NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|29387293|gb|AAH48371|]
View 

Acyl-Coenzyme A binding domain containing 4 [Mus musculus]

Protein Classification

acyl-CoA-binding protein( domain architecture ID 1012)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
ACBP super family cl00221
Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a ...
11-95 6.31e-35

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.


The actual alignment was detected with superfamily member cd00435:

Pssm-ID: 469667  Cd Length: 85  Bit Score: 122.43  E-value: 6.31e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29387293  11 QKQFQAAVSVIQNLPKngsyRPSYEEMLRFYSYYKQATMGPCLVPRPGFWDPIGRYKWDAWNRLGKMSREEAMSAYISEM 90
Cdd:cd00435   2 QEEFEAAAEKVKKLKT----KPSNEEKLQLYSLYKQATVGDCNTERPGMFDLKGRAKWDAWNSLKGMSKEDAMKAYIAKV 77

                ....*.
gi 29387293  91 K-LVAQ 95
Cdd:cd00435  78 EeLIAK 83
 
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 ...
11-95 6.31e-35

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: 122.43  E-value: 6.31e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29387293  11 QKQFQAAVSVIQNLPKngsyRPSYEEMLRFYSYYKQATMGPCLVPRPGFWDPIGRYKWDAWNRLGKMSREEAMSAYISEM 90
Cdd:cd00435   2 QEEFEAAAEKVKKLKT----KPSNEEKLQLYSLYKQATVGDCNTERPGMFDLKGRAKWDAWNSLKGMSKEDAMKAYIAKV 77

                ....*.
gi 29387293  91 K-LVAQ 95
Cdd:cd00435  78 EeLIAK 83
ACBP pfam00887
Acyl CoA binding protein;
11-88 9.88e-35

Acyl CoA binding protein;


Pssm-ID: 459982  Cd Length: 76  Bit Score: 121.55  E-value: 9.88e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29387293    11 QKQFQAAVSVIQNLPKngsyRPSYEEMLRFYSYYKQATMGPCLVPRPGFWDPIGRYKWDAWNRLGKMSREEAMSAYIS 88
Cdd:pfam00887   1 EEKFEAAAEFVKKLKS----KPSNEEKLELYGLYKQATVGDCNTPRPGMFDFKGKAKWDAWKKLGGMSKEEAMAKYVE 74
ACB COG4281
Acyl-CoA-binding protein [Lipid transport and metabolism];
9-87 4.74e-26

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


Pssm-ID: 443422  Cd Length: 87  Bit Score: 99.15  E-value: 4.74e-26
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29387293   9 DCQKQFQAAVSVIQNLPKngsyRPSYEEMLRFYSYYKQATMGPCLVPRPGFWDPIGRYKWDAWNRLGKMSREEAMSAYI 87
Cdd:COG4281   3 DLQAAFEAAVARVKTLTE----RPDNDTLLKLYALYKQATEGDVTGKRPGMTDFVGRAKYDAWAQLKGMSKDEAMQQYI 77
PTZ00458 PTZ00458
acyl CoA binding protein; Provisional
14-87 6.40e-11

acyl CoA binding protein; Provisional


Pssm-ID: 185637  Cd Length: 90  Bit Score: 57.91  E-value: 6.40e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29387293   14 FQAAVSVIQNLPKNGSYrpSYEEMLRFYSYYKQATMGPCLVPRPGFWDPIGRYKWDAWNRLGKMSREEAMSAYI 87
Cdd:PTZ00458   5 FEECVSFINSLPKTVNL--SVEIKLDLYKYYKQSTVGNCNIKEPSMFKYQDRKKYEAWKSIENLNREDAKKRYV 76
 
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 ...
11-95 6.31e-35

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: 122.43  E-value: 6.31e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29387293  11 QKQFQAAVSVIQNLPKngsyRPSYEEMLRFYSYYKQATMGPCLVPRPGFWDPIGRYKWDAWNRLGKMSREEAMSAYISEM 90
Cdd:cd00435   2 QEEFEAAAEKVKKLKT----KPSNEEKLQLYSLYKQATVGDCNTERPGMFDLKGRAKWDAWNSLKGMSKEDAMKAYIAKV 77

                ....*.
gi 29387293  91 K-LVAQ 95
Cdd:cd00435  78 EeLIAK 83
ACBP pfam00887
Acyl CoA binding protein;
11-88 9.88e-35

Acyl CoA binding protein;


Pssm-ID: 459982  Cd Length: 76  Bit Score: 121.55  E-value: 9.88e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29387293    11 QKQFQAAVSVIQNLPKngsyRPSYEEMLRFYSYYKQATMGPCLVPRPGFWDPIGRYKWDAWNRLGKMSREEAMSAYIS 88
Cdd:pfam00887   1 EEKFEAAAEFVKKLKS----KPSNEEKLELYGLYKQATVGDCNTPRPGMFDFKGKAKWDAWKKLGGMSKEEAMAKYVE 74
ACB COG4281
Acyl-CoA-binding protein [Lipid transport and metabolism];
9-87 4.74e-26

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


Pssm-ID: 443422  Cd Length: 87  Bit Score: 99.15  E-value: 4.74e-26
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29387293   9 DCQKQFQAAVSVIQNLPKngsyRPSYEEMLRFYSYYKQATMGPCLVPRPGFWDPIGRYKWDAWNRLGKMSREEAMSAYI 87
Cdd:COG4281   3 DLQAAFEAAVARVKTLTE----RPDNDTLLKLYALYKQATEGDVTGKRPGMTDFVGRAKYDAWAQLKGMSKDEAMQQYI 77
PTZ00458 PTZ00458
acyl CoA binding protein; Provisional
14-87 6.40e-11

acyl CoA binding protein; Provisional


Pssm-ID: 185637  Cd Length: 90  Bit Score: 57.91  E-value: 6.40e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29387293   14 FQAAVSVIQNLPKNGSYrpSYEEMLRFYSYYKQATMGPCLVPRPGFWDPIGRYKWDAWNRLGKMSREEAMSAYI 87
Cdd:PTZ00458   5 FEECVSFINSLPKTVNL--SVEIKLDLYKYYKQSTVGNCNIKEPSMFKYQDRKKYEAWKSIENLNREDAKKRYV 76
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH