ID   POLG_TMEVD              Reviewed;        2301 AA.
AC   P13899; Q88564; Q88565; Q88566; Q88567; Q88568; Q88569; Q88570; Q88571;
AC   Q88572; Q88573; Q88574; Q89580; S4UVR9;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   24-JAN-2024, entry version 190.
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 DA) (TMEV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Picornaviridae; Caphthovirinae; Cardiovirus; Cardiovirus B.
OX   NCBI_TaxID=12126;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2834872; DOI=10.1016/0042-6822(88)90642-3;
RA   Ohara Y., Stein S., Fu J., Stillman L., Klaman L., Roos R.P.;
RT   "Molecular cloning and sequence determination of DA strain of Theiler's
RT   murine encephalomyelitis viruses.";
RL   Virology 164:245-255(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA], FUNCTION (LEADER PROTEIN), AND
RP   INTERACTION WITH MOUSE RNASEL (LEADER PROTEIN).
RX   PubMed=23825954; DOI=10.1371/journal.ppat.1003474;
RA   Sorgeloos F., Jha B.K., Silverman R.H., Michiels T.;
RT   "Evasion of Antiviral Innate Immunity by Theiler's Virus L* Protein through
RT   Direct Inhibition of RNase L.";
RL   PLoS Pathog. 9:E1003474-E1003474(2013).
RN   [3]
RP   ALTERNATIVE INITIATION.
RX   PubMed=2033677; DOI=10.1128/jvi.65.6.3395-3399.1991;
RA   Kong W.P., Roos R.P.;
RT   "Alternative translation initiation site in the DA strain of Theiler's
RT   murine encephalomyelitis virus.";
RL   J. Virol. 65:3395-3399(1991).
RN   [4]
RP   FUNCTION (LEADER PROTEIN).
RX   PubMed=15047849; DOI=10.1128/jvi.78.8.4357-4362.2004;
RA   Delhaye S., van Pesch V., Michiels T.;
RT   "The leader protein of Theiler's virus interferes with nucleocytoplasmic
RT   trafficking of cellular proteins.";
RL   J. Virol. 78:4357-4362(2004).
RN   [5]
RP   FUNCTION (LEADER PROTEIN).
RX   PubMed=19088287; DOI=10.1099/vir.0.005678-0;
RA   Ricour C., Delhaye S., Hato S.V., Olenyik T.D., Michel B.,
RA   van Kuppeveld F.J., Gustin K.E., Michiels T.;
RT   "Inhibition of mRNA export and dimerization of interferon regulatory factor
RT   3 by Theiler's virus leader protein.";
RL   J. Gen. Virol. 90:177-186(2009).
RN   [6]
RP   FUNCTION (LEADER PROTEIN), AND DOMAIN (LEADER PROTEIN).
RX   PubMed=19710133; DOI=10.1128/jvi.00829-09;
RA   Ricour C., Borghese F., Sorgeloos F., Hato S.V., van Kuppeveld F.J.,
RA   Michiels T.;
RT   "Random mutagenesis defines a domain of Theiler's virus leader protein that
RT   is essential for antagonism of nucleocytoplasmic trafficking and cytokine
RT   gene expression.";
RL   J. Virol. 83:11223-11232(2009).
RN   [7]
RP   FUNCTION (LEADER PROTEIN), AND INTERACTION WITH MOUSE RNASEL (LEADER
RP   PROTEIN).
RX   PubMed=29652922; DOI=10.1371/journal.ppat.1006989;
RA   Drappier M., Jha B.K., Stone S., Elliott R., Zhang R., Vertommen D.,
RA   Weiss S.R., Silverman R.H., Michiels T.;
RT   "A novel mechanism of RNase L inhibition: Theiler's virus L* protein
RT   prevents 2-5A from binding to RNase L.";
RL   PLoS Pathog. 14:E1006989-E1006989(2018).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX   PubMed=1549565; DOI=10.1073/pnas.89.6.2061;
RA   Grant R.A., Filman D.J., Fujinami R.S., Icenogle J.P., Hogle J.M.;
RT   "Three-dimensional structure of Theiler virus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:2061-2065(1992).
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
CC       (Probable). 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 (PubMed:19088287). 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 (PubMed:23825954,
CC       PubMed:29652922). {ECO:0000250|UniProtKB:Q66765,
CC       ECO:0000269|PubMed:19088287, ECO:0000269|PubMed:23825954,
CC       ECO:0000269|PubMed:29652922, ECO:0000305|PubMed:15047849,
CC       ECO:0000305|PubMed:19710133}.
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). {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 (By similarity). It displays
CC       RNA-binding, nucleotide binding and NTPase activities (By similarity).
CC       {ECO:0000250|UniProtKB:P03305, ECO:0000250|UniProtKB:P08545}.
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: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 (PubMed:29652922,
CC       PubMed:23825954). {ECO:0000250|UniProtKB:P08544,
CC       ECO:0000250|UniProtKB:Q66765, ECO:0000269|PubMed:29652922}.
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}; 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 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   -!- 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:0000269|PubMed:19710133}.
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   -!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1tme";
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DR   EMBL; M20301; AAA47928.1; -; Genomic_RNA.
DR   EMBL; JX443418; AGM61326.1; -; Genomic_RNA.
DR   PIR; A31228; GNNYTN.
DR   PDB; 1TME; X-ray; 2.80 A; 1=647-920, 2=148-414, 3=415-650, 4=77-147.
DR   PDB; 1TMF; X-ray; 3.50 A; 4=90-130.
DR   PDBsum; 1TME; -.
DR   PDBsum; 1TMF; -.
DR   SMR; P13899; -.
DR   MEROPS; C03.010; -.
DR   EvolutionaryTrace; P13899; -.
DR   Proteomes; UP000000283; Genome.
DR   Proteomes; UP000098676; Segment.
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: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:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 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 nucleus; Host-virus interaction; Hydrolase;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host IRF3 by virus; Inhibition of host RLR pathway by virus;
KW   Ion channel; Ion transport; Lipoprotein; Membrane; Metal-binding;
KW   Myristate; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
KW   Protease; 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..2301
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000446098"
FT   CHAIN           1..76
FT                   /note="Leader protein"
FT                   /id="PRO_0000040180"
FT   CHAIN           77..414
FT                   /note="Capsid protein VP0"
FT                   /id="PRO_0000310971"
FT   CHAIN           77..147
FT                   /note="Capsid protein VP4"
FT                   /id="PRO_0000040181"
FT   CHAIN           148..414
FT                   /note="Capsid protein VP2"
FT                   /id="PRO_0000040182"
FT   CHAIN           415..646
FT                   /note="Capsid protein VP3"
FT                   /id="PRO_0000040183"
FT   CHAIN           647..920
FT                   /note="Capsid protein VP1"
FT                   /id="PRO_0000040184"
FT   CHAIN           921..1053
FT                   /note="Protein 2A"
FT                   /id="PRO_0000040185"
FT   CHAIN           1054..1189
FT                   /note="Protein 2B"
FT                   /id="PRO_0000040186"
FT   CHAIN           1190..1515
FT                   /note="Protein 2C"
FT                   /id="PRO_0000040187"
FT   CHAIN           1516..1603
FT                   /note="Protein 3A"
FT                   /id="PRO_0000040188"
FT   CHAIN           1604..1623
FT                   /note="VPg"
FT                   /id="PRO_0000040189"
FT   CHAIN           1624..1840
FT                   /note="Protease 3C"
FT                   /id="PRO_0000040190"
FT   CHAIN           1841..2301
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000040191"
FT   DOMAIN          1281..1446
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   DOMAIN          1634..1827
FT                   /note="Peptidase C3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   DOMAIN          2069..2187
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:0000269|PubMed:19710133"
FT   REGION          1039..1045
FT                   /note="Host EIF4E binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q66765"
FT   ACT_SITE        1678
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1712
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1791
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        2075
FT                   /note="For RdRp activity"
FT                   /evidence="ECO:0000250|UniProtKB:P12296"
FT   ACT_SITE        2173
FT                   /note="For RdRp activity"
FT                   /evidence="ECO:0000250|UniProtKB:P12296"
FT   BINDING         1310..1317
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            920..921
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   SITE            1053..1054
FT                   /note="Cleavage; by ribosomal skip"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   SITE            1189..1190
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   SITE            1515..1516
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   SITE            1603..1604
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   SITE            1623..1624
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   SITE            1840..1841
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   MOD_RES         1606
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        288
FT                   /note="K -> N (in Ref. 2; AGM61326)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        377
FT                   /note="F -> L (in Ref. 2; AGM61326)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        489
FT                   /note="T -> P (in Ref. 2; AGM61326)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        503
FT                   /note="C -> R (in Ref. 2; AGM61326)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        616
FT                   /note="A -> T (in Ref. 2; AGM61326)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        644
FT                   /note="A -> V (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        648
FT                   /note="S -> T (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1104
FT                   /note="F -> V (in Ref. 2; AGM61326)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1458
FT                   /note="P -> S (in Ref. 2; AGM61326)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1967
FT                   /note="N -> D (in Ref. 2; AGM61326)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2060
FT                   /note="P -> R (in Ref. 2; AGM61326)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2132
FT                   /note="L -> P (in Ref. 2; AGM61326)"
FT                   /evidence="ECO:0000305"
FT   STRAND          90..92
FT                   /evidence="ECO:0007829|PDB:1TMF"
FT   HELIX           103..106
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          162..166
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          169..175
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          179..181
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   HELIX           182..184
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   HELIX           204..206
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          210..217
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          226..231
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   HELIX           233..235
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   HELIX           238..240
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   HELIX           241..247
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          250..262
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          270..279
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   TURN            289..291
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          292..295
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          316..318
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   HELIX           330..335
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          336..342
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   TURN            343..345
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          347..353
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          358..362
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   HELIX           364..366
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          370..381
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          390..406
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   TURN            423..426
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          438..440
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   HELIX           458..463
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          477..486
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          492..497
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   TURN            503..506
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   HELIX           508..513
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          516..521
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          523..529
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          536..544
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          546..548
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   HELIX           554..557
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          560..566
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          568..570
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          572..577
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          582..584
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          586..589
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          601..611
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          618..628
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          633..637
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   HELIX           651..653
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   TURN            661..664
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   HELIX           679..683
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          687..692
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          710..715
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          721..723
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          744..749
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          751..755
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   HELIX           758..762
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          766..779
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          786..792
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   HELIX           810..812
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          813..816
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          818..823
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          828..833
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          838..845
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          869..875
FT                   /evidence="ECO:0007829|PDB:1TME"
FT   STRAND          878..892
FT                   /evidence="ECO:0007829|PDB:1TME"
SQ   SEQUENCE   2301 AA;  256161 MW;  0B6095DF153DBFDF CRC64;
     MACKHGYPDV CPICTAVDVT PGFEYLLLAD GEWFPTDLLC VDLDDDVFWP SNSSNQSETM
     EWTDLPLVRD IVMEPQGNAS SSDKSNSQSS GNEGVIINNF YSNQYQNSID LSASGGNAGD
     APQNNGQLSN ILGGAANAFA TMAPLLLDQN TEEMENLSDR VASDKAGNSA TNTQSTVGRL
     CGYGEAHHGE HPASCADTAT DKVLAAERYY TIDLASWTTT QEAFSHIRIP LPHVLAGEDG
     GVFGATLRRH YLCKTGWRVQ VQCNASQFHA GSLLVFMAPE FYTGKGTKTG DMEPTDPFTM
     DTTWRAPQGA PTGYRYDSRT GFFAMNHQNQ WQWTVYPHQI LNLRTNTTVD LEVPYVNIAP
     TSSWTQHANW TLVVAVFSPL QYASGSSSDV QITASIQPVN PVFNGLRHET VIAQSPIAVT
     VREHKGCFYS TNPDTTVPIY GKTISTPNDY MCGEFSDLLE LCKLPTFLGN PNSNNKRYPY
     FSATNSVPTT SLVDYQVALS CSCMCNSMLA AVARNFNQYR GSLNFLFVFT GAAMVKGKFL
     IAYTPPGAGK PTTRDQAMQA TYAIWDLGLN SSFVFTAPFI SPTHYRQTSY TSATIASVDG
     WVTVWQLTPL TYPSGAPVNS DILTLVSAGD DFTLRMPISP TKWAPQGSDN AEKGKVSNDD
     ASVDFVAEPV KLPENQTRVA FFYDRAVPIG MLRPGQNIES TFVYQENDLR LNCLLLTPLP
     SFCPDSTSGP VKTKAPVQWR WVRSGGTTNF PLMTKQDYAF LCFSPFTYYK CDLEVTVSAL
     GTDTVASVLR WAPTGAPADV TDQLIGYTPS LGETRNPHMW LVGAGNTQIS FVVPYNSPLS
     VLPAAWFNGW SDFGNTKDFG VAPNADFGRL WIQGNTSASV RIRYKKMKVF CPRPTLFFPW
     PVSTRSKINA DNPVPILELE NPAAFYRIDL FITFIDEFIT FDYKVHGRPV LTFRIPGFGL
     TPAGRMLVCM GEKPAHGPFT SSRSLYHVIF TATCSSFSFS IYKGRYRSWK KPIHDELVDR
     GYTTFGEFFR AVRAYHADYY KQRLIHDVEM NPGPVQSVFQ PQGAVLTKSL APQAGIQNLL
     LRLLGIDGDC SEVSKAITVV TDLFAAWERA KTTLVSPEFW SKLILKTTKF IAASVLYLHN
     PDFTTTVCLS LMTGVDLLTN DSVFDWLKNK LSSFFRTPPP VCPNVLQPQG PLREANEGFT
     FAKNIEWAMK TIQSIVNWLT SWFKQEEDHP QSKLDKFLME FPDHCRNIMD MRNGRKAYCE
     CTASFKYFDE LYNLAVTCKR IPLASLCEKF KNRHDHSVTR PEPVVVVLRG AAGQGKSVTS
     QIIAQSVSKM AFGRQSVYSM PPDSEYFDGY ENQFSVIMDD LGQNPDGEDF TVFCQMVSST
     NFLPNMAHLE RKGTPFTSSF IVATTNLPKF RPVTVAHYPA VDRRITFDFT VTAGPHCTTS
     NGMLDIEKAF DEIPGSKPQL ACFSADCPLL HKRGVMFTCN RTKAVYNLQQ VVKMVNDTIT
     RKTENVKKMN SLVAQSPPDW EHFENILTCL RQNNAALQDQ LDELQEAFAQ ARERSDFLSD
     WLKVSAIIFA GIASLSAVIK LASKFKESIW PSPVRVELSE GEQAAYAGRA RAQKQALQVL
     DIQGGGKVLA QAGNPVMDFE LFCAKNMVAP ITFYYPDKAE VTQSCLLLRA HLFVVNRHVA
     ETEWTAFKLK DVRHERDTVV TRSVNRSGAE TDLTFIKVTK GPLFKDNVNK FCSNKDDFPA
     RNDAVTGIMN TGLAFVYSGN FLIGNQPVNT TTGACFNHCL HYRAQTRRGW CGSAVICNVN
     GKKAVYGMHS AGGGGLAAAT IITRELIEAA EKSMLALEPQ GAIVDISTGS VVHVPRKTKL
     RRTVAHDVFQ PKFEPAVLSR YDPRTDKDVD VVAFSKHTTN MESLPPVFDI VCDEYANRVF
     TILGKDNGLL TVEQAVLGLP GMDPMEKDTS PGLPYTQQGL RRTDLLNFNT AKMTPQLDYA
     HSKLVLGVYD DVVYQSFLKD EIRPLEKIHE AKTRIVDVPP FAHCIWGRQL LGRFASKFQT
     KPGLELGSAI GTDPDVDWTP YAAELSGFNY VYDVDYSNFD ASHSTAMFEC LIKNFFTEQN
     GFDRRIAEYL RSLAVSRHAY EDRRVLIRGG LLSGCAATSM LNTIMNNVII RAALYLTYSN
     FEFDDIKVLS YGDDLLIGTN YQIDFNLVKE RLAPFGYKIT PANKTTTFPL TSHLQDVTFL
     KRRFVRFNSY LFRPQMDAVN LKAMVSYCKP GTLKEKLMSI ALLAVHSGPD IYDEIFLPFR
     NVGIVVPTYS SMLYRWLSLF R
//