVWRRARGSLPD-DPRLHQCALAYLSDLTLLPTAL 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915605 159 LPHQSKYKVNFM-ASLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVIR 227
Cdd:TIGR00189 202 NPHNKAGFCHSMaASLDHSIWFHRPFRADDWLLYKCSSPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
5-226 |
1.01e-76 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 237.31 E-value: 1.01e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915605 5 TGDPKVPVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQMQPSpLQHQFS-MPSVPPPEDLLDHEALIDQYLRDP 83
Cdd:PLN02868 193 VGDINLPIIYQVERIRDGHNFATRRVDAIQKGKVIFTLFASFQKEEQG-FEHQEStMPHVPPPETLLSREELRERRLTDP 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915605 84 NLHKKYRvglNRVAAQEV---PIEIKVVNPPTLTQLQALEPKQMFWVRARGYIGEgDIKMHCCVAAYISDYAFLGTALLP 160
Cdd:PLN02868 272 RLPRSYR---NKVAAKPFvpwPIEIRFCEPNNSTNQTKSPPRLRYWFRAKGKLSD-DQALHRCVAAYASDLIFLGTSLNP 347
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568915605 161 HQSKYKVNFMASLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVI 226
Cdd:PLN02868 348 HRTKGLKFAALSLDHSMWFHRPFRADDWLLFVIVSPAAHNGRGFATGHMFNRKGELVVSLTQEALL 413
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
6-229 |
5.35e-75 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 228.22 E-value: 5.35e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915605 6 GDPKVPVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQMQPSpLQHQFSMPSVPPPEDLLD-HEALIDQYLRDpn 84
Cdd:COG1946 66 GDPDGPIEYEVERLRDGRSFSTRRVTAIQGGRVIFTATASFGVPEEG-LEHQAPMPDVPPPEDLPSlPELLIAGVLPL-- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915605 85 lhkkyrvglnRVAAQEVPIEIKVVNPPTLTQLQALEPKQMFWVRARGyiGEGDIKMHCCVAAYISDYAFLGTALLPHQSK 164
Cdd:COG1946 143 ----------RFFAFLRPFDIRPVEGPLPFAPPSGEPRQRVWMRARD--PLPDDPLHAALLAYASDATPPATALLSWLGP 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568915605 165 YKvnFMASLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVIRLK 229
Cdd:COG1946 211 PL--PAASLDHAMWFHRPFRADDWLLYDADSPSASGGRGLERGRIWDRDGRLVASSRQEGLVRGR 273
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
123-226 |
5.49e-48 |
|
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: 153.56 E-value: 5.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915605 123 QMFWVRARGYIGEgDIKMHCCVAAYISDYAFLGTALLPHQSK-YKVNFMASLDHSMWFHAPFRADHWMLYECESPWAGGS 201
Cdd:cd03444 1 LRVWVRARGPLPD-DPRLHAAALAYLSDSLLLGTALRPHGLPlFDASASASLDHAIWFHRPFRADDWLLYEQRSPRAGNG 79
|
90 100
....*....|....*....|....*
gi 568915605 202 RGLVHGRLWRRDGVLAVTCAQEGVI 226
Cdd:cd03444 80 RGLVEGRIFTRDGELVASVAQEGLL 104
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
11-226 |
2.44e-43 |
|
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: 146.32 E-value: 2.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915605 11 PVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQMQPSPLQ-HQFSMPSVPPPEDLLDHEalidqylrDPNLHKKY 89
Cdd:pfam13622 48 PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRLRSSEWElTPAAPPPLPPPEDCPLAA--------DEAPFPLF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915605 90 RVGLNRVAaqevPIEIKVVNPPTLTQlQALEPKQMFWVRARgyigEGDIKMHCCVAAYISDyAFLGTALLPHQSKYKVNF 169
Cdd:pfam13622 120 RRVPGFLD----PFEPRFARGGGPFS-PGGPGRVRLWVRLR----DGGEPDPLAALAYLAD-AFPPRVLSLRLDPPASGW 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568915605 170 MASLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVI 226
Cdd:pfam13622 190 FPTLDLTVYFHRRPPPGEWLLLRAETPVAGDGRGDVEARLWDEDGRLVATSRQEVLV 246
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
3-227 |
9.99e-95 |
|
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: 278.47 E-value: 9.99e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915605 3 ISTGDPKVPVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQmQPSPLQHQFSMPSVPPPEDlldhealidQYLRD 82
Cdd:TIGR00189 54 VRAGDPKKPIIYDVERLRDGRSFITRRVKAVQHGKTIFTLQASFQA-EKSGIEHQSTMPKVPPPES---------ELPRE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915605 83 PNLHKKYRVGLNRVAAQEVP----IEIKVVNPPTLTQLQALePKQMFWVRARGYIGEgDIKMHCCVAAYISDYAFLGTAL 158
Cdd:TIGR00189 124 NQLATKYPATLPRFLKHVVPferpFEIRPVNLLNYLGGKED-PPQYVWRRARGSLPD-DPRLHQCALAYLSDLTLLPTAL 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915605 159 LPHQSKYKVNFM-ASLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVIR 227
Cdd:TIGR00189 202 NPHNKAGFCHSMaASLDHSIWFHRPFRADDWLLYKCSSPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
5-226 |
1.01e-76 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 237.31 E-value: 1.01e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915605 5 TGDPKVPVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQMQPSpLQHQFS-MPSVPPPEDLLDHEALIDQYLRDP 83
Cdd:PLN02868 193 VGDINLPIIYQVERIRDGHNFATRRVDAIQKGKVIFTLFASFQKEEQG-FEHQEStMPHVPPPETLLSREELRERRLTDP 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915605 84 NLHKKYRvglNRVAAQEV---PIEIKVVNPPTLTQLQALEPKQMFWVRARGYIGEgDIKMHCCVAAYISDYAFLGTALLP 160
Cdd:PLN02868 272 RLPRSYR---NKVAAKPFvpwPIEIRFCEPNNSTNQTKSPPRLRYWFRAKGKLSD-DQALHRCVAAYASDLIFLGTSLNP 347
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568915605 161 HQSKYKVNFMASLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVI 226
Cdd:PLN02868 348 HRTKGLKFAALSLDHSMWFHRPFRADDWLLFVIVSPAAHNGRGFATGHMFNRKGELVVSLTQEALL 413
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
6-229 |
5.35e-75 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 228.22 E-value: 5.35e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915605 6 GDPKVPVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQMQPSpLQHQFSMPSVPPPEDLLD-HEALIDQYLRDpn 84
Cdd:COG1946 66 GDPDGPIEYEVERLRDGRSFSTRRVTAIQGGRVIFTATASFGVPEEG-LEHQAPMPDVPPPEDLPSlPELLIAGVLPL-- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915605 85 lhkkyrvglnRVAAQEVPIEIKVVNPPTLTQLQALEPKQMFWVRARGyiGEGDIKMHCCVAAYISDYAFLGTALLPHQSK 164
Cdd:COG1946 143 ----------RFFAFLRPFDIRPVEGPLPFAPPSGEPRQRVWMRARD--PLPDDPLHAALLAYASDATPPATALLSWLGP 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568915605 165 YKvnFMASLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVIRLK 229
Cdd:COG1946 211 PL--PAASLDHAMWFHRPFRADDWLLYDADSPSASGGRGLERGRIWDRDGRLVASSRQEGLVRGR 273
|
|
| PRK10526 |
PRK10526 |
acyl-CoA thioesterase II; Provisional |
6-230 |
5.16e-57 |
|
acyl-CoA thioesterase II; Provisional
Pssm-ID: 182519 [Multi-domain] Cd Length: 286 Bit Score: 182.64 E-value: 5.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915605 6 GDPKVPVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQMQPSpLQHQFSMPSVPPPEDLLDHEALIDQ--YLRDP 83
Cdd:PRK10526 68 GDSQKPIIYDVETLRDGNSFSARRVAAIQNGKPIFYMTASFQAPEAG-FEHQKTMPSAPAPDGLPSETDIAQSlaHLLPP 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915605 84 NLHKKYrvglnrvaAQEVPIEIKVV---NPptlTQLQALEPKQMFWVRARGYIGEgDIKMHCCVAAYISDYAFLGTALLP 160
Cdd:PRK10526 147 VLKDKF--------ICDRPLEIRPVefhNP---LKGHVAEPVRQVWIRANGSVPD-DLRVHQYLLGYASDLNFLPVALQP 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568915605 161 HQSKYKVNFM--ASLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVIRLKP 230
Cdd:PRK10526 215 HGIGFLEPGMqiATIDHSMWFHRPFNLNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMRNHN 286
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
123-226 |
5.49e-48 |
|
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: 153.56 E-value: 5.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915605 123 QMFWVRARGYIGEgDIKMHCCVAAYISDYAFLGTALLPHQSK-YKVNFMASLDHSMWFHAPFRADHWMLYECESPWAGGS 201
Cdd:cd03444 1 LRVWVRARGPLPD-DPRLHAAALAYLSDSLLLGTALRPHGLPlFDASASASLDHAIWFHRPFRADDWLLYEQRSPRAGNG 79
|
90 100
....*....|....*....|....*
gi 568915605 202 RGLVHGRLWRRDGVLAVTCAQEGVI 226
Cdd:cd03444 80 RGLVEGRIFTRDGELVASVAQEGLL 104
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
11-226 |
2.44e-43 |
|
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: 146.32 E-value: 2.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915605 11 PVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQMQPSPLQ-HQFSMPSVPPPEDLLDHEalidqylrDPNLHKKY 89
Cdd:pfam13622 48 PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRLRSSEWElTPAAPPPLPPPEDCPLAA--------DEAPFPLF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915605 90 RVGLNRVAaqevPIEIKVVNPPTLTQlQALEPKQMFWVRARgyigEGDIKMHCCVAAYISDyAFLGTALLPHQSKYKVNF 169
Cdd:pfam13622 120 RRVPGFLD----PFEPRFARGGGPFS-PGGPGRVRLWVRLR----DGGEPDPLAALAYLAD-AFPPRVLSLRLDPPASGW 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568915605 170 MASLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVI 226
Cdd:pfam13622 190 FPTLDLTVYFHRRPPPGEWLLLRAETPVAGDGRGDVEARLWDEDGRLVATSRQEVLV 246
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
123-226 |
1.53e-36 |
|
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: 124.38 E-value: 1.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915605 123 QMFWVRARGYIGeGDIKMHCCVAAYISDYAFLGTALLPHQSKykvnFMASLDHSMWFHAPFRADHWMLYECESPWAGGSR 202
Cdd:cd00556 1 DRFWGRAPGPLP-DDRRVFGGQLAAQSDLAALRTVPRPHGAS----GFASLDHHIYFHRPGDADEWLLYEVESLRDGRSR 75
|
90 100
....*....|....*....|....
gi 568915605 203 GLVHGRLWRRDGVLAVTCAQEGVI 226
Cdd:cd00556 76 ALRRGRAYQRDGKLVASATQSFLV 99
|
|
| Acyl_CoA_thio |
pfam02551 |
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ... |
108-225 |
1.47e-24 |
|
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: 94.62 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915605 108 VNPPTLTQL---QALEPKQMfWVRARGYIGEgDIKMHCCVAAYISDYAFLGTALLPHQSkYKVNFMASLDHSMWFHAPFR 184
Cdd:pfam02551 14 VRPGELRRTfggQVVAHQQS-WVAALGTVPD-DPRLHSCALAYLSDLTLLLTALYPHGF-LCDGIQVSLDHSIYFHRPGD 90
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 568915605 185 ADHWMLYECESPWAGGSRGLVHGRLWR-RDGVLAVTCAQEGV 225
Cdd:pfam02551 91 LNKWILYDVESPSASGGRGLRQGRNFStQSGKLIASVQQEGL 132
|
|
| Thioesterase_II_repeat2 |
cd03445 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
6-48 |
4.84e-17 |
|
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: 73.42 E-value: 4.84e-17
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 568915605 6 GDPKVPVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQ 48
Cdd:cd03445 52 GDPDQPIEYEVERLRDGRSFATRRVRAVQNGKVIFTATASFQR 94
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
125-225 |
7.97e-10 |
|
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: 7.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915605 125 FWVRARGYIGEGDIKMHCCVAAYISDYAFLGTALLPHQSKYkvnFMASLDHSMWFHAPFRADHWMLYECESPWAGGSRGL 204
Cdd:cd03440 3 LRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGL---GAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVT 79
|
90 100
....*....|....*....|.
gi 568915605 205 VHGRLWRRDGVLAVTCAQEGV 225
Cdd:cd03440 80 VEVEVRNEDGKLVATATATFV 100
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
6-47 |
5.48e-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: 49.26 E-value: 5.48e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 568915605 6 GDPKVPVLYHVERIRTGASFSVRAVKAVQH-GKAIFICQASFQ 47
Cdd:cd00556 56 GDADEWLLYEVESLRDGRSRALRRGRAYQRdGKLVASATQSFL 98
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