| IED ID | IndEnz0002001974 |
| Enzyme Type ID | protease001974 |
| Protein Name |
Calcium-dependent protein kinase 5 EC 2.7.11.1 PfCDPK5 |
| Gene Name | CDPK5 PF3D7_1337800 |
| Organism | Plasmodium falciparum (isolate 3D7) |
| Taxonomic Lineage | cellular organisms Eukaryota Sar Alveolata Apicomplexa Aconoidasida Haemosporida (haemosporidians) Plasmodiidae Plasmodium Plasmodium (Laverania) Plasmodium falciparum Plasmodium falciparum (isolate 3D7) |
| Enzyme Sequence | MKETEVEDMDTNRKDGKIKKKEKIVNMKNEEVKSTTKSTLADSDEDYSIITLCTKCLSKKLEDNKNRIILDSKAFKDNRLKGRCSVSSNEDPLDNKLNLSPYFDRSQIIQEIILMNNDELSDVYEIDRYKLGKGSYGNVVKAVSKRTGQQRAIKIIEKKKIHNIERLKREILIMKQMDHPNIIKLYEVYEDNEKLYLVLELCDGGELFDKIVKYGSFSEYEAYKIMKQIFSALYYCHSKNIMHRDLKPENILYVDNTEDSPIQIIDWGFASKCMNNHNLKSVVGTPYYIAPEILRGKYDKRCDIWSSGVIMYILLCGYPPFNGKNNDEILKKVEKGEFVFDSNYWARVSDDAKDLICQCLNYNYKERIDVEQVLKHRWFKKFKSNNLIINKTLNKTLIEKFKEFHKLCKIKKLAVTCIAYQLNEKDIGKLKKTFEAFDHNGDGVLTISEIFQCLKVNDNEFDRELYFLLKQLDTDGNGLIDYTEFLAACLDHSIFQQDVICRNAFNVFDLDGDGVITKDELFKILSFSAVQVSFSKEIIENLIKEVDSNNDGFIDYDEFYKMMTGVKE |
| Enzyme Length | 568 |
| Uniprot Accession Number | A0A5K1K8H0 |
| Absorption | |
| Active Site | ACT_SITE 245; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10027 |
| Activity Regulation | ACTIVITY REGULATION: Activated by calcium (PubMed:20466936). 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 (By similarity). This, in turn, may facilitate the autophosphorylation of the activation loop at Thr-285, which leads to the kinase activation (By similarity). {ECO:0000250|UniProtKB:Q8IBS5, ECO:0000269|PubMed:20466936}. |
| Binding Site | BINDING 154; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| Calcium Binding | |
| catalytic Activity | 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:20466936, ECO:0000269|PubMed:31915223}; 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:20466936, ECO:0000269|PubMed:31915223}; |
| DNA Binding | |
| EC Number | 2.7.11.1 |
| Enzyme Function | 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:20466936, PubMed:31915223). Plays a central role in host erythrocytes and hepatocytes infection cycles (PubMed:20466936, PubMed:29487234). During the liver stage, involved in sporozoite motility and thus in sporozoite invasion of host hepatocytes, probably together with CDPK1 and CDPK4 (By similarity). Involved in merosome egress from host hepatocytes, probably together with CDPK4 (By similarity). Required for the release of hepatic merozoites from merosomes in the host blood stream (By similarity). During the asexual blood stage, required for merozoite egress from host erythrocytes by triggering microneme secretion (PubMed:20466936, PubMed:29487234). Phosphorylates transporter NPT1 at late schizont stage (PubMed:31915223). {ECO:0000250|UniProtKB:A0A509AQE6, ECO:0000269|PubMed:20466936, ECO:0000269|PubMed:29487234, ECO:0000269|PubMed:31915223}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 131..139; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| Features | Active site (1); Binding site (1); Chain (1); Domain (5); Metal binding (16); Motif (2); Nucleotide binding (1); Region (1) |
| Keywords | ATP-binding;Calcium;Cell membrane;Cytoplasm;Cytoplasmic vesicle;Kinase;Lipoprotein;Membrane;Metal-binding;Nucleotide-binding;Palmitate;Phosphoprotein;Reference proteome;Repeat;Serine/threonine-protein kinase;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29487234}. Cytoplasmic vesicle, secretory vesicle, microneme membrane {ECO:0000269|PubMed:29487234}; Peripheral membrane protein {ECO:0000269|PubMed:29487234}; Cytoplasmic side {ECO:0000269|PubMed:29487234}. Cell membrane {ECO:0000269|PubMed:20466936, ECO:0000269|PubMed:29487234, ECO:0000269|PubMed:31915223}; Peripheral membrane protein {ECO:0000303|PubMed:20466936}; Cytoplasmic side {ECO:0000305}. Note=During the late stages of schizogony, localizes to the cytoplasm in immature daughter merozoites, co-localizes with AMA1 to a subset of micronemes and to the apical region in maturing daughter merozoites, and near the plasma membrane in mature daughter and free merozoites. {ECO:0000269|PubMed:29487234}. |
| Modified Residue | |
| Post Translational Modification | PTM: May be palmitoylated. {ECO:0000303|PubMed:12368867}.; PTM: Autophosphorylated in vitro. {ECO:0000269|PubMed:20466936}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 400..408; /note=J domain autoinhibitory motif; /evidence=ECO:0000250|UniProtKB:Q8IBS5; MOTIF 409..418; /note=J domain EF-hand interaction motif; /evidence=ECO:0000250|UniProtKB:Q8IBS5 |
| Gene Encoded By | |
| Mass | 66,248 |
| Kinetics | |
| Metal Binding | METAL 438; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 440; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 442; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 449; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 473; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 475; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 477; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 484; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 509; /note=Calcium 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 511; /note=Calcium 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 513; /note=Calcium 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 520; /note=Calcium 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 547; /note=Calcium 4; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 549; /note=Calcium 4; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 551; /note=Calcium 4; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 558; /note=Calcium 4; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448 |
| Rhea ID | RHEA:17989; RHEA:46608 |
| Cross Reference Brenda |