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Conserved domains on  [gi|755542479|ref|XP_011242377|]
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acyl-coenzyme A thioesterase 5 isoform X2 [Mus musculus]

Protein Classification

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 2.56e-59

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: 184.36  E-value: 2.56e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542479   16 DEPLSIAVRGLAPEQPVTLRTALRDEKGALFRAHARYRADSHGELDLARTPALGGSFSGLEPMGLLWAMEPDRPFW-RLI 94
Cdd:pfam04775   1 DEPVHIRVSGLPPGQPVTLRALLTDEKGGLFESYAVYRADENGEVDLSRDAPLGGSYTGVDPMGLFWSMKPEPGFRpRLY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 755542479   95 KRDVQ-TPFVVELEVLDGHEPDgGRLLARAVHERHFMAPGVRRVPVRE 141
Cdd:pfam04775  81 KRDVLpTPFVVTLSVYDGSEES-GKPLASVTVERWYMAPGVRRIEVRE 127
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 203-221 9.35e-05

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member pfam08840:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 211  Bit Score: 42.27  E-value: 9.35e-05
                          10
                  ....*....|....*....
gi 755542479  203 LHLEYFEEAVTYLLSHPQV 221
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKV 19
DLH super family cl43135
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
142-223 1.04e-04

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


The actual alignment was detected with superfamily member COG0412:

Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 42.26  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542479 142 GRVRATLFLPPGTGPFPGII---DLFGVGGGlLEYRASLLAGKGFAVMALAYYKYDDLPKVIDI-----------LHLEY 207
Cdd:COG0412   14 VTLPGYLARPAGGGPRPGVVvlhEIFGLNPH-IRDVARRLAAAGYVVLAPDLYGRGGPGDDPDEaralmgaldpeLLAAD 92

                         90
                 ....*....|....*.
gi 755542479 208 FEEAVTYLLSHPQVRT 223
Cdd:COG0412   93 LRAALDWLKAQPEVDA 108
 
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 2.56e-59

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: 184.36  E-value: 2.56e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542479   16 DEPLSIAVRGLAPEQPVTLRTALRDEKGALFRAHARYRADSHGELDLARTPALGGSFSGLEPMGLLWAMEPDRPFW-RLI 94
Cdd:pfam04775   1 DEPVHIRVSGLPPGQPVTLRALLTDEKGGLFESYAVYRADENGEVDLSRDAPLGGSYTGVDPMGLFWSMKPEPGFRpRLY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 755542479   95 KRDVQ-TPFVVELEVLDGHEPDgGRLLARAVHERHFMAPGVRRVPVRE 141
Cdd:pfam04775  81 KRDVLpTPFVVTLSVYDGSEES-GKPLASVTVERWYMAPGVRRIEVRE 127
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
 203-221 9.35e-05

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: 42.27  E-value: 9.35e-05
                          10
                  ....*....|....*....
gi 755542479  203 LHLEYFEEAVTYLLSHPQV 221
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKV 19
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
142-223 1.04e-04

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 42.26  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542479 142 GRVRATLFLPPGTGPFPGII---DLFGVGGGlLEYRASLLAGKGFAVMALAYYKYDDLPKVIDI-----------LHLEY 207
Cdd:COG0412   14 VTLPGYLARPAGGGPRPGVVvlhEIFGLNPH-IRDVARRLAAAGYVVLAPDLYGRGGPGDDPDEaralmgaldpeLLAAD 92

                         90
                 ....*....|....*.
gi 755542479 208 FEEAVTYLLSHPQVRT 223
Cdd:COG0412   93 LRAALDWLKAQPEVDA 108
 
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 2.56e-59

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: 184.36  E-value: 2.56e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542479   16 DEPLSIAVRGLAPEQPVTLRTALRDEKGALFRAHARYRADSHGELDLARTPALGGSFSGLEPMGLLWAMEPDRPFW-RLI 94
Cdd:pfam04775   1 DEPVHIRVSGLPPGQPVTLRALLTDEKGGLFESYAVYRADENGEVDLSRDAPLGGSYTGVDPMGLFWSMKPEPGFRpRLY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 755542479   95 KRDVQ-TPFVVELEVLDGHEPDgGRLLARAVHERHFMAPGVRRVPVRE 141
Cdd:pfam04775  81 KRDVLpTPFVVTLSVYDGSEES-GKPLASVTVERWYMAPGVRRIEVRE 127
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
 203-221 9.35e-05

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: 42.27  E-value: 9.35e-05
                          10
                  ....*....|....*....
gi 755542479  203 LHLEYFEEAVTYLLSHPQV 221
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKV 19
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
142-223 1.04e-04

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 42.26  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542479 142 GRVRATLFLPPGTGPFPGII---DLFGVGGGlLEYRASLLAGKGFAVMALAYYKYDDLPKVIDI-----------LHLEY 207
Cdd:COG0412   14 VTLPGYLARPAGGGPRPGVVvlhEIFGLNPH-IRDVARRLAAAGYVVLAPDLYGRGGPGDDPDEaralmgaldpeLLAAD 92

                         90
                 ....*....|....*.
gi 755542479 208 FEEAVTYLLSHPQVRT 223
Cdd:COG0412   93 LRAALDWLKAQPEVDA 108
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
136-221 1.19e-04

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 42.31  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755542479 136 RVPVREG-RVRATLFLPPGTGPFPGIIDLFGVGGGLLE---YRASLLAGKGFAVMALAYYKYDDLPKVIDILHLEYFEEA 211
Cdd:COG1506    1 TFKSADGtTLPGWLYLPADGKKYPVVVYVHGGPGSRDDsflPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVDDVLAA 80

                         90
                 ....*....|
gi 755542479 212 VTYLLSHPQV 221
Cdd:COG1506   81 IDYLAARPYV 90
 
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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