Domain

Protein kinase-like domain (IPR011009)

Short name: Kinase-like_dom

Domain relationships

Description

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

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0016772 transferase activity, transferring phosphorus-containing groups

Cellular Component

No terms assigned in this category.

Contributing signatures

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