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:

Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

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 16437: Ubiquitin carboxyl-terminal hydrolase 14

There are 4 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
Ubiquitinyl hydrolase 1. [EC:]
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
  • Links to polypeptides smaller than 60 residues are hydrolyzed more readily than those to larger polypeptides.
  • Isoforms exist with quantitatively different specificities among the best known being UCH-L1 and UCH-L3, major proteins of the brain of mammals.
  • Inhibited by ubiquitin aldehyde (in which Gly76 is replaced by aminoacetaldehyde).
  • Belongs to peptidase family C12.
24 A0A178WJ56 A0A1D5QG07 A0A1J1H648 B3MPR0 B3N970 B4G7H7 B4KJF9 B4LR09 B4N080 B4NZ95
(14 more...)
Deleted entry. [EC:]
    2 B7PWY6 B9T7A3
    Non-specific serine/threonine protein kinase. [EC:]
    ATP + a protein = ADP + a phosphoprotein.
    • This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date.
    • Formerly EC and EC
    1 A0A061IHR2
    Peptidylprolyl isomerase. [EC:]
    Peptidylproline (omega=180) = peptidylproline (omega=0).
    • The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A.
    • Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli.
    • The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively.
    1 A0A182IY54