Homologous Superfamily

Protein kinase-like domain superfamily (IPR011009)

Short name: Kinase-like_dom_sf

Overlapping entries



Protein kinases (IPR000719) modify other proteins by chemically adding phosphate groups to them. This process is fundamental to most signalling and regulatory processes in the eukaryotic cell [PMID: 12191603].

The protein kinases contain a catalytic core that is common to both serine/threonine and tyrosine protein kinases. The catalytic domain contains the nucleotide-binding site and the catalytic apparatus in an inter-lobe cleft. Structurally it shares functional and structural similarities with the ATP-grasp fold, which is found in enzymes that catalyse the formation of an amide bond.

The three-dimensional fold of the protein kinase catalytic domain is similar to domains found in several other proteins. These include:

  • the catalytic domain of phosphoinositide-3-kinase (PI3K), which phosphorylates phosphoinositides and, as such, is involved in a number of fundamental cellular processes such as apoptosis, proliferation, motility and adhesion [PMID: 11090628]
  • choline kinase, which catalyses the ATP-dependent phosphorylation of choline during the biosynthesis of phosphatidylcholine [PMID: 12791258]
  • 3',5'-aminoglycoside phosphotransferase type IIIa, a bacterial enzyme that confers resistance to a range of aminoglycoside antibiotics [PMID: 11467935]

This superfamily represents the protein-kinase domain and other related domains that share a similar structure.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.