ID   POLG_TMEVG              Reviewed;        2303 AA.
AC   P08545; Q88593; Q88594;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 2.
DT   27-MAR-2024, entry version 170.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=Leader protein;
DE              Short=L;
DE   Contains:
DE     RecName: Full=Capsid protein VP0;
DE     AltName: Full=VP4-VP2;
DE   Contains:
DE     RecName: Full=Capsid protein VP4;
DE     AltName: Full=P1A;
DE     AltName: Full=Virion protein 4;
DE   Contains:
DE     RecName: Full=Capsid protein VP2;
DE     AltName: Full=P1B;
DE     AltName: Full=Virion protein 2;
DE   Contains:
DE     RecName: Full=Capsid protein VP3;
DE     AltName: Full=P1C;
DE     AltName: Full=Virion protein 3;
DE   Contains:
DE     RecName: Full=Capsid protein VP1;
DE     AltName: Full=P1D;
DE     AltName: Full=Virion protein 1;
DE   Contains:
DE     RecName: Full=Protein 2A;
DE              Short=P2A;
DE   Contains:
DE     RecName: Full=Protein 2B;
DE              Short=P2B;
DE   Contains:
DE     RecName: Full=Protein 2C;
DE              Short=P2C;
DE              EC=3.6.4.13;
DE   Contains:
DE     RecName: Full=Protein 3A;
DE              Short=P3A;
DE   Contains:
DE     RecName: Full=VPg;
DE              Short=P3B;
DE     AltName: Full=Protein 3B;
DE   Contains:
DE     RecName: Full=Protease 3C;
DE              Short=P3C;
DE              EC=3.4.22.28 {ECO:0000250|UniProtKB:P12296};
DE     AltName: Full=Picornain 3C;
DE   Contains:
DE     RecName: Full=RNA-directed RNA polymerase;
DE              Short=RdRp;
DE              EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
DE     AltName: Full=3D polymerase;
DE              Short=3Dpol;
DE     AltName: Full=Protein 3D;
DE              Short=3D;
DE   Flags: Precursor;
OS   Theiler's murine encephalomyelitis virus (strain GDVII) (TMEV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Picornaviridae; Caphthovirinae; Cardiovirus; Cardiovirus B.
OX   NCBI_TaxID=12127;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2838951; DOI=10.1016/0042-6822(88)90652-6;
RA   Pevear D.C., Borkowski J., Calenoff M., Oh C.K., Ostrawski B., Lipton H.L.;
RT   "Insights into Theiler's virus neurovirulence based on a genomic comparison
RT   of the neurovirulent GDVII and less virulent BeAn strains.";
RL   Virology 165:1-12(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1704-2303.
RX   PubMed=3023668; DOI=10.1128/jvi.60.3.1163-1165.1986;
RA   Ozden S., Tangy F., Chamorro M., Brahic M.;
RT   "Theiler's virus genome is closely related to that of encephalomyocarditis
RT   virus, the prototype cardiovirus.";
RL   J. Virol. 60:1163-1165(1986).
RN   [3]
RP   SUBCELLULAR LOCATION (PROTEIN 2C).
RX   PubMed=20471424; DOI=10.1016/j.jviromet.2010.05.009;
RA   Jauka T., Mutsvunguma L., Boshoff A., Edkins A.L., Knox C.;
RT   "Localisation of Theiler's murine encephalomyelitis virus protein 2C to the
RT   Golgi apparatus using antibodies generated against a peptide region.";
RL   J. Virol. Methods 168:162-169(2010).
RN   [4]
RP   RIBOSOMAL FRAMESHIFT.
RX   PubMed=26063423; DOI=10.1128/jvi.01043-15;
RA   Finch L.K., Ling R., Napthine S., Olspert A., Michiels T., Lardinois C.,
RA   Bell S., Loughran G., Brierley I., Firth A.E.;
RT   "Characterization of Ribosomal Frameshifting in Theiler's Murine
RT   Encephalomyelitis Virus.";
RL   J. Virol. 89:8580-8589(2015).
CC   -!- FUNCTION: [Leader protein]: Forms a complex with host RAN and probably
CC       binds to exportins carrying activated MAPK in order to mediate the
CC       hyperphosphorylation of host Phe/Gly containing nuclear pore proteins
CC       (Nups) resulting in cessation of active nucleocytoplasmic transport (By
CC       similarity). Proteins with NLS signals fail to import, cellular mRNAs
CC       fail to export, and some proteins small enough for diffusion are not
CC       retained anymore (efflux) (By similarity). The resulting inhibition of
CC       cellular protein synthesis serves to ensure maximal viral gene
CC       expression and to evade host immune response (By similarity). The
CC       leader protein also inhibits host interferon regulatory factor 3 (IRF3)
CC       dimerization, thereby blocking the transcriptional activation of IFN
CC       genes (By similarity). Binds to host RNase L thereby preventing its
CC       activation by 2'-5' oligoadenylates in order to counteract the
CC       antiviral interferon-inducible OAS/RNase L pathway (By similarity).
CC       Inhibits the integrated stress response (ISR) in the infected cell.
CC       Inhibits the host EIF2AK2/PKR by rendering this kinase unable to detect
CC       double-stranded RNA. Also impairs host stress granule formation
CC       probably by acting on a step downstream of EIF2AK2/PKR activation (By
CC       similarity). {ECO:0000250|UniProtKB:P08544,
CC       ECO:0000250|UniProtKB:P13899, ECO:0000250|UniProtKB:Q66765}.
CC   -!- FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo
CC       T=3 symmetry with capsid proteins VP2 and VP3. Together they form an
CC       icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3,
CC       with a diameter of approximately 300 Angstroms.VP4 lies on the inner
CC       surface of the protein shell formed by VP1, VP2 and VP3. All the three
CC       latter proteins contain a beta-sheet structure called beta-barrel jelly
CC       roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are
CC       located at the quasi-sixfold axes. {ECO:0000250|UniProtKB:C0MHL9}.
CC   -!- FUNCTION: [Capsid protein VP2]: Forms an icosahedral capsid of pseudo
CC       T=3 symmetry with capsid proteins VP2 and VP3. Together they form an
CC       icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3,
CC       with a diameter of approximately 300 Angstroms.VP4 lies on the inner
CC       surface of the protein shell formed by VP1, VP2 and VP3. All the three
CC       latter proteins contain a beta-sheet structure called beta-barrel jelly
CC       roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are
CC       located at the quasi-sixfold axes. {ECO:0000250|UniProtKB:C0MHL9}.
CC   -!- FUNCTION: [Capsid protein VP3]: Forms an icosahedral capsid of pseudo
CC       T=3 symmetry with capsid proteins VP2 and VP3. Together they form an
CC       icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3,
CC       with a diameter of approximately 300 Angstroms.VP4 lies on the inner
CC       surface of the protein shell formed by VP1, VP2 and VP3. All the three
CC       latter proteins contain a beta-sheet structure called beta-barrel jelly
CC       roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are
CC       located at the quasi-sixfold axes. {ECO:0000250|UniProtKB:C0MHL9}.
CC   -!- FUNCTION: [Capsid protein VP4]: Lies on the inner surface of the capsid
CC       shell (By similarity). After binding to the host receptor, the capsid
CC       undergoes conformational changes (By similarity). Capsid protein VP4 is
CC       released, capsid protein VP1 N-terminus is externalized, and together,
CC       they shape a pore in the host membrane through which the viral genome
CC       is translocated into the host cell cytoplasm (By similarity). After
CC       genome has been released, the channel shrinks (By similarity).
CC       {ECO:0000250|UniProtKB:C0MHL9, ECO:0000250|UniProtKB:P03300}.
CC   -!- FUNCTION: [Capsid protein VP0]: VP0 precursor is a component of
CC       immature procapsids. {ECO:0000250|UniProtKB:P08617}.
CC   -!- FUNCTION: [Protein 2A]: Involved in host translation shutoff by
CC       inhibiting cap-dependent mRNA translation (By similarity). Nuclear
CC       localization is required for this function (By similarity). The
CC       resulting inhibition of cellular protein synthesis serves to ensure
CC       maximal viral gene expression and to evade host immune response (By
CC       similarity). Inhibits the phosphorylation of the leader protein (By
CC       similarity). Binds to the RNA stem-loop essential for the ribosomal
CC       frameshift event and trans-activates the production of protein 2B* (By
CC       similarity). {ECO:0000250|UniProtKB:P12296,
CC       ECO:0000250|UniProtKB:Q66765}.
CC   -!- FUNCTION: [Protein 2B]: Affects membrane integrity and causes an
CC       increase in membrane permeability. {ECO:0000250}.
CC   -!- FUNCTION: [Protein 2C]: Associates with and induces structural
CC       rearrangements of intracellular membranes (Probable). It displays RNA-
CC       binding, nucleotide binding and NTPase activities (By similarity).
CC       {ECO:0000250|UniProtKB:P03305, ECO:0000305|PubMed:20471424}.
CC   -!- FUNCTION: [Protein 3A]: Serves as membrane anchor via its hydrophobic
CC       domain. {ECO:0000250}.
CC   -!- FUNCTION: [VPg]: Forms a primer, VPg-pU, which is utilized by the
CC       polymerase for the initiation of RNA chains.
CC       {ECO:0000250|UniProtKB:P03304}.
CC   -!- FUNCTION: [Protease 3C]: Cysteine protease that generates mature viral
CC       proteins from the precursor polyprotein (By similarity). In addition to
CC       its proteolytic activity, it binds to viral RNA, and thus influences
CC       viral genome replication. RNA and substrate cooperatively bind to the
CC       protease. Cleaves host PABP1, this cleavage is important for viral
CC       replication (By similarity). {ECO:0000250|UniProtKB:P03304,
CC       ECO:0000250|UniProtKB:P12296}.
CC   -!- FUNCTION: [RNA-directed RNA polymerase]: Replicates the genomic and
CC       antigenomic RNAs by recognizing replications specific signals (By
CC       similarity). Performs VPg uridylylation (By similarity).
CC       {ECO:0000250|UniProtKB:P12296}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC         Evidence={ECO:0000305};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus
CC         polyprotein. In other picornavirus reactions Glu may be substituted
CC         for Gln, and Ser or Thr for Gly.; EC=3.4.22.28;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU01222};
CC   -!- SUBUNIT: [Protein 2A]: Interacts with host EIF4E (By similarity).
CC       Interacts with the leader protein (By similarity).
CC       {ECO:0000250|UniProtKB:P08544, ECO:0000250|UniProtKB:P13899,
CC       ECO:0000250|UniProtKB:Q66765}.
CC   -!- SUBUNIT: [Leader protein]: Interacts with host RAN; the complex L-RAN
CC       recruits cellular kinases responsible for the L-induced
CC       nucleocytoplasmic trafficking inhibition (By similarity). The complex
CC       L-RAN can further bind to the host exportins XPO1/CRM1 and CSE1L/CAS
CC       (By similarity). Interacts with the protein 2A (By similarity).
CC       Interacts with host RNASEL; this interaction prevents RNASEL activation
CC       by its substrate 2'-5' oligoadenylates (By similarity).
CC       {ECO:0000250|UniProtKB:P08544, ECO:0000250|UniProtKB:P13899,
CC       ECO:0000250|UniProtKB:Q66765}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion
CC       {ECO:0000250|UniProtKB:C0MHL9}. Host cytoplasm {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion
CC       {ECO:0000250|UniProtKB:C0MHL9}. Host cytoplasm {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion
CC       {ECO:0000250|UniProtKB:C0MHL9}. Host cytoplasm {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Protein 2A]: Host nucleus, host nucleolus
CC       {ECO:0000250|UniProtKB:Q66765}.
CC   -!- SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane
CC       {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC       side {ECO:0000305}. Note=Probably localizes to the surface of
CC       intracellular membrane vesicles that are induced after virus infection
CC       as the site for viral RNA replication. These vesicles are probably
CC       autophagosome-like vesicles. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Protein 2C]: Host cytoplasmic vesicle membrane
CC       {ECO:0000305|PubMed:20471424}; Peripheral membrane protein
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes
CC       to the surface of intracellular membrane vesicles that are induced
CC       after virus infection as the site for viral RNA replication
CC       (PubMed:20471424). These vesicles are probably autophagosome-like
CC       vesicles (Probable). {ECO:0000269|PubMed:20471424, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane
CC       {ECO:0000250|UniProtKB:P03304}; Peripheral membrane protein
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes
CC       to the surface of intracellular membrane vesicles that are induced
CC       after virus infection as the site for viral RNA replication. These
CC       vesicles are probably autophagosome-like vesicles.
CC       {ECO:0000250|UniProtKB:P03304}.
CC   -!- SUBCELLULAR LOCATION: [VPg]: Virion {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host cytoplasmic
CC       vesicle membrane {ECO:0000305}; Peripheral membrane protein
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes
CC       to the surface of intracellular membrane vesicles that are induced
CC       after virus infection as the site for viral RNA replication. These
CC       vesicles are probably autophagosome-like vesicles. {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=2;
CC       Name=Genome polyprotein;
CC         IsoId=P08545-1; Sequence=Displayed;
CC       Name=2B*;
CC         IsoId=P0DOK5-1; Sequence=External;
CC   -!- DOMAIN: [Leader protein]: The Theilo and zinc-finger regions may both
CC       play a role in the inhibition of host nucleocytoplasmic trafficking and
CC       IRF-3 dimerization antagonism by the L protein.
CC       {ECO:0000250|UniProtKB:P13899}.
CC   -!- PTM: [Leader protein]: Phosphorylated. {ECO:0000250|UniProtKB:Q66765}.
CC   -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages by the viral
CC       protease in vivo yield a variety of precursors and mature proteins (By
CC       similarity). The polyprotein seems to be cotranslationally cleaved at
CC       the 2A/2B junction by a ribosomal skip from one codon to the next
CC       without formation of a peptide bond (By similarity). This process would
CC       release the P1-2A peptide from the translational complex (By
CC       similarity). {ECO:0000250|UniProtKB:P03304}.
CC   -!- PTM: [Capsid protein VP0]: During virion maturation, immature virions
CC       are rendered infectious following cleavage of VP0 into VP4 and VP2.
CC       This maturation seems to be an autocatalytic event triggered by the
CC       presence of RNA in the capsid and is followed by a conformational
CC       change of the particle. {ECO:0000250|UniProtKB:P03300}.
CC   -!- PTM: [VPg]: Uridylylated by the polymerase and is covalently linked to
CC       the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-
CC       peptide primer for the polymerase. {ECO:0000250|UniProtKB:P12296}.
CC   -!- PTM: [Capsid protein VP4]: Myristoylation is required during RNA
CC       encapsidation and formation of the mature virus particle.
CC       {ECO:0000250|UniProtKB:Q66282}.
CC   -!- MISCELLANEOUS: Persistent strains of Theiler's virus (e.g. DA, TO,
CC       BeAn) cause persistent demyelinating disease whereas neurovirulent
CC       strains (such as GDVII) cause acute encephalitis.
CC   -!- MISCELLANEOUS: [Isoform Genome polyprotein]: Produced by conventional
CC       translation. {ECO:0000269|PubMed:26063423}.
CC   -!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
CC       {ECO:0000305}.
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DR   EMBL; M20562; AAA47929.1; -; Genomic_RNA.
DR   EMBL; M14703; AAA47933.1; -; Genomic_RNA.
DR   PIR; A26100; A26100.
DR   PIR; A29193; GNNYTP.
DR   PDB; 7NBV; X-ray; 1.87 A; A=923-1055.
DR   PDBsum; 7NBV; -.
DR   SMR; P08545; -.
DR   MEROPS; C03.010; -.
DR   Proteomes; UP000008247; Genome.
DR   GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0039618; C:T=pseudo3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005216; F:monoatomic ion channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0039520; P:induction by virus of host autophagy; ISS:UniProtKB.
DR   GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR   GO; GO:0039522; P:suppression by virus of host mRNA export from nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0039580; P:suppression by virus of host PKR signaling; IEA:UniProtKB-KW.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0039540; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host RIG-I activity; IEA:UniProtKB-KW.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039707; P:virus-mediated pore formation in host cell membrane; IEA:UniProtKB-KW.
DR   CDD; cd23211; Cardiovirus_RdRp; 1.
DR   CDD; cd00205; rhv_like; 3.
DR   Gene3D; 1.20.960.20; -; 1.
DR   Gene3D; 2.60.120.20; -; 3.
DR   Gene3D; 3.30.70.270; -; 2.
DR   Gene3D; 4.10.90.10; Capsid protein VP4 superfamily, Picornavirus; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR015031; Capsid_VP4_Picornavir.
DR   InterPro; IPR037080; Capsid_VP4_sf_Picornavirus.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
DR   InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR   InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR   InterPro; IPR044067; PCV_3C_PRO.
DR   InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001676; Picornavirus_capsid.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR033703; Rhv-like.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR029053; Viral_coat.
DR   Pfam; PF00548; Peptidase_C3; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   Pfam; PF00073; Rhv; 2.
DR   Pfam; PF00910; RNA_helicase; 1.
DR   Pfam; PF08935; VP4_2; 1.
DR   PRINTS; PR00918; CALICVIRUSNS.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF88633; Positive stranded ssRNA viruses; 2.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS51874; PCV_3C_PRO; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR   PROSITE; PS51218; SF3_HELICASE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Capsid protein; Covalent protein-RNA linkage;
KW   Disulfide bond; Eukaryotic host gene expression shutoff by virus;
KW   Eukaryotic host translation shutoff by virus; Helicase; Host cytoplasm;
KW   Host cytoplasmic vesicle; Host gene expression shutoff by virus;
KW   Host membrane; Host mRNA suppression by virus; Host nucleus;
KW   Host-virus interaction; Hydrolase;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host interferon signaling pathway by virus;
KW   Inhibition of host mRNA nuclear export by virus;
KW   Inhibition of host PKR by virus; Inhibition of host RIG-I by virus;
KW   Inhibition of host RLR pathway by virus;
KW   Interferon antiviral system evasion; Ion channel; Ion transport;
KW   Lipoprotein; Membrane; Metal-binding; Myristate; Nucleotide-binding;
KW   Nucleotidyltransferase; Phosphoprotein; Protease; Ribosomal frameshifting;
KW   RNA-binding; RNA-directed RNA polymerase;
KW   T=pseudo3 icosahedral capsid protein; Thiol protease; Transferase;
KW   Transport; Viral attachment to host cell; Viral immunoevasion;
KW   Viral ion channel; Viral RNA replication; Virion;
KW   Virus entry into host cell; Zinc; Zinc-finger.
FT   CHAIN           1..2303
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000446099"
FT   CHAIN           1..76
FT                   /note="Leader protein"
FT                   /id="PRO_0000040192"
FT   CHAIN           77..414
FT                   /note="Capsid protein VP0"
FT                   /id="PRO_0000310972"
FT   CHAIN           77..147
FT                   /note="Capsid protein VP4"
FT                   /id="PRO_0000040193"
FT   CHAIN           148..414
FT                   /note="Capsid protein VP2"
FT                   /id="PRO_0000040194"
FT   CHAIN           415..646
FT                   /note="Capsid protein VP3"
FT                   /id="PRO_0000040195"
FT   CHAIN           647..922
FT                   /note="Capsid protein VP1"
FT                   /id="PRO_0000040196"
FT   CHAIN           923..1055
FT                   /note="Protein 2A"
FT                   /id="PRO_0000040197"
FT   CHAIN           1056..1191
FT                   /note="Protein 2B"
FT                   /id="PRO_0000040198"
FT   CHAIN           1192..1517
FT                   /note="Protein 2C"
FT                   /id="PRO_0000040199"
FT   CHAIN           1518..1605
FT                   /note="Protein 3A"
FT                   /id="PRO_0000040200"
FT   CHAIN           1606..1625
FT                   /note="VPg"
FT                   /id="PRO_0000040201"
FT   CHAIN           1626..1842
FT                   /note="Protease 3C"
FT                   /id="PRO_0000040202"
FT   CHAIN           1843..2303
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000040203"
FT   DOMAIN          1283..1448
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   DOMAIN          1636..1829
FT                   /note="Peptidase C3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   DOMAIN          2071..2189
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   ZN_FING         3..14
FT                   /evidence="ECO:0000250|UniProtKB:P12296"
FT   REGION          30..46
FT                   /note="Acidic"
FT                   /evidence="ECO:0000305"
FT   REGION          60..73
FT                   /note="Theilo"
FT                   /evidence="ECO:0000250|UniProtKB:P13899"
FT   REGION          73..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1041..1047
FT                   /note="Host EIF4E binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q66765"
FT   COMPBIAS        74..93
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1680
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1714
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1793
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        2077
FT                   /note="For RdRp activity"
FT                   /evidence="ECO:0000250|UniProtKB:P12296"
FT   ACT_SITE        2175
FT                   /note="For RdRp activity"
FT                   /evidence="ECO:0000250|UniProtKB:P12296"
FT   BINDING         1312..1319
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   SITE            147..148
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
FT   SITE            414..415
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   SITE            646..647
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   SITE            922..923
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   SITE            1055..1056
FT                   /note="Cleavage; by ribosomal skip"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   SITE            1191..1192
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   SITE            1517..1518
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   SITE            1605..1606
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   SITE            1625..1626
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   SITE            1842..1843
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   MOD_RES         1608
FT                   /note="O-(5'-phospho-RNA)-tyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   LIPID           77
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:Q66282"
FT   DISULFID        501..503
FT                   /evidence="ECO:0000250|UniProtKB:C0MHL9"
FT   CONFLICT        1747..1750
FT                   /note="VTGI -> CYRD (in Ref. 2; AAA47933)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1992..2000
FT                   /note="DDVVYQSFL -> GRRCLPIIF (in Ref. 2; AAA47933)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2003
FT                   /note="E -> Q (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2008
FT                   /note="E -> H (in Ref. 2; AAA47933)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2046
FT                   /note="F -> L (in Ref. 2; AAA47933)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2128..2134
FT                   /note="LIRGGLP -> YSWGPA (in Ref. 2; AAA47933)"
FT                   /evidence="ECO:0000305"
FT   STRAND          928..936
FT                   /evidence="ECO:0007829|PDB:7NBV"
FT   STRAND          938..947
FT                   /evidence="ECO:0007829|PDB:7NBV"
FT   STRAND          950..958
FT                   /evidence="ECO:0007829|PDB:7NBV"
FT   HELIX           964..972
FT                   /evidence="ECO:0007829|PDB:7NBV"
FT   STRAND          986..994
FT                   /evidence="ECO:0007829|PDB:7NBV"
FT   STRAND          999..1007
FT                   /evidence="ECO:0007829|PDB:7NBV"
FT   STRAND          1015..1021
FT                   /evidence="ECO:0007829|PDB:7NBV"
FT   HELIX           1027..1036
FT                   /evidence="ECO:0007829|PDB:7NBV"
FT   HELIX           1039..1042
FT                   /evidence="ECO:0007829|PDB:7NBV"
SQ   SEQUENCE   2303 AA;  256344 MW;  5D0FBE6E47F72A04 CRC64;
     MACKHGYPDV CPICTAVDAT PDFEYLLMAD GEWFPTDLLC VDLDDDVFWP SDTSTQPQTM
     EWTDVPLVCD TVMEPQGNAS SSDKSNSQSS GNEGVIINNF YSNQYQNSID LSASGGNAGD
     APQNNGQLSS ILGGAANAFA TMAPLLMDQN TEEMENLSDR VASDKAGNSA TNTQSTVGRL
     CGYGKSHHGE HPTSCADAAT DKVLAAERYY TIDLASWTTS QEAFSHIRIP LPHVLAGEDG
     GVFGATLRRH YLCKTGWRVQ VQCNASQFHA GSLLVFMAPE FYTGKGTKSG TMEPSDPFTM
     DTTWRSPQSA PTGYRYDRQA GFFAMNHQNQ WQWTVYPHQI LNLRTNTTVD LEVPYVNVAP
     SSSWTQHANW TLVVAVLSPL QYATGSSPDV QITASLQPVN PVFNGLRHET VLAQSPIPVT
     VREHQGCFYS TNPDTTVPIY GKTISTPSDY MCGEFSDLLE LCKLPTFLGN PSTDNKRYPY
     FSATNSVPAT SLVDYQVALS CSCTANSMLA AVARNFNQYR GSLNFLFVFT GAAMVKGKFR
     IAYTPPGAGK PTTRDQAMQA TYAIWDLGLN SSFNFTAPFI SPTHYRQTSY TSPTITSVDG
     WVTVWQLTPL TYPSGTPTHS DILTLVSAGD DFTLRMPISP TKWVPQGIDN AEKGKVSNDD
     ASVDFVAEPV KLPENQTRVA FFYDRAVPIG MLRPGQNMET TFSYQENDFR LNCLLLTPLP
     SYCPDSSSGP VRTKAPVQWR WVRSGGANGA NFPLMTKQDY AFLCFSPFTY YKCDLEVTVS
     AMGAGTVSSV LRWAPTGAPA DVTDQLIGYT PSLGETRNPH MWIVGSGNSQ ISFVVPYNSP
     LSVLPAAWFN GWSDFGNTKD FGVAPTSDFG RIWIQGNSSA SVRIRYKKMK VFCPRPTLFF
     PWPTPTTTKI NADNPVPILE LENPASLYRI DLFITFTDEL ITFDYKVHGR PVLTFRIPGF
     GLTPAGRMLV CMGAKPAHSP FTSSKSLYHV IFTSTCNSFS FTIYKGRYRS WKKPIHDELV
     DRGYTTFREF FKAVRGYHAD YYKQRLIHDV EMNPGPVQSV FQPQGAVLTK SLAPQAGIQN
     ILLRLLGIEG DCSEVSKAIT VVTDLVAAWE KAKTTLVSPE FWSELILKTT KFIAASVLYL
     HNPDFTTTVC LSLMTGVDLL TNDSVFDWLK SKLSSFFRTP PPACPNVMQP QGPLREANEG
     FTFAKNIEWA TKTIQSIVNW LTSWFKQEED HPQSKLDKLL MEFPDHCRNI MDMRNGRKAY
     CECTASFKYF DDLYNLAVTC KRIPLASLCE KFKNRHDHSV TRPEPVVAVL RGAAGQGKSV
     TSQIIAQSVS KMAFGRQSVY SMPPDSEYFD GYENQFSVIM DDLGQNPDGE DFTVFCQMVS
     STNFLPNMAH LERKGTPFTS SFIVATTNLP KFRPVTVAHY PAVDRRITFD FTVTAGPHCK
     TPAGMLDIEK AFDEIPGSKP QLACFSADCP LLHKRGVMFT CNRTKTVYNL QQVVKMVNDT
     ITRKTENVKK MNSLVAQSPP DWQHFENILT CLRQNNAALQ DQVDELQEAF TQARERSDFL
     SDWLKVSAII FAGIVSLSAV IKLASKFKES IWPTPVRVEL SEGEQAAYAG RARAQKQALQ
     VLDIQGGGKV LAQAGNPVMD FELFCAKNMV SPITFYYPDK AEVTQSCLLL RAHLFVVNRH
     VAETEWTAFK LRDVRHERDT VVMRSVNRSG AETDLTFVKV TKGPLFKDNV NKFCSNKDDF
     PARNDTVTGI MNTGLAFVYS GNFLIGNQPV NTTTGACFNH CLHYRAQTRR GWCGSAIICN
     VNGKKAVYGM HSAGGGGLAA ATIITRELIE AAEKSMLALE PQGAIVDIST GSVVHVPRKT
     KLRRTVAHDV FQPKFEPAVL SRYDPRTDKD VDVVAFSKHT TNMESLPPIF DIVCGEYANR
     VFTILGKDNG LLTVEQAVLG LSGMDPMEKD TSPGLPYTQQ GLRRTDLLDF NTAKMTPQLD
     YAHSKLVLGV YDDVVYQSFL KDEIRPLEKI HEAKTRIVDV PPFAHCIWGR QLLGRFASKF
     QTKPGFELGS AIGTDPDVDW TRYAAELSGF NYVYDVDYSN FDASHSTAMF ECLINNFFTE
     QNGFDRRIAE YLRSLAVSRH AYEDRRVLIR GGLPSGCAAT SMLNTIMNNV IIRAALYLTY
     SNFEFDDIKV LSYGDDLLIG TNYQIDFNLV KERLAPFGYK ITPANKTTTF PLTSHLQDVT
     FLKRRFVRFN SYLFRPQMDA VNLKAMVSYC KPGTLKEKLM SIALLAVHSG PDIYDEIFLP
     FRNVGIVVPT YDSMLYRWLS LFR
//