Eukaryotic protein kinases [1,2,3,4,5] are enzymes that belong to a very
extensive family of proteins which share a conserved catalytic core common to
both serine/threonine and tyrosine protein kinases. There are a number of
conserved regions in the catalytic domain of protein kinases. We have selected
two of these regions to build signature patterns. The first region, which is
located in the N-terminal extremity of the catalytic domain, is a glycine-rich
stretch of residues in the vicinity of a lysine residue, which has been shown
to be involved in ATP binding. The second region, which is located in the
central part of the catalytic domain, contains a conserved aspartic acid
residue which is important for the catalytic activity of the enzyme [6]; we
have derived two signature patterns for that region: one specific for serine/
threonine kinases and the other for tyrosine kinases. We also developed a
profile which is based on the alignment in [1] and covers the entire catalytic
domain.
Note:
If a protein analyzed includes the two protein kinase signatures, the
probability of it being a protein kinase is close to 100%
Note:
Eukaryotic-type protein kinases have also been found in prokaryotes
such as Myxococcus xanthus [11] and Yersinia pseudotuberculosis.
Note:
The patterns shown above has been updated since their publication in
[7].
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