  We identified latent periodicity in catalytic domains of approximately 85% of
serine/threonine and tyrosine protein kinases. Similar results were obtained
for other 22 protein domains. We also designed the method of noise
decomposition, which is aimed to distinguish between different periodicity
types of the same period length. The method is to be used in conjunction with
the cyclic profile alignment, and this combination is able to reveal
structure-related or function-related patterns of latent periodicity. Possible
origins of the periodic structure of protein kinase active sites are discussed.
Summarizing, we presume that latent periodicity is the common property of many
catalytic protein domains.
