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UniProtKB - Q5XXP4 (POLN_CHIK3)

Entry version 109 (02 Dec 2020)
Sequence version 1 (23 Nov 2004)
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Protein

Polyprotein P1234

Gene
N/A
Organism
Chikungunya virus (strain 37997) (CHIKV)
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>-Protein inferred from homologyi <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

Inactive precursor of the viral replicase, which is activated by cleavages carried out by the viral protease nsP2.By similarity
The early replication complex formed by the polyprotein P123 and nsP4 synthesizes minus-strand RNAs (By similarity). As soon P123 is cleaved into mature proteins, the plus-strand RNAs synthesis begins (By similarity).By similarity
The early replication complex formed by the polyprotein P123' and nsP4 synthesizes minus-strand RNAs (Probable). Polyprotein P123' is a short-lived polyprotein that accumulates during early stage of infection (Probable). As soon P123' is cleaved into mature proteins, the plus-strand RNAs synthesis begins (Probable).Curated
Cytoplasmic capping enzyme that catalyzes two virus-specific reactions: methyltransferase and nsP1 guanylyltransferase (By similarity). mRNA-capping is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus (Probable). The enzymatic reaction involves a covalent link between 7-methyl-GMP and nsP1, whereas eukaryotic capping enzymes form a covalent complex only with GMP (Probable). nsP1 capping consists in the following reactions: GTP is first methylated into 7-methyl-GMP and then is covalently linked to nsP1 to form the m7GMp-nsP1 complex from which 7-methyl-GMP complex is transferred to the mRNA to create the cap structure (By similarity). NsP1 is also needed for the initiation of the minus-strand RNAs synthesis (By similarity). Probably serves as a membrane anchor for the replication complex composed of nsP1-nsP4 (By similarity). Palmitoylated nsP1 is remodeling host cell cytoskeleton, and induces filopodium-like structure formation at the surface of the host cell (By similarity).By similarityCurated
Multifunctional protein whose N-terminus is part of the RNA polymerase complex and displays NTPase, RNA triphosphatase and helicase activities (By similarity). NTPase and RNA triphosphatase are involved in viral RNA capping and helicase keeps a check on the dsRNA replication intermediates (By similarity). The C-terminus harbors a protease that specifically cleaves the polyproteins and releases the mature proteins (By similarity). Required for the shutoff of minus-strand RNAs synthesis (By similarity). Specifically inhibits the host IFN response by promoting the nuclear export of host STAT1 (By similarity). Also inhibits host transcription by inducing the rapid proteasome-dependent degradation of POLR2A, a catalytic subunit of the RNAPII complex (By similarity). The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity).By similarity
Seems to be essential for minus-strand RNAs and subgenomic 26S mRNAs synthesis (By similarity). Displays mono-ADP-ribosylhydrolase activity (Probable). ADP-ribosylation is a post-translational modification that controls various processes of the host cell and the virus probably needs to revert it for optimal viral replication (Probable). Binds proteins of FXR family and sequesters them into the viral RNA replication complexes thereby inhibiting the formation of host stress granules on viral mRNAs (Probable). The nsp3'-FXR complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes, thanks to the ability of FXR family members to self-assemble and bind DNA (Probable).By similarityCurated
Seems to be essential for minus-strand RNAs and subgenomic 26S mRNAs synthesis (By similarity). Displays mono-ADP-ribosylhydrolase activity (By similarity). ADP-ribosylation is a post-translational modification that controls various processes of the host cell and the virus probably needs to revert it for optimal viral replication (By similarity). Binds proteins of G3BP family and sequesters them into the viral RNA replication complexes thereby inhibiting the formation of host stress granules on viral mRNAs (By similarity). The nsp3-G3BP complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes, thanks to the ability of G3BP family members to self-assemble and bind DNA (By similarity).By similarity
RNA dependent RNA polymerase (By similarity). Replicates genomic and antigenomic RNA by recognizing replications specific signals. The early replication complex formed by the polyprotein P123 and nsP4 synthesizes minus-strand RNAs (By similarity). The late replication complex composed of fully processed nsP1-nsP4 is responsible for the production of genomic and subgenomic plus-strand RNAs (By similarity).By similarity

Miscellaneous

Viral replication produces dsRNA in the late phase of infection, resulting in a strong activation of host EIF2AK2/PKR, leading to almost complete phosphorylation of EIF2A (By similarity). This inactivates completely cellular translation initiation, resulting shutoff of host proteins synthesis (By similarity). However, phosphorylation of EIF2A is probably not the only mechanism responsible for the host translation shutoff (By similarity). The viral translation can still occur normally because it relies on a hairpin structure in the coding region of sgRNA and is EIF2A-, EIF2D-, EIF4G- EIF4A-independent (By similarity).By similarity
The genome codes for P123, but readthrough of a terminator codon UGA occurs between the codons for Leu-1856 and Leu-1858 giving rise to P1234 (Probable). P1234 is cleaved quickly by nsP2 into P123' and nsP4 (By similarity). Further processing of p123' gives nsP1, nsP2 and nsP3' which is 6 amino acids longer than nsP3 since the cleavage site is after the readthrough (By similarity). This unusual molecular mechanism ensures that few nsP4 are produced compared to other non-structural proteins (By similarity). Mutant viruses with no alternative termination site grow significantly slower than wild-type virus (By similarity). The opal termination codon is frequently mutated to a sense codon on passage in cell culture (By similarity). The presence of the opal codon may be a requirement for viral maintenance in both vertebrate and invertebrate hosts and a selective advantage may be conferred in cell culture for the sense codon (By similarity).By similarityCurated

<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

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Sitei37Involved in the phosphoramide link with 7-methyl-GMPBy similarity1
<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 sitei1013For cysteine protease nsP2 activityPROSITE-ProRule annotation1
Active sitei1083For cysteine protease nsP2 activityPROSITE-ProRule annotation1
<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 sitei1343ADP-riboseBy similarity1
Binding sitei1357ADP-riboseBy similarity1
Binding sitei1365ADP-riboseBy similarity1
Binding sitei1445ADP-riboseBy similarity1
Binding sitei1446ADP-riboseBy similarity1
Binding sitei1447ADP-riboseBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi1595ZincBy similarity1
Metal bindingi1597ZincBy similarity1
Metal bindingi1620ZincBy similarity1
Metal bindingi1638ZincBy similarity1

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 bindingi721 – 728NTPPROSITE-ProRule annotation8

<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 functionHelicase, Hydrolase, Methyltransferase, Multifunctional enzyme, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Thiol protease, Transferase
Biological processEukaryotic host gene expression shutoff by virus, Eukaryotic host transcription shutoff by virus, Host gene expression shutoff by virus, Host-virus interaction, Inhibition of host RNA polymerase II by virus, mRNA capping, mRNA processing, Viral RNA replication
LigandATP-binding, GTP-binding, Metal-binding, Nucleotide-binding, S-adenosyl-L-methionine, Zinc

<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:
Polyprotein P1234
Short name:
P1234
Alternative name(s):
Non-structural polyprotein
Cleaved into the following 7 chains:
Polyprotein P123'
Short name:
P123'
Polyprotein P123
Short name:
P123
mRNA-capping enzyme nsP1 (EC:2.1.1.-By similarity, EC:2.7.7.-By similarity)
Alternative name(s):
Non-structural protein 1
Protease nsP2 (EC:3.1.3.33By similarity, EC:3.4.22.-By similarity, EC:3.6.1.15By similarity, EC:3.6.4.13By similarity)
Alternative name(s):
Non-structural protein 2
Short name:
nsP2
Non-structural protein 3' (EC:3.1.3.84Curated)
Short name:
nsP3'
Non-structural protein 3 (EC:3.1.3.84By similarity)
Short name:
nsP3
RNA-directed RNA polymerase nsP4 (EC:2.7.7.19By similarity, EC:2.7.7.48PROSITE-ProRule annotation)
Alternative name(s):
Non-structural protein 4
Short name:
nsP4
<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>OrganismiChikungunya virus (strain 37997) (CHIKV)
<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 identifieri371095 [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 lineageiViruses › Riboviria › Orthornavirae › Kitrinoviricota › Alsuviricetes › Martellivirales › Togaviridae › Alphavirus ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiAedes aegypti (Yellowfever mosquito) (Culex aegypti) [TaxID: 7159]
Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta) [TaxID: 7160]
Aedes furcifer (Mosquito) [TaxID: 299627]
Aedes polynesiensis (Polynesian tiger mosquito) [TaxID: 188700]
Cercopithecus [TaxID: 9533]
Homo sapiens (Human) [TaxID: 9606]
Macaca (macaques) [TaxID: 9539]
Pan troglodytes (Chimpanzee) [TaxID: 9598]
Papio (baboons) [TaxID: 9554]
Presbytis [TaxID: 9573]
<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
  • UP000008450 <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: Genome

<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

  • Host cytoplasmic vesicle membrane By similarity; Peripheral membrane protein Curated
    • Note: In the late phase of infection, the polyprotein is quickly cleaved before localization to cellular membranes. Then nsP3 and nsP3' form aggregates in cytoplasm (By similarity). NsP3' is also part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex (By similarity).By similarity
  • Host cytoplasmic vesicle membrane By similarity; Peripheral membrane protein Curated
    • Note: In the late phase of infection, the polyprotein is quickly cleaved before localization to cellular membranes. Then nsP3 and nsP3' form aggregates in cytoplasm (By similarity). NsP3 is also part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Host cell membrane, Host cell projection, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Host nucleus, Membrane

<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_00003083961 – 2474Polyprotein P1234Add BLAST2474
ChainiPRO_00002277651 – 1863Polyprotein P123'Add BLAST1863
ChainiPRO_00004466481 – 1856Polyprotein P123Add BLAST1856
ChainiPRO_00002277661 – 535mRNA-capping enzyme nsP1Add BLAST535
ChainiPRO_0000227767536 – 1333Protease nsP2Add BLAST798
ChainiPRO_00002277681334 – 1863Non-structural protein 3'Add BLAST530
ChainiPRO_00004466491334 – 1856Non-structural protein 3Add BLAST523
ChainiPRO_00002277691864 – 2474RNA-directed RNA polymerase nsP4Add BLAST611

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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>Lipidationi417S-palmitoyl cysteine; by hostBy similarity1
Lipidationi419S-palmitoyl cysteine; by hostBy similarity1

<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

Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The processing of the polyprotein is temporally regulated (By similarity). In early stages (1.7 hpi), P1234 is first cleaved in trans through its nsP2 protease activity, releasing P123' and nsP4, which associate to form the early replication complex (By similarity). At the same time, P1234 is also cut at the nsP1/nsP2 site early in infection but with lower efficiency (By similarity). After replication of the viral minus-strand RNAs (4 hpi), the polyproteins are cut at the nsP1/nsP2 and nsP2/nsP3 sites very efficiently, preventing accumulation of P123' and P1234 and allowing the formation of the late replication complex (By similarity). NsP3'/nsP4 site is not cleaved anymore and P34 is produced rather than nsP4 (By similarity).By similarity
Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The processing of the polyprotein is temporally regulated (By similarity). In early stages (1.7 hpi), P123 is cleaved at the nsP1/nsP2 site with low efficiency (By similarity). After replication of the viral minus-strand RNAs (4 hpi), the polyproteins are cut at the nsP1/nsP2 and nsP2/nsP3 sites very efficiently, preventing accumulation of P123 and allowing the formation of the late replication complex (By similarity).By similarity
Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The processing of the polyprotein is temporally regulated (By similarity). In early stages (1.7 hpi), P123' is cleaved at the nsP1/nsP2 site with low efficiency (By similarity). After replication of the viral minus-strand RNAs (4 hpi), the polyproteins are cut at the nsP1/nsP2 and nsP2/nsP3 sites very efficiently, preventing accumulation of P123' and allowing the formation of the late replication complex (By similarity).By similarity
Palmitoylated by host palmitoyltransferases ZDHHC2 and ZDHHC19.By similarity
Phosphorylated by host on serines and threonines.By similarity
Phosphorylated by host on serines and threonines.By similarity
ubiquitinated; targets the protein for rapid degradation via the ubiquitin system (By similarity). Nsp4 is present in extremely low quantities due to low frequency of translation through the amber stop-codon and the degradation by the ubiquitin pathway (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei535 – 536Cleavage; by protease nsP2By similarity2
Sitei1333 – 1334Cleavage; by protease nsP2By similarity2
Sitei1863 – 1864Cleavage; by protease nsP2By similarity2

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		Q5XXP4

<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

Interacts with non-structural protein 3 (By similarity).

Interacts with RNA-directed RNA polymerase nsP4 (By similarity).

Interacts with protease nsP2 (By similarity). interacts with itself (By similarity).

By similarity

Interacts with mRNA-capping enzyme nsP1 (By similarity).

Interacts with host DDX1 (By similarity).

Interacts with host DDX3 (By similarity).

Interacts (via C-terminus) with host G3BP1; this interaction inhibits the formation of host stress granules on viral mRNAs and the nsp3-G3BP1 complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes (By similarity).

Interacts (via C-terminus) with host G3BP2; this interaction inhibits the formation of host stress granules on viral mRNAs and the nsp3-G3BP2 complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes (By similarity).

By similarity

Interacts with mRNA-capping enzyme nsP1 (By similarity).

Interacts with protease nsP2 (By similarity). interacts with itself (By similarity).

By similarity

Interacts with RNA-directed RNA polymerase nsP4 (By similarity).

Interacts with mRNA-capping enzyme nsP1 (By similarity).

Interacts with KPNA1/karyopherin-alpha1; this interaction probably allows the active transport of protease nsP2 into the host nucleus (By similarity).

By similarity

<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>Domaini28 – 259Alphavirus-like MTPROSITE-ProRule annotationAdd BLAST232
Domaini690 – 842(+)RNA virus helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST153
Domaini843 – 991(+)RNA virus helicase C-terminalPROSITE-ProRule annotationAdd BLAST149
Domaini1004 – 1327Peptidase C9PROSITE-ProRule annotationAdd BLAST324
Domaini1334 – 1493MacroPROSITE-ProRule annotationAdd BLAST160
Domaini2228 – 2343RdRp catalyticPROSITE-ProRule annotationAdd BLAST116

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>Regioni244 – 263NsP1 membrane-bindingBy similarityAdd BLAST20
Regioni1005 – 1024Nucleolus localization signalBy similarityAdd BLAST20

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>Motifi1058 – 1067Nuclear export signalBy similarity10
Motifi1182 – 1186Nuclear localization signalBy similarity5
Motifi1812 – 1815FGDF; binding to host G3BP1By similarity4
Motifi1830 – 1833FGDF; binding to host G3BP1By similarity4

<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 N-terminus exhibits NTPase and RNA triphosphatase activities and is proposed to have helicase activity, whereas the C-terminus possesses protease activity (By similarity). Contains a nuclear localization signal and a nuclear export signal, these two motifs are probably involved in the shuttling between the cytoplasm and the nucleus of nsP2 (By similarity). The C-terminus is required for promoting the export of host STAT1 (By similarity).By similarity
In the N-terminus, the macro domain displays a mono-ADP-ribosylhydrolase activity (By similarity). The central part has a zinc-binding function (By similarity). The C-terminus contains two FGDF motifs necessary and sufficient for formation of the nsP3/G3BP1 complex (By similarity).By similarity
In the N-terminus, the macro domain displays a mono-ADP-ribosylhydrolase activity (By similarity). The central part has a zinc-binding function (By similarity). The C-terminus contains two FGDF motifs necessary and sufficient for formation of the nsP3'/G3BP1 complex (By similarity).By similarity

Family and domain databases

Database of protein disorder

More...DisProti		DP01188

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.220.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR027351, (+)RNA_virus_helicase_core_dom
IPR002588, Alphavirus-like_MT_dom
IPR002620, Alphavirus_nsp2pro
IPR043502, DNA/RNA_pol_sf
IPR002589, Macro_dom
IPR043472, Macro_dom-like
IPR027417, P-loop_NTPase
IPR007094, RNA-dir_pol_PSvirus
IPR001788, Tymovirus_RNA-dep_RNA_pol

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01661, Macro, 1 hit
PF01707, Peptidase_C9, 1 hit
PF00978, RdRP_2, 1 hit
PF01443, Viral_helicase1, 1 hit
PF01660, Vmethyltransf, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00506, A1pp, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52540, SSF52540, 1 hit
SSF52949, SSF52949, 1 hit
SSF56672, SSF56672, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51743, ALPHAVIRUS_MT, 1 hit
PS51154, MACRO, 1 hit
PS51520, NSP2PRO, 1 hit
PS51657, PSRV_HELICASE, 1 hit
PS50507, RDRP_SSRNA_POS, 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.

<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 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.

Q5XXP4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDPVYVDIDA DSAFLKALQR AYPMFEVEPR QVTPNDHANA RAFSHLAIKL 
        60         70         80         90        100
IEQEIDPDST ILDIGSAPAR RMMSDRKYHC VCPMRSAEDP ERLANYARKL 
       110        120        130        140        150
ASAAGKVLDR NISEKIGDLQ AVMAVPDAET PTFCLHTDVS CRQRADVAIY 
       160        170        180        190        200
QDVYAVHAPT SLYHQAIKGV RVAYWIGFDT TPFMYNAMAG AYPSYSTNWA 
       210        220        230        240        250
DEQVLKAKNI GLCSTDLTEG RRGKLSIMRG KKMKPCDRVL FSVGSTLYPE 
       260        270        280        290        300
SRKLLKSWHL PSVFHLKGKL SFTCRCDTVV SCEGYVVKRI TISPGLYGKT 
       310        320        330        340        350
TGYAVTHHAD GFLMCKTTDT VDGERVSFSV CTYVPATICD QMTGILATEV 
       360        370        380        390        400
TPEDAQKLLV GLNQRIVVNG RTQRNTNTMK NYLLPVVAQA FSKWAKECRK 
       410        420        430        440        450
DMEDEKLLGI RERTLTCCCL WAFKKQKTHT VYKRPDTQSI QKVPAEFDSF 
       460        470        480        490        500
VVPSLWSSGL SIPLRTRIKW LLSKVPKTDL IPYSGDAKEA RDAEKEAEEE 
       510        520        530        540        550
REAELTREAL PPLQAAQDDV QVEIDVEQLE DRAGAGIIET PRGAIKVTAQ 
       560        570        580        590        600
PTDHVVGEYL VLSPQTVLRS QKLSLIHALA EQVKTCTHSG RAGRYAVEAY 
       610        620        630        640        650
DGRILVPSGY AISPEDFQSL SESATMVYNE REFVNRKLHH IALHGPALNT 
       660        670        680        690        700
DEESYELVRA ERTEHEYVYD VDQRRCCKKE EAAGLVLVGD LTNPPYHEFA 
       710        720        730        740        750
YEGLRIRPAC PYKTAVIGVF GVPGSGKSAI IKNLVTRQDL VTSGKKENCQ 
       760        770        780        790        800
EISTDVMRQR NLEISARTVD SLLLNGCNRP VDVLYVDEAF ACHSGTLLAL 
       810        820        830        840        850
IALVRPRQKV VLCGDPKQCG FFNMMQMKVN YNHNICTQVY HKSISRRCTL 
       860        870        880        890        900
PVTAIVSSLH YEGKMRTTNE YNKPIVVDTT GSTKPDPGDL VLTCFRGWVK 
       910        920        930        940        950
QLQIDYRGHE VMTAAASQGL TRKGVYAVRQ KVNENPLYAS TSEHVNVLLT 
       960        970        980        990       1000
RTEGKLVWKT LSGDPWIKTL QNPPKGNFKA TIKEWEVEHA SIMAGICNHQ 
      1010       1020       1030       1040       1050
VTFDTFQNKA NVCWAKSLVP ILETAGIKLN DRQWSQIIQA FKEDRAYSPE 
      1060       1070       1080       1090       1100
VALNEICTRM YGVDLDSGLF SKPLVSVHYA DNHWDNRPGG KMFGFNPEAA 
      1110       1120       1130       1140       1150
SILERKYPFT KGKWNTNKQI CVTTRRIEDF NPNTNIIPAN RRLPHSLVAE 
      1160       1170       1180       1190       1200
HRPVKGERME WLVNKINGHH VLLVSGYNLV LPTKRVTWVA PLGIRGADYT 
      1210       1220       1230       1240       1250
YNLELGLPAT LGRYDLVIIN IHTPFRIHHY QQCVDHAMKL QMLGGDSLRL 
      1260       1270       1280       1290       1300
LKPGGSLLIR AYGYADRTSE RVVCVLGRKF RSSRALKPPC VTSNTEMFFL 
      1310       1320       1330       1340       1350
FSNFDNGRRN FTTHVMNNQL NAAFVGQATR AGCAPSYRVK RMDIAKNDEE 
      1360       1370       1380       1390       1400
CVVNAANPRG LPGDGVCKAV YKKWPESFKN SATPVGTAKT VMCGTYPVIH 
      1410       1420       1430       1440       1450
AVGPNFSNYS ESEGDRELAA AYREVAKEVT RLGVNSVAIP LLSTGVYSGG 
      1460       1470       1480       1490       1500
KDRLTQSLNH LFTALDSTDA DVVIYCRDKE WEKKIAEAIQ MRTQVELLDE 
      1510       1520       1530       1540       1550
HISVDCDIIR VHPDSSLAGR KGYSTTEGSL YSYLEGTRFH QTAVDMAEVY 
      1560       1570       1580       1590       1600
TMWPKQTEAN EQVCLYALGE SIESIRQKCP VDDADASSPP KTVPCLCRYA 
      1610       1620       1630       1640       1650
MTPERVTRLR MNHVTSIIVC SSFPLPKYKI EGVQKVKCSK VMLFDHNVPS 
      1660       1670       1680       1690       1700
RVSPREYKSP QETAQEVSST TSLTHSQFDL SVDGEELPAP SDLEADAPIP 
      1710       1720       1730       1740       1750
EPTPDDRAVL TLPPTIDNFS AVSDWVMNTA PVAPPRRRRG KNLNVTCDER 
      1760       1770       1780       1790       1800
EGNVLPMASV RFFRADLHSI VQETAEIRDT AASLQAPLSV ATEPNQLPIS 
      1810       1820       1830       1840       1850
FGAPNETFPI TFGDFDEGEI ESLSSELLTF GDFSPGEVDD LTDSDWSTCS 
      1860       1870       1880       1890       1900
DTDDELXLDR AGGYIFSSDT GPGHLQQRSV RQTVLPVNTL EEVQEEKCYP 
      1910       1920       1930       1940       1950
PKLDEVKEQL LLKKLQESAS MANRSRYQSR KVENMKATIV QRLKGGCKLY 
      1960       1970       1980       1990       2000
LMSETPKVPT YRTTYPAPVY SPPINIRLSN PESAVAACNE FLARNYPTVA 
      2010       2020       2030       2040       2050
SYQITDEYDA YLDMVDGSES CLDRATFNPS KLRSYPKQHS YHAPTIRSAV 
      2060       2070       2080       2090       2100
PSPFQNTLQN VLAAATKRNC NVTQMRELPT LDSAVFNVEC FKKFACNQEY 
      2110       2120       2130       2140       2150
WKEFAASPIR ITTENLTTYV TKLKGPKAAA LFAKTHNLLP LQEVPMDRFT 
      2160       2170       2180       2190       2200
VDMKRDVKVT PGTKHTEERP KVQVIQAAEP LATAYLCGIH RELVRRLNAV 
      2210       2220       2230       2240       2250
LLPNVHTLFD MSAEDFDAII AAHFKPGDAV LETDIASFDK SQDDSLALTA 
      2260       2270       2280       2290       2300
LMLLEDLGVD HPLLDLIEAA FGEISSCHLP TGTRFKFGAM MKSGMFLTLF 
      2310       2320       2330       2340       2350
VNTLLNITIA SRVLEDRLTR SACAAFIGDD NIIHGVVSDE LMAARCATWM 
      2360       2370       2380       2390       2400
NMEVKIIDAV VSQKAPYFCG GFILYDTVAG TACRVADPLK RLFKLGKPLA 
      2410       2420       2430       2440       2450
AGDEQDDDRR RALADEVVRW QRTGLTDELE KAVHSRYEVQ GISVVVMSMA 
      2460       2470 
TFASSRSNFE KLRGPVVTLY GGPK
Length:2,474
Mass (Da):275,933
Last modified:November 23, 2004 - 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:i0699DB0485FB3097
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
AY726732 Genomic RNA Translation: AAU43880.1

Keywords - Coding sequence diversityi

RNA suppression of termination

<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
AY726732 Genomic RNA Translation: AAU43880.1

3D structure databases

Database of comparative protein structure models

More...ModBasei		Search...

Proteomic databases

PRIDEiQ5XXP4

Family and domain databases

DisProtiDP01188
Gene3Di3.40.220.10, 1 hit
InterProiView protein in InterPro
IPR027351, (+)RNA_virus_helicase_core_dom
IPR002588, Alphavirus-like_MT_dom
IPR002620, Alphavirus_nsp2pro
IPR043502, DNA/RNA_pol_sf
IPR002589, Macro_dom
IPR043472, Macro_dom-like
IPR027417, P-loop_NTPase
IPR007094, RNA-dir_pol_PSvirus
IPR001788, Tymovirus_RNA-dep_RNA_pol
PfamiView protein in Pfam
PF01661, Macro, 1 hit
PF01707, Peptidase_C9, 1 hit
PF00978, RdRP_2, 1 hit
PF01443, Viral_helicase1, 1 hit
PF01660, Vmethyltransf, 1 hit
SMARTiView protein in SMART
SM00506, A1pp, 1 hit
SUPFAMiSSF52540, SSF52540, 1 hit
SSF52949, SSF52949, 1 hit
SSF56672, SSF56672, 1 hit
PROSITEiView protein in PROSITE
PS51743, ALPHAVIRUS_MT, 1 hit
PS51154, MACRO, 1 hit
PS51520, NSP2PRO, 1 hit
PS51657, PSRV_HELICASE, 1 hit
PS50507, RDRP_SSRNA_POS, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

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 nameiPOLN_CHIK3
<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: Q5XXP4
<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: March 21, 2006
Last sequence update: November 23, 2004
Last modified: December 2, 2020
This is version 109 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)
Annotation programViral Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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