The domain within your query sequence starts at position 52 and ends at position 227; the E-value for the Pkinase domain shown below is 3.4e-26.

FKIKDKIGEGTFSSVYLATAQLQEGHEEKIALKHLIPTSHPMRIAAELQCLTVAGGQDNV
MGLKYCFRKNDHVVIAMPYLEHESFLDILNSLSFQEVREYMYNLFVALKRIHQFGIVHRD
VKPSNFLYNRRLKKYALVDFGLAQGTRDTKIELLKFVQSEAQQEDCSRNKYHGVVG

Pkinase

Pkinase
PFAM accession number:PF00069
Interpro abstract (IPR000719):

Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity [(PUBMED:3291115)]:

  • Serine/threonine-protein kinases
  • Tyrosine-protein kinases
  • Dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)

Protein kinase function is evolutionarily conserved from Escherichia coli to human [(PUBMED:12471243)]. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation [(PUBMED:12368087)]. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [(PUBMED:15078142)], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [(PUBMED:15320712)].

Eukaryotic protein kinases [(PUBMED:12734000), (PUBMED:7768349), (PUBMED:1835513), (PUBMED:1956325), (PUBMED:3291115)] are enzymes that belong to a very extensive family of proteins which share a conserved catalytic core common with both serine/threonine and tyrosine protein kinases. There are a number of conserved regions in the catalytic domain of protein kinases. In the N-terminal extremity of the catalytic domain there is a glycine-rich stretch of residues in the vicinity of a lysine residue, which has been shown to be involved in ATP binding. In the central part of the catalytic domain there is a conserved aspartic acid residue which is important for the catalytic activity of the enzyme [(PUBMED:1862342)].

This entry represents the protein kinase domain containing the catalytic function of protein kinases [(PUBMED:1956325)]. This domain is found in serine/threonine-protein kinases, tyrosine-protein kinases and dual specificity protein kinases.

GO process:protein phosphorylation (GO:0006468)
GO function:protein kinase activity (GO:0004672), ATP binding (GO:0005524)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Pkinase