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UniProtKB - Q8I719 (KGP_PLAF7)

Entry version 149 (25 May 2022)
Sequence version 1 (01 Mar 2003)
Previous versions | rss
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Protein

cGMP-dependent protein kinase

Gene

PKG

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

Serine/threonine protein kinase which acts as a downstream effector of the second messenger cGMP (PubMed:12068803, PubMed:12817987, PubMed:26149123).

Controls the release of Ca2+ from intracellular stores by regulating phosphoinositide biosynthesis (PubMed:24594931).

Ca2+ signals are essential for merozoite and sporozoite invasion and egress from host hepatocytes and erythrocytes, and, in the mosquito vector, for gametocyte activation, and ookinete and sporozoite motility (PubMed:24594931).

During the host liver stage, regulates the initial invasion of host hepatocytes by sporozoites by regulating sporozoite motility and microneme exocytosis (By similarity).

Following parasite development in the hepatocytes, required for the release of merosomes, a vesicle containing the mature merozoites (By similarity).

During the asexual blood stage, required for the progression from schizont to the ring stage following merozoite invasion of host erythrocytes and for merozoite egress (PubMed:19915077, PubMed:26149123, PubMed:25646845).

Regulates merozoite egress by promoting the release of exonemes and micronemes which contain proteins essential for egress (PubMed:23675297).

Phosphorylates CDPK1 predominantly at the late schizont stage; phosphorylation at 'Ser-64' regulates CDPK1 protein-protein interaction and phosphorylation at 'Thr-231' may regulate CDPK1 kinase activity (PubMed:26149123).

Phosphorylates MyoA at 'Ser-19' (PubMed:26149123).

In the mosquito vector, required for the initiation of gametogenesis induced by xanthurenic acid, specifically the gametocyte differentiation from the crescent-shaped form to the spherical form (PubMed:18532880).

Required for the gliding motility of ookinetes to reach and penetrate the midgut epithelium by promoting Ca2+-mediated activation of CDPK1 and CDPK4 (By similarity).

Also required for microneme secretion in ookinete by promoting Ca2+-mediated activation of CDPK3 (By similarity).

By similarity8 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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%5Fsection">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 cGMP (PubMed:12068803, PubMed:12817987, PubMed:26149123, PubMed:29251493, PubMed:25646845, PubMed:31239348). Not activated by cAMP (PubMed:12068803, PubMed:12817987). cGMP binding allosterically triggers a conformational change at the alpha C-helix of cGMP-binding domain 4, which bridges the regulatory and catalytic domains, causing the capping triad, composed of Arg-484, Gln-532 and Asp-533, to form and stabilize the active conformation (PubMed:29251493, PubMed:25646845). The cGMP-binding domains acts cooperatively to activate PKG (PubMed:29251493, PubMed:12817987).6 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>pH dependencei

Optimum pH is 7.0.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei1133',5'-cGMP 1; allosteric activatorCombined sources1 Publication1
Binding sitei1223',5'-cGMP 1; via amide nitrogen; allosteric activatorCombined sources1 Publication1
Binding sitei1233',5'-cGMP 1; allosteric activatorCombined sources1 Publication1
Binding sitei1253',5'-cGMP 1; via amide nitrogen; allosteric activatorCombined sources1 Publication1
Binding sitei1323',5'-cGMP 1; allosteric activatorCombined sources1 Publication1
Binding sitei1333',5'-cGMP 1; allosteric activatorCombined sources1 Publication1
Binding sitei4733',5'-cGMP 2; allosteric activatorCombined sources1 Publication1
Binding sitei4823',5'-cGMP 2; via amide nitrogen; allosteric activatorCombined sources1 Publication1
Binding sitei4833',5'-cGMP 2; allosteric activatorCombined sources1 Publication1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei484Part of a catalytic triad required for cGMP binding and cGMP-dependent kinase activity1 Publication1
Binding sitei4853',5'-cGMP 2; via amide nitrogen; allosteric activatorCombined sources1 Publication1
Binding sitei4923',5'-cGMP 2; allosteric activatorCombined sources1 Publication1
Binding sitei4933',5'-cGMP 2; allosteric activatorCombined sources1 Publication1
Sitei532Part of a catalytic triad required for cGMP binding and cGMP-dependent kinase activity1 Publication1
Sitei533Part of a catalytic triad required for cGMP binding and cGMP-dependent kinase activity1 Publication1
Binding sitei570ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei664Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi547 – 555ATPPROSITE-ProRule annotation9

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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, cGMP, cGMP-binding, Magnesium, Metal-binding, Nucleotide-binding

<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%5Fand%5Ftaxonomy%5Fsection">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:
cGMP-dependent protein kinase1 Publication (EC:2.7.11.127 Publications)
Alternative name(s):
PfPKG1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:PKG1 Publication
ORF Names:PF3D7_1436600Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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)Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Sar › Alveolata › Apicomplexa › Aconoidasida › Haemosporida › Plasmodiidae › Plasmodium › Plasmodium (Laverania) ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 14

Organism-specific databases

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		PlasmoDB:PF3D7_1436600

<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

Cytoplasm, Endoplasmic reticulum, 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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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 – 518Missing : Loss of catalytic activity and irresponsive to cGMP, with peptides as substrates. 1 PublicationAdd BLAST517
Mutagenesisi2 – 434Missing : Loss of catalytic activity. 1 PublicationAdd BLAST433
Mutagenesisi2 – 400Missing : Low basal catalytic activity. Normal increase in catalytic activity in presence of cGMP. 1 PublicationAdd BLAST399
Mutagenesisi2 – 274Missing : Low basal catalytic activity. Normal increase in catalytic activity in presence of cGMP. 1 PublicationAdd BLAST273
Mutagenesisi2 – 157Missing : Low basal catalytic activity. Normal increase in catalytic activity in presence of cGMP. 1 PublicationAdd BLAST156
Mutagenesisi2 – 114Missing : Has low catalytic activity in absence of cGMP. Normal increase in catalytic activity in presence of cGMP. 1 PublicationAdd BLAST113
Mutagenesisi2 – 31Missing : Has low catalytic activity in absence of cGMP. cGMP binding is still required for full activation. 1 PublicationAdd BLAST30
Mutagenesisi2 – 29Missing : Has low catalytic activity in absence of cGMP. 1 PublicationAdd BLAST28
Mutagenesisi133S → A: No effect on cGMP-mediated catalytic activity. Slight reduction in cGMP-mediated catalytic activity; when associated with A-251. Severe loss of cGMP-mediated catalytic activity; when associated with A-493 or A-251 and A-493. 1 Publication1
Mutagenesisi251S → A: 12% reduction in cGMP-mediated catalytic activity. Slight reduction in cGMP-mediated catalytic activity; when associated with A-133. Severe loss of cGMP-mediated catalytic activity; when associated with A-493 or A-133 and A-493. 1 Publication1
Mutagenesisi360G → E: 55% loss in cGMP-mediated catalytic activity. 1 Publication1
Mutagenesisi484R → A: Reduces affinity for cGMP and severe loss of kinase activity. 1 Publication1
Mutagenesisi493T → A: 42% reduction in cGMP-mediated catalytic activity. Severe loss of cGMP-mediated catalytic activity; when associated with A-133, A-251 or A-133 and A-251. 1 Publication1
Mutagenesisi532Q → A: Reduces affinity for cGMP and severe loss of kinase activity. 1 Publication1
Mutagenesisi533D → A: Reduces affinity for cGMP and severe loss of kinase activity. 1 Publication1
Mutagenesisi618T → Q: 4.5-fold reduction in affinity for ATP. No defect in schizogony during host erythrocyte invasion. However, Ca(2+) increase in response to cGMP is reduced in schizonts. Does not affect merozoite egress from host erythrocytes. Resistant to trisubstituted pyrrole compound 1 (C1) and imidazopyridine-based compound 2 (C2) inhibitors. 4 Publications1

Chemistry databases

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		3013

<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 '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_00004519081 – 853cGMP-dependent protein kinaseAdd BLAST853

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Autophosphorylated.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		Q8I719

<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 the parasite blood stage, expression is low at the ring stage and in early trophozoites, then increases during the parasite maturation to peak at the late schizont stage (at protein level) (PubMed:31239348, PubMed:19915077, PubMed:23139764, PubMed:12068803). Expression is low in gametocytes (at protein level) (PubMed:23139764).4 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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

2 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		5833.PF14_0346

<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

Secondary structure

1853
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		Q8I719

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

More...SMRi		Q8I719

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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%5Fand%5Fdomains%5Fsection">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>Domaini541 – 798Protein kinasePROSITE-ProRule annotationAdd BLAST258
Domaini799 – 853AGC-kinase C-terminalPROSITE-ProRule annotationAdd BLAST55

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 – 29Autoinhibitory segment1 PublicationAdd BLAST29
Regioni58 – 173cNMP-binding domain 1PROSITE-ProRule annotationAdd BLAST116
Regioni176 – 275cNMP-binding domain 2PROSITE-ProRule annotationAdd BLAST100
Regioni295 – 398cNMP-binding domain 3PROSITE-ProRule annotationAdd BLAST104
Regioni418 – 517cNMP-binding domain 4PROSITE-ProRule annotationAdd BLAST100
Regioni827 – 853DisorderedSequence analysisAdd BLAST27

<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 cNMP-binding domains 1, 2 and 4 bind preferentially cGMP (PubMed:25646845). The cNMP-binding domain 4 binds cGMP with the highest affinity and is highly selective for cGMP (PubMed:29251493, PubMed:25646845, PubMed:31239348). The cNMP-binding domain 3 does not bind cGMP but is required for cGMP-dependent catalytic activity (PubMed:12817987). The cNMP-binding domains 1, 2 and 4 can bind cAMP but with less affinity (PubMed:25646845).4 Publications
The autoinhibitory segment (AIS) interacts with the active site and inhibits catalytic activity.1 Publication

<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. AGC Ser/Thr protein kinase family. cGMP subfamily.Curated

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000288_73_2_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q8I719

Identification of Orthologs from Complete Genome Data

More...OMAi		SKNPDGH

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q8I719

Family and domain databases

Conserved Domains Database

More...CDDi		cd00038, CAP_ED, 4 hits
cd05572, STKc_cGK, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.60.120.10, 4 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000961, AGC-kinase_C
IPR002374, cGMP_dep_kinase
IPR018490, cNMP-bd-like
IPR018488, cNMP-bd_CS
IPR000595, cNMP-bd_dom
IPR011009, Kinase-like_dom_sf
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
IPR014710, RmlC-like_jellyroll
IPR008271, Ser/Thr_kinase_AS
IPR035014, STKc_cGK

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00027, cNMP_binding, 3 hits
PF00069, Pkinase, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000559, cGMP-dep_kinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00100, cNMP, 4 hits
SM00220, S_TKc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF51206, SSF51206, 4 hits
SSF56112, SSF56112, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51285, AGC_KINASE_CTER, 1 hit
PS00888, CNMP_BINDING_1, 3 hits
PS00889, CNMP_BINDING_2, 3 hits
PS50042, CNMP_BINDING_3, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

Q8I719-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEEDDNLKKG NERNKKKAIF SNDDFTGEDS LMEDHLELRE KLSEDIDMIK 
        60         70         80         90        100
TSLKNNLVCS TLNDNEILTL SNYMQFFVFK SGNLVIKQGE KGSYFFIINS 
       110        120        130        140        150
GKFDVYVNDK KVKTMGKGSS FGEAALIHNT QRSATIIAET DGTLWGVQRS 
       160        170        180        190        200
TFRATLKQLS NRNFNENRTF IDSVSVFDML TEAQKNMITN ACVIQNFKSG 
       210        220        230        240        250
ETIVKQGDYG DVLYILKEGK ATVYINDEEI RVLEKGSYFG ERALLYDEPR 
       260        270        280        290        300
SATIIAKEPT ACASICRKLL NIVLGNLQVV LFRNIMTEAL QQSEIFKQFS 
       310        320        330        340        350
GDQLNDLADT AIVRDYPANY NILHKDKVKS VKYIIVLEGK VELFLDDTSI 
       360        370        380        390        400
GILSRGMSFG DQYVLNQKQP FKHTIKSLEV CKIALITETC LADCLGNNNI 
       410        420        430        440        450
DASIDYNNKK SIIKKMYIFR YLTDKQCNLL IEAFRTTRYE EGDYIIQEGE 
       460        470        480        490        500
VGSRFYIIKN GEVEIVKNKK RLRTLGKNDY FGERALLYDE PRTASVISKV 
       510        520        530        540        550
NNVECWFVDK SVFLQIIQGP MLAHLEERIK MQDTKVEMDE LETERIIGRG 
       560        570        580        590        600
TFGTVKLVHH KPTKIRYALK CVSKRSIINL NQQNNIKLER EITAENDHPF 
       610        620        630        640        650
IIRLVRTFKD SKYFYFLTEL VTGGELYDAI RKLGLLSKSQ AQFYLGSIIL 
       660        670        680        690        700
AIEYLHERNI VYRDLKPENI LLDKQGYVKL IDFGCAKKVQ GRAYTLVGTP 
       710        720        730        740        750
HYMAPEVILG KGYGCTVDIW ALGICLYEFI CGPLPFGNDE EDQLEIFRDI 
       760        770        780        790        800
LTGQLTFPDY VTDTDSINLM KRLLCRLPQG RIGCSINGFK DIKDHPFFSN 
       810        820        830        840        850
FNWDKLAGRL LDPPLVSKSE TYAEDIDIKQ IEEEDAEDDE EPLNDEDNWD 

IDF
Length:853
Mass (Da):97,694
Last modified:March 1, 2003 - v1
<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:iDBBB189707A480E2
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
LN999946 Genomic DNA Translation: CZU00064.1

NCBI Reference Sequences

More...RefSeqi		XP_001348520.1, XM_001348484.1

Genome annotation databases

Ensembl protists genome annotation project

More...EnsemblProtistsi		CZU00064; CZU00064; PF3D7_1436600

Database of genes from NCBI RefSeq genomes

More...GeneIDi		811928

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		pfa:PF3D7_1436600

<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
LN999946 Genomic DNA Translation: CZU00064.1
RefSeqiXP_001348520.1, XM_001348484.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4OFFX-ray1.89A401-542[»]
4OFGX-ray2.00A401-542[»]
5DYKX-ray2.45A1-853[»]
5E16X-ray1.65A21-162[»]
AlphaFoldDBiQ8I719
SMRiQ8I719
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi5833.PF14_0346

Chemistry databases

GuidetoPHARMACOLOGYi3013

Proteomic databases

PRIDEiQ8I719

Genome annotation databases

EnsemblProtistsiCZU00064; CZU00064; PF3D7_1436600
GeneIDi811928
KEGGipfa:PF3D7_1436600

Organism-specific databases

VEuPathDBiPlasmoDB:PF3D7_1436600

Phylogenomic databases

HOGENOMiCLU_000288_73_2_1
InParanoidiQ8I719
OMAiSKNPDGH
PhylomeDBiQ8I719

Family and domain databases

CDDicd00038, CAP_ED, 4 hits
cd05572, STKc_cGK, 1 hit
Gene3Di2.60.120.10, 4 hits
InterProiView protein in InterPro
IPR000961, AGC-kinase_C
IPR002374, cGMP_dep_kinase
IPR018490, cNMP-bd-like
IPR018488, cNMP-bd_CS
IPR000595, cNMP-bd_dom
IPR011009, Kinase-like_dom_sf
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
IPR014710, RmlC-like_jellyroll
IPR008271, Ser/Thr_kinase_AS
IPR035014, STKc_cGK
PfamiView protein in Pfam
PF00027, cNMP_binding, 3 hits
PF00069, Pkinase, 1 hit
PIRSFiPIRSF000559, cGMP-dep_kinase, 1 hit
SMARTiView protein in SMART
SM00100, cNMP, 4 hits
SM00220, S_TKc, 1 hit
SUPFAMiSSF51206, SSF51206, 4 hits
SSF56112, SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS51285, AGC_KINASE_CTER, 1 hit
PS00888, CNMP_BINDING_1, 3 hits
PS00889, CNMP_BINDING_2, 3 hits
PS50042, CNMP_BINDING_3, 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

More...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 nameiKGP_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: Q8I719
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 10, 2021
Last sequence update: March 1, 2003
Last modified: May 25, 2022
This is version 149 of the entry and version 1 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

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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