|
Name |
Accession |
Description |
Interval |
E-value |
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
58-348 |
5.12e-135 |
|
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: 385.56 E-value: 5.12e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 58 TELKKDSFSPSTLSNGRQAHhGAAYGGLIFSQALAAAEKTVDEQFKPHSMHSYFILNVDTKEPISYNVRRIRDGRSFITR 137
Cdd:TIGR00189 1 EKIDENLFRGSHLSKGRQFL-NRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 138 TVEAVQKDKVCFVLQCSFHvEEKSSIIHQSEMPKVPEPEvlmsmrDAVPYMKELVEKgevtpPPAMLARLQSYDSKVysd 217
Cdd:TIGR00189 80 RVKAVQHGKTIFTLQASFQ-AEKSGIEHQSTMPKVPPPE------SELPRENQLATK-----YPATLPRFLKHVVPF--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 218 dQDLFEMRCTNLGNYYGFASDkkPELYFWMRARGDLSNDERFHRWLIAYNSDSLLVSTAVSPHYTTGFCSSMLFSLDHCV 297
Cdd:TIGR00189 145 -ERPFEIRPVNLLNYLGGKED--PPQYVWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAGFCHSMAASLDHSI 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 17531885 298 WFHRsEVKADEWLLFECKSRIASGSRATIEGRIWRRDGVLIASCQQEALVR 348
Cdd:TIGR00189 222 WFHR-PFRADDWLLYKCSSPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
78-348 |
4.59e-80 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 245.94 E-value: 4.59e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 78 HGAAYGGLIFSQALAAAEKTVDEQFKPHSMHSYFILNVDTKEPISYNVRRIRDGRSFITRTVEAVQKDKVCFVLQCSFHV 157
Cdd:COG1946 29 LRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFSTRRVTAIQGGRVIFTATASFGV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 158 EEkSSIIHQSEMPKVPEPEVLMSMRDAVpyMKELVekgevtpPPAMLARLQSydskvysddqdlFEMRCTNLGNYYGfAS 237
Cdd:COG1946 109 PE-EGLEHQAPMPDVPPPEDLPSLPELL--IAGVL-------PLRFFAFLRP------------FDIRPVEGPLPFA-PP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 238 DKKPELYFWMRARGDLSNDERfHRWLIAYNSDSLLVSTAVSPHYTTGFCSSmlfSLDHCVWFHRsEVKADEWLLFECKSR 317
Cdd:COG1946 166 SGEPRQRVWMRARDPLPDDPL-HAALLAYASDATPPATALLSWLGPPLPAA---SLDHAMWFHR-PFRADDWLLYDADSP 240
|
250 260 270
....*....|....*....|....*....|.
gi 17531885 318 IASGSRATIEGRIWRRDGVLIASCQQEALVR 348
Cdd:COG1946 241 SASGGRGLERGRIWDRDGRLVASSRQEGLVR 271
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
79-346 |
5.05e-67 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 216.90 E-value: 5.05e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 79 GAAYGGLIFSQALAAAEKTVDEQFKPHSMHSYFILNVDTKEPISYNVRRIRDGRSFITRTVEAVQKDKVCFVLQCSFHVE 158
Cdd:PLN02868 158 GKVFGGQLVGQALAAASKTVDPLKLVHSLHAYFLLVGDINLPIIYQVERIRDGHNFATRRVDAIQKGKVIFTLFASFQKE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 159 EKsSIIHQ-SEMPKVPEPEVLMSmrdavpyMKELVEKgEVTPPpamlaRL-QSYDSKVYSDDQDLF--EMRCTNLGNYYG 234
Cdd:PLN02868 238 EQ-GFEHQeSTMPHVPPPETLLS-------REELRER-RLTDP-----RLpRSYRNKVAAKPFVPWpiEIRFCEPNNSTN 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 235 fASDKKPELYFWMRARGDLSNDERFHRWLIAYNSDSLLVSTAVSPHYTTGFcSSMLFSLDHCVWFHRSeVKADEWLLFEC 314
Cdd:PLN02868 304 -QTKSPPRLRYWFRAKGKLSDDQALHRCVAAYASDLIFLGTSLNPHRTKGL-KFAALSLDHSMWFHRP-FRADDWLLFVI 380
|
250 260 270
....*....|....*....|....*....|..
gi 17531885 315 KSRIASGSRATIEGRIWRRDGVLIASCQQEAL 346
Cdd:PLN02868 381 VSPAAHNGRGFATGHMFNRKGELVVSLTQEAL 412
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
79-347 |
1.89e-53 |
|
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: 176.37 E-value: 1.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 79 GAAYGGLIFSQALAAAEKTVDEQFkPHSMHSYFILNVDTkEPISYNVRRIRDGRSFITRTVEAVQKDKVCFVLQCSFHVE 158
Cdd:pfam13622 9 RAPHGGYVAALLLRAAERTVPPDP-LHSLHVDFLRPVPP-GPVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 159 EKSSIIHQS-EMPKVPEPEVLMSMRDAVPYmkelvekgevTPPPAMLARLQSydskvysddqdlFEMRCTNLGNyyGFAS 237
Cdd:pfam13622 87 RSSEWELTPaAPPPLPPPEDCPLAADEAPF----------PLFRRVPGFLDP------------FEPRFARGGG--PFSP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 238 DKKPELYFWMRARGDlsnDERFHRWLIAYNSDSLlvSTAVSPHYTTGFCSSMLFSLDHCVWFHRsEVKADEWLLFECKSR 317
Cdd:pfam13622 143 GGPGRVRLWVRLRDG---GEPDPLAALAYLADAF--PPRVLSLRLDPPASGWFPTLDLTVYFHR-RPPPGEWLLLRAETP 216
|
250 260 270
....*....|....*....|....*....|
gi 17531885 318 IASGSRATIEGRIWRRDGVLIASCQQEALV 347
Cdd:pfam13622 217 VAGDGRGDVEARLWDEDGRLVATSRQEVLV 246
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
243-347 |
4.47e-43 |
|
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: 144.70 E-value: 4.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 243 LYFWMRARGDLSNDERFHRWLIAYNSDSLLVSTAVSPHYTTGFCSSMLFSLDHCVWFHRsEVKADEWLLFECKSRIASGS 322
Cdd:cd03444 1 LRVWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHGLPLFDASASASLDHAIWFHR-PFRADDWLLYEQRSPRAGNG 79
|
90 100
....*....|....*....|....*
gi 17531885 323 RATIEGRIWRRDGVLIASCQQEALV 347
Cdd:cd03444 80 RGLVEGRIFTRDGELVASVAQEGLL 104
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
58-348 |
5.12e-135 |
|
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: 385.56 E-value: 5.12e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 58 TELKKDSFSPSTLSNGRQAHhGAAYGGLIFSQALAAAEKTVDEQFKPHSMHSYFILNVDTKEPISYNVRRIRDGRSFITR 137
Cdd:TIGR00189 1 EKIDENLFRGSHLSKGRQFL-NRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 138 TVEAVQKDKVCFVLQCSFHvEEKSSIIHQSEMPKVPEPEvlmsmrDAVPYMKELVEKgevtpPPAMLARLQSYDSKVysd 217
Cdd:TIGR00189 80 RVKAVQHGKTIFTLQASFQ-AEKSGIEHQSTMPKVPPPE------SELPRENQLATK-----YPATLPRFLKHVVPF--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 218 dQDLFEMRCTNLGNYYGFASDkkPELYFWMRARGDLSNDERFHRWLIAYNSDSLLVSTAVSPHYTTGFCSSMLFSLDHCV 297
Cdd:TIGR00189 145 -ERPFEIRPVNLLNYLGGKED--PPQYVWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAGFCHSMAASLDHSI 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 17531885 298 WFHRsEVKADEWLLFECKSRIASGSRATIEGRIWRRDGVLIASCQQEALVR 348
Cdd:TIGR00189 222 WFHR-PFRADDWLLYKCSSPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
78-348 |
4.59e-80 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 245.94 E-value: 4.59e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 78 HGAAYGGLIFSQALAAAEKTVDEQFKPHSMHSYFILNVDTKEPISYNVRRIRDGRSFITRTVEAVQKDKVCFVLQCSFHV 157
Cdd:COG1946 29 LRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFSTRRVTAIQGGRVIFTATASFGV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 158 EEkSSIIHQSEMPKVPEPEVLMSMRDAVpyMKELVekgevtpPPAMLARLQSydskvysddqdlFEMRCTNLGNYYGfAS 237
Cdd:COG1946 109 PE-EGLEHQAPMPDVPPPEDLPSLPELL--IAGVL-------PLRFFAFLRP------------FDIRPVEGPLPFA-PP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 238 DKKPELYFWMRARGDLSNDERfHRWLIAYNSDSLLVSTAVSPHYTTGFCSSmlfSLDHCVWFHRsEVKADEWLLFECKSR 317
Cdd:COG1946 166 SGEPRQRVWMRARDPLPDDPL-HAALLAYASDATPPATALLSWLGPPLPAA---SLDHAMWFHR-PFRADDWLLYDADSP 240
|
250 260 270
....*....|....*....|....*....|.
gi 17531885 318 IASGSRATIEGRIWRRDGVLIASCQQEALVR 348
Cdd:COG1946 241 SASGGRGLERGRIWDRDGRLVASSRQEGLVR 271
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
79-346 |
5.05e-67 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 216.90 E-value: 5.05e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 79 GAAYGGLIFSQALAAAEKTVDEQFKPHSMHSYFILNVDTKEPISYNVRRIRDGRSFITRTVEAVQKDKVCFVLQCSFHVE 158
Cdd:PLN02868 158 GKVFGGQLVGQALAAASKTVDPLKLVHSLHAYFLLVGDINLPIIYQVERIRDGHNFATRRVDAIQKGKVIFTLFASFQKE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 159 EKsSIIHQ-SEMPKVPEPEVLMSmrdavpyMKELVEKgEVTPPpamlaRL-QSYDSKVYSDDQDLF--EMRCTNLGNYYG 234
Cdd:PLN02868 238 EQ-GFEHQeSTMPHVPPPETLLS-------REELRER-RLTDP-----RLpRSYRNKVAAKPFVPWpiEIRFCEPNNSTN 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 235 fASDKKPELYFWMRARGDLSNDERFHRWLIAYNSDSLLVSTAVSPHYTTGFcSSMLFSLDHCVWFHRSeVKADEWLLFEC 314
Cdd:PLN02868 304 -QTKSPPRLRYWFRAKGKLSDDQALHRCVAAYASDLIFLGTSLNPHRTKGL-KFAALSLDHSMWFHRP-FRADDWLLFVI 380
|
250 260 270
....*....|....*....|....*....|..
gi 17531885 315 KSRIASGSRATIEGRIWRRDGVLIASCQQEAL 346
Cdd:PLN02868 381 VSPAAHNGRGFATGHMFNRKGELVVSLTQEAL 412
|
|
| PRK10526 |
PRK10526 |
acyl-CoA thioesterase II; Provisional |
82-351 |
2.40e-55 |
|
acyl-CoA thioesterase II; Provisional
Pssm-ID: 182519 [Multi-domain] Cd Length: 286 Bit Score: 182.64 E-value: 2.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 82 YGGLIFSQALAAAEKTVDEQFKPHSMHSYFILNVDTKEPISYNVRRIRDGRSFITRTVEAVQKDKVCFVLQCSFHVEEkS 161
Cdd:PRK10526 35 FGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSQKPIIYDVETLRDGNSFSARRVAAIQNGKPIFYMTASFQAPE-A 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 162 SIIHQSEMPKVPEPEVLMSMRDAVPYMKELVekgevtpPPAMlarlqsydSKVYSDDQDlFEMRCTNLGN-YYGFASdkK 240
Cdd:PRK10526 114 GFEHQKTMPSAPAPDGLPSETDIAQSLAHLL-------PPVL--------KDKFICDRP-LEIRPVEFHNpLKGHVA--E 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 241 PELYFWMRARGDLSNDERFHRWLIAYNSDSLLVSTAVSPHyTTGFCSS--MLFSLDHCVWFHRSeVKADEWLLFECKSRI 318
Cdd:PRK10526 176 PVRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPH-GIGFLEPgmQIATIDHSMWFHRP-FNLNEWLLYSVESTS 253
|
250 260 270
....*....|....*....|....*....|...
gi 17531885 319 ASGSRATIEGRIWRRDGVLIASCQQEALVRSKS 351
Cdd:PRK10526 254 ASSARGFVRGEFYTQDGVLVASTVQEGVMRNHN 286
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
79-347 |
1.89e-53 |
|
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: 176.37 E-value: 1.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 79 GAAYGGLIFSQALAAAEKTVDEQFkPHSMHSYFILNVDTkEPISYNVRRIRDGRSFITRTVEAVQKDKVCFVLQCSFHVE 158
Cdd:pfam13622 9 RAPHGGYVAALLLRAAERTVPPDP-LHSLHVDFLRPVPP-GPVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 159 EKSSIIHQS-EMPKVPEPEVLMSMRDAVPYmkelvekgevTPPPAMLARLQSydskvysddqdlFEMRCTNLGNyyGFAS 237
Cdd:pfam13622 87 RSSEWELTPaAPPPLPPPEDCPLAADEAPF----------PLFRRVPGFLDP------------FEPRFARGGG--PFSP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 238 DKKPELYFWMRARGDlsnDERFHRWLIAYNSDSLlvSTAVSPHYTTGFCSSMLFSLDHCVWFHRsEVKADEWLLFECKSR 317
Cdd:pfam13622 143 GGPGRVRLWVRLRDG---GEPDPLAALAYLADAF--PPRVLSLRLDPPASGWFPTLDLTVYFHR-RPPPGEWLLLRAETP 216
|
250 260 270
....*....|....*....|....*....|
gi 17531885 318 IASGSRATIEGRIWRRDGVLIASCQQEALV 347
Cdd:pfam13622 217 VAGDGRGDVEARLWDEDGRLVATSRQEVLV 246
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
243-347 |
4.47e-43 |
|
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: 144.70 E-value: 4.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 243 LYFWMRARGDLSNDERFHRWLIAYNSDSLLVSTAVSPHYTTGFCSSMLFSLDHCVWFHRsEVKADEWLLFECKSRIASGS 322
Cdd:cd03444 1 LRVWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHGLPLFDASASASLDHAIWFHR-PFRADDWLLYEQRSPRAGNG 79
|
90 100
....*....|....*....|....*
gi 17531885 323 RATIEGRIWRRDGVLIASCQQEALV 347
Cdd:cd03444 80 RGLVEGRIFTRDGELVASVAQEGLL 104
|
|
| Thioesterase_II_repeat2 |
cd03445 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
63-157 |
2.28e-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: 239529 [Multi-domain] Cd Length: 94 Bit Score: 137.37 E-value: 2.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 63 DSFSPSTLSNGRQaHHGAAYGGLIFSQALAAAEKTVDEQFKPHSMHSYFILNVDTKEPISYNVRRIRDGRSFITRTVEAV 142
Cdd:cd03445 1 DRFRGVSPPVPPG-QGRGVFGGQVLAQALVAAARTVPDDRVPHSLHSYFLRPGDPDQPIEYEVERLRDGRSFATRRVRAV 79
|
90
....*....|....*
gi 17531885 143 QKDKVCFVLQCSFHV 157
Cdd:cd03445 80 QNGKVIFTATASFQR 94
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
243-347 |
2.90e-31 |
|
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: 113.98 E-value: 2.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 243 LYFWMRARGDLSNDERFHRWLIAYNSDSLLVSTAVSPHYTTGFCSsmlfsLDHCVWFHRSeVKADEWLLFECKSRIASGS 322
Cdd:cd00556 1 DRFWGRAPGPLPDDRRVFGGQLAAQSDLAALRTVPRPHGASGFAS-----LDHHIYFHRP-GDADEWLLYEVESLRDGRS 74
|
90 100
....*....|....*....|....*
gi 17531885 323 RATIEGRIWRRDGVLIASCQQEALV 347
Cdd:cd00556 75 RALRRGRAYQRDGKLVASATQSFLV 99
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
71-157 |
2.18e-20 |
|
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: 84.70 E-value: 2.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 71 SNGRQAHHGAAYGGLIFSQALAAAEKTVDE-----QFKPHSMHSYFILNVDTKEPISYNVRRIRDGRSFITRTVEAVQKD 145
Cdd:cd00556 7 APGPLPDDRRVFGGQLAAQSDLAALRTVPRphgasGFASLDHHIYFHRPGDADEWLLYEVESLRDGRSRALRRGRAYQRD 86
|
90
....*....|...
gi 17531885 146 -KVCFVLQCSFHV 157
Cdd:cd00556 87 gKLVASATQSFLV 99
|
|
| Acyl_CoA_thio |
pfam02551 |
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ... |
235-346 |
9.81e-20 |
|
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: 84.22 E-value: 9.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 235 FASDKKPELYFWMRARGDLSNDERFHRWLIAYNSDSLLVSTAVSPHytTGFCSSMLFSLDHCVWFHRSeVKADEWLLFEC 314
Cdd:pfam02551 23 FGGQVVAHQQSWVAALGTVPDDPRLHSCALAYLSDLTLLLTALYPH--GFLCDGIQVSLDHSIYFHRP-GDLNKWILYDV 99
|
90 100 110
....*....|....*....|....*....|...
gi 17531885 315 KSRIASGSRATIEGRIWR-RDGVLIASCQQEAL 346
Cdd:pfam02551 100 ESPSASGGRGLRQGRNFStQSGKLIASVQQEGL 132
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
245-346 |
1.09e-07 |
|
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: 49.40 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 245 FWMRARGDLSNDERF-HRWLIAYNSDSLLVSTAvsphYTTGFCSSMLFSLDHCVWFHRsEVKADEWLLFECKSRIASGSR 323
Cdd:cd03440 3 LRLTVTPEDIDGGGIvHGGLLLALADEAAGAAA----ARLGGRGLGAVTLSLDVRFLR-PVRPGDTLTVEAEVVRVGRSS 77
|
90 100
....*....|....*....|...
gi 17531885 324 ATIEGRIWRRDGVLIASCQQEAL 346
Cdd:cd03440 78 VTVEVEVRNEDGKLVATATATFV 100
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
77-155 |
6.15e-05 |
|
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: 41.69 E-value: 6.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531885 77 HHGAAYGGLIFSQALAAAEKTVDEQFKP------HSMHSYFILNVDTKEPISYNVRRIRDGRSFITRTVEA-VQKDKVCF 149
Cdd:cd03440 14 GGGIVHGGLLLALADEAAGAAAARLGGRglgavtLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVrNEDGKLVA 93
|
....*.
gi 17531885 150 VLQCSF 155
Cdd:cd03440 94 TATATF 99
|
|
|