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CATH Superfamily 1.25.10.10

Leucine-rich Repeat Variant

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:

"
Leucine-rich Repeat Variant
".

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 68662: Protein phosphatase 2A regulatory subunit

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
Protein-serine/threonine phosphatase. [EC: 3.1.3.16]
[a protein]-serine/threonine phosphate + H(2)O = [a protein]- serine/threonine + phosphate.
  • A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48).
  • The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1).
 7 A0A061HU79 A0A0J5PPM3 A2RAI7 A8J709 B0XP53 G3YDW8 Q4WJL0
[Phosphorylase] phosphatase. [EC: 3.1.3.17]
[Phosphorylase a] + 4 H(2)O = 2 [phosphorylase b] + 4 phosphate.
    		 2 Q92138 Q92139
    Proteasome endopeptidase complex. [EC: 3.4.25.1]
    Cleavage of peptide bonds with very broad specificity.
    • A 20-S protein composed of 28 subunits arranged in four rings of seven.
    • The outer rings are composed of alpha subunits, but the beta subunits forming the inner rings are responsible for peptidase activity.
    • In eukaryotic organisms there are up to seven different types of beta subunits, three of which may carry the N-terminal threonine residues that are the nucleophiles in catalysis, and show different specificities.
    • The molecule is barrel-shaped, and the active sites are on the inner surfaces.
    • Terminal apertures restrict access of substrates to the active sites.
    • Inhibited by mercurial reagents and some inhibitors of serine endopeptidases.
    • Belongs to peptidase family T1.
    • Formerly EC 3.4.22.21, EC 3.4.24.5 and EC 3.4.99.46.
    		 1 A0A1B0G4K6
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