Protein kinases with calmodulin-like domains: novel targets of calcium signals in plants.
Recently, a novel calcium-dependent protein kinase has been identified that is structurally distinguished by the localization of a calcium-binding regulatory domain fused to a serine/threonine catalytic domain. The regulatory domain is homologous to calmodulin and contains four helix-loop-helix calcium-binding sites. As a result, the kinase is directly activated by calcium without a requirement for other effector molecules.
Department of Biochemistry, University of Tennessee, Knoxville 37996-0840.
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D000595:Amino Acid Sequence; D001665:Binding Sites; D002118:Calcium / Q000494:pharmacology; D002147:Calmodulin / Q000737:chemistry*; D004789:Enzyme Activation / Q000187:drug effects; D008969:Molecular Sequence Data; D010944:Plants / Q000201:enzymology*; D011494:Protein Kinases / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid
D002147:Calmodulin; D011494:Protein Kinases; D002118:Calcium