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:

"
YVTN repeat-like/Quinoprotein amine dehydrogenase
".

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 103978: Protein Bm13695, isoform d

There are 2 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
Mitogen-activated protein kinase. [EC: 2.7.11.24]
ATP + a protein = ADP + a phosphoprotein.
  • Phosphorylation of specific tyrosine and threonine residues in the activation loop of this enzyme by EC 2.7.12.2 is necessary for enzyme activation.
  • Once activated, the enzyme phosphorylates target substrates on serine or threonine residues followed by a proline.
  • A distinguishing feature of all MAPKs is the conserved sequence Thr- Xaa-Tyr (TXY).
  • Mitogen-activated protein kinase (MAPK) signal transduction pathways are among the most widespread mechanisms of cellular regulation.
  • Mammalian MAPK pathways can be recruited by a wide variety of stimuli including hormones (e.g. insulin and growth hormone), mitogens (e.g. epidermal growth factor and platelet-derived growth factor), vasoactive peptides (e.g. angiotensin-II and endothelin), inflammatory cytokines of the tumor necrosis factor (TNF) family and environmental stresses such as osmotic shock, ionizing radiation and ischemeic injury.
  • Formerly EC 2.7.1.37.
4 A0A0B0PJA8 A0A0B0PJA8 A0A0B0PNV9 A0A0B0PNV9
Histone acetyltransferase. [EC: 2.3.1.48]
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine.
  • A group of enzymes acetylating histones.
  • Several of the enzymes can also acetylate lysines in other proteins.
2 B7Q8X2 B7Q8X2