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Entry version 115 (18 Sep 2019)
Sequence version 1 (01 Oct 2002)
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Protein

Polyprotein P1234

Gene
N/A
Organism
Chikungunya virus (strain S27-African prototype) (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>
-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

Polyprotein P1234: Inactive precursor of the viral replicase, which is activated by cleavages carried out by the viral protease nsP2.1 Publication
Polyprotein P123: 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
mRNA-capping enzyme nsP1: 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 (By similarity). 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 (PubMed:30404808).By similarityCurated1 Publication
Protease nsP2: Multifunctional protein whose N-terminus is part of the RNA polymerase complex and displays NTPase, RNA triphosphatase and helicase activities (PubMed:21811589, PubMed:24407286). 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 (PubMed:27845418, PubMed:26597768). 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 (PubMed:29925658). Also inhibits host transcription by inducing the rapid proteasome-dependent degradation of POLR2A, a catalytic subunit of the RNAPII complex (PubMed:22514352). The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (Probable).By similarity1 Publication6 Publications
Non-structural protein 3: Seems to be essential for minus-strand RNAs and subgenomic 26S mRNAs synthesis (By similarity). Displays mono-ADP-ribosylhydrolase activity (PubMed:28143925, PubMed:28150709). 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 (PubMed:28143925, PubMed:28150709). 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 (PubMed:25653451). 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 (PubMed:27509095, PubMed:27383630) (Probable).By similarity1 Publication5 Publications
RNA-directed RNA polymerase nsP4: 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

Caution

There is no stop codon readthrough before nsP4 like in other CHIKV strains. The opal termination codon may have been mutated to a sense codon on passage in cell culture. The presence of an 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 (PubMed:29138302).Curated1 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

Protein has several cofactor binding sites:

<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 7.2 for nsP2 NTPase.2 Publications

Temperature dependencei

Optimum temperature is 37 degrees Celsius for nsP2 NTPase.1 Publication

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_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 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_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 sitei1343ADP-ribose1 Publication1
Binding sitei1357ADP-ribose1 Publication1
Binding sitei1365ADP-ribose1 Publication1
Binding sitei1445ADP-ribose1 Publication1
Binding sitei1446ADP-ribose1 Publication1
Binding sitei1447ADP-ribose1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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_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 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

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 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 innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host RNA polymerase II by virus, Inhibition of host STAT1 by virus, mRNA capping, mRNA processing, Viral immunoevasion, Viral RNA replication
LigandATP-binding, GTP-binding, Metal-binding, Nucleotide-binding, S-adenosyl-L-methionine, Zinc

Protein family/group databases

MEROPS protease database

More...
MEROPSi
C09.001

<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:
Polyprotein P1234
Short name:
P1234
Alternative name(s):
Non-structural polyprotein
Cleaved into the following 5 chains:
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:3.1.3.331 Publication, EC:3.4.22.-2 Publications, EC:3.6.1.152 Publications, EC:3.6.4.132 Publications)
Alternative name(s):
Non-structural protein 2
Short name:
nsP2
Non-structural protein 3 (EC:3.1.3.841 Publication)
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_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>OrganismiChikungunya virus (strain S27-African prototype) (CHIKV)
<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 identifieri371094 [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 lineageiVirusesRiboviriaTogaviridaeAlphavirus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_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
  • UP000000569 <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: 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

Polyprotein P1234 :
Polyprotein P123 :
mRNA-capping enzyme nsP1 :
Protease nsP2 :
Non-structural protein 3 :
  • 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 forms 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
RNA-directed RNA polymerase nsP4 :

GO - Cellular componenti

Keywords - Cellular componenti

Host cell membrane, Host cell projection, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Host nucleus, 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_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>Mutagenesisi417C → A: Loss of palmitoylation. 1 Publication1
Mutagenesisi419C → A: Loss of palmitoylation. 1 Publication1
Mutagenesisi727K → A: 5 fold reduction of NTPase activity and 50% loss of RTPase activity. 1 Publication1
Mutagenesisi787 – 788DE → AA: 5 fold reduction of NTPase activity and 50% loss of RTPase activity. 1 Publication2
Mutagenesisi1013C → A: Complete loss of nsP2 protease activity; when associated with A-1017. 2 Publications1
Mutagenesisi1014W → A: Complete loss of nsP2 protease activity. 1 Publication1
Mutagenesisi1017S → A: Complete loss of nsP2 protease activity; when associated with A-1013. 2 Publications1
Mutagenesisi1084W → A: Increased nsP2 protease activity. 1 Publication1
Mutagenesisi1084W → F: Decreased nsP2 protease activity. 1 Publication1
Mutagenesisi1184 – 1185KR → AA: Complete loss of nuclear localization and inhibition of JAK/STAT signaling. 1 Publication2
Mutagenesisi1253P → A: Complete loss of host transcription shutoff, still able to localize in the nucleus and inhibit JAK/STAT signaling. 1 Publication1
Mutagenesisi1343D → A: Partial loss of ADP-ribose 1" phosphate phosphatase activity. 1 Publication1
Mutagenesisi1357N → A: Partial loss of mono-ADP-ribosylhydrolase activity; complete loss of ADP-ribose 1" phosphate phosphatase activity. 2 Publications1
Mutagenesisi1357N → R or Y: Almost complete loss of mono-ADP-ribosylhydrolase activity. 1 Publication1
Mutagenesisi1366V → A: Partial loss of mono-ADP-ribosylhydrolase activity. 1 Publication1
Mutagenesisi1366V → E or F: Almost complete loss of mono-ADP-ribosylhydrolase activity. 1 Publication1
Mutagenesisi1447Y → A: Partial loss of mono-ADP-ribosylhydrolase activity; complete loss of ADP-ribose 1" phosphate phosphatase activity. 2 Publications1
Mutagenesisi1447Y → V or W: Almost complete loss of mono-ADP-ribosylhydrolase activity. 1 Publication1
Mutagenesisi1812F → A: Complete loss of binding to host G3BP1; when associated with A-1830. 1 Publication1
Mutagenesisi1830F → A: Complete loss of binding to host G3BP1; when associated with A-1812. 1 Publication1

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003083951 – 2474Polyprotein P1234Add BLAST2474
ChainiPRO_00002277601 – 1863Polyprotein P123Add BLAST1863
ChainiPRO_00002277611 – 535mRNA-capping enzyme nsP1Add BLAST535
ChainiPRO_0000227762536 – 1333Protease nsP2Add BLAST798
ChainiPRO_00002277631334 – 1863Non-structural protein 3Add BLAST530
ChainiPRO_00002277641864 – 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_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>Lipidationi417S-palmitoyl cysteine; by host1 Publication1
Lipidationi419S-palmitoyl cysteine; by host1 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

Polyprotein P1234: Specific enzymatic cleavages in vivo yield mature proteins (PubMed:27845418). 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 similarity1 Publication
Polyprotein P123: 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
mRNA-capping enzyme nsP1: Palmitoylated by host palmitoyltransferases ZDHHC2 and ZDHHC19.1 Publication
Non-structural protein 3: Phosphorylated by host on serines and threonines.By similarity
RNA-directed RNA polymerase nsP4: 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 nsP21 Publication2

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q8JUX6

<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

mRNA-capping enzyme nsP1:

Interacts with non-structural protein 3 (PubMed:22951312). Non-structural protein 3:

Interacts with mRNA-capping enzyme nsP1 (PubMed:22951312). mRNA-capping enzyme nsP1:

Interacts with RNA-directed RNA polymerase nsP4 (PubMed:22951312). RNA-directed RNA polymerase nsP4:

Interacts with mRNA-capping enzyme nsP1 (PubMed:22951312). RNA-directed RNA polymerase nsP4:

Interacts with protease nsP2 (PubMed:22951312). Protease nsP2:

Interacts with RNA-directed RNA polymerase nsP4 (PubMed:22951312). mRNA-capping enzyme nsP1:

Interacts with protease nsP2 (PubMed:22951312). Protease nsP2:

Interacts with mRNA-capping enzyme nsP1 (PubMed:22951312). RNA-directed RNA polymerase nsP4 interacts with itself (PubMed:22951312). mRNA-capping enzyme nsP1 interacts with itself (PubMed:22951312). Protease nsP2:

Interacts with KPNA1/karyopherin-alpha1; this interaction probably allows the active transport of protease nsP2 into the host nucleus (By similarity). Non-structural protein 3:

Interacts with host DDX1 (By similarity). Non-structural protein 3:

Interacts with host DDX3 (By similarity). Non-structural protein 3:

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 (PubMed:24623412, PubMed:27383630, PubMed:27509095). Non-structural protein 3:

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 similarity4 Publications

<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

12474
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
Q8JUX6

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q8JUX6

<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>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 G3BP11 Publication4
Motifi1830 – 1833FGDF; binding to host G3BP11 Publication4

<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

Protease nsP2: The N-terminus exhibits NTPase and RNA triphosphatase activities and is proposed to have helicase activity, whereas the C-terminus possesses protease activity (PubMed:24407286). 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 (PubMed:29925658).By similarity2 Publications
Non-structural protein 3: In the N-terminus, the macro domain displays a mono-ADP-ribosylhydrolase activity (PubMed:28150709, PubMed:28143925). 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 (Probable) (PubMed:27383630, PubMed:27509095).By similarity1 Publication4 Publications

Family and domain databases

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
IPR002589 Macro_dom
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

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_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.

Q8JUX6-1 [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 NISGKIGDLQ AVMAVPDTET PTFCLHTDVS CRQRADVAIY
160 170 180 190 200
QDVYAVHAPT SLYHQAIKGV RLAYWVGFDT TPFMYNAMAG AYPSYSTNWA
210 220 230 240 250
DEQVLKAKNI GLCSTDLTEG RRGKLSIMRG KKLEPCDRVL FSVGSTLYPE
260 270 280 290 300
SRKLLKSWHL PSVFHLKGKL SFTCRCDTVV SCEGYVVKRI TMSPGLYGKT
310 320 330 340 350
TGYAVTHHAD GFLMCKTTDT VDGERVSFSV CTYVPATICD QMTGILATEV
360 370 380 390 400
TPEDAQKLLV GLNQRIVVNG RTQRNTNTMK NYMIPVVAQA FSKWAKECRK
410 420 430 440 450
DMEDEKLLGV RERTLTCCCL WAFKKQKTHT VYKRPDTQSI QKVQAEFDSF
460 470 480 490 500
VVPSLWSSGL SIPLRTRIKW LLSKVPKTDL TPYSGDAQEA RDAEKEAEEE
510 520 530 540 550
REAELTLEAL PPLQAAQEDV QVEIDVEQLE DRAGAGIIET PRGAIKVTAQ
560 570 580 590 600
PTDHVVGEYL VLSPQTVLRS QKLSLIHALA EQVKTCTHSG RAGRYAVEAY
610 620 630 640 650
DGRVLVPSGY AISPEDFQSL SESATMVYNE REFVNRKLHH IAMHGPALNT
660 670 680 690 700
DEESYELVRA ERTEHEYVYD VDQRRCCKKE EAAGLVLVGD LTNPPYHEFA
710 720 730 740 750
YEGLKIRPAC PYKIAVIGVF GVPGSGKSAI IKNLVTRQDL VTSGKKENCQ
760 770 780 790 800
EITTDVMRQR GLEISARTVD 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 SIMAGICSHQ
1010 1020 1030 1040 1050
MTFDTFQNKA NVCWAKSLVP ILETAGIKLN DRQWSQIIQA FKEDKAYSPE
1060 1070 1080 1090 1100
VALNEICTRM YGVDLDSGLF SKPLVSVYYA DNHWDNRPGG KMFGFNPEAA
1110 1120 1130 1140 1150
SILERKYPFT KGKWNINKQI CVTTRRIEDF NPTTNIIPAN RRLPHSLVAE
1160 1170 1180 1190 1200
HRPVKGERME WLVNKINGHH VLLVSGCSLA LPTKRVTWVA PLGVRGADYT
1210 1220 1230 1240 1250
YNLELGLPAT LGRYDLVVIN IHTPFRIHHY QQCVDHAMKL QMLGGDSLRL
1260 1270 1280 1290 1300
LKPGGSLLIR AYGYADRTSE RVICVLGRKF 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 LFTAMDSTDA DVVIYCRDKE WEKKISEAIQ MRTQVELLDE
1510 1520 1530 1540 1550
HISIDCDVVR VHPDSSLAGR KGYSTTEGAL YSYLEGTRFH QTAVDMAEIY
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
RVSPREYRPS QESVQEASTT TSLTHSQFDL SVDGKILPVP SDLDADAPAL
1710 1720 1730 1740 1750
EPALDDGAIH TLPSATGNLA AVSDWVMSTV PVAPPRRRRG RNLTVTCDER
1760 1770 1780 1790 1800
EGNITPMASV RFFRAELCPV VQETAETRDT AMSLQAPPST ATELSHPPIS
1810 1820 1830 1840 1850
FGAPSETFPI TFGDFNEGEI ESLSSELLTF GDFLPGEVDD LTDSDWSTCS
1860 1870 1880 1890 1900
DTDDELRLDR AGGYIFSSDT GPGHLQQKSV RQSVLPVNTL EEVHEEKCYP
1910 1920 1930 1940 1950
PKLDEAKEQL LLKKLQESAS MANRSRYQSR KVENMKATII QRLKRGCRLY
1960 1970 1980 1990 2000
LMSETPKVPT YRTTYPAPVY SPPINVRLSN PESAVAACNE FLARNYPTVS
2010 2020 2030 2040 2050
SYQITDEYDA YLDMVDGSES CLDRATFNPS KLRSYPKQHA YHAPSIRSAV
2060 2070 2080 2090 2100
PSPFQNTLQN VLAAATKRNC NVTQMRELPT LDSAVFNVEC FKKFACNQEY
2110 2120 2130 2140 2150
WEEFAASPIR ITTENLTTYV TKLKGPKAAA LFAKTHNLLP LQEVPMDRFT
2160 2170 2180 2190 2200
VDMKRDVKVT PGTKHTEERP KVQVIQAAEP LATAYLCGIH RELVRRLNAV
2210 2220 2230 2240 2250
LLPNVHTLFD MSAEDFDAII AAHFKPGDTV LETDIASFDK SQDDSLALTA
2260 2270 2280 2290 2300
LMLLEDLGVD HSLLDLIEAA FGEISSCHLP TGTRFKFGAM MKSGMFLTLF
2310 2320 2330 2340 2350
VNTLLNITIA SRVLEDRLTK SACAAFIGDD NIIHGVVSDE LMAARCATWM
2360 2370 2380 2390 2400
NMEVKIIDAV VSQKAPYFCG GFILHDIVTG TACRVADPLK RLFKLGKPLA
2410 2420 2430 2440 2450
AGDEQDEDRR RALADEVVRW QRTGLIDELE KAVYSRYEVQ GISVVVMSMA
2460 2470
TFASSRSNFE KLRGPVVTLY GGPK
Length:2,474
Mass (Da):275,652
Last modified:October 1, 2002 - 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:i97D250B9EB5A3BB0
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
AF369024 Genomic RNA Translation: AAN05101.1

NCBI Reference Sequences

More...
RefSeqi
NP_690588.1, NC_004162.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
956309

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
vg:956309

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
AF369024 Genomic RNA Translation: AAN05101.1
RefSeqiNP_690588.1, NC_004162.2

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
3GPGX-ray1.65A/B/C/D1334-1493[»]
3GPOX-ray1.90A/B/C/D1334-1493[»]
3GPQX-ray2.00A/B/C/D1334-1493[»]
3TRKX-ray2.40A1006-1326[»]
4TU0X-ray2.30A/B/C/D1334-1493[»]
5I22NMR-B1728-1744[»]
SMRiQ8JUX6
ModBaseiSearch...

Protein family/group databases

MEROPSiC09.001

Proteomic databases

PRIDEiQ8JUX6

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi956309
KEGGivg:956309

Miscellaneous databases

EvolutionaryTraceiQ8JUX6

Family and domain databases

InterProiView protein in InterPro
IPR027351 (+)RNA_virus_helicase_core_dom
IPR002588 Alphavirus-like_MT_dom
IPR002620 Alphavirus_nsp2pro
IPR002589 Macro_dom
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
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_CHIKS
<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: Q8JUX6
<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: March 21, 2006
Last sequence update: October 1, 2002
Last modified: September 18, 2019
This is version 115 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

<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, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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