<p>This entry represents elongation factor 2 kinase (eEF-2 kinase), a highly specific kinase that phosphorylates and inactivates eukaryotic elongation factor-2 (eEF-2), and thus can modulate the rate of polypeptide chain elongation during translation. eEF-2 kinase is part of the family of alpha-kinases, whose catalytic domains display no sequence homology to conventional eukaryotic protein kinases [<cite idref="PUB00044644"/>]. This family also includes Dictyostelium myosin heavy chain kinases A, B, and C, and several mammalian putative protein kinases. </p><p>The domain organisation of eEF-2 kinase appears to consist of two domains connected by a linker region, where the N-terminal domain contains the catalytic site, and the C-terminal domain contains the eEF-2 target region. The calmodulin-binding region is located between residues 51 and 96 [<cite idref="PUB00044645"/>].</p>