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Conserved domains on  [gi|1439309305|emb|STM63721|]
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acyl-CoA thioesterase [Escherichia coli]

Protein Classification

acyl-CoA thioesterase II( domain architecture ID 11484767)

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
PRK10526 PRK10526
acyl-CoA thioesterase II; Provisional
 1-286 0e+00

acyl-CoA thioesterase II; Provisional


:

Pssm-ID: 182519 [Multi-domain]  Cd Length: 286  Bit Score: 638.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305   1 MSQALKNLLTLLNLEKIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSKKPIIYDVET 80
Cdd:PRK10526    1 MSQALKNLLTLLNLEKIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSQKPIIYDVET 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305  81 LRDGNSFSARRVAAIQNGKPIFYMTASFQAPEAGFEHQKTMPSAPAPDGLPSETQIAQSLAHLLPPVLKDKFICDRPLEV 160
Cdd:PRK10526   81 LRDGNSFSARRVAAIQNGKPIFYMTASFQAPEAGFEHQKTMPSAPAPDGLPSETDIAQSLAHLLPPVLKDKFICDRPLEI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305 161 RPVEFHNPLKGHVAEPHRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGIQIATIDHSMWFHRPFN 240
Cdd:PRK10526  161 RPVEFHNPLKGHVAEPVRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGMQIATIDHSMWFHRPFN 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1439309305 241 LNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMRNHN 286
Cdd:PRK10526  241 LNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMRNHN 286
 
Name Accession Description Interval E-value
PRK10526 PRK10526
acyl-CoA thioesterase II; Provisional
 1-286 0e+00

acyl-CoA thioesterase II; Provisional


Pssm-ID: 182519 [Multi-domain]  Cd Length: 286  Bit Score: 638.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305   1 MSQALKNLLTLLNLEKIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSKKPIIYDVET 80
Cdd:PRK10526    1 MSQALKNLLTLLNLEKIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSQKPIIYDVET 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305  81 LRDGNSFSARRVAAIQNGKPIFYMTASFQAPEAGFEHQKTMPSAPAPDGLPSETQIAQSLAHLLPPVLKDKFICDRPLEV 160
Cdd:PRK10526   81 LRDGNSFSARRVAAIQNGKPIFYMTASFQAPEAGFEHQKTMPSAPAPDGLPSETDIAQSLAHLLPPVLKDKFICDRPLEI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305 161 RPVEFHNPLKGHVAEPHRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGIQIATIDHSMWFHRPFN 240
Cdd:PRK10526  161 RPVEFHNPLKGHVAEPVRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGMQIATIDHSMWFHRPFN 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1439309305 241 LNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMRNHN 286
Cdd:PRK10526  241 LNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMRNHN 286
tesB TIGR00189
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ...
 15-283 4.97e-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: 385.56  E-value: 4.97e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305  15 EKIEEGLFRGQSEDLGLR---QVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSKKPIIYDVETLRDGNSFSARR 91
Cdd:TIGR00189   1 EKIDENLFRGSHLSKGRQflnRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305  92 VAAIQNGKPIFYMTASFQAPEAGFEHQKTMPSAPAPD-GLPSETQIAQSLAHLLPPVLKDKFICDRPLEVRPVEFHNPLK 170
Cdd:TIGR00189  81 VKAVQHGKTIFTLQASFQAEKSGIEHQSTMPKVPPPEsELPRENQLATKYPATLPRFLKHVVPFERPFEIRPVNLLNYLG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305 171 GHVAEPHRqVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLePGIQIATIDHSMWFHRPFNLNEWLLYSVE 250
Cdd:TIGR00189 161 GKEDPPQY-VWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAGF-CHSMAASLDHSIWFHRPFRADDWLLYKCS 238

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1439309305 251 STSASSARGFVRGEFYTQDGVLVASTVQEGVMR 283
Cdd:TIGR00189 239 SPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
TesB COG1946
Acyl-CoA thioesterase [Lipid transport and metabolism];
15-283 4.23e-133

Acyl-CoA thioesterase [Lipid transport and metabolism];


Pssm-ID: 441549 [Multi-domain]  Cd Length: 273  Bit Score: 378.07  E-value: 4.23e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305  15 EKIEEGLFRGQ-SEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSKKPIIYDVETLRDGNSFSARRVA 93
Cdd:COG1946    12 ERLEDGLFRGEiSPDQGLRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFSTRRVT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305  94 AIQNGKPIFYMTASFQAPEAGFEHQKTMPSAPAPDGLPSETQIAqsLAHLLPPvlkDKFICDRPLEVRPVEFHNPLKGHV 173
Cdd:COG1946    92 AIQGGRVIFTATASFGVPEEGLEHQAPMPDVPPPEDLPSLPELL--IAGVLPL---RFFAFLRPFDIRPVEGPLPFAPPS 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305 174 AEPHRQVWIRANGSVPDDlRVHQYLLGYASDLNFLPVALQPhgigFLEPGIQIATIDHSMWFHRPFNLNEWLLYSVESTS 253
Cdd:COG1946   167 GEPRQRVWMRARDPLPDD-PLHAALLAYASDATPPATALLS----WLGPPLPAASLDHAMWFHRPFRADDWLLYDADSPS 241

                         250       260       270
                  ....*....|....*....|....*....|
gi 1439309305 254 ASSARGFVRGEFYTQDGVLVASTVQEGVMR 283
Cdd:COG1946   242 ASGGRGLERGRIWDRDGRLVASSRQEGLVR 271
Acyl_CoA_thio pfam02551
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ...
 147-281 6.35e-57

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: 179.36  E-value: 6.35e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305 147 VLKDKFICDRPLEVRPVEFHNPLKGHVAePHRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGigFLEPGIQI 226
Cdd:pfam02551   1 VANDLFRGEYPVAVRPGELRRTFGGQVV-AHQQSWVAALGTVPDDPRLHSCALAYLSDLTLLLTALYPHG--FLCDGIQV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1439309305 227 aTIDHSMWFHRPFNLNEWLLYSVESTSASSARGFVRGEFY-TQDGVLVASTVQEGV 281
Cdd:pfam02551  78 -SLDHSIYFHRPGDLNKWILYDVESPSASGGRGLRQGRNFsTQSGKLIASVQQEGL 132
Thioesterase_II_repeat1 cd03444
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 178-282 8.90e-44

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: 8.90e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305 178 RQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGiQIATIDHSMWFHRPFNLNEWLLYSVESTSASSA 257
Cdd:cd03444     1 LRVWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHGLPLFDAS-ASASLDHAIWFHRPFRADDWLLYEQRSPRAGNG 79

                          90       100
                  ....*....|....*....|....*
gi 1439309305 258 RGFVRGEFYTQDGVLVASTVQEGVM 282
Cdd:cd03444    80 RGLVEGRIFTRDGELVASVAQEGLL 104
 
Name Accession Description Interval E-value
PRK10526 PRK10526
acyl-CoA thioesterase II; Provisional
 1-286 0e+00

acyl-CoA thioesterase II; Provisional


Pssm-ID: 182519 [Multi-domain]  Cd Length: 286  Bit Score: 638.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305   1 MSQALKNLLTLLNLEKIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSKKPIIYDVET 80
Cdd:PRK10526    1 MSQALKNLLTLLNLEKIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSQKPIIYDVET 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305  81 LRDGNSFSARRVAAIQNGKPIFYMTASFQAPEAGFEHQKTMPSAPAPDGLPSETQIAQSLAHLLPPVLKDKFICDRPLEV 160
Cdd:PRK10526   81 LRDGNSFSARRVAAIQNGKPIFYMTASFQAPEAGFEHQKTMPSAPAPDGLPSETDIAQSLAHLLPPVLKDKFICDRPLEI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305 161 RPVEFHNPLKGHVAEPHRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGIQIATIDHSMWFHRPFN 240
Cdd:PRK10526  161 RPVEFHNPLKGHVAEPVRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGMQIATIDHSMWFHRPFN 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1439309305 241 LNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMRNHN 286
Cdd:PRK10526  241 LNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMRNHN 286
tesB TIGR00189
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ...
 15-283 4.97e-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: 385.56  E-value: 4.97e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305  15 EKIEEGLFRGQSEDLGLR---QVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSKKPIIYDVETLRDGNSFSARR 91
Cdd:TIGR00189   1 EKIDENLFRGSHLSKGRQflnRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305  92 VAAIQNGKPIFYMTASFQAPEAGFEHQKTMPSAPAPD-GLPSETQIAQSLAHLLPPVLKDKFICDRPLEVRPVEFHNPLK 170
Cdd:TIGR00189  81 VKAVQHGKTIFTLQASFQAEKSGIEHQSTMPKVPPPEsELPRENQLATKYPATLPRFLKHVVPFERPFEIRPVNLLNYLG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305 171 GHVAEPHRqVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLePGIQIATIDHSMWFHRPFNLNEWLLYSVE 250
Cdd:TIGR00189 161 GKEDPPQY-VWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAGF-CHSMAASLDHSIWFHRPFRADDWLLYKCS 238

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1439309305 251 STSASSARGFVRGEFYTQDGVLVASTVQEGVMR 283
Cdd:TIGR00189 239 SPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
TesB COG1946
Acyl-CoA thioesterase [Lipid transport and metabolism];
15-283 4.23e-133

Acyl-CoA thioesterase [Lipid transport and metabolism];


Pssm-ID: 441549 [Multi-domain]  Cd Length: 273  Bit Score: 378.07  E-value: 4.23e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305  15 EKIEEGLFRGQ-SEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSKKPIIYDVETLRDGNSFSARRVA 93
Cdd:COG1946    12 ERLEDGLFRGEiSPDQGLRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFSTRRVT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305  94 AIQNGKPIFYMTASFQAPEAGFEHQKTMPSAPAPDGLPSETQIAqsLAHLLPPvlkDKFICDRPLEVRPVEFHNPLKGHV 173
Cdd:COG1946    92 AIQGGRVIFTATASFGVPEEGLEHQAPMPDVPPPEDLPSLPELL--IAGVLPL---RFFAFLRPFDIRPVEGPLPFAPPS 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305 174 AEPHRQVWIRANGSVPDDlRVHQYLLGYASDLNFLPVALQPhgigFLEPGIQIATIDHSMWFHRPFNLNEWLLYSVESTS 253
Cdd:COG1946   167 GEPRQRVWMRARDPLPDD-PLHAALLAYASDATPPATALLS----WLGPPLPAASLDHAMWFHRPFRADDWLLYDADSPS 241

                         250       260       270
                  ....*....|....*....|....*....|
gi 1439309305 254 ASSARGFVRGEFYTQDGVLVASTVQEGVMR 283
Cdd:COG1946   242 ASGGRGLERGRIWDRDGRLVASSRQEGLVR 271
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 15-282 1.23e-88

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 270.05  E-value: 1.23e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305  15 EKIEEGLFRG----QSEDLGlrQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSKKPIIYDVETLRDGNSFSAR 90
Cdd:PLN02868  139 EPLEVDIFRGitlpDAPTFG--KVFGGQLVGQALAAASKTVDPLKLVHSLHAYFLLVGDINLPIIYQVERIRDGHNFATR 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305  91 RVAAIQNGKPIFYMTASFQAPEAGFEHQK-TMPSAPAPDGLPSETQIAQSLAH--LLPPVLKDKFICDR----PLEVRPV 163
Cdd:PLN02868  217 RVDAIQKGKVIFTLFASFQKEEQGFEHQEsTMPHVPPPETLLSREELRERRLTdpRLPRSYRNKVAAKPfvpwPIEIRFC 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305 164 EFHNPLKGHVAEPHRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEpgIQIATIDHSMWFHRPFNLNE 243
Cdd:PLN02868  297 EPNNSTNQTKSPPRLRYWFRAKGKLSDDQALHRCVAAYASDLIFLGTSLNPHRTKGLK--FAALSLDHSMWFHRPFRADD 374

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1439309305 244 WLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVM 282
Cdd:PLN02868  375 WLLFVIVSPAAHNGRGFATGHMFNRKGELVVSLTQEALL 413
Acyl_CoA_thio pfam02551
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ...
 147-281 6.35e-57

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: 179.36  E-value: 6.35e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305 147 VLKDKFICDRPLEVRPVEFHNPLKGHVAePHRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGigFLEPGIQI 226
Cdd:pfam02551   1 VANDLFRGEYPVAVRPGELRRTFGGQVV-AHQQSWVAALGTVPDDPRLHSCALAYLSDLTLLLTALYPHG--FLCDGIQV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1439309305 227 aTIDHSMWFHRPFNLNEWLLYSVESTSASSARGFVRGEFY-TQDGVLVASTVQEGV 281
Cdd:pfam02551  78 -SLDHSIYFHRPGDLNKWILYDVESPSASGGRGLRQGRNFsTQSGKLIASVQQEGL 132
4HBT_3 pfam13622
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 32-282 7.10e-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: 172.90  E-value: 7.10e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305  32 RQVFGGQVVGQALYAAKETVPEERLvHSFHSYFLRPGDSKkPIIYDVETLRDGNSFSARRVAAIQNGKPIFYMTASFQAP 111
Cdd:pfam13622   9 RAPHGGYVAALLLRAAERTVPPDPL-HSLHVDFLRPVPPG-PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305 112 EAGF--EHQKTMPSAPAPDGLPSETQIAqsLAHLLPPVlkDKFIcdRPLEVRPVEFHNPLKGHvAEPHRQVWIRANgsvP 189
Cdd:pfam13622  87 RSSEweLTPAAPPPLPPPEDCPLAADEA--PFPLFRRV--PGFL--DPFEPRFARGGGPFSPG-GPGRVRLWVRLR---D 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305 190 DDLRVHQYLLGYASDLnFLPVAlqpHGIGFLEPGI-QIATIDHSMWFHRPFNLNEWLLYSVESTSASSARGFVRGEFYTQ 268
Cdd:pfam13622 157 GGEPDPLAALAYLADA-FPPRV---LSLRLDPPASgWFPTLDLTVYFHRRPPPGEWLLLRAETPVAGDGRGDVEARLWDE 232

                         250
                  ....*....|....
gi 1439309305 269 DGVLVASTVQEGVM 282
Cdd:pfam13622 233 DGRLVATSRQEVLV 246
Thioesterase_II_repeat1 cd03444
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 178-282 8.90e-44

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: 8.90e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305 178 RQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGiQIATIDHSMWFHRPFNLNEWLLYSVESTSASSA 257
Cdd:cd03444     1 LRVWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHGLPLFDAS-ASASLDHAIWFHRPFRADDWLLYEQRSPRAGNG 79

                          90       100
                  ....*....|....*....|....*
gi 1439309305 258 RGFVRGEFYTQDGVLVASTVQEGVM 282
Cdd:cd03444    80 RGLVEGRIFTRDGELVASVAQEGLL 104
Thioesterase_II_repeat2 cd03445
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 21-109 2.63e-42

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: 140.45  E-value: 2.63e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305  21 LFRGQS---EDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSKKPIIYDVETLRDGNSFSARRVAAIQN 97
Cdd:cd03445     2 RFRGVSppvPPGQGRGVFGGQVLAQALVAAARTVPDDRVPHSLHSYFLRPGDPDQPIEYEVERLRDGRSFATRRVRAVQN 81

                          90
                  ....*....|..
gi 1439309305  98 GKPIFYMTASFQ 109
Cdd:cd03445    82 GKVIFTATASFQ 93
Thioesterase_II cd00556
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 180-282 5.16e-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: 111.67  E-value: 5.16e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305 180 VWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLepgiqiATIDHSMWFHRPFNLNEWLLYSVESTSASSARG 259
Cdd:cd00556     3 FWGRAPGPLPDDRRVFGGQLAAQSDLAALRTVPRPHGASGF------ASLDHHIYFHRPGDADEWLLYEVESLRDGRSRA 76

                          90       100
                  ....*....|....*....|...
gi 1439309305 260 FVRGEFYTQDGVLVASTVQEGVM 282
Cdd:cd00556    77 LRRGRAYQRDGKLVASATQSFLV 99
Thioesterase_II cd00556
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 32-109 6.13e-24

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: 93.18  E-value: 6.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305  32 RQVFGGQVVGQALYAAKETVPEE-----RLVHSFHSYFLRPGDSKKPIIYDVETLRDGNSFSARRVAAIQN-GKPIFYMT 105
Cdd:cd00556    15 RRVFGGQLAAQSDLAALRTVPRPhgasgFASLDHHIYFHRPGDADEWLLYEVESLRDGRSRALRRGRAYQRdGKLVASAT 94


                  ....
gi 1439309305 106 ASFQ 109
Cdd:cd00556    95 QSFL 98
Acyl_CoA_thio pfam02551
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ...
 17-115 7.16e-13

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: 64.57  E-value: 7.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305  17 IEEGLFRGQ---SEDLG-LRQVFGGQVVG--QALYAAKETVPEERLVHSF------------------------------ 60
Cdd:pfam02551   1 VANDLFRGEypvAVRPGeLRRTFGGQVVAhqQSWVAALGTVPDDPRLHSCalaylsdltllltalyphgflcdgiqvsld 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1439309305  61 HS-YFLRPGDSKKPIIYDVET--------LRDGNSFSarrvaaIQNGKPIFYmtasfqAPEAGF 115
Cdd:pfam02551  81 HSiYFHRPGDLNKWILYDVESpsasggrgLRQGRNFS------TQSGKLIAS------VQQEGL 132
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 205-281 1.98e-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: 50.94  E-value: 1.98e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1439309305 205 LNFLPVALQPHGIGFLEPGIQIATIDHSMWFHRPFNLNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGV 281
Cdd:cd03440    24 LALADEAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRNEDGKLVATATATFV 100
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 34-108 5.37e-03

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: 35.91  E-value: 5.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439309305  34 VFGGQVVGQALYAAKETVPEERL------VHSFHSYFLRPGDSKKPIIYDVETLRDGNSFSARRVAAI-QNGKPIFYMTA 106
Cdd:cd03440    18 VHGGLLLALADEAAGAAAARLGGrglgavTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRnEDGKLVATATA 97


                  ..
gi 1439309305 107 SF 108
Cdd:cd03440    98 TF 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.
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