Fig. 1From: Functional characterization and regulatory mechanism of wheat CPK34 kinase in response to drought stressSequences and domain structure of TaCPK 34 protein. a, Nucleotide and amino acid sequences of TaCPK34. b, Domain structure of TaCPK 34 protein. Plant CPK members consist of variable N terminal domain (VNTD) containing N-myristoylation/N-palmitoylation region fused to a catalytic kinase domain, an inhibitory junction domain and a calmodulin like domain (CaM-LD). Inhibitory junction and CaM-LD forms CPK activation domain (CAD). CaMLD contains four calcium binding EF hands motifs that are organized in N terminal and C terminal lobes.section may be divided by subheadings. It provides a concise description of the experimental results, their interpretation as well as the experimental conclusions are drawnBack to article page