The domain within your query sequence starts at position 25 and ends at position 281; the E-value for the Pkinase_Tyr domain shown below is 3.3e-35.

YEVGKIIGHGSYGTVYEAYYTKQKVMVAVKIISKKKASEDYLNKFLPREIQVMKVLRHKY
LINFYQAIETTSRVYIILELAQGGDVLEWIQRYGACAETLAGKWFSQMALGIAYLHSKGI
VHRLTPSLSAAGRDLKLENLLLDKRENVKISDFGFAKMVPSSQPVHSSPSYRQMNSLSHL
SQTYCGSFAYACPEILLGLPYNPFLSDTWSMGVILYTLVVARLPFDDTNLKKLLRETQKE
VTFPANLTISQECKVLA

Pkinase_Tyr

 Pkinase_Tyr
PFAM accession number:PF07714
Interpro abstract (IPR001245):

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)].

This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include catalytic domain of dual specificity kinases.
GO process:protein phosphorylation (GO:0006468)
GO function:protein kinase activity (GO:0004672)

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