Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels probably in part downstream of cGMP-activated PKG kinase (By similarity). During the liver stage, involved in sporozoite motility and thus in sporozoite invasion of host hepatocytes, probably together with CDPK4 and CDPK5 (PubMed:32866196). In the mosquito midgut and during the last stage of male gamete exflagellation, may play a role in the rupture of the host erythrocyte membrane (PubMed:22817984). In the mosquito midgut, required for the differentiation of the zygote into the ookinete by promoting the translational activation of a subset of repressed mRNAs; these mRNAs are kept repressed in the zygote by the DOZI- or CITH-containing mRNP complexes (PubMed:22817984, PubMed:24265753). Dispensable during the asexual blood stage (PubMed:24265753). ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Activated by calcium. Upon calcium binding to the EF-hand domains, the C-terminus of the junction domain (J domain) undergoes a conformational change which results in the dissociation of the pseudo-substrate inhibitory motif from the catalytic domain. This, in turn may facilitate the autophosphorylation of the activation loop at Thr-230, which leads to the kinase activation. Monomer. Calcium and/or autophosphorylation does not affect membrane localization. During the asexual blood stage, expressed in schizonts (PubMed:22817984). Expressed in gametocytes (PubMed:22817984). Expressed in ookinetes and oocyst early stages (PubMed:22817984). Expressed in sporozoites (PubMed:22817984, PubMed:32866196). Not expressed during the liver stage (PubMed:32866196). The junction domain (J domain) is composed of 2 motifs that maintain the kinase inactive. The N-terminal autoinhibitory motif acts as a pseudosubstrate inhibiting the catalytic domain while the C-terminal motif binds the EF-hand domains. Myristoylated. Myristoylation and palmitoylation are required for the localization to the parasitophorous vacuole membrane. Palmitoylated. Palmitoylation increases in merozoites in response to low level of extracellular K(+) in the host blood. Myristoylation and palmitoylation are required for the localization to the parasitophorous vacuole membrane. Phosphorylation at Thr-230 may regulate CDPK1 kinase activity. Phosphorylation increases in response to an increase in intracellular Ca(2+) levels. Autophosphorylated in vitro. Autophosphorylation does not affect membrane localization in vitro. In the mosquito midgut, male gametocyte exflagellation is normal; however, the rupture of the host erythrocyte cell membrane is delayed (PubMed:22817984). Fertilization is normal, however zygote development into ookinetes is arrested at the retort stage where ookinetes are still immotile (PubMed:22817984, PubMed:24265753). In arrested ookinetes, protein levels, but not mRNA levels, of a subset of proteins including MyoA and MTIP, two components of the motor complex, CTRP and SOAP are strongly reduced (PubMed:22817984). In arrested ookinetes, apical complex including collar, apical rings and micronemes and the pellicle, consisting of the plasma membrane, the inner membrane complex and the subpellicular microtubules are normally assembled (PubMed:22817984). During host liver invasion, sporozoite attachment to the substrate is normal but sporozoite uninterrupted circular movement is impaired (PubMed:32866196). No effect on cell traversal but reduces invasion of host hepatocytes (PubMed:32866196). No defect in the asexual erythrocyte stage; infection, development and egress from host erythrocytes are normal (PubMed:24265753). Conditional knockout in sporozoites, does not affect sporozoite invasion of the mosquito salivary gland or invasion of host hepatocytes (PubMed:22817984). Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDPK subfamily. Unlike P.falciparum CDPK1, appears not to be involved in the asexual blood stage and in male gamete exflagellation prior host erythrocyte membrane rupture.