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Conserved domains on  [gi|156120525|ref|NP_001095408|]
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acyl-coenzyme A thioesterase 2, mitochondrial [Bos taurus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
246-455 1.18e-124

BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C terminal of acyl-CoA thioester hydrolases and bile acid-CoA:amino acid N-acetyltransferases (BAAT).


:

Pssm-ID: 430252 [Multi-domain]  Cd Length: 211  Bit Score: 360.83  E-value: 1.18e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120525  246 LHLEYFEEAVNYLLNHPQVKGPGVGLLGISKGGELCLSMASFLKGISAAVIINGSVAYVGGNLHYKGEIMPPVGFNQNRI 325
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120525  326 KMTKDGFVDIVEVLNSPLEGPDQKSFIPVERAECPFLFLVGQDDHNWKSEFYANEASKRLQAHGK-AKPQVICYPGTGHY 404
Cdd:pfam08840  81 KVNKDGLLDIRDMFNDPLSKPDPKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKeVEVQLVCYPGAGHL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 156120525  405 IEPPYFPLCPASLHTIVGAPVIWGGEPRAHARAQVDAWQQLQTFFHKHLGG 455
Cdd:pfam08840 161 IEPPYFPHCGASFHALVGMPVLWGGEPKAHAKAQEDAWKKIQAFFHKHLGG 211
Bile_Hydr_Trans pfam04775
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
59-183 3.05e-57

Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini of acyl-CoA thioester hydrolase and bile acid-CoA:amino acid N-acetyltransferase (BAAT). This region is not thought to contain the active site of either enzyme. Thioesterase isoforms have been identified in peroxisomes, cytoplasm and mitochondria, where they are thought to have distinct functions in lipid metabolism. For example, in peroxisomes, the hydrolase acts on bile-CoA esters.


:

Pssm-ID: 461422  Cd Length: 127  Bit Score: 185.13  E-value: 3.05e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120525   59 DEPVRITVRGLAPGQPVTLRASLRDEKGALFRAHARYCADAAGLLDLERAPALGGSFTGLEPMGLFWAMEPEKPF-LRLV 137
Cdd:pfam04775   1 DEPVHIRVSGLPPGQPVTLRALLTDEKGGLFESYAVYRADENGEVDLSRDAPLGGSYTGVDPMGLFWSMKPEPGFrPRLY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 156120525  138 KRDVQ-TPFAVELEVLDNHEPRvGRLLGRVVHERDFLAPGVRREPVR 183
Cdd:pfam04775  81 KRDVLpTPFVVTLSVYDGSEES-GKPLASVTVERWYMAPGVRRIEVR 126
Axe1 super family cl34617
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, ...
182-295 1.27e-05

Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism];


The actual alignment was detected with superfamily member COG3458:

Pssm-ID: 442681 [Multi-domain]  Cd Length: 318  Bit Score: 47.11  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120525 182 VRAGRVRATLFLPPEPGPFPGIVDILGAGGG-LLEYRASLLAGKGFAVMAL---------------AYYNYEDLP----K 241
Cdd:COG3458   64 FGGARIYGWLLRPKGEGPLPAVVEFHGYGGGrGLPHEDLDWAAAGYAVLVMdtrgqgsswgdtpdpGGYSGGALPgymtR 143
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156120525 242 GLENLHLEYFEE-------AVNYLLNHPQVKGPGVGLLGISKGGELCLSMASFLKGISAAV 295
Cdd:COG3458  144 GIDDPDTYYYRRvyldavrAVDALRSLPEVDGKRIGVTGGSQGGGLALAAAALDPRVKAAA 204
 
Name Accession Description Interval E-value
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
246-455 1.18e-124

BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C terminal of acyl-CoA thioester hydrolases and bile acid-CoA:amino acid N-acetyltransferases (BAAT).


Pssm-ID: 430252 [Multi-domain]  Cd Length: 211  Bit Score: 360.83  E-value: 1.18e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120525  246 LHLEYFEEAVNYLLNHPQVKGPGVGLLGISKGGELCLSMASFLKGISAAVIINGSVAYVGGNLHYKGEIMPPVGFNQNRI 325
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120525  326 KMTKDGFVDIVEVLNSPLEGPDQKSFIPVERAECPFLFLVGQDDHNWKSEFYANEASKRLQAHGK-AKPQVICYPGTGHY 404
Cdd:pfam08840  81 KVNKDGLLDIRDMFNDPLSKPDPKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKeVEVQLVCYPGAGHL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 156120525  405 IEPPYFPLCPASLHTIVGAPVIWGGEPRAHARAQVDAWQQLQTFFHKHLGG 455
Cdd:pfam08840 161 IEPPYFPHCGASFHALVGMPVLWGGEPKAHAKAQEDAWKKIQAFFHKHLGG 211
Bile_Hydr_Trans pfam04775
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
59-183 3.05e-57

Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini of acyl-CoA thioester hydrolase and bile acid-CoA:amino acid N-acetyltransferase (BAAT). This region is not thought to contain the active site of either enzyme. Thioesterase isoforms have been identified in peroxisomes, cytoplasm and mitochondria, where they are thought to have distinct functions in lipid metabolism. For example, in peroxisomes, the hydrolase acts on bile-CoA esters.


Pssm-ID: 461422  Cd Length: 127  Bit Score: 185.13  E-value: 3.05e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120525   59 DEPVRITVRGLAPGQPVTLRASLRDEKGALFRAHARYCADAAGLLDLERAPALGGSFTGLEPMGLFWAMEPEKPF-LRLV 137
Cdd:pfam04775   1 DEPVHIRVSGLPPGQPVTLRALLTDEKGGLFESYAVYRADENGEVDLSRDAPLGGSYTGVDPMGLFWSMKPEPGFrPRLY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 156120525  138 KRDVQ-TPFAVELEVLDNHEPRvGRLLGRVVHERDFLAPGVRREPVR 183
Cdd:pfam04775  81 KRDVLpTPFVVTLSVYDGSEES-GKPLASVTVERWYMAPGVRRIEVR 126
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
185-449 1.38e-15

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 75.77  E-value: 1.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120525 185 GRVRATLFLPPEPGPFPGIVDILGAGGGLLEYR--ASLLAGKGFAVMALAYYNYEDLPKGLE-----------NLHLEYF 251
Cdd:COG0412   14 VTLPGYLARPAGGGPRPGVVVLHEIFGLNPHIRdvARRLAAAGYVVLAPDLYGRGGPGDDPDearalmgaldpELLAADL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120525 252 EEAVNYLLNHPQVKGPGVGLLGISKGGELCLSMASFLKGISAAVIINGSvayvggnlhykgeimppvgfnqnrikmtkdg 331
Cdd:COG0412   94 RAALDWLKAQPEVDAGRVGVVGFCFGGGLALLAAARGPDLAAAVSFYGG------------------------------- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120525 332 fvdivevlnspleGPDQKSFIPVERAECPFLFLVGQDDHNWKSEfYANEASKRLQAHGKAKpQVICYPGTGHYIEPPyfp 411
Cdd:COG0412  143 -------------LPADDLLDLAARIKAPVLLLYGEKDPLVPPE-QVAALEAALAAAGVDV-ELHVYPGAGHGFTNP--- 204
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 156120525 412 lcpaslhtivgapviwgGEPRAHARAQVDAWQQLQTFF 449
Cdd:COG0412  205 -----------------GRPRYDPAAAEDAWQRTLAFL 225
Axe1 COG3458
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, ...
182-295 1.27e-05

Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442681 [Multi-domain]  Cd Length: 318  Bit Score: 47.11  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120525 182 VRAGRVRATLFLPPEPGPFPGIVDILGAGGG-LLEYRASLLAGKGFAVMAL---------------AYYNYEDLP----K 241
Cdd:COG3458   64 FGGARIYGWLLRPKGEGPLPAVVEFHGYGGGrGLPHEDLDWAAAGYAVLVMdtrgqgsswgdtpdpGGYSGGALPgymtR 143
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156120525 242 GLENLHLEYFEE-------AVNYLLNHPQVKGPGVGLLGISKGGELCLSMASFLKGISAAV 295
Cdd:COG3458  144 GIDDPDTYYYRRvyldavrAVDALRSLPEVDGKRIGVTGGSQGGGLALAAAALDPRVKAAA 204
 
Name Accession Description Interval E-value
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
246-455 1.18e-124

BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C terminal of acyl-CoA thioester hydrolases and bile acid-CoA:amino acid N-acetyltransferases (BAAT).


Pssm-ID: 430252 [Multi-domain]  Cd Length: 211  Bit Score: 360.83  E-value: 1.18e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120525  246 LHLEYFEEAVNYLLNHPQVKGPGVGLLGISKGGELCLSMASFLKGISAAVIINGSVAYVGGNLHYKGEIMPPVGFNQNRI 325
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120525  326 KMTKDGFVDIVEVLNSPLEGPDQKSFIPVERAECPFLFLVGQDDHNWKSEFYANEASKRLQAHGK-AKPQVICYPGTGHY 404
Cdd:pfam08840  81 KVNKDGLLDIRDMFNDPLSKPDPKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKeVEVQLVCYPGAGHL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 156120525  405 IEPPYFPLCPASLHTIVGAPVIWGGEPRAHARAQVDAWQQLQTFFHKHLGG 455
Cdd:pfam08840 161 IEPPYFPHCGASFHALVGMPVLWGGEPKAHAKAQEDAWKKIQAFFHKHLGG 211
Bile_Hydr_Trans pfam04775
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
59-183 3.05e-57

Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini of acyl-CoA thioester hydrolase and bile acid-CoA:amino acid N-acetyltransferase (BAAT). This region is not thought to contain the active site of either enzyme. Thioesterase isoforms have been identified in peroxisomes, cytoplasm and mitochondria, where they are thought to have distinct functions in lipid metabolism. For example, in peroxisomes, the hydrolase acts on bile-CoA esters.


Pssm-ID: 461422  Cd Length: 127  Bit Score: 185.13  E-value: 3.05e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120525   59 DEPVRITVRGLAPGQPVTLRASLRDEKGALFRAHARYCADAAGLLDLERAPALGGSFTGLEPMGLFWAMEPEKPF-LRLV 137
Cdd:pfam04775   1 DEPVHIRVSGLPPGQPVTLRALLTDEKGGLFESYAVYRADENGEVDLSRDAPLGGSYTGVDPMGLFWSMKPEPGFrPRLY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 156120525  138 KRDVQ-TPFAVELEVLDNHEPRvGRLLGRVVHERDFLAPGVRREPVR 183
Cdd:pfam04775  81 KRDVLpTPFVVTLSVYDGSEES-GKPLASVTVERWYMAPGVRRIEVR 126
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
185-449 1.38e-15

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 75.77  E-value: 1.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120525 185 GRVRATLFLPPEPGPFPGIVDILGAGGGLLEYR--ASLLAGKGFAVMALAYYNYEDLPKGLE-----------NLHLEYF 251
Cdd:COG0412   14 VTLPGYLARPAGGGPRPGVVVLHEIFGLNPHIRdvARRLAAAGYVVLAPDLYGRGGPGDDPDearalmgaldpELLAADL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120525 252 EEAVNYLLNHPQVKGPGVGLLGISKGGELCLSMASFLKGISAAVIINGSvayvggnlhykgeimppvgfnqnrikmtkdg 331
Cdd:COG0412   94 RAALDWLKAQPEVDAGRVGVVGFCFGGGLALLAAARGPDLAAAVSFYGG------------------------------- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120525 332 fvdivevlnspleGPDQKSFIPVERAECPFLFLVGQDDHNWKSEfYANEASKRLQAHGKAKpQVICYPGTGHYIEPPyfp 411
Cdd:COG0412  143 -------------LPADDLLDLAARIKAPVLLLYGEKDPLVPPE-QVAALEAALAAAGVDV-ELHVYPGAGHGFTNP--- 204
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 156120525 412 lcpaslhtivgapviwgGEPRAHARAQVDAWQQLQTFF 449
Cdd:COG0412  205 -----------------GRPRYDPAAAEDAWQRTLAFL 225
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
186-411 1.18e-14

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 73.13  E-value: 1.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120525 186 RVRATLFLPPEPGPFPGIVDILGAGGGLLE---YRASLLAGKGFAVMALAYYNYEDLPKGLENLHLEYFEEAVNYLLNHP 262
Cdd:COG1506    9 TLPGWLYLPADGKKYPVVVYVHGGPGSRDDsflPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVDDVLAAIDYLAARP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120525 263 QVKGPGVGLLGISKGGELCLSMASFLKGISAAVIINGSVA----YVGGNLHYKGEIMPpvGFNQNRIKMTKdgfvdivev 338
Cdd:COG1506   89 YVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSdlrsYYGTTREYTERLMG--GPWEDPEAYAA--------- 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156120525 339 lNSPLEGpdqksfipVERAECPFLFLVGQDDHNWKSEfYANEASKRLQAHGKAKpQVICYPGTGHYIEPPYFP 411
Cdd:COG1506  158 -RSPLAY--------ADKLKTPLLLIHGEADDRVPPE-QAERLYEALKKAGKPV-ELLVYPGEGHGFSGAGAP 219
Axe1 COG3458
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, ...
182-295 1.27e-05

Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442681 [Multi-domain]  Cd Length: 318  Bit Score: 47.11  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120525 182 VRAGRVRATLFLPPEPGPFPGIVDILGAGGG-LLEYRASLLAGKGFAVMAL---------------AYYNYEDLP----K 241
Cdd:COG3458   64 FGGARIYGWLLRPKGEGPLPAVVEFHGYGGGrGLPHEDLDWAAAGYAVLVMdtrgqgsswgdtpdpGGYSGGALPgymtR 143
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156120525 242 GLENLHLEYFEE-------AVNYLLNHPQVKGPGVGLLGISKGGELCLSMASFLKGISAAV 295
Cdd:COG3458  144 GIDDPDTYYYRRvyldavrAVDALRSLPEVDGKRIGVTGGSQGGGLALAAAALDPRVKAAA 204
 
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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