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UniProtKB - P27282 (POLN_EEVVT)

Entry version 157 (02 Jun 2021)
Sequence version 3 (10 Apr 2019)
Previous versions | rss
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Protein

Polyprotein P1234

Gene
N/A
Organism
Venezuelan equine encephalitis virus (strain Trinidad donkey) (VEEV)
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

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 the minus-strand RNAs (antigenome) (By similarity).

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 (By similarity).

By similarityCurated

The early replication complex formed by the polyprotein P123' and nsP4 synthesizes minus-strand RNAs (antigenome) (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 (PubMed:26041283).

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 (PubMed:26041283).

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).

Nsp1 is needed for the initiation of the minus-strand RNAs synthesis (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 similarityCurated1 Publication

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).

Inhibits host translation to ensure maximal viral gene expression and evade host immune response (PubMed:27318152).

By similarity1 Publication

Seems to be essential for minus-strand RNAs and subgenomic 26S mRNAs synthesis (By similarity).

Displays mono-ADP-ribosylhydrolase activity (PubMed:28150709, PubMed:27440879).

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:28150709).

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 (PubMed:27509095).

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 (PubMed:27509095).

By similarity3 Publications

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 similarity3 Publications

RNA dependent RNA polymerase (By similarity).

Replicates genomic and antigenomic RNA by recognizing replications specific signals. The early replication complex formed by the polyproteins P123/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 Gln-1879 and Arg-1881 giving rise to P1234 (By similarity). 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 similarity

<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:

<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

Inhibited by sinefungin.1 Publication

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

  1. KM=110 µM for a 12 residues substrate for nsp2 protease activity1 Publication

    pH dependencei

    Optimum pH is 7 for nsP1 guanylylation.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-GMP1 Publication1
    <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 sitei1012For cysteine protease nsP2 activityPROSITE-ProRule annotation1 Publication1
    Active sitei1081For cysteine protease nsP2 activityPROSITE-ProRule annotation1 Publication1
    <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 sitei1339ADP-riboseBy similarity1
    Binding sitei1353ADP-riboseBy similarity1
    Binding sitei1361ADP-riboseBy similarity1
    Binding sitei1441ADP-riboseBy similarity1
    Binding sitei1442ADP-riboseBy similarity1
    Binding sitei1443ADP-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 bindingi1596ZincBy similarity1
    Metal bindingi1598ZincBy similarity1
    Metal bindingi1621ZincBy similarity1
    Metal bindingi1639ZincBy 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

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		3.4.22.B79, 9640

    Protein family/group databases

    MEROPS protease database

    More...    MEROPSi    		S03.001

    <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%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.-1 Publication, EC:2.7.7.-1 Publication)
    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:3.1.3.841 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%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>OrganismiVenezuelan equine encephalitis virus (strain Trinidad donkey) (VEEV)
    <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 identifieri11038 [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 hostiBos taurus (Bovine) [TaxID: 9913]
    Didelphis marsupialis (Southern opossum) [TaxID: 9268]
    Equus asinus (Donkey) (Equus africanus asinus) [TaxID: 9793]
    Equus caballus (Horse) [TaxID: 9796]
    Homo sapiens (Human) [TaxID: 9606]
    Melanoconion [TaxID: 53535]
    Philander opossum (Gray four-eyed opossum) [TaxID: 9272]
    Proechimys [TaxID: 10162]
    Sigmodon hispidus (Hispid cotton rat) [TaxID: 42415]
    <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
    • UP000158519 <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
    • UP000100999 Componenti: Genome
    • UP000127220 Componenti: Genome
    • UP000146452 Componenti: Genome
    • UP000008659 Componenti: Genome
    • UP000131973 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 By similarity
    • Host nucleus 1 Publication
    • Host cytoplasm 1 Publication
      • Note: In the late phase of infection, the polyprotein is quickly cleaved before localization to cellular membranes. Then approximately half of nsP2 is found in the nucleus (By similarity). Shuttles between cytoplasm and nucleus (PubMed:17652399). NsP2 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 similarity1 Publication
    • 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 Curated; 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 (Probable).By similarityCurated

    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%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>Mutagenesisi37H → A: Complete loss of nsP1 guanylylation; increased methyltransferase activity. 1 Publication1
    Mutagenesisi45H → A: Almost no effect on nsP1 guanylylation; 50% loss of methyltransferase activity. 1 Publication1
    Mutagenesisi63D → A: Complete loss of nsP1 guanylylation; 80% loss of methyltransferase activity. 1 Publication1
    Mutagenesisi118E → A: Almost no effect on formation of nsP1 guanylylation. 1 Publication1
    Mutagenesisi285Y → A: 85% loss of formation of nsP1 guanylylation; 70% loss of methyltransferase activity. 1 Publication1
    Mutagenesisi354D → A: Increased formation of nsP1 guanylylation; slightly increased methyltransferase activity. 1 Publication1
    Mutagenesisi365R → A: Increased formation of nsP1 guanylylation; slightly increased methyltransferase activity. 1 Publication1
    Mutagenesisi369N → A: 50% loss of formation of nsP1 guanylylation; 50% loss of methyltransferase activity. 1 Publication1
    Mutagenesisi375N → A: 50% loss of formation of nsP1 guanylylation; 40% loss of methyltransferase activity. 1 Publication1
    Mutagenesisi538V → A: Increased viral replication and cytopathogenicity. 1 Publication1
    Mutagenesisi540T → A: Increased viral replication and cytopathogenicity. 1 Publication1
    Mutagenesisi1006Q → A: Increased viral replication and cytopathogenicity. 1 Publication1
    Mutagenesisi1010N → A: 24 fold reduced Kcat/Km for nsP2 protease activity. 1 Publication1
    Mutagenesisi1010N → A: NsP2 is in a self-inhibited state. 1 Publication1
    Mutagenesisi1015K → A: 9 fold reduced Kcat/Km for nsP2 protease activity. 1 Publication1
    Mutagenesisi1056V → A: No effect on nuclear export of nsP2. 1 Publication1
    Mutagenesisi1061L → A: Inhibits the nuclear export of nsP2; when associated with Ala-1063. 1 Publication1
    Mutagenesisi1063L → A: Inhibits the nuclear export of nsP2; when associated with Ala-1061. 1 Publication1
    Mutagenesisi1181K → D: Decreased protease nsP2 nuclear localization. 1 Publication1
    Mutagenesisi1197R → A or K: 16 fold reduced Kcat/Km for nsP2 protease activity. 1 Publication1
    Mutagenesisi1248P → S: No effect on host shutoff induction by nsP2 at 6h p.i. 1 Publication1
    Mutagenesisi1274Q → L: 50% loss of host shutoff induction by nsP2 at 6h p.i. 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003083911 – 2493Polyprotein P1234Add BLAST2493
    ChainiPRO_00002287701 – 1886Polyprotein P123'Add BLAST1886
    ChainiPRO_00002287711 – 1879Polyprotein P123Add BLAST1879
    ChainiPRO_00000412081 – 535mRNA-capping enzyme nsP1Add BLAST535
    ChainiPRO_0000041209536 – 1329Protease nsP2Add BLAST794
    ChainiPRO_00002287721330 – 1886Non-structural protein 3'Add BLAST557
    ChainiPRO_00000412101330 – 1879Non-structural protein 3Add BLAST550
    ChainiPRO_00000412111887 – 2493RNA-directed RNA polymerase nsP4Add BLAST607

    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>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
    Sitei1329 – 1330Cleavage; by protease nsP2By similarity2
    Sitei1886 – 1887Cleavage; by protease nsP2By similarity2

    Keywords - PTMi

    Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRoteomics IDEntifications database

    More...    PRIDEi    		P27282

    <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 (PubMed:27105836).

    Interacts with host DDX3 (PubMed:27105836).

    Interacts (via C-terminus) with host FXR1; this interaction inhibits the formation of host stress granules on viral mRNAs and the nsp3-FXR1 complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes (PubMed:27509095).

    Interacts (via C-terminus) with host FXR2; this interaction inhibits the formation of host stress granules on viral mRNAs and the nsp3-FXR2 complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes (PubMed:27509095).

    Interacts (via C-terminus) with host FMR1; this interaction inhibits the formation of host stress granules on viral mRNAs and the nsp3-FMR1 complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes (PubMed:27509095).

    By similarity2 Publications

    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 (PubMed:17652399).

    By similarity1 Publication

    <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

    12493
    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

    More...    SMRi    		P27282

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    Protein Data Bank in Europe - Knowledge Base

    More...    PDBe-KBi    		Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...    EvolutionaryTracei    		P27282

    <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 – 841(+)RNA virus helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST152
    Domaini842 – 990(+)RNA virus helicase C-terminalPROSITE-ProRule annotationAdd BLAST149
    Domaini1003 – 1322Peptidase C9PROSITE-ProRule annotation1 PublicationAdd BLAST320
    Domaini1330 – 1489MacroPROSITE-ProRule annotation1 PublicationAdd BLAST160
    <p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati1818 – 183911 PublicationAdd BLAST22
    Repeati1852 – 187321 PublicationAdd BLAST22
    Domaini2250 – 2365RdRp 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
    Regioni1004 – 1023Nucleolus localization signalBy similarityAdd BLAST20
    Regioni1660 – 1696DisorderedSequence analysisAdd BLAST37
    Regioni1791 – 1812DisorderedSequence analysisAdd BLAST22
    Regioni1818 – 18732 X 21 AA approximate repeats, binding to host FXR family members1 PublicationAdd BLAST56

    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>Motifi1056 – 1065Nuclear export signal1 Publication10
    Motifi1179 – 1183Nuclear localization signal1 Publication5

    Compositional bias

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1669 – 1684Polar residuesSequence analysisAdd BLAST16
    Compositional biasi1792 – 1806Pro residuesSequence analysisAdd BLAST15

    <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 (PubMed:17652399).By similarity1 Publication
    In the N-terminus, the macro domain displays a mono-ADP-ribosylhydrolase activity (PubMed:28150709, PubMed:27440879). The central part has a zinc-binding function (By similarity). The C-terminus contains two approximate repeats necessary and sufficient for formation of the nsP3/FXR complex (PubMed:27509095).By similarity3 Publications
    In the N-terminus, the macro domain displays a mono-ADP-ribosylhydrolase activity (Probable). The central part has a zinc-binding function (By similarity). The C-terminus contains two approximate repeats necessary and sufficient for formation of the nsP3'/FXR complex (Probable).By similarity3 Publications

    Keywords - Domaini

    Repeat

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd21557, Macro_X_Nsp3-like, 1 hit

    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
    IPR044371, Macro_X_NSP3-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.

    P27282-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MEKVHVDIEE DSPFLRALQR SFPQFEVEAK QVTDNDHANA RAFSHLASKL 
            60         70         80         90        100
    IETEVDPSDT ILDIGSAPAR RMYSKHKYHC ICPMRCAEDP DRLYKYATKL 
           110        120        130        140        150
    KKNCKEITDK ELDKKMKELA AVMSDPDLET ETMCLHDDES CRYEGQVAVY 
           160        170        180        190        200
    QDVYAVDGPT SLYHQANKGV RVAYWIGFDT TPFMFKNLAG AYPSYSTNWA 
           210        220        230        240        250
    DETVLTARNI GLCSSDVMER SRRGMSILRK KYLKPSNNVL FSVGSTIYHE 
           260        270        280        290        300
    KRDLLRSWHL PSVFHLRGKQ NYTCRCETIV SCDGYVVKRI AISPGLYGKP 
           310        320        330        340        350
    SGYAATMHRE GFLCCKVTDT LNGERVSFPV CTYVPATLCD QMTGILATDV 
           360        370        380        390        400
    SADDAQKLLV GLNQRIVVNG RTQRNTNTMK NYLLPVVAQA FARWAKEYKE 
           410        420        430        440        450
    DQEDERPLGL RDRQLVMGCC WAFRRHKITS IYKRPDTQTI IKVNSDFHSF 
           460        470        480        490        500
    VLPRIGSNTL EIGLRTRIRK MLEEHKEPSP LITAEDVQEA KCAADEAKEV 
           510        520        530        540        550
    REAEELRAAL PPLAADVEEP TLEADVDLML QEAGAGSVET PRGLIKVTSY 
           560        570        580        590        600
    AGEDKIGSYA VLSPQAVLKS EKLSCIHPLA EQVIVITHSG RKGRYAVEPY 
           610        620        630        640        650
    HGKVVVPEGH AIPVQDFQAL SESATIVYNE REFVNRYLHH IATHGGALNT 
           660        670        680        690        700
    DEEYYKTVKP SEHDGEYLYD IDRKQCVKKE LVTGLGLTGE LVDPPFHEFA 
           710        720        730        740        750
    YESLRTRPAA PYQVPTIGVY GVPGSGKSGI IKSAVTKKDL VVSAKKENCA 
           760        770        780        790        800
    EIIRDVKKMK GLDVNARTVD SVLLNGCKHP VETLYIDEAF ACHAGTLRAL 
           810        820        830        840        850
    IAIIRPKKAV LCGDPKQCGF FNMMCLKVHF NHEICTQVFH KSISRRCTKS 
           860        870        880        890        900
    VTSVVSTLFY DKKMRTTNPK ETKIVIDTTG STKPKQDDLI LTCFRGWVKQ 
           910        920        930        940        950
    LQIDYKGNEI MTAAASQGLT RKGVYAVRYK VNENPLYAPT SEHVNVLLTR 
           960        970        980        990       1000
    TEDRIVWKTL AGDPWIKTLT AKYPGNFTAT IEEWQAEHDA IMRHILERPD 
          1010       1020       1030       1040       1050
    PTDVFQNKAN VCWAKALVPV LKTAGIDMTT EQWNTVDYFE TDKAHSAEIV 
          1060       1070       1080       1090       1100
    LNQLCVRFFG LDLDSGLFSA PTVPLSIRNN HWDNSPSPNM YGLNKEVVRQ 
          1110       1120       1130       1140       1150
    LSRRYPQLPR AVATGRVYDM NTGTLRNYDP RINLVPVNRR LPHALVLHHN 
          1160       1170       1180       1190       1200
    EHPQSDFSSF VSKLKGRTVL VVGEKLSVPG KMVDWLSDRP EATFRARLDL 
          1210       1220       1230       1240       1250
    GIPGDVPKYD IIFVNVRTPY KYHHYQQCED HAIKLSMLTK KACLHLNPGG 
          1260       1270       1280       1290       1300
    TCVSIGYGYA DRASESIIGA IARQFKFSRV CKPKSSLEET EVLFVFIGYD 
          1310       1320       1330       1340       1350
    RKARTHNPYK LSSTLTNIYT GSRLHEAGCA PSYHVVRGDI ATATEGVIIN 
          1360       1370       1380       1390       1400
    AANSKGQPGG GVCGALYKKF PESFDLQPIE VGKARLVKGA AKHIIHAVGP 
          1410       1420       1430       1440       1450
    NFNKVSEVEG DKQLAEAYES IAKIVNDNNY KSVAIPLLST GIFSGNKDRL 
          1460       1470       1480       1490       1500
    TQSLNHLLTA LDTTDADVAI YCRDKKWEMT LKEAVARREA VEEICISDDS 
          1510       1520       1530       1540       1550
    SVTEPDAELV RVHPKSSLAG RKGYSTSDGK TFSYLEGTKF HQAAKDIAEI 
          1560       1570       1580       1590       1600
    NAMWPVATEA NEQVCMYILG ESMSSIRSKC PVEESEASTP PSTLPCLCIH 
          1610       1620       1630       1640       1650
    AMTPERVQRL KASRPEQITV CSSFPLPKYR ITGVQKIQCS QPILFSPKVP 
          1660       1670       1680       1690       1700
    AYIHPRKYLV ETPPVDETPE PSAENQSTEG TPEQPPLITE DETRTRTPEP 
          1710       1720       1730       1740       1750
    IIIEEEEEDS ISLLSDGPTH QVLQVEADIH GPPSVSSSSW SIPHASDFDV 
          1760       1770       1780       1790       1800
    DSLSILDTLE GASVTSGATS AETNSYFAKS MEFLARPVPA PRTVFRNPPH 
          1810       1820       1830       1840       1850
    PAPRTRTPSL APSRACSRTS LVSTPPGVNR VITREELEAL TPSRTPSRSV 
          1860       1870       1880       1890       1900
    SRTSLVSNPP GVNRVITREE FEAFVAQQQX RFDAGAYIFS SDTGQGHLQQ 
          1910       1920       1930       1940       1950
    KSVRQTVLSE VVLERTELEI SYAPRLDQEK EELLRKKLQL NPTPANRSRY 
          1960       1970       1980       1990       2000
    QSRKVENMKA ITARRILQGL GHYLKAEGKV ECYRTLHPVP LYSSSVNRAF 
          2010       2020       2030       2040       2050
    SSPKVAVEAC NAMLKENFPT VASYCIIPEY DAYLDMVDGA SCCLDTASFC 
          2060       2070       2080       2090       2100
    PAKLRSFPKK HSYLEPTIRS AVPSAIQNTL QNVLAAATKR NCNVTQMREL 
          2110       2120       2130       2140       2150
    PVLDSAAFNV ECFKKYACNN EYWETFKENP IRLTEENVVN YITKLKGPKA 
          2160       2170       2180       2190       2200
    AALFAKTHNL NMLQDIPMDR FVMDLKRDVK VTPGTKHTEE RPKVQVIQAA 
          2210       2220       2230       2240       2250
    DPLATAYLCG IHRELVRRLN AVLLPNIHTL FDMSAEDFDA IIAEHFQPGD 
          2260       2270       2280       2290       2300
    CVLETDIASF DKSEDDAMAL TALMILEDLG VDAELLTLIE AAFGEISSIH 
          2310       2320       2330       2340       2350
    LPTKTKFKFG AMMKSGMFLT LFVNTVINIV IASRVLRERL TGSPCAAFIG 
          2360       2370       2380       2390       2400
    DDNIVKGVKS DKLMADRCAT WLNMEVKIID AVVGEKAPYF CGGFILCDSV 
          2410       2420       2430       2440       2450
    TGTACRVADP LKRLFKLGKP LAADDEHDDD RRRALHEEST RWNRVGILSE 
          2460       2470       2480       2490 
    LCKAVESRYE TVGTSIIVMA MTTLASSVKS FSYLRGAPIT LYG
    Length:2,493
    Mass (Da):277,887
    Last modified:April 10, 2019 - v3
    <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:iC9FDF4AB76E242DC
    GO

    <p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence ALE15112 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti21S → T in AAB02518 (PubMed:2524126).Curated1
    Sequence conflicti497A → R in AAB02518 (PubMed:2524126).Curated1
    Sequence conflicti1589T → S in AAB02518 (PubMed:2524126).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti222R → C in strain: 71-180 and COAN5506. 1
    Natural varianti551A → D in strain: TC-83. 1

    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
    		J04332 Genomic RNA Translation: AAB02518.1
    L01442 Genomic RNA Translation: AAC19321.2
    L01443 Genomic RNA Translation: AAB02516.1
    AF069903 Genomic RNA Translation: AAC24033.1
    AY741139 Genomic RNA Translation: AAU89533.1
    KR260736 Genomic RNA Translation: ALE15112.1 Different initiation.

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		A31467, MNWVTD

    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
    		J04332 Genomic RNA Translation: AAB02518.1
    L01442 Genomic RNA Translation: AAC19321.2
    L01443 Genomic RNA Translation: AAB02516.1
    AF069903 Genomic RNA Translation: AAC24033.1
    AY741139 Genomic RNA Translation: AAU89533.1
    KR260736 Genomic RNA Translation: ALE15112.1 Different initiation.
    PIRiA31467, MNWVTD

    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
    2HWKX-ray2.45A1003-1322[»]
    5EZQX-ray1.66A992-1327[»]
    5EZSX-ray2.16A992-1327[»]
    6BCMX-ray2.10A1003-1338[»]
    SMRiP27282
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein family/group databases

    MEROPSiS03.001

    Proteomic databases

    PRIDEiP27282

    Enzyme and pathway databases

    BRENDAi3.4.22.B79, 9640

    Miscellaneous databases

    EvolutionaryTraceiP27282

    Family and domain databases

    CDDicd21557, Macro_X_Nsp3-like, 1 hit
    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
    IPR044371, Macro_X_NSP3-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

    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_EEVVT
    <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: P27282
    Secondary accession number(s): A0A0M3T9D8
    , O90163, Q5XQC5, Q66592, Q66594
    <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: August 1, 1992
    Last sequence update: April 10, 2019
    Last modified: June 2, 2021
    This is version 157 of the entry and version 3 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

    Documents

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