Calcium-activated and phospholipid-dependent serine/threonine-protein kinase involved in various processes such as regulation of the B-cell receptor (BCR) signalosome, apoptosis and transcription regulation. Plays a key role in B-cell activation and function by regulating BCR-induced NF-kappa-B activation and B-cell survival. Required for recruitment and activation of the IKK kinase to lipid rafts and mediates phosphorylation of card11/carma1, leading to activate the NF-kappa-B signaling. Involved in apoptosis following oxidative damage: in case of oxidative conditions, specifically phosphorylates isoform p66Shc of shc1, leading to mitochondrial accumulation of p66Shc, where p66Shc acts as a reactive oxygen species producer. Acts as a coactivator of androgen receptor (andr)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional activation (By similarity). ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domain. Activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. Phosphorylation on Thr-497 within the activation loop renders it competent to autophosphorylate. Subsequent autophosphorylation of Thr-638 maintains catalytic competence, and autophosphorylation on Ser-657 appears to release the kinase into the cytosol (By similarity). Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.