|
Name |
Accession |
Description |
Interval |
E-value |
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
9-230 |
1.10e-93 |
|
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: 275.77 E-value: 1.10e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498806 9 GDPKVPVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQmQPSPLQHQFSMPSVPPPEDlldhealidQYLRDPNL 88
Cdd:TIGR00189 57 GDPKKPIIYDVERLRDGRSFITRRVKAVQHGKTIFTLQASFQA-EKSGIEHQSTMPKVPPPES---------ELPRENQL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498806 89 HKKYRVGLNRVAAQEVP----IEIKVVNPPTLTQLQALePKQMFWVRARGYIGEgDIKMHCCVAAYISDYAFLGTALLPH 164
Cdd:TIGR00189 127 ATKYPATLPRFLKHVVPferpFEIRPVNLLNYLGGKED-PPQYVWRRARGSLPD-DPRLHQCALAYLSDLTLLPTALNPH 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755498806 165 QSKYKVNFM-ASLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVIR 230
Cdd:TIGR00189 205 NKAGFCHSMaASLDHSIWFHRPFRADDWLLYKCSSPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
7-229 |
1.88e-76 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 236.54 E-value: 1.88e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498806 7 LEGDPKVPVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQMQPSpLQHQFS-MPSVPPPEDLLDHEALIDQYLRD 85
Cdd:PLN02868 192 LVGDINLPIIYQVERIRDGHNFATRRVDAIQKGKVIFTLFASFQKEEQG-FEHQEStMPHVPPPETLLSREELRERRLTD 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498806 86 PNLHKKYRvglNRVAAQEV---PIEIKVVNPPTLTQLQALEPKQMFWVRARGYIGEgDIKMHCCVAAYISDYAFLGTALL 162
Cdd:PLN02868 271 PRLPRSYR---NKVAAKPFvpwPIEIRFCEPNNSTNQTKSPPRLRYWFRAKGKLSD-DQALHRCVAAYASDLIFLGTSLN 346
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755498806 163 PHQSKYKVNFMASLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVI 229
Cdd:PLN02868 347 PHRTKGLKFAALSLDHSMWFHRPFRADDWLLFVIVSPAAHNGRGFATGHMFNRKGELVVSLTQEALL 413
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
9-232 |
2.65e-74 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 226.68 E-value: 2.65e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498806 9 GDPKVPVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQMQPSpLQHQFSMPSVPPPEDLLD-HEALIDQYLRDpn 87
Cdd:COG1946 66 GDPDGPIEYEVERLRDGRSFSTRRVTAIQGGRVIFTATASFGVPEEG-LEHQAPMPDVPPPEDLPSlPELLIAGVLPL-- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498806 88 lhkkyrvglnRVAAQEVPIEIKVVNPPTLTQLQALEPKQMFWVRARGyiGEGDIKMHCCVAAYISDYAFLGTALLPHQSK 167
Cdd:COG1946 143 ----------RFFAFLRPFDIRPVEGPLPFAPPSGEPRQRVWMRARD--PLPDDPLHAALLAYASDATPPATALLSWLGP 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755498806 168 YKvnFMASLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVIRLK 232
Cdd:COG1946 211 PL--PAASLDHAMWFHRPFRADDWLLYDADSPSASGGRGLERGRIWDRDGRLVASSRQEGLVRGR 273
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
126-229 |
1.01e-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: 153.17 E-value: 1.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498806 126 QMFWVRARGYIGEgDIKMHCCVAAYISDYAFLGTALLPHQSK-YKVNFMASLDHSMWFHAPFRADHWMLYECESPWAGGS 204
Cdd:cd03444 1 LRVWVRARGPLPD-DPRLHAAALAYLSDSLLLGTALRPHGLPlFDASASASLDHAIWFHRPFRADDWLLYEQRSPRAGNG 79
|
90 100
....*....|....*....|....*
gi 755498806 205 RGLVHGRLWRRDGVLAVTCAQEGVI 229
Cdd:cd03444 80 RGLVEGRIFTRDGELVASVAQEGLL 104
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
14-229 |
4.69e-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: 145.94 E-value: 4.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498806 14 PVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQMQPSPLQ-HQFSMPSVPPPEDLLDHealidqylRDPNLHKKY 92
Cdd:pfam13622 48 PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRLRSSEWElTPAAPPPLPPPEDCPLA--------ADEAPFPLF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498806 93 RVGLNRVAaqevPIEIKVVNPPTLTQlQALEPKQMFWVRARgyigEGDIKMHCCVAAYISDyAFLGTALLPHQSKYKVNF 172
Cdd:pfam13622 120 RRVPGFLD----PFEPRFARGGGPFS-PGGPGRVRLWVRLR----DGGEPDPLAALAYLAD-AFPPRVLSLRLDPPASGW 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 755498806 173 MASLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVI 229
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. ... |
9-230 |
1.10e-93 |
|
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: 275.77 E-value: 1.10e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498806 9 GDPKVPVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQmQPSPLQHQFSMPSVPPPEDlldhealidQYLRDPNL 88
Cdd:TIGR00189 57 GDPKKPIIYDVERLRDGRSFITRRVKAVQHGKTIFTLQASFQA-EKSGIEHQSTMPKVPPPES---------ELPRENQL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498806 89 HKKYRVGLNRVAAQEVP----IEIKVVNPPTLTQLQALePKQMFWVRARGYIGEgDIKMHCCVAAYISDYAFLGTALLPH 164
Cdd:TIGR00189 127 ATKYPATLPRFLKHVVPferpFEIRPVNLLNYLGGKED-PPQYVWRRARGSLPD-DPRLHQCALAYLSDLTLLPTALNPH 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755498806 165 QSKYKVNFM-ASLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVIR 230
Cdd:TIGR00189 205 NKAGFCHSMaASLDHSIWFHRPFRADDWLLYKCSSPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
7-229 |
1.88e-76 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 236.54 E-value: 1.88e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498806 7 LEGDPKVPVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQMQPSpLQHQFS-MPSVPPPEDLLDHEALIDQYLRD 85
Cdd:PLN02868 192 LVGDINLPIIYQVERIRDGHNFATRRVDAIQKGKVIFTLFASFQKEEQG-FEHQEStMPHVPPPETLLSREELRERRLTD 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498806 86 PNLHKKYRvglNRVAAQEV---PIEIKVVNPPTLTQLQALEPKQMFWVRARGYIGEgDIKMHCCVAAYISDYAFLGTALL 162
Cdd:PLN02868 271 PRLPRSYR---NKVAAKPFvpwPIEIRFCEPNNSTNQTKSPPRLRYWFRAKGKLSD-DQALHRCVAAYASDLIFLGTSLN 346
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755498806 163 PHQSKYKVNFMASLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVI 229
Cdd:PLN02868 347 PHRTKGLKFAALSLDHSMWFHRPFRADDWLLFVIVSPAAHNGRGFATGHMFNRKGELVVSLTQEALL 413
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
9-232 |
2.65e-74 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 226.68 E-value: 2.65e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498806 9 GDPKVPVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQMQPSpLQHQFSMPSVPPPEDLLD-HEALIDQYLRDpn 87
Cdd:COG1946 66 GDPDGPIEYEVERLRDGRSFSTRRVTAIQGGRVIFTATASFGVPEEG-LEHQAPMPDVPPPEDLPSlPELLIAGVLPL-- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498806 88 lhkkyrvglnRVAAQEVPIEIKVVNPPTLTQLQALEPKQMFWVRARGyiGEGDIKMHCCVAAYISDYAFLGTALLPHQSK 167
Cdd:COG1946 143 ----------RFFAFLRPFDIRPVEGPLPFAPPSGEPRQRVWMRARD--PLPDDPLHAALLAYASDATPPATALLSWLGP 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755498806 168 YKvnFMASLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVIRLK 232
Cdd:COG1946 211 PL--PAASLDHAMWFHRPFRADDWLLYDADSPSASGGRGLERGRIWDRDGRLVASSRQEGLVRGR 273
|
|
| PRK10526 |
PRK10526 |
acyl-CoA thioesterase II; Provisional |
9-233 |
1.67e-56 |
|
acyl-CoA thioesterase II; Provisional
Pssm-ID: 182519 [Multi-domain] Cd Length: 286 Bit Score: 181.49 E-value: 1.67e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498806 9 GDPKVPVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQMQPSpLQHQFSMPSVPPPEDLLDHEALIDQ--YLRDP 86
Cdd:PRK10526 68 GDSQKPIIYDVETLRDGNSFSARRVAAIQNGKPIFYMTASFQAPEAG-FEHQKTMPSAPAPDGLPSETDIAQSlaHLLPP 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498806 87 NLHKKYrvglnrvaAQEVPIEIKVV---NPptlTQLQALEPKQMFWVRARGYIGEgDIKMHCCVAAYISDYAFLGTALLP 163
Cdd:PRK10526 147 VLKDKF--------ICDRPLEIRPVefhNP---LKGHVAEPVRQVWIRANGSVPD-DLRVHQYLLGYASDLNFLPVALQP 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755498806 164 HQSKYKVNFM--ASLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVIRLKP 233
Cdd:PRK10526 215 HGIGFLEPGMqiATIDHSMWFHRPFNLNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMRNHN 286
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
126-229 |
1.01e-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: 153.17 E-value: 1.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498806 126 QMFWVRARGYIGEgDIKMHCCVAAYISDYAFLGTALLPHQSK-YKVNFMASLDHSMWFHAPFRADHWMLYECESPWAGGS 204
Cdd:cd03444 1 LRVWVRARGPLPD-DPRLHAAALAYLSDSLLLGTALRPHGLPlFDASASASLDHAIWFHRPFRADDWLLYEQRSPRAGNG 79
|
90 100
....*....|....*....|....*
gi 755498806 205 RGLVHGRLWRRDGVLAVTCAQEGVI 229
Cdd:cd03444 80 RGLVEGRIFTRDGELVASVAQEGLL 104
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
14-229 |
4.69e-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: 145.94 E-value: 4.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498806 14 PVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQMQPSPLQ-HQFSMPSVPPPEDLLDHealidqylRDPNLHKKY 92
Cdd:pfam13622 48 PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRLRSSEWElTPAAPPPLPPPEDCPLA--------ADEAPFPLF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498806 93 RVGLNRVAaqevPIEIKVVNPPTLTQlQALEPKQMFWVRARgyigEGDIKMHCCVAAYISDyAFLGTALLPHQSKYKVNF 172
Cdd:pfam13622 120 RRVPGFLD----PFEPRFARGGGPFS-PGGPGRVRLWVRLR----DGGEPDPLAALAYLAD-AFPPRVLSLRLDPPASGW 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 755498806 173 MASLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVI 229
Cdd:pfam13622 190 FPTLDLTVYFHRRPPPGEWLLLRAETPVAGDGRGDVEARLWDEDGRLVATSRQEVLV 246
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
126-229 |
2.25e-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: 123.99 E-value: 2.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498806 126 QMFWVRARGYIGeGDIKMHCCVAAYISDYAFLGTALLPHQSKykvnFMASLDHSMWFHAPFRADHWMLYECESPWAGGSR 205
Cdd:cd00556 1 DRFWGRAPGPLP-DDRRVFGGQLAAQSDLAALRTVPRPHGAS----GFASLDHHIYFHRPGDADEWLLYEVESLRDGRSR 75
|
90 100
....*....|....*....|....
gi 755498806 206 GLVHGRLWRRDGVLAVTCAQEGVI 229
Cdd:cd00556 76 ALRRGRAYQRDGKLVASATQSFLV 99
|
|
| Acyl_CoA_thio |
pfam02551 |
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ... |
111-228 |
1.76e-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: 94.23 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498806 111 VNPPTLTQL---QALEPKQMfWVRARGYIGEgDIKMHCCVAAYISDYAFLGTALLPHQSkYKVNFMASLDHSMWFHAPFR 187
Cdd:pfam02551 14 VRPGELRRTfggQVVAHQQS-WVAALGTVPD-DPRLHSCALAYLSDLTLLLTALYPHGF-LCDGIQVSLDHSIYFHRPGD 90
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 755498806 188 ADHWMLYECESPWAGGSRGLVHGRLWR-RDGVLAVTCAQEGV 228
Cdd:pfam02551 91 LNKWILYDVESPSASGGRGLRQGRNFStQSGKLIASVQQEGL 132
|
|
| Thioesterase_II_repeat2 |
cd03445 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
9-51 |
5.68e-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: 5.68e-17
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 755498806 9 GDPKVPVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQ 51
Cdd:cd03445 52 GDPDQPIEYEVERLRDGRSFATRRVRAVQNGKVIFTATASFQR 94
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
128-228 |
7.68e-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: 7.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498806 128 FWVRARGYIGEGDIKMHCCVAAYISDYAFLGTALLPHQSKYkvnFMASLDHSMWFHAPFRADHWMLYECESPWAGGSRGL 207
Cdd:cd03440 3 LRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGL---GAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVT 79
|
90 100
....*....|....*....|.
gi 755498806 208 VHGRLWRRDGVLAVTCAQEGV 228
Cdd:cd03440 80 VEVEVRNEDGKLVATATATFV 100
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
9-50 |
6.48e-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: 6.48e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 755498806 9 GDPKVPVLYHVERIRTGASFSVRAVKAVQH-GKAIFICQASFQ 50
Cdd:cd00556 56 GDADEWLLYEVESLRDGRSRALRRGRAYQRdGKLVASATQSFL 98
|
|
| |
