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Entry version 159 (16 Oct 2019)
Sequence version 2 (21 Mar 2006)
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Protein

Polyprotein P1234

Gene
N/A
Organism
Semliki forest virus (SFV)
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.By similarity
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
Polyprotein P123': The early replication complex formed by the polyprotein P123' and nsP4 synthesizes minus-strand RNAs (Probable). Polyprotein P123' is a short-lived polyprotein that accumulates during early stage of infection (Probable). As soon P123' is cleaved into mature proteins, the plus-strand RNAs synthesis begins (Probable).Curated
mRNA-capping enzyme nsP1: Cytoplasmic capping enzyme that catalyzes two virus-specific reactions: methyltransferase and nsP1 guanylyltransferase (PubMed:7831320). mRNA-capping is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus (Probable). The enzymatic reaction involves a covalent link between 7-methyl-GMP and nsP1, whereas eukaryotic capping enzymes form a covalent complex only with GMP (Probable). nsP1 capping consists in the following reactions: GTP is first methylated into 7-methyl-GMP and then is covalently linked to nsP1 to form the m7GMp-nsP1 complex from which 7-methyl-GMP complex is transferred to the mRNA to create the cap structure (Probable). 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 (Probable). 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
Protease nsP2: Multifunctional protein whose N-terminus is part of the RNA polymerase complex and displays NTPase, RNA triphosphatase and helicase activities (PubMed:8057461, PubMed:10217401, PubMed:10748213). NTPase and RNA triphosphatase are involved in viral RNA capping and helicase keeps a check on the dsRNA replication intermediates (Probable). The C-terminus harbors a protease that specifically cleaves and releases the mature proteins (PubMed:11257180). Required for the shutoff of minus-strand RNAs synthesis (PubMed:16352561). Specifically inhibits the host IFN response by promoting the nuclear export of host STAT1 (By similarity). Also inhibits host transcription by inducing rapid proteasome-dependent degradation of POLR2A, a catalytic subunit of the RNAPII complex (PubMed:22514352, PubMed:17108023). The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (Probable).By similarity2 Publications7 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 (Probable). ADP-ribosylation is a post-translational modification that controls various processes of the host cell and the virus probably needs to revert it for optimal viral replication (Probable). Binds proteins of FXR family and sequesters them into the viral RNA replication complexes thereby inhibiting the formation of host stress granules on viral mRNAs (Probable). The nsp3'-FXR complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes, thanks to the ability of FXR family members to self-assemble and bind DNA (Probable).By similarityCurated
Non-structural protein 3: Seems to be essential for minus-strand RNAs and subgenomic 26S mRNAs synthesis (By similarity). Displays mono-ADP-ribosylhydrolase activity (By similarity). ADP-ribosylation is a post-translational modification that controls various processes of the host cell and the virus probably needs to revert it for optimal viral replication (By similarity). Binds proteins of G3BP family and sequesters them into the viral RNA replication complexes thereby inhibiting the formation of host stress granules on viral mRNAs (PubMed:23087212). 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:27383630).By similarity2 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 (PubMed:15930128, PubMed:16391235). This inactivates completely cellular translation initiation, resulting shutoff of host proteins synthesis (PubMed:16391235). 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 similarity2 Publications

Caution

There is no stop codon readthrough before nsP4 in the prototype strain sequence. The opal termination codon may have been mutated to a sense codon on passage in cell culture since the prototype strain SFV4 is derived from the L10 strain, which is a laboratory strain resulting from extensive passaging. Isolate Me Tri virus, which has clearly been identified as a Semliki virus isolate, has an opal codon instead of Arg-1812 further confirming the idea that the opal codon may have muted in many SFV strains (PubMed:18753222). In the isolates that have an opal codon, the genome codes for P123, but readthrough of a terminator codon UGA occurs between the codons for Leu-1811 and Leu-1813 giving rise to P1234. 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). 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 similarityCurated1 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 <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Protease Nsp2: Inhibited by N-ethylmaleimide, Zn2+, and Cu22+.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=2.99 mM for nsP2 RNA triphosphatase activity (at pH 8.0)1 Publication
  2. KM=90 mM for nsP2 NTPase activity (at pH 7.5)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>Sitei38Involved 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 sitei1015For cysteine protease nsP2 activityPROSITE-ProRule annotation1
    Active sitei1085For 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 sitei1346ADP-riboseBy similarity1
    Binding sitei1360ADP-riboseBy similarity1
    Binding sitei1368ADP-riboseBy similarity1
    Binding sitei1448ADP-riboseBy similarity1
    Binding sitei1449ADP-riboseBy similarity1
    Binding sitei1450ADP-riboseBy similarity1
    <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 bindingi1598ZincBy similarity1
    Metal bindingi1600ZincBy similarity1
    Metal bindingi1623ZincBy similarity1
    Metal bindingi1641ZincBy 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 bindingi723 – 730NTPPROSITE-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

    Enzyme and pathway databases

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P08411

    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 7 chains:
    Polyprotein P123'
    Short name:
    P123'
    Polyprotein P123
    Short name:
    P123
    mRNA-capping enzyme nsP1 (EC:2.1.1.-By similarity, EC:2.7.7.-By similarity)
    Alternative name(s):
    Non-structural protein 1
    Protease nsP2 (EC:3.1.3.331 Publication, EC:3.4.22.-By similarity, EC:3.6.1.151 Publication, EC:3.6.4.131 Publication)
    Alternative name(s):
    Non-structural protein 2
    Short name:
    nsP2
    Non-structural protein 3 (EC:3.1.3.84By similarity)
    Short name:
    nsP3
    Non-structural protein 3' (EC:3.1.3.84By similarity)
    Short name:
    nsP3'
    RNA-directed RNA polymerase nsP4 (EC:2.7.7.19By similarity, EC:2.7.7.48PROSITE-ProRule annotation)
    Alternative name(s):
    Non-structural protein 4
    Short name:
    nsP4
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_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>OrganismiSemliki forest virus (SFV)
    <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 identifieri11033 [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 [TaxID: 7158]
    Atelerix albiventris (Middle-African hedgehog) (Four-toed hedgehog) [TaxID: 9368]
    Culex tritaeniorhynchus (Mosquito) [TaxID: 7178]
    Halcyon [TaxID: 170865]
    Homo sapiens (Human) [TaxID: 9606]
    Quelea [TaxID: 158617]
    Rhipicephalus [TaxID: 34630]
    <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
    • UP000100607 <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
    • UP000125835 Componenti: Genome
    • UP000166518 Componenti: Genome
    • UP000174511 Componenti: Genome
    • UP000000570 Componenti: Genome
    • UP000136172 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' :
    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 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
    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 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
    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>Mutagenesisi19L → E: Complete loss of guanylyltransferase and guanine-7-methyl transferase activity in vitro. 1 Publication1
    Mutagenesisi38H → A: Complete loss of guanylyltransferase and guanine-7-methyl transferase activity in vitro. 1 Publication1
    Mutagenesisi64D → A: 60% increase of guanine-7-methyl transferase activity in vitro. Complete loss of guanylyltransferase activity in vitro. 1 Publication1
    Mutagenesisi81 – 83CVC → AVA: 60% loss of guanine-7-methyl transferase activity and complete loss of guanylyltransferase activity in vitro. 1 Publication3
    Mutagenesisi90D → A: Complete loss of guanylyltransferase and guanine-7-methyl transferase activity in vitro. 1 Publication1
    Mutagenesisi93R → A: Complete loss of guanylyltransferase and guanine-7-methyl transferase activity in vitro. 1 Publication1
    Mutagenesisi135C → A: 90% loss of guanine-7-methyl transferase activity and complete loss of guanylyltransferase activity in vitro. 1 Publication1
    Mutagenesisi142C → A: Complete loss of guanylyltransferase and guanine-7-methyl transferase activity in vitro. 1 Publication1
    Mutagenesisi153D → A: No effect on guanylyltransferase and guanine-7-methyl transferase activity in vitro. 1 Publication1
    Mutagenesisi169K → A: 50% loss of guanine-7-methyl transferase activity and no effect on guanylyltransferase activity in vitro. 1 Publication1
    Mutagenesisi180D → A: No effect on guanine-7-methyl transferase activity in vitro. 1 Publication1
    Mutagenesisi203E → A: No effect on guanylyltransferase and guanine-7-methyl transferase activity in vitro. 1 Publication1
    Mutagenesisi214C → A: 90% loss of guanylyltransferase and guanine-7-methyl transferase activity in vitro. 1 Publication1
    Mutagenesisi249Y → A: 97% loss of guanine-7-methyl transferase activity and complete loss of guanylyltransferase activity in vitro. 1 Publication1
    Mutagenesisi253R → A: Nsp1 accumulates in the cytoplasm and is poorly palmitoylated. 1 Publication1
    Mutagenesisi259W → A: Nsp1 accumulates in the cytoplasm and is poorly palmitoylated. 1 Publication1
    Mutagenesisi317K → A: 95% loss of guanine-7-methyl transferase activity and 98% loss of guanylyltransferase activity in vitro. 1 Publication1
    Mutagenesisi418 – 420CCC → AAA: Complete loss of palmitoylation. Complete loss of pathogenicity in mice. 2 Publications3
    Mutagenesisi729K → N: Complete loss of NTPase and helicase activity. 4 Publications1
    Mutagenesisi1015C → A: Complete loss of polyprotein processing. 1 Publication1
    Mutagenesisi1186R → D: Complete loss of nuclear localization for nsP2. 1 Publication1
    Mutagenesisi1680T → A: Complete loss of threonine phosphorylation. 1 Publication1
    Mutagenesisi1681T → A: Complete loss of threonine phosphorylation. 1 Publication1
    Mutagenesisi1786T → A: Weak interaction with host G3BP1. 1 Publication1
    Mutagenesisi1787F → A: Complete loss of interaction with host G3BP1. 1 Publication1
    Mutagenesisi1788G → A: Complete loss of interaction with host G3BP1. 1 Publication1
    Mutagenesisi1789D → A: Complete loss of interaction with host G3BP1. 1 Publication1
    Mutagenesisi1790F → A: Complete loss of interaction with host G3BP1. 1 Publication1
    Mutagenesisi1791D → A: No loss of interaction with host G3BP1. 1 Publication1
    Mutagenesisi1803T → A: Weak interaction with host G3BP1. 1 Publication1
    Mutagenesisi1804F → A: Complete loss of interaction with host G3BP1. 1 Publication1
    Mutagenesisi1805G → A: Complete loss of interaction with host G3BP1. 1 Publication1
    Mutagenesisi1806D → A: Complete loss of interaction with host G3BP1. 1 Publication1
    Mutagenesisi1807F → A: Complete loss of interaction with host G3BP1. 1 Publication1
    Mutagenesisi1808D → A: No loss of interaction with host G3BP1. 1 Publication1
    Mutagenesisi1824D → A: No effect on polyprotein processing. 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_00003084031 – 2432Polyprotein P1234Add BLAST2432
    ChainiPRO_00002277701 – 1818Polyprotein P123'Add BLAST1818
    ChainiPRO_00004466571 – 1811Polyprotein P123Add BLAST1811
    ChainiPRO_00000412281 – 537mRNA-capping enzyme nsP1Add BLAST537
    ChainiPRO_0000041229538 – 1336Protease nsP2Add BLAST799
    ChainiPRO_00000412301337 – 1818Non-structural protein 3'Add BLAST482
    ChainiPRO_00004466581337 – 1811Non-structural protein 3Add BLAST475
    ChainiPRO_00000412311819 – 2431RNA-directed RNA polymerase nsP4Add BLAST613

    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>Lipidationi418S-palmitoyl cysteine; by host2 Publications1
    Lipidationi420S-palmitoyl cysteine; by host2 Publications1
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1680Phosphothreonine; by host1 Publication1
    Modified residuei1681Phosphothreonine; 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:11257180, PubMed:12917405, PubMed:29695431). The processing of the polyprotein is temporally regulated (PubMed:12917405, PubMed:29695431). 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 (PubMed:12917405). At the same time, P1234 is also cut at the nsP1/nsP2 site early in infection but with lower efficiency (PubMed:12917405). 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 (PubMed:12917405). NsP3'/nsP4 site is not cleaved anymore and P34 is produced rather than nsP4 (By similarity).By similarity3 Publications
    Polyprotein P123': Specific enzymatic cleavages in vivo yield mature proteins (PubMed:11257180, PubMed:12917405, PubMed:29695431). The processing of the polyprotein is temporally regulated (PubMed:12917405, PubMed:29695431). In early stages (1.7 hpi), P123' is cleaved at the nsP1/nsP2 site with low efficiency (PubMed:12917405). 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 (PubMed:12917405).3 Publications
    Polyprotein P123: Specific enzymatic cleavages in vivo yield mature proteins (PubMed:11257180, PubMed:12917405, PubMed:29695431). The processing of the polyprotein is temporally regulated (PubMed:12917405, PubMed:29695431). In early stages (1.7 hpi), P123 is cleaved at the nsP1/nsP2 site with low efficiency (PubMed:12917405). 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 (PubMed:12917405).3 Publications
    mRNA-capping enzyme nsP1: Palmitoylated by host palmitoyltransferases ZDHHC2 and ZDHHC19.By similarity2 Publications
    Non-structural protein 3: Phosphorylated by host on serines and threonines.1 Publication
    Non-structural protein 3': Phosphorylated by host on serines and threonines.1 Publication
    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
    Sitei537 – 538Cleavage; by protease nsP2By similarity2
    Sitei1336 – 1337Cleavage; by protease nsP2By similarity2
    Sitei1818 – 1819Cleavage; by protease nsP2By similarity2

    Keywords - PTMi

    Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P08411

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P08411

    SwissPalm database of S-palmitoylation events

    More...
    SwissPalmi
    P08411

    <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 (By similarity). Non-structural protein 3:

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

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

    Interacts with mRNA-capping enzyme nsP1 (By similarity). RNA-directed RNA polymerase nsP4:

    Interacts with protease nsP2 (By similarity). Protease nsP2:

    Interacts with RNA-directed RNA polymerase nsP4 (By similarity). mRNA-capping enzyme nsP1:

    Interacts with protease nsP2 (By similarity). Protease nsP2:

    Interacts with mRNA-capping enzyme nsP1 (By similarity). RNA-directed RNA polymerase nsP4 interacts with itself (By similarity). mRNA-capping enzyme nsP1 interacts with itself (By similarity). 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:23087212, PubMed:25658430, PubMed:27383630). 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

    Protein-protein interaction databases

    The Eukaryotic Linear Motif resource for Functional Sites in Proteins

    More...
    ELMi
    P08411

    <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

    12432
    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
    P08411

    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
    P08411

    <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>Domaini29 – 260Alphavirus-like MTPROSITE-ProRule annotationAdd BLAST232
    Domaini692 – 844(+)RNA virus helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST153
    Domaini845 – 993(+)RNA virus helicase C-terminalPROSITE-ProRule annotationAdd BLAST149
    Domaini1006 – 1329Peptidase C9PROSITE-ProRule annotationAdd BLAST324
    Domaini1337 – 1495MacroPROSITE-ProRule annotationAdd BLAST159
    Domaini2182 – 2297RdRp 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>Regioni245 – 264NsP1 membrane-binding1 PublicationAdd BLAST20
    Regioni1007 – 1026Nucleolus localization signal1 PublicationAdd 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>Motifi1060 – 1069Nuclear export signalBy similarity10
    Motifi1184 – 1188Nuclear localization signal2 Publications5
    Motifi1787 – 1790FGDF; binding to host G3BP11 Publication1 Publication4
    Motifi1804 – 1807FGDF; binding to host G3BP11 Publication1 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 (By similarity). Contains a nuclear localization signal and a nuclear export signal, these two motifs are probably involved in the shuttling between the cytoplasm and the nucleus of nsP2 (By similarity). The C-terminus is required for promoting the export of host STAT1 (By similarity).By similarity
    Non-structural protein 3: In the N-terminus, the macro domain displays a mono-ADP-ribosylhydrolase activity (By similarity). The central part has a zinc-binding function (By similarity). The C-terminus contains two FGDF motifs necessary and sufficient for formation of the nsP3/G3BP1 complex (PubMed:24623412, PubMed:25658430, PubMed:27383630).By similarity3 Publications
    Non-structural protein 3': In the N-terminus, the macro domain displays a mono-ADP-ribosylhydrolase activity (By similarity). The central part has a zinc-binding function (By similarity). The C-terminus contains two FGDF motifs necessary and sufficient for formation of the nsP3'/G3BP1 complex (Probable).By similarity3 Publications

    Phylogenomic databases

    Database of Orthologous Groups

    More...
    OrthoDBi
    37at10239

    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.

    P08411-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MAAKVHVDIE ADSPFIKSLQ KAFPSFEVES LQVTPNDHAN ARAFSHLATK
    60 70 80 90 100
    LIEQETDKDT LILDIGSAPS RRMMSTHKYH CVCPMRSAED PERLVCYAKK
    110 120 130 140 150
    LAAASGKVLD REIAGKITDL QTVMATPDAE SPTFCLHTDV TCRTAAEVAV
    160 170 180 190 200
    YQDVYAVHAP TSLYHQAMKG VRTAYWIGFD TTPFMFDALA GAYPTYATNW
    210 220 230 240 250
    ADEQVLQARN IGLCAASLTE GRLGKLSILR KKQLKPCDTV MFSVGSTLYT
    260 270 280 290 300
    ESRKLLRSWH LPSVFHLKGK QSFTCRCDTI VSCEGYVVKK ITMCPGLYGK
    310 320 330 340 350
    TVGYAVTYHA EGFLVCKTTD TVKGERVSFP VCTYVPSTIC DQMTGILATD
    360 370 380 390 400
    VTPEDAQKLL VGLNQRIVVN GRTQRNTNTM KNYLLPIVAV AFSKWAREYK
    410 420 430 440 450
    ADLDDEKPLG VRERSLTCCC LWAFKTRKMH TMYKKPDTQT IVKVPSEFNS
    460 470 480 490 500
    FVIPSLWSTG LAIPVRSRIK MLLAKKTKRE LIPVLDASSA RDAEQEEKER
    510 520 530 540 550
    LEAELTREAL PPLVPIAPAE TGVVDVDVEE LEYHAGAGVV ETPRSALKVT
    560 570 580 590 600
    AQPNDVLLGN YVVLSPQTVL KSSKLAPVHP LAEQVKIITH NGRAGRYQVD
    610 620 630 640 650
    GYDGRVLLPC GSAIPVPEFQ ALSESATMVY NEREFVNRKL YHIAVHGPSL
    660 670 680 690 700
    NTDEENYEKV RAERTDAEYV FDVDKKCCVK REEASGLVLV GELTNPPFHE
    710 720 730 740 750
    FAYEGLKIRP SAPYKTTVVG VFGVPGSGKS AIIKSLVTKH DLVTSGKKEN
    760 770 780 790 800
    CQEIVNDVKK HRGLDIQAKT VDSILLNGCR RAVDILYVDE AFACHSGTLL
    810 820 830 840 850
    ALIALVKPRS KVVLCGDPKQ CGFFNMMQLK VNFNHNICTE VCHKSISRRC
    860 870 880 890 900
    TRPVTAIVST LHYGGKMRTT NPCNKPIIID TTGQTKPKPG DIVLTCFRGW
    910 920 930 940 950
    VKQLQLDYRG HEVMTAAASQ GLTRKGVYAV RQKVNENPLY APASEHVNVL
    960 970 980 990 1000
    LTRTEDRLVW KTLAGDPWIK VLSNIPQGNF TATLEEWQEE HDKIMKVIEG
    1010 1020 1030 1040 1050
    PAAPVDAFQN KANVCWAKSL VPVLDTAGIR LTAEEWSTII TAFKEDRAYS
    1060 1070 1080 1090 1100
    PVVALNEICT KYYGVDLDSG LFSAPKVSLY YENNHWDNRP GGRMYGFNAA
    1110 1120 1130 1140 1150
    TAARLEARHT FLKGQWHTGK QAVIAERKIQ PLSVLDNVIP INRRLPHALV
    1160 1170 1180 1190 1200
    AEYKTVKGSR VEWLVNKVRG YHVLLVSEYN LALPRRRVTW LSPLNVTGAD
    1210 1220 1230 1240 1250
    RCYDLSLGLP ADAGRFDLVF VNIHTEFRIH HYQQCVDHAM KLQMLGGDAL
    1260 1270 1280 1290 1300
    RLLKPGGSLL MRAYGYADKI SEAVVSSLSR KFSSARVLRP DCVTSNTEVF
    1310 1320 1330 1340 1350
    LLFSNFDNGK RPSTLHQMNT KLSAVYAGEA MHTAGCAPSY RVKRADIATC
    1360 1370 1380 1390 1400
    TEAAVVNAAN ARGTVGDGVC RAVAKKWPSA FKGAATPVGT IKTVMCGSYP
    1410 1420 1430 1440 1450
    VIHAVAPNFS ATTEAEGDRE LAAVYRAVAA EVNRLSLSSV AIPLLSTGVF
    1460 1470 1480 1490 1500
    SGGRDRLQQS LNHLFTAMDA TDADVTIYCR DKSWEKKIQE AIDMRTAVEL
    1510 1520 1530 1540 1550
    LNDDVELTTD LVRVHPDSSL VGRKGYSTTD GSLYSYFEGT KFNQAAIDMA
    1560 1570 1580 1590 1600
    EILTLWPRLQ EANEQICLYA LGETMDNIRS KCPVNDSDSS TPPRTVPCLC
    1610 1620 1630 1640 1650
    RYAMTAERIA RLRSHQVKSM VVCSSFPLPK YHVDGVQKVK CEKGLLFDPT
    1660 1670 1680 1690 1700
    VPSVVSPRKY AASTTDHSDR SLRGFDLDWT TDSSSTASDT MSLPSLQSCD
    1710 1720 1730 1740 1750
    IDSIYEPMAP IVVTADVHPE PAGIADLAAD VHPEPADHVD LENPIPPPRP
    1760 1770 1780 1790 1800
    KRAAYLASRA AERPVPAPRK PTPAPRTAFR NKLPLTFGDF DEHEVDALAS
    1810 1820 1830 1840 1850
    GITFGDFDDV LRLGRAGAYI FSSDTGSGHL QQKSVRQHNL QCAQLDAVEE
    1860 1870 1880 1890 1900
    EKMYPPKLDT EREKLLLLKM QMHPSEANKS RYQSRKVENM KATVVDRLTS
    1910 1920 1930 1940 1950
    GARLYTGADV GRIPTYAVRY PRPVYSPTVI ERFSSPDVAI AACNEYLSRN
    1960 1970 1980 1990 2000
    YPTVASYQIT DEYDAYLDMV DGSDSCLDRA TFCPAKLRCY PKHHAYHQPT
    2010 2020 2030 2040 2050
    VRSAVPSPFQ NTLQNVLAAA TKRNCNVTQM RELPTMDSAV FNVECFKRYA
    2060 2070 2080 2090 2100
    CSGEYWEEYA KQPIRITTEN ITTYVTKLKG PKAAALFAKT HNLVPLQEVP
    2110 2120 2130 2140 2150
    MDRFTVDMKR DVKVTPGTKH TEERPKVQVI QAAEPLATAY LCGIHRELVR
    2160 2170 2180 2190 2200
    RLNAVLRPNV HTLFDMSAED FDAIIASHFH PGDPVLETDI ASFDKSQDDS
    2210 2220 2230 2240 2250
    LALTGLMILE DLGVDQYLLD LIEAAFGEIS SCHLPTGTRF KFGAMMKSGM
    2260 2270 2280 2290 2300
    FLTLFINTVL NITIASRVLE QRLTDSACAA FIGDDNIVHG VISDKLMAER
    2310 2320 2330 2340 2350
    CASWVNMEVK IIDAVMGEKP PYFCGGFIVF DSVTQTACRV SDPLKRLFKL
    2360 2370 2380 2390 2400
    GKPLTAEDKQ DEDRRRALSD EVSKWFRTGL GAELEVALTS RYEVEGCKSI
    2410 2420 2430
    LIAMATLARD IKAFKKLRGP VIHLYGGPRL VR
    Length:2,432
    Mass (Da):269,512
    Last modified:March 21, 2006 - v2
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iBE7104A1EC3EF6EE
    GO

    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 conflicti1537F → L in ACB12687 (PubMed:18753222).Curated1
    Sequence conflicti1591T → S in ACB12687 (PubMed:18753222).Curated1
    Sequence conflicti1644G → V in ACB12687 (PubMed:18753222).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 varianti6H → Y in strain: Isolate L10. 1
    Natural varianti95 – 96VC → DS in strain: Isolate Garoff/Takkinen. 2
    Natural varianti119D → N in strain: Isolate Ts14. 1
    Natural varianti311E → K in strain: Isolate L10. 1
    Natural varianti427R → K in strain: Isolate Me Tri virus. 1 Publication1
    Natural varianti470K → E in strain: Isolate Me Tri virus. 1 Publication1
    Natural varianti482I → M in strain: Isolate Me Tri virus. 1 Publication1
    Natural varianti529E → D in strain: Isolate Ts10. 1
    Natural varianti596R → G in strain: Isolate Garoff/Takkinen. 1
    Natural varianti761H → Y in strain: Isolate Me Tri virus. 1 Publication1
    Natural varianti764 – 771LDIQAKTV → KGTSRENS in strain: Isolate Garoff/Takkinen. 8
    Natural varianti764 – 771LDIQAKTV → NWTSRKNS in strain: Isolate L10. 8
    Natural varianti817D → N in strain: Isolate L10. 1
    Natural varianti826M → T in strain: Isolate L10. 1
    Natural varianti843H → N in strain: Isolate L10. 1
    Natural varianti845S → N in strain: Isolate Ts1. 1
    Natural varianti859S → C in strain: Isolate L10. 1
    Natural varianti869T → S in strain: Isolate Ts13. 1
    Natural varianti901V → A in strain: Isolate Garoff/Takkinen. 1
    Natural varianti981T → M in strain: Isolate Me Tri virus. 1 Publication1
    Natural varianti1052V → E in strain: Isolate Me Tri virus. 1 Publication1
    Natural varianti1114G → R in strain: Isolate Ts11. 1
    Natural varianti1199A → T in strain: Isolate Ts6. 1
    Natural varianti1258 – 1259SL → I in strain: Isolate Garoff/Takkinen and Isolate L10. 2
    Natural varianti1384A → E in strain: Isolate L10 clone SFV4. 1
    Natural varianti1406A → G in strain: Isolate Me Tri virus. 1 Publication1
    Natural varianti1565Q → R in strain: Isolate Garoff/Takkinen. 1
    Natural varianti1579R → G in strain: Isolate Garoff/Takkinen. 1
    Natural varianti1644G → V in strain: Isolate Garoff/Takkinen, Isolate L10 and Isolate L10 clone SFV4. 1
    Natural varianti1849E → Q in strain: Isolate Garoff/Takkinen. 1
    Natural varianti1921P → R in strain: Isolate L10. 1
    Natural varianti1938V → A in strain: Isolate L10. 1
    Natural varianti2060A → V in strain: Isolate Ts13. 1
    Natural varianti2088A → D in strain: Isolate L10. 1
    Natural varianti2405A → T in strain: Isolate Garoff/Takkinen. 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
    X04129 Genomic RNA Translation: CAA27741.1
    AJ251359 Genomic RNA Translation: CAB62256.1
    AY112987 Genomic RNA Translation: AAM64226.1
    DQ189079 Genomic RNA Translation: ABA29023.1
    DQ189080 Genomic RNA Translation: ABA29024.1
    DQ189081 Genomic RNA Translation: ABA29025.1
    DQ189082 Genomic RNA Translation: ABA29026.1
    DQ189083 Genomic RNA Translation: ABA29028.1
    DQ189084 Genomic RNA Translation: ABA29029.1
    DQ189085 Genomic RNA Translation: ABA29031.1
    DQ189086 Genomic RNA Translation: ABA29032.1
    EU350586 Genomic RNA Translation: ACB12687.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A23592 MNWVSF

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_463457.1, NC_003215.1

    Genome annotation databases

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    922350

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    vg:922350

    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
    X04129 Genomic RNA Translation: CAA27741.1
    AJ251359 Genomic RNA Translation: CAB62256.1
    AY112987 Genomic RNA Translation: AAM64226.1
    DQ189079 Genomic RNA Translation: ABA29023.1
    DQ189080 Genomic RNA Translation: ABA29024.1
    DQ189081 Genomic RNA Translation: ABA29025.1
    DQ189082 Genomic RNA Translation: ABA29026.1
    DQ189083 Genomic RNA Translation: ABA29028.1
    DQ189084 Genomic RNA Translation: ABA29029.1
    DQ189085 Genomic RNA Translation: ABA29031.1
    DQ189086 Genomic RNA Translation: ABA29032.1
    EU350586 Genomic RNA Translation: ACB12687.1
    PIRiA23592 MNWVSF
    RefSeqiNP_463457.1, NC_003215.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1FW5NMR-A245-264[»]
    5DRVX-ray2.75B1785-1792[»]
    5FW5X-ray1.92C1785-1809[»]
    SMRiP08411
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    ELMiP08411

    Protein family/group databases

    MEROPSiC09.001

    PTM databases

    iPTMnetiP08411
    SwissPalmiP08411

    Proteomic databases

    PRIDEiP08411

    Genome annotation databases

    GeneIDi922350
    KEGGivg:922350

    Phylogenomic databases

    OrthoDBi37at10239

    Enzyme and pathway databases

    SABIO-RKiP08411

    Miscellaneous databases

    EvolutionaryTraceiP08411

    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_SFV
    <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: P08411
    Secondary accession number(s): B3TP00
    , Q3LRQ3, Q3LRQ4, Q3LRQ6, Q3LRQ7, Q3LRQ9, Q3LRR0, Q3LRR1, Q3LRR2, Q8JMP6, Q9QBM1
    <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: August 1, 1988
    Last sequence update: March 21, 2006
    Last modified: October 16, 2019
    This is version 159 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    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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