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Conserved domains on  [gi|27229192|ref|NP_083069|]
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acyl-CoA-binding domain-containing protein 5 isoform c [Mus musculus]

Protein Classification

acyl-CoA-binding protein( domain architecture ID 10087334)

acyl-CoA-binding protein binds acyl-CoA esters and may play a role in housekeeping and/or trafficking

CATH:  1.20.80.10
Gene Ontology:  GO:0000062
PubMed:  16018771
SCOP:  4000745

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ACBP cd00435
Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a ...
 9-96 3.02e-40

Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a one-to-one binding mode with high specificity and affinity. Acyl-CoAs are important intermediates in fatty lipid synthesis and fatty acid degradation and play a role in regulation of intermediary metabolism and gene regulation. The suggested role of ACBP is to act as a intracellular acyl-CoA transporter and pool former. ACBPs are present in a large group of eukaryotic species and several tissue-specific isoforms have been detected.


:

Pssm-ID: 238248  Cd Length: 85  Bit Score: 139.38  E-value: 3.02e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229192   9 ETRFEAAVKVIQSLPKNgsfqPTNEMMLKFYSFYKQATEGPCKLSRPGFWDPIGRYKWDAWSSLGDMTKEEAMIAYVEEM 88
Cdd:cd00435   2 QEEFEAAAEKVKKLKTK----PSNEEKLQLYSLYKQATVGDCNTERPGMFDLKGRAKWDAWNSLKGMSKEDAMKAYIAKV 77


                ....*...
gi 27229192  89 KKIIETMP 96
Cdd:cd00435  78 EELIAKYA 85
 
Name Accession Description Interval E-value
ACBP cd00435
Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a ...
 9-96 3.02e-40

Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a one-to-one binding mode with high specificity and affinity. Acyl-CoAs are important intermediates in fatty lipid synthesis and fatty acid degradation and play a role in regulation of intermediary metabolism and gene regulation. The suggested role of ACBP is to act as a intracellular acyl-CoA transporter and pool former. ACBPs are present in a large group of eukaryotic species and several tissue-specific isoforms have been detected.


Pssm-ID: 238248  Cd Length: 85  Bit Score: 139.38  E-value: 3.02e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229192   9 ETRFEAAVKVIQSLPKNgsfqPTNEMMLKFYSFYKQATEGPCKLSRPGFWDPIGRYKWDAWSSLGDMTKEEAMIAYVEEM 88
Cdd:cd00435   2 QEEFEAAAEKVKKLKTK----PSNEEKLQLYSLYKQATVGDCNTERPGMFDLKGRAKWDAWNSLKGMSKEDAMKAYIAKV 77


                ....*...
gi 27229192  89 KKIIETMP 96
Cdd:cd00435  78 EELIAKYA 85
ACBP pfam00887
Acyl CoA binding protein;
9-86 1.50e-34

Acyl CoA binding protein;


Pssm-ID: 459982  Cd Length: 76  Bit Score: 123.86  E-value: 1.50e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27229192     9 ETRFEAAVKVIQSLPKngsfQPTNEMMLKFYSFYKQATEGPCKLSRPGFWDPIGRYKWDAWSSLGDMTKEEAMIAYVE 86
Cdd:pfam00887   1 EEKFEAAAEFVKKLKS----KPSNEEKLELYGLYKQATVGDCNTPRPGMFDFKGKAKWDAWKKLGGMSKEEAMAKYVE 74
ACB COG4281
Acyl-CoA-binding protein [Lipid transport and metabolism];
9-92 5.75e-27

Acyl-CoA-binding protein [Lipid transport and metabolism];


Pssm-ID: 443422  Cd Length: 87  Bit Score: 103.78  E-value: 5.75e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229192   9 ETRFEAAVKVIQSLPKngsfQPTNEMMLKFYSFYKQATEGPCKLSRPGFWDPIGRYKWDAWSSLGDMTKEEAMIAYVEEM 88
Cdd:COG4281   5 QAAFEAAVARVKTLTE----RPDNDTLLKLYALYKQATEGDVTGKRPGMTDFVGRAKYDAWAQLKGMSKDEAMQQYIDLV 80


                ....
gi 27229192  89 KKII 92
Cdd:COG4281  81 NSLL 84
PTZ00458 PTZ00458
acyl CoA binding protein; Provisional
 12-91 2.93e-12

acyl CoA binding protein; Provisional


Pssm-ID: 185637  Cd Length: 90  Bit Score: 62.53  E-value: 2.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229192   12 FEAAVKVIQSLPKNGSFqpTNEMMLKFYSFYKQATEGPCKLSRPGFWDPIGRYKWDAWSSLGDMTKEEAMIAYVEEMKKI 91
Cdd:PTZ00458   5 FEECVSFINSLPKTVNL--SVEIKLDLYKYYKQSTVGNCNIKEPSMFKYQDRKKYEAWKSIENLNREDAKKRYVEIVTEL 82
 
Name Accession Description Interval E-value
ACBP cd00435
Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a ...
 9-96 3.02e-40

Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a one-to-one binding mode with high specificity and affinity. Acyl-CoAs are important intermediates in fatty lipid synthesis and fatty acid degradation and play a role in regulation of intermediary metabolism and gene regulation. The suggested role of ACBP is to act as a intracellular acyl-CoA transporter and pool former. ACBPs are present in a large group of eukaryotic species and several tissue-specific isoforms have been detected.


Pssm-ID: 238248  Cd Length: 85  Bit Score: 139.38  E-value: 3.02e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229192   9 ETRFEAAVKVIQSLPKNgsfqPTNEMMLKFYSFYKQATEGPCKLSRPGFWDPIGRYKWDAWSSLGDMTKEEAMIAYVEEM 88
Cdd:cd00435   2 QEEFEAAAEKVKKLKTK----PSNEEKLQLYSLYKQATVGDCNTERPGMFDLKGRAKWDAWNSLKGMSKEDAMKAYIAKV 77


                ....*...
gi 27229192  89 KKIIETMP 96
Cdd:cd00435  78 EELIAKYA 85
ACBP pfam00887
Acyl CoA binding protein;
9-86 1.50e-34

Acyl CoA binding protein;


Pssm-ID: 459982  Cd Length: 76  Bit Score: 123.86  E-value: 1.50e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27229192     9 ETRFEAAVKVIQSLPKngsfQPTNEMMLKFYSFYKQATEGPCKLSRPGFWDPIGRYKWDAWSSLGDMTKEEAMIAYVE 86
Cdd:pfam00887   1 EEKFEAAAEFVKKLKS----KPSNEEKLELYGLYKQATVGDCNTPRPGMFDFKGKAKWDAWKKLGGMSKEEAMAKYVE 74
ACB COG4281
Acyl-CoA-binding protein [Lipid transport and metabolism];
9-92 5.75e-27

Acyl-CoA-binding protein [Lipid transport and metabolism];


Pssm-ID: 443422  Cd Length: 87  Bit Score: 103.78  E-value: 5.75e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229192   9 ETRFEAAVKVIQSLPKngsfQPTNEMMLKFYSFYKQATEGPCKLSRPGFWDPIGRYKWDAWSSLGDMTKEEAMIAYVEEM 88
Cdd:COG4281   5 QAAFEAAVARVKTLTE----RPDNDTLLKLYALYKQATEGDVTGKRPGMTDFVGRAKYDAWAQLKGMSKDEAMQQYIDLV 80


                ....
gi 27229192  89 KKII 92
Cdd:COG4281  81 NSLL 84
PTZ00458 PTZ00458
acyl CoA binding protein; Provisional
 12-91 2.93e-12

acyl CoA binding protein; Provisional


Pssm-ID: 185637  Cd Length: 90  Bit Score: 62.53  E-value: 2.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229192   12 FEAAVKVIQSLPKNGSFqpTNEMMLKFYSFYKQATEGPCKLSRPGFWDPIGRYKWDAWSSLGDMTKEEAMIAYVEEMKKI 91
Cdd:PTZ00458   5 FEECVSFINSLPKTVNL--SVEIKLDLYKYYKQSTVGNCNIKEPSMFKYQDRKKYEAWKSIENLNREDAKKRYVEIVTEL 82
 
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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