Converts transient diacylglycerol (DAG) signals into prolonged physiological effects, independently of PKC. Role in the regulation of growth and neuromuscular control of movement. Involved in immune response to S.aureus bacterium by activating transcription factor hlh-30 downstream of phospholipase plc-1. ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Activated by DAG and phorbol esters. Phorbol-ester/DAG-type domain 1 binds phorbol ester with high affinity and mediates accumulation at the cell periphery. Phorbol-ester/DAG-type domain 2 binds phorbol ester with low affinity but may mediate initial contact, resulting in a conformational change allowing previously occluded domain 1 to anchor the kinase. Phosphorylation on Thr-626 is then also required for activation and may also result in a further conformational change (By similarity). Translocation to the cell membrane is required for kinase activation. On activation, the protein may migrate back to the cytoplasm (By similarity). The PH domain inhibits PKD catalytic activity in the absence of DAG, either by direct steric occlusion or distortion of the PKD catalytic cleft. Prolonged phosphorylation at Thr-626 results in ubiquitination and degradation. Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. PKD subfamily.