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Entry version 128 (29 Sep 2021)
Sequence version 2 (23 Jan 2007)
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Protein

Calcium-dependent protein kinase 1

Gene

CDPK1

Organism
Plasmodium falciparum (isolate 3D7)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca2+ levels probably in part downstream of cGMP-activated PKG kinase (PubMed:18768477, PubMed:19307175, PubMed:28680058, PubMed:29716996).

By phosphorylating various proteins, required for microneme secretion and thus merozoite egress from and invasion of host erythrocytes (PubMed:23204525, PubMed:28680058, PubMed:29716996).

During gametogenesis, essential for the development of both male and female gametes (By similarity).

Phosphorylates SERA5 p50 which enhances SERA5 p50 protease activity; however, SERA5 p50 protease activity has been shown in other studies to be controversial (PubMed:29716996).

Probably by phosphorylating SERA5 p50, plays a role in merozoite egress from host erythrocytes (PubMed:29716996).

Probably prior or during merozoite invasion of host erythrocytes, phosphorylates rhoptry protein RhopH3 which is required for RhopH3 localization to rhoptries and for its secretion (PubMed:33024030).

Probably in late schizonts, phosphorylates myosin A tail domain-interacting protein MTIP and glideosome-associated protein 45 GAP45, both of which are components of the motor complex that generates the force required by the parasite to invade host cells (PubMed:18768477, PubMed:28680058, PubMed:22539638).

In late schizonts, phosphorylates inner membrane complex protein IMC1g (PubMed:28680058).

In late schizonts, phosphorylates PKA regulatory subunit PKAr in a calcium-dependent manner, which may contribute to the dissociation of regulatory PKAr and catalytic PKAc subunits and promote the activation of PKAc (PubMed:28680058).

May phosphorylate raf kinase inhibitory protein RKIP which in turn may regulate CDPK1 catalytic activity (PubMed:17123645).

May phosphorylate proteins of the host erythrocyte membranes (By similarity).

By similarity8 Publications

Caution

Unlike P.berghei CDPK1, appears to be involved in the asexual blood stage and in male gamete exflagellation prior host erythrocyte membrane rupture.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activated by calcium (PubMed:29716996, PubMed:18768477, PubMed:23204525, PubMed:17123645, PubMed:32484216). 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 (Probable) (PubMed:23204525). This, in turn may facilitate the autophosphorylation of the activation loop at Thr-231, which leads to the kinase activation (PubMed:19307175). May be negatively regulated by PKA-mediated phosphorylation (PubMed:28680058). Inhibited by purfalcamine (PubMed:23204525, PubMed:29716996).1 Publication7 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=9 µM for MTIP (at 30 degrees Celsius)1 Publication
  2. KM=18 µM for GAP45 (at 30 degrees Celsius)1 Publication
  3. KM=125 µM for ATP (with MTIP as substrate and at 30 degrees Celsius)1 Publication
  4. KM=96 µM for ATP (with GAP45 as substrate and at 30 degrees Celsius)1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei85ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei191Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi62 – 70ATPPROSITE-ProRule annotation9
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) of the calcium-binding region(s) within the protein. One common calcium-binding motif is the EF-hand, but other calcium-binding motifs also exist.<p><a href='/help/ca_bind' target='_top'>More...</a></p>Calcium bindingi385 – 3961PROSITE-ProRule annotationAdd BLAST12
Calcium bindingi429 – 4402PROSITE-ProRule annotationAdd BLAST12
Calcium bindingi465 – 4763PROSITE-ProRule annotationAdd BLAST12
Calcium bindingi499 – 5104PROSITE-ProRule annotationAdd BLAST12

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
LigandATP-binding, Calcium, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.11.1, 4889

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Calcium-dependent protein kinase 1 (EC:2.7.11.17 Publications)
Alternative name(s):
PfCDPK11 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CDPK11 Publication
Synonyms:CPK1
ORF Names:PF3D7_0217500, PFB0815w
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiPlasmodium falciparum (isolate 3D7)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri36329 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaSarAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Laverania)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001450 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

Organism-specific databases

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
PlasmoDB:PF3D7_0217500

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cell membrane, Cell projection, Cilium, Cytoplasm, Flagellum, Host cell membrane, Host membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Conditional knockdown at the ring stage produces the development of mature schizonts and the subsequent release of merozoites from the host erythrocytes; however, the invasion of new erythrocytes by these merozoites is severely reduced due to a severe defect in adhesion to the erythrocyte membrane (PubMed:28680058). In merozoites, release of host glycophorin A/GYPA ligand EBA-175 from micronemes is impaired but not AMA1 (PubMed:28680058). In late schizont, phosphorylation of several proteins including GAP45, IMC1g and PKAr is reduced (PubMed:28680058). Reduced PKA activity (PubMed:28680058). Rhoptry protein RhopH3 phosphorylation and secretion are reduced in merozoites (PubMed:33024030).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi2 – 50Missing : Severe loss of catalytic activity. 1 PublicationAdd BLAST49
Mutagenesisi2 – 40Missing : Severe loss of catalytic activity. 1 PublicationAdd BLAST39
Mutagenesisi2 – 30Missing : Severe loss of catalytic activity. 1 PublicationAdd BLAST29
Mutagenesisi2 – 20Missing : No effect on catalytic activity. 1 PublicationAdd BLAST19
Mutagenesisi2G → V: Loss of myristoylation. Severe reduction in membrane binding. Loss of membrane binding; when associated with 10-K--T-20 DEL. 1 Publication1
Mutagenesisi10 – 20Missing : Does not affect myristoylation. Severe reduction in membrane binding. Loss of membrane binding; when associated with V-2. 1 PublicationAdd BLAST11
Mutagenesisi27K → A: Severe loss of ATP binding. Partial loss of catalytic activity. 1 Publication1
Mutagenesisi64S → A: Loss of phosphorylation. No effect on catalytic activity. 1 Publication1
Mutagenesisi152E → A: Severe loss of catalytic activity. 1 Publication1
Mutagenesisi154F → A: Severe loss of catalytic activity. 1 Publication1
Mutagenesisi155E → A: No effect on catalytic activity. 1 Publication1
Mutagenesisi157 – 158II → AA: Severe loss of catalytic activity. 1 Publication2
Mutagenesisi191D → N: Loss of catalytic activity. 2 Publications1
Mutagenesisi231T → A: Loss of catalytic activity. 1 Publication1
Mutagenesisi335S → A: Loss of phosphorylation. Loss of catalytic activity. 1 Publication1
Mutagenesisi335S → D: Phospho-mimetic mutant.No effect on catalytic activity. 1 Publication1
Mutagenesisi339T → D: No effect on catalytic activity. 1 Publication1
Mutagenesisi342 – 524Missing : Constitutively active. 1 PublicationAdd BLAST183
Mutagenesisi347M → A: Severe loss of catalytic activity. 1 Publication1
Mutagenesisi350F → A: Severe loss of catalytic activity. 2 Publications1
Mutagenesisi353S → A: No effect on catalytic activity. 1 Publication1
Mutagenesisi355K → A: No effect on catalytic activity. 1 Publication1
Mutagenesisi356L → A: Severe loss of catalytic activity. 1 Publication1
Mutagenesisi363 – 364FI → AA: Severe loss of catalytic activity. 1 Publication2
Mutagenesisi366S → A: Slight decrease in catalytic activity. 1 Publication1
Mutagenesisi369 – 370TT → AA: Slight decrease in catalytic activity. 1 Publication2
Mutagenesisi456R → A: Severe loss of catalytic activity. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1908387

Drug and drug target database

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DrugBanki
DB12010, Fostamatinib

DrugCentral

More...
DrugCentrali
P62344

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000858342 – 524Calcium-dependent protein kinase 1Add BLAST523

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi2N-myristoyl glycine1 Publication1
Lipidationi3S-palmitoyl cysteine2 Publications1
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei17Phosphoserine; by autocatalysis2 Publications1
Modified residuei28Phosphoserine; by autocatalysis2 Publications1
Modified residuei34Phosphoserine; by autocatalysis1 Publication1
Modified residuei64Phosphoserine; by PKG; by autocatalysis3 Publications1
Modified residuei100Phosphothreonine; by autocatalysis1 Publication1
Modified residuei118Phosphoserine; by autocatalysis1 Publication1
Modified residuei217Phosphoserine2 Publications1
Modified residuei220Phosphoserine; by autocatalysis1 Publication1
Modified residuei231Phosphothreonine; by PKG; by autocatalysis2 Publications1
Modified residuei335Phosphoserine; by autocatalysis1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Myristoylated (PubMed:15491359). Myristoylation, palmitoylation and the basic cluster motif are required for the localization to the parasitophorous vacuole membrane (PubMed:15491359).1 Publication
Palmitoylated (Probable) (PubMed:32003970). Palmitoylation increases in merozoites in response to low level of extracellular K+ in the host blood (PubMed:32003970). Myristoylation, palmitoylation and the basic cluster motif are required for the localization to the parasitophorous vacuole membrane (PubMed:15491359).1 Publication2 Publications
Phosphorylation at Ser-64 occurs at late schizont stage and regulates CDPK1 protein-protein interaction (PubMed:26149123). Phosphorylated at Ser-28, Ser-34 and Ser-64 in merozoites in response to low extracellular level of K+ (PubMed:32817103). Phosphorylation at Thr-231 may regulate CDPK1 kinase activity (PubMed:26149123). Phosphorylation increases in response to an increase in intracellular Ca2+ levels (PubMed:32484216). Autophosphorylated in vitro (PubMed:17123645, PubMed:22539638, PubMed:23204525, PubMed:26149123, PubMed:32484216). Autophosphorylation does not affect membrane localization in vitro (PubMed:15491359).7 Publications

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P62344

PTM databases

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P62344

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed during parasite asexual blood stages, specifically at the ring and schizont stages, in free merozoites and to a lesser extent in trophozoites (at protein level).9 Publications

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer (PubMed:26149123).

Forms a high molecular weight (250 and 400 kDa) complex (PubMed:26149123).

Forms a complex composed of CDPK1, PKA regulatory subunit PKAr and 14-3-3I; the complex is formed in merozoites in response to low extracellular level of K+ and may play a role in microneme secretion (PubMed:32817103).

Interacts (when phosphorylated) with 14-3-3I in a Ca2+-independent manner; the interaction does not regulate CDPK1 catalytic activity but is required for merozoite invasion of host erythrocytes (PubMed:32484216, PubMed:32817103).

Interacts with PKA regulatory subunit PKAr; in a Ca2+-dependent manner (PubMed:28680058, PubMed:32817103).

Interacts with SERA5 p50 in the late schizont stage (PubMed:29716996).

Interacts with inner membrane complex protein IMC1g in late schizonts (PubMed:28680058).

Interacts with rhoptry protein RhopH3 in merozoites (PubMed:33024030).

6 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
1208081, 9 interactors

Protein interaction database and analysis system

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IntActi
P62344, 8 interactors

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P62344

Database of comparative protein structure models

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ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini56 – 325Protein kinasePROSITE-ProRule annotationAdd BLAST270
Domaini372 – 407EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini416 – 451EF-hand 2PROSITE-ProRule annotationAdd BLAST36
Domaini452 – 487EF-hand 3PROSITE-ProRule annotationAdd BLAST36
Domaini486 – 521EF-hand 4PROSITE-ProRule annotationAdd BLAST36

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 34DisorderedSequence analysisAdd BLAST34
Regioni346 – 364J domain1 PublicationAdd BLAST19

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi10 – 20Basic cluster involved in membrane binding1 PublicationAdd BLAST11
Motifi346 – 353J domain autoinhibitory motif1 Publication8
Motifi354 – 364J domain interacts with the EF-hand domains1 Publication1 PublicationAdd BLAST11

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi18 – 34Polar residuesSequence analysisAdd BLAST17

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The junction domain (J domain) is composed of 2 motifs that maintain the kinase inactive (PubMed:19307175). The N-terminal autoinhibitory motif acts as a pseudosubstrate inhibiting the catalytic domain while the C-terminal motif binds the EF-hand domains (PubMed:19307175, PubMed:23204525).2 Publications

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDPK subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_000288_37_4_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P62344

Identification of Orthologs from Complete Genome Data

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OMAi
KFDECDA

Database for complete collections of gene phylogenies

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PhylomeDBi
P62344

Family and domain databases

Conserved Domains Database

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CDDi
cd00051, EFh, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011992, EF-hand-dom_pair
IPR018247, EF_Hand_1_Ca_BS
IPR002048, EF_hand_dom
IPR011009, Kinase-like_dom_sf
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
IPR008271, Ser/Thr_kinase_AS

Pfam protein domain database

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Pfami
View protein in Pfam
PF13499, EF-hand_7, 2 hits
PF00069, Pkinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00054, EFh, 4 hits
SM00220, S_TKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47473, SSF47473, 1 hit
SSF56112, SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00018, EF_HAND_1, 4 hits
PS50222, EF_HAND_2, 4 hits
PS00107, PROTEIN_KINASE_ATP, 1 hit
PS50011, PROTEIN_KINASE_DOM, 1 hit
PS00108, PROTEIN_KINASE_ST, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P62344-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGCSQSSNVK DFKTRRSKFT NGNNYGKSGN NKNSEDLAIN PGMYVRKKEG
60 70 80 90 100
KIGESYFKVR KLGSGAYGEV LLCREKHGHG EKAIKVIKKS QFDKMKYSIT
110 120 130 140 150
NKIECDDKIH EEIYNEISLL KSLDHPNIIK LFDVFEDKKY FYLVTEFYEG
160 170 180 190 200
GELFEQIINR HKFDECDAAN IMKQILSGIC YLHKHNIVHR DIKPENILLE
210 220 230 240 250
NKHSLLNIKI VDFGLSSFFS KDNKLRDRLG TAYYIAPEVL RKKYNEKCDV
260 270 280 290 300
WSCGVILYIL LCGYPPFGGQ NDQDIIKKVE KGKYYFDFND WKNISEEAKE
310 320 330 340 350
LIKLMLTYDY NKRITAKEAL NSKWIKKYAN NINKSDQKTL CGALSNMRKF
360 370 380 390 400
EGSQKLAQAA ILFIGSKLTT LEERKELTDI FKKLDKNGDG QLDKKELIEG
410 420 430 440 450
YNILRSFKNE LGELKNVEEE VDNILKEVDF DKNGYIEYSE FISVCMDKQI
460 470 480 490 500
LFSEERLRDA FNLFDTDKSG KITKEELANL FGLTSISEQM WNEVLGEADK
510 520
NKDNMIDFDE FVNMMHKICD NKSS
Length:524
Mass (Da):60,800
Last modified:January 23, 2007 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD2A45E1579D2C951
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
LN999943 Genomic DNA Translation: CZT98189.1

Protein sequence database of the Protein Information Resource

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PIRi
A45472

NCBI Reference Sequences

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RefSeqi
XP_001349680.1, XM_001349644.1

Genome annotation databases

Ensembl protists genome annotation project

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EnsemblProtistsi
CZT98189; CZT98189; PF3D7_0217500

GeneDB pathogen genome database from Sanger Institute

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GeneDBi
PF3D7_0217500.1:pep

Database of genes from NCBI RefSeq genomes

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GeneIDi
812762

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
pfa:PF3D7_0217500

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
LN999943 Genomic DNA Translation: CZT98189.1
PIRiA45472
RefSeqiXP_001349680.1, XM_001349644.1

3D structure databases

SMRiP62344
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi1208081, 9 interactors
IntActiP62344, 8 interactors

Chemistry databases

ChEMBLiCHEMBL1908387
DrugBankiDB12010, Fostamatinib
DrugCentraliP62344

PTM databases

SwissPalmiP62344

Proteomic databases

PRIDEiP62344

Genome annotation databases

EnsemblProtistsiCZT98189; CZT98189; PF3D7_0217500
GeneDBiPF3D7_0217500.1:pep
GeneIDi812762
KEGGipfa:PF3D7_0217500

Organism-specific databases

VEuPathDBiPlasmoDB:PF3D7_0217500

Phylogenomic databases

HOGENOMiCLU_000288_37_4_1
InParanoidiP62344
OMAiKFDECDA
PhylomeDBiP62344

Enzyme and pathway databases

BRENDAi2.7.11.1, 4889

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P62344

Family and domain databases

CDDicd00051, EFh, 1 hit
InterProiView protein in InterPro
IPR011992, EF-hand-dom_pair
IPR018247, EF_Hand_1_Ca_BS
IPR002048, EF_hand_dom
IPR011009, Kinase-like_dom_sf
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
IPR008271, Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF13499, EF-hand_7, 2 hits
PF00069, Pkinase, 1 hit
SMARTiView protein in SMART
SM00054, EFh, 4 hits
SM00220, S_TKc, 1 hit
SUPFAMiSSF47473, SSF47473, 1 hit
SSF56112, SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00018, EF_HAND_1, 4 hits
PS50222, EF_HAND_2, 4 hits
PS00107, PROTEIN_KINASE_ATP, 1 hit
PS50011, PROTEIN_KINASE_DOM, 1 hit
PS00108, PROTEIN_KINASE_ST, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCDPK1_PLAF7
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P62344
Secondary accession number(s): A0A143ZWW4, Q27731
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: January 23, 2007
Last modified: September 29, 2021
This is version 128 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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