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Conserved domains on  [gi|17556462|ref|NP_497593|]
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ACB domain-containing protein [Caenorhabditis elegans]

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

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List of domain hits

 Name Accession Description Interval E-value
B41 super family cl33382
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 71-137 2.03e-04

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


The actual alignment was detected with superfamily member smart00295:

Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 39.59  E-value: 2.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556462     71 HGDFEVPAERYEELNALYMQATVGDYDGNTALKCG--------------------------QYWKKHSGKTQIEAIREYI 124
Cdd:smart00295 108 EGRLPCPEEEALLLAALALQAEFGDYDEELHDLRGelslkrflpkqlldsrklkewrerivELHKELIGLSPEEAKLKYL 187

                           90
                   ....*....|...
gi 17556462    125 KLTnQTLTKYGWN 137
Cdd:smart00295 188 ELA-RKLPTYGVE 199
 
Name Accession Description Interval E-value
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 71-137 2.03e-04

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 39.59  E-value: 2.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556462     71 HGDFEVPAERYEELNALYMQATVGDYDGNTALKCG--------------------------QYWKKHSGKTQIEAIREYI 124
Cdd:smart00295 108 EGRLPCPEEEALLLAALALQAEFGDYDEELHDLRGelslkrflpkqlldsrklkewrerivELHKELIGLSPEEAKLKYL 187

                           90
                   ....*....|...
gi 17556462    125 KLTnQTLTKYGWN 137
Cdd:smart00295 188 ELA-RKLPTYGVE 199
ACBP cd00435
Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a ...
 83-135 2.28e-03

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: 34.99  E-value: 2.28e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17556462  83 ELNALYMQATVGDYD----GNTALKcGQY----WKKHSGKTQIEAIREYIKLTNQTLTKYG 135
Cdd:cd00435  26 QLYSLYKQATVGDCNterpGMFDLK-GRAkwdaWNSLKGMSKEDAMKAYIAKVEELIAKYA 85
 
Name Accession Description Interval E-value
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 71-137 2.03e-04

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 39.59  E-value: 2.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556462     71 HGDFEVPAERYEELNALYMQATVGDYDGNTALKCG--------------------------QYWKKHSGKTQIEAIREYI 124
Cdd:smart00295 108 EGRLPCPEEEALLLAALALQAEFGDYDEELHDLRGelslkrflpkqlldsrklkewrerivELHKELIGLSPEEAKLKYL 187

                           90
                   ....*....|...
gi 17556462    125 KLTnQTLTKYGWN 137
Cdd:smart00295 188 ELA-RKLPTYGVE 199
ACBP cd00435
Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a ...
 83-135 2.28e-03

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: 34.99  E-value: 2.28e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17556462  83 ELNALYMQATVGDYD----GNTALKcGQY----WKKHSGKTQIEAIREYIKLTNQTLTKYG 135
Cdd:cd00435  26 QLYSLYKQATVGDCNterpGMFDLK-GRAkwdaWNSLKGMSKEDAMKAYIAKVEELIAKYA 85
 
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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