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Conserved domains on  [gi|507222356|gb|AGM44893|]
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acyl-CoA thioesterase [Aeromonas hydrophila ML09-119]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10526 super family cl29845
acyl-CoA thioesterase II; Provisional
 16-287 5.64e-167

acyl-CoA thioesterase II; Provisional


The actual alignment was detected with superfamily member PRK10526:

Pssm-ID: 182519 [Multi-domain]  Cd Length: 286  Bit Score: 464.22  E-value: 5.64e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356  16 KIEEGLFRGQSQDLGLRAVFGGQVMGQALSAAKQTVASDRQVHSFHSYFLRPGDANRPIVYDVENIRDGQTVSTRRVKAI 95
Cdd:PRK10526  16 KIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSQKPIIYDVETLRDGNSFSARRVAAI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356  96 QGGKPIFYLNASFQVEADGFEHQIAMPAgITPPEQLKSELELVRPYEQQIPPALRDKIMCEKPIEIRPVTLVDPIRPDVH 175
Cdd:PRK10526  96 QNGKPIFYMTASFQAPEAGFEHQKTMPS-APAPDGLPSETDIAQSLAHLLPPVLKDKFICDRPLEIRPVEFHNPLKGHVA 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356 176 EPLRHVWFKANGQMPDDQRVHKYLLAYASDFHFLFTALQPHGVSYWEPDMQVATIDHSMWFHRDFRLDDWLLYVVDSPSA 255
Cdd:PRK10526 175 EPVRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGMQIATIDHSMWFHRPFNLNEWLLYSVESTSA 254

                        250       260       270
                 ....*....|....*....|....*....|..
gi 507222356 256 SAGRGLVRGQFFTRDGVLVASTAQEGVIRRRG 287
Cdd:PRK10526 255 SSARGFVRGEFYTQDGVLVASTVQEGVMRNHN 286
 
Name Accession Description Interval E-value
PRK10526 PRK10526
acyl-CoA thioesterase II; Provisional
 16-287 5.64e-167

acyl-CoA thioesterase II; Provisional


Pssm-ID: 182519 [Multi-domain]  Cd Length: 286  Bit Score: 464.22  E-value: 5.64e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356  16 KIEEGLFRGQSQDLGLRAVFGGQVMGQALSAAKQTVASDRQVHSFHSYFLRPGDANRPIVYDVENIRDGQTVSTRRVKAI 95
Cdd:PRK10526  16 KIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSQKPIIYDVETLRDGNSFSARRVAAI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356  96 QGGKPIFYLNASFQVEADGFEHQIAMPAgITPPEQLKSELELVRPYEQQIPPALRDKIMCEKPIEIRPVTLVDPIRPDVH 175
Cdd:PRK10526  96 QNGKPIFYMTASFQAPEAGFEHQKTMPS-APAPDGLPSETDIAQSLAHLLPPVLKDKFICDRPLEIRPVEFHNPLKGHVA 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356 176 EPLRHVWFKANGQMPDDQRVHKYLLAYASDFHFLFTALQPHGVSYWEPDMQVATIDHSMWFHRDFRLDDWLLYVVDSPSA 255
Cdd:PRK10526 175 EPVRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGMQIATIDHSMWFHRPFNLNEWLLYSVESTSA 254

                        250       260       270
                 ....*....|....*....|....*....|..
gi 507222356 256 SAGRGLVRGQFFTRDGVLVASTAQEGVIRRRG 287
Cdd:PRK10526 255 SSARGFVRGEFYTQDGVLVASTVQEGVMRNHN 286
TesB COG1946
Acyl-CoA thioesterase [Lipid transport and metabolism];
16-286 2.31e-127

Acyl-CoA thioesterase [Lipid transport and metabolism];


Pssm-ID: 441549 [Multi-domain]  Cd Length: 273  Bit Score: 363.43  E-value: 2.31e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356  16 KIEEGLFRGQ-SQDLGLRAVFGGQVMGQALSAAKQTVASDRQVHSFHSYFLRPGDANRPIVYDVENIRDGQTVSTRRVKA 94
Cdd:COG1946   13 RLEDGLFRGEiSPDQGLRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFSTRRVTA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356  95 IQGGKPIFYLNASFQVEADGFEHQIAMPAGItPPEQLKSELELVrpYEQQIPPALRdkiMCEKPIEIRPVTLVDPIRPDV 174
Cdd:COG1946   93 IQGGRVIFTATASFGVPEEGLEHQAPMPDVP-PPEDLPSLPELL--IAGVLPLRFF---AFLRPFDIRPVEGPLPFAPPS 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356 175 HEPLRHVWFKANGQMPDDQrVHKYLLAYASDFHFLFTALQphgvSYWEPDMQVATIDHSMWFHRDFRLDDWLLYVVDSPS 254
Cdd:COG1946  167 GEPRQRVWMRARDPLPDDP-LHAALLAYASDATPPATALL----SWLGPPLPAASLDHAMWFHRPFRADDWLLYDADSPS 241

                        250       260       270
                 ....*....|....*....|....*....|..
gi 507222356 255 ASAGRGLVRGQFFTRDGVLVASTAQEGVIRRR 286
Cdd:COG1946  242 ASGGRGLERGRIWDRDGRLVASSRQEGLVRGR 273
tesB TIGR00189
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ...
 16-284 2.94e-116

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: 335.10  E-value: 2.94e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356   16 KIEEGLFRGQSQDLGLR---AVFGGQVMGQALSAAKQTVASDRQVHSFHSYFLRPGDANRPIVYDVENIRDGQTVSTRRV 92
Cdd:TIGR00189   2 KIDENLFRGSHLSKGRQflnRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356   93 KAIQGGKPIFYLNASFQVEADGFEHQIAMPAGITPPEQLKSELELVRPYEQQIPPALRDKIMCEKPIEIRPVTLVDPIrP 172
Cdd:TIGR00189  82 KAVQHGKTIFTLQASFQAEKSGIEHQSTMPKVPPPESELPRENQLATKYPATLPRFLKHVVPFERPFEIRPVNLLNYL-G 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356  173 DVHEPLRHVWFKANGQMPDDQRVHKYLLAYASDFHFLFTALQPHGVSyWEPDMQVATIDHSMWFHRDFRLDDWLLYVVDS 252
Cdd:TIGR00189 161 GKEDPPQYVWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKA-GFCHSMAASLDHSIWFHRPFRADDWLLYKCSS 239

                         250       260       270
                  ....*....|....*....|....*....|..
gi 507222356  253 PSASAGRGLVRGQFFTRDGVLVASTAQEGVIR 284
Cdd:TIGR00189 240 PSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
4HBT_3 pfam13622
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 32-283 8.20e-51

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: 167.51  E-value: 8.20e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356   32 RAVFGGQVMGQALSAAKQTVASDrQVHSFHSYFLRPGDANrPIVYDVENIRDGQTVSTRRVKAIQGGKPIFYLNASFQVE 111
Cdd:pfam13622   9 RAPHGGYVAALLLRAAERTVPPD-PLHSLHVDFLRPVPPG-PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356  112 ADG-FEHQIAMPAGITPPEQLKSEL-ELVRPYEQQIPPALRdkimcekPIEIRPVTLVDPIRPDvHEPLRHVWFKANgqm 189
Cdd:pfam13622  87 RSSeWELTPAAPPPLPPPEDCPLAAdEAPFPLFRRVPGFLD-------PFEPRFARGGGPFSPG-GPGRVRLWVRLR--- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356  190 PDDQRVHKYLLAYASDfhflftALQPHGVSYWEPDMQV---ATIDHSMWFHRDFRLDDWLLYVVDSPSASAGRGLVRGQF 266
Cdd:pfam13622 156 DGGEPDPLAALAYLAD------AFPPRVLSLRLDPPASgwfPTLDLTVYFHRRPPPGEWLLLRAETPVAGDGRGDVEARL 229

                         250
                  ....*....|....*..
gi 507222356  267 FTRDGVLVASTAQEGVI 283
Cdd:pfam13622 230 WDEDGRLVATSRQEVLV 246
Thioesterase_II_repeat1 cd03444
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 179-283 9.88e-48

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: 154.71  E-value: 9.88e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356 179 RHVWFKANGQMPDDQRVHKYLLAYASDFHFLFTALQPHGVSyWEPDMQVATIDHSMWFHRDFRLDDWLLYVVDSPSASAG 258
Cdd:cd03444    1 LRVWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHGLP-LFDASASASLDHAIWFHRPFRADDWLLYEQRSPRAGNG 79

                         90       100
                 ....*....|....*....|....*
gi 507222356 259 RGLVRGQFFTRDGVLVASTAQEGVI 283
Cdd:cd03444   80 RGLVEGRIFTRDGELVASVAQEGLL 104
 
Name Accession Description Interval E-value
PRK10526 PRK10526
acyl-CoA thioesterase II; Provisional
 16-287 5.64e-167

acyl-CoA thioesterase II; Provisional


Pssm-ID: 182519 [Multi-domain]  Cd Length: 286  Bit Score: 464.22  E-value: 5.64e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356  16 KIEEGLFRGQSQDLGLRAVFGGQVMGQALSAAKQTVASDRQVHSFHSYFLRPGDANRPIVYDVENIRDGQTVSTRRVKAI 95
Cdd:PRK10526  16 KIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSQKPIIYDVETLRDGNSFSARRVAAI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356  96 QGGKPIFYLNASFQVEADGFEHQIAMPAgITPPEQLKSELELVRPYEQQIPPALRDKIMCEKPIEIRPVTLVDPIRPDVH 175
Cdd:PRK10526  96 QNGKPIFYMTASFQAPEAGFEHQKTMPS-APAPDGLPSETDIAQSLAHLLPPVLKDKFICDRPLEIRPVEFHNPLKGHVA 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356 176 EPLRHVWFKANGQMPDDQRVHKYLLAYASDFHFLFTALQPHGVSYWEPDMQVATIDHSMWFHRDFRLDDWLLYVVDSPSA 255
Cdd:PRK10526 175 EPVRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGMQIATIDHSMWFHRPFNLNEWLLYSVESTSA 254

                        250       260       270
                 ....*....|....*....|....*....|..
gi 507222356 256 SAGRGLVRGQFFTRDGVLVASTAQEGVIRRRG 287
Cdd:PRK10526 255 SSARGFVRGEFYTQDGVLVASTVQEGVMRNHN 286
TesB COG1946
Acyl-CoA thioesterase [Lipid transport and metabolism];
16-286 2.31e-127

Acyl-CoA thioesterase [Lipid transport and metabolism];


Pssm-ID: 441549 [Multi-domain]  Cd Length: 273  Bit Score: 363.43  E-value: 2.31e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356  16 KIEEGLFRGQ-SQDLGLRAVFGGQVMGQALSAAKQTVASDRQVHSFHSYFLRPGDANRPIVYDVENIRDGQTVSTRRVKA 94
Cdd:COG1946   13 RLEDGLFRGEiSPDQGLRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFSTRRVTA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356  95 IQGGKPIFYLNASFQVEADGFEHQIAMPAGItPPEQLKSELELVrpYEQQIPPALRdkiMCEKPIEIRPVTLVDPIRPDV 174
Cdd:COG1946   93 IQGGRVIFTATASFGVPEEGLEHQAPMPDVP-PPEDLPSLPELL--IAGVLPLRFF---AFLRPFDIRPVEGPLPFAPPS 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356 175 HEPLRHVWFKANGQMPDDQrVHKYLLAYASDFHFLFTALQphgvSYWEPDMQVATIDHSMWFHRDFRLDDWLLYVVDSPS 254
Cdd:COG1946  167 GEPRQRVWMRARDPLPDDP-LHAALLAYASDATPPATALL----SWLGPPLPAASLDHAMWFHRPFRADDWLLYDADSPS 241

                        250       260       270
                 ....*....|....*....|....*....|..
gi 507222356 255 ASAGRGLVRGQFFTRDGVLVASTAQEGVIRRR 286
Cdd:COG1946  242 ASGGRGLERGRIWDRDGRLVASSRQEGLVRGR 273
tesB TIGR00189
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ...
 16-284 2.94e-116

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: 335.10  E-value: 2.94e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356   16 KIEEGLFRGQSQDLGLR---AVFGGQVMGQALSAAKQTVASDRQVHSFHSYFLRPGDANRPIVYDVENIRDGQTVSTRRV 92
Cdd:TIGR00189   2 KIDENLFRGSHLSKGRQflnRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356   93 KAIQGGKPIFYLNASFQVEADGFEHQIAMPAGITPPEQLKSELELVRPYEQQIPPALRDKIMCEKPIEIRPVTLVDPIrP 172
Cdd:TIGR00189  82 KAVQHGKTIFTLQASFQAEKSGIEHQSTMPKVPPPESELPRENQLATKYPATLPRFLKHVVPFERPFEIRPVNLLNYL-G 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356  173 DVHEPLRHVWFKANGQMPDDQRVHKYLLAYASDFHFLFTALQPHGVSyWEPDMQVATIDHSMWFHRDFRLDDWLLYVVDS 252
Cdd:TIGR00189 161 GKEDPPQYVWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKA-GFCHSMAASLDHSIWFHRPFRADDWLLYKCSS 239

                         250       260       270
                  ....*....|....*....|....*....|..
gi 507222356  253 PSASAGRGLVRGQFFTRDGVLVASTAQEGVIR 284
Cdd:TIGR00189 240 PSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 16-283 4.63e-91

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 276.22  E-value: 4.63e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356  16 KIEEGLFRG----QSQDLGlrAVFGGQVMGQALSAAKQTVASDRQVHSFHSYFLRPGDANRPIVYDVENIRDGQTVSTRR 91
Cdd:PLN02868 140 PLEVDIFRGitlpDAPTFG--KVFGGQLVGQALAAASKTVDPLKLVHSLHAYFLLVGDINLPIIYQVERIRDGHNFATRR 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356  92 VKAIQGGKPIFYLNASFQVEADGFEHQIA-MPAgITPPEQLKSELELVRPY--EQQIPPALRDKIMCEK----PIEIRPV 164
Cdd:PLN02868 218 VDAIQKGKVIFTLFASFQKEEQGFEHQEStMPH-VPPPETLLSREELRERRltDPRLPRSYRNKVAAKPfvpwPIEIRFC 296

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356 165 TLVDPIRPDVHEPLRHVWFKANGQMPDDQRVHKYLLAYASDFHFLFTALQPHGvsywEPDMQVA--TIDHSMWFHRDFRL 242
Cdd:PLN02868 297 EPNNSTNQTKSPPRLRYWFRAKGKLSDDQALHRCVAAYASDLIFLGTSLNPHR----TKGLKFAalSLDHSMWFHRPFRA 372

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 507222356 243 DDWLLYVVDSPSASAGRGLVRGQFFTRDGVLVASTAQEGVI 283
Cdd:PLN02868 373 DDWLLFVIVSPAAHNGRGFATGHMFNRKGELVVSLTQEALL 413
4HBT_3 pfam13622
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 32-283 8.20e-51

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: 167.51  E-value: 8.20e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356   32 RAVFGGQVMGQALSAAKQTVASDrQVHSFHSYFLRPGDANrPIVYDVENIRDGQTVSTRRVKAIQGGKPIFYLNASFQVE 111
Cdd:pfam13622   9 RAPHGGYVAALLLRAAERTVPPD-PLHSLHVDFLRPVPPG-PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356  112 ADG-FEHQIAMPAGITPPEQLKSEL-ELVRPYEQQIPPALRdkimcekPIEIRPVTLVDPIRPDvHEPLRHVWFKANgqm 189
Cdd:pfam13622  87 RSSeWELTPAAPPPLPPPEDCPLAAdEAPFPLFRRVPGFLD-------PFEPRFARGGGPFSPG-GPGRVRLWVRLR--- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356  190 PDDQRVHKYLLAYASDfhflftALQPHGVSYWEPDMQV---ATIDHSMWFHRDFRLDDWLLYVVDSPSASAGRGLVRGQF 266
Cdd:pfam13622 156 DGGEPDPLAALAYLAD------AFPPRVLSLRLDPPASgwfPTLDLTVYFHRRPPPGEWLLLRAETPVAGDGRGDVEARL 229

                         250
                  ....*....|....*..
gi 507222356  267 FTRDGVLVASTAQEGVI 283
Cdd:pfam13622 230 WDEDGRLVATSRQEVLV 246
Thioesterase_II_repeat1 cd03444
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 179-283 9.88e-48

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: 154.71  E-value: 9.88e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356 179 RHVWFKANGQMPDDQRVHKYLLAYASDFHFLFTALQPHGVSyWEPDMQVATIDHSMWFHRDFRLDDWLLYVVDSPSASAG 258
Cdd:cd03444    1 LRVWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHGLP-LFDASASASLDHAIWFHRPFRADDWLLYEQRSPRAGNG 79

                         90       100
                 ....*....|....*....|....*
gi 507222356 259 RGLVRGQFFTRDGVLVASTAQEGVI 283
Cdd:cd03444   80 RGLVEGRIFTRDGELVASVAQEGLL 104
Acyl_CoA_thio pfam02551
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ...
 149-282 2.70e-41

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: 139.30  E-value: 2.70e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356  149 LRDKIMCEKPIEIRPVTLVDPIRPDVhEPLRHVWFKANGQMPDDQRVHKYLLAYASDFHFLFTALQPHGvsyWEPDMQVA 228
Cdd:pfam02551   2 ANDLFRGEYPVAVRPGELRRTFGGQV-VAHQQSWVAALGTVPDDPRLHSCALAYLSDLTLLLTALYPHG---FLCDGIQV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 507222356  229 TIDHSMWFHRDFRLDDWLLYVVDSPSASAGRGLVRGQFF-TRDGVLVASTAQEGV 282
Cdd:pfam02551  78 SLDHSIYFHRPGDLNKWILYDVESPSASGGRGLRQGRNFsTQSGKLIASVQQEGL 132
Thioesterase_II_repeat2 cd03445
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 21-110 7.50e-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: 134.29  E-value: 7.50e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356  21 LFRGQSQ---DLGLRAVFGGQVMGQALSAAKQTVASDRQVHSFHSYFLRPGDANRPIVYDVENIRDGQTVSTRRVKAIQG 97
Cdd:cd03445    2 RFRGVSPpvpPGQGRGVFGGQVLAQALVAAARTVPDDRVPHSLHSYFLRPGDPDQPIEYEVERLRDGRSFATRRVRAVQN 81

                         90
                 ....*....|...
gi 507222356  98 GKPIFYLNASFQV 110
Cdd:cd03445   82 GKVIFTATASFQR 94
Thioesterase_II cd00556
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 179-283 4.92e-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: 113.98  E-value: 4.92e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356 179 RHVWFKANGQMPDDQRVHKYLLAYASDFHFLFTALQPHGVSywepdmQVATIDHSMWFHRDFRLDDWLLYVVDSPSASAG 258
Cdd:cd00556    1 DRFWGRAPGPLPDDRRVFGGQLAAQSDLAALRTVPRPHGAS------GFASLDHHIYFHRPGDADEWLLYEVESLRDGRS 74

                         90       100
                 ....*....|....*....|....*
gi 507222356 259 RGLVRGQFFTRDGVLVASTAQEGVI 283
Cdd:cd00556   75 RALRRGRAYQRDGKLVASATQSFLV 99
Thioesterase_II cd00556
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 32-110 2.79e-21

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: 85.86  E-value: 2.79e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356  32 RAVFGGQVMGQALSAAKQTV-----ASDRQVHSFHSYFLRPGDANRPIVYDVENIRDGQTVSTRRVKAIQ-GGKPIFYLN 105
Cdd:cd00556   15 RRVFGGQLAAQSDLAALRTVprphgASGFASLDHHIYFHRPGDADEWLLYEVESLRDGRSRALRRGRAYQrDGKLVASAT 94


                 ....*
gi 507222356 106 ASFQV 110
Cdd:cd00556   95 QSFLV 99
Acyl_CoA_thio pfam02551
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ...
 17-103 1.73e-07

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: 49.17  E-value: 1.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356   17 IEEGLFRGQ---SQDLG-LRAVFGGQVMG--QALSAAKQTVASDRQVHSF------------------------------ 60
Cdd:pfam02551   1 VANDLFRGEypvAVRPGeLRRTFGGQVVAhqQSWVAALGTVPDDPRLHSCalaylsdltllltalyphgflcdgiqvsld 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 507222356   61 HS-YFLRPGDANRPIVYDVENIRDGQTVSTRRVK--AIQGGKPIFY 103
Cdd:pfam02551  81 HSiYFHRPGDLNKWILYDVESPSASGGRGLRQGRnfSTQSGKLIAS 126
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 180-282 7.27e-06

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: 44.00  E-value: 7.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356 180 HVWFKANGQMPDDQR-VHKYLLAYASDFHFLFTALQPHGvsywePDMQVATIDHSMWFHRDFRLDDWLLYVVDSPSASAG 258
Cdd:cd03440    2 VLRLTVTPEDIDGGGiVHGGLLLALADEAAGAAAARLGG-----RGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRS 76

                         90       100
                 ....*....|....*....|....
gi 507222356 259 RGLVRGQFFTRDGVLVASTAQEGV 282
Cdd:cd03440   77 SVTVEVEVRNEDGKLVATATATFV 100
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 30-108 2.82e-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: 36.68  E-value: 2.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507222356  30 GLRAVFGGQVMGQALSAAKQTVASDRQ------VHSFHSYFLRPGDANRPIVYDVENIRDGQTVSTRRVKAI-QGGKPIF 102
Cdd:cd03440   14 GGGIVHGGLLLALADEAAGAAAARLGGrglgavTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRnEDGKLVA 93


                 ....*.
gi 507222356 103 YLNASF 108
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.
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