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<entry dataset="Swiss-Prot" created="1992-05-01" modified="2021-04-07" version="117" xmlns="http://uniprot.org/uniprot">
    <accession>P25180</accession>
    <name>HN_SV41</name>
    <protein>
        <recommendedName>
            <fullName>Hemagglutinin-neuraminidase</fullName>
            <ecNumber>3.2.1.18</ecNumber>
        </recommendedName>
    </protein>
    <gene>
        <name type="primary">HN</name>
    </gene>
    <organism>
        <name type="scientific">Simian virus 41</name>
        <name type="common">SV41</name>
        <dbReference type="NCBI Taxonomy" id="2560766"/>
        <lineage>
            <taxon>Viruses</taxon>
            <taxon>Riboviria</taxon>
            <taxon>Orthornavirae</taxon>
            <taxon>Negarnaviricota</taxon>
            <taxon>Haploviricotina</taxon>
            <taxon>Monjiviricetes</taxon>
            <taxon>Mononegavirales</taxon>
            <taxon>Paramyxoviridae</taxon>
            <taxon>Rubulavirinae</taxon>
            <taxon>Orthorubulavirus</taxon>
        </lineage>
    </organism>
    <organismHost>
        <name type="scientific">Simiiformes</name>
        <dbReference type="NCBI Taxonomy" id="314293"/>
    </organismHost>
    <reference key="1">
        <citation type="journal article" date="1990" name="Virology" volume="179" first="738" last="748">
            <title>Antigenic and structural properties of a paramyxovirus simian virus 41 (SV41) reveal a close relationship with human parainfluenza type 2 virus.</title>
            <authorList>
                <person name="Tsurudome M."/>
                <person name="Bando H."/>
                <person name="Nishio M."/>
                <person name="Iwamoto Y."/>
                <person name="Kawano M."/>
                <person name="Kondo K."/>
                <person name="Komada H."/>
                <person name="Ito Y."/>
            </authorList>
            <dbReference type="PubMed" id="2173260"/>
            <dbReference type="DOI" id="10.1016/0042-6822(90)90141-D"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC RNA]</scope>
        <source>
            <strain>Toshiba/Chanock</strain>
        </source>
    </reference>
    <comment type="function">
        <text evidence="1">Attaches the virus to sialic acid-containing cell receptors and thereby initiating infection. Binding of HN protein to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion.</text>
    </comment>
    <comment type="function">
        <text evidence="1">Neuraminidase activity ensures the efficient spread of the virus by dissociating the mature virions from the neuraminic acid containing glycoproteins.</text>
    </comment>
    <comment type="catalytic activity">
        <reaction>
            <text>Hydrolysis of alpha-(2-&gt;3)-, alpha-(2-&gt;6)-, alpha-(2-&gt;8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.</text>
            <dbReference type="EC" id="3.2.1.18"/>
        </reaction>
    </comment>
    <comment type="subcellular location">
        <subcellularLocation>
            <location evidence="3">Virion membrane</location>
            <topology evidence="3">Single-pass type II membrane protein</topology>
        </subcellularLocation>
        <subcellularLocation>
            <location evidence="3">Host cell membrane</location>
            <topology evidence="3">Single-pass type II membrane protein</topology>
        </subcellularLocation>
    </comment>
    <comment type="similarity">
        <text evidence="3">Belongs to the paramyxoviruses hemagglutinin-neuraminidase family.</text>
    </comment>
    <dbReference type="EC" id="3.2.1.18"/>
    <dbReference type="EMBL" id="M62733">
        <property type="protein sequence ID" value="AAA47451.1"/>
        <property type="molecule type" value="Genomic_RNA"/>
    </dbReference>
    <dbReference type="EMBL" id="X64275">
        <property type="protein sequence ID" value="CAA45568.1"/>
        <property type="molecule type" value="Genomic_RNA"/>
    </dbReference>
    <dbReference type="PIR" id="A36419">
        <property type="entry name" value="HNNZ41"/>
    </dbReference>
    <dbReference type="SMR" id="P25180"/>
    <dbReference type="CAZy" id="GH83">
        <property type="family name" value="Glycoside Hydrolase Family 83"/>
    </dbReference>
    <dbReference type="PRIDE" id="P25180"/>
    <dbReference type="Proteomes" id="UP000108270">
        <property type="component" value="Genome"/>
    </dbReference>
    <dbReference type="CDD" id="cd15469">
        <property type="entry name" value="HN"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR016285">
        <property type="entry name" value="Hemagglutn-neuramid"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR000665">
        <property type="entry name" value="Hemagglutn/HN"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR036278">
        <property type="entry name" value="Sialidase_sf"/>
    </dbReference>
    <dbReference type="Pfam" id="PF00423">
        <property type="entry name" value="HN"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="PIRSF" id="PIRSF001072">
        <property type="entry name" value="Hemagglut-neuramid_paramyxoV"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="SUPFAM" id="SSF50939">
        <property type="entry name" value="SSF50939"/>
        <property type="match status" value="1"/>
    </dbReference>
    <proteinExistence type="inferred from homology"/>
    <keyword id="KW-0325">Glycoprotein</keyword>
    <keyword id="KW-0348">Hemagglutinin</keyword>
    <keyword id="KW-1032">Host cell membrane</keyword>
    <keyword id="KW-1043">Host membrane</keyword>
    <keyword id="KW-0945">Host-virus interaction</keyword>
    <keyword id="KW-0378">Hydrolase</keyword>
    <keyword id="KW-0472">Membrane</keyword>
    <keyword id="KW-1185">Reference proteome</keyword>
    <keyword id="KW-0735">Signal-anchor</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-0946">Virion</keyword>
    <keyword id="KW-1160">Virus entry into host cell</keyword>
    <feature type="chain" id="PRO_0000142645" description="Hemagglutinin-neuraminidase">
        <location>
            <begin position="1"/>
            <end position="568"/>
        </location>
    </feature>
    <feature type="topological domain" description="Intravirion" evidence="2">
        <location>
            <begin position="1"/>
            <end position="18"/>
        </location>
    </feature>
    <feature type="transmembrane region" description="Helical" evidence="2">
        <location>
            <begin position="19"/>
            <end position="39"/>
        </location>
    </feature>
    <feature type="topological domain" description="Virion surface" evidence="2">
        <location>
            <begin position="40"/>
            <end position="568"/>
        </location>
    </feature>
    <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine; by host" evidence="2">
        <location>
            <position position="44"/>
        </location>
    </feature>
    <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine; by host" evidence="2">
        <location>
            <position position="111"/>
        </location>
    </feature>
    <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine; by host" evidence="2">
        <location>
            <position position="268"/>
        </location>
    </feature>
    <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine; by host" evidence="2">
        <location>
            <position position="280"/>
        </location>
    </feature>
    <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine; by host" evidence="2">
        <location>
            <position position="382"/>
        </location>
    </feature>
    <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine; by host" evidence="2">
        <location>
            <position position="513"/>
        </location>
    </feature>
    <evidence type="ECO:0000250" key="1"/>
    <evidence type="ECO:0000255" key="2"/>
    <evidence type="ECO:0000305" key="3"/>
    <sequence length="568" mass="61733" checksum="7C09738E2715F548" modified="1992-05-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1992-05-01" modified="2022-05-25" version="108" xmlns="http://uniprot.org/uniprot">
    <accession>P25181</accession>
    <name>FUS_SV41</name>
    <protein>
        <recommendedName>
            <fullName>Fusion glycoprotein F0</fullName>
        </recommendedName>
        <component>
            <recommendedName>
                <fullName>Fusion glycoprotein F2</fullName>
            </recommendedName>
        </component>
        <component>
            <recommendedName>
                <fullName>Fusion glycoprotein F1</fullName>
            </recommendedName>
        </component>
    </protein>
    <gene>
        <name type="primary">F</name>
    </gene>
    <organism>
        <name type="scientific">Simian virus 41</name>
        <name type="common">SV41</name>
        <dbReference type="NCBI Taxonomy" id="2560766"/>
        <lineage>
            <taxon>Viruses</taxon>
            <taxon>Riboviria</taxon>
            <taxon>Orthornavirae</taxon>
            <taxon>Negarnaviricota</taxon>
            <taxon>Haploviricotina</taxon>
            <taxon>Monjiviricetes</taxon>
            <taxon>Mononegavirales</taxon>
            <taxon>Paramyxoviridae</taxon>
            <taxon>Rubulavirinae</taxon>
            <taxon>Orthorubulavirus</taxon>
        </lineage>
    </organism>
    <organismHost>
        <name type="scientific">Simiiformes</name>
        <dbReference type="NCBI Taxonomy" id="314293"/>
    </organismHost>
    <reference key="1">
        <citation type="journal article" date="1990" name="Virology" volume="179" first="738" last="748">
            <title>Antigenic and structural properties of a paramyxovirus simian virus 41 (SV41) reveal a close relationship with human parainfluenza type 2 virus.</title>
            <authorList>
                <person name="Tsurudome M."/>
                <person name="Bando H."/>
                <person name="Nishio M."/>
                <person name="Iwamoto Y."/>
                <person name="Kawano M."/>
                <person name="Kondo K."/>
                <person name="Komada H."/>
                <person name="Ito Y."/>
            </authorList>
            <dbReference type="PubMed" id="2173260"/>
            <dbReference type="DOI" id="10.1016/0042-6822(90)90141-D"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE</scope>
        <source>
            <strain>Toshiba/Chanock</strain>
        </source>
    </reference>
    <reference key="2">
        <citation type="journal article" date="1991" name="Virology" volume="184" first="93" last="100">
            <title>Transcripts of simian virus 41 (SV41) matrix gene are exclusively dicistronic with the fusion gene which is also transcribed as a monocistron.</title>
            <authorList>
                <person name="Tsurudome M."/>
                <person name="Bando H."/>
                <person name="Kawano M."/>
                <person name="Matsumura H."/>
                <person name="Komada H."/>
                <person name="Nishio M."/>
                <person name="Ito Y."/>
            </authorList>
            <dbReference type="PubMed" id="1651608"/>
            <dbReference type="DOI" id="10.1016/0042-6822(91)90825-V"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE</scope>
        <source>
            <strain>Toshiba/Chanock</strain>
        </source>
    </reference>
    <comment type="function">
        <text evidence="1">Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with HN at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis.</text>
    </comment>
    <comment type="subunit">
        <text evidence="1">Homotrimer of disulfide-linked F1-F2.</text>
    </comment>
    <comment type="subcellular location">
        <subcellularLocation>
            <location evidence="1">Virion membrane</location>
            <topology evidence="1">Single-pass type I membrane protein</topology>
        </subcellularLocation>
        <subcellularLocation>
            <location evidence="1">Host cell membrane</location>
            <topology evidence="1">Single-pass membrane protein</topology>
        </subcellularLocation>
    </comment>
    <comment type="PTM">
        <text evidence="1">The inactive precursor F0 is glycosylated and proteolytically cleaved into F1 and F2 to be functionally active. The cleavage is mediated by cellular proteases during the transport and maturation of the polypeptide.</text>
    </comment>
    <comment type="similarity">
        <text evidence="3">Belongs to the paramyxoviruses fusion glycoprotein family.</text>
    </comment>
    <dbReference type="EMBL" id="S48627">
        <property type="protein sequence ID" value="AAB19494.1"/>
        <property type="molecule type" value="mRNA"/>
    </dbReference>
    <dbReference type="EMBL" id="X64275">
        <property type="protein sequence ID" value="CAA45567.1"/>
        <property type="molecule type" value="Genomic_RNA"/>
    </dbReference>
    <dbReference type="EMBL" id="M62733">
        <property type="status" value="NOT_ANNOTATED_CDS"/>
        <property type="molecule type" value="Genomic_RNA"/>
    </dbReference>
    <dbReference type="PIR" id="B40563">
        <property type="entry name" value="VGNZ41"/>
    </dbReference>
    <dbReference type="SMR" id="P25181"/>
    <dbReference type="Proteomes" id="UP000108270">
        <property type="component" value="Genome"/>
    </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: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:0019064">
        <property type="term" value="P:fusion of virus membrane with host plasma membrane"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-KW"/>
    </dbReference>
    <dbReference type="GO" id="GO:0046718">
        <property type="term" value="P:viral entry into host cell"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-KW"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR000776">
        <property type="entry name" value="Fusion_F0_Paramyxovir"/>
    </dbReference>
    <dbReference type="Pfam" id="PF00523">
        <property type="entry name" value="Fusion_gly"/>
        <property type="match status" value="1"/>
    </dbReference>
    <proteinExistence type="evidence at transcript level"/>
    <keyword id="KW-0165">Cleavage on pair of basic residues</keyword>
    <keyword id="KW-0175">Coiled coil</keyword>
    <keyword id="KW-1015">Disulfide bond</keyword>
    <keyword id="KW-1169">Fusion of virus membrane with host cell 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-1043">Host membrane</keyword>
    <keyword id="KW-0472">Membrane</keyword>
    <keyword id="KW-1185">Reference proteome</keyword>
    <keyword id="KW-0732">Signal</keyword>
    <keyword id="KW-0812">Transmembrane</keyword>
    <keyword id="KW-1133">Transmembrane helix</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-1160">Virus entry into host cell</keyword>
    <feature type="signal peptide" evidence="2">
        <location>
            <begin position="1"/>
            <end position="26"/>
        </location>
    </feature>
    <feature type="chain" id="PRO_0000039381" description="Fusion glycoprotein F0">
        <location>
            <begin position="27"/>
            <end position="561"/>
        </location>
    </feature>
    <feature type="chain" id="PRO_0000039382" description="Fusion glycoprotein F2">
        <location>
            <begin position="27"/>
            <end position="109"/>
        </location>
    </feature>
    <feature type="chain" id="PRO_0000039383" description="Fusion glycoprotein F1">
        <location>
            <begin position="110"/>
            <end position="561"/>
        </location>
    </feature>
    <feature type="topological domain" description="Extracellular" evidence="1">
        <location>
            <begin position="27"/>
            <end position="495"/>
        </location>
    </feature>
    <feature type="transmembrane region" description="Helical" evidence="1">
        <location>
            <begin position="496"/>
            <end position="516"/>
        </location>
    </feature>
    <feature type="topological domain" description="Cytoplasmic" evidence="1">
        <location>
            <begin position="517"/>
            <end position="561"/>
        </location>
    </feature>
    <feature type="region of interest" description="Fusion peptide" evidence="1">
        <location>
            <begin position="110"/>
            <end position="134"/>
        </location>
    </feature>
    <feature type="coiled-coil region" evidence="2">
        <location>
            <begin position="135"/>
            <end position="163"/>
        </location>
    </feature>
    <feature type="coiled-coil region" evidence="2">
        <location>
            <begin position="459"/>
            <end position="484"/>
        </location>
    </feature>
    <feature type="site" description="Cleavage; by host" evidence="1">
        <location>
            <begin position="109"/>
            <end position="110"/>
        </location>
    </feature>
    <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine; by host" evidence="2">
        <location>
            <position position="72"/>
        </location>
    </feature>
    <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine; by host" evidence="2">
        <location>
            <position position="80"/>
        </location>
    </feature>
    <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine; by host" evidence="2">
        <location>
            <position position="359"/>
        </location>
    </feature>
    <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine; by host" evidence="2">
        <location>
            <position position="434"/>
        </location>
    </feature>
    <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine; by host" evidence="2">
        <location>
            <position position="440"/>
        </location>
    </feature>
    <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine; by host" evidence="2">
        <location>
            <position position="464"/>
        </location>
    </feature>
    <feature type="disulfide bond" description="Interchain (between F2 and F1 chains)" evidence="1">
        <location>
            <begin position="71"/>
            <end position="192"/>
        </location>
    </feature>
    <feature type="disulfide bond" evidence="1">
        <location>
            <begin position="331"/>
            <end position="340"/>
        </location>
    </feature>
    <feature type="disulfide bond" evidence="1">
        <location>
            <begin position="355"/>
            <end position="363"/>
        </location>
    </feature>
    <feature type="disulfide bond" evidence="1">
        <location>
            <begin position="387"/>
            <end position="392"/>
        </location>
    </feature>
    <feature type="disulfide bond" evidence="1">
        <location>
            <begin position="394"/>
            <end position="417"/>
        </location>
    </feature>
    <evidence type="ECO:0000250" key="1"/>
    <evidence type="ECO:0000255" key="2"/>
    <evidence type="ECO:0000305" key="3"/>
    <sequence length="561" mass="59819" checksum="EEBA618D72418D9B" modified="1992-05-01" version="1" precursor="true"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1992-05-01" modified="2021-09-29" version="70" xmlns="http://uniprot.org/uniprot">
    <accession>P25182</accession>
    <name>MATRX_SV41</name>
    <protein>
        <recommendedName>
            <fullName>Matrix protein</fullName>
        </recommendedName>
    </protein>
    <gene>
        <name type="primary">M</name>
    </gene>
    <organism>
        <name type="scientific">Simian virus 41</name>
        <name type="common">SV41</name>
        <dbReference type="NCBI Taxonomy" id="2560766"/>
        <lineage>
            <taxon>Viruses</taxon>
            <taxon>Riboviria</taxon>
            <taxon>Orthornavirae</taxon>
            <taxon>Negarnaviricota</taxon>
            <taxon>Haploviricotina</taxon>
            <taxon>Monjiviricetes</taxon>
            <taxon>Mononegavirales</taxon>
            <taxon>Paramyxoviridae</taxon>
            <taxon>Rubulavirinae</taxon>
            <taxon>Orthorubulavirus</taxon>
        </lineage>
    </organism>
    <organismHost>
        <name type="scientific">Simiiformes</name>
        <dbReference type="NCBI Taxonomy" id="314293"/>
    </organismHost>
    <reference key="1">
        <citation type="journal article" date="1990" name="Virology" volume="179" first="738" last="748">
            <title>Antigenic and structural properties of a paramyxovirus simian virus 41 (SV41) reveal a close relationship with human parainfluenza type 2 virus.</title>
            <authorList>
                <person name="Tsurudome M."/>
                <person name="Bando H."/>
                <person name="Nishio M."/>
                <person name="Iwamoto Y."/>
                <person name="Kawano M."/>
                <person name="Kondo K."/>
                <person name="Komada H."/>
                <person name="Ito Y."/>
            </authorList>
            <dbReference type="PubMed" id="2173260"/>
            <dbReference type="DOI" id="10.1016/0042-6822(90)90141-D"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE</scope>
        <source>
            <strain>Toshiba/Chanock</strain>
        </source>
    </reference>
    <reference key="2">
        <citation type="journal article" date="1991" name="Virology" volume="184" first="93" last="100">
            <title>Transcripts of simian virus 41 (SV41) matrix gene are exclusively dicistronic with the fusion gene which is also transcribed as a monocistron.</title>
            <authorList>
                <person name="Tsurudome M."/>
                <person name="Bando H."/>
                <person name="Kawano M."/>
                <person name="Matsumura H."/>
                <person name="Komada H."/>
                <person name="Nishio M."/>
                <person name="Ito Y."/>
            </authorList>
            <dbReference type="PubMed" id="1651608"/>
            <dbReference type="DOI" id="10.1016/0042-6822(91)90825-V"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [MRNA]</scope>
        <source>
            <strain>Toshiba/Chanock</strain>
        </source>
    </reference>
    <comment type="function">
        <text>The M protein has a crucial role in virus assembly and interacts with the RNP complex as well as with the viral membrane.</text>
    </comment>
    <comment type="subcellular location">
        <subcellularLocation>
            <location evidence="1">Virion</location>
        </subcellularLocation>
    </comment>
    <comment type="similarity">
        <text evidence="1">Belongs to the morbillivirus/respirovirus/rubulavirus M protein family.</text>
    </comment>
    <dbReference type="EMBL" id="S48627">
        <property type="protein sequence ID" value="AAB19493.1"/>
        <property type="molecule type" value="mRNA"/>
    </dbReference>
    <dbReference type="EMBL" id="X64275">
        <property type="protein sequence ID" value="CAA45566.1"/>
        <property type="molecule type" value="Genomic_RNA"/>
    </dbReference>
    <dbReference type="EMBL" id="M62733">
        <property type="status" value="NOT_ANNOTATED_CDS"/>
        <property type="molecule type" value="Genomic_RNA"/>
    </dbReference>
    <dbReference type="PIR" id="A40563">
        <property type="entry name" value="MFNZ41"/>
    </dbReference>
    <dbReference type="SMR" id="P25182"/>
    <dbReference type="Proteomes" id="UP000108270">
        <property type="component" value="Genome"/>
    </dbReference>
    <dbReference type="Gene3D" id="2.70.20.50">
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="Gene3D" id="2.70.20.60">
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR000982">
        <property type="entry name" value="Matrix"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR042539">
        <property type="entry name" value="Matrix_C"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR042540">
        <property type="entry name" value="Matrix_N"/>
    </dbReference>
    <dbReference type="Pfam" id="PF00661">
        <property type="entry name" value="Matrix"/>
        <property type="match status" value="1"/>
    </dbReference>
    <proteinExistence type="evidence at transcript level"/>
    <keyword id="KW-1185">Reference proteome</keyword>
    <keyword id="KW-0468">Viral matrix protein</keyword>
    <keyword id="KW-0946">Virion</keyword>
    <feature type="chain" id="PRO_0000142778" description="Matrix protein">
        <location>
            <begin position="1"/>
            <end position="382"/>
        </location>
    </feature>
    <evidence type="ECO:0000305" key="1"/>
    <sequence length="382" mass="42155" checksum="B4C6DCE968E4A855" modified="1992-05-01" version="1">MPTISIPADPASPDQGLKPFPIQLDSKDGKSGKLVKQIRIKYLTEPNSRSPPLTFINTYGFIYARDLSGGIMNEQSSGIQSGSVTACMMTLGPGPDIKNANRVLAALNGFYVKVRKTSSLKEEAVFELVNVPKLLANHALCKQGRLVCSAEKFVKNPSKMMAGQEYLYFPTFVSLTYCPSNLNYQVAKPILKIRSRFVYSIHMEIIFRLLCKPDSPLLKTYATDPEGRGCLASVWIHVCNILKNKKIKQRGVDSYFSSKAISMQLTVSIADTWGPTVIIKANGHIPKTAAPFFSKDGVACHPLQDVSPALTKSLWSVGCEITKARLILQESNISDLLKTQDLITDQIKIKKGHSHFGRSSFNPFKKAISLPNLTQLGQDDED</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1992-08-01" modified="2021-06-02" version="80" xmlns="http://uniprot.org/uniprot">
    <accession>P27018</accession>
    <name>NCAP_SV41</name>
    <protein>
        <recommendedName>
            <fullName>Nucleoprotein</fullName>
        </recommendedName>
        <alternativeName>
            <fullName>Nucleocapsid protein</fullName>
            <shortName>NP</shortName>
            <shortName>Protein N</shortName>
        </alternativeName>
    </protein>
    <gene>
        <name type="primary">N</name>
        <name type="synonym">NP</name>
    </gene>
    <organism>
        <name type="scientific">Simian virus 41</name>
        <name type="common">SV41</name>
        <dbReference type="NCBI Taxonomy" id="2560766"/>
        <lineage>
            <taxon>Viruses</taxon>
            <taxon>Riboviria</taxon>
            <taxon>Orthornavirae</taxon>
            <taxon>Negarnaviricota</taxon>
            <taxon>Haploviricotina</taxon>
            <taxon>Monjiviricetes</taxon>
            <taxon>Mononegavirales</taxon>
            <taxon>Paramyxoviridae</taxon>
            <taxon>Rubulavirinae</taxon>
            <taxon>Orthorubulavirus</taxon>
        </lineage>
    </organism>
    <organismHost>
        <name type="scientific">Simiiformes</name>
        <dbReference type="NCBI Taxonomy" id="314293"/>
    </organismHost>
    <reference key="1">
        <citation type="journal article" date="1991" name="J. Gen. Virol." volume="72" first="2289" last="2292">
            <title>Molecular relationships between human parainfluenza virus type 2, and simian viruses 41 and 5: determination of nucleoprotein gene sequences of simian viruses 41 and 5.</title>
            <authorList>
                <person name="Tsurudome M."/>
                <person name="Oki N."/>
                <person name="Higuchi Y."/>
                <person name="Miyahara K."/>
                <person name="Yoshimoto M."/>
                <person name="Mutsuga N."/>
                <person name="Kitada S."/>
                <person name="Ogawa M."/>
                <person name="Miyahara Y."/>
                <person name="Okamoto K."/>
                <person name="Kawano M."/>
                <person name="Komada H."/>
                <person name="Matsumura H."/>
                <person name="Kusagawa S."/>
                <person name="Nishio M."/>
                <person name="Ito Y."/>
            </authorList>
            <dbReference type="PubMed" id="1654380"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [MRNA]</scope>
        <source>
            <strain>Toshiba/Chanock</strain>
        </source>
    </reference>
    <comment type="function">
        <text>Encapsidates the genome, protecting it from nucleases. The nucleocapsid (NC) has a helical structure. The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication. During replication, encapsidation by N is coupled to RNA synthesis and all replicative products are resistant to nucleases.</text>
    </comment>
    <comment type="subunit">
        <text evidence="1">Homomultimerizes to form the nucleocapsid. Binds to viral genomic RNA. In nucleocapsid, binds the P protein and thereby positions the polymerase on the template.</text>
    </comment>
    <comment type="subcellular location">
        <subcellularLocation>
            <location evidence="3">Virion</location>
        </subcellularLocation>
        <subcellularLocation>
            <location evidence="1">Host cytoplasm</location>
        </subcellularLocation>
    </comment>
    <comment type="domain">
        <text evidence="1">Ncore is globular and carries regions required for N self-assembly and RNA-binding. Ntail is an intrinsically disordered monomeric domain.</text>
    </comment>
    <comment type="similarity">
        <text evidence="3">Belongs to the paramyxoviruses nucleocapsid family.</text>
    </comment>
    <dbReference type="EMBL" id="S56065">
        <property type="protein sequence ID" value="AAB19770.1"/>
        <property type="molecule type" value="mRNA"/>
    </dbReference>
    <dbReference type="EMBL" id="X64275">
        <property type="protein sequence ID" value="CAA45570.1"/>
        <property type="molecule type" value="Genomic_RNA"/>
    </dbReference>
    <dbReference type="PIR" id="JQ1270">
        <property type="entry name" value="JQ1270"/>
    </dbReference>
    <dbReference type="SMR" id="P27018"/>
    <dbReference type="Proteomes" id="UP000108270">
        <property type="component" value="Genome"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR002021">
        <property type="entry name" value="Paramyx_ncap"/>
    </dbReference>
    <dbReference type="Pfam" id="PF00973">
        <property type="entry name" value="Paramyxo_ncap"/>
        <property type="match status" value="1"/>
    </dbReference>
    <proteinExistence type="evidence at transcript level"/>
    <keyword id="KW-0167">Capsid protein</keyword>
    <keyword id="KW-1139">Helical capsid protein</keyword>
    <keyword id="KW-1035">Host cytoplasm</keyword>
    <keyword id="KW-1185">Reference proteome</keyword>
    <keyword id="KW-0687">Ribonucleoprotein</keyword>
    <keyword id="KW-0694">RNA-binding</keyword>
    <keyword id="KW-0543">Viral nucleoprotein</keyword>
    <keyword id="KW-0946">Virion</keyword>
    <feature type="chain" id="PRO_0000142685" description="Nucleoprotein">
        <location>
            <begin position="1"/>
            <end position="543"/>
        </location>
    </feature>
    <feature type="region of interest" description="Ncore" evidence="1">
        <location>
            <begin position="1"/>
            <end position="400"/>
        </location>
    </feature>
    <feature type="region of interest" description="Ntail" evidence="1">
        <location>
            <begin position="401"/>
            <end position="543"/>
        </location>
    </feature>
    <feature type="region of interest" description="Disordered" evidence="2">
        <location>
            <begin position="448"/>
            <end position="543"/>
        </location>
    </feature>
    <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
        <location>
            <begin position="461"/>
            <end position="475"/>
        </location>
    </feature>
    <feature type="compositionally biased region" description="Polar residues" evidence="2">
        <location>
            <begin position="503"/>
            <end position="517"/>
        </location>
    </feature>
    <evidence type="ECO:0000250" key="1"/>
    <evidence type="ECO:0000256" key="2">
        <source>
            <dbReference type="SAM" id="MobiDB-lite"/>
        </source>
    </evidence>
    <evidence type="ECO:0000305" key="3"/>
    <sequence length="543" mass="60576" checksum="3992B016A89766E4" modified="1992-08-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1994-06-01" modified="2022-08-03" version="118" xmlns="http://uniprot.org/uniprot">
    <accession>P35341</accession>
    <name>L_SV41</name>
    <protein>
        <recommendedName>
            <fullName>RNA-directed RNA polymerase L</fullName>
            <shortName>Protein L</shortName>
        </recommendedName>
        <alternativeName>
            <fullName>Large structural protein</fullName>
        </alternativeName>
        <alternativeName>
            <fullName>Replicase</fullName>
        </alternativeName>
        <alternativeName>
            <fullName>Transcriptase</fullName>
        </alternativeName>
        <domain>
            <recommendedName>
                <fullName>RNA-directed RNA polymerase</fullName>
                <ecNumber evidence="3">2.7.7.48</ecNumber>
            </recommendedName>
        </domain>
        <domain>
            <recommendedName>
                <fullName evidence="2">GTP phosphohydrolase</fullName>
                <ecNumber evidence="2">3.6.1.-</ecNumber>
            </recommendedName>
        </domain>
        <domain>
            <recommendedName>
                <fullName evidence="7">GDP polyribonucleotidyltransferase</fullName>
                <ecNumber evidence="2">2.7.7.88</ecNumber>
            </recommendedName>
            <alternativeName>
                <fullName evidence="7">PRNTase</fullName>
            </alternativeName>
        </domain>
        <domain>
            <recommendedName>
                <fullName evidence="7">mRNA cap methyltransferase</fullName>
                <ecNumber evidence="2">2.1.1.375</ecNumber>
            </recommendedName>
            <alternativeName>
                <fullName evidence="2">mRNA (guanine-N(7)-)-methyltransferase</fullName>
                <shortName evidence="2">G-N7-MTase</shortName>
            </alternativeName>
            <alternativeName>
                <fullName evidence="2">mRNA (nucleoside-2'-O-)-methyltransferase</fullName>
                <shortName evidence="2">N1-2'-O-MTase</shortName>
            </alternativeName>
        </domain>
    </protein>
    <gene>
        <name type="primary">L</name>
    </gene>
    <organism>
        <name type="scientific">Simian virus 41</name>
        <name type="common">SV41</name>
        <dbReference type="NCBI Taxonomy" id="2560766"/>
        <lineage>
            <taxon>Viruses</taxon>
            <taxon>Riboviria</taxon>
            <taxon>Orthornavirae</taxon>
            <taxon>Negarnaviricota</taxon>
            <taxon>Haploviricotina</taxon>
            <taxon>Monjiviricetes</taxon>
            <taxon>Mononegavirales</taxon>
            <taxon>Paramyxoviridae</taxon>
            <taxon>Rubulavirinae</taxon>
            <taxon>Orthorubulavirus</taxon>
        </lineage>
    </organism>
    <organismHost>
        <name type="scientific">Simiiformes</name>
        <dbReference type="NCBI Taxonomy" id="314293"/>
    </organismHost>
    <reference key="1">
        <citation type="journal article" date="1992" name="J. Gen. Virol." volume="73" first="2743" last="2750">
            <title>Nucleotide sequence analysis of the simian virus 41 gene encoding the large (L) protein and construction of a phylogenetic tree for the L proteins of paramyxoviruses.</title>
            <authorList>
                <person name="Ogawa M."/>
                <person name="Mutsuga N."/>
                <person name="Tsurudome M."/>
                <person name="Kawano M."/>
                <person name="Matsumura H."/>
                <person name="Kusagawa S."/>
                <person name="Komada H."/>
                <person name="Nishio M."/>
                <person name="Ito Y."/>
            </authorList>
            <dbReference type="PubMed" id="1328485"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC RNA]</scope>
        <source>
            <strain>Toshiba/Chanock</strain>
        </source>
    </reference>
    <comment type="function">
        <text evidence="2">RNA-directed RNA polymerase that catalyzes the transcription of viral mRNAs, their capping and polyadenylation. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). The viral polymerase binds to the genomic RNA at the 3' leader promoter, and transcribes subsequently all viral mRNAs with a decreasing efficiency. The first gene is the most transcribed, and the last the least transcribed. The viral phosphoprotein acts as a processivity factor. Capping is concommitant with initiation of mRNA transcription. Indeed, a GDP polyribonucleotidyl transferase (PRNTase) adds the cap structure when the nascent RNA chain length has reached few nucleotides. Ribose 2'-O methylation of viral mRNA cap precedes and facilitates subsequent guanine-N-7 methylation, both activities being carried by the viral polymerase. Polyadenylation of mRNAs occur by a stuttering mechanism at a slipery stop site present at the end viral genes. After finishing transcription of a mRNA, the polymerase can resume transcription of the downstream gene.</text>
    </comment>
    <comment type="function">
        <text evidence="2">RNA-directed RNA polymerase that catalyzes the replication of viral genomic RNA. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). The replicase mode is dependent on intracellular N protein concentration. In this mode, the polymerase replicates the whole viral genome without recognizing transcriptional signals, and the replicated genome is not caped or polyadenylated.</text>
    </comment>
    <comment type="catalytic activity">
        <reaction evidence="5">
            <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>a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + 2 S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-adenosine in mRNA + H(+) + 2 S-adenosyl-L-homocysteine</text>
            <dbReference type="Rhea" id="RHEA:65376"/>
            <dbReference type="Rhea" id="RHEA-COMP:16797"/>
            <dbReference type="Rhea" id="RHEA-COMP:16798"/>
            <dbReference type="ChEBI" id="CHEBI:15378"/>
            <dbReference type="ChEBI" id="CHEBI:57856"/>
            <dbReference type="ChEBI" id="CHEBI:59789"/>
            <dbReference type="ChEBI" id="CHEBI:156483"/>
            <dbReference type="ChEBI" id="CHEBI:156484"/>
            <dbReference type="EC" id="2.1.1.375"/>
        </reaction>
    </comment>
    <comment type="catalytic activity">
        <reaction evidence="2">
            <text>a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-methionine = a 5'-end (5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-adenosine in mRNA + H(+) + S-adenosyl-L-homocysteine</text>
            <dbReference type="Rhea" id="RHEA:65380"/>
            <dbReference type="Rhea" id="RHEA-COMP:16797"/>
            <dbReference type="Rhea" id="RHEA-COMP:16801"/>
            <dbReference type="ChEBI" id="CHEBI:15378"/>
            <dbReference type="ChEBI" id="CHEBI:57856"/>
            <dbReference type="ChEBI" id="CHEBI:59789"/>
            <dbReference type="ChEBI" id="CHEBI:156482"/>
            <dbReference type="ChEBI" id="CHEBI:156484"/>
        </reaction>
    </comment>
    <comment type="catalytic activity">
        <reaction evidence="3">
            <text>a 5'-end triphospho-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + GDP + H(+) = a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + diphosphate</text>
            <dbReference type="Rhea" id="RHEA:65436"/>
            <dbReference type="Rhea" id="RHEA-COMP:16797"/>
            <dbReference type="Rhea" id="RHEA-COMP:16799"/>
            <dbReference type="ChEBI" id="CHEBI:15378"/>
            <dbReference type="ChEBI" id="CHEBI:33019"/>
            <dbReference type="ChEBI" id="CHEBI:58189"/>
            <dbReference type="ChEBI" id="CHEBI:156484"/>
            <dbReference type="ChEBI" id="CHEBI:156503"/>
            <dbReference type="EC" id="2.7.7.88"/>
        </reaction>
    </comment>
    <comment type="catalytic activity">
        <reaction evidence="2">
            <text>a 5'-end (5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-homocysteine</text>
            <dbReference type="Rhea" id="RHEA:65440"/>
            <dbReference type="Rhea" id="RHEA-COMP:16798"/>
            <dbReference type="Rhea" id="RHEA-COMP:16801"/>
            <dbReference type="ChEBI" id="CHEBI:57856"/>
            <dbReference type="ChEBI" id="CHEBI:59789"/>
            <dbReference type="ChEBI" id="CHEBI:156482"/>
            <dbReference type="ChEBI" id="CHEBI:156483"/>
        </reaction>
    </comment>
    <comment type="catalytic activity">
        <reaction evidence="3">
            <text>GTP + H2O = GDP + H(+) + phosphate</text>
            <dbReference type="Rhea" id="RHEA:19669"/>
            <dbReference type="ChEBI" id="CHEBI:15377"/>
            <dbReference type="ChEBI" id="CHEBI:15378"/>
            <dbReference type="ChEBI" id="CHEBI:37565"/>
            <dbReference type="ChEBI" id="CHEBI:43474"/>
            <dbReference type="ChEBI" id="CHEBI:58189"/>
        </reaction>
    </comment>
    <comment type="subunit">
        <text evidence="1">Interacts with the P protein.</text>
    </comment>
    <comment type="subcellular location">
        <subcellularLocation>
            <location evidence="7">Virion</location>
        </subcellularLocation>
        <subcellularLocation>
            <location evidence="1">Host cytoplasm</location>
        </subcellularLocation>
    </comment>
    <comment type="similarity">
        <text evidence="7">Belongs to the paramyxovirus L protein family.</text>
    </comment>
    <dbReference type="EC" id="2.7.7.48" evidence="3"/>
    <dbReference type="EC" id="3.6.1.-" evidence="2"/>
    <dbReference type="EC" id="2.7.7.88" evidence="2"/>
    <dbReference type="EC" id="2.1.1.375" evidence="2"/>
    <dbReference type="EMBL" id="X64275">
        <property type="protein sequence ID" value="CAA45569.1"/>
        <property type="molecule type" value="Genomic_RNA"/>
    </dbReference>
    <dbReference type="PIR" id="JQ1750">
        <property type="entry name" value="JQ1750"/>
    </dbReference>
    <dbReference type="SMR" id="P35341"/>
    <dbReference type="Proteomes" id="UP000108270">
        <property type="component" value="Genome"/>
    </dbReference>
    <dbReference type="GO" id="GO:0030430">
        <property type="term" value="C:host cell cytoplasm"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-SubCell"/>
    </dbReference>
    <dbReference type="GO" id="GO:0005524">
        <property type="term" value="F:ATP binding"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-KW"/>
    </dbReference>
    <dbReference type="GO" id="GO:0003924">
        <property type="term" value="F:GTPase activity"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="RHEA"/>
    </dbReference>
    <dbReference type="GO" id="GO:0004482">
        <property type="term" value="F:mRNA (guanine-N7-)-methyltransferase activity"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="InterPro"/>
    </dbReference>
    <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="Gene3D" id="3.40.50.150">
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR024352">
        <property type="entry name" value="L_methyltrans_paramyxo"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR039736">
        <property type="entry name" value="L_poly_C"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR026890">
        <property type="entry name" value="Mononeg_mRNAcap"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR014023">
        <property type="entry name" value="Mononeg_RNA_pol_cat"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR025786">
        <property type="entry name" value="Mononega_L_MeTrfase"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR016269">
        <property type="entry name" value="RNA-dir_pol_paramyxovirus"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR002877">
        <property type="entry name" value="RNA_MeTrfase_FtsJ_dom"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR029063">
        <property type="entry name" value="SAM-dependent_MTases_sf"/>
    </dbReference>
    <dbReference type="Pfam" id="PF01728">
        <property type="entry name" value="FtsJ"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="Pfam" id="PF12803">
        <property type="entry name" value="G-7-MTase"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="Pfam" id="PF14318">
        <property type="entry name" value="Mononeg_mRNAcap"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="Pfam" id="PF00946">
        <property type="entry name" value="Mononeg_RNA_pol"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="PIRSF" id="PIRSF000830">
        <property type="entry name" value="RNA_pol_ParamyxoV"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="TIGRFAMs" id="TIGR04198">
        <property type="entry name" value="paramyx_RNAcap"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="PROSITE" id="PS50526">
        <property type="entry name" value="RDRP_SSRNA_NEG_NONSEG"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="PROSITE" id="PS51590">
        <property type="entry name" value="SAM_MT_MNV_L"/>
        <property type="match status" value="1"/>
    </dbReference>
    <proteinExistence type="inferred from homology"/>
    <keyword id="KW-0067">ATP-binding</keyword>
    <keyword id="KW-1035">Host cytoplasm</keyword>
    <keyword id="KW-0378">Hydrolase</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-1185">Reference proteome</keyword>
    <keyword id="KW-0696">RNA-directed RNA polymerase</keyword>
    <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
    <keyword id="KW-0808">Transferase</keyword>
    <keyword id="KW-0693">Viral RNA replication</keyword>
    <keyword id="KW-0946">Virion</keyword>
    <feature type="chain" id="PRO_0000142741" description="RNA-directed RNA polymerase L">
        <location>
            <begin position="1"/>
            <end position="2269"/>
        </location>
    </feature>
    <feature type="domain" description="RdRp catalytic" evidence="5">
        <location>
            <begin position="666"/>
            <end position="850"/>
        </location>
    </feature>
    <feature type="domain" description="Mononegavirus-type SAM-dependent 2'-O-MTase" evidence="6">
        <location>
            <begin position="1785"/>
            <end position="1998"/>
        </location>
    </feature>
    <feature type="binding site" evidence="4">
        <location>
            <begin position="1815"/>
            <end position="1824"/>
        </location>
        <ligand>
            <name>ATP</name>
            <dbReference type="ChEBI" id="CHEBI:30616"/>
        </ligand>
    </feature>
    <evidence type="ECO:0000250" key="1"/>
    <evidence type="ECO:0000250" key="2">
        <source>
            <dbReference type="UniProtKB" id="P03523"/>
        </source>
    </evidence>
    <evidence type="ECO:0000250" key="3">
        <source>
            <dbReference type="UniProtKB" id="P28887"/>
        </source>
    </evidence>
    <evidence type="ECO:0000255" key="4"/>
    <evidence type="ECO:0000255" key="5">
        <source>
            <dbReference type="PROSITE-ProRule" id="PRU00539"/>
        </source>
    </evidence>
    <evidence type="ECO:0000255" key="6">
        <source>
            <dbReference type="PROSITE-ProRule" id="PRU00923"/>
        </source>
    </evidence>
    <evidence type="ECO:0000305" key="7"/>
    <sequence length="2269" mass="256432" checksum="3BD60C14AA161F5B" modified="1994-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1994-06-01" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
    <accession>P36315</accession>
    <name>V_SV41</name>
    <protein>
        <recommendedName>
            <fullName>Non-structural protein V</fullName>
        </recommendedName>
    </protein>
    <gene>
        <name type="primary">P/V</name>
    </gene>
    <organism>
        <name type="scientific">Simian virus 41</name>
        <name type="common">SV41</name>
        <dbReference type="NCBI Taxonomy" id="2560766"/>
        <lineage>
            <taxon>Viruses</taxon>
            <taxon>Riboviria</taxon>
            <taxon>Orthornavirae</taxon>
            <taxon>Negarnaviricota</taxon>
            <taxon>Haploviricotina</taxon>
            <taxon>Monjiviricetes</taxon>
            <taxon>Mononegavirales</taxon>
            <taxon>Paramyxoviridae</taxon>
            <taxon>Rubulavirinae</taxon>
            <taxon>Orthorubulavirus</taxon>
        </lineage>
    </organism>
    <organismHost>
        <name type="scientific">Simiiformes</name>
        <dbReference type="NCBI Taxonomy" id="314293"/>
    </organismHost>
    <reference key="1">
        <citation type="journal article" date="1993" name="J. Gen. Virol." volume="74" first="911" last="916">
            <title>Sequence determination of the P gene of simian virus 41: presence of irregular deletions near the RNA-editing sites of paramyxoviruses.</title>
            <authorList>
                <person name="Kawano M."/>
                <person name="Tsurudome M."/>
                <person name="Oki N."/>
                <person name="Nishio M."/>
                <person name="Komada H."/>
                <person name="Matsumura H."/>
                <person name="Kusagawa S."/>
                <person name="Ohta H."/>
                <person name="Ito Y."/>
            </authorList>
            <dbReference type="PubMed" id="8492098"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC RNA]</scope>
        <scope>RNA EDITING</scope>
        <source>
            <strain>Toshiba/Chanock</strain>
        </source>
    </reference>
    <reference key="2">
        <citation type="journal article" date="2001" name="J. Virol." volume="75" first="9165" last="9176">
            <title>High resistance of human parainfluenza type 2 virus protein-expressing cells to the antiviral and anti-cell proliferative activities of alpha/beta interferons: cysteine-rich V-specific domain is required for high resistance to the interferons.</title>
            <authorList>
                <person name="Nishio M."/>
                <person name="Tsurudome M."/>
                <person name="Ito M."/>
                <person name="Kawano M."/>
                <person name="Komada H."/>
                <person name="Ito Y."/>
            </authorList>
            <dbReference type="PubMed" id="11533180"/>
            <dbReference type="DOI" id="10.1128/JVI.75.19.9165-9176.2001"/>
        </citation>
        <scope>FUNCTION</scope>
    </reference>
    <comment type="function">
        <text evidence="1 3">Plays an essential role in the inhibition of host immune response. Prevents the establishment of cellular antiviral state by blocking interferon-alpha/beta (IFN-alpha/beta) production and signaling pathway (By similarity). Interacts with host IFIH1/MDA5 and DHX58/LGP2 to inhibit the transduction pathway involved in the activation of IFN-beta promoter, thus protecting the virus against cell antiviral state. Efficiently blocks type I and type II IFN signaling following infection, probably by targeting host STAT1 for proteasomal degradation.</text>
    </comment>
    <comment type="subcellular location">
        <subcellularLocation>
            <location evidence="1">Host cytoplasm</location>
        </subcellularLocation>
    </comment>
    <comment type="RNA editing">
        <location>
            <position position="164" evidence="4"/>
        </location>
        <text>Partially edited. RNA editing at this position consists of an insertion of two guanine nucleotides. The sequence displayed here is the V protein, derived from the unedited RNA. The edited RNA gives rise to the P protein (AC Q86606).</text>
    </comment>
    <comment type="similarity">
        <text evidence="5">Belongs to the paramyxoviruses V protein family.</text>
    </comment>
    <dbReference type="EMBL" id="S60811">
        <property type="protein sequence ID" value="AAB26639.1"/>
        <property type="molecule type" value="Genomic_RNA"/>
    </dbReference>
    <dbReference type="EMBL" id="X64275">
        <property type="protein sequence ID" value="CAA45571.1"/>
        <property type="molecule type" value="Genomic_RNA"/>
    </dbReference>
    <dbReference type="PIR" id="JQ2040">
        <property type="entry name" value="JQ2040"/>
    </dbReference>
    <dbReference type="SMR" id="P36315"/>
    <dbReference type="Proteomes" id="UP000108270">
        <property type="component" value="Genome"/>
    </dbReference>
    <dbReference type="GO" id="GO:0030430">
        <property type="term" value="C:host cell cytoplasm"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-SubCell"/>
    </dbReference>
    <dbReference type="GO" id="GO:0046872">
        <property type="term" value="F:metal ion binding"/>
        <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: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:0039554">
        <property type="term" value="P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host MDA-5 activity"/>
        <property type="evidence" value="ECO:0007669"/>
        <property type="project" value="UniProtKB-KW"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR024279">
        <property type="entry name" value="Paramyx_V_Zn-bd"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR025909">
        <property type="entry name" value="Soyouz_module"/>
    </dbReference>
    <dbReference type="Pfam" id="PF14313">
        <property type="entry name" value="Soyouz_module"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="Pfam" id="PF13008">
        <property type="entry name" value="zf-Paramyx-P"/>
        <property type="match status" value="1"/>
    </dbReference>
    <proteinExistence type="inferred from homology"/>
    <keyword id="KW-1035">Host cytoplasm</keyword>
    <keyword id="KW-0945">Host-virus interaction</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-1089">Inhibition of host MDA5 by virus</keyword>
    <keyword id="KW-1113">Inhibition of host RLR pathway by virus</keyword>
    <keyword id="KW-1105">Inhibition of host STAT1 by virus</keyword>
    <keyword id="KW-0922">Interferon antiviral system evasion</keyword>
    <keyword id="KW-0479">Metal-binding</keyword>
    <keyword id="KW-1185">Reference proteome</keyword>
    <keyword id="KW-0691">RNA editing</keyword>
    <keyword id="KW-0899">Viral immunoevasion</keyword>
    <keyword id="KW-0862">Zinc</keyword>
    <feature type="chain" id="PRO_0000142831" description="Non-structural protein V">
        <location>
            <begin position="1"/>
            <end position="225"/>
        </location>
    </feature>
    <feature type="region of interest" description="Disordered" evidence="2">
        <location>
            <begin position="145"/>
            <end position="172"/>
        </location>
    </feature>
    <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
        <location>
            <begin position="158"/>
            <end position="172"/>
        </location>
    </feature>
    <feature type="binding site" evidence="1">
        <location>
            <position position="174"/>
        </location>
        <ligand>
            <name>Zn(2+)</name>
            <dbReference type="ChEBI" id="CHEBI:29105"/>
            <label>1</label>
        </ligand>
    </feature>
    <feature type="binding site" evidence="1">
        <location>
            <position position="193"/>
        </location>
        <ligand>
            <name>Zn(2+)</name>
            <dbReference type="ChEBI" id="CHEBI:29105"/>
            <label>1</label>
        </ligand>
    </feature>
    <feature type="binding site" evidence="1">
        <location>
            <position position="197"/>
        </location>
        <ligand>
            <name>Zn(2+)</name>
            <dbReference type="ChEBI" id="CHEBI:29105"/>
            <label>2</label>
        </ligand>
    </feature>
    <feature type="binding site" evidence="1">
        <location>
            <position position="209"/>
        </location>
        <ligand>
            <name>Zn(2+)</name>
            <dbReference type="ChEBI" id="CHEBI:29105"/>
            <label>2</label>
        </ligand>
    </feature>
    <feature type="binding site" evidence="1">
        <location>
            <position position="211"/>
        </location>
        <ligand>
            <name>Zn(2+)</name>
            <dbReference type="ChEBI" id="CHEBI:29105"/>
            <label>2</label>
        </ligand>
    </feature>
    <feature type="binding site" evidence="1">
        <location>
            <position position="214"/>
        </location>
        <ligand>
            <name>Zn(2+)</name>
            <dbReference type="ChEBI" id="CHEBI:29105"/>
            <label>2</label>
        </ligand>
    </feature>
    <feature type="binding site" evidence="1">
        <location>
            <position position="218"/>
        </location>
        <ligand>
            <name>Zn(2+)</name>
            <dbReference type="ChEBI" id="CHEBI:29105"/>
            <label>1</label>
        </ligand>
    </feature>
    <feature type="binding site" evidence="1">
        <location>
            <position position="221"/>
        </location>
        <ligand>
            <name>Zn(2+)</name>
            <dbReference type="ChEBI" id="CHEBI:29105"/>
            <label>1</label>
        </ligand>
    </feature>
    <evidence type="ECO:0000250" key="1"/>
    <evidence type="ECO:0000256" key="2">
        <source>
            <dbReference type="SAM" id="MobiDB-lite"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="3">
        <source>
            <dbReference type="PubMed" id="11533180"/>
        </source>
    </evidence>
    <evidence type="ECO:0000269" key="4">
        <source>
            <dbReference type="PubMed" id="8492098"/>
        </source>
    </evidence>
    <evidence type="ECO:0000305" key="5"/>
    <sequence length="225" mass="24048" checksum="1A749260CAB7D71E" modified="1994-06-01" version="1">MAEEPTYTAEQVNDVVHAGLGTVDFFLSRPVDGQSSLGKGSVPPGITAVLTNAAELKAKTAAAAPVKPKRKKIQHMTPAYTIADNGDPNRLPANTPIANPLIPIERPPGRMTDLDLATGTVTQGTYKGVELAKAGKNALLTRFSSGPSLTDQASSKDPNFKRGGEIDGRHKGRHRREWSIAWVGDEVKVYEWCNPTCAPVTATDRKFSCTCGTCPDRCGECEGDN</sequence>
</entry>
<entry dataset="TrEMBL" created="2005-05-10" modified="2021-06-02" version="57" xmlns="http://uniprot.org/uniprot">
    <accession>Q5KU50</accession>
    <name>Q5KU50_SV41</name>
    <protein>
        <recommendedName>
            <fullName evidence="3">Phosphoprotein</fullName>
        </recommendedName>
    </protein>
    <gene>
        <name evidence="6" type="primary">P-V gene</name>
    </gene>
    <organism evidence="6 7">
        <name type="scientific">Simian virus 41</name>
        <name type="common">SV41</name>
        <dbReference type="NCBI Taxonomy" id="2560766"/>
        <lineage>
            <taxon>Viruses</taxon>
            <taxon>Riboviria</taxon>
            <taxon>Orthornavirae</taxon>
            <taxon>Negarnaviricota</taxon>
            <taxon>Haploviricotina</taxon>
            <taxon>Monjiviricetes</taxon>
            <taxon>Mononegavirales</taxon>
            <taxon>Paramyxoviridae</taxon>
            <taxon>Rubulavirinae</taxon>
            <taxon>Orthorubulavirus</taxon>
        </lineage>
    </organism>
    <organismHost>
        <name type="scientific">Simiiformes</name>
        <dbReference type="NCBI Taxonomy" id="314293"/>
    </organismHost>
    <reference evidence="6 7" key="1">
        <citation type="journal article" date="1992" name="J. Gen. Virol." volume="73" first="2743" last="2750">
            <title>Nucleotide sequence analysis of the simian virus 41 gene encoding the large (L) protein and construction of a phylogenetic tree for the L proteins of paramyxoviruses.</title>
            <authorList>
                <person name="Ogawa M."/>
                <person name="Mutsuga N."/>
                <person name="Tsurudome M."/>
                <person name="Kawano M."/>
                <person name="Matsumura H."/>
                <person name="Kusagawa S."/>
                <person name="Komada H."/>
                <person name="Nishio M."/>
                <person name="Ito Y."/>
            </authorList>
            <dbReference type="PubMed" id="1328485"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain evidence="6">Toshiba/Chanock</strain>
        </source>
    </reference>
    <reference evidence="6 7" key="2">
        <citation type="journal article" date="1993" name="J. Gen. Virol." volume="74" first="911" last="916">
            <title>Sequence determination of the P gene of simian virus 41: presence of irregular deletions near the RNA-editing site of paramyxoviruses.</title>
            <authorList>
                <person name="Kawano M."/>
                <person name="Tsurudome M."/>
                <person name="Oki N."/>
                <person name="Nishio M."/>
                <person name="Komado H."/>
                <person name="Matsumura H."/>
                <person name="Kusagawa S."/>
                <person name="Ohta H."/>
                <person name="Ito Y."/>
            </authorList>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
        <source>
            <strain evidence="6">Toshiba/Chanock</strain>
        </source>
    </reference>
    <comment type="function">
        <text evidence="1">Essential component of the RNA polymerase and the nascent chain assembly complex. Also required during RNA synthesis.</text>
    </comment>
    <comment type="similarity">
        <text evidence="2">Belongs to the rubulavirus/avulavirus P protein family.</text>
    </comment>
    <dbReference type="EMBL" id="X64275">
        <property type="protein sequence ID" value="CAA45572.2"/>
        <property type="molecule type" value="Genomic_RNA"/>
    </dbReference>
    <dbReference type="SMR" id="Q5KU50"/>
    <dbReference type="Proteomes" id="UP000108270">
        <property type="component" value="Genome"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR004897">
        <property type="entry name" value="P/V_Pprotein_paramyxoviral"/>
    </dbReference>
    <dbReference type="InterPro" id="IPR025909">
        <property type="entry name" value="Soyouz_module"/>
    </dbReference>
    <dbReference type="Pfam" id="PF03210">
        <property type="entry name" value="Paramyx_P_V_C"/>
        <property type="match status" value="1"/>
    </dbReference>
    <dbReference type="Pfam" id="PF14313">
        <property type="entry name" value="Soyouz_module"/>
        <property type="match status" value="1"/>
    </dbReference>
    <proteinExistence type="inferred from homology"/>
    <keyword evidence="7" id="KW-1185">Reference proteome</keyword>
    <feature type="domain" description="Soyouz_module" evidence="5">
        <location>
            <begin position="6"/>
            <end position="60"/>
        </location>
    </feature>
    <feature type="region of interest" description="Disordered" evidence="4">
        <location>
            <begin position="143"/>
            <end position="183"/>
        </location>
    </feature>
    <feature type="compositionally biased region" description="Polar residues" evidence="4">
        <location>
            <begin position="143"/>
            <end position="157"/>
        </location>
    </feature>
    <evidence type="ECO:0000256" key="1">
        <source>
            <dbReference type="ARBA" id="ARBA00002047"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="2">
        <source>
            <dbReference type="ARBA" id="ARBA00009016"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="3">
        <source>
            <dbReference type="ARBA" id="ARBA00020572"/>
        </source>
    </evidence>
    <evidence type="ECO:0000256" key="4">
        <source>
            <dbReference type="SAM" id="MobiDB-lite"/>
        </source>
    </evidence>
    <evidence type="ECO:0000259" key="5">
        <source>
            <dbReference type="Pfam" id="PF14313"/>
        </source>
    </evidence>
    <evidence type="ECO:0000313" key="6">
        <source>
            <dbReference type="EMBL" id="CAA45572.2"/>
        </source>
    </evidence>
    <evidence type="ECO:0000313" key="7">
        <source>
            <dbReference type="Proteomes" id="UP000108270"/>
        </source>
    </evidence>
    <sequence length="395" mass="41921" checksum="6E97477FBF483D30" modified="2005-05-10" version="1">MAEEPTYTAEQVNDVVHAGLGTVDFFLSRPVDGQSSLGKGSVPPGITAVLTNAAELKAKTAAAAPVKPKRKKIQHMTPAYTIADNGDPNRLPANTPIANPLIPIERPPGRMTDLDLATGTVTQGTYKGVELAKAGKNALLTRFSSGPSLTDQASSKDPNFKRGGEKLTDATKADIGGSGASPGSETKLRFMSGAIQHVPQLLPLTASSPVLVEPAPIGAENVKEIIEILRGLDLRMQSLEGKVDKILATSATITALKNEVTSLKANVATVEGMMTTMKIMDPSTPTNVPVEKIRKNLKDTPVIISGPLSESHITEGSDMIVLDELARPSLSSTKKIVRRPEPKKDLTGMKLMLIQLANDCMGKPDQKAEIVAKIHAATREAQLLDIKRSIIKSAI</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>