NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2462557646|ref|XP_054173224|]
View 

acyl-CoA-binding domain-containing protein 4 isoform X12 [Homo sapiens]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 13-97 4.27e-37

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: 126.67  E-value: 4.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557646  13 QKQFQAAVSVIQNLPKngsyRPSYEEMLRFYSYYKQATMGPCLVPRPGFWDPIGRYKWDAWNSLGKMSREEAMSAYITEM 92
Cdd:cd00435     2 QEEFEAAAEKVKKLKT----KPSNEEKLQLYSLYKQATVGDCNTERPGMFDLKGRAKWDAWNSLKGMSKEDAMKAYIAKV 77


                  ....*.
gi 2462557646  93 K-LVAQ 97
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 ...
 13-97 4.27e-37

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: 126.67  E-value: 4.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557646  13 QKQFQAAVSVIQNLPKngsyRPSYEEMLRFYSYYKQATMGPCLVPRPGFWDPIGRYKWDAWNSLGKMSREEAMSAYITEM 92
Cdd:cd00435     2 QEEFEAAAEKVKKLKT----KPSNEEKLQLYSLYKQATVGDCNTERPGMFDLKGRAKWDAWNSLKGMSKEDAMKAYIAKV 77


                  ....*.
gi 2462557646  93 K-LVAQ 97
Cdd:cd00435    78 EeLIAK 83
ACBP pfam00887
Acyl CoA binding protein;
13-89 1.81e-36

Acyl CoA binding protein;


Pssm-ID: 459982  Cd Length: 76  Bit Score: 124.63  E-value: 1.81e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462557646  13 QKQFQAAVSVIQNLPKngsyRPSYEEMLRFYSYYKQATMGPCLVPRPGFWDPIGRYKWDAWNSLGKMSREEAMSAYI 89
Cdd:pfam00887   1 EEKFEAAAEFVKKLKS----KPSNEEKLELYGLYKQATVGDCNTPRPGMFDFKGKAKWDAWKKLGGMSKEEAMAKYV 73
ACB COG4281
Acyl-CoA-binding protein [Lipid transport and metabolism];
11-89 4.91e-26

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


Pssm-ID: 443422  Cd Length: 87  Bit Score: 98.00  E-value: 4.91e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462557646  11 DCQKQFQAAVSVIQNLPKngsyRPSYEEMLRFYSYYKQATMGPCLVPRPGFWDPIGRYKWDAWNSLGKMSREEAMSAYI 89
Cdd:COG4281     3 DLQAAFEAAVARVKTLTE----RPDNDTLLKLYALYKQATEGDVTGKRPGMTDFVGRAKYDAWAQLKGMSKDEAMQQYI 77
PTZ00458 PTZ00458
acyl CoA binding protein; Provisional
 16-89 8.96e-13

acyl CoA binding protein; Provisional


Pssm-ID: 185637  Cd Length: 90  Bit Score: 62.92  E-value: 8.96e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462557646  16 FQAAVSVIQNLPKNGSYrpSYEEMLRFYSYYKQATMGPCLVPRPGFWDPIGRYKWDAWNSLGKMSREEAMSAYI 89
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 ...
 13-97 4.27e-37

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: 126.67  E-value: 4.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557646  13 QKQFQAAVSVIQNLPKngsyRPSYEEMLRFYSYYKQATMGPCLVPRPGFWDPIGRYKWDAWNSLGKMSREEAMSAYITEM 92
Cdd:cd00435     2 QEEFEAAAEKVKKLKT----KPSNEEKLQLYSLYKQATVGDCNTERPGMFDLKGRAKWDAWNSLKGMSKEDAMKAYIAKV 77


                  ....*.
gi 2462557646  93 K-LVAQ 97
Cdd:cd00435    78 EeLIAK 83
ACBP pfam00887
Acyl CoA binding protein;
13-89 1.81e-36

Acyl CoA binding protein;


Pssm-ID: 459982  Cd Length: 76  Bit Score: 124.63  E-value: 1.81e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462557646  13 QKQFQAAVSVIQNLPKngsyRPSYEEMLRFYSYYKQATMGPCLVPRPGFWDPIGRYKWDAWNSLGKMSREEAMSAYI 89
Cdd:pfam00887   1 EEKFEAAAEFVKKLKS----KPSNEEKLELYGLYKQATVGDCNTPRPGMFDFKGKAKWDAWKKLGGMSKEEAMAKYV 73
ACB COG4281
Acyl-CoA-binding protein [Lipid transport and metabolism];
11-89 4.91e-26

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


Pssm-ID: 443422  Cd Length: 87  Bit Score: 98.00  E-value: 4.91e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462557646  11 DCQKQFQAAVSVIQNLPKngsyRPSYEEMLRFYSYYKQATMGPCLVPRPGFWDPIGRYKWDAWNSLGKMSREEAMSAYI 89
Cdd:COG4281     3 DLQAAFEAAVARVKTLTE----RPDNDTLLKLYALYKQATEGDVTGKRPGMTDFVGRAKYDAWAQLKGMSKDEAMQQYI 77
PTZ00458 PTZ00458
acyl CoA binding protein; Provisional
 16-89 8.96e-13

acyl CoA binding protein; Provisional


Pssm-ID: 185637  Cd Length: 90  Bit Score: 62.92  E-value: 8.96e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462557646  16 FQAAVSVIQNLPKNGSYrpSYEEMLRFYSYYKQATMGPCLVPRPGFWDPIGRYKWDAWNSLGKMSREEAMSAYI 89
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