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Conserved domains on  [gi|1039739823|ref|XP_017170456|]
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peroxisomal succinyl-coenzyme A thioesterase isoform X1 [Mus musculus]

Protein Classification

acyl-CoA thioesterase/bile acid-CoA:amino acid N-acyltransferase family protein( domain architecture ID 10521448)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Bile_Hydr_Trans pfam04775
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
 16-141 1.07e-58

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: 180.12  E-value: 1.07e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739823  16 DEPLSIAVRGLAPEQPVTLRSVLRDEKGALFRAHARYRADSHGELDLARVPALGGSFSGLEPMGLLWAMEPDRPFW-RLI 94
Cdd:pfam04775   1 DEPVHIRVSGLPPGQPVTLRALLTDEKGGLFESYAVYRADENGEVDLSRDAPLGGSYTGVDPMGLFWSMKPEPGFRpRLY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1039739823  95 KRDVQ-TPFLVELEVLDGHEPDgGRRLARTVHERHFMAPGVRRVPVRE 141
Cdd:pfam04775  81 KRDVLpTPFVVTLSVYDGSEES-GKPLASVTVERWYMAPGVRRIEVRE 127
 
Name Accession Description Interval E-value
Bile_Hydr_Trans pfam04775
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
 16-141 1.07e-58

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: 180.12  E-value: 1.07e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739823  16 DEPLSIAVRGLAPEQPVTLRSVLRDEKGALFRAHARYRADSHGELDLARVPALGGSFSGLEPMGLLWAMEPDRPFW-RLI 94
Cdd:pfam04775   1 DEPVHIRVSGLPPGQPVTLRALLTDEKGGLFESYAVYRADENGEVDLSRDAPLGGSYTGVDPMGLFWSMKPEPGFRpRLY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1039739823  95 KRDVQ-TPFLVELEVLDGHEPDgGRRLARTVHERHFMAPGVRRVPVRE 141
Cdd:pfam04775  81 KRDVLpTPFVVTLSVYDGSEES-GKPLASVTVERWYMAPGVRRIEVRE 127
 
Name Accession Description Interval E-value
Bile_Hydr_Trans pfam04775
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
 16-141 1.07e-58

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: 180.12  E-value: 1.07e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739823  16 DEPLSIAVRGLAPEQPVTLRSVLRDEKGALFRAHARYRADSHGELDLARVPALGGSFSGLEPMGLLWAMEPDRPFW-RLI 94
Cdd:pfam04775   1 DEPVHIRVSGLPPGQPVTLRALLTDEKGGLFESYAVYRADENGEVDLSRDAPLGGSYTGVDPMGLFWSMKPEPGFRpRLY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1039739823  95 KRDVQ-TPFLVELEVLDGHEPDgGRRLARTVHERHFMAPGVRRVPVRE 141
Cdd:pfam04775  81 KRDVLpTPFVVTLSVYDGSEES-GKPLASVTVERWYMAPGVRRIEVRE 127
 
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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