|
Name |
Accession |
Description |
Interval |
E-value |
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
3-224 |
1.49e-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: 275.39 E-value: 1.49e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498808 3 GDPKVPVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQmQPSPLQHQFSMPSVPPPEDlldhealidQYLRDPNL 82
Cdd:TIGR00189 57 GDPKKPIIYDVERLRDGRSFITRRVKAVQHGKTIFTLQASFQA-EKSGIEHQSTMPKVPPPES---------ELPRENQL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498808 83 HKKYRVGLNRVAAQEVP----IEIKVVNPPTLTQLQALePKQMFWVRARGYIGEgDIKMHCCVAAYISDYAFLGTALLPH 158
Cdd:TIGR00189 127 ATKYPATLPRFLKHVVPferpFEIRPVNLLNYLGGKED-PPQYVWRRARGSLPD-DPRLHQCALAYLSDLTLLPTALNPH 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755498808 159 QSKYKVNFM-ASLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVIR 224
Cdd:TIGR00189 205 NKAGFCHSMaASLDHSIWFHRPFRADDWLLYKCSSPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
3-223 |
2.48e-76 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 236.16 E-value: 2.48e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498808 3 GDPKVPVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQMQPSpLQHQFS-MPSVPPPEDLLDHEALIDQYLRDPN 81
Cdd:PLN02868 194 GDINLPIIYQVERIRDGHNFATRRVDAIQKGKVIFTLFASFQKEEQG-FEHQEStMPHVPPPETLLSREELRERRLTDPR 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498808 82 LHKKYRvglNRVAAQEV---PIEIKVVNPPTLTQLQALEPKQMFWVRARGYIGEgDIKMHCCVAAYISDYAFLGTALLPH 158
Cdd:PLN02868 273 LPRSYR---NKVAAKPFvpwPIEIRFCEPNNSTNQTKSPPRLRYWFRAKGKLSD-DQALHRCVAAYASDLIFLGTSLNPH 348
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755498808 159 QSKYKVNFMASLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVI 223
Cdd:PLN02868 349 RTKGLKFAALSLDHSMWFHRPFRADDWLLFVIVSPAAHNGRGFATGHMFNRKGELVVSLTQEALL 413
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
3-226 |
1.81e-74 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 226.68 E-value: 1.81e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498808 3 GDPKVPVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQMQPSpLQHQFSMPSVPPPEDLLD-HEALIDQYLRDpn 81
Cdd:COG1946 66 GDPDGPIEYEVERLRDGRSFSTRRVTAIQGGRVIFTATASFGVPEEG-LEHQAPMPDVPPPEDLPSlPELLIAGVLPL-- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498808 82 lhkkyrvglnRVAAQEVPIEIKVVNPPTLTQLQALEPKQMFWVRARGyiGEGDIKMHCCVAAYISDYAFLGTALLPHQSK 161
Cdd:COG1946 143 ----------RFFAFLRPFDIRPVEGPLPFAPPSGEPRQRVWMRARD--PLPDDPLHAALLAYASDATPPATALLSWLGP 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755498808 162 YKvnFMASLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVIRLK 226
Cdd:COG1946 211 PL--PAASLDHAMWFHRPFRADDWLLYDADSPSASGGRGLERGRIWDRDGRLVASSRQEGLVRGR 273
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
120-223 |
1.03e-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: 152.79 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498808 120 QMFWVRARGYIGEgDIKMHCCVAAYISDYAFLGTALLPHQSK-YKVNFMASLDHSMWFHAPFRADHWMLYECESPWAGGS 198
Cdd:cd03444 1 LRVWVRARGPLPD-DPRLHAAALAYLSDSLLLGTALRPHGLPlFDASASASLDHAIWFHRPFRADDWLLYEQRSPRAGNG 79
|
90 100
....*....|....*....|....*
gi 755498808 199 RGLVHGRLWRRDGVLAVTCAQEGVI 223
Cdd:cd03444 80 RGLVEGRIFTRDGELVASVAQEGLL 104
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
8-223 |
4.71e-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: 145.55 E-value: 4.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498808 8 PVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQMQPSPLQ-HQFSMPSVPPPEDLLDHealidqylRDPNLHKKY 86
Cdd:pfam13622 48 PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRLRSSEWElTPAAPPPLPPPEDCPLA--------ADEAPFPLF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498808 87 RVGLNRVAaqevPIEIKVVNPPTLTQlQALEPKQMFWVRARgyigEGDIKMHCCVAAYISDyAFLGTALLPHQSKYKVNF 166
Cdd:pfam13622 120 RRVPGFLD----PFEPRFARGGGPFS-PGGPGRVRLWVRLR----DGGEPDPLAALAYLAD-AFPPRVLSLRLDPPASGW 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 755498808 167 MASLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVI 223
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. ... |
3-224 |
1.49e-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: 275.39 E-value: 1.49e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498808 3 GDPKVPVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQmQPSPLQHQFSMPSVPPPEDlldhealidQYLRDPNL 82
Cdd:TIGR00189 57 GDPKKPIIYDVERLRDGRSFITRRVKAVQHGKTIFTLQASFQA-EKSGIEHQSTMPKVPPPES---------ELPRENQL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498808 83 HKKYRVGLNRVAAQEVP----IEIKVVNPPTLTQLQALePKQMFWVRARGYIGEgDIKMHCCVAAYISDYAFLGTALLPH 158
Cdd:TIGR00189 127 ATKYPATLPRFLKHVVPferpFEIRPVNLLNYLGGKED-PPQYVWRRARGSLPD-DPRLHQCALAYLSDLTLLPTALNPH 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755498808 159 QSKYKVNFM-ASLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVIR 224
Cdd:TIGR00189 205 NKAGFCHSMaASLDHSIWFHRPFRADDWLLYKCSSPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
3-223 |
2.48e-76 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 236.16 E-value: 2.48e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498808 3 GDPKVPVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQMQPSpLQHQFS-MPSVPPPEDLLDHEALIDQYLRDPN 81
Cdd:PLN02868 194 GDINLPIIYQVERIRDGHNFATRRVDAIQKGKVIFTLFASFQKEEQG-FEHQEStMPHVPPPETLLSREELRERRLTDPR 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498808 82 LHKKYRvglNRVAAQEV---PIEIKVVNPPTLTQLQALEPKQMFWVRARGYIGEgDIKMHCCVAAYISDYAFLGTALLPH 158
Cdd:PLN02868 273 LPRSYR---NKVAAKPFvpwPIEIRFCEPNNSTNQTKSPPRLRYWFRAKGKLSD-DQALHRCVAAYASDLIFLGTSLNPH 348
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755498808 159 QSKYKVNFMASLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVI 223
Cdd:PLN02868 349 RTKGLKFAALSLDHSMWFHRPFRADDWLLFVIVSPAAHNGRGFATGHMFNRKGELVVSLTQEALL 413
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
3-226 |
1.81e-74 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 226.68 E-value: 1.81e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498808 3 GDPKVPVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQMQPSpLQHQFSMPSVPPPEDLLD-HEALIDQYLRDpn 81
Cdd:COG1946 66 GDPDGPIEYEVERLRDGRSFSTRRVTAIQGGRVIFTATASFGVPEEG-LEHQAPMPDVPPPEDLPSlPELLIAGVLPL-- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498808 82 lhkkyrvglnRVAAQEVPIEIKVVNPPTLTQLQALEPKQMFWVRARGyiGEGDIKMHCCVAAYISDYAFLGTALLPHQSK 161
Cdd:COG1946 143 ----------RFFAFLRPFDIRPVEGPLPFAPPSGEPRQRVWMRARD--PLPDDPLHAALLAYASDATPPATALLSWLGP 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755498808 162 YKvnFMASLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVIRLK 226
Cdd:COG1946 211 PL--PAASLDHAMWFHRPFRADDWLLYDADSPSASGGRGLERGRIWDRDGRLVASSRQEGLVRGR 273
|
|
| PRK10526 |
PRK10526 |
acyl-CoA thioesterase II; Provisional |
3-227 |
7.41e-57 |
|
acyl-CoA thioesterase II; Provisional
Pssm-ID: 182519 [Multi-domain] Cd Length: 286 Bit Score: 182.26 E-value: 7.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498808 3 GDPKVPVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQMQPSpLQHQFSMPSVPPPEDLLDHEALIDQ--YLRDP 80
Cdd:PRK10526 68 GDSQKPIIYDVETLRDGNSFSARRVAAIQNGKPIFYMTASFQAPEAG-FEHQKTMPSAPAPDGLPSETDIAQSlaHLLPP 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498808 81 NLHKKYrvglnrvaAQEVPIEIKVV---NPptlTQLQALEPKQMFWVRARGYIGEgDIKMHCCVAAYISDYAFLGTALLP 157
Cdd:PRK10526 147 VLKDKF--------ICDRPLEIRPVefhNP---LKGHVAEPVRQVWIRANGSVPD-DLRVHQYLLGYASDLNFLPVALQP 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755498808 158 HQSKYKVNFM--ASLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVIRLKP 227
Cdd:PRK10526 215 HGIGFLEPGMqiATIDHSMWFHRPFNLNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMRNHN 286
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
120-223 |
1.03e-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: 152.79 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498808 120 QMFWVRARGYIGEgDIKMHCCVAAYISDYAFLGTALLPHQSK-YKVNFMASLDHSMWFHAPFRADHWMLYECESPWAGGS 198
Cdd:cd03444 1 LRVWVRARGPLPD-DPRLHAAALAYLSDSLLLGTALRPHGLPlFDASASASLDHAIWFHRPFRADDWLLYEQRSPRAGNG 79
|
90 100
....*....|....*....|....*
gi 755498808 199 RGLVHGRLWRRDGVLAVTCAQEGVI 223
Cdd:cd03444 80 RGLVEGRIFTRDGELVASVAQEGLL 104
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
8-223 |
4.71e-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: 145.55 E-value: 4.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498808 8 PVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQMQPSPLQ-HQFSMPSVPPPEDLLDHealidqylRDPNLHKKY 86
Cdd:pfam13622 48 PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRLRSSEWElTPAAPPPLPPPEDCPLA--------ADEAPFPLF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498808 87 RVGLNRVAaqevPIEIKVVNPPTLTQlQALEPKQMFWVRARgyigEGDIKMHCCVAAYISDyAFLGTALLPHQSKYKVNF 166
Cdd:pfam13622 120 RRVPGFLD----PFEPRFARGGGPFS-PGGPGRVRLWVRLR----DGGEPDPLAALAYLAD-AFPPRVLSLRLDPPASGW 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 755498808 167 MASLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVI 223
Cdd:pfam13622 190 FPTLDLTVYFHRRPPPGEWLLLRAETPVAGDGRGDVEARLWDEDGRLVATSRQEVLV 246
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
120-223 |
2.45e-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: 123.61 E-value: 2.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498808 120 QMFWVRARGYIGeGDIKMHCCVAAYISDYAFLGTALLPHQSKykvnFMASLDHSMWFHAPFRADHWMLYECESPWAGGSR 199
Cdd:cd00556 1 DRFWGRAPGPLP-DDRRVFGGQLAAQSDLAALRTVPRPHGAS----GFASLDHHIYFHRPGDADEWLLYEVESLRDGRSR 75
|
90 100
....*....|....*....|....
gi 755498808 200 GLVHGRLWRRDGVLAVTCAQEGVI 223
Cdd:cd00556 76 ALRRGRAYQRDGKLVASATQSFLV 99
|
|
| Acyl_CoA_thio |
pfam02551 |
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ... |
105-222 |
1.78e-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: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498808 105 VNPPTLTQL---QALEPKQMfWVRARGYIGEgDIKMHCCVAAYISDYAFLGTALLPHQSkYKVNFMASLDHSMWFHAPFR 181
Cdd:pfam02551 14 VRPGELRRTfggQVVAHQQS-WVAALGTVPD-DPRLHSCALAYLSDLTLLLTALYPHGF-LCDGIQVSLDHSIYFHRPGD 90
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 755498808 182 ADHWMLYECESPWAGGSRGLVHGRLWR-RDGVLAVTCAQEGV 222
Cdd:pfam02551 91 LNKWILYDVESPSASGGRGLRQGRNFStQSGKLIASVQQEGL 132
|
|
| Thioesterase_II_repeat2 |
cd03445 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
3-45 |
5.24e-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: 5.24e-17
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 755498808 3 GDPKVPVLYHVERIRTGASFSVRAVKAVQHGKAIFICQASFQQ 45
Cdd:cd03445 52 GDPDQPIEYEVERLRDGRSFATRRVRAVQNGKVIFTATASFQR 94
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
122-222 |
8.60e-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: 8.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498808 122 FWVRARGYIGEGDIKMHCCVAAYISDYAFLGTALLPHQSKYkvnFMASLDHSMWFHAPFRADHWMLYECESPWAGGSRGL 201
Cdd:cd03440 3 LRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGL---GAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVT 79
|
90 100
....*....|....*....|.
gi 755498808 202 VHGRLWRRDGVLAVTCAQEGV 222
Cdd:cd03440 80 VEVEVRNEDGKLVATATATFV 100
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
3-44 |
6.51e-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: 49.26 E-value: 6.51e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 755498808 3 GDPKVPVLYHVERIRTGASFSVRAVKAVQH-GKAIFICQASFQ 44
Cdd:cd00556 56 GDADEWLLYEVESLRDGRSRALRRGRAYQRdGKLVASATQSFL 98
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