NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|115532456|ref|NP_001040743|]
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. ...
 27-317 7.16e-136

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: 386.33  E-value: 7.16e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456   27 TELKKDSFSPSTLSNGRQAHhGAAYGGLIFSQALAAAEKTVDEQFKPHSMHSYFILNVDTKEPISYNVRRIRDGRSFITR 106
Cdd:TIGR00189   1 EKIDENLFRGSHLSKGRQFL-NRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456  107 TVEAVQKDKVCFVLQCSFHvEEKSSIIHQSEMPKVPEPEvlmsmrDAVPYMKELVEKgevtpPPAMLARLQSYDSKVysd 186
Cdd:TIGR00189  80 RVKAVQHGKTIFTLQASFQ-AEKSGIEHQSTMPKVPPPE------SELPRENQLATK-----YPATLPRFLKHVVPF--- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456  187 dQDLFEMRCTNLGNYYGFASDkkPELYFWMRARGDLSNDERFHRWLIAYNSDSLLVSTAVSPHYTTGFCSSMLFSLDHCV 266
Cdd:TIGR00189 145 -ERPFEIRPVNLLNYLGGKED--PPQYVWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAGFCHSMAASLDHSI 221

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 115532456  267 WFHRsEVKADEWLLFECKSRIASGSRATIEGRIWRRDGVLIASCQQEALVR 317
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. ...
 27-317 7.16e-136

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: 386.33  E-value: 7.16e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456   27 TELKKDSFSPSTLSNGRQAHhGAAYGGLIFSQALAAAEKTVDEQFKPHSMHSYFILNVDTKEPISYNVRRIRDGRSFITR 106
Cdd:TIGR00189   1 EKIDENLFRGSHLSKGRQFL-NRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456  107 TVEAVQKDKVCFVLQCSFHvEEKSSIIHQSEMPKVPEPEvlmsmrDAVPYMKELVEKgevtpPPAMLARLQSYDSKVysd 186
Cdd:TIGR00189  80 RVKAVQHGKTIFTLQASFQ-AEKSGIEHQSTMPKVPPPE------SELPRENQLATK-----YPATLPRFLKHVVPF--- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456  187 dQDLFEMRCTNLGNYYGFASDkkPELYFWMRARGDLSNDERFHRWLIAYNSDSLLVSTAVSPHYTTGFCSSMLFSLDHCV 266
Cdd:TIGR00189 145 -ERPFEIRPVNLLNYLGGKED--PPQYVWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAGFCHSMAASLDHSI 221

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 115532456  267 WFHRsEVKADEWLLFECKSRIASGSRATIEGRIWRRDGVLIASCQQEALVR 317
Cdd:TIGR00189 222 WFHR-PFRADDWLLYKCSSPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
TesB COG1946
Acyl-CoA thioesterase [Lipid transport and metabolism];
47-317 1.65e-80

Acyl-CoA thioesterase [Lipid transport and metabolism];


Pssm-ID: 441549 [Multi-domain]  Cd Length: 273  Bit Score: 245.94  E-value: 1.65e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456  47 HGAAYGGLIFSQALAAAEKTVDEQFKPHSMHSYFILNVDTKEPISYNVRRIRDGRSFITRTVEAVQKDKVCFVLQCSFHV 126
Cdd:COG1946   29 LRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFSTRRVTAIQGGRVIFTATASFGV 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456 127 EEkSSIIHQSEMPKVPEPEVLMSMRDAVpyMKELVekgevtpPPAMLARLQSydskvysddqdlFEMRCTNLGNYYGfAS 206
Cdd:COG1946  109 PE-EGLEHQAPMPDVPPPEDLPSLPELL--IAGVL-------PLRFFAFLRP------------FDIRPVEGPLPFA-PP 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456 207 DKKPELYFWMRARGDLSNDERfHRWLIAYNSDSLLVSTAVSPHYTTGFCSSmlfSLDHCVWFHRsEVKADEWLLFECKSR 286
Cdd:COG1946  166 SGEPRQRVWMRARDPLPDDPL-HAALLAYASDATPPATALLSWLGPPLPAA---SLDHAMWFHR-PFRADDWLLYDADSP 240

                        250       260       270
                 ....*....|....*....|....*....|.
gi 115532456 287 IASGSRATIEGRIWRRDGVLIASCQQEALVR 317
Cdd:COG1946  241 SASGGRGLERGRIWDRDGRLVASSRQEGLVR 271
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 48-315 1.64e-67

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 216.90  E-value: 1.64e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456  48 GAAYGGLIFSQALAAAEKTVDEQFKPHSMHSYFILNVDTKEPISYNVRRIRDGRSFITRTVEAVQKDKVCFVLQCSFHVE 127
Cdd:PLN02868 158 GKVFGGQLVGQALAAASKTVDPLKLVHSLHAYFLLVGDINLPIIYQVERIRDGHNFATRRVDAIQKGKVIFTLFASFQKE 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456 128 EKsSIIHQ-SEMPKVPEPEVLMSmrdavpyMKELVEKgEVTPPpamlaRL-QSYDSKVYSDDQDLF--EMRCTNLGNYYG 203
Cdd:PLN02868 238 EQ-GFEHQeSTMPHVPPPETLLS-------REELRER-RLTDP-----RLpRSYRNKVAAKPFVPWpiEIRFCEPNNSTN 303

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456 204 fASDKKPELYFWMRARGDLSNDERFHRWLIAYNSDSLLVSTAVSPHYTTGFcSSMLFSLDHCVWFHRSeVKADEWLLFEC 283
Cdd:PLN02868 304 -QTKSPPRLRYWFRAKGKLSDDQALHRCVAAYASDLIFLGTSLNPHRTKGL-KFAALSLDHSMWFHRP-FRADDWLLFVI 380

                        250       260       270
                 ....*....|....*....|....*....|..
gi 115532456 284 KSRIASGSRATIEGRIWRRDGVLIASCQQEAL 315
Cdd:PLN02868 381 VSPAAHNGRGFATGHMFNRKGELVVSLTQEAL 412
4HBT_3 pfam13622
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 48-316 7.80e-54

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: 7.80e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456   48 GAAYGGLIFSQALAAAEKTVDEQFkPHSMHSYFILNVDTkEPISYNVRRIRDGRSFITRTVEAVQKDKVCFVLQCSFHVE 127
Cdd:pfam13622   9 RAPHGGYVAALLLRAAERTVPPDP-LHSLHVDFLRPVPP-GPVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456  128 EKSSIIHQS-EMPKVPEPEVLMSMRDAVPYmkelvekgevTPPPAMLARLQSydskvysddqdlFEMRCTNLGNyyGFAS 206
Cdd:pfam13622  87 RSSEWELTPaAPPPLPPPEDCPLAADEAPF----------PLFRRVPGFLDP------------FEPRFARGGG--PFSP 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456  207 DKKPELYFWMRARGDlsnDERFHRWLIAYNSDSLlvSTAVSPHYTTGFCSSMLFSLDHCVWFHRsEVKADEWLLFECKSR 286
Cdd:pfam13622 143 GGPGRVRLWVRLRDG---GEPDPLAALAYLADAF--PPRVLSLRLDPPASGWFPTLDLTVYFHR-RPPPGEWLLLRAETP 216

                         250       260       270
                  ....*....|....*....|....*....|
gi 115532456  287 IASGSRATIEGRIWRRDGVLIASCQQEALV 316
Cdd:pfam13622 217 VAGDGRGDVEARLWDEDGRLVATSRQEVLV 246
Thioesterase_II_repeat1 cd03444
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 212-316 1.45e-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: 145.08  E-value: 1.45e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456 212 LYFWMRARGDLSNDERFHRWLIAYNSDSLLVSTAVSPHYTTGFCSSMLFSLDHCVWFHRsEVKADEWLLFECKSRIASGS 291
Cdd:cd03444    1 LRVWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHGLPLFDASASASLDHAIWFHR-PFRADDWLLYEQRSPRAGNG 79

                         90       100
                 ....*....|....*....|....*
gi 115532456 292 RATIEGRIWRRDGVLIASCQQEALV 316
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. ...
 27-317 7.16e-136

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: 386.33  E-value: 7.16e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456   27 TELKKDSFSPSTLSNGRQAHhGAAYGGLIFSQALAAAEKTVDEQFKPHSMHSYFILNVDTKEPISYNVRRIRDGRSFITR 106
Cdd:TIGR00189   1 EKIDENLFRGSHLSKGRQFL-NRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456  107 TVEAVQKDKVCFVLQCSFHvEEKSSIIHQSEMPKVPEPEvlmsmrDAVPYMKELVEKgevtpPPAMLARLQSYDSKVysd 186
Cdd:TIGR00189  80 RVKAVQHGKTIFTLQASFQ-AEKSGIEHQSTMPKVPPPE------SELPRENQLATK-----YPATLPRFLKHVVPF--- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456  187 dQDLFEMRCTNLGNYYGFASDkkPELYFWMRARGDLSNDERFHRWLIAYNSDSLLVSTAVSPHYTTGFCSSMLFSLDHCV 266
Cdd:TIGR00189 145 -ERPFEIRPVNLLNYLGGKED--PPQYVWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAGFCHSMAASLDHSI 221

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 115532456  267 WFHRsEVKADEWLLFECKSRIASGSRATIEGRIWRRDGVLIASCQQEALVR 317
Cdd:TIGR00189 222 WFHR-PFRADDWLLYKCSSPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
TesB COG1946
Acyl-CoA thioesterase [Lipid transport and metabolism];
47-317 1.65e-80

Acyl-CoA thioesterase [Lipid transport and metabolism];


Pssm-ID: 441549 [Multi-domain]  Cd Length: 273  Bit Score: 245.94  E-value: 1.65e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456  47 HGAAYGGLIFSQALAAAEKTVDEQFKPHSMHSYFILNVDTKEPISYNVRRIRDGRSFITRTVEAVQKDKVCFVLQCSFHV 126
Cdd:COG1946   29 LRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFSTRRVTAIQGGRVIFTATASFGV 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456 127 EEkSSIIHQSEMPKVPEPEVLMSMRDAVpyMKELVekgevtpPPAMLARLQSydskvysddqdlFEMRCTNLGNYYGfAS 206
Cdd:COG1946  109 PE-EGLEHQAPMPDVPPPEDLPSLPELL--IAGVL-------PLRFFAFLRP------------FDIRPVEGPLPFA-PP 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456 207 DKKPELYFWMRARGDLSNDERfHRWLIAYNSDSLLVSTAVSPHYTTGFCSSmlfSLDHCVWFHRsEVKADEWLLFECKSR 286
Cdd:COG1946  166 SGEPRQRVWMRARDPLPDDPL-HAALLAYASDATPPATALLSWLGPPLPAA---SLDHAMWFHR-PFRADDWLLYDADSP 240

                        250       260       270
                 ....*....|....*....|....*....|.
gi 115532456 287 IASGSRATIEGRIWRRDGVLIASCQQEALVR 317
Cdd:COG1946  241 SASGGRGLERGRIWDRDGRLVASSRQEGLVR 271
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 48-315 1.64e-67

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 216.90  E-value: 1.64e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456  48 GAAYGGLIFSQALAAAEKTVDEQFKPHSMHSYFILNVDTKEPISYNVRRIRDGRSFITRTVEAVQKDKVCFVLQCSFHVE 127
Cdd:PLN02868 158 GKVFGGQLVGQALAAASKTVDPLKLVHSLHAYFLLVGDINLPIIYQVERIRDGHNFATRRVDAIQKGKVIFTLFASFQKE 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456 128 EKsSIIHQ-SEMPKVPEPEVLMSmrdavpyMKELVEKgEVTPPpamlaRL-QSYDSKVYSDDQDLF--EMRCTNLGNYYG 203
Cdd:PLN02868 238 EQ-GFEHQeSTMPHVPPPETLLS-------REELRER-RLTDP-----RLpRSYRNKVAAKPFVPWpiEIRFCEPNNSTN 303

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456 204 fASDKKPELYFWMRARGDLSNDERFHRWLIAYNSDSLLVSTAVSPHYTTGFcSSMLFSLDHCVWFHRSeVKADEWLLFEC 283
Cdd:PLN02868 304 -QTKSPPRLRYWFRAKGKLSDDQALHRCVAAYASDLIFLGTSLNPHRTKGL-KFAALSLDHSMWFHRP-FRADDWLLFVI 380

                        250       260       270
                 ....*....|....*....|....*....|..
gi 115532456 284 KSRIASGSRATIEGRIWRRDGVLIASCQQEAL 315
Cdd:PLN02868 381 VSPAAHNGRGFATGHMFNRKGELVVSLTQEAL 412
PRK10526 PRK10526
acyl-CoA thioesterase II; Provisional
 51-320 9.25e-56

acyl-CoA thioesterase II; Provisional


Pssm-ID: 182519 [Multi-domain]  Cd Length: 286  Bit Score: 182.64  E-value: 9.25e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456  51 YGGLIFSQALAAAEKTVDEQFKPHSMHSYFILNVDTKEPISYNVRRIRDGRSFITRTVEAVQKDKVCFVLQCSFHVEEkS 130
Cdd:PRK10526  35 FGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSQKPIIYDVETLRDGNSFSARRVAAIQNGKPIFYMTASFQAPE-A 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456 131 SIIHQSEMPKVPEPEVLMSMRDAVPYMKELVekgevtpPPAMlarlqsydSKVYSDDQDlFEMRCTNLGN-YYGFASdkK 209
Cdd:PRK10526 114 GFEHQKTMPSAPAPDGLPSETDIAQSLAHLL-------PPVL--------KDKFICDRP-LEIRPVEFHNpLKGHVA--E 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456 210 PELYFWMRARGDLSNDERFHRWLIAYNSDSLLVSTAVSPHyTTGFCSS--MLFSLDHCVWFHRSeVKADEWLLFECKSRI 287
Cdd:PRK10526 176 PVRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPH-GIGFLEPgmQIATIDHSMWFHRP-FNLNEWLLYSVESTS 253

                        250       260       270
                 ....*....|....*....|....*....|...
gi 115532456 288 ASGSRATIEGRIWRRDGVLIASCQQEALVRSKS 320
Cdd:PRK10526 254 ASSARGFVRGEFYTQDGVLVASTVQEGVMRNHN 286
4HBT_3 pfam13622
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 48-316 7.80e-54

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: 7.80e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456   48 GAAYGGLIFSQALAAAEKTVDEQFkPHSMHSYFILNVDTkEPISYNVRRIRDGRSFITRTVEAVQKDKVCFVLQCSFHVE 127
Cdd:pfam13622   9 RAPHGGYVAALLLRAAERTVPPDP-LHSLHVDFLRPVPP-GPVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456  128 EKSSIIHQS-EMPKVPEPEVLMSMRDAVPYmkelvekgevTPPPAMLARLQSydskvysddqdlFEMRCTNLGNyyGFAS 206
Cdd:pfam13622  87 RSSEWELTPaAPPPLPPPEDCPLAADEAPF----------PLFRRVPGFLDP------------FEPRFARGGG--PFSP 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456  207 DKKPELYFWMRARGDlsnDERFHRWLIAYNSDSLlvSTAVSPHYTTGFCSSMLFSLDHCVWFHRsEVKADEWLLFECKSR 286
Cdd:pfam13622 143 GGPGRVRLWVRLRDG---GEPDPLAALAYLADAF--PPRVLSLRLDPPASGWFPTLDLTVYFHR-RPPPGEWLLLRAETP 216

                         250       260       270
                  ....*....|....*....|....*....|
gi 115532456  287 IASGSRATIEGRIWRRDGVLIASCQQEALV 316
Cdd:pfam13622 217 VAGDGRGDVEARLWDEDGRLVATSRQEVLV 246
Thioesterase_II_repeat1 cd03444
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 212-316 1.45e-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: 145.08  E-value: 1.45e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456 212 LYFWMRARGDLSNDERFHRWLIAYNSDSLLVSTAVSPHYTTGFCSSMLFSLDHCVWFHRsEVKADEWLLFECKSRIASGS 291
Cdd:cd03444    1 LRVWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHGLPLFDASASASLDHAIWFHR-PFRADDWLLYEQRSPRAGNG 79

                         90       100
                 ....*....|....*....|....*
gi 115532456 292 RATIEGRIWRRDGVLIASCQQEALV 316
Cdd:cd03444   80 RGLVEGRIFTRDGELVASVAQEGLL 104
Thioesterase_II_repeat2 cd03445
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 32-126 1.09e-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: 1.09e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456  32 DSFSPSTLSNGRQaHHGAAYGGLIFSQALAAAEKTVDEQFKPHSMHSYFILNVDTKEPISYNVRRIRDGRSFITRTVEAV 111
Cdd:cd03445    1 DRFRGVSPPVPPG-QGRGVFGGQVLAQALVAAARTVPDDRVPHSLHSYFLRPGDPDQPIEYEVERLRDGRSFATRRVRAV 79

                         90
                 ....*....|....*
gi 115532456 112 QKDKVCFVLQCSFHV 126
Cdd:cd03445   80 QNGKVIFTATASFQR 94
Thioesterase_II cd00556
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 212-316 1.77e-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: 113.59  E-value: 1.77e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456 212 LYFWMRARGDLSNDERFHRWLIAYNSDSLLVSTAVSPHYTTGFCSsmlfsLDHCVWFHRSeVKADEWLLFECKSRIASGS 291
Cdd:cd00556    1 DRFWGRAPGPLPDDRRVFGGQLAAQSDLAALRTVPRPHGASGFAS-----LDHHIYFHRP-GDADEWLLYEVESLRDGRS 74

                         90       100
                 ....*....|....*....|....*
gi 115532456 292 RATIEGRIWRRDGVLIASCQQEALV 316
Cdd:cd00556   75 RALRRGRAYQRDGKLVASATQSFLV 99
Thioesterase_II cd00556
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 40-126 1.64e-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: 1.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456  40 SNGRQAHHGAAYGGLIFSQALAAAEKTVDE-----QFKPHSMHSYFILNVDTKEPISYNVRRIRDGRSFITRTVEAVQKD 114
Cdd:cd00556    7 APGPLPDDRRVFGGQLAAQSDLAALRTVPRphgasGFASLDHHIYFHRPGDADEWLLYEVESLRDGRSRALRRGRAYQRD 86

                         90
                 ....*....|...
gi 115532456 115 -KVCFVLQCSFHV 126
Cdd:cd00556   87 gKLVASATQSFLV 99
Acyl_CoA_thio pfam02551
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ...
 204-315 4.21e-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: 84.60  E-value: 4.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456  204 FASDKKPELYFWMRARGDLSNDERFHRWLIAYNSDSLLVSTAVSPHytTGFCSSMLFSLDHCVWFHRSeVKADEWLLFEC 283
Cdd:pfam02551  23 FGGQVVAHQQSWVAALGTVPDDPRLHSCALAYLSDLTLLLTALYPH--GFLCDGIQVSLDHSIYFHRP-GDLNKWILYDV 99

                          90       100       110
                  ....*....|....*....|....*....|...
gi 115532456  284 KSRIASGSRATIEGRIWR-RDGVLIASCQQEAL 315
Cdd:pfam02551 100 ESPSASGGRGLRQGRNFStQSGKLIASVQQEGL 132
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 214-315 9.94e-08

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: 9.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456 214 FWMRARGDLSNDERF-HRWLIAYNSDSLLVSTAvsphYTTGFCSSMLFSLDHCVWFHRsEVKADEWLLFECKSRIASGSR 292
Cdd:cd03440    3 LRLTVTPEDIDGGGIvHGGLLLALADEAAGAAA----ARLGGRGLGAVTLSLDVRFLR-PVRPGDTLTVEAEVVRVGRSS 77

                         90       100
                 ....*....|....*....|...
gi 115532456 293 ATIEGRIWRRDGVLIASCQQEAL 315
Cdd:cd03440   78 VTVEVEVRNEDGKLVATATATFV 100
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 46-124 5.54e-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: 5.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532456  46 HHGAAYGGLIFSQALAAAEKTVDEQFKP------HSMHSYFILNVDTKEPISYNVRRIRDGRSFITRTVEA-VQKDKVCF 118
Cdd:cd03440   14 GGGIVHGGLLLALADEAAGAAAARLGGRglgavtLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVrNEDGKLVA 93


                 ....*.
gi 115532456 119 VLQCSF 124
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