NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|17531885|ref|NP_495075|]
View 

palmitoyl-CoA hydrolase [Caenorhabditis elegans]

Protein Classification

acyl-CoA thioesterase II( domain architecture ID 11488671)

acyl-coenzyme A thioesterase II catalyzes the hydrolysis of acyl-CoAs to the free fatty acid and CoA

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH