The name of this superfamily has been modified since the most recent official CATH+ release (v4_4_0). At the point of the last release, this superfamily was named:

"
DNA helicase RuvA subunit, C-terminal 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 14: Non-specific serine/threonine protein kinase

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
Non-specific serine/threonine protein kinase. [EC: 2.7.11.1]
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 2.7.1.37 and EC 2.7.1.70.
140 A0A096MX27 A0A096MX27 A0A096MX27 A0A096MX27 A0A096MX27 A0A096MX27 A0A096MX27 A0A096MX27 A0A096MX27 A0A2K5E9M7
(130 more...)
[Hydroxymethylglutaryl-CoA reductase (NADPH)] kinase. [EC: 2.7.11.31]
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)] = ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate.
  • Activated by AMP.
  • EC 1.1.1.34 is inactivated by the phosphorylation of the enzyme protein.
  • Histones can also act as acceptors.
  • Can also phosphorylate EC 6.4.1.2 and EC 3.1.1.79.
  • Thr-172 within the catalytic subunit (alpha-subunit) is the major site phosphorylated by the AMP-activated protein kinase kinase.
  • GTP can act instead of ATP.
  • Formerly EC 2.7.1.109.
140 A0A096MX27 A0A096MX27 A0A096MX27 A0A096MX27 A0A096MX27 A0A096MX27 A0A096MX27 A0A096MX27 A0A096MX27 A0A2K5E9M7
(130 more...)
[Acetyl-CoA carboxylase] kinase. [EC: 2.7.11.27]
ATP + [acetyl-CoA carboxylase] = ADP + [acetyl-CoA carboxylase] phosphate.
  • Phosphorylates and inactivates EC 6.4.1.2, which can be dephosphorylated and reactivated by EC 3.1.3.17.
  • More active toward the dimeric form of acetyl-CoA carboxylase than the polymeric form.
  • Phosphorylates serine residues.
  • Formerly EC 2.7.1.111 and EC 2.7.1.128.
140 A0A096MX27 A0A096MX27 A0A096MX27 A0A096MX27 A0A096MX27 A0A096MX27 A0A096MX27 A0A096MX27 A0A096MX27 A0A2K5E9M7
(130 more...)
[Tau protein] kinase. [EC: 2.7.11.26]
ATP + [tau protein] = ADP + [tau protein] phosphate.
  • Activated by tubulin.
  • Involved in the formation of paired helical filaments, which are the main fibrous component of all fibrillary lesions in brain and are associated with Alzheimer's disease.
  • Formerly EC 2.7.1.135.
52 A0A2K5E9M7 A0A2K5E9M7 A0A2K5E9M7 A0A2K5E9M7 A0A2K5E9M7 A0A2K5E9M7 A0A2K5E9M7 A0A2K5R157 A0A2K5R157 A0A2K5R157
(42 more...)
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