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Conserved domains on  [gi|1953408426|ref|XP_038530072|]
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acyl-coenzyme A thioesterase 1 [Canis lupus familiaris]

Protein Classification

acyl-CoA thioesterase/bile acid-CoA:amino acid N-acyltransferase family protein( domain architecture ID 10521460)

acyl-CoA thioesterase/bile acid-CoA:amino acid N-acyltransferase (BAAT) family protein may catalyze the hydrolysis of acyl-CoA or catalyze the amidation of bile acids with the amino acids taurine and glycine

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  19508187|12369917
SCOP:  3000102

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 ...
234-443 9.28e-119

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: 345.42  E-value: 9.28e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408426 234 LHLEYFEEAVNYLLDHPQVKGLGVGLLGNSKGGELCLSMASFLKGITASVIINGSVANVGGTLHYKDEILPPVGLDANRM 313
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408426 314 RVTKDGLADILDVLNSPLEGADQKSFIPVERAESAFLFLVGLDDHNWKSEFYANEASKRLQAHGREQ-PQIICYPMAGHY 392
Cdd:pfam08840  81 KVNKDGLLDIRDMFNDPLSKPDPKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKEVeVQLVCYPGAGHL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953408426 393 IEPPYFPMCRASLHTLVGGPVIWGGEPRAHAMAQMDAWKQLQTFFHKHLGG 443
Cdd:pfam08840 161 IEPPYFPHCGASFHALVGMPVLWGGEPKAHAKAQEDAWKKIQAFFHKHLGG 211
Bile_Hydr_Trans pfam04775
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
47-171 5.39e-54

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: 176.27  E-value: 5.39e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408426  47 DEPVRISVRGLAPGQPVTLRASLRDERGALFRAHARYRADDRGLLDLARAPALGGSFVGLEPMGLLWALEPEKPL-VRLV 125
Cdd:pfam04775   1 DEPVHIRVSGLPPGQPVTLRALLTDEKGGLFESYAVYRADENGEVDLSRDAPLGGSYTGVDPMGLFWSMKPEPGFrPRLY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1953408426 126 KRDVQ-TPFAVELEVLDGHEPDaGRLLGRALHARHFLRPGVRRVPVR 171
Cdd:pfam04775  81 KRDVLpTPFVVTLSVYDGSEES-GKPLASVTVERWYMAPGVRRIEVR 126
 
Name Accession Description Interval E-value
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
234-443 9.28e-119

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: 345.42  E-value: 9.28e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408426 234 LHLEYFEEAVNYLLDHPQVKGLGVGLLGNSKGGELCLSMASFLKGITASVIINGSVANVGGTLHYKDEILPPVGLDANRM 313
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408426 314 RVTKDGLADILDVLNSPLEGADQKSFIPVERAESAFLFLVGLDDHNWKSEFYANEASKRLQAHGREQ-PQIICYPMAGHY 392
Cdd:pfam08840  81 KVNKDGLLDIRDMFNDPLSKPDPKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKEVeVQLVCYPGAGHL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953408426 393 IEPPYFPMCRASLHTLVGGPVIWGGEPRAHAMAQMDAWKQLQTFFHKHLGG 443
Cdd:pfam08840 161 IEPPYFPHCGASFHALVGMPVLWGGEPKAHAKAQEDAWKKIQAFFHKHLGG 211
Bile_Hydr_Trans pfam04775
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
47-171 5.39e-54

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: 176.27  E-value: 5.39e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408426  47 DEPVRISVRGLAPGQPVTLRASLRDERGALFRAHARYRADDRGLLDLARAPALGGSFVGLEPMGLLWALEPEKPL-VRLV 125
Cdd:pfam04775   1 DEPVHIRVSGLPPGQPVTLRALLTDEKGGLFESYAVYRADENGEVDLSRDAPLGGSYTGVDPMGLFWSMKPEPGFrPRLY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1953408426 126 KRDVQ-TPFAVELEVLDGHEPDaGRLLGRALHARHFLRPGVRRVPVR 171
Cdd:pfam04775  81 KRDVLpTPFVVTLSVYDGSEES-GKPLASVTVERWYMAPGVRRIEVR 126
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
174-399 7.29e-13

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 67.73  E-value: 7.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408426 174 RVRGTLFLPPEPGPFPGIVDIYGVGSGLLE---YRASLLAGKGFAVMALAYHNYEDLPKGLEILHLEYFEEAVNYLLDHP 250
Cdd:COG1506     9 TLPGWLYLPADGKKYPVVVYVHGGPGSRDDsflPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVDDVLAAIDYLAARP 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408426 251 QVKGLGVGLLGNSKGGELCLSMASFLKGITASVIINGSVANVggtlhykdeilppvgldANRMRVTKDGLADILDVLNSP 330
Cdd:COG1506    89 YVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDL-----------------RSYYGTTREYTERLMGGPWED 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408426 331 LEGADQKSFIP-VERAESAFLFLVGLDDHNWKSEfYANEASKRLQAHGREqPQIICYPMAGHYIEPPYFP 399
Cdd:COG1506   152 PEAYAARSPLAyADKLKTPLLLIHGEADDRVPPE-QAERLYEALKKAGKP-VELLVYPGEGHGFSGAGAP 219
 
Name Accession Description Interval E-value
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
234-443 9.28e-119

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: 345.42  E-value: 9.28e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408426 234 LHLEYFEEAVNYLLDHPQVKGLGVGLLGNSKGGELCLSMASFLKGITASVIINGSVANVGGTLHYKDEILPPVGLDANRM 313
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408426 314 RVTKDGLADILDVLNSPLEGADQKSFIPVERAESAFLFLVGLDDHNWKSEFYANEASKRLQAHGREQ-PQIICYPMAGHY 392
Cdd:pfam08840  81 KVNKDGLLDIRDMFNDPLSKPDPKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKEVeVQLVCYPGAGHL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953408426 393 IEPPYFPMCRASLHTLVGGPVIWGGEPRAHAMAQMDAWKQLQTFFHKHLGG 443
Cdd:pfam08840 161 IEPPYFPHCGASFHALVGMPVLWGGEPKAHAKAQEDAWKKIQAFFHKHLGG 211
Bile_Hydr_Trans pfam04775
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
47-171 5.39e-54

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: 176.27  E-value: 5.39e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408426  47 DEPVRISVRGLAPGQPVTLRASLRDERGALFRAHARYRADDRGLLDLARAPALGGSFVGLEPMGLLWALEPEKPL-VRLV 125
Cdd:pfam04775   1 DEPVHIRVSGLPPGQPVTLRALLTDEKGGLFESYAVYRADENGEVDLSRDAPLGGSYTGVDPMGLFWSMKPEPGFrPRLY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1953408426 126 KRDVQ-TPFAVELEVLDGHEPDaGRLLGRALHARHFLRPGVRRVPVR 171
Cdd:pfam04775  81 KRDVLpTPFVVTLSVYDGSEES-GKPLASVTVERWYMAPGVRRIEVR 126
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
174-399 7.29e-13

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 67.73  E-value: 7.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408426 174 RVRGTLFLPPEPGPFPGIVDIYGVGSGLLE---YRASLLAGKGFAVMALAYHNYEDLPKGLEILHLEYFEEAVNYLLDHP 250
Cdd:COG1506     9 TLPGWLYLPADGKKYPVVVYVHGGPGSRDDsflPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVDDVLAAIDYLAARP 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408426 251 QVKGLGVGLLGNSKGGELCLSMASFLKGITASVIINGSVANVggtlhykdeilppvgldANRMRVTKDGLADILDVLNSP 330
Cdd:COG1506    89 YVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDL-----------------RSYYGTTREYTERLMGGPWED 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408426 331 LEGADQKSFIP-VERAESAFLFLVGLDDHNWKSEfYANEASKRLQAHGREqPQIICYPMAGHYIEPPYFP 399
Cdd:COG1506   152 PEAYAARSPLAyADKLKTPLLLIHGEADDRVPPE-QAERLYEALKKAGKP-VELLVYPGEGHGFSGAGAP 219
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
173-437 8.68e-09

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 55.74  E-value: 8.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408426 173 GRVRGTLFLPPEPGPFPGIV---DIYGVGSGlLEYRASLLAGKGFAVMAL-AYHNYEDLPKGLEILHL----------EY 238
Cdd:COG0412    14 VTLPGYLARPAGGGPRPGVVvlhEIFGLNPH-IRDVARRLAAAGYVVLAPdLYGRGGPGDDPDEARALmgaldpellaAD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408426 239 FEEAVNYLLDHPQVKGLGVGLLGNSKGGELCLSMASFLKGITASVIINGsvanvggtlhykdeilppvgldanrmRVTKD 318
Cdd:COG0412    93 LRAALDWLKAQPEVDAGRVGVVGFCFGGGLALLAAARGPDLAAAVSFYG--------------------------GLPAD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408426 319 GLADILDVLNSPLegadqksfipveraesafLFLVGLDDHNWKSEfYANEASKRLQAHGREQpQIICYPMAGHYIEPPyf 398
Cdd:COG0412   147 DLLDLAARIKAPV------------------LLLYGEKDPLVPPE-QVAALEAALAAAGVDV-ELHVYPGAGHGFTNP-- 204
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1953408426 399 pmcraslhtlvggpviwgGEPRAHAMAQMDAWKQLQTFF 437
Cdd:COG0412   205 ------------------GRPRYDPAAAEDAWQRTLAFL 225
 
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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