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Conserved domains on  [gi|805282394|emb|CRF26501|]
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acyl-CoA thioesterase [Mycobacterium tuberculosis]

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

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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. ...
 10-271 4.80e-138

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: 390.18  E-value: 4.80e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394   10 EQLEVNIYRGSVFSPESGFLQRTFGGHVAGQSLVSAVRTVDPRYMVHSLHGYFLRPGDAKERTVFLVERIRDGGSFCTRR 89
Cdd:TIGR00189   1 EKIDENLFRGSHLSKGRQFLNRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394   90 VNAVQHGETIFSMAASFQTEQEGITHQDVMPAAPPPD-GLPGLNSIKVFDDAGFRQFD------EWDVCIVPRERLRLLP 162
Cdd:TIGR00189  81 VKAVQHGKTIFTLQASFQAEKSGIEHQSTMPKVPPPEsELPRENQLATKYPATLPRFLkhvvpfERPFEIRPVNLLNYLG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394  163 GKAS-QQQVWLRHRDPLPDDPVLHICALAYMSDLTLLGSAQVNHLDVR-DQLQVASLDHAMWFMRPFRADEWLLYDQSSP 240
Cdd:TIGR00189 161 GKEDpPQYVWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAGfCHSMAASLDHSIWFHRPFRADDWLLYKCSSP 240

                         250       260       270
                  ....*....|....*....|....*....|.
gi 805282394  241 SASGGRALTRGEIFTRSGEMVAAVMQEGLTR 271
Cdd:TIGR00189 241 SAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
 
Name Accession Description Interval E-value
tesB TIGR00189
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ...
 10-271 4.80e-138

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: 390.18  E-value: 4.80e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394   10 EQLEVNIYRGSVFSPESGFLQRTFGGHVAGQSLVSAVRTVDPRYMVHSLHGYFLRPGDAKERTVFLVERIRDGGSFCTRR 89
Cdd:TIGR00189   1 EKIDENLFRGSHLSKGRQFLNRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394   90 VNAVQHGETIFSMAASFQTEQEGITHQDVMPAAPPPD-GLPGLNSIKVFDDAGFRQFD------EWDVCIVPRERLRLLP 162
Cdd:TIGR00189  81 VKAVQHGKTIFTLQASFQAEKSGIEHQSTMPKVPPPEsELPRENQLATKYPATLPRFLkhvvpfERPFEIRPVNLLNYLG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394  163 GKAS-QQQVWLRHRDPLPDDPVLHICALAYMSDLTLLGSAQVNHLDVR-DQLQVASLDHAMWFMRPFRADEWLLYDQSSP 240
Cdd:TIGR00189 161 GKEDpPQYVWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAGfCHSMAASLDHSIWFHRPFRADDWLLYKCSSP 240

                         250       260       270
                  ....*....|....*....|....*....|.
gi 805282394  241 SASGGRALTRGEIFTRSGEMVAAVMQEGLTR 271
Cdd:TIGR00189 241 SAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
TesB COG1946
Acyl-CoA thioesterase [Lipid transport and metabolism];
1-273 1.91e-116

Acyl-CoA thioesterase [Lipid transport and metabolism];


Pssm-ID: 441549 [Multi-domain]  Cd Length: 273  Bit Score: 335.31  E-value: 1.91e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394   1 MSIEEILDLEQLEVNIYRGSVfsPESGFLQRTFGGHVAGQSLVSAVRTVDPRYMVHSLHGYFLRPGDAKERTVFLVERIR 80
Cdd:COG1946    3 MELLDLLDLERLEDGLFRGEI--SPDQGLRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394  81 DGGSFCTRRVNAVQHGETIFSMAASFQTEQEGITHQDVMPAAPPPDGLPGLNSIKVFDDAGFRQFDEW---DVCIVPRER 157
Cdd:COG1946   81 DGRSFSTRRVTAIQGGRVIFTATASFGVPEEGLEHQAPMPDVPPPEDLPSLPELLIAGVLPLRFFAFLrpfDIRPVEGPL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394 158 LRLLPGKASQQQVWLRHRDPLPDDPvLHICALAYMSDLTLLGSAQVNHLDvrDQLQVASLDHAMWFMRPFRADEWLLYDQ 237
Cdd:COG1946  161 PFAPPSGEPRQRVWMRARDPLPDDP-LHAALLAYASDATPPATALLSWLG--PPLPAASLDHAMWFHRPFRADDWLLYDA 237

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 805282394 238 SSPSASGGRALTRGEIFTRSGEMVAAVMQEGLTRHR 273
Cdd:COG1946  238 DSPSASGGRGLERGRIWDRDGRLVASSRQEGLVRGR 273
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 3-269 1.42e-81

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 251.56  E-value: 1.42e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394   3 IEEILDLEQLEVNIYRGsVFSPESGFLQRTFGGHVAGQSLVSAVRTVDPRYMVHSLHGYFLRPGDAKERTVFLVERIRDG 82
Cdd:PLN02868 132 VERILHLEPLEVDIFRG-ITLPDAPTFGKVFGGQLVGQALAAASKTVDPLKLVHSLHAYFLLVGDINLPIIYQVERIRDG 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394  83 GSFCTRRVNAVQHGETIFSMAASFQTEQEGITHQ-DVMPAAPPPDGLPGLNSI--KVFDDAGF----------RQFDEWD 149
Cdd:PLN02868 211 HNFATRRVDAIQKGKVIFTLFASFQKEEQGFEHQeSTMPHVPPPETLLSREELreRRLTDPRLprsyrnkvaaKPFVPWP 290

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394 150 VCIVPRERLRLLPGKAS--QQQVWLRHRDPLPDDPVLHICALAYMSDLTLLGSAQVNHLdvRDQLQVA--SLDHAMWFMR 225
Cdd:PLN02868 291 IEIRFCEPNNSTNQTKSppRLRYWFRAKGKLSDDQALHRCVAAYASDLIFLGTSLNPHR--TKGLKFAalSLDHSMWFHR 368

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 805282394 226 PFRADEWLLYDQSSPSASGGRALTRGEIFTRSGEMVAAVMQEGL 269
Cdd:PLN02868 369 PFRADDWLLFVIVSPAAHNGRGFATGHMFNRKGELVVSLTQEAL 412
Acyl_CoA_thio pfam02551
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ...
 139-269 5.52e-55

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: 173.97  E-value: 5.52e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394  139 DAGFRQFDEWDVCIVPRERLRLLPGK-ASQQQVWLRHRDPLPDDPVLHICALAYMSDLTLLGSAQVNHLDVRDQLQVaSL 217
Cdd:pfam02551   1 VANDLFRGEYPVAVRPGELRRTFGGQvVAHQQSWVAALGTVPDDPRLHSCALAYLSDLTLLLTALYPHGFLCDGIQV-SL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 805282394  218 DHAMWFMRPFRADEWLLYDQSSPSASGGRALTRGEIF-TRSGEMVAAVMQEGL 269
Cdd:pfam02551  80 DHSIYFHRPGDLNKWILYDVESPSASGGRGLRQGRNFsTQSGKLIASVQQEGL 132
Thioesterase_II_repeat1 cd03444
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 168-269 9.82e-45

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: 146.62  E-value: 9.82e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394 168 QQVWLRHRDPLPDDPVLHICALAYMSDLTLLGSAQVNH-LDVRDQLQVASLDHAMWFMRPFRADEWLLYDQSSPSASGGR 246
Cdd:cd03444    1 LRVWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHgLPLFDASASASLDHAIWFHRPFRADDWLLYEQRSPRAGNGR 80

                         90       100
                 ....*....|....*....|...
gi 805282394 247 ALTRGEIFTRSGEMVAAVMQEGL 269
Cdd:cd03444   81 GLVEGRIFTRDGELVASVAQEGL 103
 
Name Accession Description Interval E-value
tesB TIGR00189
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ...
 10-271 4.80e-138

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: 390.18  E-value: 4.80e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394   10 EQLEVNIYRGSVFSPESGFLQRTFGGHVAGQSLVSAVRTVDPRYMVHSLHGYFLRPGDAKERTVFLVERIRDGGSFCTRR 89
Cdd:TIGR00189   1 EKIDENLFRGSHLSKGRQFLNRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394   90 VNAVQHGETIFSMAASFQTEQEGITHQDVMPAAPPPD-GLPGLNSIKVFDDAGFRQFD------EWDVCIVPRERLRLLP 162
Cdd:TIGR00189  81 VKAVQHGKTIFTLQASFQAEKSGIEHQSTMPKVPPPEsELPRENQLATKYPATLPRFLkhvvpfERPFEIRPVNLLNYLG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394  163 GKAS-QQQVWLRHRDPLPDDPVLHICALAYMSDLTLLGSAQVNHLDVR-DQLQVASLDHAMWFMRPFRADEWLLYDQSSP 240
Cdd:TIGR00189 161 GKEDpPQYVWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAGfCHSMAASLDHSIWFHRPFRADDWLLYKCSSP 240

                         250       260       270
                  ....*....|....*....|....*....|.
gi 805282394  241 SASGGRALTRGEIFTRSGEMVAAVMQEGLTR 271
Cdd:TIGR00189 241 SAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
TesB COG1946
Acyl-CoA thioesterase [Lipid transport and metabolism];
1-273 1.91e-116

Acyl-CoA thioesterase [Lipid transport and metabolism];


Pssm-ID: 441549 [Multi-domain]  Cd Length: 273  Bit Score: 335.31  E-value: 1.91e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394   1 MSIEEILDLEQLEVNIYRGSVfsPESGFLQRTFGGHVAGQSLVSAVRTVDPRYMVHSLHGYFLRPGDAKERTVFLVERIR 80
Cdd:COG1946    3 MELLDLLDLERLEDGLFRGEI--SPDQGLRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394  81 DGGSFCTRRVNAVQHGETIFSMAASFQTEQEGITHQDVMPAAPPPDGLPGLNSIKVFDDAGFRQFDEW---DVCIVPRER 157
Cdd:COG1946   81 DGRSFSTRRVTAIQGGRVIFTATASFGVPEEGLEHQAPMPDVPPPEDLPSLPELLIAGVLPLRFFAFLrpfDIRPVEGPL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394 158 LRLLPGKASQQQVWLRHRDPLPDDPvLHICALAYMSDLTLLGSAQVNHLDvrDQLQVASLDHAMWFMRPFRADEWLLYDQ 237
Cdd:COG1946  161 PFAPPSGEPRQRVWMRARDPLPDDP-LHAALLAYASDATPPATALLSWLG--PPLPAASLDHAMWFHRPFRADDWLLYDA 237

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 805282394 238 SSPSASGGRALTRGEIFTRSGEMVAAVMQEGLTRHR 273
Cdd:COG1946  238 DSPSASGGRGLERGRIWDRDGRLVASSRQEGLVRGR 273
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 3-269 1.42e-81

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 251.56  E-value: 1.42e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394   3 IEEILDLEQLEVNIYRGsVFSPESGFLQRTFGGHVAGQSLVSAVRTVDPRYMVHSLHGYFLRPGDAKERTVFLVERIRDG 82
Cdd:PLN02868 132 VERILHLEPLEVDIFRG-ITLPDAPTFGKVFGGQLVGQALAAASKTVDPLKLVHSLHAYFLLVGDINLPIIYQVERIRDG 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394  83 GSFCTRRVNAVQHGETIFSMAASFQTEQEGITHQ-DVMPAAPPPDGLPGLNSI--KVFDDAGF----------RQFDEWD 149
Cdd:PLN02868 211 HNFATRRVDAIQKGKVIFTLFASFQKEEQGFEHQeSTMPHVPPPETLLSREELreRRLTDPRLprsyrnkvaaKPFVPWP 290

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394 150 VCIVPRERLRLLPGKAS--QQQVWLRHRDPLPDDPVLHICALAYMSDLTLLGSAQVNHLdvRDQLQVA--SLDHAMWFMR 225
Cdd:PLN02868 291 IEIRFCEPNNSTNQTKSppRLRYWFRAKGKLSDDQALHRCVAAYASDLIFLGTSLNPHR--TKGLKFAalSLDHSMWFHR 368

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 805282394 226 PFRADEWLLYDQSSPSASGGRALTRGEIFTRSGEMVAAVMQEGL 269
Cdd:PLN02868 369 PFRADDWLLFVIVSPAAHNGRGFATGHMFNRKGELVVSLTQEAL 412
PRK10526 PRK10526
acyl-CoA thioesterase II; Provisional
 6-274 2.26e-79

acyl-CoA thioesterase II; Provisional


Pssm-ID: 182519 [Multi-domain]  Cd Length: 286  Bit Score: 241.58  E-value: 2.26e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394   6 ILDLEQLEVNIYRGSvfSPESGfLQRTFGGHVAGQSLVSAVRTVDPRYMVHSLHGYFLRPGDAKERTVFLVERIRDGGSF 85
Cdd:PRK10526  11 LLNLEKIEEGLFRGQ--SEDLG-LRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSQKPIIYDVETLRDGNSF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394  86 CTRRVNAVQHGETIFSMAASFQTEQEGITHQDVMPAAPPPDGLPGLNSI-----KVFDDAGFRQF-DEWDVCIVPRERLR 159
Cdd:PRK10526  88 SARRVAAIQNGKPIFYMTASFQAPEAGFEHQKTMPSAPAPDGLPSETDIaqslaHLLPPVLKDKFiCDRPLEIRPVEFHN 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394 160 LLPGKAS--QQQVWLRHRDPLPDDPVLHICALAYMSDLTLLGSAQVNHLD--VRDQLQVASLDHAMWFMRPFRADEWLLY 235
Cdd:PRK10526 168 PLKGHVAepVRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIgfLEPGMQIATIDHSMWFHRPFNLNEWLLY 247

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 805282394 236 DQSSPSASGGRALTRGEIFTRSGEMVAAVMQEGLTRHRR 274
Cdd:PRK10526 248 SVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMRNHN 286
Acyl_CoA_thio pfam02551
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ...
 139-269 5.52e-55

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: 173.97  E-value: 5.52e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394  139 DAGFRQFDEWDVCIVPRERLRLLPGK-ASQQQVWLRHRDPLPDDPVLHICALAYMSDLTLLGSAQVNHLDVRDQLQVaSL 217
Cdd:pfam02551   1 VANDLFRGEYPVAVRPGELRRTFGGQvVAHQQSWVAALGTVPDDPRLHSCALAYLSDLTLLLTALYPHGFLCDGIQV-SL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 805282394  218 DHAMWFMRPFRADEWLLYDQSSPSASGGRALTRGEIF-TRSGEMVAAVMQEGL 269
Cdd:pfam02551  80 DHSIYFHRPGDLNKWILYDVESPSASGGRGLRQGRNFsTQSGKLIASVQQEGL 132
4HBT_3 pfam13622
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 33-269 4.40e-48

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: 160.19  E-value: 4.40e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394   33 FGGHVAGQSLVSAVRTVDPRyMVHSLHGYFLRPGDAkERTVFLVERIRDGGSFCTRRVNAVQHGETIFSMAASFQTEQEG 112
Cdd:pfam13622  12 HGGYVAALLLRAAERTVPPD-PLHSLHVDFLRPVPP-GPVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRLRSS 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394  113 ITHQD--VMPAAPPPDGLPGlnSIKVFDDAGFRQFDEWDVCIVPR---ERLRLLPGKASQQQVWLRHRDPlpdDPVLHIC 187
Cdd:pfam13622  90 EWELTpaAPPPLPPPEDCPL--AADEAPFPLFRRVPGFLDPFEPRfarGGGPFSPGGPGRVRLWVRLRDG---GEPDPLA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394  188 ALAYMSDLtLLGSAQVNHLDVRDQLQVASLDHAMWFMRPFRADEWLLYDQSSPSASGGRALTRGEIFTRSGEMVAAVMQE 267
Cdd:pfam13622 165 ALAYLADA-FPPRVLSLRLDPPASGWFPTLDLTVYFHRRPPPGEWLLLRAETPVAGDGRGDVEARLWDEDGRLVATSRQE 243


                  ..
gi 805282394  268 GL 269
Cdd:pfam13622 244 VL 245
Thioesterase_II_repeat1 cd03444
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 168-269 9.82e-45

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: 146.62  E-value: 9.82e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394 168 QQVWLRHRDPLPDDPVLHICALAYMSDLTLLGSAQVNH-LDVRDQLQVASLDHAMWFMRPFRADEWLLYDQSSPSASGGR 246
Cdd:cd03444    1 LRVWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHgLPLFDASASASLDHAIWFHRPFRADDWLLYEQRSPRAGNGR 80

                         90       100
                 ....*....|....*....|...
gi 805282394 247 ALTRGEIFTRSGEMVAAVMQEGL 269
Cdd:cd03444   81 GLVEGRIFTRDGELVASVAQEGL 103
Thioesterase_II_repeat2 cd03445
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 15-107 3.15e-38

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: 129.66  E-value: 3.15e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394  15 NIYRGSVFSPESGFLQRTFGGHVAGQSLVSAVRTVDPRYMVHSLHGYFLRPGDAKERTVFLVERIRDGGSFCTRRVNAVQ 94
Cdd:cd03445    1 DRFRGVSPPVPPGQGRGVFGGQVLAQALVAAARTVPDDRVPHSLHSYFLRPGDPDQPIEYEVERLRDGRSFATRRVRAVQ 80

                         90
                 ....*....|...
gi 805282394  95 HGETIFSMAASFQ 107
Cdd:cd03445   81 NGKVIFTATASFQ 93
Thioesterase_II cd00556
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 168-269 1.23e-32

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: 115.52  E-value: 1.23e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394 168 QQVWLRHRDPLPDDPVLHICALAYMSDLTLLGSAqvnhLDVRDQLQVASLDHAMWFMRPFRADEWLLYDQSSPSASGGRA 247
Cdd:cd00556    1 DRFWGRAPGPLPDDRRVFGGQLAAQSDLAALRTV----PRPHGASGFASLDHHIYFHRPGDADEWLLYEVESLRDGRSRA 76

                         90       100
                 ....*....|....*....|..
gi 805282394 248 LTRGEIFTRSGEMVAAVMQEGL 269
Cdd:cd00556   77 LRRGRAYQRDGKLVASATQSFL 98
Thioesterase_II cd00556
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 30-107 6.24e-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: 82.39  E-value: 6.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394  30 QRTFGGHVAGQSLVSAVRTVDPR-----YMVHSLHGYFLRPGDAKERTVFLVERIRDGGSFCTRRVNAVQH-GETIFSMA 103
Cdd:cd00556   15 RRVFGGQLAAQSDLAALRTVPRPhgasgFASLDHHIYFHRPGDADEWLLYEVESLRDGRSRALRRGRAYQRdGKLVASAT 94


                 ....
gi 805282394 104 ASFQ 107
Cdd:cd00556   95 QSFL 98
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 170-269 4.03e-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: 4.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805282394 170 VWLRHRDPLPD-DPVLHICALAYMSDLTLLGSAQVNHLDvrdQLQVASLDHAMWFMRPFRADEWLLYDQSSPSASGGRAL 248
Cdd:cd03440    3 LRLTVTPEDIDgGGIVHGGLLLALADEAAGAAAARLGGR---GLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVT 79

                         90       100
                 ....*....|....*....|.
gi 805282394 249 TRGEIFTRSGEMVAAVMQEGL 269
Cdd:cd03440   80 VEVEVRNEDGKLVATATATFV 100
 
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.
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