The CAMK Group
The CAMK group are primarily characterised by Calcium/Calmodulin modulation of their activity. Most of the members of this group exhibit activation by the binding of Calcium or Calmodulin to a small domain C-terminal to the catalytic domain.
As with the closely related AGC
group, the CAMK group, in general, appear to prefer substrates containing basic residues. The CaMK, MLCK, CDPK and AMPK enzymes all prefer a substrate with basic residues N-terminal to the acceptor site wheras EF2K and PhK prefer sites where basic residues are located both N- and C- terminal to the acceptor site.
The plant enzymes typified by CDPK contain an intrinsic calmodulin-like domain allowing these enzymes to self-activate in the presence of Calcium ions.
Klimecka M, Muszyska G.
Structure and functions of plant calcium-dependent protein kinases.
Acta Biochim Pol.
Nakayama S, Moncrief ND, Kretsinger RH.
Evolution of EF-hand calcium-modulated proteins. II. Domains of several subfamilies have diverse evolutionary histories.
J Mol Evol.
Nagamune K, Sibley LD.
Comparative genomic and phylogenetic analyses of calcium ATPases and calcium-regulated proteins in the apicomplexa.
Mol Biol Evol.
Zhu G, Fujii K, Liu Y, Codrea V, Herrero J, Shaw S.
A single pair of acidic residues in the kinase major groove mediates strong substrate preference for P-2 or P-5 arginine in the AGC, CAMK, and STE kinase families.
J Biol Chem.