UniProt functional annotation for O15865

UniProt code: O15865.

Organism: Plasmodium falciparum (isolate K1 / Thailand).
Taxonomy: Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; Plasmodiidae; Plasmodium; Plasmodium (Laverania).
 
Function: 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 (PubMed:9247932). During male gametogenesis in the mosquito gut, required for male exflagellation, possibly by regulating male gamete exit from the host erythrocytes. Not required for asexual blood stage proliferation (By similarity). {ECO:0000250|UniProtKB:Q8ICR0, ECO:0000269|PubMed:9247932}.
 
Catalytic activity: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:9247932};
Catalytic activity: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:9247932};
Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8ICR0};
Activity regulation: Activated by calcium (PubMed:9247932). 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-232, which leads to the kinase activation (By similarity). {ECO:0000250|UniProtKB:Q8IBS5, ECO:0000269|PubMed:9247932}.
Subunit: Monomer. {ECO:0000250|UniProtKB:Q8ICR0}.
Developmental stage: Expressed in ring, trophozoite, schizont and segmenter stages. {ECO:0000269|PubMed:9247932}.
Domain: 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. {ECO:0000250|UniProtKB:Q8IBS5}.
Ptm: Myristoylated; myristoylation may target it to different subcellular compartments. {ECO:0000250|UniProtKB:P62344}.
Ptm: Autophosphorylated in vitro. {ECO:0000269|PubMed:9247932}.
Similarity: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDPK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.

Annotations taken from UniProtKB at the EBI.