Abstract
Reversible protein phosphorylation by protein kinases and phosphatases is a common event in various cellular processes. The eukaryotic protein kinase superfamily, which is one of the largest superfamilies of eukaryotic proteins, plays several roles in cell signaling and diseases. We identified 482 eukaryotic protein kinases and 39 atypical protein kinases in the bovine genome, by searching publicly accessible genetic-sequence databases. Bovines have 512 putative protein kinases, each orthologous to a human kinase. Whereas orthologous kinase pairs are, on an average, 90.6% identical, orthologous kinase catalytic domain pairs are, on an average, 95.9% identical at the amino acid level. This bioinformatic study of bovine protein kinases provides a suitable framework for further characterization of their functional and structural properties.
Highlights
The protein kinase family is one of the largest families of proteins
Protein kinases play important roles in many intracellular or intercellular signaling pathways, resulting in cell proliferation, gene expression, metabolism, motility, membrane transport, apoptosis and differentiation. They modulate the activity of their substrate proteins by phosphorylating serine, threonine or tyrosine residues that mediate the activation, inhibition, translocation or degradation of substrate proteins (Brognard and Hunter, 2011)
Protein kinases are subdivided into two distinct superfamilies, referred to as eukaryotic protein kinases and atypical protein kinases (Hanks and Hunter, 1995). ePKs contain a conserved catalytic domain of approximately 250 amino acids
Summary
Chimpanzee, Orangutan, Monkey Orangutan, Monkey Chimpanzee, Orangutan Chimpanzee, Orangutan, Rat, Mouse, Horse, Chicken. Several proteins contained insertions or deletions (indels), as shown by sequence alignment (Table S1). These comparisons are informative within the conserved domains. Sixty two pairs were identical across the full domain, whereas 48 differed by only one amino acid (Table S1), indicative of strong conservative pressure throughout the catalytic domain. Of the six casein kinase 1 (CK1) family domain pairs, three were identical, and the other three differed by two residues, an average difference of only 0.4%, thereby indicating that changes in almost any amino acid within the domain destroyed some function, and have been eliminated by evolution (Figure 2A). The curated kinase dataset from the bovine genome, presented here, could serve as a framework for further investigation of this important gene family
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