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    <accession>P03315</accession>
    <accession>B3TP01</accession>
    <accession>Q809B6</accession>
    <accession>Q8JMP5</accession>
    <name>POLS_SFV</name>
    <protein>
        <recommendedName>
            <fullName>Structural polyprotein</fullName>
        </recommendedName>
        <alternativeName>
            <fullName>p130</fullName>
        </alternativeName>
        <component>
            <recommendedName>
                <fullName>Capsid protein</fullName>
                <ecNumber evidence="26">3.4.21.90</ecNumber>
            </recommendedName>
            <alternativeName>
                <fullName>Coat protein</fullName>
                <shortName>C</shortName>
            </alternativeName>
        </component>
        <component>
            <recommendedName>
                <fullName>Precursor of protein E3/E2</fullName>
            </recommendedName>
            <alternativeName>
                <fullName>p62</fullName>
            </alternativeName>
            <alternativeName>
                <fullName>pE2</fullName>
            </alternativeName>
        </component>
        <component>
            <recommendedName>
                <fullName>Assembly protein E3</fullName>
            </recommendedName>
        </component>
        <component>
            <recommendedName>
                <fullName>Spike glycoprotein E2</fullName>
            </recommendedName>
            <alternativeName>
                <fullName>E2 envelope glycoprotein</fullName>
            </alternativeName>
        </component>
        <component>
            <recommendedName>
                <fullName>6K protein</fullName>
            </recommendedName>
        </component>
        <component>
            <recommendedName>
                <fullName>Spike glycoprotein E1</fullName>
            </recommendedName>
            <alternativeName>
                <fullName>E1 envelope glycoprotein</fullName>
            </alternativeName>
        </component>
    </protein>
    <organism>
        <name type="scientific">Semliki forest virus</name>
        <name type="common">SFV</name>
        <dbReference type="NCBI Taxonomy" id="11033"/>
        <lineage>
            <taxon>Viruses</taxon>
            <taxon>Riboviria</taxon>
            <taxon>Orthornavirae</taxon>
            <taxon>Kitrinoviricota</taxon>
            <taxon>Alsuviricetes</taxon>
            <taxon>Martellivirales</taxon>
            <taxon>Togaviridae</taxon>
            <taxon>Alphavirus</taxon>
        </lineage>
    </organism>
    <organismHost>
        <name type="scientific">Aedes</name>
        <dbReference type="NCBI Taxonomy" id="7158"/>
    </organismHost>
    <organismHost>
        <name type="scientific">Culex tritaeniorhynchus</name>
        <name type="common">Mosquito</name>
        <dbReference type="NCBI Taxonomy" id="7178"/>
    </organismHost>
    <organismHost>
        <name type="scientific">Atelerix albiventris</name>
        <name type="common">Middle-African hedgehog</name>
        <name type="synonym">Four-toed hedgehog</name>
        <dbReference type="NCBI Taxonomy" id="9368"/>
    </organismHost>
    <organismHost>
        <name type="scientific">Homo sapiens</name>
        <name type="common">Human</name>
        <dbReference type="NCBI Taxonomy" id="9606"/>
    </organismHost>
    <organismHost>
        <name type="scientific">Rhipicephalus</name>
        <dbReference type="NCBI Taxonomy" id="34630"/>
    </organismHost>
    <organismHost>
        <name type="scientific">Quelea</name>
        <dbReference type="NCBI Taxonomy" id="158617"/>
    </organismHost>
    <organismHost>
        <name type="scientific">Halcyon</name>
        <dbReference type="NCBI Taxonomy" id="170865"/>
    </organismHost>
    <reference key="1">
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            <authorList>
                <person name="Tarbatt C.J."/>
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        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC RNA]</scope>
        <source>
            <strain>A7</strain>
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    </reference>
    <reference key="2">
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        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC RNA]</scope>
        <source>
            <strain>MTV</strain>
        </source>
    </reference>
    <reference key="3">
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        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC RNA]</scope>
        <source>
            <strain>L10</strain>
        </source>
    </reference>
    <reference key="4">
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            <dbReference type="PubMed" id="6935652"/>
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        <scope>NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-305</scope>
    </reference>
    <reference key="5">
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            <authorList>
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        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 266-1253</scope>
    </reference>
    <reference key="6">
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            <authorList>
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            </authorList>
            <dbReference type="PubMed" id="6087344"/>
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        </citation>
        <scope>PROTEIN SEQUENCE OF 334-402 AND 816-881</scope>
    </reference>
    <reference key="7">
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            <authorList>
                <person name="Kalkkinen N."/>
            </authorList>
            <dbReference type="PubMed" id="7398872"/>
            <dbReference type="DOI" id="10.1016/0014-5793(80)81158-6"/>
        </citation>
        <scope>PARTIAL PROTEIN SEQUENCE</scope>
    </reference>
    <reference key="8">
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                <person name="Ulmanen I."/>
                <person name="Soederlund H."/>
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            </authorList>
            <dbReference type="PubMed" id="516447"/>
        </citation>
        <scope>FUNCTION (CAPSID PROTEIN)</scope>
    </reference>
    <reference key="9">
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            <authorList>
                <person name="Melancon P."/>
                <person name="Garoff H."/>
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        </citation>
        <scope>FUNCTION (CAPSID PROTEIN)</scope>
        <scope>AUTOCATALYTIC CLEAVAGE BY CAPSID PROTEIN</scope>
        <scope>MUTAGENESIS OF 219-SER-GLY-220</scope>
        <scope>CATALYTIC ACTIVITY (CAPSID PROTEIN)</scope>
        <scope>ACTIVE SITE (CAPSID PROTEIN)</scope>
        <scope>PROTEOLYTIC CLEAVAGE (STRUCTURAL POLYPROTEIN)</scope>
    </reference>
    <reference key="10">
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            <authorList>
                <person name="Schmidt M."/>
                <person name="Schmidt M.F."/>
                <person name="Rott R."/>
            </authorList>
            <dbReference type="PubMed" id="3143715"/>
        </citation>
        <scope>STEAROYLATION AT CYS-1248</scope>
        <scope>PALMITOYLATION</scope>
    </reference>
    <reference key="11">
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            <title>The cytoplasmic domain of alphavirus E2 glycoprotein contains a short linear recognition signal required for viral budding.</title>
            <authorList>
                <person name="Kail M."/>
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                <person name="Griffiths G."/>
                <person name="Vaux D."/>
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        </citation>
        <scope>FUNCTION (SPIKE GLYCOPROTEIN E2)</scope>
    </reference>
    <reference key="12">
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            <title>Processing of the p62 envelope precursor protein of Semliki Forest virus.</title>
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                <person name="Jain S.K."/>
                <person name="DeCandido S."/>
                <person name="Kielian M."/>
            </authorList>
            <dbReference type="PubMed" id="2005112"/>
        </citation>
        <scope>MUTAGENESIS OF ARG-330 AND ARG-333</scope>
        <scope>PROTEOLYTIC CLEAVAGE (PRECURSOR OF PROTEIN E3/E2)</scope>
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    <reference key="13">
        <citation type="journal article" date="1991" name="J. Virol." volume="65" first="4292" last="4300">
            <title>Mutagenesis of the putative fusion domain of the Semliki Forest virus spike protein.</title>
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                <person name="Levy-Mintz P."/>
                <person name="Kielian M."/>
            </authorList>
            <dbReference type="PubMed" id="2072453"/>
        </citation>
        <scope>MUTAGENESIS OF ASP-890; LYS-894; GLY-898; PRO-901; MET-903 AND GLY-906</scope>
    </reference>
    <reference key="14">
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            <title>Internally located cleavable signal sequences direct the formation of Semliki Forest virus membrane proteins from a polyprotein precursor.</title>
            <authorList>
                <person name="Liljestrom P."/>
                <person name="Garoff H."/>
            </authorList>
            <dbReference type="PubMed" id="1985194"/>
        </citation>
        <scope>CLEAVAGE BY SIGNAL PEPTIDASE</scope>
        <scope>MUTAGENESIS OF ALA-755 AND ALA-815</scope>
    </reference>
    <reference key="15">
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                <person name="Lusa S."/>
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            </authorList>
            <dbReference type="PubMed" id="1962454"/>
            <dbReference type="DOI" id="10.1016/0042-6822(91)90556-Q"/>
        </citation>
        <scope>FUNCTION (PROTEIN 6K)</scope>
    </reference>
    <reference key="16">
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                <person name="Wahlberg J.M."/>
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                <person name="Wilschut J."/>
                <person name="Garoff H."/>
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            <dbReference type="PubMed" id="1433520"/>
        </citation>
        <scope>FUNCTION (SPIKE GLYCOPROTEIN E1)</scope>
        <scope>SUBUNIT (SPIKE GLYCOPROTEIN E1)</scope>
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            <title>Role of ribosomes in Semliki Forest virus nucleocapsid uncoating.</title>
            <authorList>
                <person name="Singh I."/>
                <person name="Helenius A."/>
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            <dbReference type="PubMed" id="1433506"/>
        </citation>
        <scope>FUNCTION (CAPSID PROTEIN)</scope>
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            <authorList>
                <person name="Loewy A."/>
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                <person name="Liljestrom P."/>
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        <scope>FUNCTION (6K PROTEIN)</scope>
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                <person name="Vashishtha M."/>
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                <person name="Ryu J.S."/>
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        <scope>MUTAGENESIS OF GLY-898 AND GLY-906</scope>
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        <scope>FUNCTION (CAPSID PROTEIN)</scope>
        <scope>AUTOCATALYTIC CLEAVAGE (CAPSID PROTEIN)</scope>
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                <person name="Molinari M."/>
                <person name="Helenius A."/>
            </authorList>
            <dbReference type="PubMed" id="10573423"/>
            <dbReference type="DOI" id="10.1038/47062"/>
        </citation>
        <scope>INTERACTION WITH HUMAN CHAPERONE P4HB/PDI</scope>
        <scope>INTERACTION WITH HUMAN CHAPERONE PDIA3/ERP57</scope>
    </reference>
    <reference key="22">
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                <person name="Chatterjee P.K."/>
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            <dbReference type="PubMed" id="12438597"/>
            <dbReference type="DOI" id="10.1128/JVI.76.24.12712-12722.2002"/>
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        <scope>MUTAGENESIS OF LEU-859 AND VAL-993</scope>
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            <dbReference type="PubMed" id="12584323"/>
            <dbReference type="DOI" id="10.1128/JVI.77.5.2981-2989.2003"/>
        </citation>
        <scope>PROTEOLYTIC CLEAVAGE (STRUCTURAL POLYPROTEIN)</scope>
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        <scope>FUNCTION (CAPSID PROTEIN)</scope>
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            <dbReference type="PubMed" id="21430054"/>
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        <scope>FUNCTION (ASSEMBLY PROTEIN E3)</scope>
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        <scope>X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 816-1206</scope>
        <scope>GLYCOSYLATION AT ASN-956</scope>
        <scope>DISULFIDE BONDS</scope>
        <scope>SUBUNIT (SPIKE GLYCOPROTEIN E1)</scope>
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        <scope>FUNCTION (SPIKE GLYCOPROTEIN E1)</scope>
        <scope>INTERACTION WITH HOST VLDLR AND LRP8 (SPIKE GLYCOPROTEIN E1)</scope>
        <scope>FUNCTION (SPIKE GLYCOPROTEIN E2)</scope>
        <scope>INTERACTION WITH HOST VLDLR AND LRP8 (SPIKE GLYCOPROTEIN E2)</scope>
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            <dbReference type="PubMed" id="23864626"/>
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        <scope>FUNCTION (ASSEMBLY PROTEIN E3)</scope>
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        <scope>X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 119-267</scope>
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        <scope>STRUCTURE BY ELECTRON MICROSCOPY (9.0 ANGSTROMS) OF 119-267</scope>
        <scope>DISULFIDE BONDS</scope>
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    <reference key="31">
        <citation type="journal article" date="2001" name="Cell" volume="105" first="137" last="148">
            <title>The Fusion glycoprotein shell of Semliki Forest virus: an icosahedral assembly primed for fusogenic activation at endosomal pH.</title>
            <authorList>
                <person name="Lescar J."/>
                <person name="Roussel A."/>
                <person name="Wien M.W."/>
                <person name="Navaza J."/>
                <person name="Fuller S.D."/>
                <person name="Wengler G."/>
                <person name="Wengler G."/>
                <person name="Rey F.A."/>
            </authorList>
            <dbReference type="PubMed" id="11301009"/>
            <dbReference type="DOI" id="10.1016/S0092-8674(01)00303-8"/>
        </citation>
        <scope>X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 816-1205</scope>
    </reference>
    <comment type="function">
        <molecule>Capsid protein</molecule>
        <text evidence="2 5 13 16 26 27 31">Forms an icosahedral capsid with a T=4 symmetry composed of 240 copies of the capsid protein surrounded by a lipid membrane through which penetrate 80 spikes composed of trimers of E1-E2 heterodimers (By similarity). The capsid protein binds to the viral RNA genome at a site adjacent to a ribosome binding site for viral genome translation following genome release (By similarity). Possesses a protease activity that results in its autocatalytic cleavage from the nascent structural protein (PubMed:3553612, PubMed:9642067). Following its self-cleavage, the capsid protein transiently associates with ribosomes, and within several minutes the protein binds to viral RNA and rapidly assembles into icosahedric core particles (PubMed:516447). The resulting nucleocapsid eventually associates with the cytoplasmic domain of the spike glycoprotein E2 at the cell membrane, leading to budding and formation of mature virions (By similarity). In case of infection, new virions attach to target cells and after clathrin-mediated endocytosis their membrane fuses with the host endosomal membrane (PubMed:15954801). This leads to the release of the nucleocapsid into the cytoplasm, followed by an uncoating event necessary for the genomic RNA to become accessible (PubMed:1433506). The uncoating might be triggered by the interaction of capsid proteins with ribosomes (PubMed:1433506). Binding of ribosomes would release the genomic RNA since the same region is genomic RNA-binding and ribosome-binding (PubMed:1433506). Specifically inhibits interleukin-1 receptor-associated kinase 1/IRAK1-dependent signaling during viral entry, representing a means by which the alphaviruses may evade innate immune detection and activation prior to viral gene expression.</text>
    </comment>
    <comment type="function">
        <molecule>Assembly protein E3</molecule>
        <text evidence="22 23">Provides the signal sequence for the translocation of the precursor of protein E3/E2 to the host endoplasmic reticulum. Furin-cleaved E3 remains associated with spike glycoprotein E1 and mediates pH protection of the latter during the transport via the secretory pathway. After virion release from the host cell, the assembly protein E3 is gradually released in the extracellular space.</text>
    </comment>
    <comment type="function">
        <molecule>Spike glycoprotein E2</molecule>
        <text evidence="17">Plays a role in viral attachment to target host cell, by binding to the cell receptors VLDLR or LRP8 (PubMed:34929721). Synthesized as a p62 precursor which is processed by furin at the cell membrane just before virion budding, giving rise to E2-E1 heterodimer. The p62-E1 heterodimer is stable, whereas E2-E1 is unstable and dissociate at low pH. p62 is processed at the last step, presumably to avoid E1 fusion activation before its final export to cell surface. E2 C-terminus contains a transitory transmembrane that would be disrupted by palmitoylation, resulting in reorientation of the C-terminal tail from lumenal to cytoplasmic side. This step is critical since E2 C-terminus is involved in budding by interacting with capsid proteins. This release of E2 C-terminus in cytoplasm occurs lately in protein export, and precludes premature assembly of particles at the endoplasmic reticulum membrane.</text>
    </comment>
    <comment type="function">
        <molecule>6K protein</molecule>
        <text evidence="18 29">Constitutive membrane protein involved in virus glycoprotein processing, cell permeabilization, and the budding of viral particles. Disrupts the calcium homeostasis of the cell, probably at the endoplasmic reticulum level. This leads to cytoplasmic calcium elevation. Because of its lipophilic properties, the 6K protein is postulated to influence the selection of lipids that interact with the transmembrane domains of the glycoproteins, which, in turn, affects the deformability of the bilayer required for the extreme curvature that occurs as budding proceeds. Present in low amount in virions, about 3% compared to viral glycoproteins.</text>
    </comment>
    <comment type="function">
        <molecule>Spike glycoprotein E1</molecule>
        <text evidence="14 25">Class II viral fusion protein. Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to target cell via host VLDLR or LRP8 and endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits (PubMed:34929721). This E1 trimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion. Efficient fusion requires the presence of cholesterol and sphingolipid in the target membrane. Fusion is optimal at levels of about 1 molecule of cholesterol per 2 molecules of phospholipids, and is specific for sterols containing a 3-beta-hydroxyl group.</text>
    </comment>
    <comment type="catalytic activity">
        <reaction evidence="26">
            <text>Autocatalytic release of the core protein from the N-terminus of the togavirus structural polyprotein by hydrolysis of a -Trp-|-Ser- bond.</text>
            <dbReference type="EC" id="3.4.21.90"/>
        </reaction>
    </comment>
    <comment type="subunit">
        <molecule>Capsid protein</molecule>
        <text evidence="2 4 7 32">Homodimer (By similarity). Homomultimer (Probable). Interacts with host karyopherin KPNA4; this interaction allows the nuclear import of the viral capsid protein (By similarity). Interacts with spike glycoprotein E2 (By similarity). Interacts with host IRAK1; the interaction leads to inhibition of IRAK1-dependent signaling.</text>
    </comment>
    <comment type="subunit">
        <molecule>Precursor of protein E3/E2</molecule>
        <text evidence="2 4 7">The precursor of protein E3/E2 and E1 form a heterodimer shortly after synthesis.</text>
    </comment>
    <comment type="subunit">
        <molecule>Spike glycoprotein E1</molecule>
        <text evidence="2 4 7 25">The precursor of protein E3/E2 and E1 form a heterodimer shortly after synthesis (By similarity). Processing of the precursor of protein E3/E2 into E2 and E3 results in a heterodimer of the spike glycoproteins E2 and E1 (By similarity). Spike at virion surface are constituted of three E2-E1 heterodimers (By similarity). E2-E1 heterodimers interact with host VLDLR or LRP8 to mediate viral entry (PubMed:34929721).After target cell attachment and endocytosis, E1 change conformation to form homotrimers (PubMed:1433520, PubMed:14737160). Interacts with 6K protein.</text>
    </comment>
    <comment type="subunit">
        <molecule>Spike glycoprotein E2</molecule>
        <text evidence="2 4 7">Processing of the precursor of protein E3/E2 into E2 and E3 results in a heterodimer of the spike glycoproteins E2 and E1 (By similarity). Spike at virion surface are constituted of three E2-E1 heterodimers (By similarity). E2-E1 heterodimers interact with host VLDLR or LRP8 to mediate viral entry (PubMed:34929721). Interacts with 6K protein.</text>
    </comment>
    <comment type="subunit">
        <molecule>6K protein</molecule>
        <text evidence="2 4 7">Interacts with spike glycoprotein E1 (By similarity). Interacts with spike glycoprotein E2.</text>
    </comment>
    <comment type="subcellular location">
        <molecule>Capsid protein</molecule>
        <subcellularLocation>
            <location evidence="2">Virion</location>
        </subcellularLocation>
        <subcellularLocation>
            <location evidence="7">Host cytoplasm</location>
        </subcellularLocation>
        <subcellularLocation>
            <location evidence="2">Host cell membrane</location>
        </subcellularLocation>
        <subcellularLocation>
            <location evidence="7">Host nucleus</location>
        </subcellularLocation>
        <text evidence="7">Shuttles between the cytoplasm and the nucleus.</text>
    </comment>
    <comment type="subcellular location">
        <molecule>Spike glycoprotein E2</molecule>
        <subcellularLocation>
            <location evidence="7">Virion membrane</location>
            <topology evidence="8">Single-pass type I membrane protein</topology>
        </subcellularLocation>
        <subcellularLocation>
            <location evidence="2">Host cell membrane</location>
            <topology evidence="7">Single-pass type I membrane protein</topology>
        </subcellularLocation>
    </comment>
    <comment type="subcellular location">
        <molecule>6K protein</molecule>
        <subcellularLocation>
            <location evidence="2">Host cell membrane</location>
            <topology evidence="8">Multi-pass membrane protein</topology>
        </subcellularLocation>
        <subcellularLocation>
            <location evidence="2">Virion membrane</location>
            <topology evidence="8">Multi-pass membrane protein</topology>
        </subcellularLocation>
    </comment>
    <comment type="subcellular location">
        <molecule>Spike glycoprotein E1</molecule>
        <subcellularLocation>
            <location evidence="7">Virion membrane</location>
            <topology evidence="8">Single-pass type I membrane protein</topology>
        </subcellularLocation>
        <subcellularLocation>
            <location evidence="2 7">Host cell membrane</location>
            <topology evidence="8">Single-pass type I membrane protein</topology>
        </subcellularLocation>
    </comment>
    <comment type="alternative products">
        <event type="ribosomal frameshifting"/>
        <isoform>
            <id>P03315-1</id>
            <name>Structural polyprotein</name>
            <sequence type="displayed"/>
        </isoform>
        <isoform>
            <id>P0DJZ6-1</id>
            <name>Frameshifted structural polyprotein</name>
            <sequence type="external"/>
        </isoform>
    </comment>
    <comment type="domain">
        <molecule>Capsid protein</molecule>
        <text evidence="2 7">The N-terminus contains a nuclear localization signal and a CRM1-mediated nuclear export signal (By similarity). The C-terminus functions as a protease during translation to cleave itself from the translating structural polyprotein.</text>
    </comment>
    <comment type="PTM">
        <molecule>Isoform Structural polyprotein</molecule>
        <text evidence="12 19 20 26 31">Specific enzymatic cleavages in vivo yield mature proteins. Capsid protein is auto-cleaved during polyprotein translation, unmasking a signal peptide at the N-terminus of the precursor of E3/E2 (PubMed:3553612). The remaining polyprotein is then targeted to the host endoplasmic reticulum, where host signal peptidase cleaves it into pE2, 6K and E1 proteins. pE2 is further processed to mature E3 and E2 by host furin in trans-Golgi vesicle (PubMed:12584323). Protein processing process takes about 30 minutes at physiologic temperatures. The folding of the p62/6K/E1 precursor requires the formation of intrachain disulfide bonds and has been shown to involve a transient covalent interaction between the nascent and newly synthesized heterodimer and the host-cell chaperones, P4HB/PDI and PDIA3/ERp57. The folding pathway also includes non covalent interaction with human CANX/calnexin and CALR/calreticulin.</text>
    </comment>
    <comment type="PTM">
        <molecule>Spike glycoprotein E2</molecule>
        <text evidence="24">Palmitoylated via thioester bonds. These palmitoylations may induce disruption of the C-terminus transmembrane. This would result in the reorientation of E2 C-terminus from lumenal to cytoplasmic side.</text>
    </comment>
    <comment type="PTM">
        <text evidence="15">Envelope E1, E2 and E3 proteins are N-glycosylated.</text>
    </comment>
    <comment type="PTM">
        <molecule>Spike glycoprotein E1</molecule>
        <text evidence="24">Stearoylated.</text>
    </comment>
    <comment type="PTM">
        <molecule>6K protein</molecule>
        <text evidence="24">Palmitoylated via thioester bonds with about four covalently bound fatty acids per molecule.</text>
    </comment>
    <comment type="miscellaneous">
        <text>The mature virion nucleocapsid consists of 240 copies of the capsid protein. 80 spike trimers of E1 and E2 are present at the surface of mature virion. They project about 100 Angstroms from the outer surface and are located at the local and strict three fold axis of the icosahedral lattice. The glycoproteins splay out to form a protein shell or skirt covering most of the outer surface of the membrane bilayer.</text>
    </comment>
    <comment type="miscellaneous">
        <molecule>Isoform Structural polyprotein</molecule>
        <text>Translated from a subgenomic RNA synthesized during togavirus replication.</text>
    </comment>
    <comment type="miscellaneous">
        <molecule>Isoform Structural polyprotein</molecule>
        <text>Produced by conventional translation.</text>
    </comment>
    <comment type="online information" name="Virus Particle ExploreR db">
        <link uri="https://viperdb.scripps.edu/Info_Page.php?VDB=1dwn"/>
        <text>Icosahedral capsid structure</text>
    </comment>
    <dbReference type="EC" id="3.4.21.90" evidence="26"/>
    <dbReference type="EMBL" id="Z48163">
        <property type="protein sequence ID" value="CAD90834.1"/>
        <property type="molecule type" value="Genomic_RNA"/>
    </dbReference>
    <dbReference type="EMBL" id="EU350586">
        <property type="protein sequence ID" value="ACB12688.1"/>
        <property type="molecule type" value="Genomic_RNA"/>
    </dbReference>
    <dbReference type="EMBL" id="AY112987">
        <property type="protein sequence ID" value="AAM64227.1"/>
        <property type="molecule type" value="Genomic_RNA"/>
    </dbReference>
    <dbReference type="EMBL" id="X04129">
        <property type="protein sequence ID" value="CAA27742.1"/>
        <property type="molecule type" value="Genomic_RNA"/>
    </dbReference>
    <dbReference type="PIR" id="A93861">
        <property type="entry name" value="VHWV"/>
    </dbReference>
    <dbReference type="PIR" id="S42462">
        <property type="entry name" value="S42462"/>
    </dbReference>
    <dbReference type="RefSeq" id="NP_463458.1">
        <molecule id="P03315-1"/>
        <property type="nucleotide sequence ID" value="NC_003215.1"/>
    </dbReference>
    <dbReference type="PDB" id="1DYL">
        <property type="method" value="EM"/>
        <property type="resolution" value="9.00 A"/>
        <property type="chains" value="A/B/C/D=119-267"/>
    </dbReference>
    <dbReference type="PDB" id="1I9W">
        <property type="method" value="X-ray"/>
        <property type="resolution" value="3.00 A"/>
        <property type="chains" value="A=816-1205"/>
    </dbReference>
    <dbReference type="PDB" id="1RER">
        <property type="method" value="X-ray"/>
        <property type="resolution" value="3.20 A"/>
        <property type="chains" value="A/B/C=816-1206"/>
    </dbReference>
    <dbReference type="PDB" id="1VCP">
        <property type="method" value="X-ray"/>
        <property type="resolution" value="3.00 A"/>
        <property type="chains" value="A/B/C=119-267"/>
    </dbReference>
    <dbReference type="PDB" id="1VCQ">
        <property type="method" value="X-ray"/>
        <property type="resolution" value="3.10 A"/>
        <property type="chains" value="A/B=119-267"/>
    </dbReference>
    <dbReference type="PDB" id="2ALA">
        <property type="method" value="X-ray"/>
        <property type="resolution" value="3.00 A"/>
        <property type="chains" value="A=816-1206"/>
    </dbReference>
    <dbReference type="PDB" id="2V33">
        <property type="method" value="X-ray"/>
        <property type="resolution" value="1.55 A"/>
        <property type="chains" value="A/B=1107-1197"/>
    </dbReference>
    <dbReference type="PDBsum" id="1DYL"/>
    <dbReference type="PDBsum" id="1I9W"/>
    <dbReference type="PDBsum" id="1RER"/>
    <dbReference type="PDBsum" id="1VCP"/>
    <dbReference type="PDBsum" id="1VCQ"/>
    <dbReference type="PDBsum" id="2ALA"/>
    <dbReference type="PDBsum" id="2V33"/>
    <dbReference type="SMR" id="P03315"/>
    <dbReference type="MEROPS" id="C09.001"/>
    <dbReference type="MEROPS" id="S03.001"/>
    <dbReference type="TCDB" id="1.G.4.1.1">
        <property type="family name" value="the viral pore-forming membrane fusion protein-4 (vmfp4) family"/>
    </dbReference>
    <dbReference type="GlyConnect" id="575">
        <property type="glycosylation" value="2 N-Linked glycans"/>
    </dbReference>
    <dbReference type="GlyConnect" id="576">
        <property type="glycosylation" value="2 N-Linked glycans"/>
    </dbReference>
    <dbReference type="GlyConnect" id="577">
        <property type="glycosylation" value="1 N-Linked glycan"/>
    </dbReference>
    <dbReference type="iPTMnet" id="P03315"/>
    <dbReference type="SwissPalm" id="P03315"/>
    <dbReference type="GeneID" id="922351"/>
    <dbReference type="KEGG" id="vg:922351"/>
    <dbReference type="EvolutionaryTrace" id="P03315"/>
    <dbReference type="Proteomes" id="UP000000570">
        <property type="component" value="Genome"/>
    </dbReference>
    <dbReference type="Proteomes" id="UP000108382">
        <property type="component" value="Genome"/>
    </dbReference>
    <dbReference type="Proteomes" id="UP000125835">
        <property type="component" value="Genome"/>
    </dbReference>
    <dbReference type="Proteomes" id="UP000174511">
        <property type="component" value="Genome"/>
    </dbReference>
    <dbReference type="GO" id="GO:0044174">
        <property type="term" value="C:host cell endosome"/>
        <property type="evidence" value="ECO:0000314"/>
        <property type="project" value="CACAO"/>
    </dbReference>
    <dbReference type="GO" id="GO:0042025">
        <property type="term" value="C:host cell nucleus"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-SubCell"/>
    </dbReference>
    <dbReference type="GO" id="GO:0020002">
        <property type="term" value="C:host cell plasma membrane"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-SubCell"/>
    </dbReference>
    <dbReference type="GO" id="GO:0016021">
        <property type="term" value="C:integral component of membrane"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-KW"/>
    </dbReference>
    <dbReference type="GO" id="GO:0039619">
        <property type="term" value="C:T=4 icosahedral viral capsid"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-KW"/>
    </dbReference>
    <dbReference type="GO" id="GO:0019031">
        <property type="term" value="C:viral envelope"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-KW"/>
    </dbReference>
    <dbReference type="GO" id="GO:0055036">
        <property type="term" value="C:virion membrane"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-SubCell"/>
    </dbReference>
    <dbReference type="GO" id="GO:0003723">
        <property type="term" value="F:RNA binding"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-KW"/>
    </dbReference>
    <dbReference type="GO" id="GO:0004252">
        <property type="term" value="F:serine-type endopeptidase activity"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="InterPro"/>
    </dbReference>
    <dbReference type="GO" id="GO:0005198">
        <property type="term" value="F:structural molecule activity"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="InterPro"/>
    </dbReference>
    <dbReference type="GO" id="GO:0075512">
        <property type="term" value="P:clathrin-dependent endocytosis of virus by host cell"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-KW"/>
    </dbReference>
    <dbReference type="GO" id="GO:0039654">
        <property type="term" value="P:fusion of virus membrane with host endosome membrane"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-KW"/>
    </dbReference>
    <dbReference type="GO" id="GO:0006508">
        <property type="term" value="P:proteolysis"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-KW"/>
    </dbReference>
    <dbReference type="GO" id="GO:0039722">
        <property type="term" value="P:suppression by virus of host toll-like receptor signaling pathway"/>
        <property type="evidence" value="ECO:0000250"/>
        <property type="project" value="UniProtKB"/>
    </dbReference>
    <dbReference type="GO" id="GO:0019068">
        <property type="term" value="P:virion assembly"/>
        <property type="evidence" value="ECO:0000315"/>
        <property type="project" value="CACAO"/>
    </dbReference>
    <dbReference type="GO" id="GO:0019062">
        <property type="term" value="P:virion attachment to host cell"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-KW"/>
    </dbReference>
    <dbReference type="DisProt" id="DP00999"/>
    <dbReference type="Gene3D" id="2.40.10.10">
        <property type="match status" value="2"/>
    </dbReference>
    <dbReference type="Gene3D" id="2.60.40.2400">
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="Gene3D" id="2.60.40.3200">
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="Gene3D" id="2.60.40.350">
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="Gene3D" id="2.60.40.4310">
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="Gene3D" id="2.60.98.10">
        <property type="match status" value="3"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR002548">
        <property type="entry name" value="Alpha_E1_glycop"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR000936">
        <property type="entry name" value="Alpha_E2_glycop"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR002533">
        <property type="entry name" value="Alpha_E3_glycop"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR042304">
        <property type="entry name" value="Alphavir_E2_A"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR042305">
        <property type="entry name" value="Alphavir_E2_B"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR042306">
        <property type="entry name" value="Alphavir_E2_C"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR000336">
        <property type="entry name" value="Flavivir/Alphavir_Ig-like_sf"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR036253">
        <property type="entry name" value="Glycoprot_cen/dimer_sf"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR038055">
        <property type="entry name" value="Glycoprot_E_dimer_dom"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR014756">
        <property type="entry name" value="Ig_E-set"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR009003">
        <property type="entry name" value="Peptidase_S1_PA"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR043504">
        <property type="entry name" value="Peptidase_S1_PA_chymotrypsin"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR000930">
        <property type="entry name" value="Peptidase_S3"/>
    </dbReference>
    <dbReference type="Pfam" id="PF01589">
        <property type="entry name" value="Alpha_E1_glycop"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="Pfam" id="PF00943">
        <property type="entry name" value="Alpha_E2_glycop"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="Pfam" id="PF01563">
        <property type="entry name" value="Alpha_E3_glycop"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="Pfam" id="PF00944">
        <property type="entry name" value="Peptidase_S3"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="PRINTS" id="PR00798">
        <property type="entry name" value="TOGAVIRIN"/>
    </dbReference>
    <dbReference type="SUPFAM" id="SSF50494">
        <property type="entry name" value="SSF50494"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="SUPFAM" id="SSF56983">
        <property type="entry name" value="SSF56983"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="SUPFAM" id="SSF81296">
        <property type="entry name" value="SSF81296"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="PROSITE" id="PS51690">
        <property type="entry name" value="ALPHAVIRUS_CP"/>
        <property type="match status" value="1"/>
    </dbReference>
    <proteinExistence type="evidence at protein level"/>
    <keyword id="KW-0002">3D-structure</keyword>
    <keyword id="KW-0068">Autocatalytic cleavage</keyword>
    <keyword id="KW-0167">Capsid protein</keyword>
    <keyword id="KW-1165">Clathrin-mediated endocytosis of virus by host</keyword>
    <keyword id="KW-0165">Cleavage on pair of basic residues</keyword>
    <keyword id="KW-0903">Direct protein sequencing</keyword>
    <keyword id="KW-1015">Disulfide bond</keyword>
    <keyword id="KW-1170">Fusion of virus membrane with host endosomal membrane</keyword>
    <keyword id="KW-1168">Fusion of virus membrane with host membrane</keyword>
    <keyword id="KW-0325">Glycoprotein</keyword>
    <keyword id="KW-1032">Host cell membrane</keyword>
    <keyword id="KW-1035">Host cytoplasm</keyword>
    <keyword id="KW-1043">Host membrane</keyword>
    <keyword id="KW-1048">Host nucleus</keyword>
    <keyword id="KW-0945">Host-virus interaction</keyword>
    <keyword id="KW-0378">Hydrolase</keyword>
    <keyword id="KW-0449">Lipoprotein</keyword>
    <keyword id="KW-0472">Membrane</keyword>
    <keyword id="KW-0564">Palmitate</keyword>
    <keyword id="KW-0645">Protease</keyword>
    <keyword id="KW-1185">Reference proteome</keyword>
    <keyword id="KW-0688">Ribosomal frameshifting</keyword>
    <keyword id="KW-0694">RNA-binding</keyword>
    <keyword id="KW-0720">Serine protease</keyword>
    <keyword id="KW-1144">T=4 icosahedral capsid protein</keyword>
    <keyword id="KW-0812">Transmembrane</keyword>
    <keyword id="KW-1133">Transmembrane helix</keyword>
    <keyword id="KW-1161">Viral attachment to host cell</keyword>
    <keyword id="KW-0261">Viral envelope protein</keyword>
    <keyword id="KW-1162">Viral penetration into host cytoplasm</keyword>
    <keyword id="KW-0946">Virion</keyword>
    <keyword id="KW-1164">Virus endocytosis by host</keyword>
    <keyword id="KW-1160">Virus entry into host cell</keyword>
    <feature type="chain" id="PRO_0000041311" description="Capsid protein">
        <location>
            <begin position="1"/>
            <end position="267"/>
        </location>
    </feature>
    <feature type="chain" id="PRO_0000226237" description="Precursor of protein E3/E2">
        <location>
            <begin position="268"/>
            <end position="755"/>
        </location>
    </feature>
    <feature type="chain" id="PRO_0000041312" description="Assembly protein E3">
        <location>
            <begin position="268"/>
            <end position="333"/>
        </location>
    </feature>
    <feature type="chain" id="PRO_0000041313" description="Spike glycoprotein E2">
        <location>
            <begin position="334"/>
            <end position="755"/>
        </location>
    </feature>
    <feature type="chain" id="PRO_0000041314" description="6K protein">
        <location>
            <begin position="756"/>
            <end position="815"/>
        </location>
    </feature>
    <feature type="chain" id="PRO_0000041315" description="Spike glycoprotein E1">
        <location>
            <begin position="816"/>
            <end position="1253"/>
        </location>
    </feature>
    <feature type="topological domain" description="Extracellular" evidence="8">
        <location>
            <begin position="268"/>
            <end position="701"/>
        </location>
    </feature>
    <feature type="transmembrane region" description="Helical" evidence="8">
        <location>
            <begin position="702"/>
            <end position="722"/>
        </location>
    </feature>
    <feature type="topological domain" description="Cytoplasmic" evidence="8">
        <location>
            <begin position="723"/>
            <end position="755"/>
        </location>
    </feature>
    <feature type="topological domain" description="Extracellular" evidence="8">
        <location>
            <begin position="756"/>
            <end position="770"/>
        </location>
    </feature>
    <feature type="transmembrane region" description="Helical" evidence="8">
        <location>
            <begin position="771"/>
            <end position="791"/>
        </location>
    </feature>
    <feature type="topological domain" description="Cytoplasmic" evidence="8">
        <location>
            <position position="792"/>
        </location>
    </feature>
    <feature type="transmembrane region" description="Helical" evidence="8">
        <location>
            <begin position="793"/>
            <end position="813"/>
        </location>
    </feature>
    <feature type="topological domain" description="Extracellular" evidence="8">
        <location>
            <begin position="814"/>
            <end position="1230"/>
        </location>
    </feature>
    <feature type="transmembrane region" description="Helical" evidence="8">
        <location>
            <begin position="1231"/>
            <end position="1251"/>
        </location>
    </feature>
    <feature type="topological domain" description="Cytoplasmic" evidence="8">
        <location>
            <begin position="1252"/>
            <end position="1253"/>
        </location>
    </feature>
    <feature type="domain" description="Peptidase S3" evidence="9">
        <location>
            <begin position="119"/>
            <end position="267"/>
        </location>
    </feature>
    <feature type="region of interest" description="Host transcription inhibition" evidence="3">
        <location>
            <begin position="37"/>
            <end position="71"/>
        </location>
    </feature>
    <feature type="region of interest" description="Disordered" evidence="10">
        <location>
            <begin position="58"/>
            <end position="109"/>
        </location>
    </feature>
    <feature type="region of interest" description="Binding to the viral RNA" evidence="5">
        <location>
            <begin position="87"/>
            <end position="120"/>
        </location>
    </feature>
    <feature type="region of interest" description="Ribosome-binding" evidence="5">
        <location>
            <begin position="105"/>
            <end position="119"/>
        </location>
    </feature>
    <feature type="region of interest" description="Dimerization of the capsid protein" evidence="4">
        <location>
            <begin position="189"/>
            <end position="199"/>
        </location>
    </feature>
    <feature type="region of interest" description="Dimerization of the capsid protein" evidence="4">
        <location>
            <begin position="225"/>
            <end position="229"/>
        </location>
    </feature>
    <feature type="region of interest" description="Transient transmembrane before p62-6K protein processing" evidence="8">
        <location>
            <begin position="728"/>
            <end position="748"/>
        </location>
    </feature>
    <feature type="region of interest" description="E1 fusion peptide loop" evidence="7">
        <location>
            <begin position="899"/>
            <end position="916"/>
        </location>
    </feature>
    <feature type="short sequence motif" description="Nuclear localization signal" evidence="3">
        <location>
            <begin position="64"/>
            <end position="105"/>
        </location>
    </feature>
    <feature type="short sequence motif" description="Nuclear export signal" evidence="3">
        <location>
            <begin position="150"/>
            <end position="160"/>
        </location>
    </feature>
    <feature type="compositionally biased region" description="Basic residues" evidence="10">
        <location>
            <begin position="64"/>
            <end position="81"/>
        </location>
    </feature>
    <feature type="active site" description="Charge relay system" evidence="9">
        <location>
            <position position="145"/>
        </location>
    </feature>
    <feature type="active site" description="Charge relay system" evidence="9">
        <location>
            <position position="167"/>
        </location>
    </feature>
    <feature type="active site" description="Charge relay system" evidence="9 26">
        <location>
            <position position="219"/>
        </location>
    </feature>
    <feature type="site" description="Involved in dimerization of the capsid protein" evidence="6">
        <location>
            <position position="193"/>
        </location>
    </feature>
    <feature type="site" description="Involved in dimerization of the capsid protein" evidence="6">
        <location>
            <position position="226"/>
        </location>
    </feature>
    <feature type="site" description="Cleavage; by autolysis" evidence="26">
        <location>
            <begin position="267"/>
            <end position="268"/>
        </location>
    </feature>
    <feature type="site" description="Cleavage; by host furin">
        <location>
            <begin position="333"/>
            <end position="334"/>
        </location>
    </feature>
    <feature type="site" description="Cleavage; by host signal peptidase">
        <location>
            <begin position="755"/>
            <end position="756"/>
        </location>
    </feature>
    <feature type="site" description="Cleavage; by host signal peptidase">
        <location>
            <begin position="815"/>
            <end position="816"/>
        </location>
    </feature>
    <feature type="lipid moiety-binding region" description="S-palmitoyl cysteine; by host" evidence="8">
        <location>
            <position position="718"/>
        </location>
    </feature>
    <feature type="lipid moiety-binding region" description="S-palmitoyl cysteine; by host" evidence="1">
        <location>
            <position position="728"/>
        </location>
    </feature>
    <feature type="lipid moiety-binding region" description="S-palmitoyl cysteine; by host" evidence="1">
        <location>
            <position position="748"/>
        </location>
    </feature>
    <feature type="lipid moiety-binding region" description="S-palmitoyl cysteine; by host" evidence="1">
        <location>
            <position position="749"/>
        </location>
    </feature>
    <feature type="lipid moiety-binding region" description="S-stearoyl cysteine; by host" evidence="24">
        <location>
            <position position="1248"/>
        </location>
    </feature>
    <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine; by host" evidence="8">
        <location>
            <position position="280"/>
        </location>
    </feature>
    <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine; by host" evidence="8">
        <location>
            <position position="327"/>
        </location>
    </feature>
    <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine; by host" evidence="8">
        <location>
            <position position="533"/>
        </location>
    </feature>
    <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine; by host" evidence="8">
        <location>
            <position position="595"/>
        </location>
    </feature>
    <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine; by host" evidence="15 28">
        <location>
            <position position="956"/>
        </location>
    </feature>
    <feature type="disulfide bond">
        <location>
            <begin position="119"/>
            <end position="134"/>
        </location>
    </feature>
    <feature type="disulfide bond">
        <location>
            <begin position="864"/>
            <end position="929"/>
        </location>
    </feature>
    <feature type="disulfide bond">
        <location>
            <begin position="877"/>
            <end position="909"/>
        </location>
    </feature>
    <feature type="disulfide bond">
        <location>
            <begin position="878"/>
            <end position="911"/>
        </location>
    </feature>
    <feature type="disulfide bond">
        <location>
            <begin position="883"/>
            <end position="893"/>
        </location>
    </feature>
    <feature type="disulfide bond">
        <location>
            <begin position="1074"/>
            <end position="1086"/>
        </location>
    </feature>
    <feature type="disulfide bond">
        <location>
            <begin position="1116"/>
            <end position="1191"/>
        </location>
    </feature>
    <feature type="disulfide bond">
        <location>
            <begin position="1121"/>
            <end position="1195"/>
        </location>
    </feature>
    <feature type="disulfide bond">
        <location>
            <begin position="1143"/>
            <end position="1185"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: A7.">
        <original>A</original>
        <variation>T</variation>
        <location>
            <position position="62"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: L10.">
        <original>R</original>
        <variation>G</variation>
        <location>
            <position position="63"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: A7, L10 and MTV.">
        <original>N</original>
        <variation>K</variation>
        <location>
            <position position="85"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: A7.">
        <original>A</original>
        <variation>T</variation>
        <location>
            <position position="279"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: A7.">
        <original>V</original>
        <variation>A</variation>
        <location>
            <position position="291"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: A7, L10 and MTV.">
        <original>V</original>
        <variation>I</variation>
        <location>
            <position position="370"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: A7, L10 and MTV.">
        <original>K</original>
        <variation>T</variation>
        <location>
            <position position="437"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: A7.">
        <original>N</original>
        <variation>S</variation>
        <location>
            <position position="545"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: A7 and MTV.">
        <original>M</original>
        <variation>K</variation>
        <location>
            <position position="548"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: MTV.">
        <original>E</original>
        <variation>K</variation>
        <location>
            <position position="614"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: A7.">
        <original>V</original>
        <variation>A</variation>
        <location>
            <position position="700"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: A7.">
        <original>V</original>
        <variation>A</variation>
        <location>
            <position position="704"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: A7 and MTV.">
        <original>V</original>
        <variation>A</variation>
        <location>
            <position position="722"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: A7.">
        <original>A</original>
        <variation>S</variation>
        <location>
            <position position="880"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: A7.">
        <original>R</original>
        <variation>K</variation>
        <location>
            <position position="930"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: A7 and MTV.">
        <original>M</original>
        <variation>T</variation>
        <location>
            <position position="1043"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: A7 and MTV.">
        <original>I</original>
        <variation>T</variation>
        <location>
            <position position="1112"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: A7.">
        <original>T</original>
        <variation>K</variation>
        <location>
            <position position="1134"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: A7, L10 and MTV.">
        <original>N</original>
        <variation>D</variation>
        <location>
            <position position="1138"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: MTV.">
        <original>G</original>
        <variation>R</variation>
        <location>
            <position position="1165"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: A7 and MTV.">
        <original>R</original>
        <variation>K</variation>
        <location>
            <position position="1188"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Loss of autocatalytic cleavage by capsid protein." evidence="26">
        <original>SG</original>
        <variation>RST</variation>
        <location>
            <begin position="219"/>
            <end position="220"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Complete loss of cleavage by capsid protease.">
        <original>W</original>
        <variation>A</variation>
        <variation>R</variation>
        <location>
            <position position="267"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Complete loss of p62 precursor processing." evidence="20">
        <original>R</original>
        <variation>S</variation>
        <location>
            <position position="330"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Complete loss of p62 precursor processing." evidence="20">
        <original>R</original>
        <variation>F</variation>
        <location>
            <position position="333"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Complete loss of p62 precursor-6K cleavage." evidence="19">
        <original>A</original>
        <variation>F</variation>
        <location>
            <position position="755"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Complete loss of 6K protein-E1 envelope glycoprotein cleavage." evidence="19">
        <original>A</original>
        <variation>F</variation>
        <location>
            <position position="815"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="E1 fusion is less cholesterol and sphingolipid dependent." evidence="11">
        <original>L</original>
        <variation>F</variation>
        <location>
            <position position="859"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Shifts the pH threshold for fusion to a more acidic range." evidence="21">
        <original>D</original>
        <variation>A</variation>
        <location>
            <position position="890"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="No effect on E1 fusion activity." evidence="21">
        <original>K</original>
        <variation>Q</variation>
        <location>
            <position position="894"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Shifts the pH threshold for fusion to a more acidic range." evidence="21 30">
        <original>G</original>
        <variation>A</variation>
        <location>
            <position position="898"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="No effect on E1 fusion activity." evidence="21 30">
        <original>G</original>
        <variation>D</variation>
        <location>
            <position position="898"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Retention of E1 protein in endoplasmic reticulum." evidence="21">
        <original>P</original>
        <variation>D</variation>
        <location>
            <position position="901"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="No effect on E1 fusion activity." evidence="21">
        <original>M</original>
        <variation>L</variation>
        <location>
            <position position="903"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Shifts the pH threshold for fusion to a more acidic range." evidence="21 30">
        <original>G</original>
        <variation>A</variation>
        <location>
            <position position="906"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Complete loss of E1 fusion activity." evidence="21 30">
        <original>G</original>
        <variation>D</variation>
        <location>
            <position position="906"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Retention of E1 protein in endoplasmic reticulum." evidence="21 30">
        <original>G</original>
        <variation>P</variation>
        <location>
            <position position="906"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="E1 fusion is less cholesterol and sphingolipid dependent." evidence="11">
        <original>V</original>
        <variation>A</variation>
        <location>
            <position position="993"/>
        </location>
    </feature>
    <feature type="strand" evidence="34">
        <location>
            <begin position="120"/>
            <end position="125"/>
        </location>
    </feature>
    <feature type="strand" evidence="34">
        <location>
            <begin position="128"/>
            <end position="134"/>
        </location>
    </feature>
    <feature type="strand" evidence="34">
        <location>
            <begin position="139"/>
            <end position="141"/>
        </location>
    </feature>
    <feature type="strand" evidence="34">
        <location>
            <begin position="148"/>
            <end position="152"/>
        </location>
    </feature>
    <feature type="helix" evidence="34">
        <location>
            <begin position="153"/>
            <end position="156"/>
        </location>
    </feature>
    <feature type="strand" evidence="34">
        <location>
            <begin position="161"/>
            <end position="163"/>
        </location>
    </feature>
    <feature type="turn" evidence="34">
        <location>
            <begin position="164"/>
            <end position="167"/>
        </location>
    </feature>
    <feature type="strand" evidence="34">
        <location>
            <begin position="168"/>
            <end position="172"/>
        </location>
    </feature>
    <feature type="helix" evidence="34">
        <location>
            <begin position="175"/>
            <end position="180"/>
        </location>
    </feature>
    <feature type="strand" evidence="34">
        <location>
            <begin position="190"/>
            <end position="195"/>
        </location>
    </feature>
    <feature type="strand" evidence="34">
        <location>
            <begin position="198"/>
            <end position="203"/>
        </location>
    </feature>
    <feature type="strand" evidence="34">
        <location>
            <begin position="206"/>
            <end position="210"/>
        </location>
    </feature>
    <feature type="strand" evidence="34">
        <location>
            <begin position="222"/>
            <end position="224"/>
        </location>
    </feature>
    <feature type="strand" evidence="34">
        <location>
            <begin position="230"/>
            <end position="239"/>
        </location>
    </feature>
    <feature type="strand" evidence="34">
        <location>
            <begin position="241"/>
            <end position="251"/>
        </location>
    </feature>
    <feature type="strand" evidence="34">
        <location>
            <begin position="253"/>
            <end position="259"/>
        </location>
    </feature>
    <feature type="strand" evidence="35">
        <location>
            <begin position="821"/>
            <end position="823"/>
        </location>
    </feature>
    <feature type="strand" evidence="35">
        <location>
            <begin position="830"/>
            <end position="832"/>
        </location>
    </feature>
    <feature type="strand" evidence="35">
        <location>
            <begin position="837"/>
            <end position="839"/>
        </location>
    </feature>
    <feature type="strand" evidence="35">
        <location>
            <begin position="844"/>
            <end position="863"/>
        </location>
    </feature>
    <feature type="strand" evidence="35">
        <location>
            <begin position="866"/>
            <end position="869"/>
        </location>
    </feature>
    <feature type="strand" evidence="35">
        <location>
            <begin position="874"/>
            <end position="876"/>
        </location>
    </feature>
    <feature type="strand" evidence="35">
        <location>
            <begin position="892"/>
            <end position="898"/>
        </location>
    </feature>
    <feature type="helix" evidence="35">
        <location>
            <begin position="903"/>
            <end position="907"/>
        </location>
    </feature>
    <feature type="strand" evidence="35">
        <location>
            <begin position="910"/>
            <end position="913"/>
        </location>
    </feature>
    <feature type="strand" evidence="35">
        <location>
            <begin position="916"/>
            <end position="925"/>
        </location>
    </feature>
    <feature type="turn" evidence="35">
        <location>
            <begin position="927"/>
            <end position="931"/>
        </location>
    </feature>
    <feature type="strand" evidence="35">
        <location>
            <begin position="934"/>
            <end position="954"/>
        </location>
    </feature>
    <feature type="strand" evidence="35">
        <location>
            <begin position="958"/>
            <end position="962"/>
        </location>
    </feature>
    <feature type="strand" evidence="35">
        <location>
            <begin position="964"/>
            <end position="966"/>
        </location>
    </feature>
    <feature type="strand" evidence="35">
        <location>
            <begin position="969"/>
            <end position="971"/>
        </location>
    </feature>
    <feature type="strand" evidence="35">
        <location>
            <begin position="974"/>
            <end position="978"/>
        </location>
    </feature>
    <feature type="strand" evidence="35">
        <location>
            <begin position="990"/>
            <end position="994"/>
        </location>
    </feature>
    <feature type="strand" evidence="35">
        <location>
            <begin position="999"/>
            <end position="1001"/>
        </location>
    </feature>
    <feature type="helix" evidence="33">
        <location>
            <begin position="1007"/>
            <end position="1009"/>
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    <sequence length="1253" mass="138017" checksum="2A73228D08B82AC5" modified="1986-07-21" version="1">MNYIPTQTFYGRRWRPRPAARPWPLQATPVAPVVPDFQAQQMQQLISAVNALTMRQNAIAPARPPKPKKKKTTKPKPKTQPKKINGKTQQQKKKDKQADKKKKKPGKRERMCMKIENDCIFEVKHEGKVTGYACLVGDKVMKPAHVKGVIDNADLAKLAFKKSSKYDLECAQIPVHMRSDASKYTHEKPEGHYNWHHGAVQYSGGRFTIPTGAGKPGDSGRPIFDNKGRVVAIVLGGANEGSRTALSVVTWNKDMVTRVTPEGSEEWSAPLITAMCVLANATFPCFQPPCVPCCYENNAEATLRMLEDNVDRPGYYDLLQAALTCRNGTRHRRSVSQHFNVYKATRPYIAYCADCGAGHSCHSPVAIEAVRSEATDGMLKIQFSAQIGIDKSDNHDYTKIRYADGHAIENAVRSSLKVATSGDCFVHGTMGHFILAKCPPGEFLQVSIQDTRNAVRACRIQYHHDPQPVGREKFTIRPHYGKEIPCTTYQQTTAETVEEIDMHMPPDTPDRTLLSQQSGNVKITVGGKKVKYNCTCGTGNVGTTNSDMTINTCLIEQCHVSVTDHKKWQFNSPFVPRADEPARKGKVHIPFPLDNITCRVPMAREPTVIHGKREVTLHLHPDHPTLFSYRTLGEDPQYHEEWVTAAVERTIPVPVDGMEYHWGNNDPVRLWSQLTTEGKPHGWPHQIVQYYYGLYPAATVSAVVGMSLLALISIFASCYMLVAARSKCLTPYALTPGAAVPWTLGILCCAPRAHAASVAETMAYLWDQNQALFWLEFAAPVACILIITYCLRNVLCCCKSLSFLVLLSLGATARAYEHSTVMPNVVGFPYKAHIERPGYSPLTLQMQVVETSLEPTLNLEYITCEYKTVVPSPYVKCCGASECSTKEKPDYQCKVYTGVYPFMWGGAYCFCDSENTQLSEAYVDRSDVCRHDHASAYKAHTASLKAKVRVMYGNVNQTVDVYVNGDHAVTIGGTQFIFGPLSSAWTPFDNKIVVYKDEVFNQDFPPYGSGQPGRFGDIQSRTVESNDLYANTALKLARPSPGMVHVPYTQTPSGFKYWLKEKGTALNTKAPFGCQIKTNPVRAMNCAVGNIPVSMNLPDSAFTRIVEAPTIIDLTCTVATCTHSSDFGGVLTLTYKTNKNGDCSVHSHSNVATLQEATAKVKTAGKVTLHFSTASASPSFVVSLCSARATCSASCEPPKDHIVPYAASHSNVVFPDMSGTALSWVQKISGGLGAFAIGAILVLVVVTCIGLRR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1988-08-01" modified="2022-08-03" version="170" xmlns="http://uniprot.org/uniprot">
    <accession>P08411</accession>
    <accession>B3TP00</accession>
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    <accession>Q3LRQ4</accession>
    <accession>Q3LRQ6</accession>
    <accession>Q3LRQ7</accession>
    <accession>Q3LRQ9</accession>
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    <accession>Q3LRR1</accession>
    <accession>Q3LRR2</accession>
    <accession>Q8JMP6</accession>
    <accession>Q9QBM1</accession>
    <name>POLN_SFV</name>
    <protein>
        <recommendedName>
            <fullName>Polyprotein P1234</fullName>
            <shortName>P1234</shortName>
        </recommendedName>
        <alternativeName>
            <fullName>Non-structural polyprotein</fullName>
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        <component>
            <recommendedName>
                <fullName>Polyprotein P123'</fullName>
                <shortName>P123'</shortName>
            </recommendedName>
        </component>
        <component>
            <recommendedName>
                <fullName>Polyprotein P123</fullName>
                <shortName>P123</shortName>
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        <component>
            <recommendedName>
                <fullName>mRNA-capping enzyme nsP1</fullName>
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                <ecNumber evidence="3">2.7.7.-</ecNumber>
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            <alternativeName>
                <fullName>Non-structural protein 1</fullName>
            </alternativeName>
        </component>
        <component>
            <recommendedName>
                <fullName>Protease nsP2</fullName>
                <ecNumber evidence="12">3.1.3.33</ecNumber>
                <ecNumber evidence="4">3.4.22.-</ecNumber>
                <ecNumber evidence="36">3.6.1.15</ecNumber>
                <ecNumber evidence="11">3.6.4.13</ecNumber>
            </recommendedName>
            <alternativeName>
                <fullName>Non-structural protein 2</fullName>
                <shortName>nsP2</shortName>
            </alternativeName>
        </component>
        <component>
            <recommendedName>
                <fullName>Non-structural protein 3</fullName>
                <shortName>nsP3</shortName>
                <ecNumber evidence="4">3.1.3.84</ecNumber>
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        </component>
        <component>
            <recommendedName>
                <fullName>Non-structural protein 3'</fullName>
                <shortName>nsP3'</shortName>
                <ecNumber evidence="4">3.1.3.84</ecNumber>
            </recommendedName>
        </component>
        <component>
            <recommendedName>
                <fullName>RNA-directed RNA polymerase nsP4</fullName>
                <ecNumber evidence="2">2.7.7.19</ecNumber>
                <ecNumber evidence="6">2.7.7.48</ecNumber>
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            <alternativeName>
                <fullName>Non-structural protein 4</fullName>
                <shortName>nsP4</shortName>
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    </protein>
    <organism>
        <name type="scientific">Semliki forest virus</name>
        <name type="common">SFV</name>
        <dbReference type="NCBI Taxonomy" id="11033"/>
        <lineage>
            <taxon>Viruses</taxon>
            <taxon>Riboviria</taxon>
            <taxon>Orthornavirae</taxon>
            <taxon>Kitrinoviricota</taxon>
            <taxon>Alsuviricetes</taxon>
            <taxon>Martellivirales</taxon>
            <taxon>Togaviridae</taxon>
            <taxon>Alphavirus</taxon>
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    </organism>
    <organismHost>
        <name type="scientific">Aedes</name>
        <dbReference type="NCBI Taxonomy" id="7158"/>
    </organismHost>
    <organismHost>
        <name type="scientific">Culex tritaeniorhynchus</name>
        <name type="common">Mosquito</name>
        <dbReference type="NCBI Taxonomy" id="7178"/>
    </organismHost>
    <organismHost>
        <name type="scientific">Atelerix albiventris</name>
        <name type="common">Middle-African hedgehog</name>
        <name type="synonym">Four-toed hedgehog</name>
        <dbReference type="NCBI Taxonomy" id="9368"/>
    </organismHost>
    <organismHost>
        <name type="scientific">Homo sapiens</name>
        <name type="common">Human</name>
        <dbReference type="NCBI Taxonomy" id="9606"/>
    </organismHost>
    <organismHost>
        <name type="scientific">Rhipicephalus</name>
        <dbReference type="NCBI Taxonomy" id="34630"/>
    </organismHost>
    <organismHost>
        <name type="scientific">Quelea</name>
        <dbReference type="NCBI Taxonomy" id="158617"/>
    </organismHost>
    <organismHost>
        <name type="scientific">Halcyon</name>
        <dbReference type="NCBI Taxonomy" id="170865"/>
    </organismHost>
    <reference key="1">
        <citation type="journal article" date="1986" name="Nucleic Acids Res." volume="14" first="5667" last="5682">
            <title>Complete nucleotide sequence of the nonstructural protein genes of Semliki Forest virus.</title>
            <authorList>
                <person name="Takkinen K."/>
            </authorList>
            <dbReference type="PubMed" id="3488539"/>
            <dbReference type="DOI" id="10.1093/nar/14.14.5667"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC RNA]</scope>
        <source>
            <strain>Isolate Garoff/Takkinen</strain>
        </source>
    </reference>
    <reference key="2">
        <citation type="journal article" date="2000" name="J. Virol." volume="74" first="4579" last="4589">
            <title>Replicase complex genes of Semliki Forest virus confer lethal neurovirulence.</title>
            <authorList>
                <person name="Tuittila M.T."/>
                <person name="Santagati M.G."/>
                <person name="Roeyttae M."/>
                <person name="Maeaettae J.A."/>
                <person name="Hinkkanen A.E."/>
            </authorList>
            <dbReference type="PubMed" id="10775594"/>
            <dbReference type="DOI" id="10.1128/JVI.74.10.4579-4589.2000"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC RNA]</scope>
        <source>
            <strain>Isolate L10 clone SFV4</strain>
        </source>
    </reference>
    <reference key="3">
        <citation type="submission" date="2002-05" db="EMBL/GenBank/DDBJ databases">
            <title>Semliki Forest virus -- L10 strain complete genome.</title>
            <authorList>
                <person name="Logue C."/>
                <person name="Mooney D."/>
                <person name="Shanley R."/>
                <person name="Atkins G.J."/>
            </authorList>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC RNA]</scope>
        <source>
            <strain>Isolate L10</strain>
        </source>
    </reference>
    <reference key="4">
        <citation type="journal article" date="2006" name="J. Virol." volume="80" first="3108" last="3111">
            <title>Identification of mutations causing temperature-sensitive defects in Semliki Forest virus RNA synthesis.</title>
            <authorList>
                <person name="Lulla V."/>
                <person name="Merits A."/>
                <person name="Sarin P."/>
                <person name="Kaariainen L."/>
                <person name="Keranen S."/>
                <person name="Ahola T."/>
            </authorList>
            <dbReference type="PubMed" id="16501123"/>
            <dbReference type="DOI" id="10.1128/JVI.80.6.3108-3111.2006"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC RNA]</scope>
        <source>
            <strain>Isolate Ts1</strain>
            <strain>Isolate Ts10</strain>
            <strain>Isolate Ts11</strain>
            <strain>Isolate Ts13</strain>
            <strain>Isolate Ts14</strain>
            <strain>Isolate Ts6</strain>
            <strain>Isolate Ts9</strain>
        </source>
    </reference>
    <reference key="5">
        <citation type="journal article" date="2008" name="J. Gen. Virol." volume="89" first="2132" last="2135">
            <title>Me Tri virus: a Semliki Forest virus strain from Vietnam?</title>
            <authorList>
                <person name="Tan le V."/>
                <person name="Ha do Q."/>
                <person name="Hien V.M."/>
                <person name="van der Hoek L."/>
                <person name="Farrar J."/>
                <person name="de Jong M.D."/>
            </authorList>
            <dbReference type="PubMed" id="18753222"/>
            <dbReference type="DOI" id="10.1099/vir.0.2008/002121-0"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC RNA] (POLYPROTEIN P123)</scope>
        <source>
            <strain>Isolate Me Tri virus</strain>
        </source>
    </reference>
    <reference key="6">
        <citation type="journal article" date="1988" name="J. Cell Biol." volume="107" first="2075" last="2086">
            <title>Alphavirus RNA replicase is located on the cytoplasmic surface of endosomes and lysosomes.</title>
            <authorList>
                <person name="Froshauer S."/>
                <person name="Kartenbeck J."/>
                <person name="Helenius A."/>
            </authorList>
            <dbReference type="PubMed" id="2904446"/>
            <dbReference type="DOI" id="10.1083/jcb.107.6.2075"/>
        </citation>
        <scope>SUBCELLULAR LOCATION (RNA-DIRECTED RNA POLYMERASE NSP4)</scope>
    </reference>
    <reference key="7">
        <citation type="journal article" date="1992" name="Virology" volume="189" first="462" last="473">
            <title>Nuclear and nucleolar targeting signals of Semliki Forest virus nonstructural protein nsP2.</title>
            <authorList>
                <person name="Rikkonen M."/>
                <person name="Peraenen J."/>
                <person name="Kaeaeriaeinen L."/>
            </authorList>
            <dbReference type="PubMed" id="1386484"/>
            <dbReference type="DOI" id="10.1016/0042-6822(92)90570-F"/>
        </citation>
        <scope>SUBCELLULAR LOCATION (PROTEASE NSP2)</scope>
        <scope>NUCLEAR LOCALIZATION SIGNAL</scope>
    </reference>
    <reference key="8">
        <citation type="journal article" date="1994" name="J. Virol." volume="68" first="5804" last="5810">
            <title>ATPase and GTPase activities associated with Semliki Forest virus nonstructural protein nsP2.</title>
            <authorList>
                <person name="Rikkonen M."/>
                <person name="Peraenen J."/>
                <person name="Kaeaeriaeinen L."/>
            </authorList>
            <dbReference type="PubMed" id="8057461"/>
        </citation>
        <scope>FUNCTION (PROTEASE NSP2)</scope>
        <scope>CATALYTIC ACTIVITY (PROTEASE NSP2)</scope>
        <scope>MUTAGENESIS OF LYS-729</scope>
    </reference>
    <reference key="9">
        <citation type="journal article" date="1995" name="Virology" volume="208" first="610" last="620">
            <title>The alphavirus replicase protein nsP1 is membrane-associated and has affinity to endocytic organelles.</title>
            <authorList>
                <person name="Peraenen J."/>
                <person name="Laakkonen P."/>
                <person name="Hyvoenen M."/>
                <person name="Kaeaeriaeinen L."/>
            </authorList>
            <dbReference type="PubMed" id="7747433"/>
            <dbReference type="DOI" id="10.1006/viro.1995.1192"/>
        </citation>
        <scope>SUBCELLULAR LOCATION (MRNA-CAPPING ENZYME NSP1)</scope>
    </reference>
    <reference key="10">
        <citation type="journal article" date="1995" name="Proc. Natl. Acad. Sci. U.S.A." volume="92" first="507" last="511">
            <title>Reaction in alphavirus mRNA capping: formation of a covalent complex of nonstructural protein nsP1 with 7-methyl-GMP.</title>
            <authorList>
                <person name="Ahola T."/>
                <person name="Kaeaeriaeinen L."/>
            </authorList>
            <dbReference type="PubMed" id="7831320"/>
            <dbReference type="DOI" id="10.1073/pnas.92.2.507"/>
        </citation>
        <scope>FUNCTION (MRNA-CAPPING ENZYME NSP1)</scope>
    </reference>
    <reference key="11">
        <citation type="journal article" date="1996" name="J. Biol. Chem." volume="271" first="28567" last="28571">
            <title>The effects of palmitoylation on membrane association of Semliki forest virus RNA capping enzyme.</title>
            <authorList>
                <person name="Laakkonen P."/>
                <person name="Ahola T."/>
                <person name="Kaeaeriaeinen L."/>
            </authorList>
            <dbReference type="PubMed" id="8910486"/>
            <dbReference type="DOI" id="10.1074/jbc.271.45.28567"/>
        </citation>
        <scope>PALMITOYLATION AT CYS-418 AND CYS-420</scope>
        <scope>MUTAGENESIS OF 418-CYS--CYS-420</scope>
        <scope>SUBCELLULAR LOCATION (MRNA-CAPPING ENZYME NSP1)</scope>
    </reference>
    <reference key="12">
        <citation type="journal article" date="1996" name="Virology" volume="218" first="352" last="361">
            <title>Functional significance of the nuclear-targeting and NTP-binding motifs of Semliki Forest virus nonstructural protein nsP2.</title>
            <authorList>
                <person name="Rikkonen M."/>
            </authorList>
            <dbReference type="PubMed" id="8610462"/>
            <dbReference type="DOI" id="10.1006/viro.1996.0204"/>
        </citation>
        <scope>SUBCELLULAR LOCATION (PROTEASE NSP2)</scope>
        <scope>MUTAGENESIS OF LYS-729 AND ARG-1186</scope>
        <scope>NUCLEAR LOCALIZATION SIGNAL</scope>
    </reference>
    <reference key="13">
        <citation type="journal article" date="1997" name="J. Virol." volume="71" first="392" last="397">
            <title>Critical residues of Semliki Forest virus RNA capping enzyme involved in methyltransferase and guanylyltransferase-like activities.</title>
            <authorList>
                <person name="Ahola T."/>
                <person name="Laakkonen P."/>
                <person name="Vihinen H."/>
                <person name="Kaeaeriaeinen L."/>
            </authorList>
            <dbReference type="PubMed" id="8985362"/>
        </citation>
        <scope>FUNCTION (MRNA-CAPPING ENZYME NSP1)</scope>
        <scope>MUTAGENESIS OF LEU-19; HIS-38; ASP-64; 81-CYS--CYS-83; ASP-90; ARG-93; CYS-135; CYS-142; ASP-153; LYS-169; ASP-180; GLU-203; CYS-214; TYR-249 AND LYS-317</scope>
    </reference>
    <reference key="14">
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            <title>Alphavirus replicase protein NSP1 induces filopodia and rearrangement of actin filaments.</title>
            <authorList>
                <person name="Laakkonen P."/>
                <person name="Auvinen P."/>
                <person name="Kujala P."/>
                <person name="Kaeaeriaeinen L."/>
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        <scope>FUNCTION (MRNA-CAPPING ENZYME NSP1)</scope>
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            <title>Semliki Forest virus mRNA capping enzyme requires association with anionic membrane phospholipids for activity.</title>
            <authorList>
                <person name="Ahola T."/>
                <person name="Lampio A."/>
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                <person name="Kaeaeriaeinen L."/>
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            <dbReference type="PubMed" id="10357827"/>
            <dbReference type="DOI" id="10.1093/emboj/18.11.3164"/>
        </citation>
        <scope>MEMBRANE-BINDING (MRNA-CAPPING ENZYME NSP1)</scope>
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            <title>RNA helicase activity of Semliki Forest virus replicase protein NSP2.</title>
            <authorList>
                <person name="Gomez de Cedron M."/>
                <person name="Ehsani N."/>
                <person name="Mikkola M.L."/>
                <person name="Garcia J.A."/>
                <person name="Kaeaeriaeinen L."/>
            </authorList>
            <dbReference type="PubMed" id="10217401"/>
            <dbReference type="DOI" id="10.1016/S0014-5793(99)00321-X"/>
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        <scope>FUNCTION (PROTEASE NSP2)</scope>
        <scope>MUTAGENESIS OF LYS-729</scope>
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            <title>Effects of palmitoylation of replicase protein nsP1 on alphavirus infection.</title>
            <authorList>
                <person name="Ahola T."/>
                <person name="Kujala P."/>
                <person name="Tuittila M."/>
                <person name="Blom T."/>
                <person name="Laakkonen P."/>
                <person name="Hinkkanen A."/>
                <person name="Auvinen P."/>
            </authorList>
            <dbReference type="PubMed" id="10888610"/>
            <dbReference type="DOI" id="10.1128/JVI.74.15.6725-6733.2000"/>
        </citation>
        <scope>PALMITOYLATION AT CYS-418 AND CYS-420</scope>
        <scope>MUTAGENESIS OF 418-CYS--CYS-420</scope>
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    <reference key="18">
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            <title>Identification of a novel function of the alphavirus capping apparatus. RNA 5'-triphosphatase activity of Nsp2.</title>
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                <person name="Vasiljeva L."/>
                <person name="Merits A."/>
                <person name="Auvinen P."/>
                <person name="Kaeaeriaeinen L."/>
            </authorList>
            <dbReference type="PubMed" id="10748213"/>
            <dbReference type="DOI" id="10.1074/jbc.M910340199"/>
        </citation>
        <scope>FUNCTION (PROTEASE NSP2)</scope>
        <scope>BIOPHYSICOCHEMICAL PROPERTIES (PROTEASE NSP2)</scope>
        <scope>CATALYTIC ACTIVITY (PROTEASE NSP2)</scope>
        <scope>MUTAGENESIS OF LYS-729</scope>
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    <reference key="19">
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            <title>Proteolytic processing of Semliki Forest virus-specific non-structural polyprotein by nsP2 protease.</title>
            <authorList>
                <person name="Merits A."/>
                <person name="Vasiljeva L."/>
                <person name="Ahola T."/>
                <person name="Kaeaeriaeinen L."/>
                <person name="Auvinen P."/>
            </authorList>
            <dbReference type="PubMed" id="11257180"/>
        </citation>
        <scope>ACTIVE SITE (PROTEASE NSP2)</scope>
        <scope>MUTAGENESIS OF CYS-1015 AND ASP-1824</scope>
        <scope>FUNCTION (PROTEASE NSP2)</scope>
        <scope>PROTEOLYTIC CLEAVAGE (POLYPROTEIN P1234)</scope>
        <scope>PROTEOLYTIC CLEAVAGE (POLYPROTEIN P123)</scope>
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    <reference key="20">
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            <title>Site-specific protease activity of the carboxyl-terminal domain of Semliki Forest virus replicase protein nsP2.</title>
            <authorList>
                <person name="Vasiljeva L."/>
                <person name="Valmu L."/>
                <person name="Kaeaeriaeinen L."/>
                <person name="Merits A."/>
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            <dbReference type="PubMed" id="11410598"/>
            <dbReference type="DOI" id="10.1074/jbc.M104786200"/>
        </citation>
        <scope>FUNCTION (PROTEASE NSP2)</scope>
        <scope>PROTEOLYTIC CLEAVAGE (POLYPROTEIN P1234)</scope>
        <scope>ACTIVITY REGULATION (PROTEASE NSP2)</scope>
    </reference>
    <reference key="21">
        <citation type="journal article" date="2001" name="J. Biol. Chem." volume="276" first="5745" last="5752">
            <title>Elimination of phosphorylation sites of Semliki Forest virus replicase protein nsP3.</title>
            <authorList>
                <person name="Vihinen H."/>
                <person name="Ahola T."/>
                <person name="Tuittila M."/>
                <person name="Merits A."/>
                <person name="Kaeaeriaeinen L."/>
            </authorList>
            <dbReference type="PubMed" id="11104756"/>
            <dbReference type="DOI" id="10.1074/jbc.M006077200"/>
        </citation>
        <scope>PHOSPHORYLATION AT THR-1680 AND THR-1681</scope>
        <scope>MUTAGENESIS OF THR-1680 AND THR-1681</scope>
    </reference>
    <reference key="22">
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            <title>Regulation of the sequential processing of Semliki Forest virus replicase polyprotein.</title>
            <authorList>
                <person name="Vasiljeva L."/>
                <person name="Merits A."/>
                <person name="Golubtsov A."/>
                <person name="Sizemskaja V."/>
                <person name="Kaeaeriaeinen L."/>
                <person name="Ahola T."/>
            </authorList>
            <dbReference type="PubMed" id="12917405"/>
            <dbReference type="DOI" id="10.1074/jbc.M307481200"/>
        </citation>
        <scope>PROTEOLYTIC CLEAVAGE (POLYPROTEIN P1234)</scope>
        <scope>PROTEOLYTIC CLEAVAGE (POLYPROTEIN P123)</scope>
    </reference>
    <reference key="23">
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            <title>Importance of eIF2alpha phosphorylation and stress granule assembly in alphavirus translation regulation.</title>
            <authorList>
                <person name="McInerney G.M."/>
                <person name="Kedersha N.L."/>
                <person name="Kaufman R.J."/>
                <person name="Anderson P."/>
                <person name="Liljestrom P."/>
            </authorList>
            <dbReference type="PubMed" id="15930128"/>
            <dbReference type="DOI" id="10.1091/mbc.E05-02-0124"/>
        </citation>
        <scope>HOST TRANSLATION SHUTOFF</scope>
    </reference>
    <reference key="24">
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            <title>Translational resistance of late alphavirus mRNA to eIF2alpha phosphorylation: a strategy to overcome the antiviral effect of protein kinase PKR.</title>
            <authorList>
                <person name="Ventoso I."/>
                <person name="Sanz M.A."/>
                <person name="Molina S."/>
                <person name="Berlanga J.J."/>
                <person name="Carrasco L."/>
                <person name="Esteban M."/>
            </authorList>
            <dbReference type="PubMed" id="16391235"/>
            <dbReference type="DOI" id="10.1101/gad.357006"/>
        </citation>
        <scope>HOST TRANSLATION SHUTOFF</scope>
    </reference>
    <reference key="25">
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            <title>Role for nsP2 proteins in the cessation of alphavirus minus-strand synthesis by host cells.</title>
            <authorList>
                <person name="Sawicki D.L."/>
                <person name="Perri S."/>
                <person name="Polo J.M."/>
                <person name="Sawicki S.G."/>
            </authorList>
            <dbReference type="PubMed" id="16352561"/>
            <dbReference type="DOI" id="10.1128/JVI.80.1.360-371.2006"/>
        </citation>
        <scope>FUNCTION (PROTEASE NSP2)</scope>
    </reference>
    <reference key="26">
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            <title>Role of the amphipathic peptide of Semliki forest virus replicase protein nsP1 in membrane association and virus replication.</title>
            <authorList>
                <person name="Spuul P."/>
                <person name="Salonen A."/>
                <person name="Merits A."/>
                <person name="Jokitalo E."/>
                <person name="Kaeaeriaeinen L."/>
                <person name="Ahola T."/>
            </authorList>
            <dbReference type="PubMed" id="17093195"/>
            <dbReference type="DOI" id="10.1128/JVI.01785-06"/>
        </citation>
        <scope>SUBCELLULAR LOCATION (MRNA-CAPPING ENZYME NSP1)</scope>
        <scope>MUTAGENESIS OF ARG-253 AND TRP-259</scope>
    </reference>
    <reference key="27">
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            <title>Nuclear import and export of Venezuelan equine encephalitis virus nonstructural protein 2.</title>
            <authorList>
                <person name="Montgomery S.A."/>
                <person name="Johnston R.E."/>
            </authorList>
            <dbReference type="PubMed" id="17652399"/>
            <dbReference type="DOI" id="10.1128/JVI.00371-07"/>
        </citation>
        <scope>SUBCELLULAR LOCATION (PROTEASE NSP2)</scope>
        <scope>NUCLEAR LOCALIZATION SIGNAL</scope>
        <source>
            <strain>pV3000</strain>
        </source>
    </reference>
    <reference key="28">
        <citation type="journal article" date="2007" name="J. Gen. Virol." volume="88" first="1977" last="1985">
            <title>Mutations at the palmitoylation site of non-structural protein nsP1 of Semliki Forest virus attenuate virus replication and cause accumulation of compensatory mutations.</title>
            <authorList>
                <person name="Zusinaite E."/>
                <person name="Tints K."/>
                <person name="Kiiver K."/>
                <person name="Spuul P."/>
                <person name="Karo-Astover L."/>
                <person name="Merits A."/>
                <person name="Sarand I."/>
            </authorList>
            <dbReference type="PubMed" id="17554031"/>
            <dbReference type="DOI" id="10.1099/vir.0.82865-0"/>
        </citation>
        <scope>SUBCELLULAR LOCATION (MRNA-CAPPING ENZYME NSP1)</scope>
        <scope>PALMITOYLATION (MRNA-CAPPING ENZYME NSP1)</scope>
    </reference>
    <reference key="29">
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            <title>The Old World and New World alphaviruses use different virus-specific proteins for induction of transcriptional shutoff.</title>
            <authorList>
                <person name="Garmashova N."/>
                <person name="Gorchakov R."/>
                <person name="Volkova E."/>
                <person name="Paessler S."/>
                <person name="Frolova E."/>
                <person name="Frolov I."/>
            </authorList>
            <dbReference type="PubMed" id="17108023"/>
            <dbReference type="DOI" id="10.1128/JVI.02073-06"/>
        </citation>
        <scope>FUNCTION (PROTEASE NSP2)</scope>
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    <reference key="30">
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            <title>Evasion of the innate immune response: the Old World alphavirus nsP2 protein induces rapid degradation of Rpb1, a catalytic subunit of RNA polymerase II.</title>
            <authorList>
                <person name="Akhrymuk I."/>
                <person name="Kulemzin S.V."/>
                <person name="Frolova E.I."/>
            </authorList>
            <dbReference type="PubMed" id="22514352"/>
            <dbReference type="DOI" id="10.1128/JVI.00541-12"/>
        </citation>
        <scope>FUNCTION (PROTEASE NSP2)</scope>
    </reference>
    <reference key="31">
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            <title>Sequestration of G3BP coupled with efficient translation inhibits stress granules in Semliki Forest virus infection.</title>
            <authorList>
                <person name="Panas M.D."/>
                <person name="Varjak M."/>
                <person name="Lulla A."/>
                <person name="Eng K.E."/>
                <person name="Merits A."/>
                <person name="Karlsson Hedestam G.B."/>
                <person name="McInerney G.M."/>
            </authorList>
            <dbReference type="PubMed" id="23087212"/>
            <dbReference type="DOI" id="10.1091/mbc.E12-08-0619"/>
        </citation>
        <scope>FUNCTION (NON-STRUCTURAL PROTEIN 3)</scope>
        <scope>INTERACTION WITH HOST G3BP1 (NON-STRUCTURAL PROTEIN 3)</scope>
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            <title>The C-terminal repeat domains of nsP3 from the Old World alphaviruses bind directly to G3BP.</title>
            <authorList>
                <person name="Panas M.D."/>
                <person name="Ahola T."/>
                <person name="McInerney G.M."/>
            </authorList>
            <dbReference type="PubMed" id="24623412"/>
            <dbReference type="DOI" id="10.1128/JVI.00439-14"/>
        </citation>
        <scope>DOMAIN (NON-STRUCTURAL PROTEIN 3)</scope>
        <scope>INTERACTION WITH HOST G3BP1</scope>
    </reference>
    <reference key="33">
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            <title>Viral and cellular proteins containing FGDF motifs bind G3BP to block stress granule formation.</title>
            <authorList>
                <person name="Panas M.D."/>
                <person name="Schulte T."/>
                <person name="Thaa B."/>
                <person name="Sandalova T."/>
                <person name="Kedersha N."/>
                <person name="Achour A."/>
                <person name="McInerney G.M."/>
            </authorList>
            <dbReference type="PubMed" id="25658430"/>
            <dbReference type="DOI" id="10.1371/journal.ppat.1004659"/>
        </citation>
        <scope>DOMAIN (NON-STRUCTURAL PROTEIN 3)</scope>
        <scope>INTERACTION WITH HOST G3BP1 (NON-STRUCTURAL PROTEIN 3)</scope>
        <scope>MUTAGENESIS OF PHE-1787; GLY-1788; ASP-1789; PHE-1790; ASP-1791; THR-1803; PHE-1804; GLY-1805; ASP-1806; PHE-1807 AND ASP-1808</scope>
    </reference>
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            <title>Alphavirus polymerase and RNA replication.</title>
            <authorList>
                <person name="Pietilae M.K."/>
                <person name="Hellstroem K."/>
                <person name="Ahola T."/>
            </authorList>
            <dbReference type="PubMed" id="28104453"/>
            <dbReference type="DOI" id="10.1016/j.virusres.2017.01.007"/>
        </citation>
        <scope>REVIEW</scope>
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            <title>Timeliness of proteolytic events is prerequisite for efficient functioning of the alphaviral replicase.</title>
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                <person name="Lulla V."/>
                <person name="Karo-Astover L."/>
                <person name="Rausalu K."/>
                <person name="Saul S."/>
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                <person name="Lulla A."/>
            </authorList>
            <dbReference type="PubMed" id="29695431"/>
            <dbReference type="DOI" id="10.1128/JVI.00151-18"/>
        </citation>
        <scope>PROTEOLYTIC CLEAVAGE (POLYPROTEIN P1234)</scope>
    </reference>
    <reference key="36">
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            <title>Membrane binding mechanism of an RNA virus-capping enzyme.</title>
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                <person name="Lampio A."/>
                <person name="Kilpelainen I."/>
                <person name="Pesonen S."/>
                <person name="Karhi K."/>
                <person name="Auvinen P."/>
                <person name="Somerharju P."/>
                <person name="Kaeaeriaeinen L."/>
            </authorList>
            <dbReference type="PubMed" id="10984480"/>
            <dbReference type="DOI" id="10.1074/jbc.M004865200"/>
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        <scope>STRUCTURE BY NMR OF 245-264</scope>
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            <title>Combined structural, biochemical and cellular evidence demonstrates that both FGDF motifs in alphavirus nsP3 are required for efficient replication.</title>
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            <dbReference type="PubMed" id="27383630"/>
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        </citation>
        <scope>X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 1785-1809</scope>
        <scope>INTERACTION WITH HOST G3BP1 (NON-STRUCTURAL PROTEIN 3)</scope>
        <scope>DOMAIN (NON-STRUCTURAL PROTEIN 3)</scope>
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    <comment type="function">
        <molecule>Polyprotein P1234</molecule>
        <text evidence="4">Inactive precursor of the viral replicase, which is activated by cleavages carried out by the viral protease nsP2.</text>
    </comment>
    <comment type="function">
        <molecule>Polyprotein P123</molecule>
        <text evidence="2">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.</text>
    </comment>
    <comment type="function">
        <molecule>Polyprotein P123'</molecule>
        <text evidence="41">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.</text>
    </comment>
    <comment type="function">
        <molecule>mRNA-capping enzyme nsP1</molecule>
        <text evidence="2 4 35 41 44 50">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.</text>
    </comment>
    <comment type="function">
        <molecule>Protease nsP2</molecule>
        <text evidence="4 11 12 15 20 23 27 36 42 45">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.</text>
    </comment>
    <comment type="function">
        <molecule>Non-structural protein 3'</molecule>
        <text evidence="2 41">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.</text>
    </comment>
    <comment type="function">
        <molecule>Non-structural protein 3</molecule>
        <text evidence="2 4 28 31">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).</text>
    </comment>
    <comment type="function">
        <molecule>RNA-directed RNA polymerase nsP4</molecule>
        <text evidence="2">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.</text>
    </comment>
    <comment type="catalytic activity">
        <reaction evidence="3">
            <text>GTP + S-adenosyl-L-methionine = N(7)-methyl-GTP + S-adenosyl-L-homocysteine</text>
            <dbReference type="Rhea" id="RHEA:46948"/>
            <dbReference type="ChEBI" id="CHEBI:37565"/>
            <dbReference type="ChEBI" id="CHEBI:57856"/>
            <dbReference type="ChEBI" id="CHEBI:59789"/>
            <dbReference type="ChEBI" id="CHEBI:87133"/>
        </reaction>
    </comment>
    <comment type="catalytic activity">
        <reaction evidence="35">
            <text>[nsP1 protein]-L-histidine + N(7)-methyl-GTP = [nsP1 protein]-N(tele)-(N(7)-methylguanosine 5'-phospho)-L-histidine + diphosphate</text>
            <dbReference type="Rhea" id="RHEA:54792"/>
            <dbReference type="Rhea" id="RHEA-COMP:13994"/>
            <dbReference type="Rhea" id="RHEA-COMP:13995"/>
            <dbReference type="ChEBI" id="CHEBI:29979"/>
            <dbReference type="ChEBI" id="CHEBI:33019"/>
            <dbReference type="ChEBI" id="CHEBI:87133"/>
            <dbReference type="ChEBI" id="CHEBI:138334"/>
        </reaction>
        <physiologicalReaction direction="left-to-right" evidence="35">
            <dbReference type="Rhea" id="RHEA:54793"/>
        </physiologicalReaction>
    </comment>
    <comment type="catalytic activity">
        <reaction evidence="3">
            <text>[nsP1 protein]-N(tele)-(N(7)-methylguanosine 5'-phospho)-L-histidine + a 5'-end diphospho-(purine-ribonucleoside) in mRNA + H(+) = [nsP1 protein]-L-histidine + a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(purine-ribonucleoside) in mRNA</text>
            <dbReference type="Rhea" id="RHEA:54800"/>
            <dbReference type="Rhea" id="RHEA-COMP:12925"/>
            <dbReference type="Rhea" id="RHEA-COMP:13929"/>
            <dbReference type="Rhea" id="RHEA-COMP:13994"/>
            <dbReference type="Rhea" id="RHEA-COMP:13995"/>
            <dbReference type="ChEBI" id="CHEBI:15378"/>
            <dbReference type="ChEBI" id="CHEBI:29979"/>
            <dbReference type="ChEBI" id="CHEBI:133968"/>
            <dbReference type="ChEBI" id="CHEBI:138276"/>
            <dbReference type="ChEBI" id="CHEBI:138334"/>
        </reaction>
    </comment>
    <comment type="catalytic activity">
        <reaction evidence="12">
            <text>a 5'-end triphospho-(purine-ribonucleoside) in mRNA + H2O = a 5'-end diphospho-(purine-ribonucleoside) in mRNA + H(+) + phosphate</text>
            <dbReference type="Rhea" id="RHEA:11008"/>
            <dbReference type="Rhea" id="RHEA-COMP:13929"/>
            <dbReference type="Rhea" id="RHEA-COMP:13942"/>
            <dbReference type="ChEBI" id="CHEBI:15377"/>
            <dbReference type="ChEBI" id="CHEBI:15378"/>
            <dbReference type="ChEBI" id="CHEBI:43474"/>
            <dbReference type="ChEBI" id="CHEBI:138276"/>
            <dbReference type="ChEBI" id="CHEBI:138288"/>
            <dbReference type="EC" id="3.1.3.33"/>
        </reaction>
    </comment>
    <comment type="catalytic activity">
        <reaction evidence="36">
            <text>a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate</text>
            <dbReference type="Rhea" id="RHEA:23680"/>
            <dbReference type="ChEBI" id="CHEBI:15377"/>
            <dbReference type="ChEBI" id="CHEBI:15378"/>
            <dbReference type="ChEBI" id="CHEBI:43474"/>
            <dbReference type="ChEBI" id="CHEBI:57930"/>
            <dbReference type="ChEBI" id="CHEBI:61557"/>
            <dbReference type="EC" id="3.6.1.15"/>
        </reaction>
    </comment>
    <comment type="catalytic activity">
        <reaction evidence="11">
            <text>ATP + H2O = ADP + H(+) + phosphate</text>
            <dbReference type="Rhea" id="RHEA:13065"/>
            <dbReference type="ChEBI" id="CHEBI:15377"/>
            <dbReference type="ChEBI" id="CHEBI:15378"/>
            <dbReference type="ChEBI" id="CHEBI:30616"/>
            <dbReference type="ChEBI" id="CHEBI:43474"/>
            <dbReference type="ChEBI" id="CHEBI:456216"/>
            <dbReference type="EC" id="3.6.4.13"/>
        </reaction>
    </comment>
    <comment type="catalytic activity">
        <reaction evidence="6">
            <text>a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)</text>
            <dbReference type="Rhea" id="RHEA:21248"/>
            <dbReference type="Rhea" id="RHEA-COMP:14527"/>
            <dbReference type="Rhea" id="RHEA-COMP:17342"/>
            <dbReference type="ChEBI" id="CHEBI:33019"/>
            <dbReference type="ChEBI" id="CHEBI:61557"/>
            <dbReference type="ChEBI" id="CHEBI:140395"/>
            <dbReference type="EC" id="2.7.7.48"/>
        </reaction>
    </comment>
    <comment type="catalytic activity">
        <reaction evidence="2">
            <text>ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide</text>
            <dbReference type="Rhea" id="RHEA:11332"/>
            <dbReference type="Rhea" id="RHEA-COMP:14527"/>
            <dbReference type="Rhea" id="RHEA-COMP:17347"/>
            <dbReference type="ChEBI" id="CHEBI:30616"/>
            <dbReference type="ChEBI" id="CHEBI:33019"/>
            <dbReference type="ChEBI" id="CHEBI:140395"/>
            <dbReference type="ChEBI" id="CHEBI:173115"/>
            <dbReference type="EC" id="2.7.7.19"/>
        </reaction>
    </comment>
    <comment type="catalytic activity">
        <reaction evidence="4">
            <text>4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + H2O = ADP-D-ribose + H(+) + L-aspartyl-[protein]</text>
            <dbReference type="Rhea" id="RHEA:54428"/>
            <dbReference type="Rhea" id="RHEA-COMP:9867"/>
            <dbReference type="Rhea" id="RHEA-COMP:13832"/>
            <dbReference type="ChEBI" id="CHEBI:15377"/>
            <dbReference type="ChEBI" id="CHEBI:15378"/>
            <dbReference type="ChEBI" id="CHEBI:29961"/>
            <dbReference type="ChEBI" id="CHEBI:57967"/>
            <dbReference type="ChEBI" id="CHEBI:138102"/>
        </reaction>
        <physiologicalReaction direction="left-to-right" evidence="4">
            <dbReference type="Rhea" id="RHEA:54429"/>
        </physiologicalReaction>
    </comment>
    <comment type="catalytic activity">
        <reaction evidence="4">
            <text>5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + H2O = ADP-D-ribose + H(+) + L-glutamyl-[protein]</text>
            <dbReference type="Rhea" id="RHEA:58248"/>
            <dbReference type="Rhea" id="RHEA-COMP:10208"/>
            <dbReference type="Rhea" id="RHEA-COMP:15089"/>
            <dbReference type="ChEBI" id="CHEBI:15377"/>
            <dbReference type="ChEBI" id="CHEBI:15378"/>
            <dbReference type="ChEBI" id="CHEBI:29973"/>
            <dbReference type="ChEBI" id="CHEBI:57967"/>
            <dbReference type="ChEBI" id="CHEBI:142540"/>
        </reaction>
        <physiologicalReaction direction="left-to-right" evidence="4">
            <dbReference type="Rhea" id="RHEA:58249"/>
        </physiologicalReaction>
    </comment>
    <comment type="catalytic activity">
        <reaction evidence="4">
            <text>ADP-beta-D-ribose 1''-phosphate + H2O = ADP-D-ribose + phosphate</text>
            <dbReference type="Rhea" id="RHEA:25029"/>
            <dbReference type="ChEBI" id="CHEBI:15377"/>
            <dbReference type="ChEBI" id="CHEBI:43474"/>
            <dbReference type="ChEBI" id="CHEBI:57967"/>
            <dbReference type="ChEBI" id="CHEBI:58753"/>
            <dbReference type="EC" id="3.1.3.84"/>
        </reaction>
        <physiologicalReaction direction="left-to-right" evidence="4">
            <dbReference type="Rhea" id="RHEA:25030"/>
        </physiologicalReaction>
    </comment>
    <comment type="cofactor">
        <cofactor evidence="2">
            <name>Mg(2+)</name>
            <dbReference type="ChEBI" id="CHEBI:18420"/>
        </cofactor>
        <cofactor evidence="2">
            <name>Mn(2+)</name>
            <dbReference type="ChEBI" id="CHEBI:29035"/>
        </cofactor>
        <text evidence="2">For nsP4 adenylyltransferase activity; Mn(2+) supports catalysis at 60% of the levels observed with Mg(2+).</text>
    </comment>
    <comment type="cofactor">
        <cofactor evidence="2">
            <name>Mg(2+)</name>
            <dbReference type="ChEBI" id="CHEBI:18420"/>
        </cofactor>
        <text evidence="2">For nsP4 RNA-directed RNA polymerase activity.</text>
    </comment>
    <comment type="cofactor">
        <cofactor evidence="3">
            <name>Mg(2+)</name>
            <dbReference type="ChEBI" id="CHEBI:18420"/>
        </cofactor>
        <text evidence="3">For nsP1 guanylylation.</text>
    </comment>
    <comment type="cofactor">
        <cofactor>
            <name>Mg(2+)</name>
            <dbReference type="ChEBI" id="CHEBI:18420"/>
        </cofactor>
        <text evidence="4">For nsP2 RNA triphosphatase activity.</text>
    </comment>
    <comment type="cofactor">
        <cofactor>
            <name>Mg(2+)</name>
            <dbReference type="ChEBI" id="CHEBI:18420"/>
        </cofactor>
        <text evidence="4">For nsP2 NTPase activity.</text>
    </comment>
    <comment type="activity regulation">
        <molecule>Protease nsP2</molecule>
        <text evidence="16">Inhibited by N-ethylmaleimide, Zn(2+), and Cu2(2+).</text>
    </comment>
    <comment type="biophysicochemical properties">
        <kinetics>
            <KM evidence="12">2.99 mM for nsP2 RNA triphosphatase activity (at pH 8.0)</KM>
            <KM evidence="12">90 mM for nsP2 NTPase activity (at pH 7.5)</KM>
        </kinetics>
    </comment>
    <comment type="subunit">
        <molecule>mRNA-capping enzyme nsP1</molecule>
        <text evidence="2 3">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.</text>
    </comment>
    <comment type="subunit">
        <molecule>Non-structural protein 3</molecule>
        <text evidence="2 3 28 29 30 31">Interacts with mRNA-capping enzyme nsP1 (By similarity). Interacts with host DDX1 (By similarity). Interacts with host DDX3 (By similarity). Interacts (via C-terminus) with host G3BP1; this interaction inhibits the formation of host stress granules on viral mRNAs and the nsp3-G3BP1 complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes (PubMed:24623412, PubMed:23087212, PubMed:25658430, PubMed:27383630). 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.</text>
    </comment>
    <comment type="subunit">
        <molecule>RNA-directed RNA polymerase nsP4</molecule>
        <text evidence="2 3">Interacts with mRNA-capping enzyme nsP1 (By similarity). Interacts with protease nsP2 (By similarity). interacts with itself.</text>
    </comment>
    <comment type="subunit">
        <molecule>Protease nsP2</molecule>
        <text evidence="2 3">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.</text>
    </comment>
    <comment type="subcellular location">
        <molecule>Polyprotein P1234</molecule>
        <subcellularLocation>
            <location evidence="41">Host cytoplasmic vesicle membrane</location>
            <topology evidence="41">Peripheral membrane protein</topology>
        </subcellularLocation>
        <text evidence="41">Part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex.</text>
    </comment>
    <comment type="subcellular location">
        <molecule>Polyprotein P123'</molecule>
        <subcellularLocation>
            <location evidence="41">Host cytoplasmic vesicle membrane</location>
            <topology evidence="41">Peripheral membrane protein</topology>
        </subcellularLocation>
        <text evidence="41">Part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex.</text>
    </comment>
    <comment type="subcellular location">
        <molecule>Polyprotein P123</molecule>
        <subcellularLocation>
            <location evidence="41">Host cytoplasmic vesicle membrane</location>
            <topology evidence="41">Peripheral membrane protein</topology>
        </subcellularLocation>
        <text evidence="41">Part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex.</text>
    </comment>
    <comment type="subcellular location">
        <molecule>mRNA-capping enzyme nsP1</molecule>
        <subcellularLocation>
            <location evidence="49">Host cytoplasmic vesicle membrane</location>
            <topology evidence="44 51">Lipid-anchor</topology>
        </subcellularLocation>
        <subcellularLocation>
            <location evidence="24 34">Host cell membrane</location>
            <topology evidence="44 51">Lipid-anchor</topology>
            <orientation evidence="34">Cytoplasmic side</orientation>
        </subcellularLocation>
        <subcellularLocation>
            <location evidence="24 38">Host cell projection</location>
            <location evidence="24 38">Host filopodium</location>
        </subcellularLocation>
        <text evidence="24 38 40">In the late phase of infection, the polyprotein is quickly cleaved before localization to cellular membranes. Then a fraction of nsP1 localizes to the inner surface of the plasma membrane and its filopodial extensions. Only the palmitoylated nsP1 localizes to the host filopodia (PubMed:8910486, PubMed:17554031). NsP1 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 (PubMed:28104453).</text>
    </comment>
    <comment type="subcellular location">
        <molecule>Protease nsP2</molecule>
        <subcellularLocation>
            <location evidence="43">Host cytoplasmic vesicle membrane</location>
            <topology evidence="41">Peripheral membrane protein</topology>
        </subcellularLocation>
        <subcellularLocation>
            <location evidence="18 25 37">Host nucleus</location>
        </subcellularLocation>
        <subcellularLocation>
            <location evidence="37">Host cytoplasm</location>
        </subcellularLocation>
        <text evidence="3 37 40">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 (PubMed:8610462). Shuttles between cytoplasm and nucleus (By similarity). 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 (PubMed:28104453).</text>
    </comment>
    <comment type="subcellular location">
        <molecule>Non-structural protein 3</molecule>
        <subcellularLocation>
            <location evidence="2">Host cytoplasmic vesicle membrane</location>
            <topology evidence="41">Peripheral membrane protein</topology>
        </subcellularLocation>
        <text evidence="2">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).</text>
    </comment>
    <comment type="subcellular location">
        <molecule>Non-structural protein 3'</molecule>
        <subcellularLocation>
            <location evidence="2">Host cytoplasmic vesicle membrane</location>
            <topology evidence="41">Peripheral membrane protein</topology>
        </subcellularLocation>
        <text evidence="2">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).</text>
    </comment>
    <comment type="subcellular location">
        <molecule>RNA-directed RNA polymerase nsP4</molecule>
        <subcellularLocation>
            <location>Host cytoplasmic vesicle membrane</location>
            <topology evidence="32">Peripheral membrane protein</topology>
        </subcellularLocation>
        <text evidence="40">NsP4 is part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex.</text>
    </comment>
    <comment type="domain">
        <molecule>Protease nsP2</molecule>
        <text evidence="3 4">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.</text>
    </comment>
    <comment type="domain">
        <molecule>Non-structural protein 3</molecule>
        <text evidence="2 4 29 30 31">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).</text>
    </comment>
    <comment type="domain">
        <molecule>Non-structural protein 3'</molecule>
        <text evidence="2 4 46 47 48">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.</text>
    </comment>
    <comment type="PTM">
        <molecule>Polyprotein P1234</molecule>
        <text evidence="2 15 17 33">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.</text>
    </comment>
    <comment type="PTM">
        <molecule>Polyprotein P123'</molecule>
        <text evidence="15 17 33">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).</text>
    </comment>
    <comment type="PTM">
        <molecule>Polyprotein P123</molecule>
        <text evidence="15 17 33">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).</text>
    </comment>
    <comment type="PTM">
        <molecule>mRNA-capping enzyme nsP1</molecule>
        <text evidence="4 13 38">Palmitoylated by host palmitoyltransferases ZDHHC2 and ZDHHC19.</text>
    </comment>
    <comment type="PTM">
        <molecule>Non-structural protein 3</molecule>
        <text evidence="14">Phosphorylated by host on serines and threonines.</text>
    </comment>
    <comment type="PTM">
        <molecule>Non-structural protein 3'</molecule>
        <text evidence="14">Phosphorylated by host on serines and threonines.</text>
    </comment>
    <comment type="PTM">
        <molecule>RNA-directed RNA polymerase nsP4</molecule>
        <text evidence="2">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.</text>
    </comment>
    <comment type="miscellaneous">
        <text evidence="2 19 21">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.</text>
    </comment>
    <comment type="caution">
        <text evidence="1 4 26 41">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.</text>
    </comment>
    <dbReference type="EC" id="2.1.1.-" evidence="3"/>
    <dbReference type="EC" id="2.7.7.-" evidence="3"/>
    <dbReference type="EC" id="3.1.3.33" evidence="12"/>
    <dbReference type="EC" id="3.4.22.-" evidence="4"/>
    <dbReference type="EC" id="3.6.1.15" evidence="36"/>
    <dbReference type="EC" id="3.6.4.13" evidence="11"/>
    <dbReference type="EC" id="3.1.3.84" evidence="4"/>
    <dbReference type="EC" id="2.7.7.19" evidence="2"/>
    <dbReference type="EC" id="2.7.7.48" evidence="6"/>
    <dbReference type="EMBL" id="X04129">
        <property type="protein sequence ID" value="CAA27741.1"/>
        <property type="molecule type" value="Genomic_RNA"/>
    </dbReference>
    <dbReference type="EMBL" id="AJ251359">
        <property type="protein sequence ID" value="CAB62256.1"/>
        <property type="molecule type" value="Genomic_RNA"/>
    </dbReference>
    <dbReference type="EMBL" id="AY112987">
        <property type="protein sequence ID" value="AAM64226.1"/>
        <property type="molecule type" value="Genomic_RNA"/>
    </dbReference>
    <dbReference type="EMBL" id="DQ189079">
        <property type="protein sequence ID" value="ABA29023.1"/>
        <property type="molecule type" value="Genomic_RNA"/>
    </dbReference>
    <dbReference type="EMBL" id="DQ189080">
        <property type="protein sequence ID" value="ABA29024.1"/>
        <property type="molecule type" value="Genomic_RNA"/>
    </dbReference>
    <dbReference type="EMBL" id="DQ189081">
        <property type="protein sequence ID" value="ABA29025.1"/>
        <property type="molecule type" value="Genomic_RNA"/>
    </dbReference>
    <dbReference type="EMBL" id="DQ189082">
        <property type="protein sequence ID" value="ABA29026.1"/>
        <property type="molecule type" value="Genomic_RNA"/>
    </dbReference>
    <dbReference type="EMBL" id="DQ189083">
        <property type="protein sequence ID" value="ABA29028.1"/>
        <property type="molecule type" value="Genomic_RNA"/>
    </dbReference>
    <dbReference type="EMBL" id="DQ189084">
        <property type="protein sequence ID" value="ABA29029.1"/>
        <property type="molecule type" value="Genomic_RNA"/>
    </dbReference>
    <dbReference type="EMBL" id="DQ189085">
        <property type="protein sequence ID" value="ABA29031.1"/>
        <property type="molecule type" value="Genomic_RNA"/>
    </dbReference>
    <dbReference type="EMBL" id="DQ189086">
        <property type="protein sequence ID" value="ABA29032.1"/>
        <property type="molecule type" value="Genomic_RNA"/>
    </dbReference>
    <dbReference type="EMBL" id="EU350586">
        <property type="protein sequence ID" value="ACB12687.1"/>
        <property type="molecule type" value="Genomic_RNA"/>
    </dbReference>
    <dbReference type="PIR" id="A23592">
        <property type="entry name" value="MNWVSF"/>
    </dbReference>
    <dbReference type="RefSeq" id="NP_463457.1">
        <property type="nucleotide sequence ID" value="NC_003215.1"/>
    </dbReference>
    <dbReference type="PDB" id="1FW5">
        <property type="method" value="NMR"/>
        <property type="chains" value="A=245-264"/>
    </dbReference>
    <dbReference type="PDB" id="5DRV">
        <property type="method" value="X-ray"/>
        <property type="resolution" value="2.75 A"/>
        <property type="chains" value="B=1785-1792"/>
    </dbReference>
    <dbReference type="PDB" id="5FW5">
        <property type="method" value="X-ray"/>
        <property type="resolution" value="1.92 A"/>
        <property type="chains" value="C=1785-1809"/>
    </dbReference>
    <dbReference type="PDBsum" id="1FW5"/>
    <dbReference type="PDBsum" id="5DRV"/>
    <dbReference type="PDBsum" id="5FW5"/>
    <dbReference type="SMR" id="P08411"/>
    <dbReference type="ELM" id="P08411"/>
    <dbReference type="IntAct" id="P08411">
        <property type="interactions" value="2"/>
    </dbReference>
    <dbReference type="MEROPS" id="C09.001"/>
    <dbReference type="iPTMnet" id="P08411"/>
    <dbReference type="SwissPalm" id="P08411"/>
    <dbReference type="PRIDE" id="P08411"/>
    <dbReference type="GeneID" id="922350"/>
    <dbReference type="KEGG" id="vg:922350"/>
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        <property type="organism ID" value="5671"/>
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        <property type="project" value="RHEA"/>
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        <property type="project" value="InterPro"/>
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    <dbReference type="GO" id="GO:0004651">
        <property type="term" value="F:polynucleotide 5'-phosphatase activity"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-EC"/>
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    <dbReference type="GO" id="GO:0004652">
        <property type="term" value="F:polynucleotide adenylyltransferase activity"/>
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        <property type="project" value="UniProtKB-EC"/>
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        <property type="project" value="UniProtKB-KW"/>
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    <dbReference type="GO" id="GO:0003724">
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        <property type="project" value="UniProtKB-EC"/>
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    <dbReference type="GO" id="GO:0003968">
        <property type="term" value="F:RNA-directed 5'-3' RNA polymerase activity"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-KW"/>
    </dbReference>
    <dbReference type="GO" id="GO:0006370">
        <property type="term" value="P:7-methylguanosine mRNA capping"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-KW"/>
    </dbReference>
    <dbReference type="GO" id="GO:0006508">
        <property type="term" value="P:proteolysis"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-KW"/>
    </dbReference>
    <dbReference type="GO" id="GO:0039563">
        <property type="term" value="P:suppression by virus of host JAK-STAT cascade via inhibition of STAT1 activity"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-KW"/>
    </dbReference>
    <dbReference type="GO" id="GO:0039523">
        <property type="term" value="P:suppression by virus of host mRNA transcription via inhibition of RNA polymerase II activity"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-KW"/>
    </dbReference>
    <dbReference type="GO" id="GO:0039502">
        <property type="term" value="P:suppression by virus of host type I interferon-mediated signaling pathway"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-KW"/>
    </dbReference>
    <dbReference type="GO" id="GO:0006351">
        <property type="term" value="P:transcription, DNA-templated"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="InterPro"/>
    </dbReference>
    <dbReference type="GO" id="GO:0039694">
        <property type="term" value="P:viral RNA genome replication"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="InterPro"/>
    </dbReference>
    <dbReference type="CDD" id="cd21557">
        <property type="entry name" value="Macro_X_Nsp3-like"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="Gene3D" id="3.40.220.10">
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="Gene3D" id="3.40.50.150">
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="Gene3D" id="3.40.50.300">
        <property type="match status" value="2"/>
    </dbReference>
    <dbReference type="Gene3D" id="3.90.70.110">
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR027351">
        <property type="entry name" value="(+)RNA_virus_helicase_core_dom"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR002588">
        <property type="entry name" value="Alphavirus-like_MT_dom"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR002620">
        <property type="entry name" value="Alphavirus_nsp2pro"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR044936">
        <property type="entry name" value="Alphavirus_nsp2pro_sf"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR043502">
        <property type="entry name" value="DNA/RNA_pol_sf"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR002589">
        <property type="entry name" value="Macro_dom"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR043472">
        <property type="entry name" value="Macro_dom-like"/>
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    <dbReference type="InterPro" id="IPR044371">
        <property type="entry name" value="Macro_X_NSP3-like"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR027417">
        <property type="entry name" value="P-loop_NTPase"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR007094">
        <property type="entry name" value="RNA-dir_pol_PSvirus"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR029063">
        <property type="entry name" value="SAM-dependent_MTases_sf"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR001788">
        <property type="entry name" value="Tymovirus_RNA-dep_RNA_pol"/>
    </dbReference>
    <dbReference type="Pfam" id="PF01661">
        <property type="entry name" value="Macro"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="Pfam" id="PF01707">
        <property type="entry name" value="Peptidase_C9"/>
        <property type="match status" value="1"/>
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    <dbReference type="Pfam" id="PF00978">
        <property type="entry name" value="RdRP_2"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="Pfam" id="PF01443">
        <property type="entry name" value="Viral_helicase1"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="Pfam" id="PF01660">
        <property type="entry name" value="Vmethyltransf"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="SMART" id="SM00506">
        <property type="entry name" value="A1pp"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="SUPFAM" id="SSF52540">
        <property type="entry name" value="SSF52540"/>
        <property type="match status" value="1"/>
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    <dbReference type="SUPFAM" id="SSF52949">
        <property type="entry name" value="SSF52949"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="SUPFAM" id="SSF56672">
        <property type="entry name" value="SSF56672"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="PROSITE" id="PS51743">
        <property type="entry name" value="ALPHAVIRUS_MT"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="PROSITE" id="PS51154">
        <property type="entry name" value="MACRO"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="PROSITE" id="PS51520">
        <property type="entry name" value="NSP2PRO"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="PROSITE" id="PS51657">
        <property type="entry name" value="PSRV_HELICASE"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="PROSITE" id="PS50507">
        <property type="entry name" value="RDRP_SSRNA_POS"/>
        <property type="match status" value="1"/>
    </dbReference>
    <proteinExistence type="evidence at protein level"/>
    <keyword id="KW-0002">3D-structure</keyword>
    <keyword id="KW-0067">ATP-binding</keyword>
    <keyword id="KW-1262">Eukaryotic host gene expression shutoff by virus</keyword>
    <keyword id="KW-1191">Eukaryotic host transcription shutoff by virus</keyword>
    <keyword id="KW-0342">GTP-binding</keyword>
    <keyword id="KW-0347">Helicase</keyword>
    <keyword id="KW-1032">Host cell membrane</keyword>
    <keyword id="KW-1034">Host cell projection</keyword>
    <keyword id="KW-1035">Host cytoplasm</keyword>
    <keyword id="KW-1036">Host cytoplasmic vesicle</keyword>
    <keyword id="KW-1190">Host gene expression shutoff by virus</keyword>
    <keyword id="KW-1043">Host membrane</keyword>
    <keyword id="KW-1048">Host nucleus</keyword>
    <keyword id="KW-0945">Host-virus interaction</keyword>
    <keyword id="KW-0378">Hydrolase</keyword>
    <keyword id="KW-1090">Inhibition of host innate immune response by virus</keyword>
    <keyword id="KW-1114">Inhibition of host interferon signaling pathway by virus</keyword>
    <keyword id="KW-1104">Inhibition of host RNA polymerase II by virus</keyword>
    <keyword id="KW-1105">Inhibition of host STAT1 by virus</keyword>
    <keyword id="KW-0449">Lipoprotein</keyword>
    <keyword id="KW-0472">Membrane</keyword>
    <keyword id="KW-0479">Metal-binding</keyword>
    <keyword id="KW-0489">Methyltransferase</keyword>
    <keyword id="KW-0506">mRNA capping</keyword>
    <keyword id="KW-0507">mRNA processing</keyword>
    <keyword id="KW-0511">Multifunctional enzyme</keyword>
    <keyword id="KW-0547">Nucleotide-binding</keyword>
    <keyword id="KW-0548">Nucleotidyltransferase</keyword>
    <keyword id="KW-0564">Palmitate</keyword>
    <keyword id="KW-0597">Phosphoprotein</keyword>
    <keyword id="KW-0645">Protease</keyword>
    <keyword id="KW-1185">Reference proteome</keyword>
    <keyword id="KW-1159">RNA suppression of termination</keyword>
    <keyword id="KW-0694">RNA-binding</keyword>
    <keyword id="KW-0696">RNA-directed RNA polymerase</keyword>
    <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
    <keyword id="KW-0788">Thiol protease</keyword>
    <keyword id="KW-0808">Transferase</keyword>
    <keyword id="KW-0832">Ubl conjugation</keyword>
    <keyword id="KW-0899">Viral immunoevasion</keyword>
    <keyword id="KW-0693">Viral RNA replication</keyword>
    <keyword id="KW-0862">Zinc</keyword>
    <feature type="chain" id="PRO_0000308403" description="Polyprotein P1234">
        <location>
            <begin position="1"/>
            <end position="2432"/>
        </location>
    </feature>
    <feature type="chain" id="PRO_0000227770" description="Polyprotein P123'">
        <location>
            <begin position="1"/>
            <end position="1818"/>
        </location>
    </feature>
    <feature type="chain" id="PRO_0000446657" description="Polyprotein P123">
        <location>
            <begin position="1"/>
            <end position="1811"/>
        </location>
    </feature>
    <feature type="chain" id="PRO_0000041228" description="mRNA-capping enzyme nsP1">
        <location>
            <begin position="1"/>
            <end position="537"/>
        </location>
    </feature>
    <feature type="chain" id="PRO_0000041229" description="Protease nsP2">
        <location>
            <begin position="538"/>
            <end position="1336"/>
        </location>
    </feature>
    <feature type="chain" id="PRO_0000041230" description="Non-structural protein 3'">
        <location>
            <begin position="1337"/>
            <end position="1818"/>
        </location>
    </feature>
    <feature type="chain" id="PRO_0000446658" description="Non-structural protein 3">
        <location>
            <begin position="1337"/>
            <end position="1811"/>
        </location>
    </feature>
    <feature type="chain" id="PRO_0000041231" description="RNA-directed RNA polymerase nsP4">
        <location>
            <begin position="1819"/>
            <end position="2431"/>
        </location>
    </feature>
    <feature type="domain" description="Alphavirus-like MT" evidence="9">
        <location>
            <begin position="29"/>
            <end position="260"/>
        </location>
    </feature>
    <feature type="domain" description="(+)RNA virus helicase ATP-binding" evidence="8">
        <location>
            <begin position="692"/>
            <end position="844"/>
        </location>
    </feature>
    <feature type="domain" description="(+)RNA virus helicase C-terminal" evidence="8">
        <location>
            <begin position="845"/>
            <end position="993"/>
        </location>
    </feature>
    <feature type="domain" description="Peptidase C9" evidence="7">
        <location>
            <begin position="1006"/>
            <end position="1329"/>
        </location>
    </feature>
    <feature type="domain" description="Macro" evidence="5">
        <location>
            <begin position="1337"/>
            <end position="1495"/>
        </location>
    </feature>
    <feature type="domain" description="RdRp catalytic" evidence="6">
        <location>
            <begin position="2182"/>
            <end position="2297"/>
        </location>
    </feature>
    <feature type="region of interest" description="NsP1 membrane-binding" evidence="22">
        <location>
            <begin position="245"/>
            <end position="264"/>
        </location>
    </feature>
    <feature type="region of interest" description="Nucleolus localization signal" evidence="18">
        <location>
            <begin position="1007"/>
            <end position="1026"/>
        </location>
    </feature>
    <feature type="region of interest" description="Disordered" evidence="10">
        <location>
            <begin position="1759"/>
            <end position="1779"/>
        </location>
    </feature>
    <feature type="short sequence motif" description="Nuclear export signal" evidence="3">
        <location>
            <begin position="1060"/>
            <end position="1069"/>
        </location>
    </feature>
    <feature type="short sequence motif" description="Nuclear localization signal" evidence="25 37">
        <location>
            <begin position="1184"/>
            <end position="1188"/>
        </location>
    </feature>
    <feature type="short sequence motif" description="FGDF; binding to host G3BP1" evidence="30 46">
        <location>
            <begin position="1787"/>
            <end position="1790"/>
        </location>
    </feature>
    <feature type="short sequence motif" description="FGDF; binding to host G3BP1" evidence="30 46">
        <location>
            <begin position="1804"/>
            <end position="1807"/>
        </location>
    </feature>
    <feature type="active site" description="For cysteine protease nsP2 activity" evidence="7">
        <location>
            <position position="1015"/>
        </location>
    </feature>
    <feature type="active site" description="For cysteine protease nsP2 activity" evidence="7">
        <location>
            <position position="1085"/>
        </location>
    </feature>
    <feature type="binding site" evidence="8">
        <location>
            <begin position="723"/>
            <end position="730"/>
        </location>
        <ligand>
            <name>a ribonucleoside 5'-triphosphate</name>
            <dbReference type="ChEBI" id="CHEBI:61557"/>
        </ligand>
    </feature>
    <feature type="binding site" evidence="4">
        <location>
            <position position="1346"/>
        </location>
        <ligand>
            <name>ADP-D-ribose</name>
            <dbReference type="ChEBI" id="CHEBI:57967"/>
        </ligand>
    </feature>
    <feature type="binding site" evidence="4">
        <location>
            <position position="1360"/>
        </location>
        <ligand>
            <name>ADP-D-ribose</name>
            <dbReference type="ChEBI" id="CHEBI:57967"/>
        </ligand>
    </feature>
    <feature type="binding site" evidence="4">
        <location>
            <position position="1368"/>
        </location>
        <ligand>
            <name>ADP-D-ribose</name>
            <dbReference type="ChEBI" id="CHEBI:57967"/>
        </ligand>
    </feature>
    <feature type="binding site" evidence="4">
        <location>
            <position position="1448"/>
        </location>
        <ligand>
            <name>ADP-D-ribose</name>
            <dbReference type="ChEBI" id="CHEBI:57967"/>
        </ligand>
    </feature>
    <feature type="binding site" evidence="4">
        <location>
            <position position="1449"/>
        </location>
        <ligand>
            <name>ADP-D-ribose</name>
            <dbReference type="ChEBI" id="CHEBI:57967"/>
        </ligand>
    </feature>
    <feature type="binding site" evidence="4">
        <location>
            <position position="1450"/>
        </location>
        <ligand>
            <name>ADP-D-ribose</name>
            <dbReference type="ChEBI" id="CHEBI:57967"/>
        </ligand>
    </feature>
    <feature type="binding site" evidence="2">
        <location>
            <position position="1598"/>
        </location>
        <ligand>
            <name>Zn(2+)</name>
            <dbReference type="ChEBI" id="CHEBI:29105"/>
        </ligand>
    </feature>
    <feature type="binding site" evidence="2">
        <location>
            <position position="1600"/>
        </location>
        <ligand>
            <name>Zn(2+)</name>
            <dbReference type="ChEBI" id="CHEBI:29105"/>
        </ligand>
    </feature>
    <feature type="binding site" evidence="2">
        <location>
            <position position="1623"/>
        </location>
        <ligand>
            <name>Zn(2+)</name>
            <dbReference type="ChEBI" id="CHEBI:29105"/>
        </ligand>
    </feature>
    <feature type="binding site" evidence="2">
        <location>
            <position position="1641"/>
        </location>
        <ligand>
            <name>Zn(2+)</name>
            <dbReference type="ChEBI" id="CHEBI:29105"/>
        </ligand>
    </feature>
    <feature type="site" description="Involved in the phosphoramide link with 7-methyl-GMP" evidence="3">
        <location>
            <position position="38"/>
        </location>
    </feature>
    <feature type="site" description="Cleavage; by protease nsP2" evidence="2">
        <location>
            <begin position="537"/>
            <end position="538"/>
        </location>
    </feature>
    <feature type="site" description="Cleavage; by protease nsP2" evidence="2">
        <location>
            <begin position="1336"/>
            <end position="1337"/>
        </location>
    </feature>
    <feature type="site" description="Cleavage; by protease nsP2" evidence="4">
        <location>
            <begin position="1818"/>
            <end position="1819"/>
        </location>
    </feature>
    <feature type="modified residue" description="Phosphothreonine; by host" evidence="14">
        <location>
            <position position="1680"/>
        </location>
    </feature>
    <feature type="modified residue" description="Phosphothreonine; by host" evidence="14">
        <location>
            <position position="1681"/>
        </location>
    </feature>
    <feature type="lipid moiety-binding region" description="S-palmitoyl cysteine; by host" evidence="13 38">
        <location>
            <position position="418"/>
        </location>
    </feature>
    <feature type="lipid moiety-binding region" description="S-palmitoyl cysteine; by host" evidence="13 38">
        <location>
            <position position="420"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate L10.">
        <original>H</original>
        <variation>Y</variation>
        <location>
            <position position="6"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate Garoff/Takkinen.">
        <original>VC</original>
        <variation>DS</variation>
        <location>
            <begin position="95"/>
            <end position="96"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate Ts14.">
        <original>D</original>
        <variation>N</variation>
        <location>
            <position position="119"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate L10.">
        <original>E</original>
        <variation>K</variation>
        <location>
            <position position="311"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate Me Tri virus." evidence="26">
        <original>R</original>
        <variation>K</variation>
        <location>
            <position position="427"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate Me Tri virus." evidence="26">
        <original>K</original>
        <variation>E</variation>
        <location>
            <position position="470"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate Me Tri virus." evidence="26">
        <original>I</original>
        <variation>M</variation>
        <location>
            <position position="482"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate Ts10.">
        <original>E</original>
        <variation>D</variation>
        <location>
            <position position="529"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate Garoff/Takkinen.">
        <original>R</original>
        <variation>G</variation>
        <location>
            <position position="596"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate Me Tri virus." evidence="26">
        <original>H</original>
        <variation>Y</variation>
        <location>
            <position position="761"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate Garoff/Takkinen.">
        <original>LDIQAKTV</original>
        <variation>KGTSRENS</variation>
        <location>
            <begin position="764"/>
            <end position="771"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate L10.">
        <original>LDIQAKTV</original>
        <variation>NWTSRKNS</variation>
        <location>
            <begin position="764"/>
            <end position="771"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate L10.">
        <original>D</original>
        <variation>N</variation>
        <location>
            <position position="817"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate L10.">
        <original>M</original>
        <variation>T</variation>
        <location>
            <position position="826"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate L10.">
        <original>H</original>
        <variation>N</variation>
        <location>
            <position position="843"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate Ts1.">
        <original>S</original>
        <variation>N</variation>
        <location>
            <position position="845"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate L10.">
        <original>S</original>
        <variation>C</variation>
        <location>
            <position position="859"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate Ts13.">
        <original>T</original>
        <variation>S</variation>
        <location>
            <position position="869"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate Garoff/Takkinen.">
        <original>V</original>
        <variation>A</variation>
        <location>
            <position position="901"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate Me Tri virus." evidence="26">
        <original>T</original>
        <variation>M</variation>
        <location>
            <position position="981"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate Me Tri virus." evidence="26">
        <original>V</original>
        <variation>E</variation>
        <location>
            <position position="1052"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate Ts11.">
        <original>G</original>
        <variation>R</variation>
        <location>
            <position position="1114"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate Ts6.">
        <original>A</original>
        <variation>T</variation>
        <location>
            <position position="1199"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate Garoff/Takkinen and Isolate L10.">
        <original>SL</original>
        <variation>I</variation>
        <location>
            <begin position="1258"/>
            <end position="1259"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate L10 clone SFV4.">
        <original>A</original>
        <variation>E</variation>
        <location>
            <position position="1384"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate Me Tri virus." evidence="26">
        <original>A</original>
        <variation>G</variation>
        <location>
            <position position="1406"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate Garoff/Takkinen.">
        <original>Q</original>
        <variation>R</variation>
        <location>
            <position position="1565"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate Garoff/Takkinen.">
        <original>R</original>
        <variation>G</variation>
        <location>
            <position position="1579"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate Garoff/Takkinen, Isolate L10 and Isolate L10 clone SFV4.">
        <original>G</original>
        <variation>V</variation>
        <location>
            <position position="1644"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate Garoff/Takkinen.">
        <original>E</original>
        <variation>Q</variation>
        <location>
            <position position="1849"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate L10.">
        <original>P</original>
        <variation>R</variation>
        <location>
            <position position="1921"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate L10.">
        <original>V</original>
        <variation>A</variation>
        <location>
            <position position="1938"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate Ts13.">
        <original>A</original>
        <variation>V</variation>
        <location>
            <position position="2060"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate L10.">
        <original>A</original>
        <variation>D</variation>
        <location>
            <position position="2088"/>
        </location>
    </feature>
    <feature type="sequence variant" description="In strain: Isolate Garoff/Takkinen.">
        <original>A</original>
        <variation>T</variation>
        <location>
            <position position="2405"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Complete loss of guanylyltransferase and guanine-7-methyl transferase activity in vitro." evidence="39">
        <original>L</original>
        <variation>E</variation>
        <location>
            <position position="19"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Complete loss of guanylyltransferase and guanine-7-methyl transferase activity in vitro." evidence="39">
        <original>H</original>
        <variation>A</variation>
        <location>
            <position position="38"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="60% increase of guanine-7-methyl transferase activity in vitro. Complete loss of guanylyltransferase activity in vitro." evidence="39">
        <original>D</original>
        <variation>A</variation>
        <location>
            <position position="64"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="60% loss of guanine-7-methyl transferase activity and complete loss of guanylyltransferase activity in vitro." evidence="39">
        <original>CVC</original>
        <variation>AVA</variation>
        <location>
            <begin position="81"/>
            <end position="83"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Complete loss of guanylyltransferase and guanine-7-methyl transferase activity in vitro." evidence="39">
        <original>D</original>
        <variation>A</variation>
        <location>
            <position position="90"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Complete loss of guanylyltransferase and guanine-7-methyl transferase activity in vitro." evidence="39">
        <original>R</original>
        <variation>A</variation>
        <location>
            <position position="93"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="90% loss of guanine-7-methyl transferase activity and complete loss of guanylyltransferase activity in vitro." evidence="39">
        <original>C</original>
        <variation>A</variation>
        <location>
            <position position="135"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Complete loss of guanylyltransferase and guanine-7-methyl transferase activity in vitro." evidence="39">
        <original>C</original>
        <variation>A</variation>
        <location>
            <position position="142"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="No effect on guanylyltransferase and guanine-7-methyl transferase activity in vitro." evidence="39">
        <original>D</original>
        <variation>A</variation>
        <location>
            <position position="153"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="50% loss of guanine-7-methyl transferase activity and no effect on guanylyltransferase activity in vitro." evidence="39">
        <original>K</original>
        <variation>A</variation>
        <location>
            <position position="169"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="No effect on guanine-7-methyl transferase activity in vitro." evidence="39">
        <original>D</original>
        <variation>A</variation>
        <location>
            <position position="180"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="No effect on guanylyltransferase and guanine-7-methyl transferase activity in vitro." evidence="39">
        <original>E</original>
        <variation>A</variation>
        <location>
            <position position="203"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="90% loss of guanylyltransferase and guanine-7-methyl transferase activity in vitro." evidence="39">
        <original>C</original>
        <variation>A</variation>
        <location>
            <position position="214"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="97% loss of guanine-7-methyl transferase activity and complete loss of guanylyltransferase activity in vitro." evidence="39">
        <original>Y</original>
        <variation>A</variation>
        <location>
            <position position="249"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Nsp1 accumulates in the cytoplasm and is poorly palmitoylated." evidence="22">
        <original>R</original>
        <variation>A</variation>
        <location>
            <position position="253"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Nsp1 accumulates in the cytoplasm and is poorly palmitoylated." evidence="22">
        <original>W</original>
        <variation>A</variation>
        <location>
            <position position="259"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="95% loss of guanine-7-methyl transferase activity and 98% loss of guanylyltransferase activity in vitro." evidence="39">
        <original>K</original>
        <variation>A</variation>
        <location>
            <position position="317"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Complete loss of palmitoylation. Complete loss of pathogenicity in mice." evidence="13 38">
        <original>CCC</original>
        <variation>AAA</variation>
        <location>
            <begin position="418"/>
            <end position="420"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Complete loss of NTPase and helicase activity." evidence="11 12 36">
        <original>K</original>
        <variation>N</variation>
        <location>
            <position position="729"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Complete loss of polyprotein processing." evidence="15">
        <original>C</original>
        <variation>A</variation>
        <location>
            <position position="1015"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Complete loss of nuclear localization for nsP2." evidence="37">
        <original>R</original>
        <variation>D</variation>
        <location>
            <position position="1186"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Complete loss of threonine phosphorylation." evidence="14">
        <original>T</original>
        <variation>A</variation>
        <location>
            <position position="1680"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Complete loss of threonine phosphorylation." evidence="14">
        <original>T</original>
        <variation>A</variation>
        <location>
            <position position="1681"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Weak interaction with host G3BP1." evidence="30">
        <original>T</original>
        <variation>A</variation>
        <location>
            <position position="1786"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Complete loss of interaction with host G3BP1." evidence="30">
        <original>F</original>
        <variation>A</variation>
        <location>
            <position position="1787"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Complete loss of interaction with host G3BP1." evidence="30">
        <original>G</original>
        <variation>A</variation>
        <location>
            <position position="1788"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Complete loss of interaction with host G3BP1." evidence="30">
        <original>D</original>
        <variation>A</variation>
        <location>
            <position position="1789"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Complete loss of interaction with host G3BP1." evidence="30">
        <original>F</original>
        <variation>A</variation>
        <location>
            <position position="1790"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="No loss of interaction with host G3BP1." evidence="30">
        <original>D</original>
        <variation>A</variation>
        <location>
            <position position="1791"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Weak interaction with host G3BP1." evidence="30">
        <original>T</original>
        <variation>A</variation>
        <location>
            <position position="1803"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Complete loss of interaction with host G3BP1." evidence="30">
        <original>F</original>
        <variation>A</variation>
        <location>
            <position position="1804"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Complete loss of interaction with host G3BP1." evidence="30">
        <original>G</original>
        <variation>A</variation>
        <location>
            <position position="1805"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Complete loss of interaction with host G3BP1." evidence="30">
        <original>D</original>
        <variation>A</variation>
        <location>
            <position position="1806"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="Complete loss of interaction with host G3BP1." evidence="30">
        <original>F</original>
        <variation>A</variation>
        <location>
            <position position="1807"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="No loss of interaction with host G3BP1." evidence="30">
        <original>D</original>
        <variation>A</variation>
        <location>
            <position position="1808"/>
        </location>
    </feature>
    <feature type="mutagenesis site" description="No effect on polyprotein processing." evidence="15">
        <original>D</original>
        <variation>A</variation>
        <location>
            <position position="1824"/>
        </location>
    </feature>
    <feature type="sequence conflict" description="In Ref. 5; ACB12687." evidence="41" ref="5">
        <original>F</original>
        <variation>L</variation>
        <location>
            <position position="1537"/>
        </location>
    </feature>
    <feature type="sequence conflict" description="In Ref. 5; ACB12687." evidence="41" ref="5">
        <original>T</original>
        <variation>S</variation>
        <location>
            <position position="1591"/>
        </location>
    </feature>
    <feature type="sequence conflict" description="In Ref. 5; ACB12687." evidence="41" ref="5">
        <original>G</original>
        <variation>V</variation>
        <location>
            <position position="1644"/>
        </location>
    </feature>
    <feature type="helix" evidence="53">
        <location>
            <begin position="246"/>
            <end position="259"/>
        </location>
    </feature>
    <feature type="strand" evidence="54">
        <location>
            <begin position="1786"/>
            <end position="1789"/>
        </location>
    </feature>
    <feature type="helix" evidence="55">
        <location>
            <begin position="1794"/>
            <end position="1799"/>
        </location>
    </feature>
    <evidence type="ECO:0000250" key="1">
        <source>
            <dbReference type="UniProtKB" id="O90368"/>
        </source>
    </evidence>
    <evidence type="ECO:0000250" key="2">
        <source>
            <dbReference type="UniProtKB" id="P03317"/>
        </source>
    </evidence>
    <evidence type="ECO:0000250" key="3">
        <source>
            <dbReference type="UniProtKB" id="P27282"/>
        </source>
    </evidence>
    <evidence type="ECO:0000250" key="4">
        <source>
            <dbReference type="UniProtKB" id="Q8JUX6"/>
        </source>
    </evidence>
    <evidence type="ECO:0000255" key="5">
        <source>
            <dbReference type="PROSITE-ProRule" id="PRU00490"/>
        </source>
    </evidence>
    <evidence type="ECO:0000255" key="6">
        <source>
            <dbReference type="PROSITE-ProRule" id="PRU00539"/>
        </source>
    </evidence>
    <evidence type="ECO:0000255" key="7">
        <source>
            <dbReference type="PROSITE-ProRule" id="PRU00853"/>
        </source>
    </evidence>
    <evidence type="ECO:0000255" key="8">
        <source>
            <dbReference type="PROSITE-ProRule" id="PRU00990"/>
        </source>
    </evidence>
    <evidence type="ECO:0000255" key="9">
        <source>
            <dbReference type="PROSITE-ProRule" id="PRU01079"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="10">
        <source>
            <dbReference type="SAM" id="MobiDB-lite"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="11">
        <source>
            <dbReference type="PubMed" id="10217401"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="12">
        <source>
            <dbReference type="PubMed" id="10748213"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="13">
        <source>
            <dbReference type="PubMed" id="10888610"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="14">
        <source>
            <dbReference type="PubMed" id="11104756"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="15">
        <source>
            <dbReference type="PubMed" id="11257180"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="16">
        <source>
            <dbReference type="PubMed" id="11410598"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="17">
        <source>
            <dbReference type="PubMed" id="12917405"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="18">
        <source>
            <dbReference type="PubMed" id="1386484"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="19">
        <source>
            <dbReference type="PubMed" id="15930128"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="20">
        <source>
            <dbReference type="PubMed" id="16352561"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="21">
        <source>
            <dbReference type="PubMed" id="16391235"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="22">
        <source>
            <dbReference type="PubMed" id="17093195"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="23">
        <source>
            <dbReference type="PubMed" id="17108023"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="24">
        <source>
            <dbReference type="PubMed" id="17554031"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="25">
        <source>
            <dbReference type="PubMed" id="17652399"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="26">
        <source>
            <dbReference type="PubMed" id="18753222"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="27">
        <source>
            <dbReference type="PubMed" id="22514352"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="28">
        <source>
            <dbReference type="PubMed" id="23087212"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="29">
        <source>
            <dbReference type="PubMed" id="24623412"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="30">
        <source>
            <dbReference type="PubMed" id="25658430"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="31">
        <source>
            <dbReference type="PubMed" id="27383630"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="32">
        <source>
            <dbReference type="PubMed" id="2904446"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="33">
        <source>
            <dbReference type="PubMed" id="29695431"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="34">
        <source>
            <dbReference type="PubMed" id="7747433"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="35">
        <source>
            <dbReference type="PubMed" id="7831320"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="36">
        <source>
            <dbReference type="PubMed" id="8057461"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="37">
        <source>
            <dbReference type="PubMed" id="8610462"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="38">
        <source>
            <dbReference type="PubMed" id="8910486"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="39">
        <source>
            <dbReference type="PubMed" id="8985362"/>
        </source>
    </evidence>
    <evidence type="ECO:0000303" key="40">
        <source>
            <dbReference type="PubMed" id="28104453"/>
        </source>
    </evidence>
    <evidence type="ECO:0000305" key="41"/>
    <evidence type="ECO:0000305" key="42">
        <source>
            <dbReference type="PubMed" id="10748213"/>
        </source>
    </evidence>
    <evidence type="ECO:0000305" key="43">
        <source>
            <dbReference type="PubMed" id="1386484"/>
        </source>
    </evidence>
    <evidence type="ECO:0000305" key="44">
        <source>
            <dbReference type="PubMed" id="17093195"/>
        </source>
    </evidence>
    <evidence type="ECO:0000305" key="45">
        <source>
            <dbReference type="PubMed" id="22514352"/>
        </source>
    </evidence>
    <evidence type="ECO:0000305" key="46">
        <source>
            <dbReference type="PubMed" id="24623412"/>
        </source>
    </evidence>
    <evidence type="ECO:0000305" key="47">
        <source>
            <dbReference type="PubMed" id="25658430"/>
        </source>
    </evidence>
    <evidence type="ECO:0000305" key="48">
        <source>
            <dbReference type="PubMed" id="27383630"/>
        </source>
    </evidence>
    <evidence type="ECO:0000305" key="49">
        <source>
            <dbReference type="PubMed" id="7747433"/>
        </source>
    </evidence>
    <evidence type="ECO:0000305" key="50">
        <source>
            <dbReference type="PubMed" id="7831320"/>
        </source>
    </evidence>
    <evidence type="ECO:0000305" key="51">
        <source>
            <dbReference type="PubMed" id="8910486"/>
        </source>
    </evidence>
    <evidence type="ECO:0007744" key="52">
        <source>
            <dbReference type="PDB" id="5FW5"/>
        </source>
    </evidence>
    <evidence type="ECO:0007829" key="53">
        <source>
            <dbReference type="PDB" id="1FW5"/>
        </source>
    </evidence>
    <evidence type="ECO:0007829" key="54">
        <source>
            <dbReference type="PDB" id="5DRV"/>
        </source>
    </evidence>
    <evidence type="ECO:0007829" key="55">
        <source>
            <dbReference type="PDB" id="5FW5"/>
        </source>
    </evidence>
    <sequence length="2432" mass="269512" checksum="BE7104A1EC3EF6EE" modified="2006-03-21" version="2">MAAKVHVDIEADSPFIKSLQKAFPSFEVESLQVTPNDHANARAFSHLATKLIEQETDKDTLILDIGSAPSRRMMSTHKYHCVCPMRSAEDPERLVCYAKKLAAASGKVLDREIAGKITDLQTVMATPDAESPTFCLHTDVTCRTAAEVAVYQDVYAVHAPTSLYHQAMKGVRTAYWIGFDTTPFMFDALAGAYPTYATNWADEQVLQARNIGLCAASLTEGRLGKLSILRKKQLKPCDTVMFSVGSTLYTESRKLLRSWHLPSVFHLKGKQSFTCRCDTIVSCEGYVVKKITMCPGLYGKTVGYAVTYHAEGFLVCKTTDTVKGERVSFPVCTYVPSTICDQMTGILATDVTPEDAQKLLVGLNQRIVVNGRTQRNTNTMKNYLLPIVAVAFSKWAREYKADLDDEKPLGVRERSLTCCCLWAFKTRKMHTMYKKPDTQTIVKVPSEFNSFVIPSLWSTGLAIPVRSRIKMLLAKKTKRELIPVLDASSARDAEQEEKERLEAELTREALPPLVPIAPAETGVVDVDVEELEYHAGAGVVETPRSALKVTAQPNDVLLGNYVVLSPQTVLKSSKLAPVHPLAEQVKIITHNGRAGRYQVDGYDGRVLLPCGSAIPVPEFQALSESATMVYNEREFVNRKLYHIAVHGPSLNTDEENYEKVRAERTDAEYVFDVDKKCCVKREEASGLVLVGELTNPPFHEFAYEGLKIRPSAPYKTTVVGVFGVPGSGKSAIIKSLVTKHDLVTSGKKENCQEIVNDVKKHRGLDIQAKTVDSILLNGCRRAVDILYVDEAFACHSGTLLALIALVKPRSKVVLCGDPKQCGFFNMMQLKVNFNHNICTEVCHKSISRRCTRPVTAIVSTLHYGGKMRTTNPCNKPIIIDTTGQTKPKPGDIVLTCFRGWVKQLQLDYRGHEVMTAAASQGLTRKGVYAVRQKVNENPLYAPASEHVNVLLTRTEDRLVWKTLAGDPWIKVLSNIPQGNFTATLEEWQEEHDKIMKVIEGPAAPVDAFQNKANVCWAKSLVPVLDTAGIRLTAEEWSTIITAFKEDRAYSPVVALNEICTKYYGVDLDSGLFSAPKVSLYYENNHWDNRPGGRMYGFNAATAARLEARHTFLKGQWHTGKQAVIAERKIQPLSVLDNVIPINRRLPHALVAEYKTVKGSRVEWLVNKVRGYHVLLVSEYNLALPRRRVTWLSPLNVTGADRCYDLSLGLPADAGRFDLVFVNIHTEFRIHHYQQCVDHAMKLQMLGGDALRLLKPGGSLLMRAYGYADKISEAVVSSLSRKFSSARVLRPDCVTSNTEVFLLFSNFDNGKRPSTLHQMNTKLSAVYAGEAMHTAGCAPSYRVKRADIATCTEAAVVNAANARGTVGDGVCRAVAKKWPSAFKGAATPVGTIKTVMCGSYPVIHAVAPNFSATTEAEGDRELAAVYRAVAAEVNRLSLSSVAIPLLSTGVFSGGRDRLQQSLNHLFTAMDATDADVTIYCRDKSWEKKIQEAIDMRTAVELLNDDVELTTDLVRVHPDSSLVGRKGYSTTDGSLYSYFEGTKFNQAAIDMAEILTLWPRLQEANEQICLYALGETMDNIRSKCPVNDSDSSTPPRTVPCLCRYAMTAERIARLRSHQVKSMVVCSSFPLPKYHVDGVQKVKCEKGLLFDPTVPSVVSPRKYAASTTDHSDRSLRGFDLDWTTDSSSTASDTMSLPSLQSCDIDSIYEPMAPIVVTADVHPEPAGIADLAADVHPEPADHVDLENPIPPPRPKRAAYLASRAAERPVPAPRKPTPAPRTAFRNKLPLTFGDFDEHEVDALASGITFGDFDDVLRLGRAGAYIFSSDTGSGHLQQKSVRQHNLQCAQLDAVEEEKMYPPKLDTEREKLLLLKMQMHPSEANKSRYQSRKVENMKATVVDRLTSGARLYTGADVGRIPTYAVRYPRPVYSPTVIERFSSPDVAIAACNEYLSRNYPTVASYQITDEYDAYLDMVDGSDSCLDRATFCPAKLRCYPKHHAYHQPTVRSAVPSPFQNTLQNVLAAATKRNCNVTQMRELPTMDSAVFNVECFKRYACSGEYWEEYAKQPIRITTENITTYVTKLKGPKAAALFAKTHNLVPLQEVPMDRFTVDMKRDVKVTPGTKHTEERPKVQVIQAAEPLATAYLCGIHRELVRRLNAVLRPNVHTLFDMSAEDFDAIIASHFHPGDPVLETDIASFDKSQDDSLALTGLMILEDLGVDQYLLDLIEAAFGEISSCHLPTGTRFKFGAMMKSGMFLTLFINTVLNITIASRVLEQRLTDSACAAFIGDDNIVHGVISDKLMAERCASWVNMEVKIIDAVMGEKPPYFCGGFIVFDSVTQTACRVSDPLKRLFKLGKPLTAEDKQDEDRRRALSDEVSKWFRTGLGAELEVALTSRYEVEGCKSILIAMATLARDIKAFKKLRGPVIHLYGGPRLVR</sequence>
</entry>
<copyright>
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms Distributed under the Creative Commons Attribution (CC BY 4.0) License
</copyright>
</uniprot>