The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
14-3-3 domain
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 690: 14-3-3 GF14 Pi protein

There are 3 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Phospholipase A(2). [EC: 3.1.1.4]
Phosphatidylcholine + H(2)O = 1-acylglycerophosphocholine + a carboxylate.
  • Also acts on phosphatidylethanolamine, choline plasmalogen and phosphatides, removing the fatty acid attached to the 2-position.
4 A0A0D2N2P4 A8JGV6 P52908 Q7X7A7
6-phosphofructokinase. [EC: 2.7.1.11]
ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate.
  • D-tagatose 6-phosphate and sedoheptulose 7-phosphate can act as acceptors.
  • UTP, CTP and ITP can act as donors.
  • Not identical with EC 2.7.1.105.
1 A0A182V381
Protein S-acyltransferase. [EC: 2.3.1.225]
Palmitoyl-CoA + [protein]-L-cysteine = [protein]-S-palmitoyl-L-cysteine + CoA.
  • The enzyme catalyzes the posttranslational protein palmitoylation that plays a role in protein-membrane interactions, protein trafficking, and enzyme activity.
  • Palmitoylation increases the hydrophobicity of proteins or protein domains and contributes to their membrane association.
1 M7B6A7
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